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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
SDF File Show
PDB File Show
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 (EC 1.1.1.77)
  3. Lactaldehyde reductase
  4. Lactaldehyde reductase (EC 1.1.1.77)
  5. Lactaldehyde reductase (EC 1.1.1.1)
  6. Lactaldehyde reductase
  7. Lactaldehyde dehydrogenase
  8. Aldehyde dehydrogenase B
  9. L-fuculose-phosphate aldolase
  10. L-fuculose phosphate aldolase (EC 4.1.2.17)
  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 40624
Enzyme 1 Theoretical pI 4.50
Enzyme 1 GO Classification
Function
  • binding
  • catalytic activity
  • cation binding
  • ion binding
  • iron ion binding
  • oxidoreductase activity
  • transition metal ion binding
Process
  • metabolism
  • physiological process
Component
—
Enzyme 1 General Function Energy production and conversion
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 Not Available
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 Not Available
Enzyme 1 GenBank Gene ID AE014295 Link Image
Enzyme 1 GeneCard ID Not Available
Enzyme 1 GenAtlas ID Not Available
Enzyme 1 HGNC ID Not Available
Enzyme 1 Chromosome Location Not Available
Enzyme 1 Locus Not Available
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 (EC 1.1.1.77)
Enzyme 2 Synonyms Not Available
Enzyme 2 Gene Name fucO
Enzyme 2 Protein Sequence >Putative lactaldehyde reductase (EC 1.1.1.77) 
MINRFILNEVSYFGPGAREVLPKEISRLGLHKAFVATDKDLIKFGVADKVLKVLEAAKIP
YEIFSEIKPNPTVSNVKAGVEAFASSGADFILAIGGGSSMDTAKAIGIITNNPEFSDVVS
LEGVADTKKKSVPIIALPTTAGTAAEVTINYVITDEKNQKKMVCVDPNDIPSIAIVDAEL
MYTLPKSLTAATGLDALTHAIEGLITKGAWEMSDMFEIKAIEMINRYLVTAVEEPSNAEA
RNGMAVAQYIAGMAFSNVGLGVVHGMAHPLGAIFDIPHGVANALLLPIIMEFNAPAALDK
YVEIAKAMNVYSTDMTKEKAAEAAVEAVKTLSLRVNIPQHLSDLGIQESDLDRLATAAFA
DVCTPGNPREVTKEIILDLYKKAL
Enzyme 2 Number of Residues 384
Enzyme 2 Molecular Weight 41018
Enzyme 2 Theoretical pI 4.78
Enzyme 2 GO Classification
Function
  • binding
  • catalytic activity
  • cation binding
  • ion binding
  • iron ion binding
  • oxidoreductase activity
  • transition metal ion binding
Process
  • metabolism
  • physiological process
Component
—
Enzyme 2 General Function Energy production and conversion
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] ALL_REAC R02258 R03080
  • (other) R01781 R02257
Enzyme 2 Pfam Domain Function
Enzyme 2 Signals
  • None
Enzyme 2 Transmembrane Regions
  • None
Enzyme 2 Essentiality Not Available
Enzyme 2 GenBank ID Protein Not Available
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 Not Available
Enzyme 2 GenBank Gene ID CR626927 Link Image
Enzyme 2 GeneCard ID Not Available
Enzyme 2 GenAtlas ID Not Available
Enzyme 2 HGNC ID Not Available
Enzyme 2 Chromosome Location Not Available
Enzyme 2 Locus Not Available
Enzyme 2 SNPs SNPJam Report Link Image
Enzyme 2 General References Not Available
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 41004
Enzyme 3 Theoretical pI 4.72
Enzyme 3 GO Classification
Function
  • binding
  • catalytic activity
  • cation binding
  • ion binding
  • iron ion binding
  • oxidoreductase activity
  • transition metal ion binding
Process
  • metabolism
  • physiological process
Component
—
Enzyme 3 General Function Energy production and conversion
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 Not Available
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 Not Available
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 Not Available
Enzyme 3 SNPs Not Available
Enzyme 3 General References Not Available
Enzyme 3 Metabolite References Not Available
Enzyme 4 [top]
Enzyme 4 ID 16154
Enzyme 4 Name Lactaldehyde reductase (EC 1.1.1.77)
Enzyme 4 Synonyms Not Available
Enzyme 4 Gene Name fucO
Enzyme 4 Protein Sequence >Lactaldehyde reductase (EC 1.1.1.77) 
MVNRIVLNETSYHGAGAIKEIVTEVKGRGFKKAFLCSDPDLVKFGVTGKVTSILDEANLS
YELYTNIKANPTIENVKSGVEAYKKSGADYIIAVGGGSSMDTAKAIGIIINNKEFEDVVS
LEGVAPTKNKSVPIIAVPTTAGTAAEVTINYVITDVEKNRKFVCVDTHDIPVVAIIDPEM
MQSMPKGLTAATGMDALTHAIEGYITGAAWEMTDMFHLKAIELISKHLRGAVENTPEGRE
GMALGQYIAGMGFSNVGLGIVHSMAHSLGAVYDTPHGVANAIILPTVMEYNAEETGDKYK
YIAAAMGVENTENMTVEEYRKAAVDAVKKLSEDVGIPANLKDIVKKEDIRFLAESAYNDA
CRPGNPKETSVEDIITLYESLM
Enzyme 4 Number of Residues 382
Enzyme 4 Molecular Weight 41078
Enzyme 4 Theoretical pI 4.77
Enzyme 4 GO Classification
Function
  • binding
  • catalytic activity
  • cation binding
  • ion binding
  • iron ion binding
  • oxidoreductase activity
  • transition metal ion binding
Process
  • metabolism
  • physiological process
Component
—
Enzyme 4 General Function Energy production and conversion
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] ALL_REAC R02258 R03080
  • (other) R01781 R02257
Enzyme 4 Pfam Domain Function
Enzyme 4 Signals
  • None
Enzyme 4 Transmembrane Regions
  • None
Enzyme 4 Essentiality Not Available
Enzyme 4 GenBank ID Protein Not Available
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 Not Available
Enzyme 4 GenBank Gene ID CP000246 Link Image
Enzyme 4 GeneCard ID Not Available
Enzyme 4 GenAtlas ID Not Available
Enzyme 4 HGNC ID Not Available
Enzyme 4 Chromosome Location Not Available
Enzyme 4 Locus Not Available
Enzyme 4 SNPs SNPJam Report Link Image
Enzyme 4 General References Not Available
Enzyme 4 Metabolite References Not Available
Enzyme 5 [top]
Enzyme 5 ID 16155
Enzyme 5 Name Lactaldehyde reductase (EC 1.1.1.1)
Enzyme 5 Synonyms Not Available
Enzyme 5 Gene Name Not Available
Enzyme 5 Protein Sequence >Lactaldehyde reductase (EC 1.1.1.1) 
MVNRIVLNETSYHGAGAIKEIVTEVKGRGFKKAFLCSDPDLVKFGVTGKVTSILDEANLS
YELYTNIKANPTIENVKSGVEAYKKSGADYIIAVGGGSSMDTAKAIGIIINNKEFEDVVS
LEGVAPTKNKSVPIIAIPTTAGTAAEVTINYVITDVEKNRKFVCVDTHDIPVVAIIDPEM
MQSMPKGLTAATGMDALTHAIEGYITGAAWEMTDMFHLKAIELISKHLRGAVENTPEGRE
KMALGQYIAGMGFSNVGLGIVHSMAHSLGAVYDTPHGVANAIILPTVMEYNAEETGDKYK
YIAAAMGVENTENMTVEEYRKAAVDAVKKLSEDVGIPANLKDIVKKEDIRFLAESAYNDA
CRPGNPKETSVEDIIALYESLM
Enzyme 5 Number of Residues 382
Enzyme 5 Molecular Weight 41134
Enzyme 5 Theoretical pI 4.83
Enzyme 5 GO Classification
Function
  • binding
  • catalytic activity
  • cation binding
  • ion binding
  • iron ion binding
  • oxidoreductase activity
  • transition metal ion binding
Process
  • metabolism
  • physiological process
Component
—
Enzyme 5 General Function Energy production and conversion
Enzyme 5 Specific Function Not Available
Enzyme 5 Pathways Not Available
Enzyme 5 Reactions
  • an alcohol + NAD+ = an aldehyde or ketone + NADH + H+ [RN:R07326 R07327] ALL_REAC R07326 > R00623 R00754 R01036 R04805 R04880 R06917 R06927
  • R07327 > R00624
  • (other) R01041 R05233 R05234 R07105
Enzyme 5 Pfam Domain Function
Enzyme 5 Signals
  • None
Enzyme 5 Transmembrane Regions
  • None
Enzyme 5 Essentiality Not Available
Enzyme 5 GenBank ID Protein Not Available
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 Not Available
Enzyme 5 GenBank Gene ID CP000312 Link Image
Enzyme 5 GeneCard ID Not Available
Enzyme 5 GenAtlas ID Not Available
Enzyme 5 HGNC ID Not Available
Enzyme 5 Chromosome Location Not Available
Enzyme 5 Locus Not Available
Enzyme 5 SNPs Not Available
Enzyme 5 General References Not Available
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 40645
Enzyme 6 Theoretical pI 4.91
Enzyme 6 GO Classification
Function
  • binding
  • catalytic activity
  • cation binding
  • ion binding
  • iron ion binding
  • oxidoreductase activity
  • transition metal ion binding
Process
  • metabolism
  • physiological process
Component
—
Enzyme 6 General Function Energy production and conversion
Enzyme 6 Specific Function (R)-propane-1,2-diol + NAD(+) = (R)- lactaldehyde + NADH
Enzyme 6 Pathways Not Available
Enzyme 6 Reactions Not Available
Enzyme 6 Pfam Domain Function
Enzyme 6 Signals
  • None
Enzyme 6 Transmembrane Regions
  • None
Enzyme 6 Essentiality Not Available
Enzyme 6 GenBank ID Protein Not Available
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 Not Available
Enzyme 6 GenBank Gene ID M31059 Link Image
Enzyme 6 GeneCard ID Not Available
Enzyme 6 GenAtlas ID Not Available
Enzyme 6 HGNC ID Not Available
Enzyme 6 Chromosome Location Not Available
Enzyme 6 Locus 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. 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. Glycolaldehyde dehydrogenase
  2. Aldehyde dehydrogenase A
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 52273
Enzyme 7 Theoretical pI 4.79
Enzyme 7 GO Classification Not Available
Enzyme 7 General Function Energy production and conversion
Enzyme 7 Specific Function Acts on lactaldehyde as well as other aldehydes
Enzyme 7 Pathways Not Available
Enzyme 7 Reactions Not Available
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 Not Available
Enzyme 7 GenBank Gene ID M64541 Link Image
Enzyme 7 GeneCard ID Not Available
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. 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]
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 56307
Enzyme 8 Theoretical pI 5.36
Enzyme 8 GO Classification Not Available
Enzyme 8 General Function Energy production and conversion
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 Not Available
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 Not Available
Enzyme 8 GenBank Gene ID L40742 Link Image
Enzyme 8 GeneCard ID Not Available
Enzyme 8 GenAtlas ID Not Available
Enzyme 8 HGNC ID Not Available
Enzyme 8 Chromosome Location Not Available
Enzyme 8 Locus Not Available
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]
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 24540
Enzyme 9 Theoretical pI 5.20
Enzyme 9 GO Classification Not Available
Enzyme 9 General Function Carbohydrate transport and metabolism
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 Not Available
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 Not Available
Enzyme 9 GenBank Gene ID BA000016 Link Image
Enzyme 9 GeneCard ID Not Available
Enzyme 9 GenAtlas ID Not Available
Enzyme 9 HGNC ID Not Available
Enzyme 9 Chromosome Location Not Available
Enzyme 9 Locus Not Available
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 (EC 4.1.2.17)
Enzyme 10 Synonyms Not Available
Enzyme 10 Gene Name fucA
Enzyme 10 Protein Sequence >L-fuculose phosphate aldolase (EC 4.1.2.17) 
MENTNKLKYMEIREQICDVCHKMWQLGWVAANDGNVSVKLEDGTFLATPTGISKSFITPE
KLVHIDENGEVLDGPEGAKPSSEIKMHLRCYKEREDVGAVVHAHPPTATGFAVAHLALDR
YTMIETVIAIGSIPIAPYGTPSTYEVPDSIAPYLQEHDVILLENHGALTVGADLITAYYR
METLELYAKISLTAHLLGGEKEIERKNIDRLINMRKDYGVSGKHPGFKRYRTEE
Enzyme 10 Number of Residues 234
Enzyme 10 Molecular Weight 26124
Enzyme 10 Theoretical pI 5.78
Enzyme 10 GO Classification
Function
  • G-protein coupled receptor activity
  • receptor activity
  • rhodopsin-like receptor activity
  • signal transducer activity
  • transmembrane receptor activity
Process
  • G-protein coupled receptor protein signaling pathway
  • cell communication
  • cell surface receptor linked signal transduction
  • cellular process
  • signal transduction
Component
  • cell
  • integral to membrane
  • intrinsic to membrane
  • membrane
Enzyme 10 General Function Carbohydrate transport and metabolism
Enzyme 10 Specific Function Not Available
Enzyme 10 Pathways Not Available
Enzyme 10 Reactions
  • L-fuculose 1-phosphate = glycerone phosphate + (S)-lactaldehyde [RN:R02262] ALL_REAC 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 Not Available
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 Not Available
Enzyme 10 GenBank Gene ID CP000246 Link Image
Enzyme 10 GeneCard ID Not Available
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 Not Available
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 23776
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
  • transition metal ion binding
  • zinc ion binding
Process
  • alcohol metabolism
  • cellular metabolism
  • fucose metabolism
  • hexose metabolism
  • metabolism
  • monosaccharide metabolism
  • physiological process
Component
—
Enzyme 11 General Function Carbohydrate transport and metabolism
Enzyme 11 Specific Function L-fuculose 1-phosphate = glycerone phosphate + (S)-lactaldehyde
Enzyme 11 Pathways Not Available
Enzyme 11 Reactions Not Available
Enzyme 11 Pfam Domain Function
Enzyme 11 Signals
  • None
Enzyme 11 Transmembrane Regions
  • None
Enzyme 11 Essentiality Not Available
Enzyme 11 GenBank ID Protein Not Available
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 Not Available
Enzyme 11 GenBank Gene ID M31059 Link Image
Enzyme 11 GeneCard ID Not Available
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. 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]
  5. 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]
  6. 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]
  7. 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 31694
Enzyme 12 Theoretical pI 4.97
Enzyme 12 GO Classification Not Available
Enzyme 12 General Function Carbohydrate transport and metabolism
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 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 Not Available
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 Not Available
Enzyme 12 GenBank Gene ID AL935262 Link Image
Enzyme 12 GeneCard ID Not Available
Enzyme 12 GenAtlas ID Not Available
Enzyme 12 HGNC ID Not Available
Enzyme 12 Chromosome Location Not Available
Enzyme 12 Locus Not Available
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 31466
Enzyme 13 Theoretical pI 5.43
Enzyme 13 GO Classification Not Available
Enzyme 13 General Function Carbohydrate transport and metabolism
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 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 Not Available
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 Not Available
Enzyme 13 GenBank Gene ID AE016830 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 Not Available
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 30146
Enzyme 14 Theoretical pI 5.79
Enzyme 14 GO Classification Not Available
Enzyme 14 General Function Carbohydrate transport and metabolism
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 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 Not Available
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 Not Available
Enzyme 14 GenBank Gene ID X60472 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 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]
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 40610
Enzyme 15 Theoretical pI 4.50
Enzyme 15 GO Classification
Function
  • binding
  • catalytic activity
  • cation binding
  • ion binding
  • iron ion binding
  • oxidoreductase activity
  • transition metal ion binding
Process
  • metabolism
  • physiological process
Component
—
Enzyme 15 General Function Energy production and conversion
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 Not Available
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 Not Available
Enzyme 15 GenBank Gene ID CP000605 Link Image
Enzyme 15 GeneCard ID Not Available
Enzyme 15 GenAtlas ID Not Available
Enzyme 15 HGNC ID Not Available
Enzyme 15 Chromosome Location Not Available
Enzyme 15 Locus Not Available
Enzyme 15 SNPs SNPJam Report Link Image
Enzyme 15 General References Not Available
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 40645
Enzyme 16 Theoretical pI 4.91
Enzyme 16 GO Classification
Function
  • binding
  • catalytic activity
  • cation binding
  • ion binding
  • iron ion binding
  • oxidoreductase activity
  • transition metal ion binding
Process
  • metabolism
  • physiological process
Component
—
Enzyme 16 General Function Energy production and conversion
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 Not Available
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 Not Available
Enzyme 16 GenBank Gene ID CP000948 Link Image
Enzyme 16 GeneCard ID Not Available
Enzyme 16 GenAtlas ID Not Available
Enzyme 16 HGNC ID Not Available
Enzyme 16 Chromosome Location Not Available
Enzyme 16 Locus Not Available
Enzyme 16 SNPs SNPJam Report Link Image
Enzyme 16 General References Not Available
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 52273
Enzyme 17 Theoretical pI 4.79
Enzyme 17 GO Classification Not Available
Enzyme 17 General Function Energy production and conversion
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 Not Available
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 Not Available
Enzyme 17 GenBank Gene ID CP000948 Link Image
Enzyme 17 GeneCard ID Not Available
Enzyme 17 GenAtlas ID Not Available
Enzyme 17 HGNC ID Not Available
Enzyme 17 Chromosome Location Not Available
Enzyme 17 Locus Not Available
Enzyme 17 SNPs SNPJam Report Link Image
Enzyme 17 General References Not Available
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 30146
Enzyme 18 Theoretical pI 5.79
Enzyme 18 GO Classification Not Available
Enzyme 18 General Function Carbohydrate transport and metabolism
Enzyme 18 Specific Function Not Available
Enzyme 18 Pathways Not Available
Enzyme 18 Reactions Not Available
Enzyme 18 Pfam Domain Function
Enzyme 18 Signals
  • None
Enzyme 18 Transmembrane Regions
  • None
Enzyme 18 Essentiality Not Available
Enzyme 18 GenBank ID Protein Not Available
Enzyme 18 UniProtKB/Swiss-Prot ID B1XB69 Link Image
Enzyme 18 UniProtKB/Swiss-Prot Entry Name B1XB69_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 Not Available
Enzyme 18 GenBank Gene ID CP000948 Link Image
Enzyme 18 GeneCard ID Not Available
Enzyme 18 GenAtlas ID Not Available
Enzyme 18 HGNC ID Not Available
Enzyme 18 Chromosome Location Not Available
Enzyme 18 Locus Not Available
Enzyme 18 SNPs SNPJam Report Link Image
Enzyme 18 General References Not Available
Enzyme 18 Metabolite References Not Available