HQDA_ASPNC
ID HQDA_ASPNC Reviewed; 329 AA.
AC A2QAP8;
DT 29-SEP-2021, integrated into UniProtKB/Swiss-Prot.
DT 06-MAR-2007, sequence version 1.
DT 03-AUG-2022, entry version 67.
DE RecName: Full=Intradiol ring-cleavage dioxygenase hqdA {ECO:0000303|Ref.2};
DE EC=1.13.11.- {ECO:0000269|Ref.2};
DE EC=1.13.11.1 {ECO:0000269|Ref.2};
GN Name=hqdA {ECO:0000303|Ref.2}; ORFNames=An01g12310;
OS Aspergillus niger (strain CBS 513.88 / FGSC A1513).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=425011;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 513.88 / FGSC A1513 / ATCC MYA-4892;
RX PubMed=17259976; DOI=10.1038/nbt1282;
RA Pel H.J., de Winde J.H., Archer D.B., Dyer P.S., Hofmann G., Schaap P.J.,
RA Turner G., de Vries R.P., Albang R., Albermann K., Andersen M.R.,
RA Bendtsen J.D., Benen J.A.E., van den Berg M., Breestraat S., Caddick M.X.,
RA Contreras R., Cornell M., Coutinho P.M., Danchin E.G.J., Debets A.J.M.,
RA Dekker P., van Dijck P.W.M., van Dijk A., Dijkhuizen L., Driessen A.J.M.,
RA d'Enfert C., Geysens S., Goosen C., Groot G.S.P., de Groot P.W.J.,
RA Guillemette T., Henrissat B., Herweijer M., van den Hombergh J.P.T.W.,
RA van den Hondel C.A.M.J.J., van der Heijden R.T.J.M., van der Kaaij R.M.,
RA Klis F.M., Kools H.J., Kubicek C.P., van Kuyk P.A., Lauber J., Lu X.,
RA van der Maarel M.J.E.C., Meulenberg R., Menke H., Mortimer M.A.,
RA Nielsen J., Oliver S.G., Olsthoorn M., Pal K., van Peij N.N.M.E.,
RA Ram A.F.J., Rinas U., Roubos J.A., Sagt C.M.J., Schmoll M., Sun J.,
RA Ussery D., Varga J., Vervecken W., van de Vondervoort P.J.J., Wedler H.,
RA Woesten H.A.B., Zeng A.-P., van Ooyen A.J.J., Visser J., Stam H.;
RT "Genome sequencing and analysis of the versatile cell factory Aspergillus
RT niger CBS 513.88.";
RL Nat. Biotechnol. 25:221-231(2007).
RN [2]
RP INDUCTION, FUNCTION, DISRUPTION PHENOTYPE, CATALYTIC ACTIVITY, AND SUBUNIT.
RX DOI=10.1021/acssuschemeng.9b04918;
RA Lubbers R.J.M., Dilokpimol A., Peng M., Visser J., Makela M.R.,
RA Hilden K.S., de Vries R.P.;
RT "Discovery of novel p-hydroxybenzoate-m-hydroxylase, protocatechuate 3,4
RT ring-cleavage dioxygenase, and hydroxyquinol 1,2 ring-cleavage dioxygenase
RT from the filamentous fungus Aspergillus niger.";
RL ACS Sustain. Chem. Eng. 7:19081-19089(2019).
CC -!- FUNCTION: Intradiol ring-cleavage dioxygenase involved in an
CC alternative pathway to the protocatechuic acid pathway since it is
CC active on hydroxyquinol and catechol but not on protocatechuic acid.
CC {ECO:0000269|Ref.2}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=catechol + O2 = cis,cis-muconate + 2 H(+);
CC Xref=Rhea:RHEA:23852, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:18135, ChEBI:CHEBI:32379; EC=1.13.11.1;
CC Evidence={ECO:0000269|Ref.2};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:23853;
CC Evidence={ECO:0000269|Ref.2};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=benzene-1,2,4-triol + O2 = 3-hydroxy-cis,cis-muconate + 2
CC H(+); Xref=Rhea:RHEA:19441, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:16971, ChEBI:CHEBI:58139; Evidence={ECO:0000269|Ref.2};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19442;
CC Evidence={ECO:0000269|Ref.2};
CC -!- COFACTOR:
CC Name=Fe(3+); Xref=ChEBI:CHEBI:29034;
CC Evidence={ECO:0000250|UniProtKB:P86029};
CC Note=Binds 1 Fe(3+) ion per subunit. {ECO:0000250|UniProtKB:P86029};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|Ref.2}.
CC -!- INDUCTION: Expression is slightly induced in the presence of caffeic
CC acid, p-hydroxybenzoic acid and protocatechuic acid.
CC {ECO:0000269|Ref.2}.
CC -!- DISRUPTION PHENOTYPE: Leads to reduced growth on protocatechuic acid
CC and the accumulation of hydroxyquinol, when prcA is also deleted.
CC {ECO:0000269|Ref.2}.
CC -!- SIMILARITY: Belongs to the intradiol ring-cleavage dioxygenase family.
CC {ECO:0000305}.
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DR EMBL; AM269982; CAK44129.1; -; Genomic_DNA.
DR RefSeq; XP_001389637.1; XM_001389600.1.
DR SMR; A2QAP8; -.
DR PaxDb; A2QAP8; -.
DR EnsemblFungi; CAK44129; CAK44129; An01g12310.
DR GeneID; 4978318; -.
DR KEGG; ang:ANI_1_1660014; -.
DR VEuPathDB; FungiDB:An01g12310; -.
DR HOGENOM; CLU_046727_2_0_1; -.
DR Proteomes; UP000006706; Chromosome 2R.
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 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.
PE 1: Evidence at protein level;
KW Aromatic hydrocarbons catabolism; Dioxygenase; Iron; Metal-binding;
KW Oxidoreductase; Reference proteome.
FT CHAIN 1..329
FT /note="Intradiol ring-cleavage dioxygenase hqdA"
FT /id="PRO_0000453620"
FT BINDING 167
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250|UniProtKB:Q5PXQ6"
FT BINDING 201
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250|UniProtKB:Q5PXQ6"
FT BINDING 225
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250|UniProtKB:Q5PXQ6"
FT BINDING 227
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250|UniProtKB:Q5PXQ6"
SQ SEQUENCE 329 AA; 36652 MW; 1C5742D418FAEC01 CRC64;
MDPSKVKIPP MKDLTVDNIT ENVIRINSLC QDERLKYVLE RLVTHLHDFA RETRLSTDEW
MTGLRFLTEV GKICSDVRQE YILLSDILGL SILVDSIDHP KPPNSTEGTV LGPFHTHDAE
PLTPGASISH DPAGEPLLVV CTVKDTHGNP VSDVKIDIWE TDSTGHYDVQ YAGRDGPDGR
CIMTSDKEGV FWFKAITPVP YPIPHDGPVG KLLKLLGRHP YRPSHMHFMF EKGGFDHLIT
ALYLRNDPYE TSDAVFGVKD SLVVDIGKAG PEYAAKYGVS EDHALLTYDF VLVSDEETSE
LRARNSKEAL DKLGRKVKIV NGLPVPDLD
