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Human Metabolome Database Version 2.5

 

Showing metabocard for Glycolaldehyde (HMDB03344)

Legend: metabolite field enzyme field

Version 2.5
Creation Date 2006-08-12 20:09:36
Update Date 2009-05-05 20:59:35
Accession Number HMDB03344
Secondary Accession Numbers HMDB02165
Common Name Glycolaldehyde
Description Glycolaldehyde (HOCH2-CH=O, IUPAC name 2-hydroxyethanal) is a type of diose (2-carbon monosaccharide). Glycolaldehyde is readily converted to acetyl coenzyme A. It has an aldehyde and a hydroxyl group. However, it is not actually a sugar, because there is only one hydroxyl group. Glycolaldehyde is formed from many sources, including the amino acid glycine and from purone catabolism. It can form by action of ketolase on fructose 1,6-bisphosphate in an alternate glycolysis pathway. This compound is transferred by thiamin pyrophosphate during the pentose phosphate shunt.
Synonyms
  1. 2-Hydroxyacetaldehyde
  2. 2-Hydroxyethanal
  3. 2-OH-acetaldehyde
  4. 2-Oxoethanol
  5. Diose
  6. Glycolaldehyde
  7. Glycolic aldehyde
  8. Glycollaldehyde
  9. Hydroxyacetaldehyde
  10. Hydroxyethanal
  11. Methylol formaldehyde
  12. Methylolformaldehyde
  13. Monomethylolformaldehyde
Chemical IUPAC Name 2-hydroxyacetaldehyde
Chemical Formula C2H4O2
Chemical Structure Structure
Chemical Taxonomy
Kingdom
  • Organic
Super Class
  • Alcohols
Class
  • Alcohols and Polyols
  • Aldehydes
Sub Class
  • Simple alcohols
Family
  • Microbial Metabolite
Species
  • aldehyde
  • primary alcohol
Biofunction
—
Application
—
Source
  • Endogenous
Average Molecular Weight 60.052
Monoisotopic Molecular Weight 60.021130
Isomeric SMILES OCC=O
Canonical SMILES OCC=O
KEGG Compound ID C00266 Link Image
BioCyc ID DIHYDROXYPHENYLGLYCOLALDEHYDE Link Image
BiGG ID 34446 Link Image
Wikipedia Link Glycolaldehyde Link Image
NuGOwiki Link HMDB03344 Link Image
Metagene Link HMDB03344 Link Image
METLIN ID 3205 Link Image
PubChem Compound 756 Link Image
PubChem Substance 3564 Link Image
ChEBI ID 17071 Link Image
CAS Registry Number 141-46-8
InChI Identifier InChI=1/C2H4O2/c3-1-2-4/h1,4H,2H2
Synthesis Reference Majerski, Piotr A.; Piskorz, Jan K.; Radlein, Desmond St. A. G. Production of glycolaldehyde by hydrous thermolysis of sugars. PCT Int. Appl. (2002), 41 pp.
Melting Point (Experimental) 97 oC
Experimental Water Solubility Not Available Source: PhysProp
Predicted Water Solubility 1000 mg/mL at 25 oC [MEYLAN,WM et al. (1996)]; 725.0 mg/mL [Predicted by ALOGPS] Calculated using ALOGPS
Physiological Charge 0
State Solid
Experimental LogP/Hydrophobicity Not Available Source: PhysProp
Predicted LogP/Hydrophobicity -0.99 [Predicted by ALOGPS]; -0.7 [Predicted by PubChem via XLOGP]; -1.63 [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 Not Available
Experimental 1H NMR Spectrum Not Available
Experimental 13C NMR Spectrum Not Available
Experimental 13C HSQC Spectrum Not Available
Predicted 1H NMR Spectrum Show Image
Show Peaklist
Predicted 13C NMR Spectrum Show Image
Show Peaklist
Mass Spectrum Not Available
Simplified TOCSY Spectrum Not Available
BMRB Spectrum Not Available
Cellular Location
  • Cytoplasm (Predicted from LogP)
  • mitochondria
Biofluid Location Not Available
Tissue Location
Tissue References
Neuron —
Concentrations (Normal) Not Available
Concentrations (Abnormal) Not Available
Associated Disorders Not Available
OMIM ID Not Available
Pathways
Name SMPDB Link KEGG Link
Vitamin B6 Metabolism SMP00017 Link Image map00750 Link Image
General References
  1. Takeuchi M, Yamagishi S: TAGE (toxic AGEs) hypothesis in various chronic diseases. Med Hypotheses. 2004;63(3):449-52. [PubMed Link Image]
  2. Choei H, Sasaki N, Takeuchi M, Yoshida T, Ukai W, Yamagishi S, Kikuchi S, Saito T: Glyceraldehyde-derived advanced glycation end products in Alzheimer's disease. Acta Neuropathol (Berl). 2004 Sep;108(3):189-93. Epub 2004 Jun 17. [PubMed Link Image]
  3. Wikipedia Link Image
Metabolic Enzymes
  1. Possible lactaldehyde reductase
  2. Putative lactaldehyde reductase
  3. Lactaldehyde reductase
  4. Lactaldehyde reductase
  5. Lactaldehyde reductase
  6. Lactaldehyde reductase
  7. Lactaldehyde dehydrogenase
  8. Rhamnulose-1-phosphate aldolase
  9. Rhamnulose-1-phosphate aldolase
  10. Rhamnulose-1-phosphate aldolase
  11. Dihydroneopterin aldolase
  12. SulD
  13. Putative dihydroneopterin aldolase
  14. Dihydroneopterin aldolase
  15. Dihydroneopterin aldolase
  16. Bifunctional folate synthesis protein
  17. Dihydroneopterin aldolase/2-amino-4-hydroxy-6-hydroxymethyldihydropteridine pyrophosphokinase
  18. Dihydroneopterin aldolase/2-amino-4-hydroxy-6-hydroxymethyldihydropteridine pyrophosphokinase
  19. Dihydroneopterin aldolase
  20. Dihydroneopterin aldolase
  21. 1,3-propanediol dehydrogenase
  22. L-1,2-propanediol oxidoreductase
  23. Aldehyde dehydrogenase A, NAD-linked
  24. Rhamnulose-1-phosphate aldolase
  25. Bifunctional dihydroneopterin aldolase and dihydroneopterin triphosphate 2'-epimerase
Enzyme 1 [top]
Enzyme 1 ID 16151
Enzyme 1 Name Possible lactaldehyde reductase
Enzyme 1 Synonyms Not Available
Enzyme 1 Gene Name fucO
Enzyme 1 Protein Sequence >Possible lactaldehyde reductase 
MVYRMIFNQTAYFGRGAIKEIPAVAKQHGFTKAFIVTDPVLLETGTAEKVTKVLDEAGLP
YEVFSNVKPNPPVECIKDGVAKFAESGADFLIGLGGGSPQDTCKGIGIITANPEFADVLS
LEGVADTKNPSVPIFGVPTTAGTASETTINYVVTDTANKRKFVAVDPHDIPIVAFVDPDL
TDSMPRGLKVATGLDALTHAIEGYITPGAWSLSDCLSMQTIRMIAKNLAKSADGDIPAGE
QMAYASYITGMAYSNVGLGLVHGMAHPLGGRLGVAHGVANGILLAPVMEYNKDFTGEKYR
DIADAFGVEDAYTGDLEKVREEAVQAVHKLTVDLKNPTTISEVGATEADLEPLAHDAFND
VCTPGNPRQATEEDILAIYKSLM
Enzyme 1 Number of Residues 383
Enzyme 1 Molecular Weight 40622.8
Enzyme 1 Theoretical pI 4.50
Enzyme 1 GO Classification
Function
  • binding
  • catalytic activity
  • cation binding
  • ion binding
  • metal ion binding
  • oxidoreductase activity
Process
  • metabolic process
  • oxidation reduction
Component
—
Enzyme 1 General Function Involved in oxidoreductase activity
Enzyme 1 Specific Function Not Available
Enzyme 1 Pathways Not Available
Enzyme 1 Reactions Not Available
Enzyme 1 Pfam Domain Function
Enzyme 1 Signals
  • None
Enzyme 1 Transmembrane Regions
  • None
Enzyme 1 Essentiality Not Available
Enzyme 1 GenBank ID Protein 23326965 Link Image
Enzyme 1 UniProtKB/Swiss-Prot ID Q8G3T1 Link Image
Enzyme 1 UniProtKB/Swiss-Prot Entry Name Q8G3T1_BIFLO Link Image
Enzyme 1 PDB ID Not Available
Enzyme 1 Cellular Location Not Available
Enzyme 1 Gene Sequence >1152 bp 
ATGGTGTACCGCATGATTTTCAACCAGACTGCATACTTCGGACGTGGCGCGATCAAGGAG
ATTCCGGCCGTCGCCAAGCAGCACGGCTTCACCAAGGCATTTATCGTCACCGACCCGGTG
CTGCTGGAGACCGGCACCGCCGAGAAGGTCACCAAGGTTCTGGATGAGGCCGGCCTGCCG
TACGAGGTGTTCTCCAACGTCAAGCCGAACCCGCCGGTCGAGTGCATCAAGGACGGCGTC
GCCAAGTTCGCCGAGTCCGGTGCGGACTTCCTGATCGGCCTGGGCGGTGGCTCCCCGCAA
GACACCTGCAAGGGCATCGGCATCATCACCGCCAACCCGGAGTTCGCCGACGTGCTTTCT
CTGGAAGGCGTCGCGGATACCAAGAACCCGTCCGTCCCGATCTTCGGCGTGCCGACCACC
GCCGGCACCGCCTCGGAGACGACCATCAACTACGTGGTCACCGACACGGCCAACAAGCGC
AAGTTCGTGGCTGTCGACCCGCACGACATCCCGATCGTCGCTTTCGTGGACCCGGATCTG
ACCGACTCGATGCCGCGCGGCCTGAAGGTCGCCACCGGACTTGACGCCCTGACCCACGCC
ATCGAGGGTTACATTACCCCGGGTGCCTGGAGCCTGTCCGACTGCCTGTCCATGCAGACC
ATCCGCATGATTGCCAAGAACCTGGCCAAGTCCGCCGACGGCGACATTCCGGCCGGCGAG
CAGATGGCCTACGCGTCCTACATCACCGGTATGGCCTACTCCAACGTGGGCCTCGGTCTG
GTGCACGGCATGGCTCACCCGCTGGGCGGCCGTCTGGGCGTGGCCCACGGTGTGGCCAAC
GGTATTCTGCTGGCCCCGGTCATGGAATACAACAAGGACTTCACCGGTGAGAAGTACCGC
GACATCGCCGATGCGTTCGGTGTTGAGGACGCCTACACCGGCGACCTGGAGAAGGTGCGC
GAAGAGGCCGTGCAGGCCGTCCACAAGCTGACCGTGGATCTGAAGAACCCGACCACGATT
TCCGAAGTGGGCGCCACCGAGGCCGACCTTGAGCCGCTGGCTCACGATGCCTTCAACGAC
GTGTGCACCCCCGGCAACCCGCGTCAGGCAACCGAAGAGGACATCCTCGCGATTTACAAG
TCGCTGATGTGA
Enzyme 1 GenBank Gene ID AE014295 Link Image
Enzyme 1 GeneCard ID fucO Link Image
Enzyme 1 GenAtlas ID Not Available
Enzyme 1 HGNC ID Not Available
Enzyme 1 Chromosome Location Not Available
Enzyme 1 Locus BL1673
Enzyme 1 SNPs SNPJam Report Link Image
Enzyme 1 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 1 Metabolite References Not Available
Enzyme 2 [top]
Enzyme 2 ID 16152
Enzyme 2 Name Putative lactaldehyde reductase
Enzyme 2 Synonyms Not Available
Enzyme 2 Gene Name fucO
Enzyme 2 Protein Sequence >Putative lactaldehyde reductase 
MINRFILNEVSYFGPGAREVLPKEISRLGLHKAFVATDKDLIKFGVADKVLKVLEAAKIP
YEIFSEIKPNPTVSNVKAGVEAFASSGADFILAIGGGSSMDTAKAIGIITNNPEFSDVVS
LEGVADTKKKSVPIIALPTTAGTAAEVTINYVITDEKNQKKMVCVDPNDIPSIAIVDAEL
MYTLPKSLTAATGLDALTHAIEGLITKGAWEMSDMFEIKAIEMINRYLVTAVEEPSNAEA
RNGMAVAQYIAGMAFSNVGLGVVHGMAHPLGAIFDIPHGVANALLLPIIMEFNAPAALDK
YVEIAKAMNVYSTDMTKEKAAEAAVEAVKTLSLRVNIPQHLSDLGIQESDLDRLATAAFA
DVCTPGNPREVTKEIILDLYKKAL
Enzyme 2 Number of Residues 384
Enzyme 2 Molecular Weight 41017.0
Enzyme 2 Theoretical pI 4.78
Enzyme 2 GO Classification
Function
  • binding
  • catalytic activity
  • cation binding
  • ion binding
  • metal ion binding
  • oxidoreductase activity
Process
  • metabolic process
  • oxidation reduction
Component
—
Enzyme 2 General Function Involved in oxidoreductase activity
Enzyme 2 Specific Function Not Available
Enzyme 2 Pathways Not Available
Enzyme 2 Reactions
  • (R)[or (S)]-propane-1,2-diol + NAD+ = (R)[or (S)]-lactaldehyde + NADH + H+ [RN:R02258 R03080]
Enzyme 2 Pfam Domain Function
Enzyme 2 Signals
  • None
Enzyme 2 Transmembrane Regions
  • None
Enzyme 2 Essentiality Not Available
Enzyme 2 GenBank ID Protein 60491241 Link Image
Enzyme 2 UniProtKB/Swiss-Prot ID Q5LIN7 Link Image
Enzyme 2 UniProtKB/Swiss-Prot Entry Name Q5LIN7_BACFN Link Image
Enzyme 2 PDB ID Not Available
Enzyme 2 Cellular Location Not Available
Enzyme 2 Gene Sequence >1155 bp 
ATGATTAATCGATTTATATTAAACGAAGTTTCTTACTTCGGTCCGGGAGCACGTGAAGTG
CTCCCCAAAGAGATTTCACGTTTGGGGCTGCACAAAGCATTTGTCGCAACAGACAAAGAT
TTGATAAAGTTTGGAGTAGCTGACAAAGTACTTAAGGTGCTGGAAGCTGCCAAGATTCCT
TATGAAATATTCAGTGAGATTAAGCCCAATCCTACAGTGTCGAATGTGAAAGCCGGTGTC
GAGGCATTTGCATCTTCCGGTGCAGACTTTATTTTGGCTATAGGTGGCGGATCTTCTATG
GATACGGCAAAGGCGATTGGTATTATTACCAATAACCCGGAATTCAGTGATGTCGTTTCA
TTGGAGGGAGTGGCAGATACCAAGAAGAAATCTGTTCCCATCATCGCGTTGCCTACTACT
GCAGGAACTGCGGCAGAGGTGACTATCAACTATGTGATAACGGATGAAAAGAACCAGAAG
AAGATGGTTTGTGTAGATCCTAATGATATTCCGTCTATTGCGATAGTGGATGCTGAGTTG
ATGTACACACTTCCTAAAAGTCTGACTGCAGCTACGGGACTCGACGCACTGACTCATGCT
ATTGAAGGTTTAATAACCAAAGGGGCATGGGAGATGAGTGATATGTTCGAAATTAAAGCT
ATTGAAATGATCAATCGTTATCTTGTGACTGCCGTTGAAGAACCATCGAATGCAGAGGCA
CGTAACGGTATGGCAGTGGCTCAATATATTGCAGGTATGGCTTTTTCGAATGTAGGTTTG
GGAGTTGTGCATGGTATGGCACATCCGTTGGGAGCTATTTTCGATATTCCTCATGGTGTG
GCCAATGCTCTATTATTGCCCATTATTATGGAGTTCAATGCTCCTGCAGCTCTTGACAAA
TATGTTGAGATAGCTAAAGCGATGAATGTGTATTCTACTGACATGACTAAAGAAAAGGCG
GCAGAAGCAGCAGTCGAAGCTGTAAAAACATTATCTTTGAGGGTCAATATTCCGCAACAC
TTGTCGGACTTGGGTATTCAGGAAAGTGATCTTGACCGTCTGGCCACAGCAGCGTTTGCT
GATGTATGTACGCCGGGCAATCCACGGGAAGTAACAAAAGAAATTATTCTTGATTTATAT
AAGAAAGCATTATGA
Enzyme 2 GenBank Gene ID CR626927 Link Image
Enzyme 2 GeneCard ID fucO Link Image
Enzyme 2 GenAtlas ID Not Available
Enzyme 2 HGNC ID Not Available
Enzyme 2 Chromosome Location Not Available
Enzyme 2 Locus BF0212
Enzyme 2 SNPs SNPJam Report Link Image
Enzyme 2 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 2 Metabolite References Not Available
Enzyme 3 [top]
Enzyme 3 ID 16153
Enzyme 3 Name Lactaldehyde reductase
Enzyme 3 Synonyms Not Available
Enzyme 3 Gene Name Not Available
Enzyme 3 Protein Sequence >Lactaldehyde reductase 
MINRFILNEVSYFGPGAREVLPKEISRLGLHKAFVATDKDLIKFGVADKVLKVLEAAKIP
YEIFSEIKPNPTVSNVKAGVEAFASSGADFILAIGGGSSMDTAKAIGIISNNPEFSDVVS
LEGVADTKKKSVPIIALPTTAGTAAEVTINYVITDEQNQKKMVCVDPNDIPSIAIVDAEL
MYTLPKSLTAATGLDALTHAIEGLITKGAWEMSDMFEIKAIEMINRYLVTAVEEPSNAEA
RNGMAVAQYIAGMAFSNVGLGVVHGMAHPLGAIFDIPHGVANALLLPIIMEFNAPAALDK
YVEIAKAMNVYSTDMTKEKAAEAAVEAVKTLSLRVNIPQHLSDLGIQESDLDRLATAAFA
DVCTPGNPREVTKEIILDLYKKAL
Enzyme 3 Number of Residues 384
Enzyme 3 Molecular Weight 41003.0
Enzyme 3 Theoretical pI 4.72
Enzyme 3 GO Classification
Function
  • binding
  • catalytic activity
  • cation binding
  • ion binding
  • metal ion binding
  • oxidoreductase activity
Process
  • metabolic process
  • oxidation reduction
Component
—
Enzyme 3 General Function Involved in oxidoreductase activity
Enzyme 3 Specific Function Not Available
Enzyme 3 Pathways Not Available
Enzyme 3 Reactions Not Available
Enzyme 3 Pfam Domain Function
Enzyme 3 Signals
  • None
Enzyme 3 Transmembrane Regions
  • None
Enzyme 3 Essentiality Not Available
Enzyme 3 GenBank ID Protein 52214410 Link Image
Enzyme 3 UniProtKB/Swiss-Prot ID Q64ZS3 Link Image
Enzyme 3 UniProtKB/Swiss-Prot Entry Name Q64ZS3_BACFR Link Image
Enzyme 3 PDB ID Not Available
Enzyme 3 Cellular Location Not Available
Enzyme 3 Gene Sequence >1155 bp 
ATGATTAATCGATTTATATTAAACGAAGTTTCTTACTTCGGTCCGGGAGCACGTGAAGTG
CTCCCCAAAGAGATTTCACGTTTGGGGCTGCACAAAGCATTTGTCGCAACAGACAAAGAT
TTGATAAAGTTTGGAGTAGCTGACAAAGTACTTAAGGTGCTGGAAGCTGCCAAGATTCCT
TATGAAATATTCAGTGAGATTAAGCCCAATCCTACAGTGTCGAATGTGAAAGCCGGTGTC
GAGGCATTTGCATCTTCCGGTGCAGACTTTATTTTGGCTATAGGTGGCGGATCTTCTATG
GATACGGCAAAGGCGATTGGTATTATTTCCAATAACCCGGAATTCAGTGATGTCGTTTCA
TTGGAGGGAGTGGCAGATACCAAGAAGAAATCTGTTCCCATCATCGCATTACCTACTACT
GCAGGAACTGCGGCAGAGGTGACTATCAACTATGTGATAACGGATGAACAGAACCAGAAG
AAGATGGTTTGTGTAGATCCTAATGATATTCCGTCTATTGCGATAGTGGATGCTGAGTTG
ATGTACACACTTCCTAAAAGTCTGACTGCAGCTACGGGACTCGACGCACTGACTCATGCT
ATTGAAGGTTTAATAACCAAAGGGGCATGGGAGATGAGTGATATGTTCGAAATTAAAGCT
ATTGAAATGATCAATCGTTATCTTGTGACTGCCGTTGAAGAACCATCGAATGCAGAGGCA
CGTAACGGTATGGCAGTGGCTCAATATATTGCAGGTATGGCTTTTTCGAATGTAGGTCTG
GGAGTTGTGCATGGTATGGCACATCCGTTGGGAGCTATTTTCGATATTCCTCATGGTGTG
GCCAATGCTCTATTATTGCCCATTATTATGGAGTTCAATGCTCCTGCAGCTCTTGACAAA
TATGTTGAGATAGCTAAAGCGATGAATGTGTATTCTACTGACATGACTAAAGAAAAGGCG
GCAGAAGCAGCAGTCGAAGCTGTAAAAACATTATCTTTGAGGGTCAATATTCCGCAACAC
TTGTCGGACTTGGGTATTCAGGAAAGTGATCTTGACCGTCTGGCCACAGCAGCGTTTGCT
GATGTATGTACGCCGGGCAATCCACGGGAAGTAACAAAAGAAATTATTCTTGATTTATAT
AAGAAAGCATTATGA
Enzyme 3 GenBank Gene ID AP006841 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 BF0254
Enzyme 3 SNPs Not Available
Enzyme 3 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 3 Metabolite References Not Available
Enzyme 4 [top]
Enzyme 4 ID 16154
Enzyme 4 Name Lactaldehyde reductase
Enzyme 4 Synonyms Not Available
Enzyme 4 Gene Name fucO
Enzyme 4 Protein Sequence >Lactaldehyde reductase 
MVNRIVLNETSYHGAGAIKEIVTEVKGRGFKKAFLCSDPDLVKFGVTGKVTSILDEANLS
YELYTNIKANPTIENVKSGVEAYKKSGADYIIAVGGGSSMDTAKAIGIIINNKEFEDVVS
LEGVAPTKNKSVPIIAVPTTAGTAAEVTINYVITDVEKNRKFVCVDTHDIPVVAIIDPEM
MQSMPKGLTAATGMDALTHAIEGYITGAAWEMTDMFHLKAIELISKHLRGAVENTPEGRE
GMALGQYIAGMGFSNVGLGIVHSMAHSLGAVYDTPHGVANAIILPTVMEYNAEETGDKYK
YIAAAMGVENTENMTVEEYRKAAVDAVKKLSEDVGIPANLKDIVKKEDIRFLAESAYNDA
CRPGNPKETSVEDIITLYESLM
Enzyme 4 Number of Residues 382
Enzyme 4 Molecular Weight 41077.7
Enzyme 4 Theoretical pI 4.77
Enzyme 4 GO Classification
Function
  • binding
  • catalytic activity
  • cation binding
  • ion binding
  • metal ion binding
  • oxidoreductase activity
Process
  • metabolic process
  • oxidation reduction
Component
—
Enzyme 4 General Function Involved in oxidoreductase activity
Enzyme 4 Specific Function Not Available
Enzyme 4 Pathways Not Available
Enzyme 4 Reactions
  • (R)[or (S)]-propane-1,2-diol + NAD+ = (R)[or (S)]-lactaldehyde + NADH + H+ [RN:R02258 R03080]
Enzyme 4 Pfam Domain Function
Enzyme 4 Signals
  • None
Enzyme 4 Transmembrane Regions
  • None
Enzyme 4 Essentiality Not Available
Enzyme 4 GenBank ID Protein 110674471 Link Image
Enzyme 4 UniProtKB/Swiss-Prot ID Q0TS98 Link Image
Enzyme 4 UniProtKB/Swiss-Prot Entry Name Q0TS98_CLOP1 Link Image
Enzyme 4 PDB ID Not Available
Enzyme 4 Cellular Location Not Available
Enzyme 4 Gene Sequence >1149 bp 
ATGAGTTATAAATTTTTTATGCCAGCAATAAGTTTAATGGGAGCAGATTGCTTAAAAGAC
GCTGGTGATCAAGTTGGAGAATTAGGATTTAAAAAAGCTTTAATAGTAACAGATAAAGTT
TTAGGTCAAATAGGAATAGTTAAAAAAGTAACAGATGTTTTAGATAATAAGAATATAGAA
TATGCAATATATGATGAAACTAAACCAAACCCAACAGTTAAAAATGTTAATGATGGTTTA
GCATTATTAAAAGAAAAAGAATGTGATTTTGTTATTTCATTAGGTGGAGGCTCAGCTCAT
GACTGTGCTAAAGGAATAGCTTTATTAGCTACTAATGGCGGAGAAATAAAAGATTATGAG
GGAGTAGATAAATCTAAAAAACCTCAATTACCAATGGTAGGTATAAATACAACTGCTGGT
ACTGGTAGTGAAATGACTTTATTCGCTATTATAACTGATGAAGAAAGACATATAAAAATG
GCTTTAGTAGATAAGCATTTAACACCAATAATAGCGGTTAATGATCCTATTTTAATGCTT
GCTATGCCAAAATCATTAACAGCGGCTACTGGTATGGATGCCTTAACACACGCTATAGAG
GCTTATGTTTCAACTGCTGCTACACCAATAACAGATGCTTGTGCAGAGAAAGCTATAGAA
CTTATAAGTAATTATTTAGTGAATGCTGTTGAAAATGGACAAGATGTGGAAGCTAGAGAT
ATGATGGCTTATGCTGAATACTTAGCAGGAATGGCATTTAACAATGCTAGTTTAGGATAT
GTTCACGCTATGGCTCACCAATTAGGTGGATTCTACAACTTACCTCATGGGGTATGTAAT
GCAATATTATTACCTCATGTTCAAGAATATAACAAATCTACAAGTGCTTCAAGATTAGCT
AAAATTGCTAAAATAATGGGTGGAAACATAGAAGGATTAACTGATGAGCAAGGAGCAGAT
CTTTGCATAGATATGATAAAATCATTATCACAAACTATAGGAATTCCAGAGGGACTTGGA
GTATTAGGAGTAAAAGAAAGTGATTTTGAAACTTTAGCTACTAATGCTTTAAATGATGCT
TGTTCATTAACAAATCCAAGAAAAGGAAACTTAGAAGAAGTAATAGCTATATTCAAAAAA
GCAATGTAG
Enzyme 4 GenBank Gene ID CP000246 Link Image
Enzyme 4 GeneCard ID fucO Link Image
Enzyme 4 GenAtlas ID Not Available
Enzyme 4 HGNC ID Not Available
Enzyme 4 Chromosome Location Not Available
Enzyme 4 Locus CPF_1046
Enzyme 4 SNPs SNPJam Report Link Image
Enzyme 4 General References
  1. Myers GS, Rasko DA, Cheung JK, Ravel J, Seshadri R, DeBoy RT, Ren Q, Varga J, Awad MM, Brinkac LM, Daugherty SC, Haft DH, Dodson RJ, Madupu R, Nelson WC, Rosovitz MJ, Sullivan SA, Khouri H, Dimitrov GI, Watkins KL, Mulligan S, Benton J, Radune D, Fisher DJ, Atkins HS, Hiscox T, Jost BH, Billington SJ, Songer JG, McClane BA, Titball RW, Rood JI, Melville SB, Paulsen IT: Skewed genomic variability in strains of the toxigenic bacterial pathogen, Clostridium perfringens. Genome Res. 2006 Aug;16(8):1031-40. Epub 2006 Jul 6. [PubMed Link Image]
Enzyme 4 Metabolite References Not Available
Enzyme 5 [top]
Enzyme 5 ID 16155
Enzyme 5 Name Lactaldehyde reductase
Enzyme 5 Synonyms Not Available
Enzyme 5 Gene Name fucO
Enzyme 5 Protein Sequence >Lactaldehyde reductase 
MVNRIVLNETSYHGAGAIKEIVTEVKGRGFKKAFLCSDPDLVKFGVTGKVTSILDEANLS
YELYTNIKANPTIENVKSGVEAYKKSGADYIIAVGGGSSMDTAKAIGIIINNKEFEDVVS
LEGVAPTKNKSVPIIAIPTTAGTAAEVTINYVITDVEKNRKFVCVDTHDIPVVAIIDPEM
MQSMPKGLTAATGMDALTHAIEGYITGAAWEMTDMFHLKAIELISKHLRGAVENTPEGRE
KMALGQYIAGMGFSNVGLGIVHSMAHSLGAVYDTPHGVANAIILPTVMEYNAEETGDKYK
YIAAAMGVENTENMTVEEYRKAAVDAVKKLSEDVGIPANLKDIVKKEDIRFLAESAYNDA
CRPGNPKETSVEDIIALYESLM
Enzyme 5 Number of Residues 382
Enzyme 5 Molecular Weight 41132.8
Enzyme 5 Theoretical pI 4.83
Enzyme 5 GO Classification
Function
  • binding
  • catalytic activity
  • cation binding
  • ion binding
  • metal ion binding
  • oxidoreductase activity
Process
  • metabolic process
  • oxidation reduction
Component
—
Enzyme 5 General Function Involved in oxidoreductase activity
Enzyme 5 Specific Function Not Available
Enzyme 5 Pathways Not Available
Enzyme 5 Reactions
  • (R)[or (S)]-propane-1,2-diol + NAD+ = (R)[or (S)]-lactaldehyde + NADH + H+ [RN:R02258 R03080]
Enzyme 5 Pfam Domain Function
Enzyme 5 Signals
  • None
Enzyme 5 Transmembrane Regions
  • None
Enzyme 5 Essentiality Not Available
Enzyme 5 GenBank ID Protein 110684255 Link Image
Enzyme 5 UniProtKB/Swiss-Prot ID Q0SUF6 Link Image
Enzyme 5 UniProtKB/Swiss-Prot Entry Name Q0SUF6_CLOPS Link Image
Enzyme 5 PDB ID Not Available
Enzyme 5 Cellular Location Not Available
Enzyme 5 Gene Sequence >1149 bp 
ATGAGTTATAAATTTTTTATGCCAGCAATAAGTTTAATGGGAGCAGATTGCTTAAAAGAC
GCTGGTGATCAACTTGGAGAATTAGGATTTAAAAAAGCTTTAATAGTAACAGATAAAGTT
TTAGGTCAAATAGGAATAGTTAAAAAAGTAACAGATGTTTTAGATAATAAGAATATAGAA
TATGCAATATATGATGAAACTAAACCAAACCCAACAGTTAAAAATGTTAATGATGGTTTA
GCATTATTAAAAGAAAAAGAATGTGATTTTGTTATTTCATTAGGTGGAGGCTCAGCTCAT
GACTGTGCTAAAGGAATAGCTTTATTAGCTACTAATGGCGGAGAAATAAAAGATTATGAG
GGAGTAGATAAATCTAAAAAACCTCAATTACCAATGGTAGGTATAAATACAACTGCTGGT
ACTGGTAGTGAAATGACTTTATTCGCTATTATAACTGATGAAGAAAGACATATAAAAATG
GCTTTAGTAGATAAGCATTTAACACCAATAATAGCGGTTAATGATCCTATGTTAATGCTT
GCTATGCCAAAATCATTAACAGCGGCTACTGGTATGGATGCCTTAACACACGCTATAGAG
GCTTATGTTTCAACTGCTGCTACACCAATAACAGATGCTTGTGCAGAGAAAGCTATAGAA
CTTATAAGCAATTATTTAGTGAATGCTGTTGAAAATGGACAAGATGTGGAAGCTAGAGAT
ATGATGGCTTATGCTGAATACTTAGCAGGAATGGCATTTAACAATGCTAGTTTAGGATAT
GTTCACGCTATGGCTCACCAATTAGGTGGATTCTATAACTTACCTCATGGAGTATGTAAT
GCAATATTATTACCTCATGTTCAAGAATATAACAAATCTACAAGTGCTTCAAGATTAGCT
AAAATTGCTAAAATAATGGGTGGAAACATAGAAGGATTAACTGATGAGCAAGGAGCAGAT
CTTTGCATAGATATGATAAAATCATTATCACAAACTATAGGAATTCCAGAGGGACTTGGA
GTATTAGGAGTAAAAGAAAGTGATTTTGAAACTTTAGCTACTAATGCTTTAAATGATGCT
TGTTCATTAACAAATCCAAGAAAAGGAAACTTAGAAGAAGTAATAGCTATATTTAAAAAA
GCAATGTAG
Enzyme 5 GenBank Gene ID CP000312 Link Image
Enzyme 5 GeneCard ID fucO Link Image
Enzyme 5 GenAtlas ID Not Available
Enzyme 5 HGNC ID Not Available
Enzyme 5 Chromosome Location Not Available
Enzyme 5 Locus CPR_0927
Enzyme 5 SNPs SNPJam Report Link Image
Enzyme 5 General References
  1. Myers GS, Rasko DA, Cheung JK, Ravel J, Seshadri R, DeBoy RT, Ren Q, Varga J, Awad MM, Brinkac LM, Daugherty SC, Haft DH, Dodson RJ, Madupu R, Nelson WC, Rosovitz MJ, Sullivan SA, Khouri H, Dimitrov GI, Watkins KL, Mulligan S, Benton J, Radune D, Fisher DJ, Atkins HS, Hiscox T, Jost BH, Billington SJ, Songer JG, McClane BA, Titball RW, Rood JI, Melville SB, Paulsen IT: Skewed genomic variability in strains of the toxigenic bacterial pathogen, Clostridium perfringens. Genome Res. 2006 Aug;16(8):1031-40. Epub 2006 Jul 6. [PubMed Link Image]
Enzyme 5 Metabolite References Not Available
Enzyme 6 [top]
Enzyme 6 ID 16156
Enzyme 6 Name Lactaldehyde reductase
Enzyme 6 Synonyms
  1. Propanediol oxidoreductase
Enzyme 6 Gene Name fucO
Enzyme 6 Protein Sequence >Lactaldehyde reductase 
MMANRMILNETAWFGRGAVGALTDEVKRRGYQKALIVTDKTLVQCGVVAKVTDKMDAAGL
AWAIYDGVVPNPTITVVKEGLGVFQNSGADYLIAIGGGSPQDTCKAIGIISNNPEFADVR
SLEGLSPTNKPSVPILAIPTTAGTAAEVTINYVITDEEKRRKFVCVDPHDIPQVAFIDAD
MMDGMPPALKAATGVDALTHAIEGYITRGAWALTDALHIKAIEIIAGALRGSVAGDKDAG
EEMALGQYVAGMGFSNVGLGLVHGMAHPLGAFYNTPHGVANAILLPHVMRYNADFTGEKY
RDIARVMGVKVEGMSLEEARNAAVEAVFALNRDVGIPPHLRDVGVRKEDIPALAQAALDD
VCTGGNPREATLEDIVELYHTAW
Enzyme 6 Number of Residues 383
Enzyme 6 Molecular Weight 40644.2
Enzyme 6 Theoretical pI 4.91
Enzyme 6 GO Classification
Function
  • binding
  • catalytic activity
  • cation binding
  • ion binding
  • metal ion binding
  • oxidoreductase activity
Process
  • metabolic process
  • oxidation reduction
Component
—
Enzyme 6 General Function Involved in oxidoreductase activity
Enzyme 6 Specific Function (R)-propane-1,2-diol + NAD(+) = (R)- lactaldehyde + NADH
Enzyme 6 Pathways Not Available
Enzyme 6 Reactions
  • (R)[or (S)]-propane-1,2-diol + NAD+ = (R)[or (S)]-lactaldehyde + NADH + H+ [RN:R02258 R03080]
Enzyme 6 Pfam Domain Function
Enzyme 6 Signals
  • None
Enzyme 6 Transmembrane Regions
  • None
Enzyme 6 Essentiality Not Available
Enzyme 6 GenBank ID Protein 146043 Link Image
Enzyme 6 UniProtKB/Swiss-Prot ID P0A9S1 Link Image
Enzyme 6 UniProtKB/Swiss-Prot Entry Name FUCO_ECOLI Link Image
Enzyme 6 PDB ID 1RRM Link Image
Enzyme 6 PDB File Show
Enzyme 6 3D Structure
Enzyme 6 Cellular Location Not Available
Enzyme 6 Gene Sequence >1152 bp 
ATGATGGCTAACAGAATGATTCTGAACGAAACGGCATGGTTTGGTCGGGGTGCTGTTGGG
GCTTTAACCGATGAGGTGAAACGCCGTGGTTATCAGAAGGCGCTGATCGTCACCGATAAA
ACGCTGGTGCAATGCGGCGTGGTGGCGAAAGTGACCGATAAGATGGATGCTGCAGGGCTG
GCATGGGCGATTTACGACGGCGTAGTGCCCAACCCAACAATTACTGTCGTCAAAGAAGGG
CTCGGTGTATTCCAGAATAGCGGCGCGGATTACCTGATCGCTATTGGTGGTGGTTCTCCA
CAGGATACTTGTAAAGCGATTGGCATTATCAGCAACAACCCGGAGTTTGCCGATGTGCGT
AGCCTGGAAGGGCTTTCCCCGACCAATAAACCCAGTGTACCGATTCTGGCAATTCCTACC
ACAGCAGGTACTGCGGCAGAAGTGACCATTAACTACGTGATCACTGACGAAGAGAAACGG
CGCAAGTTTGTTTGCGTTGATCCGCATGATATCCCGCAGGTGGCGTTTATTGACGCTGAC
ATGATGGATGGTATGCCTCCAGCGCTGAAAGCTGCGACGGGTGTCGATGCGCTCACTCAT
GCTATTGAGGGGTATATTACCCGTGGCGCGTGGGCGCTAACCGATGCACTGCACATTAAA
GCGATTGAAATCATTGCTGGGGCGCTGCGAGGATCGGTTGCTGGTGATAAGGATGCCGGA
GAAGAAATGGCGCTCGGGCAGTATGTTGCGGGTATGGGCTTCTCGAATGTTGGGTTAGGG
TTGGTGCATGGTATGGCGCATCCACTGGGCGCGTTTTATAACACTCCACACGGTGTTGCG
AACGCCATCCTGTTACCGCATGTCATGCGTTATAACGCTGACTTTACCGGTGAGAAGTAC
CGCGATATCGCGCGCGTTATGGGCGTGAAAGTGGAAGGTATGAGCCTGGAAGAGGCGCGT
AATGCCGCTGTTGAAGCGGTGTTTGCTCTCAACCGTGATGTCGGTATTCCGCCACATTTG
CGTGATGTTGGTGTACGCAAGGAAGACATTCCGGCACTGGCGCAGGCGGCACTGGATGAT
GTTTGTACCGGTGGCAACCCGCGTGAAGCAACGCTTGAGGATATTGTAGAGCTTTACCAT
ACCGCCTGGTAA
Enzyme 6 GenBank Gene ID M31059 Link Image
Enzyme 6 GeneCard ID fucO Link Image
Enzyme 6 GenAtlas ID Not Available
Enzyme 6 HGNC ID Not Available
Enzyme 6 Chromosome Location Not Available
Enzyme 6 Locus Not Available
Enzyme 6 SNPs SNPJam Report Link Image
Enzyme 6 General References
  1. Chen YM, Lu Z, Lin EC: Constitutive activation of the fucAO operon and silencing of the divergently transcribed fucPIK operon by an IS5 element in Escherichia coli mutants selected for growth on L-1,2-propanediol. J Bacteriol. 1989 Nov;171(11):6097-105. [PubMed Link Image]
  2. Lu Z, Lin EC: The nucleotide sequence of Escherichia coli genes for L-fucose dissimilation. Nucleic Acids Res. 1989 Jun 26;17(12):4883-4. [PubMed Link Image]
  3. Conway T, Ingram LO: Similarity of Escherichia coli propanediol oxidoreductase (fucO product) and an unusual alcohol dehydrogenase from Zymomonas mobilis and Saccharomyces cerevisiae. J Bacteriol. 1989 Jul;171(7):3754-9. [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. Shao Z, Newman EB: Sequencing and characterization of the sdaB gene from Escherichia coli K-12. Eur J Biochem. 1993 Mar 15;212(3):777-84. [PubMed Link Image]
Enzyme 6 Metabolite References Not Available
Enzyme 7 [top]
Enzyme 7 ID 16157
Enzyme 7 Name Lactaldehyde dehydrogenase
Enzyme 7 Synonyms
  1. Aldehyde dehydrogenase A
  2. Glycolaldehyde dehydrogenase
Enzyme 7 Gene Name aldA
Enzyme 7 Protein Sequence >Lactaldehyde dehydrogenase 
MSVPVQHPMYIDGQFVTWRGDAWIDVVNPATEAVISRIPDGQAEDARKAIDAAERAQPEW
EALPAIERASWLRKISAGIRERASEISALIVEEGGKIQQLAEVEVAFTADYIDYMAEWAR
RYEGEIIQSDRPGENILLFKRALGVTTGILPWNFPFFLIARKMAPALLTGNTIVIKPSEF
TPNNAIAFAKIVDEIGLPRGVFNLVLGRGETVGQELAGNPKVAMVSMTGSVSAGEKIMAT
AAKNITKVCLELGGKAPAIVMDDADLELAVKAIVDSRVINSGQVCNCAERVYVQKGIYDQ
FVNRLGEAMQAVQFGNPAERNDIAMGPLINAAALERVEQKVARAVEEGARVAFGGKAVEG
KGYYYPPTLLLDVRQEMSIMHEETFGPVLPVVAFDTLEDAISMANDSDYGLTSSIYTQNL
NVAMKAIKGLKFGETYINRENFEAMQGFHAGWRKSGIGGADGKHGLHEYLQTQVVYLQS
Enzyme 7 Number of Residues 479
Enzyme 7 Molecular Weight 52272.4
Enzyme 7 Theoretical pI 4.79
Enzyme 7 GO Classification
Function
  • catalytic activity
  • oxidoreductase activity
Process
  • metabolic process
  • oxidation reduction
Component
—
Enzyme 7 General Function Involved in oxidoreductase activity
Enzyme 7 Specific Function Acts on lactaldehyde as well as other aldehydes
Enzyme 7 Pathways Not Available
Enzyme 7 Reactions
  • (S)-lactaldehyde + NAD+ + H2O = (S)-lactate + NADH + 2 H+ [RN:R01446]
Enzyme 7 Pfam Domain Function
Enzyme 7 Signals
  • None
Enzyme 7 Transmembrane Regions
  • None
Enzyme 7 Essentiality Not Available
Enzyme 7 GenBank ID Protein Not Available
Enzyme 7 UniProtKB/Swiss-Prot ID P25553 Link Image
Enzyme 7 UniProtKB/Swiss-Prot Entry Name ALDA_ECOLI Link Image
Enzyme 7 PDB ID Not Available
Enzyme 7 Cellular Location Not Available
Enzyme 7 Gene Sequence >1440 bp 
ATGTCAGTACCCGTTCAACATCCTATGTATATCGATGGACAGTTTGTTACCTGGCGTGGA
GACGCATGGATTGATGTGGTAAACCCTGCTACAGAGGCTGTCATTTCCCGCATACCCGAT
GGTCAGGCCGAGGATGCCCGTAAGGCAATCGATGCAGCAGAACGTGCACAACCAGAATGG
GAAGCGTTGCCTGCTATTGAACGCGCCAGTTGGTTGCGCAAAATCTCCGCCGGGATCCGC
GAACGCGCCAGTGAAATCAGTGCGCTGATTGTTGAAGAAGGGGGCAAGATCCAGCAGCTG
GCTGAAGTCGAAGTGGCTTTTACTGCCGACTATATCGATTACATGGCGGAGTGGGCACGG
CGTTACGAGGGCGAGATTATTCAAAGCGATCGTCCAGGAGAAAATATTCTTTTGTTTAAA
CGTGCGCTTGGTGTGACTACCGGCATTCTGCCGTGGAACTTCCCGTTCTTCCTCATTGCC
CGCAAAATGGCTCCCGCTCTTTTGACCGGTAATACCATCGTCATTAAACCTAGTGAATTT
ACGCCAAACAATGCGATTGCATTCGCCAAAATCGTCGATGAAATAGGCCTTCCGCGCGGC
GTGTTTAACCTTGTACTGGGGCGTGGTGAAACCGTTGGGCAAGAACTGGCGGGTAACCCA
AAGGTCGCAATGGTCAGTATGACAGGCAGCGTCTCTGCAGGTGAGAAGATCATGGCGACT
GCGGCGAAAAACATCACCAAAGTGTGTCTGGAATTGGGGGGTAAAGCACCAGCTATCGTA
ATGGACGATGCCGATCTTGAACTGGCAGTCAAAGCCATCGTTGATTCACGCGTCATTAAT
AGTGGGCAAGTGTGTAACTGTGCAGAACGTGTTTATGTACAGAAAGGCATTTATGATCAG
TTCGTCAATCGGCTGGGTGAAGCGATGCAGGCGGTTCAATTTGGTAACCCCGCTGAACGC
AACGACATTGCGATGGGGCCGTTGATTAACGCCGCGGCGCTGGAAAGGGTCGAGCAAAAA
GTGGCGCGCGCAGTAGAAGAAGGGGCGAGAGTGGCGTTCGGTGGCAAAGCGGTAGAGGGG
AAAGGATATTATTATCCGCCGACATTGCTGCTGGATGTTCGCCAGGAAATGTCGATTATG
CATGAGGAAACCTTTGGCCCGGTGCTGCCAGTTGTCGCATTTGACACGCTGGAAGATGCT
ATCTCAATGGCTAATGACAGTGATTACGGCCTGACCTCATCAATCTATACCCAAAATCTG
AACGTCGCGATGAAAGCCATTAAAGGGCTGAAGTTTGGTGAAACTTACATCAACCGTGAA
AACTTCGAAGCTATGCAAGGCTTCCACGCCGGATGGCGTAAATCCGGTATTGGCGGCGCA
GATGGTAAACATGGCTTGCATGAATATCTGCAGACCCAGGTGGTTTATTTACAGTCTTAA
Enzyme 7 GenBank Gene ID M64541 Link Image
Enzyme 7 GeneCard ID aldA Link Image
Enzyme 7 GenAtlas ID Not Available
Enzyme 7 HGNC ID Not Available
Enzyme 7 Chromosome Location Not Available
Enzyme 7 Locus Not Available
Enzyme 7 SNPs SNPJam Report Link Image
Enzyme 7 General References
  1. Hidalgo E, Chen YM, Lin EC, Aguilar J: Molecular cloning and DNA sequencing of the Escherichia coli K-12 ald gene encoding aldehyde dehydrogenase. J Bacteriol. 1991 Oct;173(19):6118-23. [PubMed Link Image]
  2. Aiba H, Baba T, Hayashi K, Inada T, Isono K, Itoh T, Kasai H, Kashimoto K, Kimura S, Kitakawa M, Kitagawa M, Makino K, Miki T, Mizobuchi K, Mori H, Mori T, Motomura K, Nakade S, Nakamura Y, Nashimoto H, Nishio Y, Oshima T, Saito N, Sampei G, Horiuchi T, et al.: A 570-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 28.0-40.1 min region on the linkage map. DNA Res. 1996 Dec 31;3(6):363-77. [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]
  5. Link AJ, Robison K, Church GM: Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12. Electrophoresis. 1997 Aug;18(8):1259-313. [PubMed Link Image]
  6. Caballero E, Baldoma L, Ros J, Boronat A, Aguilar J: Identification of lactaldehyde dehydrogenase and glycolaldehyde dehydrogenase as functions of the same protein in Escherichia coli. J Biol Chem. 1983 Jun 25;258(12):7788-92. [PubMed Link Image]
  7. Baldoma L, Aguilar J: Involvement of lactaldehyde dehydrogenase in several metabolic pathways of Escherichia coli K12. J Biol Chem. 1987 Oct 15;262(29):13991-6. [PubMed Link Image]
Enzyme 7 Metabolite References Not Available
Enzyme 8 [top]
Enzyme 8 ID 16162
Enzyme 8 Name Rhamnulose-1-phosphate aldolase
Enzyme 8 Synonyms Not Available
Enzyme 8 Gene Name rhaD
Enzyme 8 Protein Sequence >Rhamnulose-1-phosphate aldolase 
MTDFIDSPYVRDMAQTTENLYRHGWDERNGGNVSLRLTKEEVEAYAGTDKVLRQIPIKFD
ASELAGKYYLVTGTGRYFKNMVEFPERDMGLIRISEVGNSVDLMWGFNDGGEPTSEFPSH
LMSHIARLKQDPDQRVIMHCHPTNLVAMTFTIPLSSKRFSRTLWKMHPESIVVFPEGVGV
IPYMCPGTNEIGEKTAAKMADYRVVVWPHHGVFAAGDSLDETYGLVETVEKSALIYTTIR
EQGGEVLQSLTDKDFRDLIKRFDLKANEDFLTPDAVGATVD
Enzyme 8 Number of Residues 281
Enzyme 8 Molecular Weight 31693.7
Enzyme 8 Theoretical pI 4.97
Enzyme 8 GO Classification
Function
  • aldehyde-lyase activity
  • binding
  • carbon-carbon lyase activity
  • catalytic activity
  • cation binding
  • ion binding
  • lyase activity
  • metal ion binding
  • rhamnulose-1-phosphate aldolase activity
Process
—
Component
—
Enzyme 8 General Function Involved in metal ion binding
Enzyme 8 Specific Function Catalyzes the reversible cleavage of L-rhamnulose-1- phosphate to dihydroxyacetone phosphate (DHAP) and L-lactaldehyde
Enzyme 8 Pathways Not Available
Enzyme 8 Reactions
  • L-rhamnulose 1-phosphate = glycerone phosphate + (S)-lactaldehyde [RN:R02263]
Enzyme 8 Pfam Domain Function
Enzyme 8 Signals
  • None
Enzyme 8 Transmembrane Regions
  • None
Enzyme 8 Essentiality Not Available
Enzyme 8 GenBank ID Protein 28272740 Link Image
Enzyme 8 UniProtKB/Swiss-Prot ID Q88S52 Link Image
Enzyme 8 UniProtKB/Swiss-Prot Entry Name RHAD_LACPL Link Image
Enzyme 8 PDB ID Not Available
Enzyme 8 Cellular Location Not Available
Enzyme 8 Gene Sequence >846 bp 
ATGACAGACTTTATTGATTCACCATATGTACGTGATATGGCACAAACAACGGAAAATTTA
TATCGACATGGCTGGGACGAACGGAATGGCGGCAACGTGAGTCTACGACTGACTAAAGAG
GAAGTTGAAGCCTATGCTGGTACGGATAAAGTTTTACGTCAGATTCCAATTAAATTTGAT
GCCAGTGAATTAGCGGGCAAGTATTACTTAGTTACGGGAACTGGCCGGTACTTTAAGAAT
ATGGTCGAATTTCCAGAACGTGACATGGGCTTGATTCGAATCAGCGAAGTCGGCAACAGT
GTTGATTTAATGTGGGGCTTCAATGATGGTGGTGAACCAACTAGCGAATTTCCATCACAC
TTAATGAGCCACATTGCTCGGTTGAAGCAAGATCCTGATCAACGGGTTATCATGCATTGC
CACCCAACTAACTTGGTTGCAATGACCTTTACGATTCCGTTGTCATCTAAGCGGTTCAGT
CGGACGCTATGGAAGATGCATCCAGAATCAATCGTTGTCTTCCCAGAAGGCGTAGGCGTT
ATCCCATATATGTGCCCAGGAACTAATGAAATCGGTGAAAAGACGGCTGCTAAGATGGCC
GACTACCGGGTAGTTGTATGGCCACACCATGGCGTCTTCGCAGCTGGTGACTCTCTGGAT
GAAACTTACGGGTTAGTTGAAACAGTTGAAAAGTCAGCATTAATCTACACGACGATTCGT
GAACAAGGTGGAGAAGTCTTGCAATCGTTGACCGACAAAGATTTCCGTGACTTAATCAAG
CGTTTTGACTTGAAAGCCAATGAAGACTTCTTAACACCAGATGCAGTCGGAGCAACGGTT
GACTAA
Enzyme 8 GenBank Gene ID AL935262 Link Image
Enzyme 8 GeneCard ID rhaD Link Image
Enzyme 8 GenAtlas ID Not Available
Enzyme 8 HGNC ID Not Available
Enzyme 8 Chromosome Location Not Available
Enzyme 8 Locus lp_3592
Enzyme 8 SNPs SNPJam Report Link Image
Enzyme 8 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 8 Metabolite References Not Available
Enzyme 9 [top]
Enzyme 9 ID 16163
Enzyme 9 Name Rhamnulose-1-phosphate aldolase
Enzyme 9 Synonyms Not Available
Enzyme 9 Gene Name rhaD
Enzyme 9 Protein Sequence >Rhamnulose-1-phosphate aldolase 
MNVLQAPFVEEMVKTTKNLYRLGWDERNGGNISYLLKEEEILPFLNPTQVLRKIPMKFDA
TKLAGKYFIVTGSGKYFKNVCDASSENLGILRVSENGQELELLWGLEDEAVPTSELPSHF
MSHIARLAVDPENRIVMHNHASHLLAMSFTHELDEKVFTRTLWQMCTECLVVFPDGVGII
PWLVPGTNEIGVATAEKMKESRLVLWPQHGIYGTGRDMDEVFGLIETAEKAAEVYTYVCA
QGGVRQTISDADLWRLAEAFGVTPKVGYLEEKVSKRRKL
Enzyme 9 Number of Residues 279
Enzyme 9 Molecular Weight 31465.0
Enzyme 9 Theoretical pI 5.43
Enzyme 9 GO Classification
Function
  • aldehyde-lyase activity
  • binding
  • carbon-carbon lyase activity
  • catalytic activity
  • cation binding
  • ion binding
  • lyase activity
  • metal ion binding
  • rhamnulose-1-phosphate aldolase activity
Process
—
Component
—
Enzyme 9 General Function Involved in metal ion binding
Enzyme 9 Specific Function Catalyzes the reversible cleavage of L-rhamnulose-1- phosphate to dihydroxyacetone phosphate (DHAP) and L-lactaldehyde
Enzyme 9 Pathways Not Available
Enzyme 9 Reactions
  • L-rhamnulose 1-phosphate = glycerone phosphate + (S)-lactaldehyde [RN:R02263]
Enzyme 9 Pfam Domain Function
Enzyme 9 Signals
  • None
Enzyme 9 Transmembrane Regions
  • None
Enzyme 9 Essentiality Not Available
Enzyme 9 GenBank ID Protein 29342173 Link Image
Enzyme 9 UniProtKB/Swiss-Prot ID Q838L1 Link Image
Enzyme 9 UniProtKB/Swiss-Prot Entry Name RHAD_ENTFA Link Image
Enzyme 9 PDB ID Not Available
Enzyme 9 Cellular Location Not Available
Enzyme 9 Gene Sequence >840 bp 
ATGGCAGAAATGCTTTCTTATGCATTTATGCAAAAGGCCTTTTTAGCAGCACTGTTTATC
TCAGTGATTGCCCCAATGCTCGGCGTCTTTCTAGTTATTCGCCGACAATCTTTAATGGCA
GATACCCTTTCACATGTGTCATTAGCCGGTGTGGCACTAGGCTTCTTTTTTAATTGGAAT
CCTAATTTAATGACCTTAATTGTCGTGATTGTGGCTGCAATCATTCTAGAATATTTACGA
ATGATTTATAGCACCTATTCAGAAATTTCGATTGCTATTTTAATGTCAGGCGGTTTGGCT
TTGGCGTTAGTTTTGATGAATTTAACAGGAGGCAATTCAGCTGCTAGTATTCAATCGTAT
TTATTTGGTTCCATCGTCACGATTACGTGGGATCAAGTGGTTATGTTGGCAATTTTATTC
GTAGTTTTAGTTCTATTGTTTATGTTATTTAAACGTCCAATGTATGTTTTAACATTTGAT
GAAGATACTGCTCATGTTGATGGGCTACCTATTCATTGGATGTCGATGCTTTTTAATGTA
ATTACTGGTGTGGCGATTGCTGTGATGATTCCGATCGCGGGAGCCTTGTTAATTTCAGCA
ATTATGGTCTTACCAGCTGCAATAGGTATGCGAATTGGTAAAGGCTTTAACACGGTGATT
ATTATCAGTGTGTTTATGGGCTTGATTGGCATGCTAACAGGGTTGACTAGCTCGTATTAT
TTGGAAACACCACCGAGTGCAAGTATTACCCTAATTTTTATTGGTTTATTCTTATTAGTC
AATATTTATCGCCGAGTGGTTGTCATGGTCCAACGAAAACAAAAAATGCAAAGAAACTAA
Enzyme 9 GenBank Gene ID AE016830 Link Image
Enzyme 9 GeneCard ID rhaD Link Image
Enzyme 9 GenAtlas ID Not Available
Enzyme 9 HGNC ID Not Available
Enzyme 9 Chromosome Location Not Available
Enzyme 9 Locus EF_0435
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 16164
Enzyme 10 Name Rhamnulose-1-phosphate aldolase
Enzyme 10 Synonyms Not Available
Enzyme 10 Gene Name rhaD
Enzyme 10 Protein Sequence >Rhamnulose-1-phosphate aldolase 
MQNITQSWFVQGMIKATTDAWLKGWDERNGGNLTLRLDDADIAPYHDNFHQQPRYIPLSQ
PMPLLANTPFIVTGSGKFFRNVQLDPAANLGIVKVDSDGAGYHILWGLTNEAVPTSELPA
HFLSHCERIKATNGKDRVIMHCHATNLIALTYVLENDTAVFTRQLWEGSTECLVVFPDGV
GILPWMVPGTDEIGQATAQEMQKHSLVLWPFHGVFGSGPTLDETFGLIDTAEKSAQVLVK
VYSMGGMKQTISREELIALGKRFGVTPLASALAL
Enzyme 10 Number of Residues 274
Enzyme 10 Molecular Weight 30145.3
Enzyme 10 Theoretical pI 5.79
Enzyme 10 GO Classification
Function
  • aldehyde-lyase activity
  • binding
  • carbon-carbon lyase activity
  • catalytic activity
  • cation binding
  • ion binding
  • lyase activity
  • metal ion binding
  • rhamnulose-1-phosphate aldolase activity
Process
—
Component
—
Enzyme 10 General Function Involved in metal ion binding
Enzyme 10 Specific Function Catalyzes the reversible cleavage of L-rhamnulose-1- phosphate to dihydroxyacetone phosphate (DHAP) and L-lactaldehyde
Enzyme 10 Pathways Not Available
Enzyme 10 Reactions
  • L-rhamnulose 1-phosphate = glycerone phosphate + (S)-lactaldehyde [RN:R02263]
Enzyme 10 Pfam Domain Function
Enzyme 10 Signals
  • None
Enzyme 10 Transmembrane Regions
  • None
Enzyme 10 Essentiality Not Available
Enzyme 10 GenBank ID Protein 396681 Link Image
Enzyme 10 UniProtKB/Swiss-Prot ID P32169 Link Image
Enzyme 10 UniProtKB/Swiss-Prot Entry Name RHAD_ECOLI Link Image
Enzyme 10 PDB ID 1GT7 Link Image
Enzyme 10 PDB File Show
Enzyme 10 3D Structure
Enzyme 10 Cellular Location Not Available
Enzyme 10 Gene Sequence >825 bp 
ATGCAAAACATTACTCAGTCCTGGTTTGTCCAGGGAATGATCAAAGCCACCACCGACGCC
TGGCTGAAAGGCTGGGATGAGCGCAACGGCGGCAACCTGACGCTACGCCTGGATGACGCC
GATATCGCACCATATCACGACAATTTCCACCAACAACCGCGCTATATCCCGCTCAGCCAG
CCCATGCCTTTACTGGCAAATACACCGTTTATTGTCACCGGCTCGGGCAAATTCTTCCGT
AACGTCCAGCTTGATCCTGCGGCTAACTTAGGCATCGTAAAAGTCGACAGCGACGGCGCG
GGCTACCACATTCTTTGGGGGTTAACCAACGAAGCCGTCCCCACTTCCGAACTTCCGGCT
CACTTCCTTTCCCACTGCGAGCGCATTAAAGCCACCAACGGCAAAGATCGGGTGATCATG
CACTGCCACGCCACCAACCTGATCGCCCTCACCTATGTACTTGAAAACGACACCGCGGTC
TTCACTCGCCAACTGTGGGAAGGCAGCACCGAGTGTCTGGTGGTATTCCCGGATGGCGTT
GGCATTTTGCCGTGGATGGTGCCCGGCACGGACGAAATCGGCCAGGCGACCGCACAAGAG
ATGCAAAAACATTCGCTGGTGTTGTGGCCCTTCCACGGCGTCTTCGGCAGCGGACCGACG
CTGGATGAAACCTTCGGTTTAATCGACACCGCAGAAAAATCAGCACAAGTATTAGTGAAG
GTTTATTCGATGGGCGGCATGAAACAGACCATCAGCCGTGAAGAGTTGATAGCGCTCGGC
AAGCGTTTCGGCGTTACGCCACTCGCCAGTGCGCTGGCGCTGTAA
Enzyme 10 GenBank Gene ID X60472 Link Image
Enzyme 10 GeneCard ID rhaD Link Image
Enzyme 10 GenAtlas ID Not Available
Enzyme 10 HGNC ID Not Available
Enzyme 10 Chromosome Location Not Available
Enzyme 10 Locus Not Available
Enzyme 10 SNPs SNPJam Report Link Image
Enzyme 10 General References
  1. Moralejo P, Egan SM, Hidalgo E, Aguilar J: Sequencing and characterization of a gene cluster encoding the enzymes for L-rhamnose metabolism in Escherichia coli. J Bacteriol. 1993 Sep;175(17):5585-94. [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]
  5. Egan SM, Schleif RF: A regulatory cascade in the induction of rhaBAD. J Mol Biol. 1993 Nov 5;234(1):87-98. [PubMed Link Image]
  6. Holcroft CC, Egan SM: Roles of cyclic AMP receptor protein and the carboxyl-terminal domain of the alpha subunit in transcription activation of the Escherichia coli rhaBAD operon. J Bacteriol. 2000 Jun;182(12):3529-35. [PubMed Link Image]
  7. Kroemer M, Schulz GE: The structure of L-rhamnulose-1-phosphate aldolase (class II) solved by low-resolution SIR phasing and 20-fold NCS averaging. Acta Crystallogr D Biol Crystallogr. 2002 May;58(Pt 5):824-32. Epub 2002 Apr 26. [PubMed Link Image]
  8. Kroemer M, Merkel I, Schulz GE: Structure and catalytic mechanism of L-rhamnulose-1-phosphate aldolase. Biochemistry. 2003 Sep 16;42(36):10560-8. [PubMed Link Image]
Enzyme 10 Metabolite References Not Available
Enzyme 11 [top]
Enzyme 11 ID 16196
Enzyme 11 Name Dihydroneopterin aldolase
Enzyme 11 Synonyms Not Available
Enzyme 11 Gene Name folB
Enzyme 11 Protein Sequence >Dihydroneopterin aldolase 
MGMIRINNLRFHTFNGVLPEERRNGQQLGLDIAIKYPIETKVQHDDVHETINYAAVRNVV
DEFVTTHSYKLIESLANHLLQTLLTSFPAADAINIKIRKYSVPMPGIFDDVEIEVEGTPN
GK
Enzyme 11 Number of Residues 122
Enzyme 11 Molecular Weight 13816.7
Enzyme 11 Theoretical pI 5.99
Enzyme 11 GO Classification
Function
  • aldehyde-lyase activity
  • carbon-carbon lyase activity
  • catalytic activity
  • dihydroneopterin aldolase activity
  • lyase activity
Process
  • cellular aromatic compound metabolic process
  • cellular metabolic process
  • folic acid and derivative metabolic process
  • metabolic process
Component
—
Enzyme 11 General Function Involved in dihydroneopterin aldolase activity
Enzyme 11 Specific Function Not Available
Enzyme 11 Pathways Not Available
Enzyme 11 Reactions
  • 2-amino-4-hydroxy-6-(D-erythro-1,2,3-trihydroxypropyl)-7,8- dihydropteridine = 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine + glycolaldehyde [RN:R03504]
Enzyme 11 Pfam Domain Function
Enzyme 11 Signals
  • None
Enzyme 11 Transmembrane Regions
  • None
Enzyme 11 Essentiality Not Available
Enzyme 11 GenBank ID Protein 28272503 Link Image
Enzyme 11 UniProtKB/Swiss-Prot ID Q88ST2 Link Image
Enzyme 11 UniProtKB/Swiss-Prot Entry Name Q88ST2_LACPL Link Image
Enzyme 11 PDB ID Not Available
Enzyme 11 Cellular Location Not Available
Enzyme 11 Gene Sequence >369 bp 
ATGGGCATGATTCGAATTAATAATTTACGCTTTCACACGTTTAACGGGGTACTTCCGGAA
GAACGGCGTAATGGTCAACAACTAGGGCTAGATATTGCCATTAAATATCCTATCGAAACC
AAGGTTCAACACGATGACGTTCACGAGACCATCAATTACGCGGCGGTCCGTAACGTGGTC
GATGAATTTGTAACGACCCATTCATACAAGTTGATTGAATCGCTAGCTAACCACTTATTG
CAGACGTTATTGACAAGTTTTCCCGCGGCGGATGCAATCAATATTAAAATTCGTAAATAT
AGCGTACCAATGCCTGGAATCTTTGATGATGTGGAAATTGAGGTGGAGGGGACGCCGAAT
GGCAAGTAG
Enzyme 11 GenBank Gene ID AL935261 Link Image
Enzyme 11 GeneCard ID folB Link Image
Enzyme 11 GenAtlas ID Not Available
Enzyme 11 HGNC ID Not Available
Enzyme 11 Chromosome Location Not Available
Enzyme 11 Locus lp_3299
Enzyme 11 SNPs SNPJam Report Link Image
Enzyme 11 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 11 Metabolite References Not Available
Enzyme 12 [top]
Enzyme 12 ID 16197
Enzyme 12 Name SulD
Enzyme 12 Synonyms Not Available
Enzyme 12 Gene Name sulD
Enzyme 12 Protein Sequence >SulD 
MDTITLTGVHANGTHGVLAFEHERPQTFVVDVTLHLDLAAAGQSDDLNDTIDYGRVAKDI
VAVIEGPHVDLIERLAQRIADKILADAPAVASIDVTVHKPHAPIVVAFADVSVSISRVRA
TDNGRTAEKHAIHNAVVALGGNVGEVESTLRAAVREIDALLGTQVTGISPLYRTAAWGMA
DGTPDFLNAVVELGTTMGRHELLAALQNIEANHGRIRENHWDSRPLDLDIIDFDGITSAD
PDLALPHPRAWQRAFVLAPWLALNPNAKLAGAHEGPVADLLAAAPDRNAVQLESEDWMLG
GHAVKQKSASESAPVSRKAIISLDSTSQDAERLFRETIVSIDSVPGNQVQGISPLYHVSH
FDSPDAMSAVIQIETKLPPADLIAVLGSIESVHDLAVDLDLVDMEGVTSDEPNCSIPWPS
ARNHASVLAPWLDMDPNASLGGDPVAFLLAMAPDAGQVGLLSDNWILSNS
Enzyme 12 Number of Residues 470
Enzyme 12 Molecular Weight 50004.7
Enzyme 12 Theoretical pI 4.46
Enzyme 12 GO Classification
Function
  • 2-amino-4-hydroxy-6-hydroxymethyldihydropteridine diphosphokinase activity
  • aldehyde-lyase activity
  • carbon-carbon lyase activity
  • catalytic activity
  • dihydroneopterin aldolase activity
  • diphosphotransferase activity
  • lyase activity
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • cellular aromatic compound metabolic process
  • cellular metabolic process
  • folic acid and derivative biosynthetic process
  • folic acid and derivative metabolic process
  • metabolic process
Component
—
Enzyme 12 General Function Involved in dihydroneopterin aldolase activity
Enzyme 12 Specific Function Not Available
Enzyme 12 Pathways Not Available
Enzyme 12 Reactions Not Available
Enzyme 12 Pfam Domain Function
Enzyme 12 Signals
  • None
Enzyme 12 Transmembrane Regions
  • None
Enzyme 12 Essentiality Not Available
Enzyme 12 GenBank ID Protein 23325894 Link Image
Enzyme 12 UniProtKB/Swiss-Prot ID Q8G3R9 Link Image
Enzyme 12 UniProtKB/Swiss-Prot Entry Name Q8G3R9_BIFLO Link Image
Enzyme 12 PDB ID Not Available
Enzyme 12 Cellular Location Not Available
Enzyme 12 Gene Sequence >1413 bp 
ATGGAGTTGAACGAATTGCCCCAGATGGATCCGCGTGCGCTGAAGGCCACGTCTGTCAAA
GCCGAAGACGAACACGCCAATTCAGCCGAACCGCAAGCACTGAAAATCACCGCCGCCAGC
TCGAACCCAAAGATGTTCACGCTGCCCTGGCACAAGCCCTTGGCGACCTGGCCTAAGGAC
CTGCTGGCCAACCTGCCGCGAGGCATCTCCCGCCACGTCGTGCGATTCGTGCACGTGGGC
GACGAGGTGTACGCCATGAAGGAGATCACGCGCCAGGTGGCCGAGCGAGAGTACGAGATC
CTGCGTCGACTGCAGAAGCTCGAACTGCCAACTGTGACCCCGATCGCTGTGGTCATCGGC
CGTCACACCCGTGAAGGGGAGCCGCTGGAGGCGATTCTGGTCACCCGGCACTTGAAGTTC
TCGCTGCCGTACCGTGCGTTGTTCGCCCGCAACCTGCGCCCGGACACCGCCGAACGACTG
ATTGACGCCCTCGCCGTGCTGCTGGTGCGCCTGCACCTGGCCGGCTTCTACTGGGGCGAT
GTGTCCCTGTCGAACGTCCTGTTCCTGCGCGACGCCGACGCTTTCTCCGCCTTCCTGGTG
GACGCCGAGACCGGTGACCTGCAAGCCCAGCTCACCGACGGCCAGCGCGAATACGATATC
GACTTGGCCCGCACCAACATCATCGGCGAACTTATGGATTTGGCGTCCGGCAAGCTACTG
CTCGGCGACGTGGATGAGATCGAGGTGGGCAACCGCCTGGTTGATCGCTACCACTCGCTG
TGGAGCGCCCTGACCGACACCGACAAGTTCAACCCGGACGAAATGTGGAAGATCGAGCAG
CGCGTCAACAAGCTCAACGAGCTGGGCTTCGACGTGGACGAGCTGGAAATGAAGACCGCC
GAGGACGGCAAGCGTGTGCTGGTCCGCCCGCGCGTGGTGGACGCCGGCTATGCCAACCGC
AAGCTGCTGCGCCTCACCGGCCTTGACGTGCAGGAGAACCAGGCCCGTCGTCTGCTCAAC
GACCTTGACGCCTACCGTGCCTCCACGTGGCGTGAGGGCGAGGATCTGGAAATCGTGGCC
ACCGACTGGATGCGCGAGGTGTTCGAGCCGACCGTGCGTATGATTCCGCGCGAATATCGC
TCCCAGATCGAGCCTGCTCAGTTCTTCCATGAGGTGCTTGACCATCGCTGGTTCCTGGCG
GAGAAGGCCGGCCACGACGTGCCGATGGGCGAGGCCGTGACCAGCTACATCGACAACGCT
CTGCCGAGCTACAGCCTTGACTCCAAGGCACTCGCCGAACTTAACGAAGAGGCCGATTCC
GGCGTCATTGACGACGAATCCACCTACAGCGACCCGGACGACGACGGCTACAACCCCGAT
GACGATCCGGATGCGGCAGTGTGGAGTCATTAA
Enzyme 12 GenBank Gene ID AE014295 Link Image
Enzyme 12 GeneCard ID sulD Link Image
Enzyme 12 GenAtlas ID Not Available
Enzyme 12 HGNC ID Not Available
Enzyme 12 Chromosome Location Not Available
Enzyme 12 Locus BL1685
Enzyme 12 SNPs SNPJam Report Link Image
Enzyme 12 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 12 Metabolite References Not Available
Enzyme 13 [top]
Enzyme 13 ID 16198
Enzyme 13 Name Putative dihydroneopterin aldolase
Enzyme 13 Synonyms Not Available
Enzyme 13 Gene Name Not Available
Enzyme 13 Protein Sequence >Putative dihydroneopterin aldolase 
MTTQHYIFLENVRFYSYHGVAPQETAIGNEFIINLRLKTDFGKATETDEVEDTVSYADIY
AALKEEMELPSKLLEHVCGRIVKRLFRDFRKIREIEIKLAKRNPPMGADIDSAGVEMHCT
RD
Enzyme 13 Number of Residues 122
Enzyme 13 Molecular Weight 14111.0
Enzyme 13 Theoretical pI 5.65
Enzyme 13 GO Classification
Function
  • aldehyde-lyase activity
  • carbon-carbon lyase activity
  • catalytic activity
  • dihydroneopterin aldolase activity
  • lyase activity
Process
  • cellular aromatic compound metabolic process
  • cellular metabolic process
  • folic acid and derivative metabolic process
  • metabolic process
Component
—
Enzyme 13 General Function Involved in dihydroneopterin aldolase activity
Enzyme 13 Specific Function Not Available
Enzyme 13 Pathways Not Available
Enzyme 13 Reactions Not Available
Enzyme 13 Pfam Domain Function
Enzyme 13 Signals
  • None
Enzyme 13 Transmembrane Regions
  • None
Enzyme 13 Essentiality Not Available
Enzyme 13 GenBank ID Protein 60492107 Link Image
Enzyme 13 UniProtKB/Swiss-Prot ID Q5L9C5 Link Image
Enzyme 13 UniProtKB/Swiss-Prot Entry Name Q5L9C5_BACFN Link Image
Enzyme 13 PDB ID Not Available
Enzyme 13 Cellular Location Not Available
Enzyme 13 Gene Sequence >369 bp 
ATGAAAGGTATTTATGCTATTTCGTTGTTGGTCGTTTCCAACATTTTTATGACATTTGCC
TGGTACGGGCATTTGAAGCTACAGGAAACAAAAATAATCAGTAATTGGCCTTTGTATGGC
GTGGTTTTGTTTTCATGGGTGATTGCGTTGGCTGAGTATTCTTGTCAGGTTCCTGCCAAC
CGGCTGGGGTTCAGCGGAAACGGAGGGCCGTTTTCATTGATGCAACTTAAAATTATCCAA
GAGGTGATCACACTGATTATATTTACCGTTTTTTCTACCTTATTATTTAAAGGGGAGTCA
CTGCATTGGAATCATGTGGCAGCTTTTGTCTGCTTGATAGCAGCGGTATATTTCGTGTTT
ATGAGGTAG
Enzyme 13 GenBank Gene ID CR626927 Link Image
Enzyme 13 GeneCard ID Not Available
Enzyme 13 GenAtlas ID Not Available
Enzyme 13 HGNC ID Not Available
Enzyme 13 Chromosome Location Not Available
Enzyme 13 Locus BF3622
Enzyme 13 SNPs Not Available
Enzyme 13 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 13 Metabolite References Not Available
Enzyme 14 [top]
Enzyme 14 ID 16199
Enzyme 14 Name Dihydroneopterin aldolase
Enzyme 14 Synonyms Not Available
Enzyme 14 Gene Name Not Available
Enzyme 14 Protein Sequence >Dihydroneopterin aldolase 
MTTQHYIFLENVRFYSYHGVAPQETAIGNEFIINLRLKTDFGKATETDEVEDTVSYADIY
ATLKEEMELPSKLLEHVCGRIVKRLFRDFRKIKEIEIKLAKRNPPMGADIDSAGVEMHCT
RD
Enzyme 14 Number of Residues 122
Enzyme 14 Molecular Weight 14113.0
Enzyme 14 Theoretical pI 5.65
Enzyme 14 GO Classification
Function
  • aldehyde-lyase activity
  • carbon-carbon lyase activity
  • catalytic activity
  • dihydroneopterin aldolase activity
  • lyase activity
Process
  • cellular aromatic compound metabolic process
  • cellular metabolic process
  • folic acid and derivative metabolic process
  • metabolic process
Component
—
Enzyme 14 General Function Involved in dihydroneopterin aldolase 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 52215337 Link Image
Enzyme 14 UniProtKB/Swiss-Prot ID Q64PK9 Link Image
Enzyme 14 UniProtKB/Swiss-Prot Entry Name Q64PK9_BACFR Link Image
Enzyme 14 PDB ID Not Available
Enzyme 14 Cellular Location Not Available
Enzyme 14 Gene Sequence >369 bp 
ATGAAAGGTATTTATGCTATTTCGTTGTTAGTCGTTTCCAACATTTTTATGACATTTGCC
TGGTACGGGCATTTGAAGCTACAGGAAACAAAAATAATCAGTAATTGGCCTTTGTATGGC
GTGGTTTTGTTTTCATGGGTGATTGCGTTGGCTGAGTATTCTTGTCAGGTTCCTGCCAAC
CGGCTGGGGTTCAGCGGAAACGGAGGGCCGTTTTCATTGATGCAACTTAAAATTATCCAA
GAGGTGATCACACTGATTATATTTACCGTTTTTTCTACCTTATTATTTAAAGGGGAGTCA
CTGCATTGGAATCATGTGGCAGCTTTTGTCTGCTTGATAGCAGCGGTATATTTCGTGTTT
ATGAGGTAG
Enzyme 14 GenBank Gene ID AP006841 Link Image
Enzyme 14 GeneCard ID Not Available
Enzyme 14 GenAtlas ID Not Available
Enzyme 14 HGNC ID Not Available
Enzyme 14 Chromosome Location Not Available
Enzyme 14 Locus BF3830
Enzyme 14 SNPs Not Available
Enzyme 14 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 14 Metabolite References Not Available
Enzyme 15 [top]
Enzyme 15 ID 16200
Enzyme 15 Name Dihydroneopterin aldolase
Enzyme 15 Synonyms Not Available
Enzyme 15 Gene Name folB
Enzyme 15 Protein Sequence >Dihydroneopterin aldolase 
MDKILLSNLGFYGYHGVLKEENFLGQKFFVDMELYIDSREAGLSDDINKSVSYAEVYNVV
KDITENKQFNLLEALAENIAEEVLNKFILINGVMVRVRKPEAPVNGIYDYFGVEIRRARD
E
Enzyme 15 Number of Residues 121
Enzyme 15 Molecular Weight 13930.8
Enzyme 15 Theoretical pI 4.44
Enzyme 15 GO Classification
Function
  • aldehyde-lyase activity
  • carbon-carbon lyase activity
  • catalytic activity
  • dihydroneopterin aldolase activity
  • lyase activity
Process
  • cellular aromatic compound metabolic process
  • cellular metabolic process
  • folic acid and derivative metabolic process
  • metabolic process
Component
—
Enzyme 15 General Function Involved in dihydroneopterin aldolase activity
Enzyme 15 Specific Function Not Available
Enzyme 15 Pathways Not Available
Enzyme 15 Reactions
  • 2-amino-4-hydroxy-6-(D-erythro-1,2,3-trihydroxypropyl)-7,8- dihydropteridine = 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine + glycolaldehyde [RN:R03504]
Enzyme 15 Pfam Domain Function
Enzyme 15 Signals
  • None
Enzyme 15 Transmembrane Regions
  • None
Enzyme 15 Essentiality Not Available
Enzyme 15 GenBank ID Protein 115249068 Link Image
Enzyme 15 UniProtKB/Swiss-Prot ID Q18BX1 Link Image
Enzyme 15 UniProtKB/Swiss-Prot Entry Name Q18BX1_CLOD6 Link Image
Enzyme 15 PDB ID Not Available
Enzyme 15 Cellular Location Not Available
Enzyme 15 Gene Sequence >366 bp 
ATGACAATAGAACAAATATTAGAAGCTATAGAAAATATGAAAGTTTTAGAATTAAATGAA
TTAGTTAAAGCTGCTGAAGAAAAATTCGGTGTATCAGCTTCAGCTCCAGTAATGGTAGCT
GGTGCAGCTGCTGGTGGACCAGCTGCTGAAGAAAAAACTGAGTTTGATGTAGTATTAACT
GACGTTGGTTCTTCAAAAGTTGGAGTTATAAAAGCAGTTAGAGAAATAACAGGATTAGGA
TTAAAAGAAGCTAAAGAAGTAGTTGACAATGCTCCTAAGACAGTTAAAGAAGGAGCTTCT
AAAGAAGAAGCTGATCAAATAAAAGAGAAATTAGAAGCTGCTGGAGCTAAAGTAGAAGTT
AAGTAG
Enzyme 15 GenBank Gene ID AM180355 Link Image
Enzyme 15 GeneCard ID folB Link Image
Enzyme 15 GenAtlas ID Not Available
Enzyme 15 HGNC ID Not Available
Enzyme 15 Chromosome Location Not Available
Enzyme 15 Locus CD1451
Enzyme 15 SNPs SNPJam Report Link Image
Enzyme 15 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 15 Metabolite References Not Available
Enzyme 16 [top]
Enzyme 16 ID 16201
Enzyme 16 Name Bifunctional folate synthesis protein
Enzyme 16 Synonyms Not Available
Enzyme 16 Gene Name folA/folK
Enzyme 16 Protein Sequence >Bifunctional folate synthesis protein 
MDKIIIKDFEVFGNHGVFEEEKRLGQKFVLSIELFLDTREAGVTGDLSKSVHYGELAHKV
EEEFKKQSYDLIETAAEKLCEFILLEYPLVKKVKVSLKKPWAPILRSLDTVSIEIERGWN
EAYLSYGSNIGDKKYYIEEALKEINKAYHTEIIKKSNLIETEPWGYTEQDEFLNGACKIK
TLLNPKELIKFLLSIEQKLKRERKIKWGPRTIDLDVIFFNDLISEDEEIILPHPRMHERS
FVLEPLNEIAPYKIHPLYRKRVFELLEELNKNK
Enzyme 16 Number of Residues 273
Enzyme 16 Molecular Weight 32115.8
Enzyme 16 Theoretical pI 5.97
Enzyme 16 GO Classification
Function
  • 2-amino-4-hydroxy-6-hydroxymethyldihydropteridine diphosphokinase activity
  • aldehyde-lyase activity
  • carbon-carbon lyase activity
  • catalytic activity
  • dihydroneopterin aldolase activity
  • diphosphotransferase activity
  • lyase activity
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • cellular aromatic compound metabolic process
  • cellular metabolic process
  • folic acid and derivative biosynthetic process
  • folic acid and derivative metabolic process
  • metabolic process
Component
—
Enzyme 16 General Function Involved in dihydroneopterin aldolase activity
Enzyme 16 Specific Function Not Available
Enzyme 16 Pathways Not Available
Enzyme 16 Reactions Not Available
Enzyme 16 Pfam Domain Function
Enzyme 16 Signals
  • None
Enzyme 16 Transmembrane Regions
  • None
Enzyme 16 Essentiality Not Available
Enzyme 16 GenBank ID Protein 18143875 Link Image
Enzyme 16 UniProtKB/Swiss-Prot ID Q8XLL9 Link Image
Enzyme 16 UniProtKB/Swiss-Prot Entry Name Q8XLL9_CLOPE Link Image
Enzyme 16 PDB ID Not Available
Enzyme 16 Cellular Location Not Available
Enzyme 16 Gene Sequence >822 bp 
ATGGGATTTATTGTATTTTGTTTGATAGCATACTTTGTAATATCTCATTTGTCAAATAAG
AAAGATGTTAGTGGAAATAAAGCTAATAGTAATTGTCCATATTGTAATGCAGCTTTTTAC
TTAACTGAAAATGGAGATTTTAATTGTTCAAATTGTGGTCGTTTATTCAAATATAGAGAT
GGTATTGTGTATAGGCAGGATGAAAGATTACCTATTGTAGTTGAGTTAGCATGTACACTT
TTTACAATATTATGTAAAGCTGATGGGGTTGTAACAAAAGATGAAGTTTCAATAACTAAA
GAACTACTTGAAAAAAATTTTGGATTAGAAGATAAAGATATGAAAATGGCTATAGATATT
TTAAATAAGTCTAAAAGTAAGCCATATACTAAAACCATAATAAATGATTTAAATAATATT
TTTAATAATTATGATTTTTCTAAGACAGATGCCGAAGACTACAAAGAACTTATACTTAGA
TGTGCTATGATTATAGCATTTTGTGATGATGGAGAACCTTCTAATAATCAAAATAAAATA
TTAGACGATATTGTTAGTATATTTAATATATCTGCTACTAAATATACAAATTTATTAAAT
TATTTTAGAGATAACTGTATTGAAAAAAATAAAAATGATTATTATGAAATATTGGGGGTT
TCAGAAGGAGCTAGTAAAGAAGAAATTAGAGCTGCTTTTAGAAAATTAAGTAAATTATAT
CATCCGGATAGATATTCATCTAAAGATCTTCCTCCTGAAATAATAAAAGAATTTGAGGAG
AAGTTAGCAAAAATAATTGAAGCTTATGAAGCATTAAAATAA
Enzyme 16 GenBank Gene ID BA000016 Link Image
Enzyme 16 GeneCard ID folA/folK Link Image
Enzyme 16 GenAtlas ID Not Available
Enzyme 16 HGNC ID Not Available
Enzyme 16 Chromosome Location Not Available
Enzyme 16 Locus CPE1022
Enzyme 16 SNPs SNPJam Report Link Image
Enzyme 16 General References
  1. Shimizu T, Ohtani K, Hirakawa H, Ohshima K, Yamashita A, Shiba T, Ogasawara N, Hattori M, Kuhara S, Hayashi H: Complete genome sequence of Clostridium perfringens, an anaerobic flesh-eater. Proc Natl Acad Sci U S A. 2002 Jan 22;99(2):996-1001. Epub 2002 Jan 15. [PubMed Link Image]
Enzyme 16 Metabolite References Not Available
Enzyme 17 [top]
Enzyme 17 ID 16202
Enzyme 17 Name Dihydroneopterin aldolase/2-amino-4-hydroxy-6-hydroxymethyldihydropteridine pyrophosphokinase
Enzyme 17 Synonyms Not Available
Enzyme 17 Gene Name folBK
Enzyme 17 Protein Sequence >Dihydroneopterin aldolase/2-amino-4-hydroxy-6-hydroxymethyldihydropteridine pyrophosphokinase 
MDKIIIKDFEVFGNHGVFEEEKRLGQKFVLSIELFLDTREAGVTGDLSKSVHYGELAHKV
EEEFKKQSYDLIETAAEKLCEFILLEYPLVKKVKVSLKKPWAPILRSLDTVSIEIERGWN
EAYLSYGSNIGDKKYYIEEALNEINKAYHTEIIKKSNLIETEPWGYTEQDEFLNGACKIK
TLLNPKELIKFLLSVEQKLKRERKIKWGPRTIDLDVIFFNDLISEDEEIILPHPRMHERS
FVLEPLNEIAPYKIHPLYRKRVFELLEELNKNK
Enzyme 17 Number of Residues 273
Enzyme 17 Molecular Weight 32087.8
Enzyme 17 Theoretical pI 5.73
Enzyme 17 GO Classification
Function
  • 2-amino-4-hydroxy-6-hydroxymethyldihydropteridine diphosphokinase activity
  • aldehyde-lyase activity
  • carbon-carbon lyase activity
  • catalytic activity
  • dihydroneopterin aldolase activity
  • diphosphotransferase activity
  • lyase activity
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • cellular aromatic compound metabolic process
  • cellular metabolic process
  • folic acid and derivative biosynthetic process
  • folic acid and derivative metabolic process
  • metabolic process
Component
—
Enzyme 17 General Function Involved in dihydroneopterin aldolase activity
Enzyme 17 Specific Function Not Available
Enzyme 17 Pathways Not Available
Enzyme 17 Reactions
  • 2-amino-4-hydroxy-6-(D-erythro-1,2,3-trihydroxypropyl)-7,8- dihydropteridine = 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine + glycolaldehyde [RN:R03504]
Enzyme 17 Pfam Domain Function
Enzyme 17 Signals
  • None
Enzyme 17 Transmembrane Regions
  • None
Enzyme 17 Essentiality Not Available
Enzyme 17 GenBank ID Protein 110674498 Link Image
Enzyme 17 UniProtKB/Swiss-Prot ID Q0TRL7 Link Image
Enzyme 17 UniProtKB/Swiss-Prot Entry Name Q0TRL7_CLOP1 Link Image
Enzyme 17 PDB ID Not Available
Enzyme 17 Cellular Location Not Available
Enzyme 17 Gene Sequence >822 bp 
TTGAAAAGGCTAAAAAGAATATATTTTTCTATTTTAATTTTGATTACACTTATTGCTCTA
GGATTTTTGTTATATCCTAGTTTTTCTAATTACATAAATAATAAATTTGCAGTTTCTACA
ATTTCTGATTATACAGAGAAGATAAATAATGTTAAGGATGAAGAAGTTGATGATTTAATA
AAAAATATTAATAAGTATAATTATGATTTATTTAATGGAACTGCTGAAAATGAATTGCCA
GATTACTTAAATATTCATGAAGGGGATGTCTTAGGGTACATAGAAATTCCTAGTATAAAT
ATTAAATTACCTATATACTATGGAAGTTCAGTTGATATTTTAAAAAAAGGTGTTGGAGTT
TTAGAGGGGACATCACTTCCTGTGGGAGGGGAAAATACTCATTCAGTTTTATCAGCTCAT
ACTGGATTAGCAAATCAAAAACTTTTTACTGATATAGACAAGCTAAAAGATGGAGATGTT
TTTTATTTACATATTTTAAAAAAGGATCTTGCTTATAAAGTGAATCAAATAAAAGTTGTT
CACCCAGATGAAATTGATGACCTAAAAATATCAGAGGATAAGGACTATGTAACTTTACTA
ACTTGTTATCCTTATGGAATTAATACTGAACGTTTATTAGTAAGGGGAGAGAGAACTGAT
TTAAGTGAAAGGACTGAAGTGCAGGTTCAAAAGGAAATAAGTACTTTTAATCATTCAAAT
GAAAATTTAATACTAATAGTTATAATATTAATTTCAGTGCTAATAATTATTTTCTTATTG
TTTTTAATTATGAAATTTAAAGGGAAAAATAAGAGTAGATAA
Enzyme 17 GenBank Gene ID CP000246 Link Image
Enzyme 17 GeneCard ID folBK Link Image
Enzyme 17 GenAtlas ID Not Available
Enzyme 17 HGNC ID Not Available
Enzyme 17 Chromosome Location Not Available
Enzyme 17 Locus CPF_1277
Enzyme 17 SNPs SNPJam Report Link Image
Enzyme 17 General References
  1. Myers GS, Rasko DA, Cheung JK, Ravel J, Seshadri R, DeBoy RT, Ren Q, Varga J, Awad MM, Brinkac LM, Daugherty SC, Haft DH, Dodson RJ, Madupu R, Nelson WC, Rosovitz MJ, Sullivan SA, Khouri H, Dimitrov GI, Watkins KL, Mulligan S, Benton J, Radune D, Fisher DJ, Atkins HS, Hiscox T, Jost BH, Billington SJ, Songer JG, McClane BA, Titball RW, Rood JI, Melville SB, Paulsen IT: Skewed genomic variability in strains of the toxigenic bacterial pathogen, Clostridium perfringens. Genome Res. 2006 Aug;16(8):1031-40. Epub 2006 Jul 6. [PubMed Link Image]
Enzyme 17 Metabolite References Not Available
Enzyme 18 [top]
Enzyme 18 ID 16203
Enzyme 18 Name Dihydroneopterin aldolase/2-amino-4-hydroxy-6-hydroxymethyldihydropteridine pyrophosphokinase
Enzyme 18 Synonyms Not Available
Enzyme 18 Gene Name folBK
Enzyme 18 Protein Sequence >Dihydroneopterin aldolase/2-amino-4-hydroxy-6-hydroxymethyldihydropteridine pyrophosphokinase 
MDKIIIKDFEVFGNHGVFKEEKRLGQKFVLSIELFLDTREAGVTGDLSKSVHYGELAHKV
EEEFKKQSYDLIETAAEKLCEFILLEYPLVKKVKVSLKKPWAPILRSLDTVSIEIERGWN
EAYLSYGSNIGDKKYYIEEALKEINKAYHTEIIKKSNLIETEPWGYTEQDEFLNGACKIK
TLLNPKELIKFLLSIEQKLKRERKIKWGPRTIDLDVIFFNDLISEDEEIILPHPRMHERS
FVLEPLNEIAPYKIHPLYRKRVFELLEELNKNK
Enzyme 18 Number of Residues 273
Enzyme 18 Molecular Weight 32114.9
Enzyme 18 Theoretical pI 6.42
Enzyme 18 GO Classification
Function
  • 2-amino-4-hydroxy-6-hydroxymethyldihydropteridine diphosphokinase activity
  • aldehyde-lyase activity
  • carbon-carbon lyase activity
  • catalytic activity
  • dihydroneopterin aldolase activity
  • diphosphotransferase activity
  • lyase activity
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • cellular aromatic compound metabolic process
  • cellular metabolic process
  • folic acid and derivative biosynthetic process
  • folic acid and derivative metabolic process
  • metabolic process
Component
—
Enzyme 18 General Function Involved in dihydroneopterin aldolase activity
Enzyme 18 Specific Function Not Available
Enzyme 18 Pathways Not Available
Enzyme 18 Reactions
  • 2-amino-4-hydroxy-6-(D-erythro-1,2,3-trihydroxypropyl)-7,8- dihydropteridine = 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine + glycolaldehyde [RN:R03504]
Enzyme 18 Pfam Domain Function
Enzyme 18 Signals
  • None
Enzyme 18 Transmembrane Regions
  • None
Enzyme 18 Essentiality Not Available
Enzyme 18 GenBank ID Protein 110682190 Link Image
Enzyme 18 UniProtKB/Swiss-Prot ID Q0STY6 Link Image
Enzyme 18 UniProtKB/Swiss-Prot Entry Name Q0STY6_CLOPS Link Image
Enzyme 18 PDB ID Not Available
Enzyme 18 Cellular Location Not Available
Enzyme 18 Gene Sequence >822 bp 
TTGAAAAGGCTAAAAAGAATATATTTTTCTATTTTAATTTTGATTACACTTATTGCTCTA
GGATTTTTGTTATATCCTAGTTTTTCTAATTACATAAATAATAAATTTGCAGTTTCTACA
ATTTCTGATTATACAGAGAAGATAAATAATGTTAAGGATGAAGAAGTTGATGATTTAATA
AAAAATATTAATAAGTATAATTATGATTTATTTAATGGAACTGCTGAAAATCAATTGCCA
GATTACTTAAATATTCATGAAGGGGATGTCTTAGGGTACATAGAAATTCCTAGTATAAAT
ATTAAGTTACCTATATACTATGGAACTTCAGTTGATATTTTGAAAAAAGGAGTTGGAGTT
TTAGAGGGGACATCACTTCCTGTAGGAGGGGAAAATACTCATTCAGTTTTATCAGCTCAT
ACTGGATTAGCAAATCAAAAACTTTTTACTGATATAGACAAACTAAAAGATGGAGATGTT
TTTTATTTGCATATTTTAAAAAAGGATCTTGCTTATAAAGTGAATCAAATAAAAGTTGTT
CACCCAGATGAAATTGATGAACTGAAAATATCAGATGACAAGGACTATGTAACTTTACTA
ACTTGTTATCCTTATGGGATTAATACTGAACGTTTATTAGTAAGGGGAGAGAGAACGGAT
TTAAGTCCAAGTAATGTAGAGCAGGTTCAAAAGGAAATAAGCACTTTTAATCATTCAAAT
GAAAATTTAATACTAATAGTTATAATATTAAATTCAGTGCTAATAATTATTTTCTTATTG
TTTTTAATTATGAAATTTAAAGGGAAAAATAAGAGTAGATAA
Enzyme 18 GenBank Gene ID CP000312 Link Image
Enzyme 18 GeneCard ID folBK Link Image
Enzyme 18 GenAtlas ID Not Available
Enzyme 18 HGNC ID Not Available
Enzyme 18 Chromosome Location Not Available
Enzyme 18 Locus CPR_1099
Enzyme 18 SNPs SNPJam Report Link Image
Enzyme 18 General References
  1. Myers GS, Rasko DA, Cheung JK, Ravel J, Seshadri R, DeBoy RT, Ren Q, Varga J, Awad MM, Brinkac LM, Daugherty SC, Haft DH, Dodson RJ, Madupu R, Nelson WC, Rosovitz MJ, Sullivan SA, Khouri H, Dimitrov GI, Watkins KL, Mulligan S, Benton J, Radune D, Fisher DJ, Atkins HS, Hiscox T, Jost BH, Billington SJ, Songer JG, McClane BA, Titball RW, Rood JI, Melville SB, Paulsen IT: Skewed genomic variability in strains of the toxigenic bacterial pathogen, Clostridium perfringens. Genome Res. 2006 Aug;16(8):1031-40. Epub 2006 Jul 6. [PubMed Link Image]
Enzyme 18 Metabolite References Not Available
Enzyme 19 [top]
Enzyme 19 ID 16204
Enzyme 19 Name Dihydroneopterin aldolase
Enzyme 19 Synonyms Not Available
Enzyme 19 Gene Name folB
Enzyme 19 Protein Sequence >Dihydroneopterin aldolase 
MDKIRINNLKFFTKNGVLAEEKRLGQQVEIDLEMQLSLAEAGRTDDVTQTVNYAEVNELI
AQRVNNHSYDLIEGLASAILDDISADYQEQLNKIIIKIRKYSVPMPGLFDNIEIEMEREV
Enzyme 19 Number of Residues 120
Enzyme 19 Molecular Weight 13756.5
Enzyme 19 Theoretical pI 4.28
Enzyme 19 GO Classification
Function
  • aldehyde-lyase activity
  • carbon-carbon lyase activity
  • catalytic activity
  • dihydroneopterin aldolase activity
  • lyase activity
Process
  • cellular aromatic compound metabolic process
  • cellular metabolic process
  • folic acid and derivative metabolic process
  • metabolic process
Component
—
Enzyme 19 General Function Involved in dihydroneopterin aldolase activity
Enzyme 19 Specific Function Not Available
Enzyme 19 Pathways Not Available
Enzyme 19 Reactions Not Available
Enzyme 19 Pfam Domain Function
Enzyme 19 Signals
  • None
Enzyme 19 Transmembrane Regions
  • None
Enzyme 19 Essentiality Not Available
Enzyme 19 GenBank ID Protein 29342702 Link Image
Enzyme 19 UniProtKB/Swiss-Prot ID Q82Z10 Link Image
Enzyme 19 UniProtKB/Swiss-Prot Entry Name Q82Z10_ENTFA Link Image
Enzyme 19 PDB ID Not Available
Enzyme 19 Cellular Location Not Available
Enzyme 19 Gene Sequence >363 bp 
ATGACAACGACAACAGTGTATTATGCAAGCAATAATGAAAAACAGCCGAACCGTTTTCAA
CTAGTTATCGGTAGCTGTAGCTATGAACTTCCAAAAATAGAAATCTACGAAATCCTGGAA
TGTGTCGCTTCAGCATATGGCTATCAAAAAGAACCATTCATTGAAGAACAAACAGAATGT
TTTGTTAAAGGCAACCGTTGTATACATGTTTCCCAACAAGCGACGACGTTGACTTTTGTT
GTGAATGATCTGCGTTTAGTAATGGAAAAACAATGCCGGAATCACGAAGAAGTCTTTCAA
GAAGTAAATCATATTTTATTGAATATTTTTGAGGAGACCCCTTGTGTTTTTCTCGAAAAG
TAG
Enzyme 19 GenBank Gene ID AE016830 Link Image
Enzyme 19 GeneCard ID folB Link Image
Enzyme 19 GenAtlas ID Not Available
Enzyme 19 HGNC ID Not Available
Enzyme 19 Chromosome Location Not Available
Enzyme 19 Locus EF_3269
Enzyme 19 SNPs SNPJam Report Link Image
Enzyme 19 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 19 Metabolite References Not Available
Enzyme 20 [top]
Enzyme 20 ID 16205
Enzyme 20 Name Dihydroneopterin aldolase
Enzyme 20 Synonyms
  1. DHNA
Enzyme 20 Gene Name folB
Enzyme 20 Protein Sequence >Dihydroneopterin aldolase 
MDIVFIEQLSVITTIGVYDWEQTIEQKLVFDIEMAWDNRKAAKSDDVADCLSYADIAETV
VSHVEGARFALVERVAEEVAELLLARFNSPWVRIKLSKPGAVARAANVGVIIERGNNLKE
NN
Enzyme 20 Number of Residues 122
Enzyme 20 Molecular Weight 13619.4
Enzyme 20 Theoretical pI 4.41
Enzyme 20 GO Classification
Function
  • aldehyde-lyase activity
  • carbon-carbon lyase activity
  • catalytic activity
  • dihydroneopterin aldolase activity
  • lyase activity
Process
  • cellular aromatic compound metabolic process
  • cellular metabolic process
  • folic acid and derivative metabolic process
  • metabolic process
Component
—
Enzyme 20 General Function Involved in dihydroneopterin aldolase activity
Enzyme 20 Specific Function Catalyzes the conversion of 7,8-dihydroneopterin to 6- hydroxymethyl-7,8-dihydropterin. Can use L-threo-dihydroneopterin and D-erythro-dihydroneopterin as substrates for the formation of 6-hydroxymethyldihydropterin, but it can also catalyze the epimerization of carbon 2' of dihydroneopterin and dihydromonapterin at appreciable velocity
Enzyme 20 Pathways Not Available
Enzyme 20 Reactions
  • 2-amino-4-hydroxy-6-(D-erythro-1,2,3-trihydroxypropyl)-7,8- dihydropteridine = 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine + glycolaldehyde [RN:R03504]
Enzyme 20 Pfam Domain Function
Enzyme 20 Signals
  • None
Enzyme 20 Transmembrane Regions
  • None
Enzyme 20 Essentiality Not Available
Enzyme 20 GenBank ID Protein 85674637 Link Image
Enzyme 20 UniProtKB/Swiss-Prot ID P0AC16 Link Image
Enzyme 20 UniProtKB/Swiss-Prot Entry Name FOLB_ECOLI Link Image
Enzyme 20 PDB ID Not Available
Enzyme 20 Cellular Location Not Available
Enzyme 20 Gene Sequence >369 bp 
ATGAAATATAGTTCAATATTTTCGATGCTTTCATTTTTTATACTATTTGCCTGTAATGAG
ACAGCTGTTTACGGTTCTGATGAAAACATTATTTTTATGAGGTATGTGGAAAAATTACAT
TTAGATAAATACTCTGTTAAAAATACGGTAAAAACTGAAACAATGGCGATACAATTAGCT
GAAATATATGTTAGGTATCGCTATGGCGAACGGATTGCAGAAGAAGAAAAACCATATTTA
ATTACGGAACTACCAGATAGTTGGGTTGTTGAGGGAGCAAAGTTACCTTATGAAGTTGCG
GGTGGTGTATTTATTATAGAAATTAATAAGAAAAATGGATGTGTTTTGAATTTCCTACAT
AGTAAATAA
Enzyme 20 GenBank Gene ID AP009048 Link Image
Enzyme 20 GeneCard ID folB Link Image
Enzyme 20 GenAtlas ID Not Available
Enzyme 20 HGNC ID Not Available
Enzyme 20 Chromosome Location Not Available
Enzyme 20 Locus b3058
Enzyme 20 SNPs SNPJam Report Link Image
Enzyme 20 General References
  1. Cain BD, Norton PJ, Eubanks W, Nick HS, Allen CM: Amplification of the bacA gene confers bacitracin resistance to Escherichia coli. J Bacteriol. 1993 Jun;175(12):3784-9. [PubMed Link Image]
  2. 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]
  3. 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]
  4. Haussmann C, Rohdich F, Schmidt E, Bacher A, Richter G: Biosynthesis of pteridines in Escherichia coli. Structural and mechanistic similarity of dihydroneopterin-triphosphate epimerase and dihydroneopterin aldolase. J Biol Chem. 1998 Jul 10;273(28):17418-24. [PubMed Link Image]
Enzyme 20 Metabolite References Not Available
Enzyme 21 [top]
Enzyme 21 ID 16804
Enzyme 21 Name 1,3-propanediol dehydrogenase
Enzyme 21 Synonyms Not Available
Enzyme 21 Gene Name dhaT
Enzyme 21 Protein Sequence >1,3-propanediol dehydrogenase 
MVYRMIFNQTAYFGRGAIKEIPAVAKQHGFTKAFIVTDPVLLETGTAEKVTKVLDEAGLP
YEVFSNVKPNPPVECIKDGVAKFADSGADFLIGLGGGSPQDTCKGIGIITANPEFADVLS
LEGVADTKNPSVPIFGVPTTAGTASETTINYVVTDTANKRKFVAVDPHDIPIVAFVDPDL
TDSMPRGLKVATGLDALTHAIEGYITPGAWSLSDCLSMQTIRMIAKNLAKSADGDIPAGE
QMAYASYITGMAYSNVGLGLVHGMAHPLGGRLGVAHGVANGILLAPVMEYNKDFTGEKYR
DIADAFGVEDAYTGDLEKVREEAVQAVHKLTVDLKNPTTISEVGATEADLEPLAHDAFND
VCTPGNPRQATEEDILAIYKSLM
Enzyme 21 Number of Residues 383
Enzyme 21 Molecular Weight 40608.8
Enzyme 21 Theoretical pI 4.50
Enzyme 21 GO Classification
Function
  • binding
  • catalytic activity
  • cation binding
  • ion binding
  • metal ion binding
  • oxidoreductase activity
Process
  • metabolic process
  • oxidation reduction
Component
—
Enzyme 21 General Function Involved in oxidoreductase activity
Enzyme 21 Specific Function Not Available
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 189428274 Link Image
Enzyme 21 UniProtKB/Swiss-Prot ID B3DR01 Link Image
Enzyme 21 UniProtKB/Swiss-Prot Entry Name B3DR01_BIFLD Link Image
Enzyme 21 PDB ID Not Available
Enzyme 21 Cellular Location Not Available
Enzyme 21 Gene Sequence >1152 bp 
ATGACTTACGTTTCTGAAAGCTTCTGGCACGACGCCGTCAACAAAGCCACCACCGATCTG
TTCACCTTCGGCTACAAGCACATCATCAAACCGAACTTCGTGTTCAACCACCGCCCCGAT
GAGGCACACGATCAGATGATCGAGTTCTGCCACGTCGTCAAGAACGTCCCGCCGCTGCTG
CTCGCCGAACAGCTGATGCTCGACTACACCGACCCCATTCTGGAAACGAATGTGATGGGC
GTCGATTTCACCAACCCGTTCGGCCTGTCCGCCGGCCTCGACAAGAACTGCGAGATGCCC
GTGGTGCTGGACCATGCCGGCTTCGGCTTCGAAACCGTAGGCTCCACCACCTCGCGTCCC
TGCCCGGGCAACGCCAAGCCGTGGTTCCACCGTCTGCCTGAATACGATTCGATGATGGTG
CACGTCGGCCTCGCCAACATCGGTTCGGACAAGGTCATCGAGCGCGCCGAGAAGGCTTGG
ACTCAGGCCCGCCAGATGCAGCTGTCCGTGTCGATCGCCCGCACCAACGACGACCAGTGC
GGCGATTTGGACGAAGGCATTGAGGATTACTGCATTTCAATGCGCCGCGCCGCCGGCCGC
ACCGCGATGGTGGAGGTCAACGTCTCCTGCCCGAACACGCACGTCGGCGAACCGTTCACC
GCGACTCCGGAAGCGCTCGACCGTCTGTTTACGGCGCTCGACAAGATCGACCGCCCGCAG
CCCACGCTGGTCAAGATGCCGTTGAACAAGCCGTGGGGCGAGTACAAGGAACTGCTCGAT
GTGCTGGCCGAGCACAATGTGCAGGGGCTGTCCATCGCCAATCTGCAGAAGGACCGCACC
GGCCTCGAGATTCCGCGCGATTGGGAGGGCGGCCTGTCCGGCGGCCCGTGCACCAACGCC
AGCACCGAGCTGATTCGCAAGGTGTATAAAGAGTATGGCGACCGGTTCGCTATCGCCGGC
ATCGGTGGCGTCTTTACCCCCGAGCAAGCCTATGCGAAGATTCGTTCCGGCTCCAGCTTG
GTCATGTTCATCAGTTCGCTGATGTACCGAGGCCCGCAGCAGATTACCGTGTTGAAGCGC
GGTCTGGCCCAGCTGCTGCGCCGCGACGGATTCGAGCACGTCTCCGACGCCGTCGGCGTA
GACGTGGAGTGA
Enzyme 21 GenBank Gene ID CP000605 Link Image
Enzyme 21 GeneCard ID dhaT Link Image
Enzyme 21 GenAtlas ID Not Available
Enzyme 21 HGNC ID Not Available
Enzyme 21 Chromosome Location Not Available
Enzyme 21 Locus BLD_1839
Enzyme 21 SNPs SNPJam Report Link Image
Enzyme 21 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 21 Metabolite References Not Available
Enzyme 22 [top]
Enzyme 22 ID 16805
Enzyme 22 Name L-1,2-propanediol oxidoreductase
Enzyme 22 Synonyms Not Available
Enzyme 22 Gene Name fucO
Enzyme 22 Protein Sequence >L-1,2-propanediol oxidoreductase 
MMANRMILNETAWFGRGAVGALTDEVKRRGYQKALIVTDKTLVQCGVVAKVTDKMDAAGL
AWAIYDGVVPNPTITVVKEGLGVFQNSGADYLIAIGGGSPQDTCKAIGIISNNPEFADVR
SLEGLSPTNKPSVPILAIPTTAGTAAEVTINYVITDEEKRRKFVCVDPHDIPQVAFIDAD
MMDGMPPALKAATGVDALTHAIEGYITRGAWALTDALHIKAIEIIAGALRGSVAGDKDAG
EEMALGQYVAGMGFSNVGLGLVHGMAHPLGAFYNTPHGVANAILLPHVMRYNADFTGEKY
RDIARVMGVKVEGMSLEEARNAAVEAVFALNRDVGIPPHLRDVGVRKEDIPALAQAALDD
VCTGGNPREATLEDIVELYHTAW
Enzyme 22 Number of Residues 383
Enzyme 22 Molecular Weight 40644.2
Enzyme 22 Theoretical pI 4.91
Enzyme 22 GO Classification
Function
  • binding
  • catalytic activity
  • cation binding
  • ion binding
  • metal ion binding
  • oxidoreductase activity
Process
  • metabolic process
  • oxidation reduction
Component
—
Enzyme 22 General Function Involved in oxidoreductase activity
Enzyme 22 Specific Function Not Available
Enzyme 22 Pathways Not Available
Enzyme 22 Reactions Not Available
Enzyme 22 Pfam Domain Function
Enzyme 22 Signals
  • None
Enzyme 22 Transmembrane Regions
  • None
Enzyme 22 Essentiality Not Available
Enzyme 22 GenBank ID Protein 169887569 Link Image
Enzyme 22 UniProtKB/Swiss-Prot ID B1XDK8 Link Image
Enzyme 22 UniProtKB/Swiss-Prot Entry Name B1XDK8_ECODH Link Image
Enzyme 22 PDB ID 1RRM Link Image
Enzyme 22 PDB File Show
Enzyme 22 3D Structure
Enzyme 22 Cellular Location Not Available
Enzyme 22 Gene Sequence >1152 bp 
ATGTTTGAACCAATGGAACTTACCAATGACGCGGTGATTAAAGTCATCGGCGTCGGCGGC
GGCGGCGGTAATGCTGTTGAACACATGGTGCGCGAGCGCATTGAAGGTGTTGAATTCTTC
GCGGTAAATACCGATGCACAAGCGCTGCGTAAAACAGCGGTTGGACAGACGATTCAAATC
GGTAGCGGTATCACCAAAGGACTGGGCGCTGGCGCTAATCCAGAAGTTGGCCGCAATGCG
GCTGATGAGGATCGCGATGCATTGCGTGCGGCGCTGGAAGGTGCAGACATGGTCTTTATT
GCTGCGGGTATGGGTGGTGGTACCGGTACAGGTGCAGCACCAGTCGTCGCTGAAGTGGCA
AAAGATTTGGGTATCCTGACCGTTGCTGTCGTCACTAAGCCTTTCAACTTTGAAGGCAAG
AAGCGTATGGCATTCGCGGAGCAGGGGATCACTGAACTGTCCAAGCATGTGGACTCTCTG
ATCACTATCCCGAACGACAAACTGCTGAAAGTTCTGGGCCGCGGTATCTCCCTGCTGGAT
GCGTTTGGCGCAGCGAACGATGTACTGAAAGGCGCTGTGCAAGGTATCGCTGAACTGATT
ACTCGTCCGGGTTTGATGAACGTGGACTTTGCAGACGTACGCACCGTAATGTCTGAGATG
GGCTACGCAATGATGGGTTCTGGCGTGGCGAGCGGTGAAGACCGTGCGGAAGAAGCTGCT
GAAATGGCTATCTCTTCTCCGCTGCTGGAAGATATCGACCTGTCTGGCGCGCGCGGCGTG
CTGGTTAACATCACGGCGGGCTTCGACCTGCGTCTGGATGAGTTCGAAACGGTAGGTAAC
ACCATCCGTGCATTTGCTTCCGACAACGCGACTGTGGTTATCGGTACTTCTCTTGACCCG
GATATGAATGACGAGCTGCGCGTAACCGTTGTTGCGACAGGTATCGGCATGGACAAACGT
CCTGAAATCACTCTGGTGACCAATAAGCAGGTTCAGCAGCCAGTGATGGATCGCTACCAG
CAGCATGGGATGGCTCCGCTGACCCAGGAGCAGAAGCCGGTTGCTAAAGTCGTGAATGAC
AATGCGCCGCAAACTGCGAAAGAGCCGGATTATCTGGATATCCCAGCATTCCTGCGTAAG
CAAGCTGATTAA
Enzyme 22 GenBank Gene ID CP000948 Link Image
Enzyme 22 GeneCard ID fucO Link Image
Enzyme 22 GenAtlas ID Not Available
Enzyme 22 HGNC ID Not Available
Enzyme 22 Chromosome Location Not Available
Enzyme 22 Locus ECDH10B_2968
Enzyme 22 SNPs SNPJam Report Link Image
Enzyme 22 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 22 Metabolite References Not Available
Enzyme 23 [top]
Enzyme 23 ID 16806
Enzyme 23 Name Aldehyde dehydrogenase A, NAD-linked
Enzyme 23 Synonyms Not Available
Enzyme 23 Gene Name aldA
Enzyme 23 Protein Sequence >Aldehyde dehydrogenase A, NAD-linked 
MSVPVQHPMYIDGQFVTWRGDAWIDVVNPATEAVISRIPDGQAEDARKAIDAAERAQPEW
EALPAIERASWLRKISAGIRERASEISALIVEEGGKIQQLAEVEVAFTADYIDYMAEWAR
RYEGEIIQSDRPGENILLFKRALGVTTGILPWNFPFFLIARKMAPALLTGNTIVIKPSEF
TPNNAIAFAKIVDEIGLPRGVFNLVLGRGETVGQELAGNPKVAMVSMTGSVSAGEKIMAT
AAKNITKVCLELGGKAPAIVMDDADLELAVKAIVDSRVINSGQVCNCAERVYVQKGIYDQ
FVNRLGEAMQAVQFGNPAERNDIAMGPLINAAALERVEQKVARAVEEGARVAFGGKAVEG
KGYYYPPTLLLDVRQEMSIMHEETFGPVLPVVAFDTLEDAISMANDSDYGLTSSIYTQNL
NVAMKAIKGLKFGETYINRENFEAMQGFHAGWRKSGIGGADGKHGLHEYLQTQVVYLQS
Enzyme 23 Number of Residues 479
Enzyme 23 Molecular Weight 52272.4
Enzyme 23 Theoretical pI 4.79
Enzyme 23 GO Classification
Function
  • catalytic activity
  • oxidoreductase activity
Process
  • metabolic process
  • oxidation reduction
Component
—
Enzyme 23 General Function Involved in oxidoreductase activity
Enzyme 23 Specific Function Not Available
Enzyme 23 Pathways Not Available
Enzyme 23 Reactions Not Available
Enzyme 23 Pfam Domain Function
Enzyme 23 Signals
  • None
Enzyme 23 Transmembrane Regions
  • None
Enzyme 23 Essentiality Not Available
Enzyme 23 GenBank ID Protein 169888926 Link Image
Enzyme 23 UniProtKB/Swiss-Prot ID B1XDC8 Link Image
Enzyme 23 UniProtKB/Swiss-Prot Entry Name B1XDC8_ECODH Link Image
Enzyme 23 PDB ID Not Available
Enzyme 23 Cellular Location Not Available
Enzyme 23 Gene Sequence >1440 bp 
ATGTCAGTACCCGTTCAACATCCTATGTATATCGATGGACAGTTTGTTACCTGGCGTGGA
GACGCATGGATTGATGTGGTAAACCCTGCTACAGAGGCTGTCATTTCCCGCATACCCGAT
GGTCAGGCCGAGGATGCCCGTAAGGCAATCGATGCAGCAGAACGTGCACAACCAGAATGG
GAAGCGTTGCCTGCTATTGAACGCGCCAGTTGGTTGCGCAAAATCTCCGCCGGGATCCGC
GAACGCGCCAGTGAAATCAGTGCGCTGATTGTTGAAGAAGGGGGCAAGATCCAGCAGCTG
GCTGAAGTCGAAGTGGCTTTTACTGCCGACTATATCGATTACATGGCGGAGTGGGCACGG
CGTTACGAGGGCGAGATTATTCAAAGCGATCGTCCAGGAGAAAATATTCTTTTGTTTAAA
CGTGCGCTTGGTGTGACTACCGGCATTCTGCCGTGGAACTTCCCGTTCTTCCTCATTGCC
CGCAAAATGGCTCCCGCTCTTTTGACCGGTAATACCATCGTCATTAAACCTAGTGAATTT
ACGCCAAACAATGCGATTGCATTCGCCAAAATCGTCGATGAAATAGGCCTTCCGCGCGGC
GTGTTTAACCTTGTACTGGGGCGTGGTGAAACCGTTGGGCAAGAACTGGCGGGTAACCCA
AAGGTCGCAATGGTCAGTATGACAGGCAGCGTCTCTGCAGGTGAGAAGATCATGGCGACT
GCGGCGAAAAACATCACCAAAGTGTGTCTGGAATTGGGGGGTAAAGCACCAGCTATCGTA
ATGGACGATGCCGATCTTGAACTGGCAGTCAAAGCCATCGTTGATTCACGCGTCATTAAT
AGTGGGCAAGTGTGTAACTGTGCAGAACGTGTTTATGTACAGAAAGGCATTTATGATCAG
TTCGTCAATCGGCTGGGTGAAGCGATGCAGGCGGTTCAATTTGGTAACCCCGCTGAACGC
AACGACATTGCGATGGGGCCGTTGATTAACGCCGCGGCGCTGGAAAGGGTCGAGCAAAAA
GTGGCGCGCGCAGTAGAAGAAGGGGCGAGAGTGGCGTTCGGTGGCAAAGCGGTAGAGGGG
AAAGGATATTATTATCCGCCGACATTGCTGCTGGATGTTCGCCAGGAAATGTCGATTATG
CATGAGGAAACCTTTGGCCCGGTGCTGCCAGTTGTCGCATTTGACACGCTGGAAGATGCT
ATCTCAATGGCTAATGACAGTGATTACGGCCTGACCTCATCAATCTATACCCAAAATCTG
AACGTCGCGATGAAAGCCATTAAAGGGCTGAAGTTTGGTGAAACTTACATCAACCGTGAA
AACTTCGAAGCTATGCAAGGCTTCCACGCCGGATGGCGTAAATCCGGTATTGGCGGCGCA
GATGGTAAACATGGCTTGCATGAATATCTGCAGACCCAGGTGGTTTATTTACAGTCTTAA
Enzyme 23 GenBank Gene ID CP000948 Link Image
Enzyme 23 GeneCard ID aldA Link Image
Enzyme 23 GenAtlas ID Not Available
Enzyme 23 HGNC ID Not Available
Enzyme 23 Chromosome Location Not Available
Enzyme 23 Locus ECDH10B_1541
Enzyme 23 SNPs SNPJam Report Link Image
Enzyme 23 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 23 Metabolite References Not Available
Enzyme 24 [top]
Enzyme 24 ID 16807
Enzyme 24 Name Rhamnulose-1-phosphate aldolase
Enzyme 24 Synonyms Not Available
Enzyme 24 Gene Name rhaD
Enzyme 24 Protein Sequence >Rhamnulose-1-phosphate aldolase 
MQNITQSWFVQGMIKATTDAWLKGWDERNGGNLTLRLDDADIAPYHDNFHQQPRYIPLSQ
PMPLLANTPFIVTGSGKFFRNVQLDPAANLGIVKVDSDGAGYHILWGLTNEAVPTSELPA
HFLSHCERIKATNGKDRVIMHCHATNLIALTYVLENDTAVFTRQLWEGSTECLVVFPDGV
GILPWMVPGTDEIGQATAQEMQKHSLVLWPFHGVFGSGPTLDETFGLIDTAEKSAQVLVK
VYSMGGMKQTISREELIALGKRFGVTPLASALAL
Enzyme 24 Number of Residues 274
Enzyme 24 Molecular Weight 30145.3
Enzyme 24 Theoretical pI 5.79
Enzyme 24 GO Classification
Function
  • aldehyde-lyase activity
  • binding
  • carbon-carbon lyase activity
  • catalytic activity
  • cation binding
  • ion binding
  • lyase activity
  • metal ion binding
  • rhamnulose-1-phosphate aldolase activity
Process
—
Component
—
Enzyme 24 General Function Involved in metal ion binding
Enzyme 24 Specific Function Catalyzes the reversible cleavage of L-rhamnulose-1- phosphate to dihydroxyacetone phosphate (DHAP) and L-lactaldehyde
Enzyme 24 Pathways Not Available
Enzyme 24 Reactions
  • L-rhamnulose 1-phosphate = glycerone phosphate + (S)-lactaldehyde [RN:R02263]
Enzyme 24 Pfam Domain Function
Enzyme 24 Signals
  • None
Enzyme 24 Transmembrane Regions
  • None
Enzyme 24 Essentiality Not Available
Enzyme 24 GenBank ID Protein 169888592 Link Image
Enzyme 24 UniProtKB/Swiss-Prot ID B1XB69 Link Image
Enzyme 24 UniProtKB/Swiss-Prot Entry Name RHAD_ECODH Link Image
Enzyme 24 PDB ID 1GT7 Link Image
Enzyme 24 PDB File Show
Enzyme 24 3D Structure
Enzyme 24 Cellular Location Not Available
Enzyme 24 Gene Sequence >825 bp 
GTGCCGTTTCGCAGCAATAATCCCATCACGCGCGACGAATTGCTGTCGCGCTTTTTCCCG
CAGTATCATCCCGTCACGACGTTTAATAGTGGGCTTAGTGGCGGGAGTTTTCTCATTGAA
CATCAGGGCCAGCGTTTTGTTGTGCGTCAGCCGCACGATCCTGATGCGCCGCAGTCCGCG
TTCTTGCGCCAGTATCGGGCTTTATCACAACTACCCGCATGCATTGCACCGAAGCCGCAT
TTATATCTCCGTGACTGGATGGTAGTCGACTATCTGCCCGGCGCGGTAAAAACGTATTTG
CCGGATACCAACGAACTGGCAGGCTTGCTGTATTATCTACATCAACAACCACGTTTTGGC
TGGCGAATAACGCTGTTGCCGTTACTGGAACTGTACTGGCAGCAAAGCGATCCGGCGCGG
CGGACAGTGGGTTGGCTGCGAATGTTAAAACGTCTGCGCAAAGCGCGGGAACCACGGCCT
TTACGCTTAAGTCCATTGCATATGGATGTCCACGCCGGAAATTTAGTGCATAGCGCGTCA
GGGTTAAAACTCATCGACTGGGAGTATGCCGGAGATGGTGATATCGCGCTGGAACTGGCG
GCGGTGTGGGTGGAAAATACTGAACAGCACCGGCAATTGGTCAATGACTATGCCACTCGC
GCGAAGATTTATCCGGCGCAATTATGGCGTCAGGTCAGGCGATGGTTTCCCTGGCTGCTG
ATGCTCAAAGCAGGGTGGTTTGAGTACCGCTGGCGACAAACCGGCGATCAACAATTTATC
AGGCTGGCCGATGACACCTGGCGGCAGCTATTAATAAAACAATAA
Enzyme 24 GenBank Gene ID CP000948 Link Image
Enzyme 24 GeneCard ID rhaD Link Image
Enzyme 24 GenAtlas ID Not Available
Enzyme 24 HGNC ID Not Available
Enzyme 24 Chromosome Location Not Available
Enzyme 24 Locus ECDH10B_4092
Enzyme 24 SNPs SNPJam Report Link Image
Enzyme 24 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 24 Metabolite References Not Available
Enzyme 25 [top]
Enzyme 25 ID 16814
Enzyme 25 Name Bifunctional dihydroneopterin aldolase and dihydroneopterin triphosphate 2'-epimerase
Enzyme 25 Synonyms Not Available
Enzyme 25 Gene Name folB
Enzyme 25 Protein Sequence >Bifunctional dihydroneopterin aldolase and dihydroneopterin triphosphate 2'-epimerase 
MDIVFIEQLSVITTIGVYDWEQTIEQKLVFDIEMAWDNRKAAKSDDVADCLSYADIAETV
VSHVEGARFALVERVAEEVAELLLARFNSPWVRIKLSKPGAVARAANVGVIIERGNNLKE
NN
Enzyme 25 Number of Residues 122
Enzyme 25 Molecular Weight 13619.4
Enzyme 25 Theoretical pI 4.41
Enzyme 25 GO Classification
Function
  • aldehyde-lyase activity
  • carbon-carbon lyase activity
  • catalytic activity
  • dihydroneopterin aldolase activity
  • lyase activity
Process
  • cellular aromatic compound metabolic process
  • cellular metabolic process
  • folic acid and derivative metabolic process
  • metabolic process
Component
—
Enzyme 25 General Function Involved in dihydroneopterin aldolase activity
Enzyme 25 Specific Function Not Available
Enzyme 25 Pathways Not Available
Enzyme 25 Reactions Not Available
Enzyme 25 Pfam Domain Function
Enzyme 25 Signals
  • None
Enzyme 25 Transmembrane Regions
  • None
Enzyme 25 Essentiality Not Available
Enzyme 25 GenBank ID Protein 169887918 Link Image
Enzyme 25 UniProtKB/Swiss-Prot ID B1XG63 Link Image
Enzyme 25 UniProtKB/Swiss-Prot Entry Name B1XG63_ECODH Link Image
Enzyme 25 PDB ID Not Available
Enzyme 25 Cellular Location Not Available
Enzyme 25 Gene Sequence >369 bp 
ATGAAATATAGTTCAATATTTTCGATGCTTTCATTTTTTATACTATTTGCCTGTAATGAG
ACAGCTGTTTACGGTTCTGATGAAAACATTATTTTTATGAGGTATGTGGAAAAATTACAT
TTAGATAAATACTCTGTTAAAAATACGGTAAAAACTGAAACAATGGCGATACAATTAGCT
GAAATATATGTTAGGTATCGCTATGGCGAACGGATTGCAGAAGAAGAAAAACCATATTTA
ATTACGGAACTACCAGATAGTTGGGTTGTTGAGGGAGCAAAGTTACCTTATGAAGTTGCG
GGTGGTGTATTTATTATAGAAATTAATAAGAAAAATGGATGTGTTTTGAATTTCCTACAT
AGTAAATAA
Enzyme 25 GenBank Gene ID CP000948 Link Image
Enzyme 25 GeneCard ID folB Link Image
Enzyme 25 GenAtlas ID Not Available
Enzyme 25 HGNC ID Not Available
Enzyme 25 Chromosome Location Not Available
Enzyme 25 Locus ECDH10B_3233
Enzyme 25 SNPs SNPJam Report Link Image
Enzyme 25 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 25 Metabolite References Not Available