ID   MHPB_COMTE              Reviewed;         321 AA.
AC   Q9S157;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   25-MAY-2022, entry version 64.
DE   RecName: Full=2,3-dihydroxyphenylpropionate/2,3-dihydroxicinnamic acid 1,2-dioxygenase;
DE            EC=1.13.11.16;
DE   AltName: Full=3-carboxyethylcatechol 2,3-dioxygenase;
GN   Name=mhpB;
OS   Comamonas testosteroni (Pseudomonas testosteroni).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Comamonas.
OX   NCBI_TaxID=285;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION IN CATABOLISM OF 3-HYDROXY
RP   DERIVATIVES OF PHENYLPROPIONIC ACID, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC   STRAIN=TA441;
RX   PubMed=10537203; DOI=10.1099/00221287-145-10-2813;
RA   Arai H., Yamamoto T., Ohishi T., Shimizu T., Nakata T., Kudo T.;
RT   "Genetic organization and characteristics of the 3-(3-
RT   hydroxyphenyl)propionic acid degradation pathway of Comamonas testosteroni
RT   TA441.";
RL   Microbiology 145:2813-2820(1999).
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:0000269|PubMed:10537203}.
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   -!- 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   -!- COFACTOR:
CC       Name=Fe(2+); Xref=ChEBI:CHEBI:29033; Evidence={ECO:0000250};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         Vmax=0.73 umol/min/mg enzyme with 3-(2,3-dihydroxyphenyl)propanoate
CC         (at pH 7.5) {ECO:0000269|PubMed:10537203};
CC         Vmax=0.45 umol/min/mg enzyme withd 2,3-dihydroxybiphenyl (at pH 7.5)
CC         {ECO:0000269|PubMed:10537203};
CC         Vmax=0.22 umol/min/mg enzyme withd 3-methylcatechol (at pH 7.5)
CC         {ECO:0000269|PubMed:10537203};
CC         Vmax=0.10 umol/min/mg enzyme withd catechol (at pH 7.5)
CC         {ECO:0000269|PubMed:10537203};
CC   -!- PATHWAY: Aromatic compound metabolism; 3-phenylpropanoate degradation.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the LigB/MhpB extradiol dioxygenase family.
CC       {ECO:0000305}.
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; AB024335; BAA82879.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q9S157; -.
DR   SMR; Q9S157; -.
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   HAMAP; MF_01653; MhpB; 1.
DR   InterPro; IPR023789; DHPP/DHXA_dioxygenase.
DR   InterPro; IPR004183; Xdiol_dOase_suB.
DR   Pfam; PF02900; LigB; 1.
PE   1: Evidence at protein level;
KW   Aromatic hydrocarbons catabolism; Dioxygenase; Iron; Oxidoreductase.
FT   CHAIN           1..321
FT                   /note="2,3-dihydroxyphenylpropionate/2,3-dihydroxicinnamic
FT                   acid 1,2-dioxygenase"
FT                   /id="PRO_0000337647"
FT   ACT_SITE        123
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        189
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   321 AA;  34366 MW;  6FC238E939E5CF64 CRC64;
     MSGSAIATAR RAFLGMSHSP LLGLNPVAAD DQIAIDKAIA AARAAVHEFA PELIVLLGPD
     HYNGFFNELM PPFCIGSQAT AVGDYLSPAG PLNVAGELAI ALADHLMDRH FDIAVSRRML
     VDHGFSQALQ FLWGDEMDTP PVIPIFMNAV AQPGIARMAR CKALGEGVGS FLDQLPLRTL
     LIGSGGLSHE PPVPTLAHPD PAVRERITVR STPTEQEREL KTERVKAAGL ALAHGDSWMK
     PLNPEWDLQW MDAMASGQLD GLCAMNEASI GAMAGNSAHE SKTWLVARSA LPANTRLSCP
     VRAYRAIPSL IAGYGVMFMH H