ID   MHPB_RHOSO              Reviewed;         314 AA.
AC   Q9KH19;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   25-MAY-2022, entry version 63.
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; Synonyms=ohpD;
OS   Rhodococcus sp.
OC   Bacteria; Actinobacteria; Corynebacteriales; Nocardiaceae; Rhodococcus.
OX   NCBI_TaxID=1831;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], CATALYTIC ACTIVITY, AND
RP   BIOPHYSICOCHEMICAL PROPERTIES.
RC   STRAIN=ATCC 19070 / V49;
RX   PubMed=10068799; DOI=10.1023/a:1001784702230;
RA   Powell J.A., Archer J.A.;
RT   "Molecular characterisation of a Rhodococcus ohp operon.";
RL   Antonie Van Leeuwenhoek 74:175-188(1998).
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. Also catalyzes the cleavage of
CC       catechol.
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:0000269|PubMed:10068799};
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:0000269|PubMed:10068799};
CC   -!- COFACTOR:
CC       Name=Fe(2+); Xref=ChEBI:CHEBI:29033; Evidence={ECO:0000250};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=30 uM for 3-(2,3-dihydroxyphenyl) propionic acid (at pH 8.1 and 8
CC         degrees Celsius) {ECO:0000269|PubMed:10068799};
CC         KM=47 uM for catechol (at pH 8.1 and 8 degrees Celsius)
CC         {ECO:0000269|PubMed:10068799};
CC         KM=62 uM for 3-methylcatechol (at pH 8.1 and 8 degrees Celsius)
CC         {ECO:0000269|PubMed:10068799};
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; AF274045; AAF81826.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q9KH19; -.
DR   SMR; Q9KH19; -.
DR   SABIO-RK; Q9KH19; -.
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   1: Evidence at protein level;
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_0000337667"
FT   ACT_SITE        115
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        179
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   314 AA;  33916 MW;  C919C10770527E64 CRC64;
     MPVALCAMSH SPLMGRNDPE QEVIDAVDAA FDHARRFVAD FAPDLIVIFA PDHYNGVFYD
     LLPPFCIGAA AQSVGDYGTE AGPLDVDRDA AYAVARDVLD SGIDVAFSER MHVDHGFAQA
     LQLLVGSITA VPTVPIFINS VAEPLGPVSR VRLLGEAVGR AAAKLDKRVL FVGSGGLSHD
     PPVPQFATAP EEVRERLIDG RNPSAAERDA REQRVITAGR DFAAGTAAIQ PLNPEWDRHL
     LDVLASGDLE QIDAWTNDWF VEQAGHSSHE VRTWIAAYAA MSAAGKYRVT STFYREIHEW
     IAGFGITTAV AVDE