HCAE_ECOLI
ID HCAE_ECOLI Reviewed; 453 AA.
AC P0ABR5; P77590; P78203; Q47139;
DT 08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 08-NOV-2005, sequence version 1.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=3-phenylpropionate/cinnamic acid dioxygenase subunit alpha;
DE EC=1.14.12.19;
GN Name=hcaE; Synonyms=digA, hcaA, hcaA1, phdC1, yfhU;
GN OrderedLocusNames=b2538, JW2522;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RA Turlin E., Gasser F., Biville F.;
RL Submitted (SEP-1994) to the EMBL/GenBank/DDBJ databases.
RN [2]
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 [3]
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 [4]
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 [5]
RP FUNCTION IN CATABOLISM OF PHENYLPROPIONIC AND CINNAMIC ACIDS.
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: Part of the multicomponent 3-phenylpropionate dioxygenase.
CC Converts 3-phenylpropionic acid (PP) and cinnamic acid (CI) into 3-
CC phenylpropionate-dihydrodiol (PP-dihydrodiol) and cinnamic acid-
CC dihydrodiol (CI-dihydrodiol), respectively.
CC {ECO:0000269|PubMed:9603882}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-phenylpropanoate + H(+) + NADH + O2 = 3-(cis-5,6-
CC dihydroxycyclohexa-1,3-dien-1-yl)propanoate + NAD(+);
CC Xref=Rhea:RHEA:20357, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:51057, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945,
CC ChEBI:CHEBI:60087; EC=1.14.12.19;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(E)-cinnamate + H(+) + NADH + O2 = (2E)-3-(cis-5,6-
CC dihydroxycyclohexa-1,3-dien-1-yl)prop-2-enoate + NAD(+);
CC Xref=Rhea:RHEA:25058, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:15669, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945,
CC ChEBI:CHEBI:61451; EC=1.14.12.19;
CC -!- COFACTOR:
CC Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135; Evidence={ECO:0000305};
CC Note=Binds 1 [2Fe-2S] cluster. {ECO:0000305};
CC -!- COFACTOR:
CC Name=Fe cation; Xref=ChEBI:CHEBI:24875; Evidence={ECO:0000305};
CC Note=Binds 1 Fe cation. {ECO:0000305};
CC -!- PATHWAY: Aromatic compound metabolism; 3-phenylpropanoate degradation.
CC -!- SUBUNIT: This dioxygenase system consists of four proteins: the two
CC subunits of the hydroxylase component (HcaE and HcaF), a ferredoxin
CC (HcaC) and a ferredoxin reductase (HcaD).
CC -!- SIMILARITY: Belongs to the bacterial ring-hydroxylating dioxygenase
CC alpha subunit family. {ECO:0000305}.
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DR EMBL; Z37966; CAA86018.1; -; Genomic_DNA.
DR EMBL; U00096; AAC75591.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA16441.1; -; Genomic_DNA.
DR PIR; A65031; A65031.
DR RefSeq; NP_417033.1; NC_000913.3.
DR RefSeq; WP_000211172.1; NZ_STEB01000011.1.
DR AlphaFoldDB; P0ABR5; -.
DR SMR; P0ABR5; -.
DR BioGRID; 4261577; 13.
DR ComplexPortal; CPX-5161; 3-phenylpropionate/cinnamic acid dioxygenase.
DR IntAct; P0ABR5; 5.
DR STRING; 511145.b2538; -.
DR PaxDb; P0ABR5; -.
DR PRIDE; P0ABR5; -.
DR EnsemblBacteria; AAC75591; AAC75591; b2538.
DR EnsemblBacteria; BAA16441; BAA16441; BAA16441.
DR GeneID; 66673574; -.
DR GeneID; 946998; -.
DR KEGG; ecj:JW2522; -.
DR KEGG; eco:b2538; -.
DR PATRIC; fig|1411691.4.peg.4196; -.
DR EchoBASE; EB3229; -.
DR eggNOG; COG4638; Bacteria.
DR HOGENOM; CLU_026244_4_0_6; -.
DR InParanoid; P0ABR5; -.
DR OMA; AQVGYNE; -.
DR PhylomeDB; P0ABR5; -.
DR BioCyc; EcoCyc:PHENYLPRODIOXY-MON; -.
DR BioCyc; MetaCyc:PHENYLPRODIOXY-MON; -.
DR UniPathway; UPA00714; -.
DR PRO; PR:P0ABR5; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0009334; C:3-phenylpropionate dioxygenase complex; IC:ComplexPortal.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0008695; F:3-phenylpropionate dioxygenase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0019380; P:3-phenylpropionate catabolic process; IMP:EcoCyc.
DR CDD; cd08881; RHO_alpha_C_NDO-like; 1.
DR Gene3D; 2.102.10.10; -; 1.
DR HAMAP; MF_01648; HcaE; 1.
DR InterPro; IPR020875; HcaE.
DR InterPro; IPR043266; RHO_NdoB-like_C.
DR InterPro; IPR017941; Rieske_2Fe-2S.
DR InterPro; IPR036922; Rieske_2Fe-2S_sf.
DR InterPro; IPR015881; Ring-hydroxy_dOase_2Fe2S_BS.
DR InterPro; IPR015879; Ring_hydroxy_dOase_asu_C_dom.
DR InterPro; IPR001663; Rng_hydr_dOase-A.
DR PANTHER; PTHR43756; PTHR43756; 1.
DR Pfam; PF00355; Rieske; 1.
DR Pfam; PF00848; Ring_hydroxyl_A; 1.
DR PRINTS; PR00090; RNGDIOXGNASE.
DR SUPFAM; SSF50022; SSF50022; 1.
DR PROSITE; PS51296; RIESKE; 1.
DR PROSITE; PS00570; RING_HYDROXYL_ALPHA; 1.
PE 1: Evidence at protein level;
KW 2Fe-2S; Aromatic hydrocarbons catabolism; Dioxygenase; Iron; Iron-sulfur;
KW Metal-binding; NAD; Oxidoreductase; Reference proteome.
FT CHAIN 1..453
FT /note="3-phenylpropionate/cinnamic acid dioxygenase subunit
FT alpha"
FT /id="PRO_0000085061"
FT DOMAIN 44..142
FT /note="Rieske"
FT BINDING 85
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000250"
FT BINDING 87
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000250"
FT BINDING 105
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000250"
FT BINDING 108
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000250"
FT BINDING 213
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250"
FT BINDING 218
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250"
FT CONFLICT 20
FT /note="V -> A (in Ref. 1; CAA86018)"
FT /evidence="ECO:0000305"
FT CONFLICT 384..453
FT /note="GHRARNSKLCLEMGLGQEKRRDDGIPGITNYIFSETAARGMYQRWADLLSSE
FT SWQEVLDKTAAYQQEVMK -> ATAPATANCVWKWGLVRKSAATTAFLALLTISFQKLP
FT LVECTNAGPIF (in Ref. 1; CAA86018)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 453 AA; 51109 MW; 02535BF5F47643FD CRC64;
MTTPSDLNIY QLIDTQNGRV TPRIYTDPDI YQLELERIFG RCWLFLAHES QIPKPGDFFN
TYMGEDAVVV VRQKDGSIKA FLNQCRHRAM RVSYADCGNT RAFTCPYHGW SYGINGELID
VPLEPRAYPQ GLCKSHWGLN EVPCVESYKG LIFGNWDTSA PGLRDYLGDI AWYLDGMLDR
REGGTEIVGG VQKWVINCNW KFPAEQFASD QYHALFSHAS AVQVLGAKDD GSDKRLGDGQ
TARPVWETAK DALQFGQDGH GSGFFFTEKP DANVWVDGAV SSYYRETYAE AEQRLGEVRA
LRLAGHNNIF PTLSWLNGTA TLRVWHPRGP DQVEVWAFCI TDKAASDEVK AAFENSATRA
FGPAGFLEQD DSENWCEIQK LLKGHRARNS KLCLEMGLGQ EKRRDDGIPG ITNYIFSETA
ARGMYQRWAD LLSSESWQEV LDKTAAYQQE VMK
