HXQD2_CORGL
ID HXQD2_CORGL Reviewed; 301 AA.
AC Q8NL92; Q6M1G2;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Hydroxyquinol 1,2-dioxygenase {ECO:0000303|Ref.2};
DE EC=1.13.11.37 {ECO:0000269|Ref.2};
GN OrderedLocusNames=Cgl3056 {ECO:0000312|EMBL:BAC00450.1};
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).
CC -!- FUNCTION: Involved in resorcinol degradation (Ref.2). Catalyzes the
CC conversion of hydroxyquinol to malelylacetate (Ref.2). Shows also weak
CC activity with catechol, 3-methylcatechol and 4-methylcatechol, but
CC cannot use 4-chlorocatechol, 4-nitrocatechol or protocatechuate
CC (Ref.2). {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|Ref.2};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:35596;
CC Evidence={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; BAC00450.1; -; Genomic_DNA.
DR RefSeq; NP_602248.1; NC_003450.3.
DR RefSeq; WP_011015596.1; NC_006958.1.
DR STRING; 196627.cg3385; -.
DR KEGG; cgl:Cgl3056; -.
DR PATRIC; fig|196627.13.peg.2988; -.
DR eggNOG; COG3485; Bacteria.
DR HOGENOM; CLU_046727_1_1_11; -.
DR OMA; MPAGDSM; -.
DR BioCyc; MetaCyc:G18NG-12677-MON; -.
DR Proteomes; UP000000582; Chromosome.
DR GO; GO:0047074; F:4-hydroxycatechol 1,2-dioxygenase activity; IEA:UniProtKB-EC.
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:0018581; F:hydroxyquinol 1,2-dioxygenase activity; IEA:UniProtKB-EC.
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..301
FT /note="Hydroxyquinol 1,2-dioxygenase"
FT /id="PRO_0000454475"
FT BINDING 169
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250|UniProtKB:Q5PXQ6"
FT BINDING 202
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"
FT BINDING 228
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250|UniProtKB:Q5PXQ6"
SQ SEQUENCE 301 AA; 33291 MW; 933623AD2C44EBF3 CRC64;
MTTTTADHNI SAQQKAVEEN LVNRVLQSFD ACENPRLKQL MESLVVHLHD FIRDVRLTED
EWNYAIDFLT AVGHITDDKR QEFVLLSDTL GASMQTIAVN NEAYENSTEA TVFGPFFLDD
APEVELGGDI AGGAQGQAAW IEGTVTDTEG NPVPNARIEV WECDEDGLYD VQYADERMAG
RAYMHTDANG DYRFWGLTPV PYPIPHDGPV GNMLKAVGRS PVRCAHLHFM VTAPELRTLV
THIFVEGDPQ LEIGDSVFGV KDSLIKKFEE QAPGTPTPDG RDLGDQTWAR TRFDIVLAPG
A