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Human Metabolome Database Version 2.5

 

Showing metabocard for L-Homoserine (HMDB00719)

Legend: metabolite field enzyme field

Version 2.5
Creation Date 2005-11-16 15:48:42
Update Date 2009-05-05 20:58:12
Accession Number HMDB00719
Secondary Accession Numbers Not Available
Common Name L-Homoserine
Description Homoserine is a more reactive variant of the amino acid serine. In this variant, the hydroxyl side chain contains an additional CH2 group which brings the hydroxyl group closer to its own carboxyl group, allowing it to chemically react to form a five-membered ring. This occurs at the point that amino acids normally join to their neighbours in a peptide bond. Homoserine is therefore unsuitable for forming proteins and has been eliminated from the repertoire of amino acids used by living things. Homoserine is the final product on the C-terminal end of the N-terminal fragment following a cyanogen bromide cleavage. (wikipedia)
Synonyms
  1. (S)-2-Amino-4-hydroxybutanoate
  2. (S)-2-Amino-4-hydroxybutanoic acid
  3. (S)-2-amino-4-hydroxy-Butanoate
  4. (S)-2-amino-4-hydroxy-Butanoic acid
  5. (S)-Homoserine
  6. 2-Amino-4-hydroxybutanoate
  7. 2-Amino-4-hydroxybutanoic acid
  8. 2-Amino-4-hydroxybutyrate
  9. 2-Amino-4-hydroxybutyric acid
  10. 2-amino-4-hydroxy-Butyrate
  11. 2-amino-4-hydroxy-Butyric acid
  12. 2-amino-4-hydroxy-L-Butyrate
  13. 2-amino-4-hydroxy-L-Butyric acid
  14. Homoserine
  15. L-Homoserine
Chemical IUPAC Name L-Homoserine
Chemical Formula C4H9NO3
Chemical Structure Structure
Chemical Taxonomy
Kingdom
  • Organic
Super Class
  • Amino acids and Amino Acid conjugates
Class
  • Amino Acids
Sub Class
  • NA
Family
  • Microbial Metabolite
Species
  • primary alcohol
  • primary amine
  • primary aliphatic amine (alkylamine)
  • carboxylic acid
  • alpha-aminoacid
Biofunction
  • Protein synthesis, amino acid biosynthesis
Application
—
Source
  • Endogenous
Average Molecular Weight 119.119
Monoisotopic Molecular Weight 119.058243
Isomeric SMILES N[C@@H](CCO)C(O)=O
Canonical SMILES NC(CCO)C(O)=O
KEGG Compound ID C00263 Link Image
BioCyc ID HOMO-SER Link Image
BiGG ID 34437 Link Image
Wikipedia Link Homoserine Link Image
NuGOwiki Link HMDB00719 Link Image
Metagene Link HMDB00719 Link Image
METLIN ID 5687 Link Image
PubChem Compound 12647 Link Image
PubChem Substance 7888224 Link Image
ChEBI ID Not Available
CAS Registry Number 672-15-1
InChI Identifier InChI=1/C4H9NO3/c5-3(1-2-6)4(7)8/h3,6H,1-2,5H2,(H,7,8)/t3-/m0/s1
Synthesis Reference Kokusenya, Yoshio; Matsuoka, Manabu. Synthesis of amino acids by electrochemical reduction. I. Synthesis of L-homoserine by electrochemical reduction of L-asparagine. Denki Kagaku oyobi Kogyo Butsuri Kagaku (1987), 55(2), 174-5.
Melting Point (Experimental) 203 oC
Experimental Water Solubility 1000.0 mg/mL [BEILSTEIN] Source: PhysProp
Predicted Water Solubility 423.0 mg/mL [Predicted by ALOGPS] Calculated using ALOGPS
Physiological Charge 0
State Solid
Experimental LogP/Hydrophobicity Not Available Source: PhysProp
Predicted LogP/Hydrophobicity -3.31 [Predicted by ALOGPS]; -3.6 [Predicted by PubChem via XLOGP]; -2.97 [MEYLAN,WM & HOWARD,PH (1995)] Calculated using ALOGPS
Material Safety Data Sheet (MSDS)
MOL File Show Link Image
SDF File Show Link Image
PDB File Show Link Image
2D Structure
3D Structure
Experimental PDB ID 1EBU Link Image
Experimental PDB File Show
Experimental PDB Structure
Experimental 1H NMR Spectrum Download Spectrum
Download FID (Varian)
Show Experimental Conditions Link Image
Experimental 13C NMR Spectrum Download Spectrum
Download FID (Bruker)
Show Experimental Conditions Link Image
Experimental 13C HSQC Spectrum Download Spectrum
Download FID (Bruker)
Show Experimental Conditions Link Image
Predicted 1H NMR Spectrum Show Image
Show Peaklist
Predicted 13C NMR Spectrum Show Image
Show Peaklist
Mass Spectrum
Low Energy
Download File
Show Experimental Conditions Link Image
Medium Energy
Download File
Show Experimental Conditions Link Image
High Energy
Download File
Show Experimental Conditions Link Image
Simplified TOCSY Spectrum Show Image
Show Peaklist
BMRB Spectrum Show Image
Show Peaklist
Cellular Location
  • Cytoplasm (Predicted from LogP)
  • Extracellular
Biofluid Location
  • Blood
  • Urine
Tissue Location Not Available
Concentrations (Normal)
Biofluid Blood
Value 12.0 (11.3-17.0) uM
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Turnell DC, Cooper JD: Rapid assay for amino acids in serum or urine by pre-column derivatization and reversed-phase liquid chromatography. Clin Chem. 1982 Mar;28(3):527-31. [PubMed Link Image]
Biofluid Urine
Value 0.29 +/- 0.37 umol/mmol creatinine
Age Infant:0-1 yr old
Sex Both
Patient information Normal
Comments Not Available
References
  • Shoemaker JD, Elliott WH: Automated screening of urine samples for carbohydrates, organic and amino acids after treatment with urease. J Chromatogr. 1991 Jan 2;562(1-2):125-38. [PubMed Link Image]
Concentrations (Abnormal) Not Available
Associated Disorders Not Available
OMIM ID Not Available
Pathways
Name SMPDB Link KEGG Link
Methionine Metabolism SMP00033 Link Image map00270 Link Image
General References
  1. Gazarian KG, Gening LV, Gazarian TG: L-Homoserine: a novel excreted metabolic marker of hepatitis B abnormally produced in liver from methionine. Med Hypotheses. 2002 Apr;58(4):279-83. [PubMed Link Image]
  2. Compagnini A, Cunsolo V, Foti S, Saletti R: Improved accuracy in the matrix-assisted laser desorption/ionization-mass spectrometry determination of the molecular mass of cyanogen bromide fragments of proteins by post-cleavage reaction with tris(hydroxymethyl)aminomethane. Proteomics. 2001 Aug;1(8):967-74. [PubMed Link Image]
  3. Shoemaker JD, Elliott WH: Automated screening of urine samples for carbohydrates, organic and amino acids after treatment with urease. J Chromatogr. 1991 Jan 2;562(1-2):125-38. [PubMed Link Image]
  4. Wikipedia Link Image
Metabolic Enzymes
  1. Homoserine dehydrogenase
  2. Homoserine dehydrogenase
  3. Homoserine dehydrogenase
  4. Homoserine dehydrogenase
  5. Putative aspartokinase I-homoserine dehydrogenase
  6. Aspartokinase/homoserine dehydrogenase
  7. Homoserine dehydrogenase
  8. Homoserine dehydrogenase
  9. Homoserine dehydrogenase
  10. Bifunctional aspartokinase/homoserine dehydrogenase 1
  11. Bifunctional aspartokinase/homoserine dehydrogenase 2
  12. Homoserine O-succinyltransferase
  13. Homoserine O-succinyltransferase
  14. Homoserine O-succinyltransferase
  15. Homoserine O-succinyltransferase
  16. Homoserine O-succinyltransferase
  17. Homoserine O-succinyltransferase
  18. Homoserine O-succinyltransferase
  19. Homoserine kinase
  20. Homoserine kinase
  21. Possible homoserine kinase
  22. Homoserine kinase
  23. Homoserine kinase
  24. Homoserine kinase
  25. Homoserine dehydrogenase
  26. Fused aspartokinase I and homoserine dehydrogenase I
  27. Fused aspartokinase II
  28. Homoserine trans-succinylase
  29. Homoserine O-succinyltransferase
  30. Homoserine kinase
  31. Homoserine kinase
Enzyme 1 [top]
Enzyme 1 ID 15478
Enzyme 1 Name Homoserine dehydrogenase
Enzyme 1 Synonyms Not Available
Enzyme 1 Gene Name hom2
Enzyme 1 Protein Sequence >Homoserine dehydrogenase 
METIKIGVVGLGTVGTGVVKMLQAHQEKISEITGRKLELACVVVHNLKKHEQVDLGDVQM
TDQIATLLDDPSIQIMVEVMGSIHPAKEYITQALQAGKHVVTANKDLIAQYGRELVQIAR
ENHRDLFYEASVAGGIPILRTIDNSFAADRIQRVMGIVNGTTNYIMTQMLTKHWSYDQAL
SSAQDLGFAESDPTNDVEGLDAAFKMIILTQFAFGMSLSLDHVQVQGITKISPEDIAEAH
QLGYTIKLLGIAEEIDDRIAVSVGPVLVSDQHPLATVQNENNAVMVTGTAVGNTMFYGPG
AGELPTANSVLSDITTVAKNIALNTTGNTFNSYRQETVLATPEDVVYPHFIALKMRDVPG
MMMKLTAIMTRAEVSFSRIIQNQLGDGNARVVIITHAMNDQQLADITREIGEQENMQLLA
SYKVLKNA
Enzyme 1 Number of Residues 428
Enzyme 1 Molecular Weight 46672.2
Enzyme 1 Theoretical pI 4.93
Enzyme 1 GO Classification
Function
  • NADP or NADPH binding
  • amino acid binding
  • binding
  • carboxylic acid binding
  • catalytic activity
  • homoserine dehydrogenase activity
  • nucleotide binding
  • oxidoreductase activity
  • oxidoreductase activity, acting on CH-OH group of donors
  • oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
Process
  • cellular amino acid and derivative metabolic process
  • cellular amino acid metabolic process
  • cellular metabolic process
  • metabolic process
  • oxidation reduction
Component
—
Enzyme 1 General Function Involved in amino acid binding
Enzyme 1 Specific Function L-homoserine + NAD(P)(+) = L-aspartate 4- semialdehyde + NAD(P)H
Enzyme 1 Pathways Not Available
Enzyme 1 Reactions
  • L-homoserine + NAD(P)+ = L-aspartate 4-semialdehyde + NAD(P)H + H+ [RN:R01773 R01775]
Enzyme 1 Pfam Domain Function
Enzyme 1 Signals
  • None
Enzyme 1 Transmembrane Regions
  • None
Enzyme 1 Essentiality Not Available
Enzyme 1 GenBank ID Protein 28270285 Link Image
Enzyme 1 UniProtKB/Swiss-Prot ID Q88Z09 Link Image
Enzyme 1 UniProtKB/Swiss-Prot Entry Name Q88Z09_LACPL Link Image
Enzyme 1 PDB ID Not Available
Enzyme 1 Cellular Location Not Available
Enzyme 1 Gene Sequence >1287 bp 
ATGGAAACGATTAAAATTGGTGTGGTCGGACTAGGCACAGTCGGGACCGGCGTTGTAAAA
ATGCTTCAAGCGCATCAGGAAAAGATTTCAGAAATTACCGGTCGTAAGTTGGAACTAGCC
TGCGTAGTTGTCCACAACTTGAAAAAGCACGAACAAGTTGATTTGGGGGACGTTCAGATG
ACCGACCAAATCGCGACCCTGCTTGATGATCCGTCCATTCAAATTATGGTCGAAGTGATG
GGTTCAATTCATCCGGCGAAGGAATATATTACGCAAGCCTTGCAAGCTGGCAAACACGTG
GTGACGGCCAATAAGGACTTGATTGCGCAATATGGCCGGGAGTTGGTTCAGATTGCTCGT
GAAAATCATCGCGACTTATTCTATGAAGCTAGTGTTGCTGGTGGGATTCCAATTTTACGG
ACGATTGATAATAGTTTCGCCGCTGACCGGATTCAACGGGTCATGGGAATCGTCAACGGG
ACCACTAATTACATCATGACGCAGATGCTGACTAAGCATTGGTCGTATGATCAAGCCTTG
AGCTCAGCACAAGACTTGGGGTTTGCCGAAAGTGATCCCACTAATGATGTCGAAGGCCTT
GATGCGGCGTTCAAGATGATTATTTTAACGCAGTTTGCCTTTGGGATGAGTCTTTCCCTC
GACCACGTTCAAGTTCAGGGAATTACGAAAATCAGCCCAGAGGATATTGCGGAAGCTCAT
CAGCTTGGGTATACGATTAAATTACTCGGGATTGCGGAAGAAATTGACGATCGCATTGCG
GTATCAGTCGGGCCTGTGCTCGTTTCTGATCAACATCCACTTGCCACGGTACAAAATGAG
AATAATGCTGTAATGGTAACGGGAACGGCTGTGGGGAACACGATGTTTTACGGTCCCGGC
GCTGGAGAACTCCCGACCGCCAACAGTGTGCTGAGTGATATTACAACGGTTGCGAAAAAT
ATTGCGTTGAATACGACTGGTAACACGTTTAACTCTTATCGCCAGGAGACAGTCTTAGCA
ACGCCTGAAGATGTTGTGTATCCTCACTTTATTGCCTTGAAGATGCGTGATGTGCCGGGG
ATGATGATGAAATTGACGGCGATTATGACCCGCGCAGAAGTTTCATTTAGTCGAATCATT
CAAAATCAATTAGGTGACGGCAACGCTCGTGTTGTGATCATTACCCATGCCATGAATGAT
CAACAGTTAGCAGATATCACTCGTGAAATCGGTGAACAAGAGAATATGCAACTATTAGCG
AGTTATAAAGTTTTAAAGAATGCGTAG
Enzyme 1 GenBank Gene ID AL935253 Link Image
Enzyme 1 GeneCard ID hom2 Link Image
Enzyme 1 GenAtlas ID Not Available
Enzyme 1 HGNC ID Not Available
Enzyme 1 Chromosome Location Not Available
Enzyme 1 Locus lp_0571
Enzyme 1 SNPs SNPJam Report Link Image
Enzyme 1 General References
  1. Kleerebezem M, Boekhorst J, van Kranenburg R, Molenaar D, Kuipers OP, Leer R, Tarchini R, Peters SA, Sandbrink HM, Fiers MW, Stiekema W, Lankhorst RM, Bron PA, Hoffer SM, Groot MN, Kerkhoven R, de Vries M, Ursing B, de Vos WM, Siezen RJ: Complete genome sequence of Lactobacillus plantarum WCFS1. Proc Natl Acad Sci U S A. 2003 Feb 18;100(4):1990-5. Epub 2003 Feb 3. [PubMed Link Image]
Enzyme 1 Metabolite References Not Available
Enzyme 2 [top]
Enzyme 2 ID 15479
Enzyme 2 Name Homoserine dehydrogenase
Enzyme 2 Synonyms Not Available
Enzyme 2 Gene Name hom1
Enzyme 2 Protein Sequence >Homoserine dehydrogenase 
MTTTIEVGMLGLGTVGSGVVERLTRSAAKIEQTQGIRLHLAAVAVNHLNAPRTVQLPIGT
RLTDSLTNVVCDRKIQLVIEVMGTVATAKKAIVAALNQGKAVVTANKDLIATAGPELAAL
AKKQGCDLFYEASVAGGIPILRTLTDSYVTDNVQAVSGIINGTANYMLSAMATGQSYEQA
LATAQATGYAEADPTNDVAGIDAAYKLMILSRFAFGQELSLPQIAPTGITHLSASVCRLA
AENGWQIKLLAQIQRHGSGLYCRVAPVAVPVDQPLSQINGVQNAVAVQSEAIGTSLYTGP
GAGSTATANSVLNDVLVAAKHLINGYRMIRNQKRSVSLTVTRFDQLPQTYLGIGPVAPEA
VKYYANEADFSVKTIADDCYQITGLSAVKRKKLRANLPLTLIPIAGTTDWKQVTENSITS
PINVAI
Enzyme 2 Number of Residues 426
Enzyme 2 Molecular Weight 44824.1
Enzyme 2 Theoretical pI 8.86
Enzyme 2 GO Classification
Function
  • NADP or NADPH binding
  • binding
  • catalytic activity
  • homoserine dehydrogenase activity
  • nucleotide binding
  • oxidoreductase activity
  • oxidoreductase activity, acting on CH-OH group of donors
  • oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
Process
  • cellular amino acid and derivative metabolic process
  • cellular amino acid metabolic process
  • cellular metabolic process
  • metabolic process
  • oxidation reduction
Component
—
Enzyme 2 General Function Involved in oxidoreductase activity
Enzyme 2 Specific Function L-homoserine + NAD(P)(+) = L-aspartate 4- semialdehyde + NAD(P)H
Enzyme 2 Pathways Not Available
Enzyme 2 Reactions
  • L-homoserine + NAD(P)+ = L-aspartate 4-semialdehyde + NAD(P)H + H+ [RN:R01773 R01775]
Enzyme 2 Pfam Domain Function
Enzyme 2 Signals
  • None
Enzyme 2 Transmembrane Regions
  • None
Enzyme 2 Essentiality Not Available
Enzyme 2 GenBank ID Protein 28271914 Link Image
Enzyme 2 UniProtKB/Swiss-Prot ID Q88UF7 Link Image
Enzyme 2 UniProtKB/Swiss-Prot Entry Name Q88UF7_LACPL Link Image
Enzyme 2 PDB ID Not Available
Enzyme 2 Cellular Location Not Available
Enzyme 2 Gene Sequence >1281 bp 
ATGACAACGACAATTGAAGTGGGCATGTTAGGGTTAGGAACTGTGGGTAGTGGGGTGGTT
GAACGGTTGACCCGCTCGGCTGCCAAAATTGAACAAACGCAGGGTATTCGGTTGCACCTA
GCAGCAGTTGCCGTTAATCATTTGAACGCGCCTCGGACTGTTCAGTTACCGATTGGGACG
CGCTTGACCGATTCATTAACGAACGTTGTTTGTGACCGAAAAATCCAACTAGTCATTGAA
GTCATGGGGACGGTCGCAACTGCTAAAAAGGCCATTGTGGCAGCACTTAATCAGGGTAAG
GCTGTCGTGACCGCTAATAAAGACTTAATTGCAACGGCGGGACCTGAATTGGCTGCGTTA
GCCAAAAAACAGGGCTGTGATTTATTTTACGAGGCTAGTGTTGCGGGGGGAATTCCGATC
TTGCGGACATTAACAGATAGTTACGTGACGGACAATGTGCAGGCGGTCAGCGGAATCATC
AACGGGACGGCTAATTATATGCTAAGTGCAATGGCAACCGGGCAATCGTACGAACAAGCT
TTAGCTACTGCACAAGCAACCGGGTACGCCGAAGCTGATCCGACTAATGATGTTGCGGGC
ATTGATGCGGCATACAAATTGATGATCCTCAGTCGCTTTGCTTTTGGGCAAGAGTTGAGC
CTGCCGCAGATTGCACCCACGGGAATCACGCATTTAAGCGCTTCGGTTTGTCGATTAGCA
GCTGAAAATGGCTGGCAGATTAAATTGCTCGCGCAGATTCAGCGACACGGATCTGGTTTG
TATTGTCGTGTGGCGCCAGTGGCCGTGCCGGTTGATCAACCCCTGAGTCAGATCAATGGG
GTCCAAAACGCGGTAGCTGTTCAAAGTGAAGCCATTGGTACCAGCTTGTATACCGGACCG
GGTGCGGGAAGTACGGCGACGGCTAATAGTGTTCTAAATGACGTCTTAGTAGCGGCCAAG
CACCTTATCAATGGTTATCGAATGATTCGTAACCAGAAAAGAAGTGTCTCGTTAACGGTC
ACTCGATTTGACCAGTTACCACAAACATACTTAGGCATTGGTCCGGTCGCACCAGAAGCC
GTGAAATATTACGCTAATGAAGCTGATTTCTCAGTAAAAACGATTGCCGATGATTGTTAT
CAGATTACTGGATTAAGTGCGGTGAAACGCAAAAAGCTGCGTGCGAACTTGCCACTGACT
TTGATACCAATTGCCGGTACAACGGACTGGAAGCAAGTGACCGAAAATTCAATAACATCT
CCCATAAATGTTGCAATTTGA
Enzyme 2 GenBank Gene ID AL935259 Link Image
Enzyme 2 GeneCard ID hom1 Link Image
Enzyme 2 GenAtlas ID Not Available
Enzyme 2 HGNC ID Not Available
Enzyme 2 Chromosome Location Not Available
Enzyme 2 Locus lp_2535
Enzyme 2 SNPs SNPJam Report Link Image
Enzyme 2 General References
  1. Kleerebezem M, Boekhorst J, van Kranenburg R, Molenaar D, Kuipers OP, Leer R, Tarchini R, Peters SA, Sandbrink HM, Fiers MW, Stiekema W, Lankhorst RM, Bron PA, Hoffer SM, Groot MN, Kerkhoven R, de Vries M, Ursing B, de Vos WM, Siezen RJ: Complete genome sequence of Lactobacillus plantarum WCFS1. Proc Natl Acad Sci U S A. 2003 Feb 18;100(4):1990-5. Epub 2003 Feb 3. [PubMed Link Image]
Enzyme 2 Metabolite References Not Available
Enzyme 3 [top]
Enzyme 3 ID 15480
Enzyme 3 Name Homoserine dehydrogenase
Enzyme 3 Synonyms Not Available
Enzyme 3 Gene Name Not Available
Enzyme 3 Protein Sequence >Homoserine dehydrogenase 
MAIKIALLGLGTVGSGVLKIIKDNQKKIKQTSGEEIIIKKALVRNIEKHKNMADTVELTT
DFTDILNDSEIKIVVELIGGLHPTKEYITEALKSGKNVVTANKDLMATYGSELISIAAKN
KCDLMYDASVAGGIPILRTIRKSYAGDIISEIQGIINGTTNYILSQMGENGLSYDEALKK
AQELGFAEADPTNDVTGKDAAYKIVILSKFAFGTKIGIDDFTIEGINNLQAFDIEQAKKM
GYTIKLIGIAKNINDKLFVEVAPCLLPENSIMAHIKNEINALQIKSQSLGTAVFTGPGAG
SSATASSVMSDVIAETNNYVKKTNGQPFSNFSRIMKLTSSEDVKYPYYLSFEAEETLLTL
SKLLSDLEIPIKEIKRVDERTVVVTEEISRQQLQDLVIQDQNLRASYKIL
Enzyme 3 Number of Residues 410
Enzyme 3 Molecular Weight 44856.2
Enzyme 3 Theoretical pI 5.38
Enzyme 3 GO Classification
Function
  • NADP or NADPH binding
  • binding
  • catalytic activity
  • homoserine dehydrogenase activity
  • nucleotide binding
  • oxidoreductase activity
  • oxidoreductase activity, acting on CH-OH group of donors
  • oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
Process
  • cellular amino acid and derivative metabolic process
  • cellular amino acid metabolic process
  • cellular metabolic process
  • metabolic process
  • oxidation reduction
Component
—
Enzyme 3 General Function Involved in oxidoreductase activity
Enzyme 3 Specific Function L-homoserine + NAD(P)(+) = L-aspartate 4- semialdehyde + NAD(P)H
Enzyme 3 Pathways Not Available
Enzyme 3 Reactions
  • L-homoserine + NAD(P)+ = L-aspartate 4-semialdehyde + NAD(P)H + H+ [RN:R01773 R01775]
Enzyme 3 Pfam Domain Function
Enzyme 3 Signals
  • None
Enzyme 3 Transmembrane Regions
  • None
Enzyme 3 Essentiality Not Available
Enzyme 3 GenBank ID Protein 58254811 Link Image
Enzyme 3 UniProtKB/Swiss-Prot ID Q5FJS6 Link Image
Enzyme 3 UniProtKB/Swiss-Prot Entry Name Q5FJS6_LACAC Link Image
Enzyme 3 PDB ID Not Available
Enzyme 3 Cellular Location Not Available
Enzyme 3 Gene Sequence >1233 bp 
ATGGCAATCAAAATCGCATTACTTGGGTTAGGCACTGTCGGCTCAGGAGTATTGAAGATT
ATTAAAGATAATCAAAAAAAGATTAAACAAACAAGTGGAGAAGAAATTATTATTAAAAAA
GCACTTGTACGTAATATTGAAAAACACAAAAATATGGCTGATACAGTTGAATTGACCACT
GATTTTACCGATATCTTAAATGATTCTGAGATTAAGATTGTTGTTGAACTAATCGGAGGG
CTGCACCCCACTAAAGAATATATTACAGAGGCATTAAAGTCTGGTAAAAATGTGGTCACT
GCTAATAAAGACTTAATGGCAACGTATGGTTCGGAATTAATTTCTATTGCTGCAAAAAAT
AAATGCGATTTAATGTATGATGCTAGTGTTGCAGGTGGAATACCAATTCTACGTACCATT
AGAAAGTCATATGCGGGTGACATAATTTCAGAAATTCAAGGAATTATCAATGGTACGACC
AATTATATTTTGTCTCAGATGGGCGAAAATGGTTTAAGTTATGATGAAGCCTTAAAAAAG
GCGCAGGAACTTGGATTTGCAGAAGCCGATCCTACAAATGATGTTACGGGAAAAGATGCG
GCGTATAAGATTGTCATTTTGAGTAAATTTGCTTTCGGTACAAAGATTGGTATTGATGAC
TTTACTATTGAAGGTATAAATAATTTACAAGCATTTGATATTGAGCAAGCTAAAAAGATG
GGTTACACAATCAAATTAATTGGTATTGCTAAAAATATTAATGATAAATTATTCGTAGAA
GTAGCCCCGTGTTTATTGCCAGAAAATTCAATTATGGCACATATAAAAAATGAAATTAAT
GCTTTGCAAATCAAGAGTCAAAGCTTAGGAACAGCTGTATTTACCGGACCAGGAGCGGGC
AGCTCTGCTACAGCTAGTTCTGTAATGAGTGACGTAATTGCAGAGACTAATAATTATGTT
AAGAAAACAAATGGTCAGCCTTTTAGTAATTTTTCTAGAATAATGAAATTAACTAGCTCA
GAAGATGTGAAGTATCCTTATTATTTGTCTTTTGAGGCCGAGGAAACATTACTTACTTTG
AGTAAACTTCTTTCTGATTTAGAAATACCAATTAAAGAAATTAAACGGGTGGATGAAAGA
ACCGTAGTGGTGACTGAGGAGATTAGTCGCCAACAATTACAAGATTTAGTGATTCAAGAT
CAAAATTTAAGAGCAAGTTACAAGATTTTATAG
Enzyme 3 GenBank Gene ID CP000033 Link Image
Enzyme 3 GeneCard ID Not Available
Enzyme 3 GenAtlas ID Not Available
Enzyme 3 HGNC ID Not Available
Enzyme 3 Chromosome Location Not Available
Enzyme 3 Locus LBA1212
Enzyme 3 SNPs Not Available
Enzyme 3 General References
  1. Altermann E, Russell WM, Azcarate-Peril MA, Barrangou R, Buck BL, McAuliffe O, Souther N, Dobson A, Duong T, Callanan M, Lick S, Hamrick A, Cano R, Klaenhammer TR: Complete genome sequence of the probiotic lactic acid bacterium Lactobacillus acidophilus NCFM. Proc Natl Acad Sci U S A. 2005 Mar 15;102(11):3906-12. Epub 2005 Jan 25. [PubMed Link Image]
Enzyme 3 Metabolite References Not Available
Enzyme 4 [top]
Enzyme 4 ID 15481
Enzyme 4 Name Homoserine dehydrogenase
Enzyme 4 Synonyms Not Available
Enzyme 4 Gene Name thrA
Enzyme 4 Protein Sequence >Homoserine dehydrogenase 
MARNNETPIRVGLLGAGTVGSQTARLIVEQKDELSARIGRPIELTGVACLDPKETEKFPW
IDQSIVTTDTLSVATNSDIVIELIGGTTVARKFVLAAIESGASVVTANKALLAKYGPEIY
SAAEAKGVDIYFEAAVGGAIPFLRPLRESLVGDKVTSMLGIVNGTTNYILDEMTTKGLQF
DDVLKDAQAKGYAEADPTGDIEGYDAANKAAIMATLGFHTSVTIDDVSVEGITKITADDI
AAATAEHKVIKLLAVVENGEAGVSARVYPALIDENHPLASVHGSFNAVFVKAEAADDLMF
YGRGAGGAPTASAVVGDVVTEARHIAAGCTGPSIPLYKNLPKAPITASKAAFAVRFLIHD
KPGVLAAIAAEFAKNGVSINGVNQDLKPTMTDPGYDGEIQQLRVVTHLTDEETLRNTVKA
VQALDFVTGDPSILRVLD
Enzyme 4 Number of Residues 438
Enzyme 4 Molecular Weight 45928.8
Enzyme 4 Theoretical pI 4.61
Enzyme 4 GO Classification
Function
  • NADP or NADPH binding
  • amino acid binding
  • binding
  • carboxylic acid binding
  • catalytic activity
  • homoserine dehydrogenase activity
  • nucleotide binding
  • oxidoreductase activity
  • oxidoreductase activity, acting on CH-OH group of donors
  • oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
Process
  • cellular amino acid and derivative metabolic process
  • cellular amino acid metabolic process
  • cellular metabolic process
  • metabolic process
  • oxidation reduction
Component
—
Enzyme 4 General Function Involved in amino acid binding
Enzyme 4 Specific Function L-homoserine + NAD(P)(+) = L-aspartate 4- semialdehyde + NAD(P)H
Enzyme 4 Pathways Not Available
Enzyme 4 Reactions
  • L-homoserine + NAD(P)+ = L-aspartate 4-semialdehyde + NAD(P)H + H+ [RN:R01773 R01775]
Enzyme 4 Pfam Domain Function
Enzyme 4 Signals
  • None
Enzyme 4 Transmembrane Regions
  • None
Enzyme 4 Essentiality Not Available
Enzyme 4 GenBank ID Protein 23325382 Link Image
Enzyme 4 UniProtKB/Swiss-Prot ID Q8G4V0 Link Image
Enzyme 4 UniProtKB/Swiss-Prot Entry Name Q8G4V0_BIFLO Link Image
Enzyme 4 PDB ID Not Available
Enzyme 4 Cellular Location Not Available
Enzyme 4 Gene Sequence >1317 bp 
ATGAAGATCAAGAAGAACCTCGTCGCGGCCACGGCGGCCGTGCTTGCGGCCGGCATGGCG
CTGGTCGGCTGCGGTTCCAGCAACGGAGGCAGCGGCGACGTCCAGAAGACCGCCGACGGC
AAGGTGAAGATCACCATGTGGCACGGCTTCTCCGAAGCCGACGGCAAGACGCTGGAATCC
ATCGTCGACGACTTCAACAAGTCCCAGGACAAGTACGAGATCGACGCCCAGCTGCAGCCA
TGGAGCACCATCGGCGAGACGATGGTCACCAAGGTCACCACCGGCGACGGCCCGGACTTC
GTCACCACCGGTGCCGACAATGGCCAGGGTTGGTCCATCGACGGCACCTTCCAGTGCGTC
TCCGATTTCTACGCCGACAAGAACAACGGCACCGGCGACTACCTCGACAACGTCGTCAAG
CAGATCACCTTCAACATCGACGGCGAGGAAGAGAAGTGCGCCGTTCCGATGGGCTACGCG
CCGACCTCCGTGTGGTACAACACCGACATGTGGAAGGCCGCCGGCCTGACCGACAAGGAC
ATTCCGACCACCTGGGACCAGCTCCTCGAGGTCGCCAAGAAGCTCACCAAGTCCGACGGT
TCGCAGTACGGCCTCGCGATGGCCGACTCCGGCTGGGCCGCCTACATGAAGGGCAACGGC
ACCGGCCTGTACACCACCGACGGCAAGGTCTCCATCAACTCCAAGGAGAACAAGGCCTTC
CTGCAGAAGATGCGTGACTTCTACAACGGCGGCTACGCCGTCCCGGGTCTGGACGACACC
GCGGCCCGCGAATCCTTCGAGTCCGGCCAGTCCGCAATGGTGATCGTCGGCCCGTGGGAA
GACCAGGCGGCCACCGACAAGGGCATCAACCACGACACCTTCGCCGTTCCGGACGGCGAC
GGCACCTACAAGTACGCCGACGGCAAGACCGGCTCCAACACCGGCTCCACCGGCCTGTAC
TGGTGGGTCACCTCGCAGGTCGGCGACTCCGAGAAGCTGCCCGGCATCTACGAGTTCTTC
AAGTTCTACAACAACCACGACAACCAGGTGAAGTGGTCCCTCGGCTCCGCCTACCCGCCG
AACAACAAGACCGTCACCGCCGATGAGCTGTCCGACCGTCCGCTGATCGCCAAGATCTCG
CAGTACACCGACAACTCCTACATCGGCATCGCCGGCCTCAAGGGCGGCTTCGGCGACATC
GCCGCCTCCCTCGACACCCTGACCCAGAACACCGTCCGCACCGGCGACGACATCCAGGGT
CTGCTCGACCAGGCCGAGAGCTCCATCTCGGGCTACCTCGACGAGTACGCCGAGTAG
Enzyme 4 GenBank Gene ID AE014295 Link Image
Enzyme 4 GeneCard ID thrA Link Image
Enzyme 4 GenAtlas ID Not Available
Enzyme 4 HGNC ID Not Available
Enzyme 4 Chromosome Location 1
Enzyme 4 Locus 17q11.2
Enzyme 4 SNPs SNPJam Report Link Image
Enzyme 4 General References
  1. Schell MA, Karmirantzou M, Snel B, Vilanova D, Berger B, Pessi G, Zwahlen MC, Desiere F, Bork P, Delley M, Pridmore RD, Arigoni F: The genome sequence of Bifidobacterium longum reflects its adaptation to the human gastrointestinal tract. Proc Natl Acad Sci U S A. 2002 Oct 29;99(22):14422-7. Epub 2002 Oct 15. [PubMed Link Image]
Enzyme 4 Metabolite References Not Available
Enzyme 5 [top]
Enzyme 5 ID 15482
Enzyme 5 Name Putative aspartokinase I-homoserine dehydrogenase
Enzyme 5 Synonyms Not Available
Enzyme 5 Gene Name thrA
Enzyme 5 Protein Sequence >Putative aspartokinase I-homoserine dehydrogenase 
MKVMKFGGTSVGSVNSILSVKKIVESAGEPVIVVVSALGGITDQLISTSRMAAMGDAAYE
GAYREIVRRHEEMVQGVIPAGETQTLLHYQVNELLDELKDIFQGIYLIKDLSPKTSDTIV
SYGERLSSLIASRLIQGAVWFDSRTFIKTEKKHNKHTLDTELTNRLVREAFKEIPRVSLV
PGFISSDKVSGDVTNLGRGGSDYTAAVIAAALDADSLEIWTDVDGFMTADPRVISTAYTI
SELTYVEATELCNFGAKVVYPPTIYPVCHKNIPILIKNTFNPDAQGTVIKQHVDHTKSKA
IKGISSINDTSLITVQGLGMVGVIGVNYRIFKALAKNGISVFLVSQASSENSTSIGVRNA
DADLACEVLNEEFAKEIEMGEISPIQAEKNLATVAIVGENMKHTPGIAGKLFGTLGRNGI
NVIACAQGASETNISFVVDSKSLRKSLNVIHDSFFLSEYQVLNLFICGVGTVGGSLVEQI
RQQQKKLMVENGLKLHVVGIIDATKAMFSRAGFDLANYREELKEKGVDSSLDTIRDEIIG
MNIFNSVFVDCTASPDIASLYKDFLQHNISVVAANKIAASSAYENYRELKLIARQRGVKY
LFETNVGAGLPIINTINDLIHSGDKILKIEAVLSGTLNYIFNKISADVPFSRTIKMAQEE
RYSEPDPRIDLSGKDVIRKLVILAREAGYKLEQEDVEKNLFVPNDFFEGSLEDFWKKVPS
LDADFEARRKVLESENKHWRFVAKLENGKASVGLQEVDRNHPFYGLEGSNNIILLTTERY
KEYPMMIQGYGAGAGVTAAGVFADIMSIANV
Enzyme 5 Number of Residues 811
Enzyme 5 Molecular Weight 88834.8
Enzyme 5 Theoretical pI 5.72
Enzyme 5 GO Classification
Function
  • NADP or NADPH binding
  • amino acid binding
  • aspartate kinase activity
  • binding
  • carboxylic acid binding
  • catalytic activity
  • homoserine dehydrogenase activity
  • nucleotide binding
  • oxidoreductase activity
  • oxidoreductase activity, acting on CH-OH group of donors
  • oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
  • phosphotransferase activity, carboxyl group as acceptor
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • aspartate family amino acid biosynthetic process
  • cellular amino acid and derivative metabolic process
  • cellular amino acid biosynthetic process
  • cellular amino acid metabolic process
  • cellular metabolic process
  • metabolic process
  • oxidation reduction
Component
—
Enzyme 5 General Function Involved in amino acid binding
Enzyme 5 Specific Function Not Available
Enzyme 5 Pathways Not Available
Enzyme 5 Reactions
  • L-homoserine + NAD(P)+ = L-aspartate 4-semialdehyde + NAD(P)H + H+ [RN:R01773 R01775]
Enzyme 5 Pfam Domain Function
Enzyme 5 Signals
  • None
Enzyme 5 Transmembrane Regions
  • None
Enzyme 5 Essentiality Not Available
Enzyme 5 GenBank ID Protein 60491560 Link Image
Enzyme 5 UniProtKB/Swiss-Prot ID Q5LHR8 Link Image
Enzyme 5 UniProtKB/Swiss-Prot Entry Name Q5LHR8_BACFN Link Image
Enzyme 5 PDB ID Not Available
Enzyme 5 Cellular Location Not Available
Enzyme 5 Gene Sequence >2436 bp 
ATGAAAGTAATGAAATTCGGCGGAACGTCCGTAGGTTCCGTGAACAGCATTTTAAGCGTA
AAGAAAATCGTAGAGTCTGCCGGTGAACCGGTAATCGTAGTAGTGTCTGCATTGGGCGGG
ATCACTGACCAGTTGATCAGTACCTCCCGAATGGCCGCCATGGGCGATGCAGCTTACGAA
GGGGCATACCGGGAAATAGTTCGCCGCCACGAAGAGATGGTGCAGGGAGTGATTCCTGCC
GGAGAGACTCAGACCCTGTTGCACTATCAGGTGAATGAATTGCTCGACGAACTGAAAGAT
ATCTTTCAGGGTATTTATCTGATTAAAGATCTTTCTCCGAAAACGTCCGATACCATTGTC
AGTTATGGTGAACGTCTGTCTTCACTGATTGCGTCAAGACTGATCCAAGGGGCTGTATGG
TTCGACTCACGTACTTTTATCAAGACAGAAAAGAAACATAATAAACATACACTGGACACG
GAACTGACCAATCGGTTGGTGCGGGAGGCTTTCAAAGAAATCCCCCGGGTTTCGCTGGTA
CCCGGATTCATCTCTTCGGATAAGGTTTCGGGAGACGTAACGAATCTGGGCAGGGGCGGT
TCCGACTATACCGCAGCTGTTATTGCCGCAGCTCTCGATGCCGATAGTCTGGAGATTTGG
ACGGATGTAGACGGCTTCATGACAGCCGACCCGCGTGTGATCAGTACGGCCTATACTATC
AGCGAGCTGACTTATGTAGAGGCTACCGAACTTTGTAATTTCGGTGCAAAAGTGGTGTAT
CCGCCTACCATCTATCCGGTATGTCACAAAAACATACCGATCCTGATTAAGAATACTTTC
AACCCGGATGCCCAGGGAACGGTGATCAAACAACACGTAGACCACACGAAGAGCAAAGCC
ATCAAAGGGATTTCGTCCATCAACGACACGAGCCTGATTACCGTACAGGGTTTAGGTATG
GTGGGCGTGATCGGTGTCAACTACCGCATCTTTAAGGCGCTGGCAAAGAATGGAATCAGT
GTGTTCCTCGTTTCGCAGGCTTCATCGGAGAACAGTACCTCTATCGGTGTGCGTAATGCC
GATGCCGATCTGGCTTGCGAAGTGCTGAACGAAGAGTTTGCCAAAGAGATCGAAATGGGT
GAGATTTCGCCTATCCAGGCAGAGAAGAACCTGGCTACGGTAGCTATCGTGGGTGAGAAC
ATGAAACATACGCCGGGCATTGCCGGAAAGCTGTTCGGTACGCTGGGACGAAATGGCATC
AATGTGATAGCCTGTGCACAGGGAGCTTCCGAGACCAACATCTCGTTTGTTGTCGATTCA
AAGTCGTTGCGTAAATCGCTGAATGTGATTCACGACTCGTTCTTCCTCTCCGAATATCAG
GTGCTCAACCTCTTTATCTGCGGTGTGGGCACGGTGGGAGGAAGTCTTGTCGAGCAGATC
CGCCAGCAGCAGAAGAAGCTGATGGTAGAAAATGGCCTGAAACTCCATGTGGTAGGTATT
ATCGATGCGACGAAGGCGATGTTCAGCCGTGCCGGATTCGATCTGGCCAACTATCGCGAA
GAGCTGAAAGAGAAGGGAGTGGACAGTTCGCTGGATACTATACGTGACGAGATTATCGGC
ATGAATATATTCAATTCGGTATTTGTGGATTGTACGGCCAGTCCGGACATTGCCTCTCTA
TATAAGGACTTCCTGCAACATAACATTTCTGTGGTGGCGGCCAATAAGATTGCTGCTTCA
TCGGCTTACGAGAATTACCGTGAACTGAAGCTGATAGCCCGCCAGCGTGGTGTGAAATAT
CTGTTTGAAACCAACGTGGGGGCCGGACTTCCGATTATCAATACCATCAATGACCTGATA
CATAGCGGTGATAAGATTCTGAAGATCGAGGCAGTGCTTTCGGGTACGCTGAACTATATT
TTCAATAAGATCAGTGCCGATGTTCCCTTCAGCCGTACCATCAAGATGGCGCAGGAAGAG
CGTTATTCGGAACCCGATCCGCGCATCGACCTGAGCGGTAAGGACGTGATCCGTAAGCTC
GTGATCCTGGCGCGTGAGGCCGGATACAAGCTGGAACAGGAAGACGTGGAGAAGAATCTT
TTCGTACCGAATGACTTCTTTGAAGGTTCGCTGGAAGACTTCTGGAAAAAAGTGCCTAGT
CTGGATGCTGATTTCGAAGCTCGCCGCAAGGTGCTCGAGAGTGAGAATAAACATTGGCGT
TTCGTTGCCAAGCTGGAGAACGGCAAAGCATCCGTCGGTTTGCAGGAAGTGGACCGCAAC
CATCCTTTCTACGGACTGGAAGGCAGCAATAACATCATCTTGCTTACCACCGAACGCTAT
AAAGAATATCCGATGATGATTCAGGGATACGGTGCGGGTGCCGGAGTGACGGCGGCCGGT
GTATTTGCTGACATTATGAGCATTGCAAACGTATAA
Enzyme 5 GenBank Gene ID CR626927 Link Image
Enzyme 5 GeneCard ID thrA Link Image
Enzyme 5 GenAtlas ID Not Available
Enzyme 5 HGNC ID Not Available
Enzyme 5 Chromosome Location 1
Enzyme 5 Locus 17q11.2
Enzyme 5 SNPs SNPJam Report Link Image
Enzyme 5 General References
  1. Cerdeno-Tarraga AM, Patrick S, Crossman LC, Blakely G, Abratt V, Lennard N, Poxton I, Duerden B, Harris B, Quail MA, Barron A, Clark L, Corton C, Doggett J, Holden MT, Larke N, Line A, Lord A, Norbertczak H, Ormond D, Price C, Rabbinowitsch E, Woodward J, Barrell B, Parkhill J: Extensive DNA inversions in the B. fragilis genome control variable gene expression. Science. 2005 Mar 4;307(5714):1463-5. [PubMed Link Image]
Enzyme 5 Metabolite References Not Available
Enzyme 6 [top]
Enzyme 6 ID 15483
Enzyme 6 Name Aspartokinase/homoserine dehydrogenase
Enzyme 6 Synonyms Not Available
Enzyme 6 Gene Name Not Available
Enzyme 6 Protein Sequence >Aspartokinase/homoserine dehydrogenase 
MKVMKFGGTSVGSVNSILSVKKIVESAGEPVIVVVSALGGITDQLISTSRMAAMGDAAYE
GAYREIVRRHEEMVQGVIPAGETQTLLHYQVNELLDELKDIFQGIYLIKDLSPKTSDTIV
SYGERLSSLIASRLIQGAVWFDSRTFIKTEKKHNKHTLDTELTNRLVREAFKEIPRVSLV
PGFISSDKVSGDVTNLGRGGSDYTAAVIAAALDADSLEIWTDVDGFMTADPRVISTAYTI
SELTYVEATELCNFGAKVVYPPTIYPVCHKNIPILIKNTFNPDARGTVIKQHVDHTKSKA
IKGISSINDTSLITVQGLGMVGVIGVNYRIFKALAKNGISVFLVSQASSENSTSIGVRNA
DADLACEVLNEEFAKEIEMGEISPIQAEKNLATVAIVGENMKHTPGIAGKLFGTLGRNGI
NVIACAQGASETNISFVVDSKSLRKSLNVIHDSFFLSEYQVLNLFICGVGTVGGSLVEQI
RQQQKKLMVENGLKLHVVGIIDATKAMFSRAGFDLANYREELKEKGVDSSLDTIRDEIIG
MNIFNSVFVDCTASPDIASLYKDFLQHNISVVAANKIAASSAYENYRELKLIARQRGVKY
LFETNVGAGLPIINTINDLIHSGDKILKIEAVLSGTLNYIFNKISADVPFSRTIKMAQEE
RYSEPDPRIDLSGKDVIRKLVILAREAGYKLEQEDVEKNLFVPNDFFEGSLEDFWKKVPS
LDADFEARRKVLESENKHWRFVAKLENGKASVGLQEVDRNHPFYGLEGSNNIILLTTERY
KEYPMMIQGYGAGAGVTAAGVFADIMSIANV
Enzyme 6 Number of Residues 811
Enzyme 6 Molecular Weight 88862.9
Enzyme 6 Theoretical pI 5.84
Enzyme 6 GO Classification
Function
  • NADP or NADPH binding
  • amino acid binding
  • aspartate kinase activity
  • binding
  • carboxylic acid binding
  • catalytic activity
  • homoserine dehydrogenase activity
  • nucleotide binding
  • oxidoreductase activity
  • oxidoreductase activity, acting on CH-OH group of donors
  • oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
  • phosphotransferase activity, carboxyl group as acceptor
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • aspartate family amino acid biosynthetic process
  • cellular amino acid and derivative metabolic process
  • cellular amino acid biosynthetic process
  • cellular amino acid metabolic process
  • cellular metabolic process
  • metabolic process
  • oxidation reduction
Component
—
Enzyme 6 General Function Involved in amino acid binding
Enzyme 6 Specific Function Not Available
Enzyme 6 Pathways Not Available
Enzyme 6 Reactions Not Available
Enzyme 6 Pfam Domain Function
Enzyme 6 Signals
  • None
Enzyme 6 Transmembrane Regions
  • None
Enzyme 6 Essentiality Not Available
Enzyme 6 GenBank ID Protein 52214764 Link Image
Enzyme 6 UniProtKB/Swiss-Prot ID Q64YR9 Link Image
Enzyme 6 UniProtKB/Swiss-Prot Entry Name Q64YR9_BACFR Link Image
Enzyme 6 PDB ID Not Available
Enzyme 6 Cellular Location Not Available
Enzyme 6 Gene Sequence >2436 bp 
ATGAAAGTAATGAAATTCGGCGGAACGTCCGTAGGTTCCGTGAACAGCATTTTAAGCGTA
AAGAAAATCGTAGAGTCTGCCGGTGAACCGGTAATCGTAGTAGTGTCTGCATTGGGCGGG
ATCACTGACCAGTTGATCAGTACCTCCCGAATGGCCGCCATGGGTGATGCAGCTTACGAA
GGGGCATACCGGGAAATAGTTCGCCGCCACGAAGAGATGGTGCAGGGAGTGATTCCTGCC
GGAGAGACTCAGACCCTGTTGCACTATCAGGTGAATGAATTGCTCGACGAACTGAAAGAT
ATCTTTCAGGGTATTTATCTGATTAAAGATCTTTCTCCGAAAACGTCCGATACCATTGTC
AGTTATGGTGAACGTCTGTCTTCACTGATTGCGTCAAGACTGATCCAAGGGGCTGTATGG
TTCGACTCACGTACTTTTATCAAGACAGAAAAGAAACATAATAAACATACACTGGACACG
GAACTGACCAATCGGTTGGTGCGGGAAGCTTTCAAAGAAATCCCCCGGGTTTCGCTGGTA
CCCGGATTCATCTCTTCGGATAAGGTTTCGGGAGACGTAACGAATCTGGGCAGGGGCGGT
TCCGACTATACCGCAGCTGTTATTGCCGCAGCTCTCGATGCCGATAGTCTGGAGATTTGG
ACGGATGTGGACGGCTTCATGACAGCCGACCCGCGTGTGATCAGTACGGCCTATACTATC
AGCGAGCTGACTTATGTAGAGGCTACCGAACTTTGTAATTTCGGTGCAAAAGTGGTGTAT
CCGCCTACCATCTATCCGGTATGTCACAAAAACATACCGATCCTGATTAAGAATACTTTC
AACCCGGATGCCCGGGGAACGGTGATCAAACAACACGTAGACCATACGAAGAGCAAAGCC
ATCAAAGGGATTTCGTCCATCAACGACACGAGCCTGATTACCGTACAGGGTTTAGGTATG
GTGGGCGTGATCGGTGTCAACTACCGCATCTTTAAGGCGCTGGCAAAGAATGGAATCAGT
GTGTTCCTCGTTTCGCAGGCTTCATCGGAGAACAGTACCTCTATCGGTGTGCGTAATGCC
GATGCCGATCTGGCTTGCGAAGTGCTGAACGAAGAGTTTGCCAAAGAGATCGAAATGGGT
GAGATTTCGCCTATCCAGGCAGAGAAGAACCTGGCTACGGTAGCTATCGTGGGTGAGAAC
ATGAAGCATACGCCGGGCATTGCCGGAAAGCTGTTCGGTACGCTGGGACGAAATGGCATC
AATGTGATAGCCTGTGCACAGGGAGCTTCTGAGACCAACATCTCGTTTGTTGTCGATTCA
AAGTCGTTGCGTAAATCGCTGAATGTGATTCACGACTCGTTCTTCCTCTCCGAATATCAG
GTGCTCAACCTCTTTATCTGCGGTGTGGGCACGGTGGGAGGAAGTCTTGTCGAGCAGATC
CGCCAGCAGCAGAAGAAGCTGATGGTGGAAAATGGCCTGAAACTCCATGTGGTAGGTATT
ATCGATGCGACGAAGGCGATGTTCAGCCGTGCCGGATTCGATCTGGCCAACTATCGCGAA
GAGCTGAAAGAGAAGGGAGTGGACAGTTCGCTGGATACTATACGTGACGAGATTATCGGC
ATGAATATATTCAATTCGGTATTTGTGGATTGTACGGCCAGTCCGGACATTGCCTCTCTA
TATAAGGACTTCCTGCAACATAACATTTCTGTGGTGGCGGCCAATAAGATTGCTGCTTCG
TCGGCTTACGAGAATTACCGTGAACTGAAGCTGATAGCCCGCCAGCGTGGTGTGAAATAT
CTGTTTGAAACCAACGTGGGGGCCGGACTTCCGATTATCAATACCATCAATGACCTGATA
CATAGCGGTGATAAGATTCTGAAGATCGAGGCAGTGCTTTCGGGTACGCTGAACTATATT
TTCAATAAGATCAGTGCCGATGTTCCCTTCAGCCGTACCATCAAGATGGCGCAGGAAGAG
CGTTATTCGGAACCCGATCCGCGCATTGACTTGAGCGGTAAGGACGTGATCCGTAAGCTC
GTGATCCTGGCGCGTGAGGCCGGATACAAGCTGGAACAGGAAGACGTGGAGAAAAATCTT
TTCGTACCGAATGACTTCTTTGAAGGTTCACTGGAAGACTTCTGGAAAAAAGTGCCTAGT
CTGGATGCTGATTTCGAAGCTCGCCGCAAGGTGCTCGAGAGTGAGAATAAACATTGGCGT
TTCGTTGCCAAGCTGGAGAACGGCAAAGCATCCGTCGGTTTGCAGGAAGTGGACCGCAAC
CATCCTTTCTACGGACTGGAAGGCAGCAATAACATCATCTTGCTTACCACCGAACGCTAT
AAAGAATATCCGATGATGATTCAGGGATACGGTGCGGGTGCCGGAGTGACGGCGGCCGGT
GTATTTGCTGACATTATGAGCATTGCAAACGTATAA
Enzyme 6 GenBank Gene ID AP006841 Link Image
Enzyme 6 GeneCard ID Not Available
Enzyme 6 GenAtlas ID Not Available
Enzyme 6 HGNC ID Not Available
Enzyme 6 Chromosome Location Not Available
Enzyme 6 Locus BF0608
Enzyme 6 SNPs Not Available
Enzyme 6 General References
  1. Kuwahara T, Yamashita A, Hirakawa H, Nakayama H, Toh H, Okada N, Kuhara S, Hattori M, Hayashi T, Ohnishi Y: Genomic analysis of Bacteroides fragilis reveals extensive DNA inversions regulating cell surface adaptation. Proc Natl Acad Sci U S A. 2004 Oct 12;101(41):14919-24. Epub 2004 Oct 4. [PubMed Link Image]
Enzyme 6 Metabolite References Not Available
Enzyme 7 [top]
Enzyme 7 ID 15484
Enzyme 7 Name Homoserine dehydrogenase
Enzyme 7 Synonyms Not Available
Enzyme 7 Gene Name hom1
Enzyme 7 Protein Sequence >Homoserine dehydrogenase 
MKIAILGYGTVGSGLIDLIENNTSKRDIEVVGILVKNKEKHKYKKYFDKITTDIEDIFDK
DIDILVEVIGGLNPAFDYVTRALNKKIHVVTANKDLLAEKGSDLIELANLNNVSIKFEAS
VAGGIPVLKPLIESLEGNNIKSINAILNGTCNFILSKMYDENLPYDVALKQAQELGFAEV
NPDADVLGYDSARKLSILSTLSYGKIVYWKDLLLEGITSIDEKDIEYAKKLNCKIKLVAR
SKYESGEVSGFVRPALVDNNNMLSKIDNEFNVVILVGDSVGELSFVGKGAGRGATGSAVY
ADIIDIIDNRSSNIKSFSKGKLDLSGLIEDECSAVVRFGGYNNKDGILECLDKYVDSYDI
IDDEELAIFVSAKSEHEIDRVLEIVKRNNYSESVKKLLKID
Enzyme 7 Number of Residues 401
Enzyme 7 Molecular Weight 44198.1
Enzyme 7 Theoretical pI 4.68
Enzyme 7 GO Classification
Function
  • NADP or NADPH binding
  • binding
  • catalytic activity
  • nucleotide binding
  • oxidoreductase activity
Process
  • cellular amino acid and derivative metabolic process
  • cellular amino acid metabolic process
  • cellular metabolic process
  • metabolic process
Component
—
Enzyme 7 General Function Involved in oxidoreductase activity
Enzyme 7 Specific Function L-homoserine + NAD(P)(+) = L-aspartate 4- semialdehyde + NAD(P)H
Enzyme 7 Pathways Not Available
Enzyme 7 Reactions
  • L-homoserine + NAD(P)+ = L-aspartate 4-semialdehyde + NAD(P)H + H+ [RN:R01773 R01775]
Enzyme 7 Pfam Domain Function
Enzyme 7 Signals
  • None
Enzyme 7 Transmembrane Regions
  • None
Enzyme 7 Essentiality Not Available
Enzyme 7 GenBank ID Protein 115249261 Link Image
Enzyme 7 UniProtKB/Swiss-Prot ID Q18B25 Link Image
Enzyme 7 UniProtKB/Swiss-Prot Entry Name Q18B25_CLOD6 Link Image
Enzyme 7 PDB ID Not Available
Enzyme 7 Cellular Location Not Available
Enzyme 7 Gene Sequence >1206 bp 
ATGAAGATACAAGCAGATTCTTATAATATTATTAAAGATATTGGGGATAGAAAAAGTTCA
TCTAAGAACAAAAATATAAAAAATAATAAATTTGAAGATAATCTATATAAGGCAACAGAC
CATAAAAAGGTTAAAGATAGAAGGGAAGTAAGTAAGCAAAATATTAGCTCAGATAAACCG
GAAAATAGTGATAATGAGTGTCATTTAGATGAAGATAAAAGTAATCACTTAGAAGATGAA
AATACATATGAAAAAGATTGTAGTAAGAATAATGAAGCTTTGCAGCAATTACTGAATCTT
TTAAAGGATAATTATAAAAAAGATAAAGATATAAACACTATATTGAATAATATAGAAAAA
CTAAGTATATCAGATGAATTAAAACAAGAACTTAAGCTTAATAAAAATATATTAAATAAG
ATTGCAAATCAAAATTCAGAGCTAAATAAAGCTAATATAAATAGCTCTAATGATATAGAA
AATTTAGACATAGTTAAATTAAGAGAACTTTTGGAAGATAATGCTAATAAAGATATTGAA
GTAATTACTAAAACTACAGAAAATGATACTAAAAATATAGATTTGTATAGTTTTGATAGC
AATAGAATGGATAATCTTAACTCAAATAAACAGAAAGATGATAGCTCTGATATTTTGGAA
AAACTAGCAGGGGTAAATGGAAATAAGAGTGGGAATTTTGGACAAGTAATAAATAAAAAT
GTTGATATGAATAAAATTAAAAATGATAATGTCAATTTAAAACAGATAGAATCAAATGTA
ATGGATGACTCTATAAAAGCTATTAAGCATATGAAAACAAATGATATACAAGAATTGACA
ATTAAATTAAGACCAAAAGAATTAGGAGATATGAATATACAATTGTTAAAAGATGGTGAA
AGTATGAGAGCTGTTGTGACTGTTTTCAATAAAGATGTCTTTGACTCTATAAATAAAAAC
ATAGCAGATTTAAAGCAACATCTTGAACTTACTAATGTAAATATAAAAGATGTATCAGTG
CAAATGCACAGCGATAATACAAATACATCTGATACCTTTGATAAAGCATTTGAACAACAG
AATAGACAAAATAACCAAGAAAACATGAGTAAGAAGAATACAAATGATAAGCATAATAAT
GTAGTCATAGAAGATGACATTAAAGAAAATATTATTGATGATGATAGAGTAGATTTACTA
GCTTAG
Enzyme 7 GenBank Gene ID AM180355 Link Image
Enzyme 7 GeneCard ID hom1 Link Image
Enzyme 7 GenAtlas ID Not Available
Enzyme 7 HGNC ID Not Available
Enzyme 7 Chromosome Location Not Available
Enzyme 7 Locus CD1166
Enzyme 7 SNPs SNPJam Report Link Image
Enzyme 7 General References
  1. Sebaihia M, Wren BW, Mullany P, Fairweather NF, Minton N, Stabler R, Thomson NR, Roberts AP, Cerdeno-Tarraga AM, Wang H, Holden MT, Wright A, Churcher C, Quail MA, Baker S, Bason N, Brooks K, Chillingworth T, Cronin A, Davis P, Dowd L, Fraser A, Feltwell T, Hance Z, Holroyd S, Jagels K, Moule S, Mungall K, Price C, Rabbinowitsch E, Sharp S, Simmonds M, Stevens K, Unwin L, Whithead S, Dupuy B, Dougan G, Barrell B, Parkhill J: The multidrug-resistant human pathogen Clostridium difficile has a highly mobile, mosaic genome. Nat Genet. 2006 Jul;38(7):779-86. Epub 2006 Jun 25. [PubMed Link Image]
Enzyme 7 Metabolite References Not Available
Enzyme 8 [top]
Enzyme 8 ID 15485
Enzyme 8 Name Homoserine dehydrogenase
Enzyme 8 Synonyms Not Available
Enzyme 8 Gene Name hom2
Enzyme 8 Protein Sequence >Homoserine dehydrogenase 
MENKVKIGVLGYGVVGSGLIDIIDNNKEKRNIEIVGILVNNLEKHKDKKYSNIITNNIDD
IFNKDIDILVEVMGGLEPSLSYIKKALNNKIHVVTANKDLLAECGDELAKLASENKVSIK
FEASVAGGIPVLKPIIESLEGNNIDSINAILNGTTNFILSKMYDENLSYDMALRQAQELG
FAEANPESDVLGYDAARKLSILSTLAYDNRVYWKDVYLEGITDIDEKDIEYAKKLNCKIK
LIGQSKYENDKVSAFVRPVLVEKDNILARIDNEFNAVIVNGDSVGEVSFVGKGAGSLATG
SAVYSDVIDIIDNRVSSIDSFTKDKIQVNKIVREKCGALLRFKKCNKDEILNIVENCLVK
FDILNDDDELAIMVYADSEYEINNSLCLIKDKGYCEKMNKMLKIS
Enzyme 8 Number of Residues 405
Enzyme 8 Molecular Weight 44975.1
Enzyme 8 Theoretical pI 4.65
Enzyme 8 GO Classification
Function
  • NADP or NADPH binding
  • binding
  • catalytic activity
  • homoserine dehydrogenase activity
  • nucleotide binding
  • oxidoreductase activity
  • oxidoreductase activity, acting on CH-OH group of donors
  • oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
Process
  • cellular amino acid and derivative metabolic process
  • cellular amino acid metabolic process
  • cellular metabolic process
  • metabolic process
  • oxidation reduction
Component
—
Enzyme 8 General Function Involved in oxidoreductase activity
Enzyme 8 Specific Function L-homoserine + NAD(P)(+) = L-aspartate 4- semialdehyde + NAD(P)H
Enzyme 8 Pathways Not Available
Enzyme 8 Reactions
  • L-homoserine + NAD(P)+ = L-aspartate 4-semialdehyde + NAD(P)H + H+ [RN:R01773 R01775]
Enzyme 8 Pfam Domain Function
Enzyme 8 Signals
  • None
Enzyme 8 Transmembrane Regions
  • None
Enzyme 8 Essentiality Not Available
Enzyme 8 GenBank ID Protein 115250091 Link Image
Enzyme 8 UniProtKB/Swiss-Prot ID Q186D4 Link Image
Enzyme 8 UniProtKB/Swiss-Prot Entry Name Q186D4_CLOD6 Link Image
Enzyme 8 PDB ID Not Available
Enzyme 8 Cellular Location Not Available
Enzyme 8 Gene Sequence >1218 bp 
ATGCAAGATTATAAAAAAAATAAAAGAAGAATGATGAATCAGCCAATGTCTACAATGAAT
GAAGAAGAAGTGTATACAGATGAAATAAATTCAGAAGACATGAGAGGTTTTAAAAAATCA
CACCATCATAATGGATGTAATACTGATAATAAGTGTGAGTGCCATGATGATTGCAATCCA
TGCAACCCATGTAATCCATGTAAACCTAACCCATGCAATCCATGCAAACCTAATCCATGT
GATGACAATTGTGGATGCCATGACAATTGTAAATGTGATTGTGAACCATGTGAAATGGAT
TCAGATGAATGTTTTGAAAACAAATGTGGACCAGAATGCTGTAATCCTATATCTCCAAGA
AACTTCTCTGTATCAAATGCAGTGCCATTTGCAATAGAGGCTAATAGAATATTTGATACT
ATGCAATTCCAAACATTTACAGATGCAACAGGACCAAATGGAGAGCCATTAACTTTTGAA
ACAGAAGTAGTAGAAGTATTTGGTTCAGTTCCAAGTGCAGGTCAAGCAAGTGTAACTATA
GAAAAAATATGCTTAAGTAATGATGGAATCGTTATAGACACAGGAATGACAACTTTAGAA
GATTTCGATTTAGACCCATTAGGAGATATAGTAGGAAGAAACTGTGAAACAACTTTTGAA
TTTGCAGTTTGTGGAGAAAGAAACTCTGAGTGCTGTAGACAAGGAAAAGGCAAATCAGTA
GCTTATAAACAAAGAGGATTAACTGTAGCAGTTCGTAATTTAGTACTAGAGCTAAGAGGT
AGATGTGGATGTACAGAGTTCGTTGCATTAGCTTTCCCAGCAGTTAGAGCAGGAGGTGGA
TGTAAGAGAAGAGTTGATTATGTAGAATTTACTTTTAACACACTTTCAGCACCAATATGC
TTGCCAGCTGACGGAAGAGCTGTTACTTTAAGACAAGAATATCAAACTAACTTAACTGTA
GATTGTATAGGAAAATCTATATTAAAATTAGAATGCAACGAATGTTGTGAACCTTTCTAT
GAATTAATTATACCAAATGATATAGATTTAGTACTTTGCTTACAAGAAACAGTTAGCACA
TTAATAAGTGAACAAATAGTAGTTTTAGCATCACCAAATCCAATCCAACCAAGACTTGTT
GATACTTTCTCTAAAGTATGTGATTTTTCGCAATGTGGACCTAATCATGGAAGTGGAAAG
CCAAGTTGCCACAGATAG
Enzyme 8 GenBank Gene ID AM180355 Link Image
Enzyme 8 GeneCard ID hom2 Link Image
Enzyme 8 GenAtlas ID Not Available
Enzyme 8 HGNC ID Not Available
Enzyme 8 Chromosome Location Not Available
Enzyme 8 Locus CD1580
Enzyme 8 SNPs SNPJam Report Link Image
Enzyme 8 General References
  1. Sebaihia M, Wren BW, Mullany P, Fairweather NF, Minton N, Stabler R, Thomson NR, Roberts AP, Cerdeno-Tarraga AM, Wang H, Holden MT, Wright A, Churcher C, Quail MA, Baker S, Bason N, Brooks K, Chillingworth T, Cronin A, Davis P, Dowd L, Fraser A, Feltwell T, Hance Z, Holroyd S, Jagels K, Moule S, Mungall K, Price C, Rabbinowitsch E, Sharp S, Simmonds M, Stevens K, Unwin L, Whithead S, Dupuy B, Dougan G, Barrell B, Parkhill J: The multidrug-resistant human pathogen Clostridium difficile has a highly mobile, mosaic genome. Nat Genet. 2006 Jul;38(7):779-86. Epub 2006 Jun 25. [PubMed Link Image]
Enzyme 8 Metabolite References Not Available
Enzyme 9 [top]
Enzyme 9 ID 15486
Enzyme 9 Name Homoserine dehydrogenase
Enzyme 9 Synonyms Not Available
Enzyme 9 Gene Name hom
Enzyme 9 Protein Sequence >Homoserine dehydrogenase 
MKDTLKIGLLGLGTVGTGVLTLLKEHQEKISQVTGMNVVIEKAFVRNLETKQAQAEEYGL
SLTTSIDDILEDKEIQIVVELMGTIEPAKTYIMKALEKGKHIVTANKDLLAQHGSELVAL
AQKHHCDLYYEASVAGGIPILRTIANSLAADNIQQVLGIVNGTTNYMLTQMVSADKSYEE
ALAEAQALGFAEADPTNDVDGIDAAYKMVILSQFAFGMNVSLPQVDIRGIRGLSLDDVAM
AKQLGYEIKLIGSAEQNENSISVEVAPMLVNQKHPIASVRNEYNAVFIKSAGVGESMYYG
PGAGAKPTATSVVSDLITIAKNIRLATTGHMFNSYQHKTQLTSSENVFGQYYFSLDVPDT
PGQFLQLTQLMTKAEVSFDQLVQQKSDGQRARIVAITHQISKAQMQQVVIAIQNTEAFQL
LNVMKVIGDE
Enzyme 9 Number of Residues 430
Enzyme 9 Molecular Weight 46742.2
Enzyme 9 Theoretical pI 4.94
Enzyme 9 GO Classification
Function
  • NADP or NADPH binding
  • binding
  • catalytic activity
  • homoserine dehydrogenase activity
  • nucleotide binding
  • oxidoreductase activity
  • oxidoreductase activity, acting on CH-OH group of donors
  • oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
Process
  • cellular amino acid and derivative metabolic process
  • cellular amino acid metabolic process
  • cellular metabolic process
  • metabolic process
  • oxidation reduction
Component
—
Enzyme 9 General Function Involved in oxidoreductase activity
Enzyme 9 Specific Function L-homoserine + NAD(P)(+) = L-aspartate 4- semialdehyde + NAD(P)H
Enzyme 9 Pathways Not Available
Enzyme 9 Reactions
  • L-homoserine + NAD(P)+ = L-aspartate 4-semialdehyde + NAD(P)H + H+ [RN:R01773 R01775]
Enzyme 9 Pfam Domain Function
Enzyme 9 Signals
  • None
Enzyme 9 Transmembrane Regions
  • None
Enzyme 9 Essentiality Not Available
Enzyme 9 GenBank ID Protein 29342132 Link Image
Enzyme 9 UniProtKB/Swiss-Prot ID Q831S8 Link Image
Enzyme 9 UniProtKB/Swiss-Prot Entry Name Q831S8_ENTFA Link Image
Enzyme 9 PDB ID Not Available
Enzyme 9 Cellular Location Not Available
Enzyme 9 Gene Sequence >1293 bp 
ATGTCATCAGTAGTAGTTGTTGGAACGCAATGGGGCGATGAAGGTAAAGGAAAAATTACA
GACTTTCTAAGTGAAAACGCAGAAGTGATCGCTCGTTACCAAGGCGGAGATAACGCCGGA
CATACCATTAAATTCGACGGCGTAACGTATAAATTACATTTAATTCCTTCAGGGATTTTC
TATAAAGAAAAAATTAGTGTAATTGGTAACGGCGTAGTTGTGAATCCAAAATCTTTAGTA
AAAGAATTAGCTTATTTAAAAGAAAATAATGTTGCCACTGATAATTTACGTATTTCAGAT
CGTGCCCATGTCATCTTGCCGTATCATATTAAATTGGATCAATTGCAAGAAGATGCGAAA
GGTGAAAACAAGATTGGGACAACGATTAAAGGAATTGGCCCAGCCTACATGGATAAAGCA
GCACGGGTGGGAATCCGTATCGCTGATTTATTGGATAAAGAAATTTTTGCGGAACGTTTG
CAAATTAACTTAGAAGAAAAAAATCGTCAATTCGTTAAAATGTTTGATAGCGAAGCCATT
GAATTTGATGATATTTTTGAAGAATACTATGAATACGGACAACAAATTAAACAATATGTT
ACAGATACTTCGGTTATTTTAAACGATGCATTAGATGCTGGAAAACGGGTTTTATTTGAA
GGGGCACAAGGTGTCATGTTGGATATCGATCAAGGAACCTATCCATTTGTTACTTCCTCT
AATCCAGTAGCTGGTGGCGTAACTATCGGTAGTGGCGTTGGTCCATCAAAAATTAATAAA
GTGGTTGGTGTCTGCAAAGCGTACACTTCACGTGTCGGTGACGGCCCATTCCCAACAGAA
TTATTTGATGAAACAGGAGAAACCATTCGTCGTGTCGGTAAAGAATACGGAACAACAACA
GGACGTCCGCGTCGTGTCGGTTGGTTTGATTCAGTAGTCATGCGTCATTCAAAACGTGTA
TCAGGGATTACAAACTTGTCATTAAACTCGATTGACGTGTTAAGTGGTTTAGAAACGGTG
AAAATTTGTACAGCTTATGAACTTGATGGTGAATTAATTTATCATTATCCAGCAAGCTTG
AAAGAATTAAGCCGCTGTAAACCAGTTTATGAAGAATTACCAGGTTGGTCTGAAGATATC
ACTGGTTGCAAAACTTTAGCCGATTTACCAGCTAATGCTCGTAACTATGTGCATCGGATT
TCAGAATTAGTTGGTGTGCGCATTTCAACATTCTCTGTAGGTCCAGACCGTAACCAAACG
AACGTTTTAGAAAGCGTTTGGGCACAAATTTAA
Enzyme 9 GenBank Gene ID AE016830 Link Image
Enzyme 9 GeneCard ID hom Link Image
Enzyme 9 GenAtlas ID Not Available
Enzyme 9 HGNC ID Not Available
Enzyme 9 Chromosome Location Not Available
Enzyme 9 Locus EF_2422
Enzyme 9 SNPs SNPJam Report Link Image
Enzyme 9 General References
  1. Paulsen IT, Banerjei L, Myers GS, Nelson KE, Seshadri R, Read TD, Fouts DE, Eisen JA, Gill SR, Heidelberg JF, Tettelin H, Dodson RJ, Umayam L, Brinkac L, Beanan M, Daugherty S, DeBoy RT, Durkin S, Kolonay J, Madupu R, Nelson W, Vamathevan J, Tran B, Upton J, Hansen T, Shetty J, Khouri H, Utterback T, Radune D, Ketchum KA, Dougherty BA, Fraser CM: Role of mobile DNA in the evolution of vancomycin-resistant Enterococcus faecalis. Science. 2003 Mar 28;299(5615):2071-4. [PubMed Link Image]
Enzyme 9 Metabolite References Not Available
Enzyme 10 [top]
Enzyme 10 ID 15487
Enzyme 10 Name Bifunctional aspartokinase/homoserine dehydrogenase 1
Enzyme 10 Synonyms
  1. Aspartokinase I/homoserine dehydrogenase I
  2. AKI-HDI
  3. Aspartokinase
  4. Homoserine dehydrogenase
Enzyme 10 Gene Name thrA
Enzyme 10 Protein Sequence >Bifunctional aspartokinase/homoserine dehydrogenase 1 
MRVLKFGGTSVANAERFLRVADILESNARQGQVATVLSAPAKITNHLVAMIEKTISGQDA
LPNISDAERIFAELLTGLAAAQPGFPLAQLKTFVDQEFAQIKHVLHGISLLGQCPDSINA
ALICRGEKMSIAIMAGVLEARGHNVTVIDPVEKLLAVGHYLESTVDIAESTRRIAASRIP
ADHMVLMAGFTAGNEKGELVVLGRNGSDYSAAVLAACLRADCCEIWTDVDGVYTCDPRQV
PDARLLKSMSYQEAMELSYFGAKVLHPRTITPIAQFQIPCLIKNTGNPQAPGTLIGASRD
EDELPVKGISNLNNMAMFSVSGPGMKGMVGMAARVFAAMSRARISVVLITQSSSEYSISF
CVPQSDCVRAERAMQEEFYLELKEGLLEPLAVTERLAIISVVGDGMRTLRGISAKFFAAL
ARANINIVAIAQGSSERSISVVVNNDDATTGVRVTHQMLFNTDQVIEVFVIGVGGVGGAL
LEQLKRQQSWLKNKHIDLRVCGVANSKALLTNVHGLNLENWQEELAQAKEPFNLGRLIRL
VKEYHLLNPVIVDCTSSQAVADQYADFLREGFHVVTPNKKANTSSMDYYHQLRYAAEKSR
RKFLYDTNVGAGLPVIENLQNLLNAGDELMKFSGILSGSLSYIFGKLDEGMSFSEATTLA
REMGYTEPDPRDDLSGMDVARKLLILARETGRELELADIEIEPVLPAEFNAEGDVAAFMA
NLSQLDDLFAARVAKARDEGKVLRYVGNIDEDGVCRVKIAEVDGNDPLFKVKNGENALAF
YSHYYQPLPLVLRGYGAGNDVTAAGVFADLLRTLSWKLGV
Enzyme 10 Number of Residues 820
Enzyme 10 Molecular Weight 89119.4
Enzyme 10 Theoretical pI 5.39
Enzyme 10 GO Classification
Function
  • NADP or NADPH binding
  • amino acid binding
  • aspartate kinase activity
  • binding
  • carboxylic acid binding
  • catalytic activity
  • homoserine dehydrogenase activity
  • nucleotide binding
  • oxidoreductase activity
  • oxidoreductase activity, acting on CH-OH group of donors
  • oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
  • phosphotransferase activity, carboxyl group as acceptor
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • aspartate family amino acid biosynthetic process
  • cellular amino acid and derivative metabolic process
  • cellular amino acid biosynthetic process
  • cellular amino acid metabolic process
  • cellular metabolic process
  • metabolic process
  • oxidation reduction
Component
—
Enzyme 10 General Function Involved in amino acid binding
Enzyme 10 Specific Function L-homoserine + NAD(P)(+) = L-aspartate 4- semialdehyde + NAD(P)H
Enzyme 10 Pathways Not Available
Enzyme 10 Reactions
  • ATP + L-aspartate = ADP + 4-phospho-L-aspartate [RN:R00480]
Enzyme 10 Pfam Domain Function
Enzyme 10 Signals
  • None
Enzyme 10 Transmembrane Regions
  • None
Enzyme 10 Essentiality Not Available
Enzyme 10 GenBank ID Protein 85674276 Link Image
Enzyme 10 UniProtKB/Swiss-Prot ID P00561 Link Image
Enzyme 10 UniProtKB/Swiss-Prot Entry Name AK1H_ECOLI Link Image
Enzyme 10 PDB ID Not Available
Enzyme 10 Cellular Location Not Available
Enzyme 10 Gene Sequence >2463 bp 
ATGCGAGTGTTGAAGTTCGGCGGTACATCAGTGGCAAATGCAGAACGTTTTCTGCGTGTT
GCCGATATTCTGGAAAGCAATGCCAGGCAGGGGCAGGTGGCCACCGTCCTCTCTGCCCCC
GCCAAAATCACCAACCACCTGGTGGCGATGATTGAAAAAACCATTAGCGGCCAGGATGCT
TTACCCAATATCAGCGATGCCGAACGTATTTTTGCCGAACTTTTGACGGGACTCGCCGCC
GCCCAGCCGGGGTTCCCGCTGGCGCAATTGAAAACTTTCGTCGATCAGGAATTTGCCCAA
ATAAAACATGTCCTGCATGGCATTAGTTTGTTGGGGCAGTGCCCGGATAGCATCAACGCT
GCGCTGATTTGCCGTGGCGAGAAAATGTCGATCGCCATTATGGCCGGCGTATTAGAAGCG
CGCGGTCACAACGTTACTGTTATCGATCCGGTCGAAAAACTGCTGGCAGTGGGGCATTAC
CTCGAATCTACCGTCGATATTGCTGAGTCCACCCGCCGTATTGCGGCAAGCCGCATTCCG
GCTGATCACATGGTGCTGATGGCAGGTTTCACCGCCGGTAATGAAAAAGGCGAACTGGTG
GTGCTTGGACGCAACGGTTCCGACTACTCTGCTGCGGTGCTGGCTGCCTGTTTACGCGCC
GATTGTTGCGAGATTTGGACGGACGTTGACGGGGTCTATACCTGCGACCCGCGTCAGGTG
CCCGATGCGAGGTTGTTGAAGTCGATGTCCTACCAGGAAGCGATGGAGCTTTCCTACTTC
GGCGCTAAAGTTCTTCACCCCCGCACCATTACCCCCATCGCCCAGTTCCAGATCCCTTGC
CTGATTAAAAATACCGGAAATCCTCAAGCACCAGGTACGCTCATTGGTGCCAGCCGTGAT
GAAGACGAATTACCGGTCAAGGGCATTTCCAATCTGAATAACATGGCAATGTTCAGCGTT
TCTGGTCCGGGGATGAAAGGGATGGTCGGCATGGCGGCGCGCGTCTTTGCAGCGATGTCA
CGCGCCCGTATTTCCGTGGTGCTGATTACGCAATCATCTTCCGAATACAGCATCAGTTTC
TGCGTTCCACAAAGCGACTGTGTGCGAGCTGAACGGGCAATGCAGGAAGAGTTCTACCTG
GAACTGAAAGAAGGCTTACTGGAGCCGCTGGCAGTGACGGAACGGCTGGCCATTATCTCG
GTGGTAGGTGATGGTATGCGCACCTTGCGTGGGATCTCGGCGAAATTCTTTGCCGCACTG
GCCCGCGCCAATATCAACATTGTCGCCATTGCTCAGGGATCTTCTGAACGCTCAATCTCT
GTCGTGGTAAATAACGATGATGCGACCACTGGCGTGCGCGTTACTCATCAGATGCTGTTC
AATACCGATCAGGTTATCGAAGTGTTTGTGATTGGCGTCGGTGGCGTTGGCGGTGCGCTG
CTGGAGCAACTGAAGCGTCAGCAAAGCTGGCTGAAGAATAAACATATCGACTTACGTGTC
TGCGGTGTTGCCAACTCGAAGGCTCTGCTCACCAATGTACATGGCCTTAATCTGGAAAAC
TGGCAGGAAGAACTGGCGCAAGCCAAAGAGCCGTTTAATCTCGGGCGCTTAATTCGCCTC
GTGAAAGAATATCATCTGCTGAACCCGGTCATTGTTGACTGCACTTCCAGCCAGGCAGTG
GCGGATCAATATGCCGACTTCCTGCGCGAAGGTTTCCACGTTGTCACGCCGAACAAAAAG
GCCAACACCTCGTCGATGGATTACTACCATCAGTTGCGTTATGCGGCGGAAAAATCGCGG
CGTAAATTCCTCTATGACACCAACGTTGGGGCTGGATTACCGGTTATTGAGAACCTGCAA
AATCTGCTCAATGCAGGTGATGAATTGATGAAGTTCTCCGGCATTCTTTCTGGTTCGCTT
TCTTATATCTTCGGCAAGTTAGACGAAGGCATGAGTTTCTCCGAGGCGACCACGCTGGCG
CGGGAAATGGGTTATACCGAACCGGACCCGCGAGATGATCTTTCTGGTATGGATGTGGCG
CGTAAACTATTGATTCTCGCTCGTGAAACGGGACGTGAACTGGAGCTGGCGGATATTGAA
ATTGAACCTGTGCTGCCCGCAGAGTTTAACGCCGAGGGTGATGTTGCCGCTTTTATGGCG
AATCTGTCACAACTCGACGATCTCTTTGCCGCGCGCGTGGCGAAGGCCCGTGATGAAGGA
AAAGTTTTGCGCTATGTTGGCAATATTGATGAAGATGGCGTCTGCCGCGTGAAGATTGCC
GAAGTGGATGGTAATGATCCGCTGTTCAAAGTGAAAAATGGCGAAAACGCCCTGGCCTTC
TATAGCCACTATTATCAGCCGCTGCCGTTGGTACTGCGCGGATATGGTGCGGGCAATGAC
GTTACAGCTGCCGGTGTCTTTGCTGATCTGCTACGTACCCTCTCATGGAAGTTAGGAGTC
TGA
Enzyme 10 GenBank Gene ID AP009048 Link Image
Enzyme 10 GeneCard ID thrA Link Image
Enzyme 10 GenAtlas ID Not Available
Enzyme 10 HGNC ID Not Available
Enzyme 10 Chromosome Location 1
Enzyme 10 Locus 17q11.2
Enzyme 10 SNPs SNPJam Report Link Image
Enzyme 10 General References
  1. Katinka M, Cossart P, Sibilli L, Saint-Girons I, Chalvignac MA, Le Bras G, Cohen GN, Yaniv M: Nucleotide sequence of the thrA gene of Escherichia coli. Proc Natl Acad Sci U S A. 1980 Oct;77(10):5730-3. [PubMed Link Image]
  2. Yura T, Mori H, Nagai H, Nagata T, Ishihama A, Fujita N, Isono K, Mizobuchi K, Nakata A: Systematic sequencing of the Escherichia coli genome: analysis of the 0-2.4 min region. Nucleic Acids Res. 1992 Jul 11;20(13):3305-8. [PubMed Link Image]
  3. Burland V, Plunkett G 3rd, Sofia HJ, Daniels DL, Blattner FR: Analysis of the Escherichia coli genome VI: DNA sequence of the region from 92.8 through 100 minutes. Nucleic Acids Res. 1995 Jun 25;23(12):2105-19. [PubMed Link Image]
  4. Blattner FR, Plunkett G 3rd, Bloch CA, Perna NT, Burland V, Riley M, Collado-Vides J, Glasner JD, Rode CK, Mayhew GF, Gregor J, Davis NW, Kirkpatrick HA, Goeden MA, Rose DJ, Mau B, Shao Y: The complete genome sequence of Escherichia coli K-12. Science. 1997 Sep 5;277(5331):1453-74. [PubMed Link Image]
  5. Hayashi K, Morooka N, Yamamoto Y, Fujita K, Isono K, Choi S, Ohtsubo E, Baba T, Wanner BL, Mori H, Horiuchi T: Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110. Mol Syst Biol. 2006;2:2006.0007. Epub 2006 Feb 21. [PubMed Link Image]
  6. Gardner JF: Initiation, pausing, and termination of transcription in the threonine operon regulatory region of Escherichia coli. J Biol Chem. 1982 Apr 10;257(7):3896-904. [PubMed Link Image]
  7. Lynn SP, Bauer CE, Chapman K, Gardner JF: Identification and characterization of mutants affecting transcription termination at the threonine operon attenuator. J Mol Biol. 1985 Jun 25;183(4):529-41. [PubMed Link Image]
  8. Sibilli L, Le Bras G, Cossart P, Chalvignac MA, Le Bras G, Briley PA, Cohen GN: The primary structure of Escherichia coli K 12 aspartokinase I-homoserine dehydrogenase I : sequence of cyanogen bromide peptide CB 3. Biochimie. 1979;61(5-6):733-9. [PubMed Link Image]
  9. Zakin MM, Duchange N, Ferrara P, Cohen GN: Nucleotide sequence of the metL gene of Escherichia coli. Its product, the bifunctional aspartokinase ii-homoserine dehydrogenase II, and the bifunctional product of the thrA gene, aspartokinase I-homoserine dehydrogenase I, derive from a common ancestor. J Biol Chem. 1983 Mar 10;258(5):3028-31. [PubMed Link Image]
  10. Cossart P, Katinka M, Yaniv M, Saint Girons I, Cohen GN: Construction and expression of a hybrid plasmid containing the Escherichia coli thrA and thrB genes. Mol Gen Genet. 1979 Aug;175(1):39-44. [PubMed Link Image]
Enzyme 10 Metabolite References Not Available
Enzyme 11 [top]
Enzyme 11 ID 15488
Enzyme 11 Name Bifunctional aspartokinase/homoserine dehydrogenase 2
Enzyme 11 Synonyms
  1. Aspartokinase II/homoserine dehydrogenase II
  2. AKII-HDII
  3. Aspartokinase
  4. Homoserine dehydrogenase
Enzyme 11 Gene Name metL
Enzyme 11 Protein Sequence >Bifunctional aspartokinase/homoserine dehydrogenase 2 
MSVIAQAGAKGRQLHKFGGSSLADVKCYLRVAGIMAEYSQPDDMMVVSAAGSTTNQLINW
LKLSQTDRLSAHQVQQTLRRYQCDLISGLLPAEEADSLISAFVSDLERLAALLDSGINDA
VYAEVVGHGEVWSARLMSAVLNQQGLPAAWLDAREFLRAERAAQPQVDEGLSYPLLQQLL
VQHPGKRLVVTGFISRNNAGETVLLGRNGSDYSATQIGALAGVSRVTIWSDVAGVYSADP
RKVKDACLLPLLRLDEASELARLAAPVLHARTLQPVSGSEIDLQLRCSYTPDQGSTRIER
VLASGTGARIVTSHDDVCLIEFQVPASQDFKLAHKEIDQILKRAQVRPLAVGVHNDRQLL
QFCYTSEVADSALKILDEAGLPGELRLRQGLALVAMVGAGVTRNPLHCHRFWQQLKGQPV
EFTWQSDDGISLVAVLRTGPTESLIQGLHQSVFRAEKRIGLVLFGKGNIGSRWLELFARE
QSTLSARTGFEFVLAGVVDSRRSLLSYDGLDASRALAFFNDEAVEQDEESLFLWMRAHPY
DDLVVLDVTASQQLADQYLDFASHGFHVISANKLAGASDSNKYRQIHDAFEKTGRHWLYN
ATVGAGLPINHTVRDLIDSGDTILSISGIFSGTLSWLFLQFDGSVPFTELVDQAWQQGLT
EPDPRDDLSGKDVMRKLVILAREAGYNIEPDQVRVESLVPAHCEGGSIDHFFENGDELNE
QMVQRLEAAREMGLVLRYVARFDANGKARVGVEAVREDHPLASLLPCDNVFAIESRWYRD
NPLVIRGPGAGRDVTAGAIQSDINRLAQLL
Enzyme 11 Number of Residues 810
Enzyme 11 Molecular Weight 88886.8
Enzyme 11 Theoretical pI 5.27
Enzyme 11 GO Classification
Function
  • NADP or NADPH binding
  • aspartate kinase activity
  • binding
  • catalytic activity
  • homoserine dehydrogenase activity
  • nucleotide binding
  • oxidoreductase activity
  • oxidoreductase activity, acting on CH-OH group of donors
  • oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
  • phosphotransferase activity, carboxyl group as acceptor
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • aspartate family amino acid biosynthetic process
  • cellular amino acid and derivative metabolic process
  • cellular amino acid biosynthetic process
  • cellular amino acid metabolic process
  • cellular metabolic process
  • metabolic process
  • oxidation reduction
Component
—
Enzyme 11 General Function Involved in cellular amino acid biosynthetic process
Enzyme 11 Specific Function L-homoserine + NAD(P)(+) = L-aspartate 4- semialdehyde + NAD(P)H
Enzyme 11 Pathways Not Available
Enzyme 11 Reactions
  • ATP + L-aspartate = ADP + 4-phospho-L-aspartate [RN:R00480]
Enzyme 11 Pfam Domain Function
Enzyme 11 Signals
  • None
Enzyme 11 Transmembrane Regions
  • None
Enzyme 11 Essentiality Not Available
Enzyme 11 GenBank ID Protein 85674369 Link Image
Enzyme 11 UniProtKB/Swiss-Prot ID P00562 Link Image
Enzyme 11 UniProtKB/Swiss-Prot Entry Name AK2H_ECOLI Link Image
Enzyme 11 PDB ID Not Available
Enzyme 11 Cellular Location Not Available
Enzyme 11 Gene Sequence >2433 bp 
ATGGCGATGAAAAAGTTGCTCATAGCGTCGCTGCTGTTTAGCAGCGCCACCGTATACGGT
GCTGAAGGGTTCGTAGTGAAAGATATTCATTTCGAAGGCCTTCAGCGTGTCGCCGTTGGT
GCGGCCCTCCTCAGTATGCCGGTGCGCACAGGCGACACGGTTAATGATGAAGATATCAGT
AATACCATTCGCGCTCTGTTTGCTACCGGCAACTTTGAGGATGTTCGCGTCCTTCGTGAT
GGTGATACCCTTCTGGTTCAGGTAAAAGAACGTCCGACCATTGCCAGCATTACTTTCTCC
GGTAACAAATCGGTGAAAGATGACATGCTGAAGCAAAACCTCGAGGCTTCTGGTGTGCGT
GTGGGCGAATCCCTCGATCGCACCACCATTGCCGATATCGAGAAAGGTCTGGAAGACTTC
TACTACAGCGTCGGTAAATATAGCGCCAGCGTAAAAGCTGTCGTGACCCCGCTGCCGCGC
AACCGTGTTGACCTAAAACTGGTGTTCCAGGAAGGTGTGTCAGCTGAAATCCAGCAAATT
AACATTGTTGGTAACCATGCTTTCACCACCGACGAACTGATCTCTCATTTCCAACTGCGT
GACGAAGTGCCGTGGTGGAACGTGGTAGGCGATCGTAAATACCAGAAACAGAAACTGGCG
GGCGACCTTGAAACCCTGCGCAGCTACTATCTGGATCGCGGTTATGCCCGTTTCAACATC
GACTCTACCCAGGTCAGTCTGACGCCAGATAAAAAAGGTATTTACGTCACGGTGAACATC
ACCGAAGGCGATCAGTACAAGCTTTCTGGCGTTGAAGTGAGCGGCAACCTTGCCGGGCAC
TCCGCTGAAATTGAGCAGCTGACTAAGATCGAGCCGGGTGAGCTGTATAACGGCACCAAA
GTGACCAAGATGGAAGATGACATCAAAAAGCTTCTCGGTCGCTATGGTTATGCCTATCCG
CGCGTACAGTCGATGCCCGAAATTAACGATGCCGACAAAACCGTTAAATTACGTGTGAAC
GTTGATGCGGGTAACCGTTTCTACGTGCGTAAGATCCGTTTTGAAGGTAACGATACCTCG
AAAGATGCCGTCCTGCGTCGCGAAATGCGTCAGATGGAAGGTGCATGGCTGGGGAGCGAT
CTGGTCGATCAGGGTAAGGAGCGTCTGAATCGTCTGGGCTTCTTTGAAACTGTCGATACC
GATACCCAACGTGTTCCGGGTAGCCCGGACCAGGTTGATGTCGTCTACAAGGTAAAAGAG
CGCAACACCGGTAGCTTCAACTTTGGTATTGGTTACGGTACTGAAAGTGGCGTGAGCTTC
CAGGCTGGTGTGCAGCAGGATAACTGGTTAGGTACAGGTTATGCTGTTGGTATCAACGGG
ACCAAAAACGATTACCAGACCTATGCTGAACTGTCGGTAACCAACCCGTACTTCACCGTA
GATGGCGTAAGCCTCGGTGGTCGTCTCTTCTATAATGACTTCCAGGCAGATGACGCCGAC
CTGTCCGACTATACCAACAAGAGTTATGGTACAGACGTGACGTTGGGCTTCCCGATTAAC
GAATATAACTCGCTGCGTGCAGGTCTGGGTTATGTACATAACTCCCTGTCCAACATGCAG
CCTCAGGTTGCGATGTGGCGTTATCTGTACTCTATGGGTGAACATCCGAGCACCTCTGAT
CAGGATAACAGCTTCAAAACGGACGACTTCACGTTCAACTATGGTTGGACCTATAACAAG
CTTGACCGTGGTTACTTCCCGACAGATGGTTCACGTGTCAACCTGACCGGTAAAGTGACC
ATTCCTGGATCGGATAACGAATACTACAAAGTGACGTTAGACACGGCGACTTATGTGCCG
ATCGATGACGATCACAAATGGGTTGTTCTGGGGCGTACCCGCTGGGGTTATGGTGATGGT
TTAGGCGGCAAAGAGATGCCGTTCTACGAGAACTTCTATGCCGGTGGTTCCAGCACCGTG
CGTGGCTTCCAGTCCAATACCATTGGTCCGAAAGCAGTTTACTTCCCGCATCAGGCCAGT
AATTATGATCCGGACTATGATTACGAATGTGCGACTCAGGACGGCGCGAAAGACCTGTGT
AAATCGGATGATGCTGTAGGCGGTAACGCCATGGCGGTTGCCAGCCTCGAGTTCATCACC
CCGACGCCGTTTATTAGCGATAAGTATGCTAACTCGGTTCGTACTTCCTTCTTCTGGGAT
ATGGGTACCGTTTGGGATACAAACTGGGATTCCAGCCAATATTCTGGATATCCGGACTAT
AGTGATCCAAGCAATATCCGTATGTCTGCGGGTATCGCATTACAATGGATGTCCCCATTG
GGGCCGTTGGTGTTCTCCTACGCCCAGCCGTTCAAAAAGTACGATGGAGACAAGGCAGAA
CAGTTCCAGTTTAACATCGGTAAAACCTGGTAA
Enzyme 11 GenBank Gene ID AP009048 Link Image
Enzyme 11 GeneCard ID metL Link Image
Enzyme 11 GenAtlas ID Not Available
Enzyme 11 HGNC ID Not Available
Enzyme 11 Chromosome Location Not Available
Enzyme 11 Locus b3940
Enzyme 11 SNPs SNPJam Report Link Image
Enzyme 11 General References
  1. Zakin MM, Duchange N, Ferrara P, Cohen GN: Nucleotide sequence of the metL gene of Escherichia coli. Its product, the bifunctional aspartokinase ii-homoserine dehydrogenase II, and the bifunctional product of the thrA gene, aspartokinase I-homoserine dehydrogenase I, derive from a common ancestor. J Biol Chem. 1983 Mar 10;258(5):3028-31. [PubMed Link Image]
  2. Plunkett G 3rd, Burland V, Daniels DL, Blattner FR: Analysis of the Escherichia coli genome. III. DNA sequence of the region from 87.2 to 89.2 minutes. Nucleic Acids Res. 1993 Jul 25;21(15):3391-8. [PubMed Link Image]
  3. Blattner FR, Plunkett G 3rd, Bloch CA, Perna NT, Burland V, Riley M, Collado-Vides J, Glasner JD, Rode CK, Mayhew GF, Gregor J, Davis NW, Kirkpatrick HA, Goeden MA, Rose DJ, Mau B, Shao Y: The complete genome sequence of Escherichia coli K-12. Science. 1997 Sep 5;277(5331):1453-74. [PubMed Link Image]
  4. Hayashi K, Morooka N, Yamamoto Y, Fujita K, Isono K, Choi S, Ohtsubo E, Baba T, Wanner BL, Mori H, Horiuchi T: Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110. Mol Syst Biol. 2006;2:2006.0007. Epub 2006 Feb 21. [PubMed Link Image]
Enzyme 11 Metabolite References Not Available
Enzyme 12 [top]
Enzyme 12 ID 15489
Enzyme 12 Name Homoserine O-succinyltransferase
Enzyme 12 Synonyms Not Available
Enzyme 12 Gene Name metA
Enzyme 12 Protein Sequence >Homoserine O-succinyltransferase 
MTVTANNGLLVARGEWANATCQESHQAQQILILNLMPTKVTTERQFLKRFAAGNTDVAVT
FMYPASHHFKSLPQAVVAAHYVTLADIQDQYFDGLIVTGAPVETLPFEAVDYWNELLTII
DWSRQHVSQTLFECWAAQAGLYAQFGIAKRAVAHKIFGIYSATSTDVKSPLISGLNAGGL
LKMPQSRHTALVMPERLPAGLQVVADNPKVGPLVLSAPKLHAVYVTGHPEYERRTLADEY
LRDRRKHLPIQLPEHYFATEQLTTVDYSWQTSSNQLYQNWLATLNLTKVGY
Enzyme 12 Number of Residues 291
Enzyme 12 Molecular Weight 32508.9
Enzyme 12 Theoretical pI 7.40
Enzyme 12 GO Classification
Function
  • acyltransferase activity
  • catalytic activity
  • transferase activity
  • transferase activity, transferring acyl groups
  • transferase activity, transferring acyl groups other than amino-acyl groups
Process
  • L-methionine biosynthetic process from L-homoserine via cystathionine
  • L-methionine biosynthetic process from homoserine via O-succinyl-L-homoserine and cystathionine
  • cellular amino acid and derivative metabolic process
  • cellular amino acid metabolic process
  • cellular metabolic process
  • homoserine metabolic process
  • metabolic process
  • serine family amino acid metabolic process
Component
  • cell part
  • cytoplasm
  • intracellular part
Enzyme 12 General Function Involved in acyltransferase activity
Enzyme 12 Specific Function Not Available
Enzyme 12 Pathways Not Available
Enzyme 12 Reactions
  • succinyl-CoA + L-homoserine = CoA + O-succinyl-L-homoserine [RN:R01777]
Enzyme 12 Pfam Domain Function
Enzyme 12 Signals
  • None
Enzyme 12 Transmembrane Regions
  • None
Enzyme 12 Essentiality Not Available
Enzyme 12 GenBank ID Protein 28271916 Link Image
Enzyme 12 UniProtKB/Swiss-Prot ID Q88UF5 Link Image
Enzyme 12 UniProtKB/Swiss-Prot Entry Name Q88UF5_LACPL Link Image
Enzyme 12 PDB ID Not Available
Enzyme 12 Cellular Location Not Available
Enzyme 12 Gene Sequence >876 bp 
ATGACAGTCACAGCAAATAATGGATTATTAGTGGCCCGTGGAGAATGGGCGAACGCAACG
TGTCAGGAAAGTCATCAGGCACAACAGATTTTAATTTTAAACTTGATGCCGACTAAGGTA
ACGACGGAGCGGCAGTTCCTAAAGCGTTTTGCAGCCGGTAACACAGATGTGGCTGTGACG
TTTATGTATCCCGCTAGTCACCATTTCAAGAGCCTGCCACAAGCAGTGGTCGCGGCACAT
TACGTGACGTTGGCTGATATTCAAGATCAGTATTTTGATGGCTTGATCGTCACCGGCGCG
CCAGTTGAGACGTTACCGTTTGAAGCAGTCGATTACTGGAACGAATTGTTAACAATCATT
GATTGGTCACGACAGCACGTTAGCCAGACTTTATTTGAATGCTGGGCAGCACAAGCAGGG
CTATACGCACAGTTTGGAATCGCAAAGCGCGCCGTTGCTCACAAGATATTCGGTATTTAT
AGTGCGACTAGTACTGATGTTAAGTCACCGCTGATTAGTGGACTGAATGCTGGAGGCTTG
CTAAAAATGCCACAGTCACGGCATACAGCATTAGTGATGCCGGAACGCTTACCCGCTGGA
TTGCAGGTTGTTGCTGACAATCCGAAGGTGGGACCGCTCGTTTTATCTGCCCCCAAGCTG
CACGCGGTCTATGTGACCGGTCATCCTGAATACGAACGGCGCACGCTTGCCGATGAATAT
TTGCGCGACCGACGTAAGCACTTGCCGATTCAGTTACCTGAACATTACTTTGCTACTGAA
CAATTAACAACAGTTGATTACAGTTGGCAAACTTCAAGCAATCAACTGTATCAAAACTGG
TTAGCAACTTTGAATTTAACGAAAGTAGGTTATTAA
Enzyme 12 GenBank Gene ID AL935259 Link Image
Enzyme 12 GeneCard ID metA Link Image
Enzyme 12 GenAtlas ID Not Available
Enzyme 12 HGNC ID Not Available
Enzyme 12 Chromosome Location Not Available
Enzyme 12 Locus lp_2537
Enzyme 12 SNPs SNPJam Report Link Image
Enzyme 12 General References
  1. Kleerebezem M, Boekhorst J, van Kranenburg R, Molenaar D, Kuipers OP, Leer R, Tarchini R, Peters SA, Sandbrink HM, Fiers MW, Stiekema W, Lankhorst RM, Bron PA, Hoffer SM, Groot MN, Kerkhoven R, de Vries M, Ursing B, de Vos WM, Siezen RJ: Complete genome sequence of Lactobacillus plantarum WCFS1. Proc Natl Acad Sci U S A. 2003 Feb 18;100(4):1990-5. Epub 2003 Feb 3. [PubMed Link Image]
Enzyme 12 Metabolite References Not Available
Enzyme 13 [top]
Enzyme 13 ID 15490
Enzyme 13 Name Homoserine O-succinyltransferase
Enzyme 13 Synonyms Not Available
Enzyme 13 Gene Name metA
Enzyme 13 Protein Sequence >Homoserine O-succinyltransferase 
MANKVKIGILNLMHDKLDTQSHFIKVLPNADLTFFYPRMHYQNRPIPPEVNMTSEPLDIN
RVSEFDGFIITGAPIDQIDFSKITYIEEIRYLLQALDNHKIQQLYFCWGAMAALNYFYGI
KKKILAEKIFGVFPHLITEPHPLLSGLSQGFMAPHARYAEMDKKQIMQDERLAINAVDDN
SHLFMVSAKDNPERNFIFSHIEYGKDSLRDEYNREINAHPERHYKKPINYSMSNPSFQWQ
DTQKIFFNNWLKKVKDNKLVLN
Enzyme 13 Number of Residues 262
Enzyme 13 Molecular Weight 30771.1
Enzyme 13 Theoretical pI 7.88
Enzyme 13 GO Classification
Function
  • acyltransferase activity
  • catalytic activity
  • transferase activity
  • transferase activity, transferring acyl groups
  • transferase activity, transferring acyl groups other than amino-acyl groups
Process
  • L-methionine biosynthetic process from L-homoserine via cystathionine
  • L-methionine biosynthetic process from homoserine via O-succinyl-L-homoserine and cystathionine
  • cellular amino acid and derivative metabolic process
  • cellular amino acid metabolic process
  • cellular metabolic process
  • homoserine metabolic process
  • metabolic process
  • serine family amino acid metabolic process
Component
  • cell part
  • cytoplasm
  • intracellular part
Enzyme 13 General Function Involved in acyltransferase activity
Enzyme 13 Specific Function Not Available
Enzyme 13 Pathways Not Available
Enzyme 13 Reactions
  • succinyl-CoA + L-homoserine = CoA + O-succinyl-L-homoserine [RN:R01777]
Enzyme 13 Pfam Domain Function
Enzyme 13 Signals
  • None
Enzyme 13 Transmembrane Regions
  • None
Enzyme 13 Essentiality Not Available
Enzyme 13 GenBank ID Protein 58253977 Link Image
Enzyme 13 UniProtKB/Swiss-Prot ID Q5FJQ4 Link Image
Enzyme 13 UniProtKB/Swiss-Prot Entry Name Q5FJQ4_LACAC Link Image
Enzyme 13 PDB ID Not Available
Enzyme 13 Cellular Location Not Available
Enzyme 13 Gene Sequence >789 bp 
ATGTTAACTAGATATAAAATGACAATGGCCTATGATGGGCACTTATTTCATGGCTTTCAA
TTACAGCCTGATCAAAGAACTGTTCAGGGAACAGTTGAAGATGCTTTGAAAAAAATGACT
AAGGGGAAAAGAATAATTGTTCAAGGTTCTGGTAGAACTGATGCAGGTGTTCATGCAATT
GGACAAGTGATACATTTTGATTATCCAGGCAAAGAAATACCAGCGAATAGGATGATTTTA
GCATTAAATTCGATGATGCCAACGGATATTGTATTTACGGATTGTCAGATAGTTGATGAG
GACTTTCATGCTAGATATTCAATAAAAGGAAAGTGGTATCGATATCGATTAAGTTTAGAT
TACTTTGTAAACCCATTTAAAAGATTTTATACAGGGCATTTTCCTTATCAATTAGATCTT
GAAAAAATGAGAATAGCGGCCCAAGATCTATTAGGAAAACACGATTTTACTAGTTTTGCT
GCAAGTGGTGGACAAATTAAAGATAAAGTCAGAACAATTTATTATATTAATATCACTAAG
GATGAAAAAGAAAATGAAATAGTATTTGATTTTATCGGTTCAGGTTTTCTTTATAATATG
GTTAGAATTATGGTCGCAGCCTTACTTGAAATAGGTAATGAGCGTCGACCTTTACATGAC
TTGCGGCGAGTAATTGCAGCTAAAGATAGACAAGAAGTTCGACAAACAGCTCAGGGAAGT
GGCTTATATTTGTATCATGTTTTTTATGATGAAATACCGCAAAAATATCGTCAGGACCAG
TATTTATAA
Enzyme 13 GenBank Gene ID CP000033 Link Image
Enzyme 13 GeneCard ID metA Link Image
Enzyme 13 GenAtlas ID Not Available
Enzyme 13 HGNC ID Not Available
Enzyme 13 Chromosome Location Not Available
Enzyme 13 Locus LBA1237
Enzyme 13 SNPs SNPJam Report Link Image
Enzyme 13 General References
  1. Altermann E, Russell WM, Azcarate-Peril MA, Barrangou R, Buck BL, McAuliffe O, Souther N, Dobson A, Duong T, Callanan M, Lick S, Hamrick A, Cano R, Klaenhammer TR: Complete genome sequence of the probiotic lactic acid bacterium Lactobacillus acidophilus NCFM. Proc Natl Acad Sci U S A. 2005 Mar 15;102(11):3906-12. Epub 2005 Jan 25. [PubMed Link Image]
Enzyme 13 Metabolite References Not Available
Enzyme 14 [top]
Enzyme 14 ID 15491
Enzyme 14 Name Homoserine O-succinyltransferase
Enzyme 14 Synonyms Not Available
Enzyme 14 Gene Name metA
Enzyme 14 Protein Sequence >Homoserine O-succinyltransferase 
MPIKIPSGLPARDILDSERIFALEKPEAERQRVRPLKLVILNLMPKKIETETQLLRLISK
SPLQVEIDFMKTSTHEATHVSADHLVKFYENLDAFKDNYYDGFVVTGAPVEHMPFEDVDY
WDEFKTILDWASTHVFSTIYLCWGAMGALYYRYGIHKVDYPEKIFGVFPQYLQDEYCFLT
NGFDEIDLQPHSRLAGVNENEVRANHDLQILTWGPQSGPGLIATRDFSEVFALGHWEYGK
YTLAEEYERDMAKGMTNVPFPKNYFPHDDPKLEPLFAWRAHANLLWRNWLNWVYQTTPYD
LTEVPQLRAEKKLGTDRSIRHEPGGPRQDDFKPFVHDGYGVIQG
Enzyme 14 Number of Residues 344
Enzyme 14 Molecular Weight 40022.1
Enzyme 14 Theoretical pI 5.27
Enzyme 14 GO Classification
Function
  • acyltransferase activity
  • catalytic activity
  • transferase activity
  • transferase activity, transferring acyl groups
  • transferase activity, transferring acyl groups other than amino-acyl groups
Process
  • L-methionine biosynthetic process from L-homoserine via cystathionine
  • L-methionine biosynthetic process from homoserine via O-succinyl-L-homoserine and cystathionine
  • cellular amino acid and derivative metabolic process
  • cellular amino acid metabolic process
  • cellular metabolic process
  • homoserine metabolic process
  • metabolic process
  • serine family amino acid metabolic process
Component
  • cell part
  • cytoplasm
  • intracellular part
Enzyme 14 General Function Involved in acyltransferase activity
Enzyme 14 Specific Function Not Available
Enzyme 14 Pathways Not Available
Enzyme 14 Reactions Not Available
Enzyme 14 Pfam Domain Function
Enzyme 14 Signals
  • None
Enzyme 14 Transmembrane Regions
  • None
Enzyme 14 Essentiality Not Available
Enzyme 14 GenBank ID Protein 23325562 Link Image
Enzyme 14 UniProtKB/Swiss-Prot ID Q8G7A5 Link Image
Enzyme 14 UniProtKB/Swiss-Prot Entry Name Q8G7A5_BIFLO Link Image
Enzyme 14 PDB ID Not Available
Enzyme 14 Cellular Location Not Available
Enzyme 14 Gene Sequence >1035 bp 
ATGCCTATCAAGATCCCCAGTGGCCTGCCGGCCAGAGATATCCTCGATTCGGAGCGCATC
TTCGCTCTGGAGAAGCCCGAGGCGGAGCGTCAGCGCGTCCGCCCGCTCAAACTGGTGATC
CTGAACTTGATGCCTAAGAAAATCGAGACTGAAACACAGCTGCTGCGTCTGATTTCCAAG
TCGCCGCTGCAGGTCGAAATCGACTTCATGAAGACCTCCACGCATGAGGCCACGCACGTT
TCCGCCGATCATCTCGTCAAGTTCTACGAAAACCTCGATGCGTTCAAAGACAACTATTAC
GACGGTTTTGTGGTCACCGGCGCGCCTGTAGAGCATATGCCGTTCGAAGATGTGGACTAC
TGGGACGAGTTCAAGACGATTCTCGACTGGGCCTCCACCCATGTGTTCTCCACCATATAC
CTGTGCTGGGGTGCGATGGGCGCACTGTACTACCGCTACGGCATCCACAAGGTGGATTAC
CCCGAGAAGATTTTCGGCGTATTCCCGCAGTACCTGCAGGACGAATACTGCTTCCTGACC
AATGGCTTCGACGAGATTGATCTGCAGCCGCACTCCCGCCTCGCCGGCGTGAACGAAAAC
GAGGTACGTGCCAACCATGACCTTCAGATCTTGACTTGGGGGCCGCAGTCCGGCCCGGGC
CTGATCGCCACGCGTGACTTCTCCGAAGTGTTCGCGCTCGGCCATTGGGAGTACGGCAAG
TACACGCTCGCCGAAGAATACGAGCGCGATATGGCCAAGGGCATGACCAACGTGCCCTTC
CCGAAGAACTACTTCCCGCATGACGATCCGAAGCTGGAACCGTTGTTCGCCTGGCGCGCC
CACGCCAATCTGCTGTGGCGCAACTGGCTCAACTGGGTGTACCAGACCACGCCGTATGAC
CTGACCGAGGTGCCGCAGCTCAGGGCTGAGAAGAAGCTCGGTACTGATCGTTCGATTCGG
CATGAGCCGGGCGGGCCGCGCCAGGATGATTTCAAGCCGTTTGTGCATGACGGGTATGGG
GTGATTCAGGGCTGA
Enzyme 14 GenBank Gene ID AE014295 Link Image
Enzyme 14 GeneCard ID metA Link Image
Enzyme 14 GenAtlas ID Not Available
Enzyme 14 HGNC ID Not Available
Enzyme 14 Chromosome Location Not Available
Enzyme 14 Locus BL0365
Enzyme 14 SNPs SNPJam Report Link Image
Enzyme 14 General References
  1. Schell MA, Karmirantzou M, Snel B, Vilanova D, Berger B, Pessi G, Zwahlen MC, Desiere F, Bork P, Delley M, Pridmore RD, Arigoni F: The genome sequence of Bifidobacterium longum reflects its adaptation to the human gastrointestinal tract. Proc Natl Acad Sci U S A. 2002 Oct 29;99(22):14422-7. Epub 2002 Oct 15. [PubMed Link Image]
Enzyme 14 Metabolite References Not Available
Enzyme 15 [top]
Enzyme 15 ID 15492
Enzyme 15 Name Homoserine O-succinyltransferase
Enzyme 15 Synonyms
  1. Homoserine O-transsuccinylase
  2. HTS
Enzyme 15 Gene Name metA
Enzyme 15 Protein Sequence >Homoserine O-succinyltransferase 
MPLNLPDKLPAIELLKEENIFVIDNSRATQQDIRPLRIVILNLMPLKITTETDLVRLLSN
TPLQVEISFMKIKSHTSKNTPIEHMKTFYTDFDKMREDRYDGMIITGAPVEQMEFEEVNY
WDEITEIFDWARTHVTSTLYICWAAQAGLYHHYGIPKYALDKKMFGIFKHRTLLPLHPIF
RGFDDEFYVPHSRHTEVRKEDILKVPELTLLSESDDSGVYMVVARGGREFFVTGHSEYSP
LTLDTEYRRDVSKGLPIEIPRNYYVNDDPDKGPLVRWRGHANLLFSNWLNYFVYQETPYN
IEDIR
Enzyme 15 Number of Residues 305
Enzyme 15 Molecular Weight 35882.7
Enzyme 15 Theoretical pI 5.59
Enzyme 15 GO Classification
Function
  • acyltransferase activity
  • catalytic activity
  • transferase activity
  • transferase activity, transferring acyl groups
  • transferase activity, transferring acyl groups other than amino-acyl groups
Process
  • L-methionine biosynthetic process from L-homoserine via cystathionine
  • L-methionine biosynthetic process from homoserine via O-succinyl-L-homoserine and cystathionine
  • cellular amino acid and derivative metabolic process
  • cellular amino acid metabolic process
  • cellular metabolic process
  • homoserine metabolic process
  • metabolic process
  • serine family amino acid metabolic process
Component
  • cell part
  • cytoplasm
  • intracellular part
Enzyme 15 General Function Involved in acyltransferase activity
Enzyme 15 Specific Function Succinyl-CoA + L-homoserine = CoA + O- succinyl-L-homoserine
Enzyme 15 Pathways Not Available
Enzyme 15 Reactions
  • succinyl-CoA + L-homoserine = CoA + O-succinyl-L-homoserine [RN:R01777]
Enzyme 15 Pfam Domain Function
Enzyme 15 Signals
  • None
Enzyme 15 Transmembrane Regions
  • None
Enzyme 15 Essentiality Not Available
Enzyme 15 GenBank ID Protein 60491551 Link Image
Enzyme 15 UniProtKB/Swiss-Prot ID Q5LHS7 Link Image
Enzyme 15 UniProtKB/Swiss-Prot Entry Name META_BACFN Link Image
Enzyme 15 PDB ID Not Available
Enzyme 15 Cellular Location Not Available
Enzyme 15 Gene Sequence >918 bp 
ATGCCTTTAAATTTACCCGATAAGCTTCCTGCGATAGAACTATTAAAAGAGGAGAATATC
TTTGTGATAGATAACTCCCGCGCAACACAACAAGACATCCGTCCGCTACGAATTGTTATC
CTCAACCTGATGCCGTTGAAGATTACGACAGAAACAGACTTGGTGCGTTTACTCTCAAAC
ACTCCGCTTCAGGTGGAAATTTCTTTTATGAAGATTAAAAGCCACACCTCGAAGAATACA
CCGATAGAGCACATGAAAACATTTTATACCGACTTCGACAAGATGAGAGAAGACAGGTAT
GACGGTATGATTATCACCGGTGCACCGGTAGAGCAAATGGAGTTTGAGGAAGTGAACTAT
TGGGATGAAATAACGGAGATATTCGACTGGGCACGTACCCATGTCACCTCCACACTCTAT
ATTTGTTGGGCAGCACAGGCGGGACTGTATCATCATTACGGTATCCCCAAGTATGCTTTG
GATAAGAAAATGTTCGGCATTTTCAAGCATCGCACGCTGCTTCCGCTGCATCCCATCTTC
CGTGGCTTCGATGATGAATTCTATGTGCCCCATAGCCGGCATACGGAAGTGCGAAAGGAA
GATATACTGAAAGTACCGGAATTGACATTACTTTCCGAGTCGGATGATTCGGGGGTATAT
ATGGTGGTAGCCCGTGGCGGACGTGAGTTTTTTGTTACCGGGCACTCCGAGTACTCTCCA
CTGACACTGGATACGGAATATCGCCGGGATGTTTCGAAAGGGCTTCCCATCGAGATTCCC
CGTAACTATTACGTGAATGATGATCCGGACAAAGGACCGCTGGTGCGTTGGCGCGGACAT
GCCAACCTGTTGTTCTCCAATTGGCTGAACTATTTCGTCTATCAGGAGACTCCTTATAAT
ATTGAAGATATCCGATGA
Enzyme 15 GenBank Gene ID CR626927 Link Image
Enzyme 15 GeneCard ID metA Link Image
Enzyme 15 GenAtlas ID Not Available
Enzyme 15 HGNC ID Not Available
Enzyme 15 Chromosome Location Not Available
Enzyme 15 Locus BF0548
Enzyme 15 SNPs SNPJam Report Link Image
Enzyme 15 General References
  1. Cerdeno-Tarraga AM, Patrick S, Crossman LC, Blakely G, Abratt V, Lennard N, Poxton I, Duerden B, Harris B, Quail MA, Barron A, Clark L, Corton C, Doggett J, Holden MT, Larke N, Line A, Lord A, Norbertczak H, Ormond D, Price C, Rabbinowitsch E, Woodward J, Barrell B, Parkhill J: Extensive DNA inversions in the B. fragilis genome control variable gene expression. Science. 2005 Mar 4;307(5714):1463-5. [PubMed Link Image]
Enzyme 15 Metabolite References Not Available
Enzyme 16 [top]
Enzyme 16 ID 15493
Enzyme 16 Name Homoserine O-succinyltransferase
Enzyme 16 Synonyms
  1. Homoserine O-transsuccinylase
  2. HTS
Enzyme 16 Gene Name metA
Enzyme 16 Protein Sequence >Homoserine O-succinyltransferase 
MPLNLPDKLPAIELLKEENIFVIDNSRATQQDIRPLRIVILNLMPLKITTETDLVRLLSN
TPLQVEISFMKIKSHTSKNTPIEHMKTFYTDFDKMREDRYDGMIITGAPVEQMDFEEVNY
WDEITEIFDWARTHVTSTLYICWAAQAGLYHHYGIPKYALDKKMFGIFKHRTLLPLHPIF
RGFDDEFYVPHSRHTEVRKEDILKVPELTLLSESDDSGVYMVVARGGREFFVTGHSEYSP
LTLDTEYRRDVSKGLPIEIPRNYYVNDDPDKGPLVRWRGHANLLFSNWLNYFVYQETPYN
IEDIR
Enzyme 16 Number of Residues 305
Enzyme 16 Molecular Weight 35868.6
Enzyme 16 Theoretical pI 5.59
Enzyme 16 GO Classification
Function
  • acyltransferase activity
  • catalytic activity
  • transferase activity
  • transferase activity, transferring acyl groups
  • transferase activity, transferring acyl groups other than amino-acyl groups
Process
  • L-methionine biosynthetic process from L-homoserine via cystathionine
  • L-methionine biosynthetic process from homoserine via O-succinyl-L-homoserine and cystathionine
  • cellular amino acid and derivative metabolic process
  • cellular amino acid metabolic process
  • cellular metabolic process
  • homoserine metabolic process
  • metabolic process
  • serine family amino acid metabolic process
Component
  • cell part
  • cytoplasm
  • intracellular part
Enzyme 16 General Function Involved in acyltransferase activity
Enzyme 16 Specific Function Succinyl-CoA + L-homoserine = CoA + O- succinyl-L-homoserine
Enzyme 16 Pathways Not Available
Enzyme 16 Reactions
  • succinyl-CoA + L-homoserine = CoA + O-succinyl-L-homoserine [RN:R01777]
Enzyme 16 Pfam Domain Function
Enzyme 16 Signals
  • None
Enzyme 16 Transmembrane Regions
  • None
Enzyme 16 Essentiality Not Available
Enzyme 16 GenBank ID Protein 52214754 Link Image
Enzyme 16 UniProtKB/Swiss-Prot ID Q64YS9 Link Image
Enzyme 16 UniProtKB/Swiss-Prot Entry Name META_BACFR Link Image
Enzyme 16 PDB ID Not Available
Enzyme 16 Cellular Location Not Available
Enzyme 16 Gene Sequence >918 bp 
ATGCCTTTAAATTTACCCGATAAGCTTCCTGCGATAGAACTATTAAAAGAGGAGAATATC
TTTGTGATAGATAACTCCCGCGCAACACAACAAGATATCCGTCCGCTACGAATTGTTATC
CTCAACCTGATGCCGTTGAAGATTACGACAGAAACAGACTTGGTGCGTTTACTCTCAAAC
ACTCCGCTTCAGGTGGAAATTTCTTTTATGAAGATTAAAAGCCACACCTCGAAGAATACA
CCGATAGAGCACATGAAAACATTTTATACCGACTTCGACAAGATGAGAGAAGACAGGTAT
GACGGTATGATTATCACCGGTGCACCGGTAGAGCAAATGGATTTTGAGGAAGTGAACTAT
TGGGATGAAATAACGGAGATATTCGACTGGGCACGTACCCATGTCACCTCCACACTCTAT
ATTTGTTGGGCAGCACAGGCGGGACTGTATCATCATTACGGTATCCCCAAGTATGCTTTG
GATAAGAAAATGTTCGGCATTTTCAAGCATCGCACGCTGCTTCCGCTGCATCCCATCTTC
CGTGGCTTCGATGATGAATTCTATGTGCCCCATAGCCGGCATACGGAAGTGCGAAAGGAA
GATATACTGAAAGTACCGGAATTGACATTACTTTCCGAGTCGGATGATTCGGGGGTATAT
ATGGTGGTAGCCCGTGGCGGACGTGAGTTTTTTGTTACCGGGCACTCCGAGTACTCTCCA
CTGACACTGGATACGGAATATCGCCGGGATGTTTCGAAAGGGCTTCCCATCGAGATTCCC
CGTAACTATTACGTGAATGATGATCCGGACAAAGGACCGCTGGTGCGTTGGCGCGGACAT
GCCAACCTGTTGTTCTCCAATTGGCTGAACTATTTCGTCTATCAGGAGACTCCTTATAAT
ATTGAAGATATCCGATGA
Enzyme 16 GenBank Gene ID AP006841 Link Image
Enzyme 16 GeneCard ID metA Link Image
Enzyme 16 GenAtlas ID Not Available
Enzyme 16 HGNC ID Not Available
Enzyme 16 Chromosome Location Not Available
Enzyme 16 Locus BF0598
Enzyme 16 SNPs SNPJam Report Link Image
Enzyme 16 General References
  1. Kuwahara T, Yamashita A, Hirakawa H, Nakayama H, Toh H, Okada N, Kuhara S, Hattori M, Hayashi T, Ohnishi Y: Genomic analysis of Bacteroides fragilis reveals extensive DNA inversions regulating cell surface adaptation. Proc Natl Acad Sci U S A. 2004 Oct 12;101(41):14919-24. Epub 2004 Oct 4. [PubMed Link Image]
Enzyme 16 Metabolite References Not Available
Enzyme 17 [top]
Enzyme 17 ID 15494
Enzyme 17 Name Homoserine O-succinyltransferase
Enzyme 17 Synonyms Not Available
Enzyme 17 Gene Name metA
Enzyme 17 Protein Sequence >Homoserine O-succinyltransferase 
MALILPKGLPVINKLLDEGIDVIYKEDFKKELKYEENIDTKIAILNLMPIKIDTELDLLR
RIDKTGFNVSVEFIKISTRESKRSCNEYVKEFYKTFDEAKGEYFDGFIITGAPVEQMEFE
EVDYWNELEEIMDYSKRKTKSTLYICWAAQASLYKYYNVKKLPLSQKCFGVFKHKVDKDS
KIVDGFENEFFAPHSRHTTVNIEALKENKELSIVSHSKEAGPYIITNSRDVFVMGHSEYD
KYTLDKEYKRDINKGDKISIPQNYYINDDPSEEPTVKWKKHSELLFRNWIKNYLIQ
Enzyme 17 Number of Residues 296
Enzyme 17 Molecular Weight 34922.6
Enzyme 17 Theoretical pI 6.02
Enzyme 17 GO Classification
Function
  • acyltransferase activity
  • catalytic activity
  • transferase activity
  • transferase activity, transferring acyl groups
  • transferase activity, transferring acyl groups other than amino-acyl groups
Process
  • L-methionine biosynthetic process from L-homoserine via cystathionine
  • L-methionine biosynthetic process from homoserine via O-succinyl-L-homoserine and cystathionine
  • cellular amino acid and derivative metabolic process
  • cellular amino acid metabolic process
  • cellular metabolic process
  • homoserine metabolic process
  • metabolic process
  • serine family amino acid metabolic process
Component
  • cell part
  • cytoplasm
  • intracellular part
Enzyme 17 General Function Involved in acyltransferase activity
Enzyme 17 Specific Function Not Available
Enzyme 17 Pathways Not Available
Enzyme 17 Reactions
  • succinyl-CoA + L-homoserine = CoA + O-succinyl-L-homoserine [RN:R01777]
Enzyme 17 Pfam Domain Function
Enzyme 17 Signals
  • None
Enzyme 17 Transmembrane Regions
  • None
Enzyme 17 Essentiality Not Available
Enzyme 17 GenBank ID Protein 115249308 Link Image
Enzyme 17 UniProtKB/Swiss-Prot ID Q187D6 Link Image
Enzyme 17 UniProtKB/Swiss-Prot Entry Name Q187D6_CLOD6 Link Image
Enzyme 17 PDB ID Not Available
Enzyme 17 Cellular Location Not Available
Enzyme 17 Gene Sequence >891 bp 
ATGGGAAACATAGTTGTCATAGGAAGTGTAAACATGGACATGGTATGTTCTGTAGATAAA
AGACCAGAAAAAGGAGAAACAGTATTAGGTAATAGTTTTTTTACATCACCTGGAGGAAAA
GGGGCTAATCAAGCTATCTCAGCTTCTAAACTAGGAGCAAATGTAAAAATGATATCATGC
ATAGGGGAAGATGGCTTAGGAGAGGAGTTAATAAGAAATTTTAGAACGAATAAAGTTGAT
TATAGCTTAGTATCCAGAAATAATCACAAAAGTTCTGGTGTTGCTGTTATAACATTATGT
GAAAATGATAATAGTATTGTTGTTGTACCAGGGACTAATGAGCTAGTAGATATAGAATTA
ATTAAAAAGAATGAAGAAGAGATAAAGAATGCAGATATAGTATTGCTACAATTAGAGATT
CCATTAAAAACAATAAATTATGTAGTGAATTTCTGTTTTGAAAATAGGATTAGGGTTTTA
TTAAATCCAGCACCAGCAGTAAAACTAAATGAAGATATAATAGAAAAAGTAACTTACTTA
ACACCAAATGAACATGAATATAAGATAGTTTTTGACACAAATGAAGGGATAGAAGAAGTA
TTAAAAAAATATCCAAATAAACTTGTAATAACAGAAGGAAAAAATGGAGCTAGATTTTAT
GATGGTGAGGAAATCAAGCATGTATCTTGTATAAGTGTTGATGTTCAAGATACCACAGGA
GCAGGAGATACATTTAATGGAGCATTGGCAGTGGCTATAACAGAAGGGCAAAATTTATAT
ACAGCAGTAGAATATGCAGTAGTAGTATCAGGTCTTTCTGTAACTAAACTAGGTGCACAA
TCTGGTATGCCATATAAAGAAGATGTTGAAAAATATTTAAATAATAAATAA
Enzyme 17 GenBank Gene ID AM180355 Link Image
Enzyme 17 GeneCard ID metA Link Image
Enzyme 17 GenAtlas ID Not Available
Enzyme 17 HGNC ID Not Available
Enzyme 17 Chromosome Location Not Available
Enzyme 17 Locus CD1826
Enzyme 17 SNPs SNPJam Report Link Image
Enzyme 17 General References
  1. Sebaihia M, Wren BW, Mullany P, Fairweather NF, Minton N, Stabler R, Thomson NR, Roberts AP, Cerdeno-Tarraga AM, Wang H, Holden MT, Wright A, Churcher C, Quail MA, Baker S, Bason N, Brooks K, Chillingworth T, Cronin A, Davis P, Dowd L, Fraser A, Feltwell T, Hance Z, Holroyd S, Jagels K, Moule S, Mungall K, Price C, Rabbinowitsch E, Sharp S, Simmonds M, Stevens K, Unwin L, Whithead S, Dupuy B, Dougan G, Barrell B, Parkhill J: The multidrug-resistant human pathogen Clostridium difficile has a highly mobile, mosaic genome. Nat Genet. 2006 Jul;38(7):779-86. Epub 2006 Jun 25. [PubMed Link Image]
Enzyme 17 Metabolite References Not Available
Enzyme 18 [top]
Enzyme 18 ID 15495
Enzyme 18 Name Homoserine O-succinyltransferase
Enzyme 18 Synonyms
  1. Homoserine O-transsuccinylase
  2. HTS
Enzyme 18 Gene Name metA
Enzyme 18 Protein Sequence >Homoserine O-succinyltransferase 
MPIRVPDELPAVNFLREENVFVMTTSRASGQEIRPLKVLILNLMPKKIETENQFLRLLSN
SPLQVDIQLLRIDSRESRNTPAEHLNNFYCNFEDIQDQNFDGLIVTGAPLGLVEFNDVAY
WPQIKQVLEWSKDHVTSTLFVCWAVQAALNILYGIPKQTRTEKLSGVYEHHILHPHALLT
RGFDDSFLAPHSRYADFPAALIRDYTDLEILAETEEGDAYLFASKDKRIAFVTGHPEYDA
QTLAQEFFRDVEAGLDPDVPYNYFPHNDPQNTPRASWRSHGNLLFTNWLNYYVYQITPYD
LRHMNPTLD
Enzyme 18 Number of Residues 309
Enzyme 18 Molecular Weight 35727.0
Enzyme 18 Theoretical pI 4.85
Enzyme 18 GO Classification
Function
  • acyltransferase activity
  • catalytic activity
  • transferase activity
  • transferase activity, transferring acyl groups
  • transferase activity, transferring acyl groups other than amino-acyl groups
Process
  • L-methionine biosynthetic process from L-homoserine via cystathionine
  • L-methionine biosynthetic process from homoserine via O-succinyl-L-homoserine and cystathionine
  • cellular amino acid and derivative metabolic process
  • cellular amino acid metabolic process
  • cellular metabolic process
  • homoserine metabolic process
  • metabolic process
  • serine family amino acid metabolic process
Component
  • cell part
  • cytoplasm
  • intracellular part
Enzyme 18 General Function Involved in acyltransferase activity
Enzyme 18 Specific Function Succinyl-CoA + L-homoserine = CoA + O- succinyl-L-homoserine
Enzyme 18 Pathways Not Available
Enzyme 18 Reactions
  • succinyl-CoA + L-homoserine = CoA + O-succinyl-L-homoserine [RN:R01777]
Enzyme 18 Pfam Domain Function
Enzyme 18 Signals
  • None
Enzyme 18 Transmembrane Regions
  • None
Enzyme 18 Essentiality Not Available
Enzyme 18 GenBank ID Protein 85674412 Link Image
Enzyme 18 UniProtKB/Swiss-Prot ID P07623 Link Image
Enzyme 18 UniProtKB/Swiss-Prot Entry Name META_ECOLI Link Image
Enzyme 18 PDB ID Not Available
Enzyme 18 Cellular Location Not Available
Enzyme 18 Gene Sequence >930 bp 
ATGATTCAGCAAGGAGATCTCATGCCGCAGTCCGCGTTGTTCACGGGAATCATTCCCCCT
GTCTCCACCATTTTTACCGCCGACGGCCAGCTCGATAAGCCGGGCACCGCCGCGCTGATC
GACGATCTGATCAAAGCAGGCGTTGACGGCCTGTTCTTCCTGGGCAGCGGTGGCGAGTTC
TCCCAGCTCGGCGCCGAAGAGCGTAAAGCCATTGCCCGCTTTGCTATCGATCATGTCGAT
CGTCGCGTGCCGGTGCTGATCGGCACCGGCGGCACCAACGCCCGGGAAACCATCGAACTC
AGCCAGCACGCGCAGCAGGCGGGCGCGGACGGCATCGTGGTGATCAACCCCTACTACTGG
AAAGTGTCGGAAGCGAACCTGATCCGCTATTTCGAGCAGGTGGCCGACAGCGTCACGCTG
CCGGTGATGCTCTATAACTTCCCGGCGCTGACCGGGCAGGATCTGACTCCGGCGCTGGTG
AAAACCCTCGCCGACTCGCGCAGCAATATTATCGGCATCAAAGACACCATCGACTCCGTC
GCCCACCTGCGCAGCATGATCCATACCGTCAAAGGTGCCCATCCGCACTTCACCGTGCTC
TGCGGCTACGACGATCATCTGTTCAATACCCTGCTGCTCGGCGGCGACGGGGCGATATCG
GCGAGCGGCAACTTTGCCCCGCAGGTGTCGGTGAATCTTCTGAAAGCCTGGCGCGACGGG
GACGTGGCGAAAGCGGCCGGGTATCATCAGACCTTGCTGCAAATTCCGCAGATGTATCAG
CTGGATACGCCGTTTGTGAACGTGATTAAAGAGGCGATCGTGCTCTGCGGTCGTCCTGTC
TCCACGCACGTGCTGCCGCCCGCCTCGCCGCTGGACGAGCCGCGCAAGGCGCAGCTGAAA
ACCCTGCTGCAACAGCTCAAGCTTTGCTGA
Enzyme 18 GenBank Gene ID AP009048 Link Image
Enzyme 18 GeneCard ID metA Link Image
Enzyme 18 GenAtlas ID Not Available
Enzyme 18 HGNC ID Not Available
Enzyme 18 Chromosome Location Not Available
Enzyme 18 Locus b4013
Enzyme 18 SNPs SNPJam Report Link Image
Enzyme 18 General References
  1. Duclos B, Cortay JC, Bleicher F, Ron EZ, Richaud C, Saint Girons I, Cozzone AJ: Nucleotide sequence of the metA gene encoding homoserine trans-succinylase in Escherichia coli. Nucleic Acids Res. 1989 Apr 11;17(7):2856. [PubMed Link Image]
  2. Born TL, Blanchard JS: Enzyme-catalyzed acylation of homoserine: mechanistic characterization of the Escherichia coli metA-encoded homoserine transsuccinylase. Biochemistry. 1999 Oct 26;38(43):14416-23. [PubMed Link Image]
  3. Blattner FR, Burland V, Plunkett G 3rd, Sofia HJ, Daniels DL: Analysis of the Escherichia coli genome. IV. DNA sequence of the region from 89.2 to 92.8 minutes. Nucleic Acids Res. 1993 Nov 25;21(23):5408-17. [PubMed Link Image]
  4. Blattner FR, Plunkett G 3rd, Bloch CA, Perna NT, Burland V, Riley M, Collado-Vides J, Glasner JD, Rode CK, Mayhew GF, Gregor J, Davis NW, Kirkpatrick HA, Goeden MA, Rose DJ, Mau B, Shao Y: The complete genome sequence of Escherichia coli K-12. Science. 1997 Sep 5;277(5331):1453-74. [PubMed Link Image]
  5. Hayashi K, Morooka N, Yamamoto Y, Fujita K, Isono K, Choi S, Ohtsubo E, Baba T, Wanner BL, Mori H, Horiuchi T: Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110. Mol Syst Biol. 2006;2:2006.0007. Epub 2006 Feb 21. [PubMed Link Image]
  6. Michaeli S, Mevarech M, Ron EZ: Regulatory region of the metA gene of Escherichia coli K-12. J Bacteriol. 1984 Dec;160(3):1158-62. [PubMed Link Image]
  7. Byrne C, Stokes HW, Ward KA: Nucleotide sequence of the aceB gene encoding malate synthase A in Escherichia coli. Nucleic Acids Res. 1988 Oct 11;16(19):9342. [PubMed Link Image]
Enzyme 18 Metabolite References Not Available
Enzyme 19 [top]
Enzyme 19 ID 15496
Enzyme 19 Name Homoserine kinase
Enzyme 19 Synonyms
  1. HK
  2. HSK
Enzyme 19 Gene Name thrB
Enzyme 19 Protein Sequence >Homoserine kinase 
MLTISVPATSANLGPGFDSIGLALDMQLTLQVLQPSDHWQIDHPFGADVPTDERNLIIKT
ALHLVPDLQPQHLQMASKIPLARGLGSSSTAIVAGLVLANELTGATRSSAELLEVATQLE
GHPDNVAPALLGGLVVATNTDGRVRAVKLPLPMLFASVYVPNEPLLTTASRQALPTELAY
HQAVTGSSVANTLVAALATQNWDVALPLLEQDQFHEQYRAKLVPALQTVRDHAHALGLTG
TYLSGAGPTVITLGDYGQLATLQAQLSQDTTLTGQLFLLPMDATGVKVQKS
Enzyme 19 Number of Residues 291
Enzyme 19 Molecular Weight 30700.9
Enzyme 19 Theoretical pI 5.19
Enzyme 19 GO Classification
Function
  • ATP binding
  • adenyl nucleotide binding
  • adenyl ribonucleotide binding
  • binding
  • catalytic activity
  • homoserine kinase activity
  • kinase activity
  • nucleoside binding
  • phosphotransferase activity, alcohol group as acceptor
  • purine nucleoside binding
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • aspartate family amino acid metabolic process
  • cellular amino acid and derivative metabolic process
  • cellular amino acid metabolic process
  • cellular metabolic process
  • metabolic process
  • phosphate metabolic process
  • phosphorus metabolic process
  • phosphorylation
  • threonine metabolic process
Component
—
Enzyme 19 General Function Involved in ATP binding
Enzyme 19 Specific Function Catalyzes the ATP-dependent phosphorylation of L- homoserine to L-homoserine phosphate
Enzyme 19 Pathways Not Available
Enzyme 19 Reactions
  • ATP + L-homoserine = ADP + O-phospho-L-homoserine [RN:R01771]
Enzyme 19 Pfam Domain Function
Enzyme 19 Signals
  • None
Enzyme 19 Transmembrane Regions
  • None
Enzyme 19 Essentiality Not Available
Enzyme 19 GenBank ID Protein 28270286 Link Image
Enzyme 19 UniProtKB/Swiss-Prot ID Q88Z08 Link Image
Enzyme 19 UniProtKB/Swiss-Prot Entry Name KHSE_LACPL Link Image
Enzyme 19 PDB ID Not Available
Enzyme 19 Cellular Location Not Available
Enzyme 19 Gene Sequence >876 bp 
ATGTTAACGATTTCGGTTCCGGCGACTTCCGCTAATCTTGGTCCCGGTTTTGATTCAATC
GGTCTGGCGCTGGACATGCAACTAACGCTACAAGTGTTGCAACCTAGTGACCATTGGCAG
ATTGACCATCCCTTTGGGGCGGATGTGCCGACGGATGAACGCAACTTAATTATTAAAACG
GCGTTGCATTTGGTACCAGATTTACAACCACAGCATTTACAGATGGCTTCAAAAATCCCG
TTAGCGCGCGGATTGGGTAGTAGCTCGACGGCCATCGTAGCCGGCTTAGTGCTGGCAAAC
GAATTGACCGGCGCAACGCGCTCTTCTGCTGAGCTACTGGAAGTTGCCACTCAACTGGAG
GGTCATCCAGATAACGTTGCACCAGCCCTATTAGGAGGCTTGGTTGTGGCGACGAACACT
GATGGACGCGTCCGTGCGGTGAAGTTACCGTTACCGATGCTTTTTGCAAGTGTCTACGTG
CCTAACGAACCGCTATTGACGACCGCCAGTCGCCAAGCCTTGCCAACTGAATTGGCGTAC
CACCAAGCCGTTACTGGTAGTAGTGTGGCAAATACGTTAGTGGCTGCTCTAGCAACTCAA
AATTGGGACGTGGCGTTACCGCTGCTAGAACAGGACCAGTTCCATGAACAGTATCGGGCT
AAGTTAGTGCCGGCACTACAAACGGTTAGAGACCATGCCCATGCTCTGGGATTAACGGGG
ACTTATTTGAGTGGTGCTGGGCCGACGGTGATTACTTTGGGTGATTACGGTCAACTCGCT
ACGTTGCAGGCACAATTGAGCCAAGATACAACACTCACCGGCCAATTATTCTTATTGCCA
ATGGATGCAACTGGTGTAAAAGTACAAAAATCTTAA
Enzyme 19 GenBank Gene ID AL935253 Link Image
Enzyme 19 GeneCard ID thrB Link Image
Enzyme 19 GenAtlas ID Not Available
Enzyme 19 HGNC ID Not Available
Enzyme 19 Chromosome Location 3
Enzyme 19 Locus 3p24.2
Enzyme 19 SNPs SNPJam Report Link Image
Enzyme 19 General References
  1. Kleerebezem M, Boekhorst J, van Kranenburg R, Molenaar D, Kuipers OP, Leer R, Tarchini R, Peters SA, Sandbrink HM, Fiers MW, Stiekema W, Lankhorst RM, Bron PA, Hoffer SM, Groot MN, Kerkhoven R, de Vries M, Ursing B, de Vos WM, Siezen RJ: Complete genome sequence of Lactobacillus plantarum WCFS1. Proc Natl Acad Sci U S A. 2003 Feb 18;100(4):1990-5. Epub 2003 Feb 3. [PubMed Link Image]
Enzyme 19 Metabolite References Not Available
Enzyme 20 [top]
Enzyme 20 ID 15497
Enzyme 20 Name Homoserine kinase
Enzyme 20 Synonyms
  1. HK
  2. HSK
Enzyme 20 Gene Name thrB
Enzyme 20 Protein Sequence >Homoserine kinase 
MIIKVPASTANLGPGFDSIGMAVSLYLEVEVLSVSDRFQVDHVIPKIPHDETNLIVKTAL
TVYPGLQPLHLRVKNDIPLAHGLGSSSSAIAAGIELADHFGKLGLSDEEKVQIGARIEGH
PDNIAPTILGGLVVGTEVDQHFDAIKAPLPPYTLVAYVPDYNLATKDARKVLPKELDFKT
ATHGSAIANTLVASLFTQNYKMAGELMESDVFHEPYREKLVPELNQIREVAHQKHAVATY
LSGAGSTVMTWIEDEHVRGFLSGLNKHGLKANTFILHPDKNGVQIIE
Enzyme 20 Number of Residues 287
Enzyme 20 Molecular Weight 31142.4
Enzyme 20 Theoretical pI 6.14
Enzyme 20 GO Classification
Function
  • ATP binding
  • adenyl nucleotide binding
  • adenyl ribonucleotide binding
  • binding
  • catalytic activity
  • homoserine kinase activity
  • kinase activity
  • nucleoside binding
  • phosphotransferase activity, alcohol group as acceptor
  • purine nucleoside binding
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • aspartate family amino acid metabolic process
  • cellular amino acid and derivative metabolic process
  • cellular amino acid metabolic process
  • cellular metabolic process
  • metabolic process
  • phosphate metabolic process
  • phosphorus metabolic process
  • phosphorylation
  • threonine metabolic process
Component
—
Enzyme 20 General Function Involved in ATP binding
Enzyme 20 Specific Function Catalyzes the ATP-dependent phosphorylation of L- homoserine to L-homoserine phosphate
Enzyme 20 Pathways Not Available
Enzyme 20 Reactions
  • ATP + L-homoserine = ADP + O-phospho-L-homoserine [RN:R01771]
Enzyme 20 Pfam Domain Function
Enzyme 20 Signals
  • None
Enzyme 20 Transmembrane Regions
  • None
Enzyme 20 Essentiality Not Available
Enzyme 20 GenBank ID Protein 58254277 Link Image
Enzyme 20 UniProtKB/Swiss-Prot ID Q5FJS7 Link Image
Enzyme 20 UniProtKB/Swiss-Prot Entry Name KHSE_LACAC Link Image
Enzyme 20 PDB ID Not Available
Enzyme 20 Cellular Location Not Available
Enzyme 20 Gene Sequence >864 bp 
ATGAGTAGTGATCCTGGAGCAGGGAATCTTTTTGATCGCTTGAAGAATCGTTTATCCGGT
GAGAAAAAAGAAAAGTCTAAAGATCATTTGGAAAAAGAAATCATCAATCTACATGATAAT
CATAAGATTGATGATACGGAATTTTCAATGTTAGAAGGAATTTTAGACTTTCAAGGTAAA
ACAGCGCGTGAAGTAATGGTTCCGCGCACAGATGCATTTATGGTTGATGCCGACGTTAGT
TTTCAGGATAATTTGAATGAAATCTTGCGAGAACCATATTCAAGAATTCCGGTATATAAA
AAAGATAAAGATAAAATTGTGGGCATTATTCACATTCGAAGTGTACTGCGTAAAGCTAGA
GAAAAAGGTTTTAAGAATCTAGATTATGAAGACGTAATGACTGAGCCTTTGTTTGCACCA
GAAACCGCCGAATTAGGTGACTTACTTATCGAAATGCAACAAACGCAGCGACAATTAGCA
ATTTTAGTAGATGAATATGGCGGAGTTACAGGGCTAGCTACAATTGAAGATTTAATCGAA
GAAATTGTAGGGGATATCGATGACGAAGTAGATCATACAGAAGTTTTGTACAATCAAATT
GCACCTAATAAATATATTATTTATGGGAAAATGCCCTTAGATGATTTTAATGAGCAATTT
GGTACAGATCTTAAAATGGAAGATGTTGATACAGTAGCAGGATATGTCATTAATACTTTA
AAAGTAATTCCGGCAAAAGGTGAAAAATTAACTGTCGATATTGGCAATGATATGACTTTG
ACAACTAGAAGAATGAAGGGGTCAAGATTGCTTACTGTTTTGTTATCAATAAATAAGAAA
AAGGAAGAAGATATAAAAGACTAA
Enzyme 20 GenBank Gene ID CP000033 Link Image
Enzyme 20 GeneCard ID thrB Link Image
Enzyme 20 GenAtlas ID Not Available
Enzyme 20 HGNC ID Not Available
Enzyme 20 Chromosome Location 3
Enzyme 20 Locus 3p24.2
Enzyme 20 SNPs SNPJam Report Link Image
Enzyme 20 General References
  1. Altermann E, Russell WM, Azcarate-Peril MA, Barrangou R, Buck BL, McAuliffe O, Souther N, Dobson A, Duong T, Callanan M, Lick S, Hamrick A, Cano R, Klaenhammer TR: Complete genome sequence of the probiotic lactic acid bacterium Lactobacillus acidophilus NCFM. Proc Natl Acad Sci U S A. 2005 Mar 15;102(11):3906-12. Epub 2005 Jan 25. [PubMed Link Image]
Enzyme 20 Metabolite References Not Available
Enzyme 21 [top]
Enzyme 21 ID 15498
Enzyme 21 Name Possible homoserine kinase
Enzyme 21 Synonyms Not Available
Enzyme 21 Gene Name thrB
Enzyme 21 Protein Sequence >Possible homoserine kinase 
MNPICNSVHVRVPATSANLGSGFDTVGLALDYHDELTFTLNDDPNDGIAHVIIHGEGADA
LPCDETHLVVSTFRRACATFGLGRLGFTLEATNNIPQARGMGSSAEAIVAGIAAAAAFAQ
TGDLNRPAVFDMAAQIEGHPDNVAPAVFGGLTVSWDFETAEGVGSVAVPGGEPLHGGFHA
VNYPVDPSITAAVFVPDYELSTEKARQALPRELPYKDAVYNVSRVGLLPAAMNPMVLAQA
AQQGKSGVAAAPAQDADTCACAGGTRESPFADELAAAQAQSNALLFTATQDKLHQPYRGT
LMPPSTELIALFRSKGYAAAVSGAGPCVLVLHYGNAREAIDQIASEQLASGHWRVLHLPI
NTAGVEIERR
Enzyme 21 Number of Residues 370
Enzyme 21 Molecular Weight 38558.9
Enzyme 21 Theoretical pI 4.73
Enzyme 21 GO Classification
Function
  • ATP binding
  • adenyl nucleotide binding
  • adenyl ribonucleotide binding
  • binding
  • catalytic activity
  • homoserine kinase activity
  • kinase activity
  • nucleoside binding
  • phosphotransferase activity, alcohol group as acceptor
  • purine nucleoside binding
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • aspartate family amino acid metabolic process
  • cellular amino acid and derivative metabolic process
  • cellular amino acid metabolic process
  • cellular metabolic process
  • metabolic process
  • phosphate metabolic process
  • phosphorus metabolic process
  • phosphorylation
  • threonine metabolic process
Component
—
Enzyme 21 General Function Involved in ATP binding
Enzyme 21 Specific Function ATP + L-homoserine = ADP + O-phospho-L- homoserine
Enzyme 21 Pathways Not Available
Enzyme 21 Reactions Not Available
Enzyme 21 Pfam Domain Function
Enzyme 21 Signals
  • None
Enzyme 21 Transmembrane Regions
  • None
Enzyme 21 Essentiality Not Available
Enzyme 21 GenBank ID Protein 23326534 Link Image
Enzyme 21 UniProtKB/Swiss-Prot ID Q8G4U9 Link Image
Enzyme 21 UniProtKB/Swiss-Prot Entry Name Q8G4U9_BIFLO Link Image
Enzyme 21 PDB ID Not Available
Enzyme 21 Cellular Location Not Available
Enzyme 21 Gene Sequence >1113 bp 
ATGAATCCAATCTGCAATAGCGTTCACGTGCGCGTGCCCGCCACGTCCGCCAACCTCGGC
TCCGGCTTCGATACCGTGGGTCTGGCGCTCGACTACCATGACGAGCTCACTTTCACGCTC
AACGACGACCCGAACGACGGCATTGCCCACGTGATCATCCACGGCGAGGGTGCCGACGCC
CTCCCATGCGACGAAACCCACCTCGTGGTCTCCACCTTCCGCCGTGCCTGTGCCACGTTC
GGCCTCGGCCGACTCGGCTTCACGCTGGAAGCGACCAACAACATCCCTCAGGCTCGTGGC
ATGGGCTCTTCCGCCGAGGCCATTGTGGCCGGCATCGCCGCCGCCGCGGCCTTCGCCCAG
ACCGGTGACCTCAACCGTCCGGCCGTCTTCGATATGGCCGCCCAGATTGAAGGACACCCG
GACAATGTGGCCCCGGCTGTGTTCGGTGGCCTGACCGTCTCTTGGGACTTCGAAACCGCA
GAAGGCGTCGGCTCGGTCGCCGTTCCTGGTGGTGAACCGCTGCACGGCGGATTCCACGCC
GTCAACTACCCGGTGGACCCGTCCATCACCGCCGCCGTGTTCGTGCCCGACTATGAGCTG
TCCACTGAGAAGGCCCGTCAGGCGCTGCCTAGGGAACTGCCATACAAGGACGCCGTCTAC
AACGTGTCTCGCGTGGGTCTGCTGCCCGCTGCGATGAATCCCATGGTGCTGGCCCAGGCC
GCCCAGCAGGGCAAGTCCGGCGTCGCCGCTGCCCCGGCTCAGGATGCCGATACGTGCGCT
TGCGCTGGCGGAACCCGTGAATCGCCGTTCGCTGACGAGCTTGCGGCCGCTCAGGCCCAG
TCCAACGCGCTACTGTTCACCGCCACGCAGGACAAGTTGCACCAGCCGTATCGCGGTACC
CTGATGCCGCCGTCCACCGAGCTCATTGCGCTCTTCCGCTCCAAGGGCTATGCCGCCGCC
GTCTCCGGTGCTGGCCCCTGCGTGCTCGTGCTGCACTACGGCAACGCCCGCGAAGCCATC
GACCAGATCGCATCGGAGCAGCTTGCTTCCGGCCACTGGCGTGTGCTTCACCTGCCCATC
AACACCGCCGGCGTCGAAATCGAGCGTCGCTAA
Enzyme 21 GenBank Gene ID AE014295 Link Image
Enzyme 21 GeneCard ID thrB Link Image
Enzyme 21 GenAtlas ID Not Available
Enzyme 21 HGNC ID Not Available
Enzyme 21 Chromosome Location 3
Enzyme 21 Locus 3p24.2
Enzyme 21 SNPs SNPJam Report Link Image
Enzyme 21 General References
  1. Schell MA, Karmirantzou M, Snel B, Vilanova D, Berger B, Pessi G, Zwahlen MC, Desiere F, Bork P, Delley M, Pridmore RD, Arigoni F: The genome sequence of Bifidobacterium longum reflects its adaptation to the human gastrointestinal tract. Proc Natl Acad Sci U S A. 2002 Oct 29;99(22):14422-7. Epub 2002 Oct 15. [PubMed Link Image]
Enzyme 21 Metabolite References Not Available
Enzyme 22 [top]
Enzyme 22 ID 15499
Enzyme 22 Name Homoserine kinase
Enzyme 22 Synonyms Not Available
Enzyme 22 Gene Name thrB
Enzyme 22 Protein Sequence >Homoserine kinase 
MIIMLEIIVPATSANIGPGFDCLGIALNIYNKFYVEEIESGLEIEGCEDAYKNENNLVYT
SMKYFFDRVKPEKIPAGIKIKIQSEVPICRGLGSSASCIVAGVIAANALSGANLDKNQLL
NIASEIEGHPDNVAPAILGNMIVSVTDNENIHYDIIKIPEELKFCAMIPNFKLSTEKARG
VLPKEIPYSDGVFNVSRVALLISALLNKNFDLLKVACQDKLHQDYRGTLIENYNDIVEKS
EQLNSIGVFLSGAGPTIMSLIKENDDSFVDNMKNYLQKLKSDWEIKELCCDSNGAVLNII
Enzyme 22 Number of Residues 300
Enzyme 22 Molecular Weight 33027.7
Enzyme 22 Theoretical pI 4.50
Enzyme 22 GO Classification
Function
  • ATP binding
  • adenyl nucleotide binding
  • adenyl ribonucleotide binding
  • binding
  • catalytic activity
  • homoserine kinase activity
  • kinase activity
  • nucleoside binding
  • phosphotransferase activity, alcohol group as acceptor
  • purine nucleoside binding
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • aspartate family amino acid metabolic process
  • cellular amino acid and derivative metabolic process
  • cellular amino acid metabolic process
  • cellular metabolic process
  • metabolic process
  • phosphate metabolic process
  • phosphorus metabolic process
  • phosphorylation
  • threonine metabolic process
Component
—
Enzyme 22 General Function Involved in ATP binding
Enzyme 22 Specific Function ATP + L-homoserine = ADP + O-phospho-L- homoserine
Enzyme 22 Pathways Not Available
Enzyme 22 Reactions
  • ATP + L-homoserine = ADP + O-phospho-L-homoserine [RN:R01771]
Enzyme 22 Pfam Domain Function
Enzyme 22 Signals
  • None
Enzyme 22 Transmembrane Regions
  • None
Enzyme 22 Essentiality Not Available
Enzyme 22 GenBank ID Protein 115249121 Link Image
Enzyme 22 UniProtKB/Swiss-Prot ID Q185Q8 Link Image
Enzyme 22 UniProtKB/Swiss-Prot Entry Name Q185Q8_CLOD6 Link Image
Enzyme 22 PDB ID Not Available
Enzyme 22 Cellular Location Not Available
Enzyme 22 Gene Sequence >903 bp 
ATGAGAAGTTTTGAAGAAGTAATTAAGTTTGCAAAAGAAAGAGGACCTAAAACTATATCA
GTAGCATGTTGCCAAGATAAAGAAGTTTTAATGGCAGTTGAAATGGCTAGAAAAGAAAAA
ATAGCAAATGCCATTTTAGTAGGAGATATAGAAAAGACTAAAGAAATTGCAAAAAGCATA
GACATGGATATCGAAAATTATGAACTGATAGATATAAAAGATTTAGCAGAAGCATCTCTA
AAATCTGTTGAATTAGTTTCACAAGGAAAAGCCGACATGGTAATGAAAGGCTTAGTAGAC
ACATCAATAATACTAAAAGCAGTTTTAAATAAAGAAGTAGGTCTTAGAACTGGAAATGTA
TTAAGTCACGTAGCAGTATTTGATGTAGAGGGATATGATAGATTATTTTTCGTAACTGAC
GCAGCTATGAACTTAGCTCCTGATACAAATACTAAAAAGCAAATCATAGAAAATGCTTGC
ACAGTAGCACATTCATTAGATATAAGTGAACCAAAAGTTGCTGCAATATGCGCAAAAGAA
AAAGTAAATCCAAAAATGAAAGATACAGTTGAAGCTAAAGAACTAGAAGAAATGTATGAA
AGAGGAGAAATCAAAGGTTGTATGGTTGGTGGACCTTTTGCAATTGATAATGCAGTATCT
TTAGAAGCAGCTAAACATAAAGGTATAAATCATCCTGTAGCAGGAAGAGCTGATATATTA
TTAGCCCCAGATATTGAAGGTGGTAACATATTATATAAAGCTTTGGTATTCTTCTCAAAA
TCAAAAAATGCAGGAGTTATAGTTGGGGCTAAAGCACCAATAATATTAACTTCTAGAGCA
GACAGTGAAGAAACTAAACTAAACTCAATAGCTTTAGGTGTTTTAATGGCAGCAAAGGCA
TAA
Enzyme 22 GenBank Gene ID AM180355 Link Image
Enzyme 22 GeneCard ID thrB Link Image
Enzyme 22 GenAtlas ID Not Available
Enzyme 22 HGNC ID Not Available
Enzyme 22 Chromosome Location 3
Enzyme 22 Locus 3p24.2
Enzyme 22 SNPs SNPJam Report Link Image
Enzyme 22 General References
  1. Sebaihia M, Wren BW, Mullany P, Fairweather NF, Minton N, Stabler R, Thomson NR, Roberts AP, Cerdeno-Tarraga AM, Wang H, Holden MT, Wright A, Churcher C, Quail MA, Baker S, Bason N, Brooks K, Chillingworth T, Cronin A, Davis P, Dowd L, Fraser A, Feltwell T, Hance Z, Holroyd S, Jagels K, Moule S, Mungall K, Price C, Rabbinowitsch E, Sharp S, Simmonds M, Stevens K, Unwin L, Whithead S, Dupuy B, Dougan G, Barrell B, Parkhill J: The multidrug-resistant human pathogen Clostridium difficile has a highly mobile, mosaic genome. Nat Genet. 2006 Jul;38(7):779-86. Epub 2006 Jun 25. [PubMed Link Image]
Enzyme 22 Metabolite References Not Available
Enzyme 23 [top]
Enzyme 23 ID 15500
Enzyme 23 Name Homoserine kinase
Enzyme 23 Synonyms
  1. HK
  2. HSK
Enzyme 23 Gene Name thrB
Enzyme 23 Protein Sequence >Homoserine kinase 
MKIRVPATSANLGPGFDSCGIALSAYLTINVLGESEFWEIQHTLGEEISTNEENLLIQTA
LKIAPELTPKVIRMVSDIPLARGLGSSSSVIVAGIELANRLAHLNLSPKEKVRLATEMEG
HPDNVAPAILGDFVVASHVENQVYHVKHHFPMCDVIAFIPEEPLFTEKSRAVLPEKLAYK
EAVAASSIANVMIAAILNGDLPLAGKMMEQDKWHETYRRSLVPHLKEIRRLTQQKGAYGS
FLSGAGPTVLILSPEERTNEIVQSLEKLSTKASIQIFNIDQEGVQVF
Enzyme 23 Number of Residues 287
Enzyme 23 Molecular Weight 31422.9
Enzyme 23 Theoretical pI 5.83
Enzyme 23 GO Classification
Function
  • ATP binding
  • adenyl nucleotide binding
  • adenyl ribonucleotide binding
  • binding
  • catalytic activity
  • homoserine kinase activity
  • kinase activity
  • nucleoside binding
  • phosphotransferase activity, alcohol group as acceptor
  • purine nucleoside binding
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • aspartate family amino acid metabolic process
  • cellular amino acid and derivative metabolic process
  • cellular amino acid metabolic process
  • cellular metabolic process
  • metabolic process
  • phosphate metabolic process
  • phosphorus metabolic process
  • phosphorylation
  • threonine metabolic process
Component
—
Enzyme 23 General Function Involved in ATP binding
Enzyme 23 Specific Function Catalyzes the ATP-dependent phosphorylation of L- homoserine to L-homoserine phosphate
Enzyme 23 Pathways Not Available
Enzyme 23 Reactions
  • ATP + L-homoserine = ADP + O-phospho-L-homoserine [RN:R01771]
Enzyme 23 Pfam Domain Function
Enzyme 23 Signals
  • None
Enzyme 23 Transmembrane Regions
  • None
Enzyme 23 Essentiality Not Available
Enzyme 23 GenBank ID Protein 29342436 Link Image
Enzyme 23 UniProtKB/Swiss-Prot ID Q831T0 Link Image
Enzyme 23 UniProtKB/Swiss-Prot Entry Name KHSE_ENTFA Link Image
Enzyme 23 PDB ID Not Available
Enzyme 23 Cellular Location Not Available
Enzyme 23 Gene Sequence >864 bp 
ATGGCTACAAAATTTTACACGAAACAATATGCAGGCTTATTAGCCAAAATTACAGAGAAA
AAATCTTATTTTTTACGTGCGTTTGGAGGAGAGTTGCAGACGTCGGATGCTGTAAAAGAT
AGCGACACATTTTTGATGCTAAAAACTTCAGATACACCTGTGGTAATGCAACCCTACAAC
ACTGGTGAAAACGTAGCGTTTGGTACAGGAACTGGCAACTCTAATCGTTTTGGGCCACGT
AAAGAAATTAAATCTATTGATACAACGGTTCCTTATGAATCTCCGTTAGCGATTCACGAA
GGAGTGGATAATATCACAGTAAACGATGACGCTGACGCAGTAGTAGCTGAAAGATTAGAG
GAACAAGCGATTGCTTGGGCTGAGTATATCGACGGTTTATTAGGTAAAGCATTATCTGAT
GCAGCCTCTGAAACGATTCGGTTTGAATTAACCAGTGAAGGAGTAACTAAGCTGTTCTCA
ACGGCGCATAAGACTTTTGTGAATAATTTAGTTTCTAAGTCTCTTGCTTGGGTTGCTTAT
GTTCACCCTGATGTTTATGATTTTTTAGTAGACAATGGTTTAGCAACAACAACTAAAAAT
TCAAGTGCTAACATTGATGAACAAACAATATATAAATTTAAAGGTTTTGTATTGGTTGAA
ATTCCAGAAAGCAAATTACAAACTGGGGAAATGGCTCAATTTTCCGCGGATAGCGTAGGT
ATTGCGGGCGTTGGTATTTCTGTAACACGTGCTATTGACTCCGAAGATTTTAACGGAGTA
GCAATCCAGGGAGCTGGAAAATATGGTAAACACATCCCTGAAAAAAATAAAGTAGCTATT
TTAAAAGCAGTAAAAAAAGCGTAA
Enzyme 23 GenBank Gene ID AE016830 Link Image
Enzyme 23 GeneCard ID thrB Link Image
Enzyme 23 GenAtlas ID Not Available
Enzyme 23 HGNC ID Not Available
Enzyme 23 Chromosome Location 3
Enzyme 23 Locus 3p24.2
Enzyme 23 SNPs SNPJam Report Link Image
Enzyme 23 General References
  1. Paulsen IT, Banerjei L, Myers GS, Nelson KE, Seshadri R, Read TD, Fouts DE, Eisen JA, Gill SR, Heidelberg JF, Tettelin H, Dodson RJ, Umayam L, Brinkac L, Beanan M, Daugherty S, DeBoy RT, Durkin S, Kolonay J, Madupu R, Nelson W, Vamathevan J, Tran B, Upton J, Hansen T, Shetty J, Khouri H, Utterback T, Radune D, Ketchum KA, Dougherty BA, Fraser CM: Role of mobile DNA in the evolution of vancomycin-resistant Enterococcus faecalis. Science. 2003 Mar 28;299(5615):2071-4. [PubMed Link Image]
Enzyme 23 Metabolite References Not Available
Enzyme 24 [top]
Enzyme 24 ID 15501
Enzyme 24 Name Homoserine kinase
Enzyme 24 Synonyms
  1. HK
  2. HSK
Enzyme 24 Gene Name thrB
Enzyme 24 Protein Sequence >Homoserine kinase 
MVKVYAPASSANMSVGFDVLGAAVTPVDGALLGDVVTVEAAETFSLNNLGRFADKLPSEP
RENIVYQCWERFCQELGKQIPVAMTLEKNMPIGSGLGSSACSVVAALMAMNEHCGKPLND
TRLLALMGELEGRISGSIHYDNVAPCFLGGMQLMIEENDIISQQVPGFDEWLWVLAYPGI
KVSTAEARAILPAQYRRQDCIAHGRHLAGFIHACYSRQPELAAKLMKDVIAEPYRERLLP
GFRQARQAVAEIGAVASGISGSGPTLFALCDKPETAQRVADWLGKNYLQNQEGFVHICRL
DTAGARVLEN
Enzyme 24 Number of Residues 310
Enzyme 24 Molecular Weight 33623.3
Enzyme 24 Theoretical pI 5.39
Enzyme 24 GO Classification
Function
  • ATP binding
  • adenyl nucleotide binding
  • adenyl ribonucleotide binding
  • binding
  • catalytic activity
  • homoserine kinase activity
  • kinase activity
  • nucleoside binding
  • phosphotransferase activity, alcohol group as acceptor
  • purine nucleoside binding
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • aspartate family amino acid metabolic process
  • cellular amino acid and derivative metabolic process
  • cellular amino acid metabolic process
  • cellular metabolic process
  • metabolic process
  • phosphate metabolic process
  • phosphorus metabolic process
  • phosphorylation
  • threonine metabolic process
Component
—
Enzyme 24 General Function Involved in ATP binding
Enzyme 24 Specific Function Catalyzes the ATP-dependent phosphorylation of L- homoserine to L-homoserine phosphate. Is also able to phosphorylate the hydroxy group on gamma-carbon of L-homoserine analogs when the functional group at the alpha-position is a carboxyl, an ester, or even a hydroxymethyl group. Neither L- threonine nor L-serine are substrates of the enzyme
Enzyme 24 Pathways Not Available
Enzyme 24 Reactions
  • ATP + L-homoserine = ADP + O-phospho-L-homoserine [RN:R01771]
Enzyme 24 Pfam Domain Function
Enzyme 24 Signals
  • None
Enzyme 24 Transmembrane Regions
  • None
Enzyme 24 Essentiality Not Available
Enzyme 24 GenBank ID Protein 85674277 Link Image
Enzyme 24 UniProtKB/Swiss-Prot ID P00547 Link Image
Enzyme 24 UniProtKB/Swiss-Prot Entry Name KHSE_ECOLI Link Image
Enzyme 24 PDB ID Not Available
Enzyme 24 Cellular Location Not Available
Enzyme 24 Gene Sequence >933 bp 
ATGGTTAAAGTTTATGCCCCGGCTTCCAGTGCCAATATGAGCGTCGGGTTTGATGTGCTC
GGGGCGGCGGTGACACCTGTTGATGGTGCATTGCTCGGAGATGTAGTCACGGTTGAGGCG
GCAGAGACATTCAGTCTCAACAACCTCGGACGCTTTGCCGATAAGCTGCCGTCAGAACCA
CGGGAAAATATCGTTTATCAGTGCTGGGAGCGTTTTTGCCAGGAACTGGGTAAGCAAATT
CCAGTGGCGATGACCCTGGAAAAGAATATGCCGATCGGTTCGGGCTTAGGCTCCAGTGCC
TGTTCGGTGGTCGCGGCGCTGATGGCGATGAATGAACACTGCGGCAAGCCGCTTAATGAC
ACTCGTTTGCTGGCTTTGATGGGCGAGCTGGAAGGCCGTATCTCCGGCAGCATTCATTAC
GACAACGTGGCACCGTGTTTTCTCGGTGGTATGCAGTTGATGATCGAAGAAAACGACATC
ATCAGCCAGCAAGTGCCAGGGTTTGATGAGTGGCTGTGGGTGCTGGCGTATCCGGGGATT
AAAGTCTCGACGGCAGAAGCCAGGGCTATTTTACCGGCGCAGTATCGCCGCCAGGATTGC
ATTGCGCACGGGCGACATCTGGCAGGCTTCATTCACGCCTGCTATTCCCGTCAGCCTGAG
CTTGCCGCGAAGCTGATGAAAGATGTTATCGCTGAACCCTACCGTGAACGGTTACTGCCA
GGCTTCCGGCAGGCGCGGCAGGCGGTCGCGGAAATCGGCGCGGTAGCGAGCGGTATCTCC
GGCTCCGGCCCGACCTTGTTCGCTCTGTGTGACAAGCCGGAAACCGCCCAGCGCGTTGCC
GACTGGTTGGGTAAGAACTACCTGCAAAATCAGGAAGGTTTTGTTCATATTTGCCGGCTG
GATACGGCGGGCGCACGAGTACTGGAAAACTAA
Enzyme 24 GenBank Gene ID AP009048 Link Image
Enzyme 24 GeneCard ID thrB Link Image
Enzyme 24 GenAtlas ID Not Available
Enzyme 24 HGNC ID Not Available
Enzyme 24 Chromosome Location 3
Enzyme 24 Locus 3p24.2
Enzyme 24 SNPs SNPJam Report Link Image
Enzyme 24 General References
  1. Cossart P, Katinka M, Yaniv M: Nucleotide sequence of the thrB gene of E. coli, and its two adjacent regions; the thrAB and thrBC junctions. Nucleic Acids Res. 1981 Jan 24;9(2):339-47. [PubMed Link Image]
  2. Yura T, Mori H, Nagai H, Nagata T, Ishihama A, Fujita N, Isono K, Mizobuchi K, Nakata A: Systematic sequencing of the Escherichia coli genome: analysis of the 0-2.4 min region. Nucleic Acids Res. 1992 Jul 11;20(13):3305-8. [PubMed Link Image]
  3. Burland V, Plunkett G 3rd, Sofia HJ, Daniels DL, Blattner FR: Analysis of the Escherichia coli genome VI: DNA sequence of the region from 92.8 through 100 minutes. Nucleic Acids Res. 1995 Jun 25;23(12):2105-19. [PubMed Link Image]
  4. Blattner FR, Plunkett G 3rd, Bloch CA, Perna NT, Burland V, Riley M, Collado-Vides J, Glasner JD, Rode CK, Mayhew GF, Gregor J, Davis NW, Kirkpatrick HA, Goeden MA, Rose DJ, Mau B, Shao Y: The complete genome sequence of Escherichia coli K-12. Science. 1997 Sep 5;277(5331):1453-74. [PubMed Link Image]
  5. Hayashi K, Morooka N, Yamamoto Y, Fujita K, Isono K, Choi S, Ohtsubo E, Baba T, Wanner BL, Mori H, Horiuchi T: Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110. Mol Syst Biol. 2006;2:2006.0007. Epub 2006 Feb 21. [PubMed Link Image]
  6. Huo X, Viola RE: Substrate specificity and identification of functional groups of homoserine kinase from Escherichia coli. Biochemistry. 1996 Dec 17;35(50):16180-5. [PubMed Link Image]
Enzyme 24 Metabolite References Not Available
Enzyme 25 [top]
Enzyme 25 ID 16645
Enzyme 25 Name Homoserine dehydrogenase
Enzyme 25 Synonyms Not Available
Enzyme 25 Gene Name thrA
Enzyme 25 Protein Sequence >Homoserine dehydrogenase 
MAHNSETPIRVGLLGAGTVGSQTARLIVEQKDELSARIGRPVELTGVACLDPKETEKFPW
IDQSIVTTDTLSVATNSDIVIELIGGTTVARKFVLAAIESGASVVTANKALLAKYGPEIY
SAAEAQGVDIYFEAAVGGAIPFLRPLRESLVGDKVTSMLGIVNGTTNYILDEMTTKGLQF
DDVLKDAQAKGYAEADPTGDIEGYDAANKAAIMATLGFHTSVTIDDVSVEGITKITADDI
AAATAEHKVIKLLAVVENGEAGVSARVYPALIDENHPLASVHGSFNAVFVKAEAADDLMF
YGRGAGGAPTASAVVGDVVTEARHIAAGCTGPSIPLYKNLPKAPITASKAAFAVRFLIHD
KPGVLAAIAAEFAKNGVSINGVNQDLKPTMTDPGYDGEIQQLRVVTHLTDEETLRNTVKA
VQALDFVTGDPSILRVLD
Enzyme 25 Number of Residues 438
Enzyme 25 Molecular Weight 45868.6
Enzyme 25 Theoretical pI 4.56
Enzyme 25 GO Classification
Function
  • NADP or NADPH binding
  • amino acid binding
  • binding
  • carboxylic acid binding
  • catalytic activity
  • homoserine dehydrogenase activity
  • nucleotide binding
  • oxidoreductase activity
  • oxidoreductase activity, acting on CH-OH group of donors
  • oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
Process
  • cellular amino acid and derivative metabolic process
  • cellular amino acid metabolic process
  • cellular metabolic process
  • metabolic process
  • oxidation reduction
Component
—
Enzyme 25 General Function Involved in amino acid binding
Enzyme 25 Specific Function L-homoserine + NAD(P)(+) = L-aspartate 4- semialdehyde + NAD(P)H
Enzyme 25 Pathways Not Available
Enzyme 25 Reactions
  • L-homoserine + NAD(P)+ = L-aspartate 4-semialdehyde + NAD(P)H + H+ [RN:R01773 R01775]
Enzyme 25 Pfam Domain Function
Enzyme 25 Signals
  • None
Enzyme 25 Transmembrane Regions
  • None
Enzyme 25 Essentiality Not Available
Enzyme 25 GenBank ID Protein 189428845 Link Image
Enzyme 25 UniProtKB/Swiss-Prot ID B3DPJ3 Link Image
Enzyme 25 UniProtKB/Swiss-Prot Entry Name B3DPJ3_BIFLD Link Image
Enzyme 25 PDB ID Not Available
Enzyme 25 Cellular Location Not Available
Enzyme 25 Gene Sequence >1317 bp 
ATGAAGATCAAGAAGAACCTCGTCGCGGCCACGGCGGCCGTGCTTGCGGCCGGCATGGCG
CTGGCCGGCTGCGGTTCCAGCAACGGAGGCAGCGGCGACGTCCAGAAGACCGCCGACGGC
AAGGTGAAGATCACCATGTGGCACGGCTTCTCCGAAGCCGACGGCAAGACGCTGGAATCC
ATCGTCGACGACTTCAACAAGTCCCAGGACAAGTACGAGATCGACGCCCAGCTGCAGCCA
TGGAGCACCATCGGCGAGACGATGGTCACCAAGGTCACCACCGGCGACGGCCCGGACTTC
GTCACCACCGGTGCCGACAATGGCCAGGGTTGGTCCATCGACGGCACCTTCCAGTGCGTC
TCCGATTTCTACGCCGACAAGAACAACGGCACCGGCGACTACCTCGACAACGTCGTCAAG
CAGATCACCTTCAACATCGACGGCGAGGAAGAGAAGTGCGCCGTTCCGATGGGCTACGCG
CCGACCTCCGTGTGGTACAACACCGACATGTGGAAGGCCGCCGGCCTGACCGACAAGGAC
ATTCCGACCACCTGGGACCAGCTCCTCGAGGTCGCCAAGAAGCTCACCAAGTCCGACGGT
TCGCAGTACGGCCTCGCGATGGCCGACTCCGGCTGGGCCGCCTACATGAAGGGCAACGGC
ACCGGCCTGTACACCACCGACGGCAAGGTCTCCATCAACTCCAAGGAGAACAAGGCCTTC
CTGCAGAAGATGCGTGACTTCTACAACGGCGGCTACGCCGTCCCGGGTCTGGACGACACC
GCGGCCCGCGAATCCTTCGAGTCCGGCCAGTCCGCAATGGTGATCGTCGGCCCGTGGGAG
GACCAGGCGGCCACCGACAAGGGCATCAACCACGACACCTTCGCCGTTCCGGACGGCGAC
GGCACCTACAAGTACGCCGACGGCAAGACCGGCTCCAACACCGGCTCCACCGGCCTGTAC
TGGTGGGTCACCTCGCAGGTCGGCGACTCCGAGAAGCTGCCCGGCATCTACGAGTTCTTC
AAGTTCTACAACAACCACGACAACCAGGTGAAGTGGTCCCTCGGCTCCGCCTACCCGCCG
AACAACAAGACCGTCACCGCCGATGAGCTGTCCGACCGTCCGCTGATCGCCAAGATCTCG
CAGTACACCGACAACTCCTACATCGGCATCGCCGGCCTCAAGGGCGGCTTCGGCGACATC
GCCGCCTCCCTCGACACCCTGACCCAGAACACCGTCCGCACCGGCGACGACATCCAGGGT
CTGCTCGACCAGGCCGAGAGCTCCATCTCGGGCTACCTCGACGAGTACGCCGAGTAG
Enzyme 25 GenBank Gene ID CP000605 Link Image
Enzyme 25 GeneCard ID thrA Link Image
Enzyme 25 GenAtlas ID Not Available
Enzyme 25 HGNC ID Not Available
Enzyme 25 Chromosome Location 1
Enzyme 25 Locus 17q11.2
Enzyme 25 SNPs SNPJam Report Link Image
Enzyme 25 General References
  1. Lee JH, Karamychev VN, Kozyavkin SA, Mills D, Pavlov AR, Pavlova NV, Polouchine NN, Richardson PM, Shakhova VV, Slesarev AI, Weimer B, O'Sullivan DJ: Comparative genomic analysis of the gut bacterium Bifidobacterium longum reveals loci susceptible to deletion during pure culture growth. BMC Genomics. 2008 May 27;9:247. [PubMed Link Image]
Enzyme 25 Metabolite References Not Available
Enzyme 26 [top]
Enzyme 26 ID 16646
Enzyme 26 Name Fused aspartokinase I and homoserine dehydrogenase I
Enzyme 26 Synonyms Not Available
Enzyme 26 Gene Name thrA
Enzyme 26 Protein Sequence >Fused aspartokinase I and homoserine dehydrogenase I 
MRVLKFGGTSVANAERFLRVADILESNARQGQVATVLSAPAKITNHLVAMIEKTISGQDA
LPNISDAERIFAELLTGLAAAQPGFPLAQLKTFVDQEFAQIKHVLHGISLLGQCPDSINA
ALICRGEKMSIAIMAGVLEARGHNVTVIDPVEKLLAVGHYLESTVDIAESTRRIAASRIP
ADHMVLMAGFTAGNEKGELVVLGRNGSDYSAAVLAACLRADCCEIWTDVDGVYTCDPRQV
PDARLLKSMSYQEAMELSYFGAKVLHPRTITPIAQFQIPCLIKNTGNPQAPGTLIGASRD
EDELPVKGISNLNNMAMFSVSGPGMKGMVGMAARVFAAMSRARISVVLITQSSSEYSISF
CVPQSDCVRAERAMQEEFYLELKEGLLEPLAVTERLAIISVVGDGMRTLRGISAKFFAAL
ARANINIVAIAQGSSERSISVVVNNDDATTGVRVTHQMLFNTDQVIEVFVIGVGGVGGAL
LEQLKRQQSWLKNKHIDLRVCGVANSKALLTNVHGLNLENWQEELAQAKEPFNLGRLIRL
VKEYHLLNPVIVDCTSSQAVADQYADFLREGFHVVTPNKKANTSSMDYYHQLRYAAEKSR
RKFLYDTNVGAGLPVIENLQNLLNAGDELMKFSGILSGSLSYIFGKLDEGMSFSEATTLA
REMGYTEPDPRDDLSGMDVARKLLILARETGRELELADIEIEPVLPAEFNAEGDVAAFMA
NLSQLDDLFAARVAKARDEGKVLRYVGNIDEDGVCRVKIAEVDGNDPLFKVKNGENALAF
YSHYYQPLPLVLRGYGAGNDVTAAGVFADLLRTLSWKLGV
Enzyme 26 Number of Residues 820
Enzyme 26 Molecular Weight 89119.4
Enzyme 26 Theoretical pI 5.39
Enzyme 26 GO Classification
Function
  • NADP or NADPH binding
  • amino acid binding
  • aspartate kinase activity
  • binding
  • carboxylic acid binding
  • catalytic activity
  • homoserine dehydrogenase activity
  • nucleotide binding
  • oxidoreductase activity
  • oxidoreductase activity, acting on CH-OH group of donors
  • oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
  • phosphotransferase activity, carboxyl group as acceptor
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • aspartate family amino acid biosynthetic process
  • cellular amino acid and derivative metabolic process
  • cellular amino acid biosynthetic process
  • cellular amino acid metabolic process
  • cellular metabolic process
  • metabolic process
  • oxidation reduction
Component
—
Enzyme 26 General Function Involved in amino acid binding
Enzyme 26 Specific Function Not Available
Enzyme 26 Pathways Not Available
Enzyme 26 Reactions Not Available
Enzyme 26 Pfam Domain Function
Enzyme 26 Signals
  • None
Enzyme 26 Transmembrane Regions
  • None
Enzyme 26 Essentiality Not Available
Enzyme 26 GenBank ID Protein 169887500 Link Image
Enzyme 26 UniProtKB/Swiss-Prot ID B1XBC7 Link Image
Enzyme 26 UniProtKB/Swiss-Prot Entry Name B1XBC7_ECODH Link Image
Enzyme 26 PDB ID Not Available
Enzyme 26 Cellular Location Not Available
Enzyme 26 Gene Sequence >2463 bp 
ATGCGAGTGTTGAAGTTCGGCGGTACATCAGTGGCAAATGCAGAACGTTTTCTGCGTGTT
GCCGATATTCTGGAAAGCAATGCCAGGCAGGGGCAGGTGGCCACCGTCCTCTCTGCCCCC
GCCAAAATCACCAACCACCTGGTGGCGATGATTGAAAAAACCATTAGCGGCCAGGATGCT
TTACCCAATATCAGCGATGCCGAACGTATTTTTGCCGAACTTTTGACGGGACTCGCCGCC
GCCCAGCCGGGGTTCCCGCTGGCGCAATTGAAAACTTTCGTCGATCAGGAATTTGCCCAA
ATAAAACATGTCCTGCATGGCATTAGTTTGTTGGGGCAGTGCCCGGATAGCATCAACGCT
GCGCTGATTTGCCGTGGCGAGAAAATGTCGATCGCCATTATGGCCGGCGTATTAGAAGCG
CGCGGTCACAACGTTACTGTTATCGATCCGGTCGAAAAACTGCTGGCAGTGGGGCATTAC
CTCGAATCTACCGTCGATATTGCTGAGTCCACCCGCCGTATTGCGGCAAGCCGCATTCCG
GCTGATCACATGGTGCTGATGGCAGGTTTCACCGCCGGTAATGAAAAAGGCGAACTGGTG
GTGCTTGGACGCAACGGTTCCGACTACTCTGCTGCGGTGCTGGCTGCCTGTTTACGCGCC
GATTGTTGCGAGATTTGGACGGACGTTGACGGGGTCTATACCTGCGACCCGCGTCAGGTG
CCCGATGCGAGGTTGTTGAAGTCGATGTCCTACCAGGAAGCGATGGAGCTTTCCTACTTC
GGCGCTAAAGTTCTTCACCCCCGCACCATTACCCCCATCGCCCAGTTCCAGATCCCTTGC
CTGATTAAAAATACCGGAAATCCTCAAGCACCAGGTACGCTCATTGGTGCCAGCCGTGAT
GAAGACGAATTACCGGTCAAGGGCATTTCCAATCTGAATAACATGGCAATGTTCAGCGTT
TCTGGTCCGGGGATGAAAGGGATGGTCGGCATGGCGGCGCGCGTCTTTGCAGCGATGTCA
CGCGCCCGTATTTCCGTGGTGCTGATTACGCAATCATCTTCCGAATACAGCATCAGTTTC
TGCGTTCCACAAAGCGACTGTGTGCGAGCTGAACGGGCAATGCAGGAAGAGTTCTACCTG
GAACTGAAAGAAGGCTTACTGGAGCCGCTGGCAGTGACGGAACGGCTGGCCATTATCTCG
GTGGTAGGTGATGGTATGCGCACCTTGCGTGGGATCTCGGCGAAATTCTTTGCCGCACTG
GCCCGCGCCAATATCAACATTGTCGCCATTGCTCAGGGATCTTCTGAACGCTCAATCTCT
GTCGTGGTAAATAACGATGATGCGACCACTGGCGTGCGCGTTACTCATCAGATGCTGTTC
AATACCGATCAGGTTATCGAAGTGTTTGTGATTGGCGTCGGTGGCGTTGGCGGTGCGCTG
CTGGAGCAACTGAAGCGTCAGCAAAGCTGGCTGAAGAATAAACATATCGACTTACGTGTC
TGCGGTGTTGCCAACTCGAAGGCTCTGCTCACCAATGTACATGGCCTTAATCTGGAAAAC
TGGCAGGAAGAACTGGCGCAAGCCAAAGAGCCGTTTAATCTCGGGCGCTTAATTCGCCTC
GTGAAAGAATATCATCTGCTGAACCCGGTCATTGTTGACTGCACTTCCAGCCAGGCAGTG
GCGGATCAATATGCCGACTTCCTGCGCGAAGGTTTCCACGTTGTCACGCCGAACAAAAAG
GCCAACACCTCGTCGATGGATTACTACCATCAGTTGCGTTATGCGGCGGAAAAATCGCGG
CGTAAATTCCTCTATGACACCAACGTTGGGGCTGGATTACCGGTTATTGAGAACCTGCAA
AATCTGCTCAATGCAGGTGATGAATTGATGAAGTTCTCCGGCATTCTTTCTGGTTCGCTT
TCTTATATCTTCGGCAAGTTAGACGAAGGCATGAGTTTCTCCGAGGCGACCACGCTGGCG
CGGGAAATGGGTTATACCGAACCGGACCCGCGAGATGATCTTTCTGGTATGGATGTGGCG
CGTAAACTATTGATTCTCGCTCGTGAAACGGGACGTGAACTGGAGCTGGCGGATATTGAA
ATTGAACCTGTGCTGCCCGCAGAGTTTAACGCCGAGGGTGATGTTGCCGCTTTTATGGCG
AATCTGTCACAACTCGACGATCTCTTTGCCGCGCGCGTGGCGAAGGCCCGTGATGAAGGA
AAAGTTTTGCGCTATGTTGGCAATATTGATGAAGATGGCGTCTGCCGCGTGAAGATTGCC
GAAGTGGATGGTAATGATCCGCTGTTCAAAGTGAAAAATGGCGAAAACGCCCTGGCCTTC
TATAGCCACTATTATCAGCCGCTGCCGTTGGTACTGCGCGGATATGGTGCGGGCAATGAC
GTTACAGCTGCCGGTGTCTTTGCTGATCTGCTACGTACCCTCTCATGGAAGTTAGGAGTC
TGA
Enzyme 26 GenBank Gene ID CP000948 Link Image
Enzyme 26 GeneCard ID thrA Link Image
Enzyme 26 GenAtlas ID Not Available
Enzyme 26 HGNC ID Not Available
Enzyme 26 Chromosome Location 1
Enzyme 26 Locus 17q11.2
Enzyme 26 SNPs SNPJam Report Link Image
Enzyme 26 General References
  1. Durfee T, Nelson R, Baldwin S, Plunkett G 3rd, Burland V, Mau B, Petrosino JF, Qin X, Muzny DM, Ayele M, Gibbs RA, Csorgo B, Posfai G, Weinstock GM, Blattner FR: The complete genome sequence of Escherichia coli DH10B: insights into the biology of a laboratory workhorse. J Bacteriol. 2008 Apr;190(7):2597-606. Epub 2008 Feb 1. [PubMed Link Image]
Enzyme 26 Metabolite References Not Available
Enzyme 27 [top]
Enzyme 27 ID 16647
Enzyme 27 Name Fused aspartokinase II
Enzyme 27 Synonyms
  1. homoserine dehydrogenase II
Enzyme 27 Gene Name metL
Enzyme 27 Protein Sequence >Fused aspartokinase II 
MSVIAQAGAKGRQLHKFGGSSLADVKCYLRVAGIMAEYSQPDDMMVVSAAGSTTNQLINW
LKLSQTDRLSAHQVQQTLRRYQCDLISGLLPAEEADSLISAFVSDLERLAALLDSGINDA
VYAEVVGHGEVWSARLMSAVLNQQGLPAAWLDAREFLRAERAAQPQVDEGLSYPLLQQLL
VQHPGKRLVVTGFISRNNAGETVLLGRNGSDYSATQIGALAGVSRVTIWSDVAGVYSADP
RKVKDACLLPLLRLDEASELARLAAPVLHARTLQPVSGSEIDLQLRCSYTPDQGSTRIER
VLASGTGARIVTSHDDVCLIEFQVPASQDFKLAHKEIDQILKRAQVRPLAVGVHNDRQLL
QFCYTSEVADSALKILDEAGLPGELRLRQGLALVAMVGAGVTRNPLHCHRFWQQLKGQPV
EFTWQSDDGISLVAVLRTGPTESLIQGLHQSVFRAEKRIGLVLFGKGNIGSRWLELFARE
QSTLSARTGFEFVLAGVVDSRRSLLSYDGLDASRALAFFNDEAVEQDEESLFLWMRAHPY
DDLVVLDVTASQQLADQYLDFASHGFHVISANKLAGASDSNKYRQIHDAFEKTGRHWLYN
ATVGAGLPINHTVRDLIDSGDTILSISGIFSGTLSWLFLQFDGSVPFTELVDQAWQQGLT
EPDPRDDLSGKDVMRKLVILAREAGYNIEPDQVRVESLVPAHCEGGSIDHFFENGDELNE
QMVQRLEAAREMGLVLRYVARFDANGKARVGVEAVREDHPLASLLPCDNVFAIESRWYRD
NPLVIRGPGAGRDVTAGAIQSDINRLAQLL
Enzyme 27 Number of Residues 810
Enzyme 27 Molecular Weight 88886.8
Enzyme 27 Theoretical pI 5.27
Enzyme 27 GO Classification
Function
  • NADP or NADPH binding
  • aspartate kinase activity
  • binding
  • catalytic activity
  • homoserine dehydrogenase activity
  • nucleotide binding
  • oxidoreductase activity
  • oxidoreductase activity, acting on CH-OH group of donors
  • oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
  • phosphotransferase activity, carboxyl group as acceptor
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • aspartate family amino acid biosynthetic process
  • cellular amino acid and derivative metabolic process
  • cellular amino acid biosynthetic process
  • cellular amino acid metabolic process
  • cellular metabolic process
  • metabolic process
  • oxidation reduction
Component
—
Enzyme 27 General Function Involved in cellular amino acid biosynthetic process
Enzyme 27 Specific Function Not Available
Enzyme 27 Pathways Not Available
Enzyme 27 Reactions Not Available
Enzyme 27 Pfam Domain Function
Enzyme 27 Signals
  • None
Enzyme 27 Transmembrane Regions
  • None
Enzyme 27 Essentiality Not Available
Enzyme 27 GenBank ID Protein 169887648 Link Image
Enzyme 27 UniProtKB/Swiss-Prot ID B1XBA6 Link Image
Enzyme 27 UniProtKB/Swiss-Prot Entry Name B1XBA6_ECODH Link Image
Enzyme 27 PDB ID Not Available
Enzyme 27 Cellular Location Not Available
Enzyme 27 Gene Sequence >2433 bp 
ATGGCGATGAAAAAGTTGCTCATAGCGTCGCTGCTGTTTAGCAGCGCCACCGTATACGGT
GCTGAAGGGTTCGTAGTGAAAGATATTCATTTCGAAGGCCTTCAGCGTGTCGCCGTTGGT
GCGGCCCTCCTCAGTATGCCGGTGCGCACAGGCGACACGGTTAATGATGAAGATATCAGT
AATACCATTCGCGCTCTGTTTGCTACCGGCAACTTTGAGGATGTTCGCGTCCTTCGTGAT
GGTGATACCCTTCTGGTTCAGGTAAAAGAACGTCCGACCATTGCCAGCATTACTTTCTCC
GGTAACAAATCGGTGAAAGATGACATGCTGAAGCAAAACCTCGAGGCTTCTGGTGTGCGT
GTGGGCGAATCCCTCGATCGCACCACCATTGCCGATATCGAGAAAGGTCTGGAAGACTTC
TACTACAGCGTCGGTAAATATAGCGCCAGCGTAAAAGCTGTCGTGACCCCGCTGCCGCGC
AACCGTGTTGACCTAAAACTGGTGTTCCAGGAAGGTGTGTCAGCTGAAATCCAGCAAATT
AACATTGTTGGTAACCATGCTTTCACCACCGACGAACTGATCTCTCATTTCCAACTGCGT
GACGAAGTGCCGTGGTGGAACGTGGTAGGCGATCGTAAATACCAGAAACAGAAACTGGCG
GGCGACCTTGAAACCCTGCGCAGCTACTATCTGGATCGCGGTTATGCCCGTTTCAACATC
GACTCTACCCAGGTCAGTCTGACGCCAGATAAAAAAGGTATTTACGTCACGGTGAACATC
ACCGAAGGCGATCAGTACAAGCTTTCTGGCGTTGAAGTGAGCGGCAACCTTGCCGGGCAC
TCCGCTGAAATTGAGCAGCTGACTAAGATCGAGCCGGGTGAGCTGTATAACGGCACCAAA
GTGACCAAGATGGAAGATGACATCAAAAAGCTTCTCGGTCGCTATGGTTATGCCTATCCG
CGCGTACAGTCGATGCCCGAAATTAACGATGCCGACAAAACCGTTAAATTACGTGTGAAC
GTTGATGCGGGTAACCGTTTCTACGTGCGTAAGATCCGTTTTGAAGGTAACGATACCTCG
AAAGATGCCGTCCTGCGTCGCGAAATGCGTCAGATGGAAGGTGCATGGCTGGGGAGCGAT
CTGGTCGATCAGGGTAAGGAGCGTCTGAATCGTCTGGGCTTCTTTGAAACTGTCGATACC
GATACCCAACGTGTTCCGGGTAGCCCGGACCAGGTTGATGTCGTCTACAAGGTAAAAGAG
CGCAACACCGGTAGCTTCAACTTTGGTATTGGTTACGGTACTGAAAGTGGCGTGAGCTTC
CAGGCTGGTGTGCAGCAGGATAACTGGTTAGGTACAGGTTATGCTGTTGGTATCAACGGG
ACCAAAAACGATTACCAGACCTATGCTGAACTGTCGGTAACCAACCCGTACTTCACCGTA
GATGGCGTAAGCCTCGGTGGTCGTCTCTTCTATAATGACTTCCAGGCAGATGACGCCGAC
CTGTCCGACTATACCAACAAGAGTTATGGTACAGACGTGACGTTGGGCTTCCCGATTAAC
GAATATAACTCGCTGCGTGCAGGTCTGGGTTATGTACATAACTCCCTGTCCAACATGCAG
CCTCAGGTTGCGATGTGGCGTTATCTGTACTCTATGGGTGAACATCCGAGCACCTCTGAT
CAGGATAACAGCTTCAAAACGGACGACTTCACGTTCAACTATGGTTGGACCTATAACAAG
CTTGACCGTGGTTACTTCCCGACAGATGGTTCACGTGTCAACCTGACCGGTAAAGTGACC
ATTCCTGGATCGGATAACGAATACTACAAAGTGACGTTAGACACGGCGACTTATGTGCCG
ATCGATGACGATCACAAATGGGTTGTTCTGGGGCGTACCCGCTGGGGTTATGGTGATGGT
TTAGGCGGCAAAGAGATGCCGTTCTACGAGAACTTCTATGCCGGTGGTTCCAGCACCGTG
CGTGGCTTCCAGTCCAATACCATTGGTCCGAAAGCAGTTTACTTCCCGCATCAGGCCAGT
AATTATGATCCGGACTATGATTACGAATGTGCGACTCAGGACGGCGCGAAAGACCTGTGT
AAATCGGATGATGCTGTAGGCGGTAACGCCATGGCGGTTGCCAGCCTCGAGTTCATCACC
CCGACGCCGTTTATTAGCGATAAGTATGCTAACTCGGTTCGTACTTCCTTCTTCTGGGAT
ATGGGTACCGTTTGGGATACAAACTGGGATTCCAGCCAATATTCTGGATATCCGGACTAT
AGTGATCCAAGCAATATCCGTATGTCTGCGGGTATCGCATTACAATGGATGTCCCCATTG
GGGCCGTTGGTGTTCTCCTACGCCCAGCCGTTCAAAAAGTACGATGGAGACAAGGCAGAA
CAGTTCCAGTTTAACATCGGTAAAACCTGGTAA
Enzyme 27 GenBank Gene ID CP000948 Link Image
Enzyme 27 GeneCard ID metL Link Image
Enzyme 27 GenAtlas ID Not Available
Enzyme 27 HGNC ID Not Available
Enzyme 27 Chromosome Location Not Available
Enzyme 27 Locus ECDH10B_4129
Enzyme 27 SNPs SNPJam Report Link Image
Enzyme 27 General References
  1. Durfee T, Nelson R, Baldwin S, Plunkett G 3rd, Burland V, Mau B, Petrosino JF, Qin X, Muzny DM, Ayele M, Gibbs RA, Csorgo B, Posfai G, Weinstock GM, Blattner FR: The complete genome sequence of Escherichia coli DH10B: insights into the biology of a laboratory workhorse. J Bacteriol. 2008 Apr;190(7):2597-606. Epub 2008 Feb 1. [PubMed Link Image]
Enzyme 27 Metabolite References Not Available
Enzyme 28 [top]
Enzyme 28 ID 16648
Enzyme 28 Name Homoserine trans-succinylase
Enzyme 28 Synonyms Not Available
Enzyme 28 Gene Name metA
Enzyme 28 Protein Sequence >Homoserine trans-succinylase 
MPIKIPSGLPARDILDSERIFALEKPEAERQRVRPLKLVILNLMPKKIETETQLLRLISK
SPLQVEIDFMKTSTHEATHVSADHLVKFYENLDAFKDNYYDGFVVTGAPVEHMPFEDVDY
WDEFKTILDWASTHVFSTMYLCWGAMGALYYRYGIHKVDYPEKIFGVFPQYLQDEYCFLT
NGFDEIDLQPHSRLAGVNENEVRANHDLQILTWGPQSGPGLIATRDFSEVFALGHWEYGK
YTLAEEYERDMAKGMTNVPFPKNYFPHDDPKLEPLFAWRAHANLLWRNWLNWVYQTTPYD
LTEVPQLRAEKKLGTDRSIRHEPGGPRQDDFKPFVHDGYGVIQG
Enzyme 28 Number of Residues 344
Enzyme 28 Molecular Weight 40040.1
Enzyme 28 Theoretical pI 5.27
Enzyme 28 GO Classification
Function
  • acyltransferase activity
  • catalytic activity
  • transferase activity
  • transferase activity, transferring acyl groups
  • transferase activity, transferring acyl groups other than amino-acyl groups
Process
  • L-methionine biosynthetic process from L-homoserine via cystathionine
  • L-methionine biosynthetic process from homoserine via O-succinyl-L-homoserine and cystathionine
  • cellular amino acid and derivative metabolic process
  • cellular amino acid metabolic process
  • cellular metabolic process
  • homoserine metabolic process
  • metabolic process
  • serine family amino acid metabolic process
Component
  • cell part
  • cytoplasm
  • intracellular part
Enzyme 28 General Function Involved in acyltransferase activity
Enzyme 28 Specific Function Not Available
Enzyme 28 Pathways Not Available
Enzyme 28 Reactions Not Available
Enzyme 28 Pfam Domain Function
Enzyme 28 Signals
  • None
Enzyme 28 Transmembrane Regions
  • None
Enzyme 28 Essentiality Not Available
Enzyme 28 GenBank ID Protein 189428428 Link Image
Enzyme 28 UniProtKB/Swiss-Prot ID B3DTV7 Link Image
Enzyme 28 UniProtKB/Swiss-Prot Entry Name B3DTV7_BIFLD Link Image
Enzyme 28 PDB ID Not Available
Enzyme 28 Cellular Location Not Available
Enzyme 28 Gene Sequence >1035 bp 
ATGCCTATCAAGATCCCCAGTGGCCTGCCGGCCAGAGATATCCTCGATTCGGAGCGCATC
TTCGCTCTGGAGAAGCCCGAGGCGGAGCGTCAGCGCGTCCGCCCGCTCAAACTGGTGATC
CTGAACTTGATGCCTAAGAAAATCGAGACTGAAACGCAGCTGCTGCGTCTGATTTCCAAG
TCGCCGTTGCAGGTCGAAATCGACTTCATGAAGACCTCCACGCATGAGGCCACGCACGTT
TCCGCCGATCATCTCGTCAAGTTCTACGAAAACCTCGATGCGTTCAAAGACAACTATTAC
GACGGTTTTGTGGTCACCGGCGCGCCTGTAGAGCATATGCCGTTCGAAGATGTGGACTAC
TGGGACGAGTTCAAGACGATTCTCGACTGGGCCTCCACCCATGTGTTCTCCACCATGTAC
CTGTGCTGGGGTGCGATGGGCGCACTGTACTACCGCTACGGCATCCACAAGGTGGATTAC
CCCGAGAAGATTTTCGGCGTATTCCCGCAGTACCTGCAGGATGAATACTGCTTCCTGACC
AATGGCTTCGACGAGATTGATCTGCAGCCGCACTCCCGCCTCGCCGGCGTGAACGAAAAC
GAGGTACGTGCCAACCATGACCTTCAGATCTTGACTTGGGGACCGCAGTCCGGCCCGGGC
CTGATCGCCACGCGTGACTTCTCCGAAGTGTTCGCGCTCGGCCATTGGGAGTACGGCAAG
TACACGCTCGCCGAAGAATACGAGCGCGATATGGCCAAGGGCATGACCAACGTGCCCTTC
CCGAAGAACTATTTCCCGCATGACGATCCGAAGCTGGAACCGTTGTTCGCCTGGCGCGCC
CACGCCAATCTGCTGTGGCGCAACTGGCTCAACTGGGTGTACCAGACCACGCCGTATGAC
CTGACCGAGGTGCCGCAGCTCAGGGCTGAGAAGAAGCTCGGTACTGATCGTTCGATTCGG
CATGAGCCGGGCGGGCCGCGCCAGGATGATTTCAAGCCGTTTGTGCATGACGGGTATGGG
GTGATTCAGGGCTGA
Enzyme 28 GenBank Gene ID CP000605 Link Image
Enzyme 28 GeneCard ID metA Link Image
Enzyme 28 GenAtlas ID Not Available
Enzyme 28 HGNC ID Not Available
Enzyme 28 Chromosome Location Not Available
Enzyme 28 Locus BLD_1130
Enzyme 28 SNPs SNPJam Report Link Image
Enzyme 28 General References
  1. Lee JH, Karamychev VN, Kozyavkin SA, Mills D, Pavlov AR, Pavlova NV, Polouchine NN, Richardson PM, Shakhova VV, Slesarev AI, Weimer B, O'Sullivan DJ: Comparative genomic analysis of the gut bacterium Bifidobacterium longum reveals loci susceptible to deletion during pure culture growth. BMC Genomics. 2008 May 27;9:247. [PubMed Link Image]
Enzyme 28 Metabolite References Not Available
Enzyme 29 [top]
Enzyme 29 ID 16649
Enzyme 29 Name Homoserine O-succinyltransferase
Enzyme 29 Synonyms
  1. Homoserine O-transsuccinylase
  2. HTS
Enzyme 29 Gene Name metA
Enzyme 29 Protein Sequence >Homoserine O-succinyltransferase 
MPIRVPDELPAVNFLREENVFVMTTSRASGQEIRPLKVLILNLMPKKIETENQFLRLLSN
SPLQVDIQLLRIDSRESRNTPAEHLNNFYCNFEDIQDQNFDGLIVTGAPLGLVEFNDVAY
WPQIKQVLEWSKDHVTSTLFVCWAVQAALNILYGIPKQTRTEKLSGVYEHHILHPHALLT
RGFDDSFLAPHSRYADFPAALIRDYTDLEILAETEEGDAYLFASKDKRIAFVTGHPEYDA
QTLAQEFFRDVEAGLDPDVPYNYFPHNDPQNTPRASWRSHGNLLFTNWLNYYVYQITPYD
LRHMNPTLD
Enzyme 29 Number of Residues 309
Enzyme 29 Molecular Weight 35727.0
Enzyme 29 Theoretical pI 4.85
Enzyme 29 GO Classification
Function
  • acyltransferase activity
  • catalytic activity
  • transferase activity
  • transferase activity, transferring acyl groups
  • transferase activity, transferring acyl groups other than amino-acyl groups
Process
  • L-methionine biosynthetic process from L-homoserine via cystathionine
  • L-methionine biosynthetic process from homoserine via O-succinyl-L-homoserine and cystathionine
  • cellular amino acid and derivative metabolic process
  • cellular amino acid metabolic process
  • cellular metabolic process
  • homoserine metabolic process
  • metabolic process
  • serine family amino acid metabolic process
Component
  • cell part
  • cytoplasm
  • intracellular part
Enzyme 29 General Function Involved in acyltransferase activity
Enzyme 29 Specific Function Succinyl-CoA + L-homoserine = CoA + O- succinyl-L-homoserine
Enzyme 29 Pathways Not Available
Enzyme 29 Reactions
  • succinyl-CoA + L-homoserine = CoA + O-succinyl-L-homoserine [RN:R01777]
Enzyme 29 Pfam Domain Function
Enzyme 29 Signals
  • None
Enzyme 29 Transmembrane Regions
  • None
Enzyme 29 Essentiality Not Available
Enzyme 29 GenBank ID Protein 169887728 Link Image
Enzyme 29 UniProtKB/Swiss-Prot ID B1XC12 Link Image
Enzyme 29 UniProtKB/Swiss-Prot Entry Name META_ECODH Link Image
Enzyme 29 PDB ID Not Available
Enzyme 29 Cellular Location Not Available
Enzyme 29 Gene Sequence >930 bp 
ATGATTCAGCAAGGAGATCTCATGCCGCAGTCCGCGTTGTTCACGGGAATCATTCCCCCT
GTCTCCACCATTTTTACCGCCGACGGCCAGCTCGATAAGCCGGGCACCGCCGCGCTGATC
GACGATCTGATCAAAGCAGGCGTTGACGGCCTGTTCTTCCTGGGCAGCGGTGGCGAGTTC
TCCCAGCTCGGCGCCGAAGAGCGTAAAGCCATTGCCCGCTTTGCTATCGATCATGTCGAT
CGTCGCGTGCCGGTGCTGATCGGCACCGGCGGCACCAACGCCCGGGAAACCATCGAACTC
AGCCAGCACGCGCAGCAGGCGGGCGCGGACGGCATCGTGGTGATCAACCCCTACTACTGG
AAAGTGTCGGAAGCGAACCTGATCCGCTATTTCGAGCAGGTGGCCGACAGCGTCACGCTG
CCGGTGATGCTCTATAACTTCCCGGCGCTGACCGGGCAGGATCTGACTCCGGCGCTGGTG
AAAACCCTCGCCGACTCGCGCAGCAATATTATCGGCATCAAAGACACCATCGACTCCGTC
GCCCACCTGCGCAGCATGATCCATACCGTCAAAGGTGCCCATCCGCACTTCACCGTGCTC
TGCGGCTACGACGATCATCTGTTCAATACCCTGCTGCTCGGCGGCGACGGGGCGATATCG
GCGAGCGGCAACTTTGCCCCGCAGGTGTCGGTGAATCTTCTGAAAGCCTGGCGCGACGGG
GACGTGGCGAAAGCGGCCGGGTATCATCAGACCTTGCTGCAAATTCCGCAGATGTATCAG
CTGGATACGCCGTTTGTGAACGTGATTAAAGAGGCGATCGTGCTCTGCGGTCGTCCTGTC
TCCACGCACGTGCTGCCGCCCGCCTCGCCGCTGGACGAGCCGCGCAAGGCGCAGCTGAAA
ACCCTGCTGCAACAGCTCAAGCTTTGCTGA
Enzyme 29 GenBank Gene ID CP000948 Link Image
Enzyme 29 GeneCard ID metA Link Image
Enzyme 29 GenAtlas ID Not Available
Enzyme 29 HGNC ID Not Available
Enzyme 29 Chromosome Location Not Available
Enzyme 29 Locus ECDH10B_4202
Enzyme 29 SNPs SNPJam Report Link Image
Enzyme 29 General References
  1. Durfee T, Nelson R, Baldwin S, Plunkett G 3rd, Burland V, Mau B, Petrosino JF, Qin X, Muzny DM, Ayele M, Gibbs RA, Csorgo B, Posfai G, Weinstock GM, Blattner FR: The complete genome sequence of Escherichia coli DH10B: insights into the biology of a laboratory workhorse. J Bacteriol. 2008 Apr;190(7):2597-606. Epub 2008 Feb 1. [PubMed Link Image]
Enzyme 29 Metabolite References Not Available
Enzyme 30 [top]
Enzyme 30 ID 16650
Enzyme 30 Name Homoserine kinase
Enzyme 30 Synonyms Not Available
Enzyme 30 Gene Name thrB
Enzyme 30 Protein Sequence >Homoserine kinase 
MNPICNSVHVRVPATSANLGSGFDTVGLALDYHDELTFTLNDDPNDGIAHVIIHGEGADA
LPCDETHLVVSTFRRACATFGLGRLGFTLEATNNIPQARGMGSSAEAIVAGIAAAAAFAQ
TGDLNRPAVFDMAAQIEGHPDNVAPAVFGGLTVSWDFETAEGVGSVAVPGGEPLHGGFHA
VNYPVDPSITAAVFVPDYELSTEKARQALPRELPYKDAVYNVSRVGLLPAAMNPVVLAQA
AQQGKSGVAAAPAQDADTCACSGGTRESAFADELAAAQAQSNALLFTATQDKLHQPYRGA
LMPPSTELIALFRSKGYAAAVSGAGPCVLVLHYGNAREAIDQIASEQLASGHWRVLHLPI
NTAGVEIERR
Enzyme 30 Number of Residues 370
Enzyme 30 Molecular Weight 38486.8
Enzyme 30 Theoretical pI 4.73
Enzyme 30 GO Classification
Function
  • ATP binding
  • adenyl nucleotide binding
  • adenyl ribonucleotide binding
  • binding
  • catalytic activity
  • homoserine kinase activity
  • kinase activity
  • nucleoside binding
  • phosphotransferase activity, alcohol group as acceptor
  • purine nucleoside binding
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • aspartate family amino acid metabolic process
  • cellular amino acid and derivative metabolic process
  • cellular amino acid metabolic process
  • cellular metabolic process
  • metabolic process
  • phosphate metabolic process
  • phosphorus metabolic process
  • phosphorylation
  • threonine metabolic process
Component
—
Enzyme 30 General Function Involved in ATP binding
Enzyme 30 Specific Function ATP + L-homoserine = ADP + O-phospho-L- homoserine
Enzyme 30 Pathways Not Available
Enzyme 30 Reactions Not Available
Enzyme 30 Pfam Domain Function
Enzyme 30 Signals
  • None
Enzyme 30 Transmembrane Regions
  • None
Enzyme 30 Essentiality Not Available
Enzyme 30 GenBank ID Protein 189428788 Link Image
Enzyme 30 UniProtKB/Swiss-Prot ID B3DPJ4 Link Image
Enzyme 30 UniProtKB/Swiss-Prot Entry Name B3DPJ4_BIFLD Link Image
Enzyme 30 PDB ID Not Available
Enzyme 30 Cellular Location Not Available
Enzyme 30 Gene Sequence >1113 bp 
ATGGCAGGCCCGTACGCGGGAACTTTATCGGATTTGCCGACTGTCCGCGACGAAGTAACA
TGTTCGATTAATGCGGAGAACCCAACGGGAGCCAAGGGTTTTGGTTGCCGTGAAACTGGT
CCGTTGGGGCCGTCGCGCAAGGGAAAACCGTGTTTGAATGACATTGCTCCCGGGCAGTCT
GTGACATTGGCAGATATTGAAGGCCCCGGTTGTATTCGGCACATGTGGTTTACCGTTACG
GATCGCACCAGTGACGCTGATCGATACGTTCTGCGCGATGCGGTGCTTGCCATCTATTGG
GATGATGAAAAGCGACCTTCTGTGGAATGTCCCCTAGGAGACTTCTTCTGTTGCGGCTTT
GGACAAAGTTGCGATGTGTTCTCAGAGCCTATTGTGGTGGCACCTACACGAGGTATGAAT
TGTTATTTCACGATGCCGTTTCGTAAACGGGCACGTATCGTAGTGCGCAATGACCACGCT
CATGCTATTCCGGCTTTGTTTTATCAGATTGATTATGCATTGGGTAATGCGTATTCCTCC
CGTGAAATGGCTTATTTCCATGCGCAATGGCGCAGACAGCCAATCACTACTTTAGGCGAG
GACTATGTAATCCTCGATGGAGTCAGCGGACGGGGCCATTACGTCGGCACATATCTTGCT
ATTTCTACGTTGCAACGATATTGGTGGGGTGAGGGAGAGATTAAGTTTTTCCTAGATGGC
GATAACGATTATCCCACAGTGTGTAGTACCGGCACCGAAGATTATTTTGGCGGTGCATGG
AGCTTCGCTGAGCAGCGAGATGGTCATACGCGCGAGCGTACTTTTTGTGCCCCATATGTA
GGATATCCATTTTATTCTGTGCGCGATGGGGCTATAGCAAACCAATATCATGACGATTAT
TGTCCACCTATGCGTGGCTTGTACCGATGGCATATTCCTGATCCCATCAGGTTTGATAGT
GAGCTTAGAGTCACGCTTCAACAAATTGGTTCAGGATATGAAGGTGCATTTGAGCGTCAG
GATGATGTGTCTAGCGTGGCGTACTGGTATCAAATTGAGCCACATTCAATTTTTCCCGAG
CTGCCCGAGCCTTCGAAACGTCATCCTAGGTGA
Enzyme 30 GenBank Gene ID CP000605 Link Image
Enzyme 30 GeneCard ID thrB Link Image
Enzyme 30 GenAtlas ID Not Available
Enzyme 30 HGNC ID Not Available
Enzyme 30 Chromosome Location 3
Enzyme 30 Locus 3p24.2
Enzyme 30 SNPs SNPJam Report Link Image
Enzyme 30 General References
  1. Lee JH, Karamychev VN, Kozyavkin SA, Mills D, Pavlov AR, Pavlova NV, Polouchine NN, Richardson PM, Shakhova VV, Slesarev AI, Weimer B, O'Sullivan DJ: Comparative genomic analysis of the gut bacterium Bifidobacterium longum reveals loci susceptible to deletion during pure culture growth. BMC Genomics. 2008 May 27;9:247. [PubMed Link Image]
Enzyme 30 Metabolite References Not Available
Enzyme 31 [top]
Enzyme 31 ID 16651
Enzyme 31 Name Homoserine kinase
Enzyme 31 Synonyms
  1. HK
  2. HSK
Enzyme 31 Gene Name thrB
Enzyme 31 Protein Sequence >Homoserine kinase 
MVKVYAPASSANMSVGFDVLGAAVTPVDGALLGDVVTVEAAETFSLNNLGRFADKLPSEP
RENIVYQCWERFCQELGKQIPVAMTLEKNMPIGSGLGSSACSVVAALMAMNEHCGKPLND
TRLLALMGELEGRISGSIHYDNVAPCFLGGMQLMIEENDIISQQVPGFDEWLWVLAYPGI
KVSTAEARAILPAQYRRQDCIAHGRHLAGFIHACYSRQPELAAKLMKDVIAEPYRERLLP
GFRQARQAVAEIGAVASGISGSGPTLFALCDKPETAQRVADWLGKNYLQNQEGFVHICRL
DTAGARVLEN
Enzyme 31 Number of Residues 310
Enzyme 31 Molecular Weight 33623.3
Enzyme 31 Theoretical pI 5.39
Enzyme 31 GO Classification
Function
  • ATP binding
  • adenyl nucleotide binding
  • adenyl ribonucleotide binding
  • binding
  • catalytic activity
  • homoserine kinase activity
  • kinase activity
  • nucleoside binding
  • phosphotransferase activity, alcohol group as acceptor
  • purine nucleoside binding
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • aspartate family amino acid metabolic process
  • cellular amino acid and derivative metabolic process
  • cellular amino acid metabolic process
  • cellular metabolic process
  • metabolic process
  • phosphate metabolic process
  • phosphorus metabolic process
  • phosphorylation
  • threonine metabolic process
Component
—
Enzyme 31 General Function Involved in ATP binding
Enzyme 31 Specific Function Catalyzes the ATP-dependent phosphorylation of L- homoserine to L-homoserine phosphate
Enzyme 31 Pathways Not Available
Enzyme 31 Reactions
  • ATP + L-homoserine = ADP + O-phospho-L-homoserine [RN:R01771]
Enzyme 31 Pfam Domain Function
Enzyme 31 Signals
  • None
Enzyme 31 Transmembrane Regions
  • None
Enzyme 31 Essentiality Not Available
Enzyme 31 GenBank ID Protein 169887501 Link Image
Enzyme 31 UniProtKB/Swiss-Prot ID B1XBC8 Link Image
Enzyme 31 UniProtKB/Swiss-Prot Entry Name KHSE_ECODH Link Image
Enzyme 31 PDB ID Not Available
Enzyme 31 Cellular Location Not Available
Enzyme 31 Gene Sequence >933 bp 
ATGGTTAAAGTTTATGCCCCGGCTTCCAGTGCCAATATGAGCGTCGGGTTTGATGTGCTC
GGGGCGGCGGTGACACCTGTTGATGGTGCATTGCTCGGAGATGTAGTCACGGTTGAGGCG
GCAGAGACATTCAGTCTCAACAACCTCGGACGCTTTGCCGATAAGCTGCCGTCAGAACCA
CGGGAAAATATCGTTTATCAGTGCTGGGAGCGTTTTTGCCAGGAACTGGGTAAGCAAATT
CCAGTGGCGATGACCCTGGAAAAGAATATGCCGATCGGTTCGGGCTTAGGCTCCAGTGCC
TGTTCGGTGGTCGCGGCGCTGATGGCGATGAATGAACACTGCGGCAAGCCGCTTAATGAC
ACTCGTTTGCTGGCTTTGATGGGCGAGCTGGAAGGCCGTATCTCCGGCAGCATTCATTAC
GACAACGTGGCACCGTGTTTTCTCGGTGGTATGCAGTTGATGATCGAAGAAAACGACATC
ATCAGCCAGCAAGTGCCAGGGTTTGATGAGTGGCTGTGGGTGCTGGCGTATCCGGGGATT
AAAGTCTCGACGGCAGAAGCCAGGGCTATTTTACCGGCGCAGTATCGCCGCCAGGATTGC
ATTGCGCACGGGCGACATCTGGCAGGCTTCATTCACGCCTGCTATTCCCGTCAGCCTGAG
CTTGCCGCGAAGCTGATGAAAGATGTTATCGCTGAACCCTACCGTGAACGGTTACTGCCA
GGCTTCCGGCAGGCGCGGCAGGCGGTCGCGGAAATCGGCGCGGTAGCGAGCGGTATCTCC
GGCTCCGGCCCGACCTTGTTCGCTCTGTGTGACAAGCCGGAAACCGCCCAGCGCGTTGCC
GACTGGTTGGGTAAGAACTACCTGCAAAATCAGGAAGGTTTTGTTCATATTTGCCGGCTG
GATACGGCGGGCGCACGAGTACTGGAAAACTAA
Enzyme 31 GenBank Gene ID CP000948 Link Image
Enzyme 31 GeneCard ID thrB Link Image
Enzyme 31 GenAtlas ID Not Available
Enzyme 31 HGNC ID Not Available
Enzyme 31 Chromosome Location 3
Enzyme 31 Locus 3p24.2
Enzyme 31 SNPs SNPJam Report Link Image
Enzyme 31 General References
  1. Durfee T, Nelson R, Baldwin S, Plunkett G 3rd, Burland V, Mau B, Petrosino JF, Qin X, Muzny DM, Ayele M, Gibbs RA, Csorgo B, Posfai G, Weinstock GM, Blattner FR: The complete genome sequence of Escherichia coli DH10B: insights into the biology of a laboratory workhorse. J Bacteriol. 2008 Apr;190(7):2597-606. Epub 2008 Feb 1. [PubMed Link Image]
Enzyme 31 Metabolite References Not Available