ID E0J0Q3_ECOLW Unreviewed; 314 AA.
AC E0J0Q3;
DT 02-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2010, sequence version 1.
DT 27-MAR-2024, entry version 74.
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:ADT73962.1};
GN OrderedLocusNames=ECW_m0426 {ECO:0000313|EMBL:ADT73962.1};
OS Escherichia coli (strain ATCC 9637 / CCM 2024 / DSM 1116 / LMG 11080 / NBRC
OS 13500 / NCIMB 8666 / NRRL B-766 / W).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=566546 {ECO:0000313|EMBL:ADT73962.1, ECO:0000313|Proteomes:UP000008525};
RN [1] {ECO:0000313|EMBL:ADT73962.1, ECO:0000313|Proteomes:UP000008525}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 9637 / CCM 2024 / DSM 1116 / LMG 11080 / NBRC 13500 /
RC NCIMB 8666 / NRRL B-766 / W {ECO:0000313|Proteomes:UP000008525};
RX PubMed=21208457; DOI=10.1186/1471-2164-12-9;
RA Archer C.T., Kim J.F., Jeong H., Park J.H., Vickers C.E., Lee S.Y.,
RA Nielsen L.K.;
RT "The genome sequence of E. coli W (ATCC 9637): comparative genome analysis
RT and an improved genome-scale reconstruction of E. coli.";
RL BMC Genomics 12:9-9(2011).
CC -!- FUNCTION: Catalyzes the non-heme iron(II)-dependent oxidative cleavage
CC of 2,3-dihydroxyphenylpropionic acid and 2,3-dihydroxicinnamic acid
CC into 2-hydroxy-6-ketononadienedioate and 2-hydroxy-6-
CC ketononatrienedioate, respectively. {ECO:0000256|HAMAP-Rule:MF_01653}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E)-3-(2,3-dihydroxyphenyl)prop-2-enoate + O2 = (2Z,4E,7E)-2-
CC hydroxy-6-oxonona-2,4,7-trienedioate + H(+); Xref=Rhea:RHEA:25054,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:58642,
CC ChEBI:CHEBI:66888; EC=1.13.11.16;
CC Evidence={ECO:0000256|ARBA:ARBA00001748, ECO:0000256|HAMAP-
CC Rule:MF_01653};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-(2,3-dihydroxyphenyl)propanoate + O2 = (2Z,4E)-2-hydroxy-6-
CC 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;
CC Evidence={ECO:0000256|ARBA:ARBA00001843, ECO:0000256|HAMAP-
CC Rule:MF_01653};
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01653};
CC -!- PATHWAY: Aromatic compound metabolism; 3-phenylpropanoate degradation.
CC {ECO:0000256|ARBA:ARBA00005207, ECO:0000256|HAMAP-Rule:MF_01653}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000256|ARBA:ARBA00011881,
CC ECO:0000256|HAMAP-Rule:MF_01653}.
CC -!- SIMILARITY: Belongs to the LigB/MhpB extradiol dioxygenase family.
CC {ECO:0000256|ARBA:ARBA00007030, ECO:0000256|HAMAP-Rule:MF_01653}.
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DR EMBL; CP002185; ADT73962.1; -; Genomic_DNA.
DR RefSeq; WP_000543459.1; NZ_WBMH01000016.1.
DR AlphaFoldDB; E0J0Q3; -.
DR SMR; E0J0Q3; -.
DR GeneID; 66671348; -.
DR KEGG; elw:ECW_m0426; -.
DR PATRIC; fig|566546.30.peg.435; -.
DR UniPathway; UPA00714; -.
DR Proteomes; UP000008525; 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 Gene3D; 3.40.830.10; LigB-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.
DR SUPFAM; SSF53213; LigB-like; 1.
PE 3: Inferred from homology;
KW Aromatic hydrocarbons catabolism {ECO:0000256|ARBA:ARBA00022797,
KW ECO:0000256|HAMAP-Rule:MF_01653};
KW Dioxygenase {ECO:0000256|ARBA:ARBA00022964, ECO:0000256|HAMAP-
KW Rule:MF_01653}; Iron {ECO:0000256|HAMAP-Rule:MF_01653};
KW Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_01653}.
FT DOMAIN 5..306
FT /note="Extradiol ring-cleavage dioxygenase class III enzyme
FT subunit B"
FT /evidence="ECO:0000259|Pfam:PF02900"
FT ACT_SITE 115
FT /note="Proton donor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01653"
FT ACT_SITE 179
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01653"
SQ SEQUENCE 314 AA; 34226 MW; 8AA5A8574E5DEA54 CRC64;
MHAYLHCLSH SPLVGYVDPA QEVLDEVNGV IASARERIAA FSPELVVLFA PDHYNGFFYD
VMPPFCLGVG ATAIGDFGSA AGELPVPVEL AEACAHAVMK SGIDLAVSYC MQVDHGFAQP
LEFLLGGLDK VPVLPVFING VATPLPGFQR TRMLGEAIGR FTSTLNKRVL FLGSGGLSHQ
PPVPELAKAD AHMRDRLLGS GKDLPASERE LRQQRVISAA EKFVEDQRTL HPLNPIWDNQ
FMTLLEQGRI QELDAVSNEE LSAIAGKSTH EIKTWVAAFA AISTFGNWRS EGRYYRPIPE
WIAGFGSLSA RTEN
//
