(data stored in ACNUC10821 zone)

SWISSPROT: C8U241_ECO10

ID   C8U241_ECO10            Unreviewed;       314 AA.
AC   C8U241;
DT   03-NOV-2009, integrated into UniProtKB/TrEMBL.
DT   03-NOV-2009, sequence version 1.
DT   05-DEC-2018, entry version 58.
DE   RecName: Full=2,3-dihydroxyphenylpropionate/2,3-dihydroxicinnamic acid 1,2-dioxygenase {ECO:0000256|HAMAP-Rule:MF_01653};
DE            EC=1.13.11.16 {ECO:0000256|HAMAP-Rule:MF_01653};
DE   AltName: Full=3-carboxyethylcatechol 2,3-dioxygenase {ECO:0000256|HAMAP-Rule:MF_01653};
GN   Name=mhpB {ECO:0000256|HAMAP-Rule:MF_01653,
GN   ECO:0000313|EMBL:BAI29199.1};
GN   OrderedLocusNames=ECO103_0330 {ECO:0000313|EMBL:BAI29199.1};
OS   Escherichia coli O103:H2 (strain 12009 / EHEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=585395 {ECO:0000313|EMBL:BAI29199.1, ECO:0000313|Proteomes:UP000000959};
RN   [1] {ECO:0000313|EMBL:BAI29199.1, ECO:0000313|Proteomes:UP000000959}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=12009 / EHEC {ECO:0000313|Proteomes:UP000000959};
RX   PubMed=19815525; DOI=10.1073/pnas.0903585106;
RA   Ogura Y., Ooka T., Iguchi A., Toh H., Asadulghani M., Oshima K.,
RA   Kodama T., Abe H., Nakayama K., Kurokawa K., Tobe T., Hattori M.,
RA   Hayashi T.;
RT   "Comparative genomics reveal the mechanism of the parallel evolution
RT   of O157 and non-O157 enterohemorrhagic Escherichia coli.";
RL   Proc. Natl. Acad. Sci. U.S.A. 106:17939-17944(2009).
CC   -!- FUNCTION: Catalyzes the non-heme iron(II)-dependent oxidative
CC       cleavage of 2,3-dihydroxyphenylpropionic acid and 2,3-
CC       dihydroxicinnamic acid into 2-hydroxy-6-ketononadienedioate and 2-
CC       hydroxy-6-ketononatrienedioate, respectively. {ECO:0000256|HAMAP-
CC       Rule:MF_01653}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2E)-3-(2,3-dihydroxyphenyl)prop-2-enoate + O2 =
CC         (2Z,4E,7E)-2-hydroxy-6-oxonona-2,4,7-trienedioate + H(+);
CC         Xref=Rhea:RHEA:25054, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC         ChEBI:CHEBI:58642, ChEBI:CHEBI:66888; EC=1.13.11.16;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_01653};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=3-(2,3-dihydroxyphenyl)propanoate + O2 = (2Z,4E)-2-
CC         hydroxy-6-oxonona-2,4-dienedioate + H(+); Xref=Rhea:RHEA:23840,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:46951,
CC         ChEBI:CHEBI:66887; EC=1.13.11.16; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_01653};
CC   -!- COFACTOR:
CC       Name=Fe(2+); Xref=ChEBI:CHEBI:29033; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_01653};
CC   -!- PATHWAY: Aromatic compound metabolism; 3-phenylpropanoate
CC       degradation. {ECO:0000256|HAMAP-Rule:MF_01653}.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000256|HAMAP-Rule:MF_01653}.
CC   -!- SIMILARITY: Belongs to the LigB/MhpB extradiol dioxygenase family.
CC       {ECO:0000256|HAMAP-Rule:MF_01653}.
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DR   EMBL; AP010958; BAI29199.1; -; Genomic_DNA.
DR   RefSeq; WP_000543452.1; NC_013353.1.
DR   EnsemblBacteria; BAI29199; BAI29199; ECO103_0330.
DR   KEGG; eoh:ECO103_0330; -.
DR   HOGENOM; HOG000069851; -.
DR   KO; K05713; -.
DR   OMA; RTWIAAF; -.
DR   BioCyc; ECOL585395:ECO103_RS01725-MONOMER; -.
DR   UniPathway; UPA00714; -.
DR   Proteomes; UP000000959; Chromosome.
DR   GO; GO:0047070; F:3-carboxyethylcatechol 2,3-dioxygenase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0008198; F:ferrous iron binding; IEA:InterPro.
DR   GO; GO:0019380; P:3-phenylpropionate catabolic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd07365; MhpB_like; 1.
DR   HAMAP; MF_01653; MhpB; 1.
DR   InterPro; IPR023789; DHPP/DHXA_dioxygenase.
DR   InterPro; IPR004183; Xdiol_dOase_suB.
DR   Pfam; PF02900; LigB; 1.
PE   3: Inferred from homology;
DR   PRODOM; C8U241.
DR   SWISS-2DPAGE; C8U241.
KW   Aromatic hydrocarbons catabolism {ECO:0000256|HAMAP-Rule:MF_01653};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000959};
KW   Dioxygenase {ECO:0000256|HAMAP-Rule:MF_01653,
KW   ECO:0000313|EMBL:BAI29199.1}; Iron {ECO:0000256|HAMAP-Rule:MF_01653};
KW   Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_01653}.
FT   DOMAIN        4    306       LigB. {ECO:0000259|Pfam:PF02900}.
FT   ACT_SITE    115    115       Proton donor. {ECO:0000256|HAMAP-Rule:
FT                                MF_01653}.
FT   ACT_SITE    179    179       Proton acceptor. {ECO:0000256|HAMAP-Rule:
FT                                MF_01653}.
SQ   SEQUENCE   314 AA;  34182 MW;  1C76726A7A8EB331 CRC64;
     MHAYLHCLSH SPLVGYVDPA QEVLDEVNGV IASARERIAA FSPELVVLFA PDHYNGFFYD
     VMPPFCLGVG ATAIGDFGSA AGDLPVPVEL AEACAHAVMK SGIDLAVSYC MQVDHGFAQP
     LEFLLGGLDK VPVLPVFING VATPLPGFQR TRMLGEAIGR FTSTLNKRVL FLGSGGLSHQ
     PPVPELAKAD AHMRDRLLGS GKDLPASERE LRQQRVISAA EKFVEDQRTL HPLNPIWDNQ
     FMTLLEQGRI QELDAVSNEE LSAIAGKSTH EIKTWVAAFA AISAFGNWRS EGRYYRPIPE
     WIAGFGSLSA RTEN
//

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