PRCA_ASPNC
ID PRCA_ASPNC Reviewed; 315 AA.
AC A2R1P9;
DT 29-SEP-2021, integrated into UniProtKB/Swiss-Prot.
DT 06-MAR-2007, sequence version 1.
DT 03-AUG-2022, entry version 69.
DE RecName: Full=Intradiol ring-cleavage dioxygenase prcA {ECO:0000303|Ref.2};
DE EC=1.13.11.3 {ECO:0000269|Ref.2};
DE AltName: Full=Protocatechuate 3,4-dioxygenase A {ECO:0000303|Ref.2};
GN Name=prcA {ECO:0000303|Ref.2}; ORFNames=An13g02000;
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; part of the benzoic acid
CC degradation pathway also known as the protocatechuic acid pathway
CC (Ref.2). Benzoic acid debradation begins with the conversion of benzoic
CC acid into 4-hydroxybenzoic acid through hydroxylation by the benzoate-
CC 4-monooxygenase bphA, and its partner NADPH-cytochrome P450 reductase
CC cprA which act as a mediator in electron donation from NADPH (By
CC similarity). 4-Hydroxybenzoic acid is then converted into 3,4-
CC dihydroxybenzoic acid (also called protocatechuic acid) by the p-
CC hydroxybenzoate-m-hydroxylase phhA (Ref.2). Protocatechuic acid is
CC converted into 3-carboxy-cis,cis-muconic acid by the intradiol ring-
CC cleavage dioxygenase prcA, which is further metabolized through the 3-
CC oxoadipate pathway to finally enter the tricarboxylic acid cycle (TCA)
CC (Ref.2). {ECO:0000250|UniProtKB:A2QTW5, ECO:0000269|Ref.2}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3,4-dihydroxybenzoate + O2 = 3-carboxy-cis,cis-muconate + 2
CC H(+); Xref=Rhea:RHEA:10084, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:36241, ChEBI:CHEBI:57496; EC=1.13.11.3;
CC Evidence={ECO:0000269|Ref.2};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10085;
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 induced in the presence of caffeic acid, p-
CC coumaric acid, p-hydroxybenzoic acid, protocatechuic acid, and benzoic
CC acid. {ECO:0000269|Ref.2}.
CC -!- DISRUPTION PHENOTYPE: Abolishes growth on benzoic acid, benzaldehyde,
CC benzyl alcohol, p-anisic acid, p-anisyl alcohol, m-hydroxybenzoic acid
CC and p-hydroxybenzoic acid; and reduces growth on p-coumaric acid,
CC cinnamic acid, protocatechuic acid, p-coumaric acid, and caffeic acid.
CC {ECO:0000269|Ref.2}.
CC -!- SIMILARITY: Belongs to the intradiol ring-cleavage dioxygenase family.
CC {ECO:0000305}.
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DR EMBL; AM270300; CAK41599.1; -; Genomic_DNA.
DR RefSeq; XP_001396338.1; XM_001396301.1.
DR SMR; A2R1P9; -.
DR PaxDb; A2R1P9; -.
DR EnsemblFungi; CAK41599; CAK41599; An13g02000.
DR GeneID; 4986648; -.
DR KEGG; ang:ANI_1_272114; -.
DR VEuPathDB; FungiDB:An13g02000; -.
DR HOGENOM; CLU_046727_1_1_1; -.
DR Proteomes; UP000006706; Chromosome 2L.
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:0018578; F:protocatechuate 3,4-dioxygenase activity; IEA:RHEA.
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.
PE 1: Evidence at protein level;
KW Aromatic hydrocarbons catabolism; Dioxygenase; Iron; Metal-binding;
KW Oxidoreductase; Reference proteome.
FT CHAIN 1..315
FT /note="Intradiol ring-cleavage dioxygenase prcA"
FT /id="PRO_0000453618"
FT REGION 287..315
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 166
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 315 AA; 35321 MW; F0BAF8549F136830 CRC64;
MSTNRRFDPN FTPYVVNSMG PKTPERARVV LGALIRHIHD FAREVELTSA EWMLGVEFIN
SIGKISTPIR NECHRICDVI GLESLVDEIA NKIVTEDGVS PTSNVILGPF WSPNAPFREL
GDSIIQDPNP NGKVTYMHGV LKDMETGAPI VGAVLDIWQA SANGQYDFQD PNQSENNLRG
KFRSNEKGEF NWYCYHPTPY SLPTDGPAGV LLNLMDRSPM RPAHIHLMIT HPDYATVINQ
IYPSDDPHLD IDSVFAVKDD LVVDFKPKTD DPKAQLDLEY NVTMALKKHH PNPNSAPPVS
SFERFNKASK TQEKL
