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Human Metabolome Database Version 2.5

 

Showing metabocard for Lactaldehyde (HMDB03052)

Legend: metabolite field enzyme field

Version 2.5
Creation Date 2006-05-22 16:12:29
Update Date 2009-05-05 20:59:37
Accession Number HMDB03052
Secondary Accession Numbers Not Available
Common Name Lactaldehyde
Description L-lactaldehyde is an intermediate metabolite in the pyruvate metabolism pathway. L-lactaldehyde is irreversibly produced from pyruvaldehyde via the enzyme aldehyde reductase (EC:1.1.1.21) which is then irreversibly converted to propylene glycol via aldehyde reductase (EC:1.1.1.21).
Synonyms
  1. (+-)-2-Hydroxypropanal
  2. 2-Hydroxypropanal
  3. 2-Hydroxypropionaldehyde
  4. Alpha-hydroxypropionaldehyde
  5. L-2-Hydroxypropionaldehyde
  6. lactaldehyde
  7. L-lactaldehyde
  8. Hydroxypropionaldehyde
  9. (S)-lactaldehyde
  10. (2S)-2-hydroxypropanal
Chemical IUPAC Name 2-hydroxypropanal
Chemical Formula C3H6O2
Chemical Structure Structure
Chemical Taxonomy
Kingdom
  • Organic
Super Class
  • Alcohols
Class
  • Alcohols and Polyols
  • Aldehydes
Sub Class
  • Simple alcohols
Family
  • Microbial Metabolite
Species
  • aldehyde
  • secondary alcohol
Biofunction
—
Application
—
Source
  • Endogenous
Average Molecular Weight 74.078
Monoisotopic Molecular Weight 74.036781
Isomeric SMILES C[C@H](O)C=O
Canonical SMILES CC(O)C=O
KEGG Compound ID C00424 Link Image
BioCyc ID LACTALD Link Image
BiGG ID 34941 Link Image
Wikipedia Link Lactaldehyde Link Image
NuGOwiki Link HMDB03052 Link Image
Metagene Link HMDB03052 Link Image
METLIN ID 3214 Link Image
PubChem Compound 439231 Link Image
PubChem Substance 3714 Link Image
ChEBI ID 18041 Link Image
CAS Registry Number 598-35-6
InChI Identifier InChI=1/C3H6O2/c1-3(5)2-4/h2-3,5H,1H3/t3-/m0/s1
Synthesis Reference Kranz, Cyrill. Synthesis of Lactic Aldehyde. Chemicke Listy pro Vedu a Prumysl (1912), 5 323-7.
Melting Point (Experimental) Not Available
Experimental Water Solubility Not Available Source: PhysProp
Predicted Water Solubility 658.0 mg/mL [Predicted by ALOGPS] Calculated using ALOGPS
Physiological Charge 0
State Solid
Experimental LogP/Hydrophobicity Not Available Source: PhysProp
Predicted LogP/Hydrophobicity -1.04 [Predicted by ALOGPS]; -0.2 [Predicted by PubChem via XLOGP] Calculated using ALOGPS
Material Safety Data Sheet (MSDS) Not Available
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 Not Available
Concentrations (Normal) Not Available
Concentrations (Abnormal) Not Available
Associated Disorders Not Available
OMIM ID Not Available
Pathways
Name SMPDB Link KEGG Link
Pyruvate Metabolism SMP00060 Link Image map00620 Link Image
General References
  1. Chen YM, Lin EC: Dual control of a common L-1,2-propanediol oxidoreductase by L-fucose and L-rhamnose in Escherichia coli. J Bacteriol. 1984 Mar;157(3):828-32. [PubMed Link Image]
  2. Casazza JP, Felver ME, Veech RL: The metabolism of acetone in rat. J Biol Chem. 1984 Jan 10;259(1):231-6. [PubMed Link Image]
  3. TING SM, SELLINGER OZ, MILLER ON: THE METABOLISM OF LACTALDEHYDE. VI. THE REDUCTION OF D- AND L-LACTALDEHYDE IN RAT LIVER. Biochim Biophys Acta. 1964 Aug 26;89:217-25. [PubMed Link Image]
  4. TING SM, MILLER ON, SELLINGER OZ: THE METABOLISM OF LACTALDEHYDE. VII. THE OXIDATION OF D-LACTALDEHYDE IN RAT LIVER. Biochim Biophys Acta. 1965 Mar 8;97:407-15. [PubMed Link Image]
  5. Akhy MT, Brown CM, Old DC: L-Rhamnose utilisation in Salmonella typhimurium. J Appl Bacteriol. 1984 Apr;56(2):269-74. [PubMed Link Image]
  6. Ros J, Aguilar J: Genetic and structural evidence for the presence of propanediol oxidoreductase isoenzymes in Escherichia coli. J Gen Microbiol. 1984 Mar;130(3):687-92. [PubMed Link Image]
  7. Di Costanzo L, Gomez GA, Christianson DW: Crystal structure of lactaldehyde dehydrogenase from Escherichia coli and inferences regarding substrate and cofactor specificity. J Mol Biol. 2007 Feb 16;366(2):481-93. Epub 2006 Nov 10. [PubMed Link Image]
  8. ENGLESBERG E: Physiological basis for rhamnose utilization by a mutant of Pasteurella pestis. I. Experiments with resting cells; the isolation of lactic aldehyde. J Bacteriol. 1957 Jul;74(1):8-11. [PubMed Link Image]
  9. Chen YM, Chakrabarti T, Lin EC: Constitutive activation of L-fucose genes by an unlinked mutation in Escherichia coli. J Bacteriol. 1984 Aug;159(2):725-9. [PubMed Link Image]
  10. SANDMAN RP, MILLER ON: Studies on the metabolism of lactaldehyde. I. Separation and determination of lactaldehyde and related 3-carbon compounds. J Biol Chem. 1958 Jan;230(1):353-9. [PubMed Link Image]
  11. 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. Aldehyde dehydrogenase B
  9. L-fuculose-phosphate aldolase
  10. L-fuculose phosphate aldolase
  11. L-fuculose phosphate aldolase
  12. Rhamnulose-1-phosphate aldolase
  13. Rhamnulose-1-phosphate aldolase
  14. Rhamnulose-1-phosphate aldolase
  15. 1,3-propanediol dehydrogenase
  16. L-1,2-propanediol oxidoreductase
  17. Aldehyde dehydrogenase A, NAD-linked
  18. Rhamnulose-1-phosphate aldolase
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 16158
Enzyme 8 Name Aldehyde dehydrogenase B
Enzyme 8 Synonyms Not Available
Enzyme 8 Gene Name aldB
Enzyme 8 Protein Sequence >Aldehyde dehydrogenase B 
MTNNPPSAQIKPGEYGFPLKLKARYDNFIGGEWVAPADGEYYQNLTPVTGQLLCEVASSG
KRDIDLALDAAHKVKDKWAHTSVQDRAAILFKIADRMEQNLELLATAETWDNGKPIRETS
AADVPLAIDHFRYFASCIRAQEGGISEVDSETVAYHFHEPLGVVGQIIPWNFPLLMASWK
MAPALAAGNCVVLKPARLTPLSVLLLMEIVGDLLPPGVVNVVNGAGGVIGEYLATSKRIA
KVAFTGSTEVGQQIMQYATQNIIPVTLELGGKSPNIFFADVMDEEDAFFDKALEGFALFA
FNQGEVCTCPSRALVQESIYERFMERAIRRVESIRSGNPLDSVTQMGAQVSHGQLETILN
YIDIGKKEGADVLTGGRRKLLEGELKDGYYLEPTILFGQNNMRVFQEEIFGPVLAVTTFK
TMEEALELANDTQYGLGAGVWSRNGNLAYKMGRGIQAGRVWTNCYHAYPAHAAFGGYKQS
GIGRETHKMMLEHYQQTKCLLVSYSDKPLGLF
Enzyme 8 Number of Residues 512
Enzyme 8 Molecular Weight 56305.9
Enzyme 8 Theoretical pI 5.36
Enzyme 8 GO Classification
Function
  • catalytic activity
  • oxidoreductase activity
Process
  • metabolic process
  • oxidation reduction
Component
—
Enzyme 8 General Function Involved in oxidoreductase activity
Enzyme 8 Specific Function Catalyzes the NADP-dependent oxidation of diverse aldehydes such as chloroacetaldehyde, acetaldehyde, propionaldehyde, benzaldehyde, mafosfamide, 4- hydroperoxycyclophosphamide. Its preferred substrates are acetaldehyde and chloroacetaldehyde
Enzyme 8 Pathways Not Available
Enzyme 8 Reactions Not Available
Enzyme 8 Pfam Domain Function
Enzyme 8 Signals
  • None
Enzyme 8 Transmembrane Regions
  • None
Enzyme 8 Essentiality Not Available
Enzyme 8 GenBank ID Protein 85674773 Link Image
Enzyme 8 UniProtKB/Swiss-Prot ID P37685 Link Image
Enzyme 8 UniProtKB/Swiss-Prot Entry Name ALDB_ECOLI Link Image
Enzyme 8 PDB ID Not Available
Enzyme 8 Cellular Location Not Available
Enzyme 8 Gene Sequence >1539 bp 
ATGGCAAGAGCTGTACACCGTAGTGGGTTAGTGGCGCTGGGCATTGCGACAGCGTTGATG
GCATCTTGTGCATTCGCTGCCAAAGATGTGGTGGTGGCGGTAGGATCGAATTTCACCACG
CTCGATCCGTATGACGCAAATGACACGTTATCTCAGGCCGTAGCGAAATCGTTTTACCAG
GGGCTGTTCGGTCTGGATAAAGAGATGAAACTGAAAAACGTGCTGGCGGAGAGTTATACC
GTTTCCGATGACGGCATTACTTACACCGTGAAATTGCGGGAAGGCATTAAATTCCAGGAT
GGCACCGATTTCAACGCCGCGGCGGTGAAAGCGAATCTGGACCGGGCCAGCGATCCGGCG
AATCATCTTAAACGCTATAACCTGTATAAGAATATTGCTAAAACGGAAGCGATCGATCCG
ACAACGGTAAAGATTACCCTCAAACAGCCGTTCTCAGCGTTTATTAATATTCTTGCCCAT
CCGGCGACCGCGATGATTTCACCGGCAGCGCTGGAAAAATATGGCAAGGAGATTGGTTTT
TATCCGGTGGGAACCGGACCGTATGAACTGGATACCTGGAATCAGACCGATTTTGTGAAG
GTGAAAAAATTCGCGGGTTACTGGCAGCCAGGATTGCCCAAACTGGACAGCATAACCTGG
CGTCCGGTGGCGGATAACAACACCCGCGCGGCAATGCTGCAAACCGGTGAAGCGCAGTTT
GCTTTCCCCATTCCTTACGAGCAGGCCACACTGCTGGAGAAAAACAAAAATATCGAGTTG
ATGGCCAGTCCGTCAATTATGCAGCGTTATATCAGTATGAACGTGACGCAAAAGCCGTTC
GATAACCCGAAGGTCCGTGAGGCGCTGAATTACGCCATTAACCGTCCGGCGCTGGTGAAA
GTTGCCTTTGCGGGCTATGCAACGCCAGCTACTGGTGTGGTACCGCCAAGTATCGCCTAC
GCGCAAAGTTATAAACCGTGGCCTTACGATCCAGTGAAAGCGCGCGAATTACTGAAAGAG
GCGGGATATCCCAACGGTTTCAGTACCACGCTGTGGTCGTCACATAACCACAGCACCGCG
CAGAAAGTGCTGCAATTTACCCAGCAGCAGTTAGCGCAGGTCGGGATTAAAGCCCAGGTG
ACTGCGATGGATGCCGGACAGCGGGCGGCAGAAGTTGAAGGTAAAGGGCAAAAAGAGAGC
GGCGTGCGGATGTTCTACACTGGCTGGTCGGCTTCAACCGGCGAAGCGGACTGGGCACTA
TCGCCGCTGTTTGCCTCGCAGAACTGGCCACCGACGCTGTTTAATACCGCGTTTTACAGC
AATAAACAGGTGGATGACTTCCTGGCTCAGGCACTGAAAACTAATGATCCGGCGGAAAAG
ACCCGCTTATATAAGGCGGCGCAGGATATCATCTGGCAAGAATCGCCGTGGATCCCGCTG
GTGGTAGAAAAACTGGTGTCGGCACACAGTAAAAACCTGACCGGTTTTTGGATCATGCCA
GACACCGGCTTCAGCTTTGAAGACGCGGATTTGCAATAA
Enzyme 8 GenBank Gene ID AP009048 Link Image
Enzyme 8 GeneCard ID aldB Link Image
Enzyme 8 GenAtlas ID Not Available
Enzyme 8 HGNC ID Not Available
Enzyme 8 Chromosome Location Not Available
Enzyme 8 Locus b3588
Enzyme 8 SNPs SNPJam Report Link Image
Enzyme 8 General References
  1. Xu J, Johnson RC: aldB, an RpoS-dependent gene in Escherichia coli encoding an aldehyde dehydrogenase that is repressed by Fis and activated by Crp. J Bacteriol. 1995 Jun;177(11):3166-75. [PubMed Link Image]
  2. Sofia HJ, Burland V, Daniels DL, Plunkett G 3rd, Blattner FR: Analysis of the Escherichia coli genome. V. DNA sequence of the region from 76.0 to 81.5 minutes. Nucleic Acids Res. 1994 Jul 11;22(13):2576-86. [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. Ho KK, Weiner H: Isolation and characterization of an aldehyde dehydrogenase encoded by the aldB gene of Escherichia coli. J Bacteriol. 2005 Feb;187(3):1067-73. [PubMed Link Image]
Enzyme 8 Metabolite References Not Available
Enzyme 9 [top]
Enzyme 9 ID 16159
Enzyme 9 Name L-fuculose-phosphate aldolase
Enzyme 9 Synonyms Not Available
Enzyme 9 Gene Name fucA
Enzyme 9 Protein Sequence >L-fuculose-phosphate aldolase 
MLMEKERKKLIEYGKKLVVEKLTKGTGGNLSVFDRNLGYIAITPSGIDFFEMKDRDIVIL
DLNGNVVEGENLPSSEWQMHLKLYKTREDIDAVIHAHTLYSTVLACLHEELPATHYMIAV
AGKNVRVANYATYGTEELAENAAKAMEERKAVLLANHGILAGSNDLLNAFNIIEEVEYCS
KIYCISKSIGEPFILPDDEMELMEKKFTSYGQRKSKEA
Enzyme 9 Number of Residues 218
Enzyme 9 Molecular Weight 24539.0
Enzyme 9 Theoretical pI 5.20
Enzyme 9 GO Classification
Function
  • binding
  • cation binding
  • ion binding
  • metal ion binding
Process
—
Component
—
Enzyme 9 General Function Involved in metal ion binding
Enzyme 9 Specific Function Not Available
Enzyme 9 Pathways Not Available
Enzyme 9 Reactions Not Available
Enzyme 9 Pfam Domain Function
Enzyme 9 Signals
  • None
Enzyme 9 Transmembrane Regions
  • None
Enzyme 9 Essentiality Not Available
Enzyme 9 GenBank ID Protein 18143860 Link Image
Enzyme 9 UniProtKB/Swiss-Prot ID Q8XNL4 Link Image
Enzyme 9 UniProtKB/Swiss-Prot Entry Name Q8XNL4_CLOPE Link Image
Enzyme 9 PDB ID Not Available
Enzyme 9 Cellular Location Not Available
Enzyme 9 Gene Sequence >657 bp 
ATGGCTAGAAAATCATCTAAAAAATATTTAAAAGAGGCAAATGCTCAAATAATATTATTT
GTTTTAATTATGATAATAATGAGAATGGTAGTTTTAAACTTTATGAGTGAAATATCAGGA
ATAGGATTTGATGAATTATCTAAGGCTAGAATTTATAATGGAGATATTACAGCAACATTA
TTTTTAGAGAGTCTTGTTAATTTTTTTGGTAACTTCATTTTAGAAACATACAAAGGAATA
ATTTTGCTTGCAATAATAAATGTATTTATTGCTTCTTATATATTAACTAAAAAAGACTTT
ACAGGTAATTCTTATTTTAATATGGTCATAGCATATCTATTTTCAGCCATAATAACAGTA
TTTTTATTATTAGCTGGTATAATTCTATTTTTTTGCATAATGCAATGCATGGTAGTTATA
AATTCATTAAAGATAGATGTGTCTTCAGAAATTTTATGGTTAGCCATATCTGTATTAGTA
GGAGTAGTCTTTATAAAGTATTTTAGGAAAAGTGTAGTTTTTTCTTTATTTGCATTTTTA
ATAATATCAGTTTATGCTTCTTACTACACTGATATAGGTAAAAAAGCAATTAACACAGAC
TATACTCAATATAGTCTAGAGGAGTTTGCTAATAATTTAAACTTAGTTGGAGAATAG
Enzyme 9 GenBank Gene ID BA000016 Link Image
Enzyme 9 GeneCard ID fucA Link Image
Enzyme 9 GenAtlas ID Not Available
Enzyme 9 HGNC ID Not Available
Enzyme 9 Chromosome Location Not Available
Enzyme 9 Locus CPE0319
Enzyme 9 SNPs SNPJam Report Link Image
Enzyme 9 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 9 Metabolite References Not Available
Enzyme 10 [top]
Enzyme 10 ID 16160
Enzyme 10 Name L-fuculose phosphate aldolase
Enzyme 10 Synonyms Not Available
Enzyme 10 Gene Name fucA
Enzyme 10 Protein Sequence >L-fuculose phosphate aldolase 
MENTNKLKYMEIREQICDVCHKMWQLGWVAANDGNVSVKLEDGTFLATPTGISKSFITPE
KLVHIDENGEVLDGPEGAKPSSEIKMHLRCYKEREDVGAVVHAHPPTATGFAVAHLALDR
YTMIETVIAIGSIPIAPYGTPSTYEVPDSIAPYLQEHDVILLENHGALTVGADLITAYYR
METLELYAKISLTAHLLGGEKEIERKNIDRLINMRKDYGVSGKHPGFKRYRTEE
Enzyme 10 Number of Residues 234
Enzyme 10 Molecular Weight 26123.6
Enzyme 10 Theoretical pI 5.78
Enzyme 10 GO Classification
Function
  • binding
  • cation binding
  • ion binding
  • metal ion binding
Process
—
Component
—
Enzyme 10 General Function Involved in metal ion binding
Enzyme 10 Specific Function Not Available
Enzyme 10 Pathways Not Available
Enzyme 10 Reactions
  • L-fuculose 1-phosphate = glycerone phosphate + (S)-lactaldehyde [RN:R02262]
Enzyme 10 Pfam Domain Function
Enzyme 10 Signals
  • None
Enzyme 10 Transmembrane Regions
  • None
Enzyme 10 Essentiality Not Available
Enzyme 10 GenBank ID Protein 110674594 Link Image
Enzyme 10 UniProtKB/Swiss-Prot ID Q0TS93 Link Image
Enzyme 10 UniProtKB/Swiss-Prot Entry Name Q0TS93_CLOP1 Link Image
Enzyme 10 PDB ID Not Available
Enzyme 10 Cellular Location Not Available
Enzyme 10 Gene Sequence >705 bp 
ATGGAAAAGTATAATGTTTTAGTTGTTGAAGACGAAAAGGAAATAGCAGAGGCTATTGAA
ATATATCTAAAAAATCAAGGATACAATGTATTTAAAGGAAGTAATGGCTTAGAAGGATTA
GAAATAGTTGAAAAAGAAGAGATTCATCTAGCTGTTGTTGACATAATGATGCCTAAAATG
GATGGAGCAACAATGGTAATGAAAATTAGAGAAAGTTATGACTTTCCTATAATAATGTTA
TCAGCAAAATCAGAAGATATGGATAAAATTTTAGGACTTAATATTGGAGCAGATGATTAT
GTAACAAAACCATTTAATCCACTAGAGCTTCTTGCAAGAGTTAATTCTCAATTAAGAAGA
TATTCTAAATACTTAAACATGGTAAAAAAGGATGAGAAGAAAACAAATTCTTATGCCATA
GGTGGATTAGAAGTTAATAGTGATAGAAAAGAAGTAATATTAGATGGAGATGTAGTAAAA
GTAACTCCTATAGAATTTAAAATACTTCAATTACTTATTAAGAGTCCAGGAAGAGTTTTT
TCAGCAGAGGAAATATATGAAAGAGTATGGAATGAAAATGCAGTAAACACAGACACTGTA
ATGGTCCATGTAAGAAATATAAGAGAAAAAATAGAGATAGATCCAAAAAATCCAAAATAT
TTAAAGGTGGTGTGGGGAGTTGGCTATAAAATCGAAAAGCAATAA
Enzyme 10 GenBank Gene ID CP000246 Link Image
Enzyme 10 GeneCard ID fucA Link Image
Enzyme 10 GenAtlas ID Not Available
Enzyme 10 HGNC ID Not Available
Enzyme 10 Chromosome Location Not Available
Enzyme 10 Locus CPF_1051
Enzyme 10 SNPs SNPJam Report Link Image
Enzyme 10 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 10 Metabolite References Not Available
Enzyme 11 [top]
Enzyme 11 ID 16161
Enzyme 11 Name L-fuculose phosphate aldolase
Enzyme 11 Synonyms
  1. L-fuculose-1-phosphate aldolase
Enzyme 11 Gene Name fucA
Enzyme 11 Protein Sequence >L-fuculose phosphate aldolase 
MERNKLARQIIDTCLEMTRLGLNQGTAGNVSVRYQDGMLITPTGIPYEKLTESHIVFIDG
NGKHEEGKLPSSEWRFHMAAYQSRPDANAVVHNHAVHCTAVSILNRSIPAIHYMIAAAGG
NSIPCAPYATFGTRELSEHVALALKNRKATLLQHHGLIACEVNLEKALWLAHEVEVLAQL
YLTTLAITDPVPVLSDEEIAVVLEKFKTYGLRIEE
Enzyme 11 Number of Residues 215
Enzyme 11 Molecular Weight 23775.1
Enzyme 11 Theoretical pI 6.58
Enzyme 11 GO Classification
Function
  • L-fuculose-phosphate aldolase activity
  • aldehyde-lyase activity
  • binding
  • carbon-carbon lyase activity
  • catalytic activity
  • cation binding
  • ion binding
  • lyase activity
  • metal ion binding
  • transition metal ion binding
  • zinc ion binding
Process
  • alcohol metabolic process
  • fucose metabolic process
  • hexose metabolic process
  • metabolic process
  • monosaccharide metabolic process
  • small molecule metabolic process
Component
—
Enzyme 11 General Function Involved in metal ion binding
Enzyme 11 Specific Function L-fuculose 1-phosphate = glycerone phosphate + (S)-lactaldehyde
Enzyme 11 Pathways Not Available
Enzyme 11 Reactions
  • L-fuculose 1-phosphate = glycerone phosphate + (S)-lactaldehyde [RN:R02262]
Enzyme 11 Pfam Domain Function
Enzyme 11 Signals
  • None
Enzyme 11 Transmembrane Regions
  • None
Enzyme 11 Essentiality Not Available
Enzyme 11 GenBank ID Protein 146042 Link Image
Enzyme 11 UniProtKB/Swiss-Prot ID P0AB87 Link Image
Enzyme 11 UniProtKB/Swiss-Prot Entry Name FUCA_ECOLI Link Image
Enzyme 11 PDB ID 4FUA Link Image
Enzyme 11 PDB File Show
Enzyme 11 3D Structure
Enzyme 11 Cellular Location Not Available
Enzyme 11 Gene Sequence >648 bp 
ATGGAACGAAATAAACTTGCTCGTCAGATTATTGACACTTGCCTGGAAATGACCCGCCTG
GGACTGAACCAGGGGACAGCGGGGAACGTCAGTGTACGTTATCAGGATGGGATGCTGATT
ACGCCTACAGGCATTCCATATGAAAAACTGACGGAGTCGCATATTGTCTTTATTGATGGC
AACGGTAAACATGAGGAAGGAAAGCTCCCCTCAAGCGAATGGCGTTTCCATATGGCAGCC
TATCAAAGCAGACCGGATGCCAACGCGGTTGTTCACAATCATGCCGTTCATTGCACGGCA
GTTTCCATTCTTAACCGATCGATCCCCGCTATTCACTACATGATTGCGGCGGCTGGCGGT
AATTCTATTCCTTGCGCGCCTTATGCGACCTTTGGAACACGCGAACTTTCTGAACATGTT
GCGCTGGCTCTCAAAAATCGTAAGGCAACTTTGTTACAACATCATGGGCTTATCGCTTGT
GAGGTGAATCTGGAAAAAGCGTTATGGCTGGCGCATGAAGTTGAAGTGCTGGCGCAACTT
TACCTGACGACCCTGGCGATTACGGACCCGGTGCCAGTGCTGAGCGATGAAGAGATTGCC
GTAGTGCTGGAGAAATTCAAAACCTATGGGTTACGAATTGAAGAGTAA
Enzyme 11 GenBank Gene ID M31059 Link Image
Enzyme 11 GeneCard ID fucA Link Image
Enzyme 11 GenAtlas ID Not Available
Enzyme 11 HGNC ID Not Available
Enzyme 11 Chromosome Location Not Available
Enzyme 11 Locus Not Available
Enzyme 11 SNPs SNPJam Report Link Image
Enzyme 11 General References
  1. 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]
  2. 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]
  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. 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]
  6. Dreyer MK, Schulz GE: The spatial structure of the class II L-fuculose-1-phosphate aldolase from Escherichia coli. J Mol Biol. 1993 Jun 5;231(3):549-53. [PubMed Link Image]
  7. Dreyer MK, Schulz GE: Catalytic mechanism of the metal-dependent fuculose aldolase from Escherichia coli as derived from the structure. J Mol Biol. 1996 Jun 14;259(3):458-66. [PubMed Link Image]
  8. Dreyer MK, Schulz GE: Refined high-resolution structure of the metal-ion dependent L-fuculose-1-phosphate aldolase (class II) from Escherichia coli. Acta Crystallogr D Biol Crystallogr. 1996 Nov 1;52(Pt 6):1082-91. [PubMed Link Image]
  9. Joerger AC, Gosse C, Fessner WD, Schulz GE: Catalytic action of fuculose 1-phosphate aldolase (class II) as derived from structure-directed mutagenesis. Biochemistry. 2000 May 23;39(20):6033-41. [PubMed Link Image]
  10. Joerger AC, Mueller-Dieckmann C, Schulz GE: Structures of l-fuculose-1-phosphate aldolase mutants outlining motions during catalysis. J Mol Biol. 2000 Nov 3;303(4):531-43. [PubMed Link Image]
Enzyme 11 Metabolite References Not Available
Enzyme 12 [top]
Enzyme 12 ID 16162
Enzyme 12 Name Rhamnulose-1-phosphate aldolase
Enzyme 12 Synonyms Not Available
Enzyme 12 Gene Name rhaD
Enzyme 12 Protein Sequence >Rhamnulose-1-phosphate aldolase 
MTDFIDSPYVRDMAQTTENLYRHGWDERNGGNVSLRLTKEEVEAYAGTDKVLRQIPIKFD
ASELAGKYYLVTGTGRYFKNMVEFPERDMGLIRISEVGNSVDLMWGFNDGGEPTSEFPSH
LMSHIARLKQDPDQRVIMHCHPTNLVAMTFTIPLSSKRFSRTLWKMHPESIVVFPEGVGV
IPYMCPGTNEIGEKTAAKMADYRVVVWPHHGVFAAGDSLDETYGLVETVEKSALIYTTIR
EQGGEVLQSLTDKDFRDLIKRFDLKANEDFLTPDAVGATVD
Enzyme 12 Number of Residues 281
Enzyme 12 Molecular Weight 31693.7
Enzyme 12 Theoretical pI 4.97
Enzyme 12 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 12 General Function Involved in metal ion binding
Enzyme 12 Specific Function Catalyzes the reversible cleavage of L-rhamnulose-1- phosphate to dihydroxyacetone phosphate (DHAP) and L-lactaldehyde
Enzyme 12 Pathways Not Available
Enzyme 12 Reactions
  • L-rhamnulose 1-phosphate = glycerone phosphate + (S)-lactaldehyde [RN:R02263]
Enzyme 12 Pfam Domain Function
Enzyme 12 Signals
  • None
Enzyme 12 Transmembrane Regions
  • None
Enzyme 12 Essentiality Not Available
Enzyme 12 GenBank ID Protein 28272740 Link Image
Enzyme 12 UniProtKB/Swiss-Prot ID Q88S52 Link Image
Enzyme 12 UniProtKB/Swiss-Prot Entry Name RHAD_LACPL Link Image
Enzyme 12 PDB ID Not Available
Enzyme 12 Cellular Location Not Available
Enzyme 12 Gene Sequence >846 bp 
ATGACAGACTTTATTGATTCACCATATGTACGTGATATGGCACAAACAACGGAAAATTTA
TATCGACATGGCTGGGACGAACGGAATGGCGGCAACGTGAGTCTACGACTGACTAAAGAG
GAAGTTGAAGCCTATGCTGGTACGGATAAAGTTTTACGTCAGATTCCAATTAAATTTGAT
GCCAGTGAATTAGCGGGCAAGTATTACTTAGTTACGGGAACTGGCCGGTACTTTAAGAAT
ATGGTCGAATTTCCAGAACGTGACATGGGCTTGATTCGAATCAGCGAAGTCGGCAACAGT
GTTGATTTAATGTGGGGCTTCAATGATGGTGGTGAACCAACTAGCGAATTTCCATCACAC
TTAATGAGCCACATTGCTCGGTTGAAGCAAGATCCTGATCAACGGGTTATCATGCATTGC
CACCCAACTAACTTGGTTGCAATGACCTTTACGATTCCGTTGTCATCTAAGCGGTTCAGT
CGGACGCTATGGAAGATGCATCCAGAATCAATCGTTGTCTTCCCAGAAGGCGTAGGCGTT
ATCCCATATATGTGCCCAGGAACTAATGAAATCGGTGAAAAGACGGCTGCTAAGATGGCC
GACTACCGGGTAGTTGTATGGCCACACCATGGCGTCTTCGCAGCTGGTGACTCTCTGGAT
GAAACTTACGGGTTAGTTGAAACAGTTGAAAAGTCAGCATTAATCTACACGACGATTCGT
GAACAAGGTGGAGAAGTCTTGCAATCGTTGACCGACAAAGATTTCCGTGACTTAATCAAG
CGTTTTGACTTGAAAGCCAATGAAGACTTCTTAACACCAGATGCAGTCGGAGCAACGGTT
GACTAA
Enzyme 12 GenBank Gene ID AL935262 Link Image
Enzyme 12 GeneCard ID rhaD Link Image
Enzyme 12 GenAtlas ID Not Available
Enzyme 12 HGNC ID Not Available
Enzyme 12 Chromosome Location Not Available
Enzyme 12 Locus lp_3592
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 16163
Enzyme 13 Name Rhamnulose-1-phosphate aldolase
Enzyme 13 Synonyms Not Available
Enzyme 13 Gene Name rhaD
Enzyme 13 Protein Sequence >Rhamnulose-1-phosphate aldolase 
MNVLQAPFVEEMVKTTKNLYRLGWDERNGGNISYLLKEEEILPFLNPTQVLRKIPMKFDA
TKLAGKYFIVTGSGKYFKNVCDASSENLGILRVSENGQELELLWGLEDEAVPTSELPSHF
MSHIARLAVDPENRIVMHNHASHLLAMSFTHELDEKVFTRTLWQMCTECLVVFPDGVGII
PWLVPGTNEIGVATAEKMKESRLVLWPQHGIYGTGRDMDEVFGLIETAEKAAEVYTYVCA
QGGVRQTISDADLWRLAEAFGVTPKVGYLEEKVSKRRKL
Enzyme 13 Number of Residues 279
Enzyme 13 Molecular Weight 31465.0
Enzyme 13 Theoretical pI 5.43
Enzyme 13 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 13 General Function Involved in metal ion binding
Enzyme 13 Specific Function Catalyzes the reversible cleavage of L-rhamnulose-1- phosphate to dihydroxyacetone phosphate (DHAP) and L-lactaldehyde
Enzyme 13 Pathways Not Available
Enzyme 13 Reactions
  • L-rhamnulose 1-phosphate = glycerone phosphate + (S)-lactaldehyde [RN:R02263]
Enzyme 13 Pfam Domain Function
Enzyme 13 Signals
  • None
Enzyme 13 Transmembrane Regions
  • None
Enzyme 13 Essentiality Not Available
Enzyme 13 GenBank ID Protein 29342173 Link Image
Enzyme 13 UniProtKB/Swiss-Prot ID Q838L1 Link Image
Enzyme 13 UniProtKB/Swiss-Prot Entry Name RHAD_ENTFA Link Image
Enzyme 13 PDB ID Not Available
Enzyme 13 Cellular Location Not Available
Enzyme 13 Gene Sequence >840 bp 
ATGGCAGAAATGCTTTCTTATGCATTTATGCAAAAGGCCTTTTTAGCAGCACTGTTTATC
TCAGTGATTGCCCCAATGCTCGGCGTCTTTCTAGTTATTCGCCGACAATCTTTAATGGCA
GATACCCTTTCACATGTGTCATTAGCCGGTGTGGCACTAGGCTTCTTTTTTAATTGGAAT
CCTAATTTAATGACCTTAATTGTCGTGATTGTGGCTGCAATCATTCTAGAATATTTACGA
ATGATTTATAGCACCTATTCAGAAATTTCGATTGCTATTTTAATGTCAGGCGGTTTGGCT
TTGGCGTTAGTTTTGATGAATTTAACAGGAGGCAATTCAGCTGCTAGTATTCAATCGTAT
TTATTTGGTTCCATCGTCACGATTACGTGGGATCAAGTGGTTATGTTGGCAATTTTATTC
GTAGTTTTAGTTCTATTGTTTATGTTATTTAAACGTCCAATGTATGTTTTAACATTTGAT
GAAGATACTGCTCATGTTGATGGGCTACCTATTCATTGGATGTCGATGCTTTTTAATGTA
ATTACTGGTGTGGCGATTGCTGTGATGATTCCGATCGCGGGAGCCTTGTTAATTTCAGCA
ATTATGGTCTTACCAGCTGCAATAGGTATGCGAATTGGTAAAGGCTTTAACACGGTGATT
ATTATCAGTGTGTTTATGGGCTTGATTGGCATGCTAACAGGGTTGACTAGCTCGTATTAT
TTGGAAACACCACCGAGTGCAAGTATTACCCTAATTTTTATTGGTTTATTCTTATTAGTC
AATATTTATCGCCGAGTGGTTGTCATGGTCCAACGAAAACAAAAAATGCAAAGAAACTAA
Enzyme 13 GenBank Gene ID AE016830 Link Image
Enzyme 13 GeneCard ID rhaD Link Image
Enzyme 13 GenAtlas ID Not Available
Enzyme 13 HGNC ID Not Available
Enzyme 13 Chromosome Location Not Available
Enzyme 13 Locus EF_0435
Enzyme 13 SNPs SNPJam Report Link Image
Enzyme 13 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 13 Metabolite References Not Available
Enzyme 14 [top]
Enzyme 14 ID 16164
Enzyme 14 Name Rhamnulose-1-phosphate aldolase
Enzyme 14 Synonyms Not Available
Enzyme 14 Gene Name rhaD
Enzyme 14 Protein Sequence >Rhamnulose-1-phosphate aldolase 
MQNITQSWFVQGMIKATTDAWLKGWDERNGGNLTLRLDDADIAPYHDNFHQQPRYIPLSQ
PMPLLANTPFIVTGSGKFFRNVQLDPAANLGIVKVDSDGAGYHILWGLTNEAVPTSELPA
HFLSHCERIKATNGKDRVIMHCHATNLIALTYVLENDTAVFTRQLWEGSTECLVVFPDGV
GILPWMVPGTDEIGQATAQEMQKHSLVLWPFHGVFGSGPTLDETFGLIDTAEKSAQVLVK
VYSMGGMKQTISREELIALGKRFGVTPLASALAL
Enzyme 14 Number of Residues 274
Enzyme 14 Molecular Weight 30145.3
Enzyme 14 Theoretical pI 5.79
Enzyme 14 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 14 General Function Involved in metal ion binding
Enzyme 14 Specific Function Catalyzes the reversible cleavage of L-rhamnulose-1- phosphate to dihydroxyacetone phosphate (DHAP) and L-lactaldehyde
Enzyme 14 Pathways Not Available
Enzyme 14 Reactions
  • L-rhamnulose 1-phosphate = glycerone phosphate + (S)-lactaldehyde [RN:R02263]
Enzyme 14 Pfam Domain Function
Enzyme 14 Signals
  • None
Enzyme 14 Transmembrane Regions
  • None
Enzyme 14 Essentiality Not Available
Enzyme 14 GenBank ID Protein 396681 Link Image
Enzyme 14 UniProtKB/Swiss-Prot ID P32169 Link Image
Enzyme 14 UniProtKB/Swiss-Prot Entry Name RHAD_ECOLI Link Image
Enzyme 14 PDB ID 1GT7 Link Image
Enzyme 14 PDB File Show
Enzyme 14 3D Structure
Enzyme 14 Cellular Location Not Available
Enzyme 14 Gene Sequence >825 bp 
ATGCAAAACATTACTCAGTCCTGGTTTGTCCAGGGAATGATCAAAGCCACCACCGACGCC
TGGCTGAAAGGCTGGGATGAGCGCAACGGCGGCAACCTGACGCTACGCCTGGATGACGCC
GATATCGCACCATATCACGACAATTTCCACCAACAACCGCGCTATATCCCGCTCAGCCAG
CCCATGCCTTTACTGGCAAATACACCGTTTATTGTCACCGGCTCGGGCAAATTCTTCCGT
AACGTCCAGCTTGATCCTGCGGCTAACTTAGGCATCGTAAAAGTCGACAGCGACGGCGCG
GGCTACCACATTCTTTGGGGGTTAACCAACGAAGCCGTCCCCACTTCCGAACTTCCGGCT
CACTTCCTTTCCCACTGCGAGCGCATTAAAGCCACCAACGGCAAAGATCGGGTGATCATG
CACTGCCACGCCACCAACCTGATCGCCCTCACCTATGTACTTGAAAACGACACCGCGGTC
TTCACTCGCCAACTGTGGGAAGGCAGCACCGAGTGTCTGGTGGTATTCCCGGATGGCGTT
GGCATTTTGCCGTGGATGGTGCCCGGCACGGACGAAATCGGCCAGGCGACCGCACAAGAG
ATGCAAAAACATTCGCTGGTGTTGTGGCCCTTCCACGGCGTCTTCGGCAGCGGACCGACG
CTGGATGAAACCTTCGGTTTAATCGACACCGCAGAAAAATCAGCACAAGTATTAGTGAAG
GTTTATTCGATGGGCGGCATGAAACAGACCATCAGCCGTGAAGAGTTGATAGCGCTCGGC
AAGCGTTTCGGCGTTACGCCACTCGCCAGTGCGCTGGCGCTGTAA
Enzyme 14 GenBank Gene ID X60472 Link Image
Enzyme 14 GeneCard ID rhaD Link Image
Enzyme 14 GenAtlas ID Not Available
Enzyme 14 HGNC ID Not Available
Enzyme 14 Chromosome Location Not Available
Enzyme 14 Locus Not Available
Enzyme 14 SNPs SNPJam Report Link Image
Enzyme 14 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 14 Metabolite References Not Available
Enzyme 15 [top]
Enzyme 15 ID 16804
Enzyme 15 Name 1,3-propanediol dehydrogenase
Enzyme 15 Synonyms Not Available
Enzyme 15 Gene Name dhaT
Enzyme 15 Protein Sequence >1,3-propanediol dehydrogenase 
MVYRMIFNQTAYFGRGAIKEIPAVAKQHGFTKAFIVTDPVLLETGTAEKVTKVLDEAGLP
YEVFSNVKPNPPVECIKDGVAKFADSGADFLIGLGGGSPQDTCKGIGIITANPEFADVLS
LEGVADTKNPSVPIFGVPTTAGTASETTINYVVTDTANKRKFVAVDPHDIPIVAFVDPDL
TDSMPRGLKVATGLDALTHAIEGYITPGAWSLSDCLSMQTIRMIAKNLAKSADGDIPAGE
QMAYASYITGMAYSNVGLGLVHGMAHPLGGRLGVAHGVANGILLAPVMEYNKDFTGEKYR
DIADAFGVEDAYTGDLEKVREEAVQAVHKLTVDLKNPTTISEVGATEADLEPLAHDAFND
VCTPGNPRQATEEDILAIYKSLM
Enzyme 15 Number of Residues 383
Enzyme 15 Molecular Weight 40608.8
Enzyme 15 Theoretical pI 4.50
Enzyme 15 GO Classification
Function
  • binding
  • catalytic activity
  • cation binding
  • ion binding
  • metal ion binding
  • oxidoreductase activity
Process
  • metabolic process
  • oxidation reduction
Component
—
Enzyme 15 General Function Involved in oxidoreductase activity
Enzyme 15 Specific Function Not Available
Enzyme 15 Pathways Not Available
Enzyme 15 Reactions Not Available
Enzyme 15 Pfam Domain Function
Enzyme 15 Signals
  • None
Enzyme 15 Transmembrane Regions
  • None
Enzyme 15 Essentiality Not Available
Enzyme 15 GenBank ID Protein 189428274 Link Image
Enzyme 15 UniProtKB/Swiss-Prot ID B3DR01 Link Image
Enzyme 15 UniProtKB/Swiss-Prot Entry Name B3DR01_BIFLD Link Image
Enzyme 15 PDB ID Not Available
Enzyme 15 Cellular Location Not Available
Enzyme 15 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 15 GenBank Gene ID CP000605 Link Image
Enzyme 15 GeneCard ID dhaT Link Image
Enzyme 15 GenAtlas ID Not Available
Enzyme 15 HGNC ID Not Available
Enzyme 15 Chromosome Location Not Available
Enzyme 15 Locus BLD_1839
Enzyme 15 SNPs SNPJam Report Link Image
Enzyme 15 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 15 Metabolite References Not Available
Enzyme 16 [top]
Enzyme 16 ID 16805
Enzyme 16 Name L-1,2-propanediol oxidoreductase
Enzyme 16 Synonyms Not Available
Enzyme 16 Gene Name fucO
Enzyme 16 Protein Sequence >L-1,2-propanediol oxidoreductase 
MMANRMILNETAWFGRGAVGALTDEVKRRGYQKALIVTDKTLVQCGVVAKVTDKMDAAGL
AWAIYDGVVPNPTITVVKEGLGVFQNSGADYLIAIGGGSPQDTCKAIGIISNNPEFADVR
SLEGLSPTNKPSVPILAIPTTAGTAAEVTINYVITDEEKRRKFVCVDPHDIPQVAFIDAD
MMDGMPPALKAATGVDALTHAIEGYITRGAWALTDALHIKAIEIIAGALRGSVAGDKDAG
EEMALGQYVAGMGFSNVGLGLVHGMAHPLGAFYNTPHGVANAILLPHVMRYNADFTGEKY
RDIARVMGVKVEGMSLEEARNAAVEAVFALNRDVGIPPHLRDVGVRKEDIPALAQAALDD
VCTGGNPREATLEDIVELYHTAW
Enzyme 16 Number of Residues 383
Enzyme 16 Molecular Weight 40644.2
Enzyme 16 Theoretical pI 4.91
Enzyme 16 GO Classification
Function
  • binding
  • catalytic activity
  • cation binding
  • ion binding
  • metal ion binding
  • oxidoreductase activity
Process
  • metabolic process
  • oxidation reduction
Component
—
Enzyme 16 General Function Involved in oxidoreductase 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 169887569 Link Image
Enzyme 16 UniProtKB/Swiss-Prot ID B1XDK8 Link Image
Enzyme 16 UniProtKB/Swiss-Prot Entry Name B1XDK8_ECODH Link Image
Enzyme 16 PDB ID 1RRM Link Image
Enzyme 16 PDB File Show
Enzyme 16 3D Structure
Enzyme 16 Cellular Location Not Available
Enzyme 16 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 16 GenBank Gene ID CP000948 Link Image
Enzyme 16 GeneCard ID fucO Link Image
Enzyme 16 GenAtlas ID Not Available
Enzyme 16 HGNC ID Not Available
Enzyme 16 Chromosome Location Not Available
Enzyme 16 Locus ECDH10B_2968
Enzyme 16 SNPs SNPJam Report Link Image
Enzyme 16 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 16 Metabolite References Not Available
Enzyme 17 [top]
Enzyme 17 ID 16806
Enzyme 17 Name Aldehyde dehydrogenase A, NAD-linked
Enzyme 17 Synonyms Not Available
Enzyme 17 Gene Name aldA
Enzyme 17 Protein Sequence >Aldehyde dehydrogenase A, NAD-linked 
MSVPVQHPMYIDGQFVTWRGDAWIDVVNPATEAVISRIPDGQAEDARKAIDAAERAQPEW
EALPAIERASWLRKISAGIRERASEISALIVEEGGKIQQLAEVEVAFTADYIDYMAEWAR
RYEGEIIQSDRPGENILLFKRALGVTTGILPWNFPFFLIARKMAPALLTGNTIVIKPSEF
TPNNAIAFAKIVDEIGLPRGVFNLVLGRGETVGQELAGNPKVAMVSMTGSVSAGEKIMAT
AAKNITKVCLELGGKAPAIVMDDADLELAVKAIVDSRVINSGQVCNCAERVYVQKGIYDQ
FVNRLGEAMQAVQFGNPAERNDIAMGPLINAAALERVEQKVARAVEEGARVAFGGKAVEG
KGYYYPPTLLLDVRQEMSIMHEETFGPVLPVVAFDTLEDAISMANDSDYGLTSSIYTQNL
NVAMKAIKGLKFGETYINRENFEAMQGFHAGWRKSGIGGADGKHGLHEYLQTQVVYLQS
Enzyme 17 Number of Residues 479
Enzyme 17 Molecular Weight 52272.4
Enzyme 17 Theoretical pI 4.79
Enzyme 17 GO Classification
Function
  • catalytic activity
  • oxidoreductase activity
Process
  • metabolic process
  • oxidation reduction
Component
—
Enzyme 17 General Function Involved in oxidoreductase activity
Enzyme 17 Specific Function Not Available
Enzyme 17 Pathways Not Available
Enzyme 17 Reactions Not Available
Enzyme 17 Pfam Domain Function
Enzyme 17 Signals
  • None
Enzyme 17 Transmembrane Regions
  • None
Enzyme 17 Essentiality Not Available
Enzyme 17 GenBank ID Protein 169888926 Link Image
Enzyme 17 UniProtKB/Swiss-Prot ID B1XDC8 Link Image
Enzyme 17 UniProtKB/Swiss-Prot Entry Name B1XDC8_ECODH Link Image
Enzyme 17 PDB ID Not Available
Enzyme 17 Cellular Location Not Available
Enzyme 17 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 17 GenBank Gene ID CP000948 Link Image
Enzyme 17 GeneCard ID aldA Link Image
Enzyme 17 GenAtlas ID Not Available
Enzyme 17 HGNC ID Not Available
Enzyme 17 Chromosome Location Not Available
Enzyme 17 Locus ECDH10B_1541
Enzyme 17 SNPs SNPJam Report Link Image
Enzyme 17 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 17 Metabolite References Not Available
Enzyme 18 [top]
Enzyme 18 ID 16807
Enzyme 18 Name Rhamnulose-1-phosphate aldolase
Enzyme 18 Synonyms Not Available
Enzyme 18 Gene Name rhaD
Enzyme 18 Protein Sequence >Rhamnulose-1-phosphate aldolase 
MQNITQSWFVQGMIKATTDAWLKGWDERNGGNLTLRLDDADIAPYHDNFHQQPRYIPLSQ
PMPLLANTPFIVTGSGKFFRNVQLDPAANLGIVKVDSDGAGYHILWGLTNEAVPTSELPA
HFLSHCERIKATNGKDRVIMHCHATNLIALTYVLENDTAVFTRQLWEGSTECLVVFPDGV
GILPWMVPGTDEIGQATAQEMQKHSLVLWPFHGVFGSGPTLDETFGLIDTAEKSAQVLVK
VYSMGGMKQTISREELIALGKRFGVTPLASALAL
Enzyme 18 Number of Residues 274
Enzyme 18 Molecular Weight 30145.3
Enzyme 18 Theoretical pI 5.79
Enzyme 18 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 18 General Function Involved in metal ion binding
Enzyme 18 Specific Function Catalyzes the reversible cleavage of L-rhamnulose-1- phosphate to dihydroxyacetone phosphate (DHAP) and L-lactaldehyde
Enzyme 18 Pathways Not Available
Enzyme 18 Reactions
  • L-rhamnulose 1-phosphate = glycerone phosphate + (S)-lactaldehyde [RN:R02263]
Enzyme 18 Pfam Domain Function
Enzyme 18 Signals
  • None
Enzyme 18 Transmembrane Regions
  • None
Enzyme 18 Essentiality Not Available
Enzyme 18 GenBank ID Protein 169888592 Link Image
Enzyme 18 UniProtKB/Swiss-Prot ID B1XB69 Link Image
Enzyme 18 UniProtKB/Swiss-Prot Entry Name RHAD_ECODH Link Image
Enzyme 18 PDB ID 1GT7 Link Image
Enzyme 18 PDB File Show
Enzyme 18 3D Structure
Enzyme 18 Cellular Location Not Available
Enzyme 18 Gene Sequence >825 bp 
GTGCCGTTTCGCAGCAATAATCCCATCACGCGCGACGAATTGCTGTCGCGCTTTTTCCCG
CAGTATCATCCCGTCACGACGTTTAATAGTGGGCTTAGTGGCGGGAGTTTTCTCATTGAA
CATCAGGGCCAGCGTTTTGTTGTGCGTCAGCCGCACGATCCTGATGCGCCGCAGTCCGCG
TTCTTGCGCCAGTATCGGGCTTTATCACAACTACCCGCATGCATTGCACCGAAGCCGCAT
TTATATCTCCGTGACTGGATGGTAGTCGACTATCTGCCCGGCGCGGTAAAAACGTATTTG
CCGGATACCAACGAACTGGCAGGCTTGCTGTATTATCTACATCAACAACCACGTTTTGGC
TGGCGAATAACGCTGTTGCCGTTACTGGAACTGTACTGGCAGCAAAGCGATCCGGCGCGG
CGGACAGTGGGTTGGCTGCGAATGTTAAAACGTCTGCGCAAAGCGCGGGAACCACGGCCT
TTACGCTTAAGTCCATTGCATATGGATGTCCACGCCGGAAATTTAGTGCATAGCGCGTCA
GGGTTAAAACTCATCGACTGGGAGTATGCCGGAGATGGTGATATCGCGCTGGAACTGGCG
GCGGTGTGGGTGGAAAATACTGAACAGCACCGGCAATTGGTCAATGACTATGCCACTCGC
GCGAAGATTTATCCGGCGCAATTATGGCGTCAGGTCAGGCGATGGTTTCCCTGGCTGCTG
ATGCTCAAAGCAGGGTGGTTTGAGTACCGCTGGCGACAAACCGGCGATCAACAATTTATC
AGGCTGGCCGATGACACCTGGCGGCAGCTATTAATAAAACAATAA
Enzyme 18 GenBank Gene ID CP000948 Link Image
Enzyme 18 GeneCard ID rhaD Link Image
Enzyme 18 GenAtlas ID Not Available
Enzyme 18 HGNC ID Not Available
Enzyme 18 Chromosome Location Not Available
Enzyme 18 Locus ECDH10B_4092
Enzyme 18 SNPs SNPJam Report Link Image
Enzyme 18 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 18 Metabolite References Not Available