HCAB_ECOLI
ID HCAB_ECOLI Reviewed; 270 AA.
AC P0CI31; P76995; P77646;
DT 30-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT 30-NOV-2010, sequence version 1.
DT 03-AUG-2022, entry version 69.
DE RecName: Full=3-phenylpropionate-dihydrodiol/cinnamic acid-dihydrodiol dehydrogenase;
DE EC=1.3.1.87;
DE AltName: Full=2,3-dihydroxy-2,3-dihydrophenylpropionate dehydrogenase;
DE AltName: Full=3-(cis-5,6-dihydroxycyclohexa-1,3-dien-1-yl)propanoate dehydrogenase;
DE AltName: Full=CI-dihydrodiol dehydrogenase;
DE AltName: Full=Cis-3-(2-carboxyethenyl)-3,5-cyclohexadiene-1,2-diol dehydrogenase;
DE AltName: Full=Cis-3-(2-carboxyethyl)-3,5-cyclohexadiene-1,2-diol dehydrogenase;
DE AltName: Full=PP-dihydrodiol dehydrogenase;
GN Name=hcaB; Synonyms=phdD, yfhX; OrderedLocusNames=b2541, JW2525;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9205837; DOI=10.1093/dnares/4.2.91;
RA Yamamoto Y., Aiba H., Baba T., Hayashi K., Inada T., Isono K., Itoh T.,
RA Kimura S., Kitagawa M., Makino K., Miki T., Mitsuhashi N., Mizobuchi K.,
RA Mori H., Nakade S., Nakamura Y., Nashimoto H., Oshima T., Oyama S.,
RA Saito N., Sampei G., Satoh Y., Sivasundaram S., Tagami H., Takahashi H.,
RA Takeda J., Takemoto K., Uehara K., Wada C., Yamagata S., Horiuchi T.;
RT "Construction of a contiguous 874-kb sequence of the Escherichia coli-K12
RT genome corresponding to 50.0-68.8 min on the linkage map and analysis of
RT its sequence features.";
RL DNA Res. 4:91-113(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [4]
RP FUNCTION IN CATABOLISM OF PHENYLPROPIONIC AND CINNAMIC ACIDS, AND CATALYTIC
RP ACTIVITY.
RC STRAIN=K12 / MC1061 / ATCC 53338 / DSM 7140;
RX PubMed=9603882; DOI=10.1128/jb.180.11.2915-2923.1998;
RA Diaz E., Ferrandez A., Garcia J.L.;
RT "Characterization of the hca cluster encoding the dioxygenolytic pathway
RT for initial catabolism of 3-phenylpropionic acid in Escherichia coli K-
RT 12.";
RL J. Bacteriol. 180:2915-2923(1998).
CC -!- FUNCTION: Converts 3-phenylpropionate-dihydrodiol (PP-dihydrodiol) and
CC cinnamic acid-dihydrodiol (CI-dihydrodiol) into 3-(2,3-
CC dihydroxylphenyl)propanoic acid (DHPP) and 2,3-dihydroxicinnamic acid
CC (DHCI), respectively. {ECO:0000250, ECO:0000269|PubMed:9603882}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-(cis-5,6-dihydroxycyclohexa-1,3-dien-1-yl)propanoate +
CC NAD(+) = 3-(2,3-dihydroxyphenyl)propanoate + H(+) + NADH;
CC Xref=Rhea:RHEA:25062, ChEBI:CHEBI:15378, ChEBI:CHEBI:46951,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:60087; EC=1.3.1.87;
CC Evidence={ECO:0000269|PubMed:9603882};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E)-3-(cis-5,6-dihydroxycyclohexa-1,3-dien-1-yl)prop-2-enoate
CC + NAD(+) = (2E)-3-(2,3-dihydroxyphenyl)prop-2-enoate + H(+) + NADH;
CC Xref=Rhea:RHEA:25066, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945, ChEBI:CHEBI:58642, ChEBI:CHEBI:61451; EC=1.3.1.87;
CC Evidence={ECO:0000269|PubMed:9603882};
CC -!- PATHWAY: Aromatic compound metabolism; 3-phenylpropanoate degradation.
CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; U00096; AAC75594.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA16444.1; -; Genomic_DNA.
DR PIR; D65031; D65031.
DR RefSeq; NP_417036.1; NC_000913.3.
DR RefSeq; WP_001281379.1; NZ_LN832404.1.
DR AlphaFoldDB; P0CI31; -.
DR SMR; P0CI31; -.
DR BioGRID; 4260604; 7.
DR DIP; DIP-9863N; -.
DR IntAct; P0CI31; 7.
DR STRING; 511145.b2541; -.
DR PaxDb; P0CI31; -.
DR PRIDE; P0CI31; -.
DR EnsemblBacteria; AAC75594; AAC75594; b2541.
DR EnsemblBacteria; BAA16444; BAA16444; BAA16444.
DR GeneID; 945346; -.
DR KEGG; ecj:JW2525; -.
DR KEGG; eco:b2541; -.
DR PATRIC; fig|1411691.4.peg.4193; -.
DR EchoBASE; EB3232; -.
DR eggNOG; COG1028; Bacteria.
DR HOGENOM; CLU_010194_1_0_6; -.
DR InParanoid; P0CI31; -.
DR OMA; VFHINVK; -.
DR PhylomeDB; P0CI31; -.
DR BioCyc; EcoCyc:PHENPRODIOLDEHYDROG-MON; -.
DR BioCyc; MetaCyc:PHENPRODIOLDEHYDROG-MON; -.
DR UniPathway; UPA00714; -.
DR PRO; PR:P0CI31; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0018498; F:2,3-dihydroxy-2,3-dihydro-phenylpropionate dehydrogenase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0019380; P:3-phenylpropionate catabolic process; IMP:EcoCyc.
DR HAMAP; MF_01647; HcaB; 1.
DR InterPro; IPR023643; Dihydrodiol_DH_HcaB.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR020904; Sc_DH/Rdtase_CS.
DR InterPro; IPR002347; SDR_fam.
DR Pfam; PF00106; adh_short; 1.
DR PRINTS; PR00081; GDHRDH.
DR PRINTS; PR00080; SDRFAMILY.
DR SUPFAM; SSF51735; SSF51735; 1.
DR PROSITE; PS00061; ADH_SHORT; 1.
PE 3: Inferred from homology;
KW Aromatic hydrocarbons catabolism; NAD; Oxidoreductase; Reference proteome.
FT CHAIN 1..270
FT /note="3-phenylpropionate-dihydrodiol/cinnamic acid-
FT dihydrodiol dehydrogenase"
FT /id="PRO_0000054704"
FT ACT_SITE 156
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 10..34
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 143
FT /ligand="substrate"
FT /evidence="ECO:0000250"
SQ SEQUENCE 270 AA; 28500 MW; 607D316E7442D3E7 CRC64;
MSDLHNESIF ITGGGSGLGL ALVERFIEEG AQVATLELSA AKVASLRQRF GEHILAVEGN
VTCYADYQRA VDQILTRSGK LDCFIGNAGI WDHNASLVNT PAETLETGFH ELFNVNVLGY
LLGAKACAPA LIASEGSMIF TLSNAAWYPG GGGPLYTASK HAATGLIRQL AYELAPKVRV
NGVGPCGMAS DLRGPQALGQ SETSIMQSLT PEKIAAILPL QFFPQPADFT GPYVMLTSRR
NNRALSGVMI NADAGLAIRG IRHVAAGLDL
