MHPB1_PSEPU
ID MHPB1_PSEPU Reviewed; 314 AA.
AC Q400K4;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 27-SEP-2005, sequence version 1.
DT 25-MAY-2022, entry version 54.
DE RecName: Full=2,3-dihydroxyphenylpropionate/2,3-dihydroxicinnamic acid 1,2-dioxygenase 1 {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 1 {ECO:0000255|HAMAP-Rule:MF_01653};
GN Name=mhpB1 {ECO:0000255|HAMAP-Rule:MF_01653}; Synonyms=orcB;
OS Pseudomonas putida (Arthrobacter siderocapsulatus).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=303;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ORC;
RA Straganz G.D., Glieder A., Steiner W.;
RT "Cloning of genes involved in meta-cleavage pathways of Pseudomonas putida
RT orc: nucleotide sequences of genes, characterization of two dioxygenases
RT and identification of the orcinol pathway.";
RL Submitted (AUG-2002) 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: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; AF534914; AAQ10534.1; -; Genomic_DNA.
DR AlphaFoldDB; Q400K4; -.
DR SMR; Q400K4; -.
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 1"
FT /id="PRO_0000337662"
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; 33843 MW; 8EA8A7FB34F13D0F CRC64;
MSAYLHCLSH TPLVGYVDPV AEVLAEVDEV VAAARARIAA FDPQLVFLFA PDHYNGFFYD
VMPSFCIGMA ATAIGDFHSL AGPLDVPRET AEACAAAVLE AGVDAAVSYR MQVDHGFAQP
LELLLGGLAE KPVVPVFING VAVPLPGFQR ARLLGEAIGR FARSTGKRVL FLGSGGLSHQ
PPVPELAKVD ARMADRLLGS GRDLPTDERQ ARQQRVISAA EGFVADQNSL HPLNPEWDNH
FLDLLEQRRF AELDGLGNAE LSALAGKSTH EVKTWVTAFA ALSAFGPYQA HERYYRPIPE
WIAGFGSLSA HSLS