ID   MHPB_MYCPA              Reviewed;         312 AA.
AC   Q742Z0;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   20-MAY-2008, sequence version 2.
DT   25-MAY-2022, entry version 92.
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}; OrderedLocusNames=MAP_0695;
OS   Mycolicibacterium paratuberculosis (strain ATCC BAA-968 / K-10)
OS   (Mycobacterium paratuberculosis).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium avium complex (MAC).
OX   NCBI_TaxID=262316;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-968 / K-10;
RX   PubMed=16116077; DOI=10.1073/pnas.0505662102;
RA   Li L., Bannantine J.P., Zhang Q., Amonsin A., May B.J., Alt D., Banerji N.,
RA   Kanjilal S., Kapur V.;
RT   "The complete genome sequence of Mycobacterium avium subspecies
RT   paratuberculosis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:12344-12349(2005).
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;
CC         Evidence={ECO:0000255|HAMAP-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=AAS03012.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AE016958; AAS03012.1; ALT_INIT; Genomic_DNA.
DR   AlphaFoldDB; Q742Z0; -.
DR   SMR; Q742Z0; -.
DR   STRING; 262316.MAP_0695; -.
DR   EnsemblBacteria; AAS03012; AAS03012; MAP_0695.
DR   KEGG; mpa:MAP_0695; -.
DR   eggNOG; COG3384; Bacteria.
DR   HOGENOM; CLU_078149_0_0_11; -.
DR   OMA; MDVDHGT; -.
DR   UniPathway; UPA00714; -.
DR   Proteomes; UP000000580; 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-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   3: Inferred from homology;
KW   Aromatic hydrocarbons catabolism; Dioxygenase; Iron; Oxidoreductase;
KW   Reference proteome.
FT   CHAIN           1..312
FT                   /note="2,3-dihydroxyphenylpropionate/2,3-dihydroxicinnamic
FT                   acid 1,2-dioxygenase"
FT                   /id="PRO_0000337654"
FT   ACT_SITE        115
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01653"
FT   ACT_SITE        179
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01653"
SQ   SEQUENCE   312 AA;  33150 MW;  49A3010C87232A85 CRC64;
     MALALCCMSH SPLLNLPGPS RDLLDDIDAA IARARGFVED YDPQLVVIFS PDHYNGFFYK
     VMPPFCIGSS ASGVGDYGTH AGPLDVPEKL AVDCAQAVLD AGVDIAVSAS MDVDHGTVQP
     LEKLFGTAIS RPVIPVFVNA IGVPLGPMHR CRALGAAVGT YLATLDKRVL VMGSGGLSHS
     PPVPTLATAP EPVLQRIVHG APMTAEQRQA RQAAVIDAAR SFAAGDSALQ PLNPTWDHRF
     LEIIDRGSLS ELDRWSNSFV THEGGGSAHE IRTWVAAFAA LQAAGPYETT MRYYTPAPEL
     IAGFAIRTAR PK