PRCA_EMENI
ID PRCA_EMENI Reviewed; 313 AA.
AC Q5AT14; A0A1U8QZ97; C8VET7;
DT 29-SEP-2021, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 1.
DT 03-AUG-2022, entry version 83.
DE RecName: Full=Intradiol ring-cleavage dioxygenase prcA {ECO:0000303|PubMed:25479309};
DE EC=1.13.11.3 {ECO:0000305|PubMed:25479309};
DE AltName: Full=Protocatechuate 3,4-dioxygenase A {ECO:0000303|PubMed:25479309};
GN ORFNames=AN8566, ANIA_08566;
OS Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 /
OS M139) (Aspergillus nidulans).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Nidulantes.
OX NCBI_TaxID=227321;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=16372000; DOI=10.1038/nature04341;
RA Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S.,
RA Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V.,
RA Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S.,
RA Braus G.H., Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H.,
RA Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K.,
RA Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R.,
RA Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C.,
RA Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L.,
RA Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.;
RT "Sequencing of Aspergillus nidulans and comparative analysis with A.
RT fumigatus and A. oryzae.";
RL Nature 438:1105-1115(2005).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=19146970; DOI=10.1016/j.fgb.2008.12.003;
RA Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J.,
RA Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H.,
RA Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M.,
RA Estrada C.G., Geysens S., Goldman G., de Groot P.W., Hansen K.,
RA Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G.,
RA Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L.,
RA Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M.,
RA van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P.,
RA Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J.,
RA Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A.,
RA Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X.,
RA Robson G., Seiboth B., van Solingen P., Specht T., Sun J.,
RA Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H.,
RA van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y.,
RA Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J.,
RA Oliver S.G., Turner G.;
RT "The 2008 update of the Aspergillus nidulans genome annotation: a community
RT effort.";
RL Fungal Genet. Biol. 46:S2-13(2009).
RN [3]
RP FUNCTION, AND INDUCTION.
RX PubMed=25479309; DOI=10.1016/j.fgb.2014.11.002;
RA Martins T.M., Hartmann D.O., Planchon S., Martins I., Renaut J.,
RA Silva Pereira C.;
RT "The old 3-oxoadipate pathway revisited: new insights in the catabolism of
RT aromatics in the saprophytic fungus Aspergillus nidulans.";
RL Fungal Genet. Biol. 74:32-44(2015).
CC -!- FUNCTION: Intradiol ring-cleavage dioxygenase; part of the benzoic acid
CC degradation pathway also known as the protocatechuic acid pathway
CC (PubMed:25479309). Benzoic acid debradation begins with the conversion
CC of benzoic acid into 4-hydroxybenzoic acid through hydroxylation by the
CC benzoate-4-monooxygenase bphA, and its partner NADPH-cytochrome P450
CC reductase cprA which act as a mediator in electron donation from NADPH
CC (By 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 (Probable). 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 (Probable). {ECO:0000250|UniProtKB:A2QTW5, ECO:0000269|PubMed:25479309,
CC ECO:0000305|PubMed:25479309}.
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:0000305|PubMed:25479309};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10085;
CC Evidence={ECO:0000305|PubMed:25479309};
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:0000250|UniProtKB:A2R1P9}.
CC -!- INDUCTION: Expression is up-regulated in the presence of benzoate.
CC {ECO:0000269|PubMed:25479309}.
CC -!- SIMILARITY: Belongs to the intradiol ring-cleavage dioxygenase family.
CC {ECO:0000305}.
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DR EMBL; AACD01000157; EAA66991.1; -; Genomic_DNA.
DR EMBL; BN001305; CBF80813.1; -; Genomic_DNA.
DR RefSeq; XP_681835.1; XM_676743.1.
DR SMR; Q5AT14; -.
DR STRING; 162425.CADANIAP00003060; -.
DR EnsemblFungi; CBF80813; CBF80813; ANIA_08566.
DR EnsemblFungi; EAA66991; EAA66991; AN8566.2.
DR GeneID; 2868682; -.
DR KEGG; ani:AN8566.2; -.
DR VEuPathDB; FungiDB:AN8566; -.
DR eggNOG; ENOG502SMA8; Eukaryota.
DR HOGENOM; CLU_046727_1_1_1; -.
DR InParanoid; Q5AT14; -.
DR OMA; YHPTAYS; -.
DR OrthoDB; 979452at2759; -.
DR Proteomes; UP000000560; Chromosome V.
DR Proteomes; UP000005890; Unassembled WGS sequence.
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: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 2: Evidence at transcript level;
KW Aromatic hydrocarbons catabolism; Dioxygenase; Iron; Metal-binding;
KW Oxidoreductase; Reference proteome.
FT CHAIN 1..313
FT /note="Intradiol ring-cleavage dioxygenase prcA"
FT /id="PRO_0000453619"
FT REGION 287..313
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 313 AA; 35189 MW; 421B7F5C362EBD66 CRC64;
MSTNPRFDPN FTPYVINSMG PKTPERARVI LGSLIRHIHD FAREVELTPA EWMLGVEFIN
SIGKISTPIR NECHRICDVI GLESLVDEIA NRIVTEQGLS PTSNVILGPF WSPNAPFREL
GDSIIQDPNP NGKVTFMHGV LRDMETGAPI AGAVLDIWQA SANGQYDFQD PNQSENNLRG
KFRSNEKGEF YWYCYHPTPY SLPTDGPAGV LLNLMDRSPM RPAHIHLMIT HPDYATVINQ
IYPSDDPHLD IDSVFAVKDD LVVDFKPKTD DPKAELDLEY NVKMALKKHH PNPNSAPPVS
SFERYNKAGK EKL
