MHPB_CUPNE
ID MHPB_CUPNE Reviewed; 313 AA.
AC P17295;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1990, sequence version 1.
DT 25-MAY-2022, entry version 83.
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=mcpI;
OS Cupriavidus necator (Alcaligenes eutrophus) (Ralstonia eutropha).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Cupriavidus.
OX NCBI_TaxID=106590;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=JMP222;
RX PubMed=2356133; DOI=10.1093/nar/18.11.3405;
RA Kabisch M., Fortnagel P.;
RT "Nucleotide sequence of metapyrocatechase I (catechol 2,3-oxygenase I) gene
RT mpcI from Alcaligenes eutrophus JMP222.";
RL Nucleic Acids Res. 18:3405-3405(1990).
RN [2]
RP FUNCTION IN CATABOLISM OF 3-HYDROXY DERIVATIVES OF PHENYLPROPIONIC ACID,
RP COFACTOR, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=8752345; DOI=10.1128/jb.178.17.5249-5256.1996;
RA Spence E.L., Kawamukai M., Sanvoisin J., Braven H., Bugg T.D.H.;
RT "Catechol dioxygenases from Escherichia coli (MhpB) and Alcaligenes
RT eutrophus (MpcI): sequence analysis and biochemical properties of a third
RT family of extradiol dioxygenases.";
RL J. Bacteriol. 178:5249-5256(1996).
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. {ECO:0000269|PubMed:8752345}.
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;
CC Evidence={ECO:0000269|PubMed:8752345};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=7.1 uM for 2,3-dihydroxyphenylpropionic acid (at 20 degrees
CC Celsius and pH 8) {ECO:0000269|PubMed:8752345};
CC KM=14 uM for 2,3-dihydroxycinnamic acid (at 20 degrees Celsius and pH
CC 8) {ECO:0000269|PubMed:8752345};
CC KM=59 uM for 3-ethylcatechol (at 20 degrees Celsius and pH 8)
CC {ECO:0000269|PubMed:8752345};
CC KM=130 uM for 3-methylcatechol (at 20 degrees Celsius and pH 8)
CC {ECO:0000269|PubMed:8752345};
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}.
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DR EMBL; X52414; CAA36665.1; -; Genomic_DNA.
DR PIR; S10154; S10154.
DR AlphaFoldDB; P17295; -.
DR SMR; P17295; -.
DR SwissLipids; SLP:000001890; -.
DR SABIO-RK; P17295; -.
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..313
FT /note="2,3-dihydroxyphenylpropionate/2,3-dihydroxicinnamic
FT acid 1,2-dioxygenase"
FT /id="PRO_0000085102"
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 313 AA; 33143 MW; E1506B3785E9D0F9 CRC64;
MPIQLECLSH TPLHGYVDPA PEVVAEVERV QAAARDRVRA FDPELVVVFA PDHFNGFFYD
VMPPFCIGAA ATAIGDFKSL AGKLPVPADL ALSLAESVMA ADIDVALSHR MQVDHGCADA
LAALTGSLHR YPVIPVFINS VAPPMATLRR ARLLGDAVGR FLSRAGKRVL VVGSGGISHE
PPVPELAGAS EEVAERLIAG RNPSPESAAR QARTVAAAKS FVAGDSHLHP LNPEWDRAFL
SLLASGELTA VDGMTNDAIT RDGGKSAHEI RTWVAAFGAL AAYGPYRASL DFYRAIPEWI
AGFATMHAEP AAV
