ID   NPCC_RHOOP              Reviewed;         300 AA.
AC   Q6F4M7;
DT   29-MAY-2013, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   03-AUG-2022, entry version 52.
DE   RecName: Full=Hydroxyquinol 1,2-dioxygenase;
DE            EC=1.13.11.37 {ECO:0000250|UniProtKB:Q5PXQ6};
GN   Name=npcC;
OS   Rhodococcus opacus (Nocardia opaca).
OC   Bacteria; Actinobacteria; Corynebacteriales; Nocardiaceae; Rhodococcus.
OX   NCBI_TaxID=37919;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, DISRUPTION PHENOTYPE,
RP   INDUCTION, AND NOMENCLATURE.
RC   STRAIN=SAO101;
RX   PubMed=15262926; DOI=10.1128/jb.186.15.4894-4902.2004;
RA   Kitagawa W., Kimura N., Kamagata Y.;
RT   "A novel p-nitrophenol degradation gene cluster from a gram-positive
RT   bacterium, Rhodococcus opacus SAO101.";
RL   J. Bacteriol. 186:4894-4902(2004).
CC   -!- FUNCTION: Involved in the degradation of para-nitrophenol (4-NP).
CC       Catalyzes the conversion of hydroxyquinol to malelylacetate.
CC       {ECO:0000269|PubMed:15262926}.
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:0000250|UniProtKB:Q5PXQ6};
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.
CC   -!- PATHWAY: Xenobiotic degradation.
CC   -!- INDUCTION: By 4-NP. {ECO:0000269|PubMed:15262926}.
CC   -!- DISRUPTION PHENOTYPE: Cells lacking this gene completely lose the
CC       ability to grow on 4-NP, 4-NCA, and hydroxyquinol.
CC       {ECO:0000269|PubMed:15262926}.
CC   -!- SIMILARITY: Belongs to the intradiol ring-cleavage dioxygenase family.
CC       {ECO:0000305}.
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DR   EMBL; AB154422; BAD30043.1; -; Genomic_DNA.
DR   RefSeq; WP_007295638.1; NZ_CP051855.1.
DR   AlphaFoldDB; Q6F4M7; -.
DR   SMR; Q6F4M7; -.
DR   BioCyc; MetaCyc:MON-13015; -.
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:0019439; P:aromatic compound catabolic process; IEA:UniProtKB-KW.
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   2: Evidence at transcript level;
KW   Aromatic hydrocarbons catabolism; Dioxygenase; Iron; Metal-binding;
KW   Oxidoreductase.
FT   CHAIN           1..300
FT                   /note="Hydroxyquinol 1,2-dioxygenase"
FT                   /id="PRO_0000422329"
FT   BINDING         167
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   300 AA;  33199 MW;  76C76AFB56AAFC81 CRC64;
     MHTTDTETFE EQFAIEQRLV DSVVASFDST TDPRLKELMQ SLTRHLHAFI REVRLSEDEW
     SNAIAFLTAV GNITDDRRQE FILLSDVLGV SMQTIAVSNP AYEDATESTV FGPFFVEDAP
     EVTLGGDIAG GATGQPCWIE GTVTDTAGNP VPEARIEVWQ NDEDGFYDVQ YSDGRVSGRA
     HLFSDAHGRY RFWGMTPVPY PIPSDGPVGK MLAATNRSPM RVAHLHFMVT ADGLRTLVTH
     IFVAGDPQLE RGDSVFGVKD SLIKDFVEQP PGTPTPDGRH IGDRNWARCE FDIVLAPEQI