ID   MHPB_AZOVD              Reviewed;         312 AA.
AC   C1DRI2;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   26-MAY-2009, sequence version 1.
DT   03-AUG-2022, entry version 65.
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=Avin_15050;
OS   Azotobacter vinelandii (strain DJ / ATCC BAA-1303).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Azotobacter.
OX   NCBI_TaxID=322710;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DJ / ATCC BAA-1303;
RX   PubMed=19429624; DOI=10.1128/jb.00504-09;
RA   Setubal J.C., Dos Santos P., Goldman B.S., Ertesvaag H., Espin G.,
RA   Rubio L.M., Valla S., Almeida N.F., Balasubramanian D., Cromes L.,
RA   Curatti L., Du Z., Godsy E., Goodner B., Hellner-Burris K., Hernandez J.A.,
RA   Houmiel K., Imperial J., Kennedy C., Larson T.J., Latreille P., Ligon L.S.,
RA   Lu J., Maerk M., Miller N.M., Norton S., O'Carroll I.P., Paulsen I.,
RA   Raulfs E.C., Roemer R., Rosser J., Segura D., Slater S., Stricklin S.L.,
RA   Studholme D.J., Sun J., Viana C.J., Wallin E., Wang B., Wheeler C., Zhu H.,
RA   Dean D.R., Dixon R., Wood D.;
RT   "Genome sequence of Azotobacter vinelandii, an obligate aerobe specialized
RT   to support diverse anaerobic metabolic processes.";
RL   J. Bacteriol. 191:4534-4545(2009).
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}.
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DR   EMBL; CP001157; ACO77720.1; -; Genomic_DNA.
DR   RefSeq; WP_012700136.1; NC_012560.1.
DR   AlphaFoldDB; C1DRI2; -.
DR   SMR; C1DRI2; -.
DR   STRING; 322710.Avin_15050; -.
DR   EnsemblBacteria; ACO77720; ACO77720; Avin_15050.
DR   KEGG; avn:Avin_15050; -.
DR   eggNOG; COG1355; Bacteria.
DR   HOGENOM; CLU_078149_0_0_6; -.
DR   OMA; MDVDHGT; -.
DR   OrthoDB; 1728007at2; -.
DR   UniPathway; UPA00714; -.
DR   Proteomes; UP000002424; 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   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   3: Inferred from homology;
KW   Aromatic hydrocarbons catabolism; Dioxygenase; Iron; Oxidoreductase.
FT   CHAIN           1..312
FT                   /note="2,3-dihydroxyphenylpropionate/2,3-dihydroxicinnamic
FT                   acid 1,2-dioxygenase"
FT                   /id="PRO_1000215852"
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;  33770 MW;  939E497D5C9ADAD4 CRC64;
     MTIKLKCLSH TPLRGLNDPG ADVVAEVDAV LARSRAEVEA FDPELIVIFA PDHYNGLFYD
     LMPPFVIATA AESVADYGTL PGPLSIPRDL ALDLTRHILD SGLDIALSHR LQVDHGCTQT
     LEELTGSLTR YPVIPIIINS VAPPFAPYRR IRKLGEAVGR FVASLGKRVL ILGTGGLSHE
     PPVPLLSGAA EEIAEFLIAG RNPTPEARAA RQARTIAAGK IYGTAESPLT PLNTDWDLAF
     IDLLVQGRLA EIDDFVVEEI STTAGRSTHE IRTWVAAFAA LAAGGAYRAR QDYYRPINEW
     IAGYGVVSAE RR