MHPB_CUPPJ
ID MHPB_CUPPJ Reviewed; 314 AA.
AC Q476N0;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2005, sequence version 1.
DT 25-MAY-2022, entry version 87.
DE RecName: Full=2,3-dihydroxyphenylpropionate/2,3-dihydroxicinnamic acid 1,2-dioxygenase {ECO:0000255|HAMAP-Rule:MF_01653};
DE EC=1.13.11.16 {ECO:0000255|HAMAP-Rule:MF_01653};
DE AltName: Full=3-carboxyethylcatechol 2,3-dioxygenase {ECO:0000255|HAMAP-Rule:MF_01653};
GN Name=mhpB {ECO:0000255|HAMAP-Rule:MF_01653}; OrderedLocusNames=Reut_A0271;
OS Cupriavidus pinatubonensis (strain JMP 134 / LMG 1197) (Cupriavidus necator
OS (strain JMP 134)).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Cupriavidus.
OX NCBI_TaxID=264198;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JMP134 / LMG 1197;
RX PubMed=20339589; DOI=10.1371/journal.pone.0009729;
RA Lykidis A., Perez-Pantoja D., Ledger T., Mavromatis K., Anderson I.J.,
RA Ivanova N.N., Hooper S.D., Lapidus A., Lucas S., Gonzalez B.,
RA Kyrpides N.C.;
RT "The complete multipartite genome sequence of Cupriavidus necator JMP134, a
RT versatile pollutant degrader.";
RL PLoS ONE 5:E9729-E9729(2010).
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:0000255|HAMAP-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; Evidence={ECO:0000255|HAMAP-
CC 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; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_01653};
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01653};
CC -!- PATHWAY: Aromatic compound metabolism; 3-phenylpropanoate degradation.
CC {ECO:0000255|HAMAP-Rule:MF_01653}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000255|HAMAP-Rule:MF_01653}.
CC -!- SIMILARITY: Belongs to the LigB/MhpB extradiol dioxygenase family.
CC {ECO:0000255|HAMAP-Rule:MF_01653}.
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; CP000090; AAZ59653.1; -; Genomic_DNA.
DR RefSeq; WP_011296461.1; NC_007347.1.
DR AlphaFoldDB; Q476N0; -.
DR SMR; Q476N0; -.
DR STRING; 264198.Reut_A0271; -.
DR EnsemblBacteria; AAZ59653; AAZ59653; Reut_A0271.
DR KEGG; reu:Reut_A0271; -.
DR eggNOG; COG3384; Bacteria.
DR HOGENOM; CLU_078149_0_0_4; -.
DR OMA; MDVDHGT; -.
DR OrthoDB; 1728007at2; -.
DR UniPathway; UPA00714; -.
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;
KW Aromatic hydrocarbons catabolism; Dioxygenase; Iron; Oxidoreductase.
FT CHAIN 1..314
FT /note="2,3-dihydroxyphenylpropionate/2,3-dihydroxicinnamic
FT acid 1,2-dioxygenase"
FT /id="PRO_0000337664"
FT ACT_SITE 115
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01653"
FT ACT_SITE 179
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01653"
SQ SEQUENCE 314 AA; 33299 MW; A5276EA6F4BA1D10 CRC64;
MPIQLECLSH TPLHGYVDPA PEVVAEVERV QAAARDRVRA FDPELVVVFA PDHFNGFFYD
VMPPFCIGAA ATAIGDFKSL AGKLPVPADL ALSLAESVMA ADIDVALSHR MQVDHGCADA
LAALTGSLHR YPVIPVFINS VAPPMATLRR ARLLGDAVGR FLSRAGKRVL VVGSGGISHE
PPVPELAGAS EEVAERLIAG RNPSPESRAA RQARTVAAAK SFVAGDSHLH PLNPEWDRAF
LSLLASGELT AVDGMTNDAI TRDGGKSAHE IRTWVAAFGA LAAYGPYRAS LDFYRAIPEW
IAGFATMHAE PAAV