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 18-JUN-2025, entry version 88. 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; Pseudomonadati; Pseudomonadota; Betaproteobacteria; OC Burkholderiales; 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}. 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; 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-UniRule. DR CDD; cd07365; MhpB_like; 1. DR Gene3D; 3.40.830.10; LigB-like; 1. DR HAMAP; MF_01653; MhpB; 1. DR InterPro; IPR023789; DHPP/DHXA_dioxygenase. DR InterPro; IPR004183; Xdiol_dOase_suB. DR NCBIfam; NF009908; PRK13370.1-2; 1. DR NCBIfam; NF009910; PRK13370.1-4; 1. DR Pfam; PF02900; LigB; 1. DR SUPFAM; SSF53213; LigB-like; 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 //