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PYRF_EMENI
ID   PYRF_EMENI              Reviewed;         274 AA.
AC   P10652; C8V298; Q5AZX3;
DT   01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2007, sequence version 2.
DT   03-AUG-2022, entry version 133.
DE   RecName: Full=Orotidine 5'-phosphate decarboxylase;
DE            EC=4.1.1.23;
DE   AltName: Full=OMP decarboxylase;
DE            Short=OMPDCase;
DE            Short=OMPdecase;
DE   AltName: Full=Uridine 5'-monophosphate synthase;
DE            Short=UMP synthase;
GN   Name=pyrG; ORFNames=AN6157;
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 [GENOMIC DNA].
RX   PubMed=3328733; DOI=10.1016/0378-1119(87)90201-0;
RA   Oakley B.R., Rinehart J.E., Mitchell B.L., Oakley C.E., Carmona C.,
RA   Gray G.L., May G.S.;
RT   "Cloning, mapping and molecular analysis of the pyrG (orotidine-5'-
RT   phosphate decarboxylase) gene of Aspergillus nidulans.";
RL   Gene 61:385-399(1987).
RN   [2]
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   [3]
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).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H(+) + orotidine 5'-phosphate = CO2 + UMP;
CC         Xref=Rhea:RHEA:11596, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC         ChEBI:CHEBI:57538, ChEBI:CHEBI:57865; EC=4.1.1.23;
CC         Evidence={ECO:0000255|PROSITE-ProRule:PRU10110};
CC   -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo pathway;
CC       UMP from orotate: step 2/2.
CC   -!- SIMILARITY: Belongs to the OMP decarboxylase family. {ECO:0000305}.
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DR   EMBL; M19132; AAB66359.1; -; Genomic_DNA.
DR   EMBL; AACD01000105; EAA57943.1; -; Genomic_DNA.
DR   EMBL; BN001301; CBF70070.1; -; Genomic_DNA.
DR   PIR; A29630; DCASOE.
DR   RefSeq; XP_663761.1; XM_658669.1.
DR   AlphaFoldDB; P10652; -.
DR   SMR; P10652; -.
DR   STRING; 162425.CADANIAP00006853; -.
DR   EnsemblFungi; CBF70070; CBF70070; ANIA_06157.
DR   EnsemblFungi; EAA57943; EAA57943; AN6157.2.
DR   GeneID; 2870752; -.
DR   KEGG; ani:AN6157.2; -.
DR   VEuPathDB; FungiDB:AN6157; -.
DR   eggNOG; KOG1377; Eukaryota.
DR   HOGENOM; CLU_030821_0_0_1; -.
DR   InParanoid; P10652; -.
DR   OMA; KNFVMGF; -.
DR   OrthoDB; 1303452at2759; -.
DR   UniPathway; UPA00070; UER00120.
DR   Proteomes; UP000000560; Chromosome I.
DR   Proteomes; UP000005890; Unassembled WGS sequence.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0004590; F:orotidine-5'-phosphate decarboxylase activity; IMP:AspGD.
DR   GO; GO:0006207; P:'de novo' pyrimidine nucleobase biosynthetic process; IMP:AspGD.
DR   GO; GO:0044205; P:'de novo' UMP biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0000909; P:sporocarp development involved in sexual reproduction; IMP:AspGD.
DR   Gene3D; 3.20.20.70; -; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR014732; OMPdecase.
DR   InterPro; IPR018089; OMPdecase_AS.
DR   InterPro; IPR001754; OMPdeCOase_dom.
DR   InterPro; IPR011060; RibuloseP-bd_barrel.
DR   PANTHER; PTHR32119:SF2; PTHR32119:SF2; 1.
DR   Pfam; PF00215; OMPdecase; 1.
DR   SMART; SM00934; OMPdecase; 1.
DR   SUPFAM; SSF51366; SSF51366; 1.
DR   TIGRFAMs; TIGR01740; pyrF; 1.
DR   PROSITE; PS00156; OMPDECASE; 1.
PE   3: Inferred from homology;
KW   Decarboxylase; Lyase; Pyrimidine biosynthesis; Reference proteome.
FT   CHAIN           1..274
FT                   /note="Orotidine 5'-phosphate decarboxylase"
FT                   /id="PRO_0000134659"
FT   ACT_SITE        95
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10110"
FT   BINDING         40
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         62..64
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         93..102
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         227
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         245
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        169..170
FT                   /note="YT -> SQ (in Ref. 1; AAB66359)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   274 AA;  30102 MW;  9724A3EFC603E70A CRC64;
     MSSKSHLPYA IRATNHPNPL TSKLFSIAEE KKTNVTVSAD VTTSAELLDL ADRLGPYIAV
     LKTHIDILTD LTPSTLSSLQ SLATKHNFLI FEDRKFIDIG NTVQKQYHGG ALRISEWAHI
     INCAILPGEG IVEALAQTTK SPDFKDANQR GLLILAEMTS KGSLATGEYT ARSVEYARKY
     KGFVMGFVST RALSEVLPEQ KEESEDFVVF TTGVNLSDKG DKLGQQYQTP GSAVGRGADF
     IIAGRGIYKA DDPVEAVQRY REEGWKAYEK RVGL
 
 
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