ID A0A171KNA4_9BURK Unreviewed; 322 AA.
AC A0A171KNA4;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 24-JAN-2024, entry version 22.
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:KKO70371.1};
GN ORFNames=AAV32_16675 {ECO:0000313|EMBL:KKO70371.1};
OS Kerstersia gyiorum.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Kerstersia.
OX NCBI_TaxID=206506 {ECO:0000313|EMBL:KKO70371.1, ECO:0000313|Proteomes:UP000078084};
RN [1] {ECO:0000313|EMBL:KKO70371.1, ECO:0000313|Proteomes:UP000078084}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CG1 {ECO:0000313|EMBL:KKO70371.1,
RC ECO:0000313|Proteomes:UP000078084};
RA Greninger A.L., Kozyreva V., Chaturvedi V.;
RT "Genome sequence of Kerstersia gyiorum CG1.";
RL Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases.
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KKO70371.1}.
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DR EMBL; LBNE01000016; KKO70371.1; -; Genomic_DNA.
DR RefSeq; WP_068375154.1; NZ_LBNE01000016.1.
DR AlphaFoldDB; A0A171KNA4; -.
DR STRING; 206506.AAV32_16675; -.
DR PATRIC; fig|206506.3.peg.3552; -.
DR UniPathway; UPA00714; -.
DR Proteomes; UP000078084; Unassembled WGS sequence.
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,
KW ECO:0000313|EMBL:KKO70371.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000078084}.
FT DOMAIN 10..303
FT /note="Extradiol ring-cleavage dioxygenase class III enzyme
FT subunit B"
FT /evidence="ECO:0000259|Pfam:PF02900"
FT ACT_SITE 118
FT /note="Proton donor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01653"
FT ACT_SITE 182
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01653"
SQ SEQUENCE 322 AA; 34595 MW; 1A94479D531FC627 CRC64;
MSTSIVKLKC LSHTPLRGLN DPAPGVVAEV DAVIAAARAD VEAFDPELIV VFAPDHYNGL
FYDLMPPFVI ATAAESVADY KTLPGPLSIP DDLALDLVRH VLDSDIDIAM SHRLQVDHGC
TQILEEMTGS LTRYPVIPII INSVAPPFGP YRRVRLLGEA VGRFIAGLGK RVLILGSGGL
SHEPPVPVFS GAKPEIAEFL IAGRNPTPEA RAARQARTIA TGQIFGTPDC DLTPLNEEWD
QAFMELLIGK DLSKVDDFEI ETISRAAGRS THEVRTWVAA FAAMSAAGAY EGRRDYYRPV
NEWIAGYGVV SAEPASPVPA AG
//
