ID   HXQD1_CORGL             Reviewed;         295 AA.
AC   Q8NR92; Q6M613;
DT   23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   03-AUG-2022, entry version 121.
DE   RecName: Full=Hydroxyquinol 1,2-dioxygenase {ECO:0000303|Ref.2};
DE            EC=1.13.11.37 {ECO:0000269|PubMed:16963551, ECO:0000269|Ref.2};
GN   OrderedLocusNames=Cgl1160 {ECO:0000312|EMBL:BAB98553.1};
OS   Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / BCRC 11384 /
OS   JCM 1318 / LMG 3730 / NCIMB 10025).
OC   Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae;
OC   Corynebacterium.
OX   NCBI_TaxID=196627;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC   10025;
RX   PubMed=12743753; DOI=10.1007/s00253-003-1328-1;
RA   Ikeda M., Nakagawa S.;
RT   "The Corynebacterium glutamicum genome: features and impacts on
RT   biotechnological processes.";
RL   Appl. Microbiol. Biotechnol. 62:99-109(2003).
RN   [2]
RP   FUNCTION, AND CATALYTIC ACTIVITY.
RX   DOI=10.1264/jsme2.20.160;
RA   Shen X.H., Huang Y., Liu S.J.;
RT   "Genomic analysis and identification of catabolic pathways for aromatic
RT   compounds in Corynebacterium glutamicum.";
RL   Microbes Environ. 20:160-167(2005).
RN   [3]
RP   FUNCTION, AND CATALYTIC ACTIVITY.
RC   STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC   10025;
RX   PubMed=16963551; DOI=10.1128/aem.01494-06;
RA   Huang Y., Zhao K.X., Shen X.H., Chaudhry M.T., Jiang C.Y., Liu S.J.;
RT   "Genetic characterization of the resorcinol catabolic pathway in
RT   Corynebacterium glutamicum.";
RL   Appl. Environ. Microbiol. 72:7238-7245(2006).
CC   -!- FUNCTION: Involved in resorcinol degradation (Ref.2, PubMed:16963551).
CC       Catalyzes the conversion of hydroxyquinol to malelylacetate (Ref.2,
CC       PubMed:16963551). Shows also weak activity with catechol, 3-
CC       methylcatechol and 4-methylcatechol, but cannot use 4-chlorocatechol,
CC       4-nitrocatechol or protocatechuate (Ref.2).
CC       {ECO:0000269|PubMed:16963551, ECO:0000269|Ref.2}.
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:16963551, ECO:0000269|Ref.2};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:35596;
CC         Evidence={ECO:0000269|PubMed:16963551, ECO:0000269|Ref.2};
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   -!- SIMILARITY: Belongs to the intradiol ring-cleavage dioxygenase family.
CC       {ECO:0000305}.
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DR   EMBL; BA000036; BAB98553.1; -; Genomic_DNA.
DR   RefSeq; NP_600386.1; NC_003450.3.
DR   RefSeq; WP_003854925.1; NC_006958.1.
DR   STRING; 196627.cg1311; -.
DR   GeneID; 58309980; -.
DR   KEGG; cgl:Cgl1160; -.
DR   PATRIC; fig|196627.13.peg.1137; -.
DR   eggNOG; COG3485; Bacteria.
DR   HOGENOM; CLU_046727_1_1_11; -.
DR   OMA; PWHLMTY; -.
DR   BioCyc; MetaCyc:G18NG-10732-MON; -.
DR   Proteomes; UP000000582; Chromosome.
DR   GO; GO:0047074; F:4-hydroxycatechol 1,2-dioxygenase activity; IEA:RHEA.
DR   GO; GO:0018576; F:catechol 1,2-dioxygenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008199; F:ferric iron binding; IEA:InterPro.
DR   GO; GO:0009712; P:catechol-containing compound metabolic process; IEA:InterPro.
DR   Gene3D; 2.60.130.10; -; 1.
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; Reference proteome.
FT   CHAIN           1..295
FT                   /note="Hydroxyquinol 1,2-dioxygenase"
FT                   /id="PRO_0000454474"
FT   BINDING         162
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000250|UniProtKB:Q5PXQ6"
FT   BINDING         195
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000250|UniProtKB:Q5PXQ6"
FT   BINDING         219
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000250|UniProtKB:Q5PXQ6"
FT   BINDING         221
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000250|UniProtKB:Q5PXQ6"
SQ   SEQUENCE   295 AA;  32774 MW;  19A9A2B5D37DFD17 CRC64;
     MTISAQQQAV EEDLVERVLA SFDSCENPRL KLVMKSLTVH LHDFIRDVRL TEEEWNYAID
     FLTKVGHITD DKRQEFVLLS DTLGASMQTI AVNNEAYEDA TEATVFGPFF VDDAPLVQNG
     DDIAFGAVGQ PAWVEGTVKD TEGNPIPNAR IEVWECDEDG LYDVQYADER SAGRAHLYSD
     ENGEYHFWGL TPVPYPIPHD GPVGQMLQAV GRSPVRCAHL HFMVTAPEKR TLVTHIFVEG
     DPQLEIGDSV FGVKDSLIKK FVEQPAGTAT PDGRDVGDQT WARTRFDIVL APGNV