ID   MHPB_MYCVP              Reviewed;         316 AA.
AC   A1TCX1;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   20-MAY-2008, sequence version 2.
DT   28-JAN-2026, entry version 96.
DE   RecName: Full=2,3-dihydroxyphenylpropionate/2,3-dihydroxicinnamic acid 1,2-dioxygenase {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 {ECO:0000255|HAMAP-Rule:MF_01653};
GN   Name=mhpB {ECO:0000255|HAMAP-Rule:MF_01653};
GN   OrderedLocusNames=Mvan_4244;
OS   Mycolicibacterium vanbaalenii (strain DSM 7251 / JCM 13017 / BCRC 16820 /
OS   KCTC 9966 / NRRL B-24157 / PYR-1) (Mycobacterium vanbaalenii).
OC   Bacteria; Bacillati; Actinomycetota; Actinomycetes; Mycobacteriales;
OC   Mycobacteriaceae; Mycolicibacterium.
OX   NCBI_TaxID=350058;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 7251 / JCM 13017 / BCRC 16820 / KCTC 9966 / NRRL B-24157 /
RC   PYR-1;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Singan V., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Anderson I.J., Miller C., Richardson P.;
RT   "Complete sequence of Mycobacterium vanbaalenii PYR-1.";
RL   Submitted (DEC-2006) 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; Evidence={ECO:0000255|HAMAP-
CC         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   -!- SEQUENCE CAUTION:
CC       Sequence=ABM15021.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; CP000511; ABM15021.1; ALT_INIT; Genomic_DNA.
DR   AlphaFoldDB; A1TCX1; -.
DR   SMR; A1TCX1; -.
DR   STRING; 350058.Mvan_4244; -.
DR   KEGG; mva:Mvan_4244; -.
DR   eggNOG; COG3384; Bacteria.
DR   HOGENOM; CLU_078149_0_0_11; -.
DR   UniPathway; UPA00714; -.
DR   Proteomes; UP000009159; Chromosome.
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; NF009910; PRK13370.1-4; 1.
DR   Pfam; PF02900; LigB; 1.
DR   SUPFAM; SSF53213; LigB-like; 1.
PE   3: Inferred from homology;
KW   Aromatic hydrocarbons catabolism; Dioxygenase; Iron; Oxidoreductase;
KW   Reference proteome.
FT   CHAIN           1..316
FT                   /note="2,3-dihydroxyphenylpropionate/2,3-dihydroxicinnamic
FT                   acid 1,2-dioxygenase"
FT                   /id="PRO_0000337660"
FT   ACT_SITE        118
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01653"
FT   ACT_SITE        182
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01653"
SQ   SEQUENCE   316 AA;  33277 MW;  E05DD6995015778B CRC64;
     MAKSQMALCC MSHSPLLNLP GPAQELLDDI EGAIAAAREF VAAFDPDLVV TFSPDHYNGF
     FYRAMPPFCV GTAAAGVGDY GTYQGPLDVP ADLAIDCARA VLDSDVDVAV SAAMDVDHGT
     VQPLQKLFGD ATAKPVIPVF VNSVATPLGP MRRVRALGAA VGTHLAGLGK RVLVIGSGGL
     SHDPPVPTLA TAPPAALDRI VRGVPMTTEQ RQARQAAVIE AAREFASGQG ALAPLNPDWD
     RAFLDLLDNG RLAEVDSWDN RWIAEQAGNS AHEVRTWVAA FAALAAQGKY ETGNRYYRAA
     PELIAGFAIR TAVCTS
//