ID   GRAB_RHIS5              Reviewed;         295 AA.
AC   A1IIX3;
DT   23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   03-AUG-2022, entry version 40.
DE   RecName: Full=Hydroxyquinol 1,2-dioxygenase {ECO:0000303|PubMed:17158677};
DE            EC=1.13.11.37 {ECO:0000269|PubMed:17158677};
GN   Name=graB {ECO:0000303|PubMed:17158677};
OS   Rhizobium sp. (strain MTP-10005).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium.
OX   NCBI_TaxID=267998;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, AND
RP   INDUCTION.
RC   STRAIN=MTP-10005;
RX   PubMed=17158677; DOI=10.1128/jb.01675-06;
RA   Yoshida M., Oikawa T., Obata H., Abe K., Mihara H., Esaki N.;
RT   "Biochemical and genetic analysis of the gamma-resorcylate (2,6-
RT   dihydroxybenzoate) catabolic pathway in Rhizobium sp. strain MTP-10005:
RT   identification and functional analysis of its gene cluster.";
RL   J. Bacteriol. 189:1573-1581(2007).
CC   -!- FUNCTION: Involved in the gamma-resorcylate (2,6-dihydroxybenzoate)
CC       catabolism (PubMed:17158677). Catalyzes the conversion of hydroxyquinol
CC       to malelylacetate (PubMed:17158677). {ECO:0000269|PubMed:17158677}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=benzene-1,2,4-triol + O2 = 2 H(+) + maleylacetate;
CC         Xref=Rhea:RHEA:35595, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC         ChEBI:CHEBI:16468, ChEBI:CHEBI:16971; EC=1.13.11.37;
CC         Evidence={ECO:0000269|PubMed:17158677};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:35596;
CC         Evidence={ECO:0000269|PubMed:17158677};
CC   -!- COFACTOR:
CC       Name=Fe(3+); Xref=ChEBI:CHEBI:29034;
CC         Evidence={ECO:0000250|UniProtKB:Q5PXQ6};
CC       Note=Binds 1 Fe(3+) ion per subunit. {ECO:0000250|UniProtKB:Q5PXQ6};
CC   -!- PATHWAY: Aromatic compound metabolism. {ECO:0000305}.
CC   -!- INDUCTION: Induced in the presence of gamma-resorcylate.
CC       {ECO:0000269|PubMed:17158677}.
CC   -!- SIMILARITY: Belongs to the intradiol ring-cleavage dioxygenase family.
CC       {ECO:0000305}.
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DR   EMBL; AB266211; BAF44523.1; -; Genomic_DNA.
DR   BioCyc; MetaCyc:MON-19793; -.
DR   GO; GO:0018576; F:catechol 1,2-dioxygenase activity; IEA:InterPro.
DR   GO; GO:0008199; F:ferric iron binding; IEA:InterPro.
DR   GO; GO:0009712; P:catechol-containing compound metabolic process; IEA:InterPro.
DR   CDD; cd03461; 1_2-HQD; 1.
DR   Gene3D; 2.60.130.10; -; 1.
DR   InterPro; IPR039390; 1_2-HQD/HQD.
DR   InterPro; IPR007535; Catechol_dOase_N.
DR   InterPro; IPR000627; Intradiol_dOase_C.
DR   InterPro; IPR015889; Intradiol_dOase_core.
DR   Pfam; PF00775; Dioxygenase_C; 1.
DR   Pfam; PF04444; Dioxygenase_N; 1.
DR   SUPFAM; SSF49482; SSF49482; 1.
DR   PROSITE; PS00083; INTRADIOL_DIOXYGENAS; 1.
PE   1: Evidence at protein level;
KW   Dioxygenase; Iron; Metal-binding; Oxidoreductase.
FT   CHAIN           1..295
FT                   /note="Hydroxyquinol 1,2-dioxygenase"
FT                   /id="PRO_0000454491"
FT   BINDING         165
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000250|UniProtKB:Q5PXQ6"
FT   BINDING         200
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000250|UniProtKB:Q5PXQ6"
FT   BINDING         224
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000250|UniProtKB:Q5PXQ6"
FT   BINDING         226
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000250|UniProtKB:Q5PXQ6"
SQ   SEQUENCE   295 AA;  33350 MW;  AB3A508BCC3C9222 CRC64;
     MDMKTTGDDG YFVEERSAET VIARMRDCDD PRLKEIMAVV TRKLHEAVKE IEPTEEEWMK
     AIHFLTEVGQ ICNEWRQEWI LFSDILGVSM LVDAINHRKP SGASESTVLG PFHVADAPEM
     PMGANICLDG KGEDMLVTGR ILDTDGVPVA GARIDVWQAN DEGFYDVQQK GIQPDFNLRG
     VFVTGEDGRY WFRAAKPKYY PIPDDGPVGQ LLRAMGRHPY RPAHLHYIVS AEGFTTLVTH
     IFDPDDPYIR SDAVFGVKES LLADFQRVED AQRAQELGFA NGWFWSVDHD FVLAR