Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P0CI31 (HCAB_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 31. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
3-phenylpropionate-dihydrodiol/cinnamic acid-dihydrodiol dehydrogenase

EC=1.3.1.87
Alternative name(s):
2,3-dihydroxy-2,3-dihydrophenylpropionate dehydrogenase
3-(cis-5,6-dihydroxycyclohexa-1,3-dien-1-yl)propanoate dehydrogenase
CI-dihydrodiol dehydrogenase
Cis-3-(2-carboxyethenyl)-3,5-cyclohexadiene-1,2-diol dehydrogenase
Cis-3-(2-carboxyethyl)-3,5-cyclohexadiene-1,2-diol dehydrogenase
PP-dihydrodiol dehydrogenase
Gene names
Name:hcaB
Synonyms:phdD, yfhX
Ordered Locus Names:b2541, JW2525
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length270 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Converts 3-phenylpropionate-dihydrodiol (PP-dihydrodiol) and cinnamic acid-dihydrodiol (CI-dihydrodiol) into 3-(2,3-dihydroxylphenyl)propanoic acid (DHPP) and 2,3-dihydroxicinnamic acid (DHCI), respectively By similarity. Ref.4

Catalytic activity

3-(cis-5,6-dihydroxycyclohexa-1,3-dien-1-yl)propanoate + NAD+ = 3-(2,3-dihydroxyphenyl)propanoate + NADH. Ref.4

(2E)-3-(cis-5,6-dihydroxycyclohexa-1,3-dien-1-yl)prop-2-enoate + NAD+ = (2E)-3-(2,3-dihydroxyphenyl)prop-2-enoate + NADH. Ref.4

Pathway

Aromatic compound metabolism; 3-phenylpropanoate degradation. HAMAP-Rule MF_01647

Sequence similarities

Belongs to the short-chain dehydrogenases/reductases (SDR) family.

Ontologies

Keywords
   Biological processAromatic hydrocarbons catabolism
   LigandNAD
   Molecular functionOxidoreductase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_process3-phenylpropionate catabolic process

Inferred from mutant phenotype PubMed 3531186. Source: EcoCyc

   Molecular_function2,3-dihydroxy-2,3-dihydro-phenylpropionate dehydrogenase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 2702703-phenylpropionate-dihydrodiol/cinnamic acid-dihydrodiol dehydrogenase HAMAP-Rule MF_01647
PRO_0000054704

Regions

Nucleotide binding10 – 3425NAD By similarity

Sites

Active site1561Proton acceptor By similarity
Binding site1431Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
P0CI31 [UniParc].

Last modified November 30, 2010. Version 1.
Checksum: 607D316E7442D3E7

FASTA27028,500
        10         20         30         40         50         60 
MSDLHNESIF ITGGGSGLGL ALVERFIEEG AQVATLELSA AKVASLRQRF GEHILAVEGN 

        70         80         90        100        110        120 
VTCYADYQRA VDQILTRSGK LDCFIGNAGI WDHNASLVNT PAETLETGFH ELFNVNVLGY 

       130        140        150        160        170        180 
LLGAKACAPA LIASEGSMIF TLSNAAWYPG GGGPLYTASK HAATGLIRQL AYELAPKVRV 

       190        200        210        220        230        240 
NGVGPCGMAS DLRGPQALGQ SETSIMQSLT PEKIAAILPL QFFPQPADFT GPYVMLTSRR 

       250        260        270 
NNRALSGVMI NADAGLAIRG IRHVAAGLDL 

« Hide

References

« Hide 'large scale' references
[1]"Construction of a contiguous 874-kb sequence of the Escherichia coli-K12 genome corresponding to 50.0-68.8 min on the linkage map and analysis of its sequence features."
Yamamoto Y., Aiba H., Baba T., Hayashi K., Inada T., Isono K., Itoh T., Kimura S., Kitagawa M., Makino K., Miki T., Mitsuhashi N., Mizobuchi K., Mori H., Nakade S., Nakamura Y., Nashimoto H., Oshima T. expand/collapse author list , Oyama S., Saito N., Sampei G., Satoh Y., Sivasundaram S., Tagami H., Takahashi H., Takeda J., Takemoto K., Uehara K., Wada C., Yamagata S., Horiuchi T.
DNA Res. 4:91-113(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[2]"The complete genome sequence of Escherichia coli K-12."
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.
Science 277:1453-1462(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / MG1655 / ATCC 47076.
[3]"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[4]"Characterization of the hca cluster encoding the dioxygenolytic pathway for initial catabolism of 3-phenylpropionic acid in Escherichia coli K-12."
Diaz E., Ferrandez A., Garcia J.L.
J. Bacteriol. 180:2915-2923(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN CATABOLISM OF PHENYLPROPIONIC AND CINNAMIC ACIDS, CATALYTIC ACTIVITY.
Strain: K12 / MC1061 / ATCC 53338 / DSM 7140.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U00096 Genomic DNA. Translation: AAC75594.1.
AP009048 Genomic DNA. Translation: BAA16444.1.
PIRD65031.
RefSeqNP_417036.1. NC_000913.3.
YP_490769.1. NC_007779.1.

3D structure databases

ProteinModelPortalP0CI31.
SMRP0CI31. Positions 4-270.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-9863N.
IntActP0CI31. 7 interactions.
MINTMINT-1239788.

Proteomic databases

PRIDEP0CI31.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC75594; AAC75594; b2541.
BAA16444; BAA16444; BAA16444.
GeneID12931610.
945346.
KEGGecj:Y75_p2494.
eco:b2541.
PATRIC32120479. VBIEscCol129921_2642.

Organism-specific databases

EchoBASEEB3232.
EcoGeneEG13459. hcaB.

Phylogenomic databases

KOK05711.
OMAPNAGIWD.
OrthoDBEOG625JVT.
PhylomeDBP0CI31.

Enzyme and pathway databases

BioCycEcoCyc:PHENPRODIOLDEHYDROG-MONOMER.
MetaCyc:PHENPRODIOLDEHYDROG-MONOMER.
UniPathwayUPA00714.

Family and domain databases

Gene3D3.40.50.720. 1 hit.
HAMAPMF_01647. HcaB.
InterProIPR002198. DH_sc/Rdtase_SDR.
IPR023643. Dihydrodiol_DH_HcaB.
IPR002347. Glc/ribitol_DH.
IPR016040. NAD(P)-bd_dom.
IPR020904. Sc_DH/Rdtase_CS.
[Graphical view]
PfamPF00106. adh_short. 1 hit.
[Graphical view]
PRINTSPR00081. GDHRDH.
PR00080. SDRFAMILY.
PROSITEPS00061. ADH_SHORT. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

PROP0CI31.

Entry information

Entry nameHCAB_ECOLI
AccessionPrimary (citable) accession number: P0CI31
Secondary accession number(s): P76995, P77646
Entry history
Integrated into UniProtKB/Swiss-Prot: November 30, 2010
Last sequence update: November 30, 2010
Last modified: April 16, 2014
This is version 31 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene