PYRF_ASPFU
ID PYRF_ASPFU Reviewed; 278 AA.
AC O13410; Q4X1Y3;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 125.
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=AFUA_2G08360;
OS Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC
OS A1100) (Aspergillus fumigatus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=330879;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=NIH 5233 / ATCC 13073;
RX PubMed=9618589; DOI=10.1007/s002940050350;
RA Weidner G., D'Enfert C., Koch A., Mol P.C., Brakhage A.A.;
RT "Development of a homologous transformation system for the human pathogenic
RT fungus Aspergillus fumigatus based on the pyrG gene encoding orotidine 5'-
RT monophosphate decarboxylase.";
RL Curr. Genet. 33:378-385(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100;
RX PubMed=16372009; DOI=10.1038/nature04332;
RA Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J.,
RA Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W., Bowyer P.,
RA Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.L.,
RA Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R., Fosker N.,
RA Fraser A., Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K.,
RA Griffith-Jones S., Gwilliam R., Haas B.J., Haas H., Harris D.E.,
RA Horiuchi H., Huang J., Humphray S., Jimenez J., Keller N., Khouri H.,
RA Kitamoto K., Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafton A.,
RA Latge J.-P., Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L.,
RA Mohamoud Y., Molina M., Monod M., Mouyna I., Mulligan S., Murphy L.D.,
RA O'Neil S., Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L.,
RA Quail M.A., Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U.,
RA Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M.,
RA Ronning C.M., Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C.,
RA Saunders D., Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F.,
RA Turner G., Vazquez de Aldana C.R., Weidman J., White O., Woodward J.R.,
RA Yu J.-H., Fraser C.M., Galagan J.E., Asai K., Machida M., Hall N.,
RA Barrell B.G., Denning D.W.;
RT "Genomic sequence of the pathogenic and allergenic filamentous fungus
RT Aspergillus fumigatus.";
RL Nature 438:1151-1156(2005).
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; Y11303; CAA72161.1; -; Genomic_DNA.
DR EMBL; AAHF01000001; EAL93132.1; -; Genomic_DNA.
DR RefSeq; XP_755170.1; XM_750077.1.
DR AlphaFoldDB; O13410; -.
DR SMR; O13410; -.
DR STRING; 746128.CADAFUBP00002374; -.
DR EnsemblFungi; EAL93132; EAL93132; AFUA_2G08360.
DR GeneID; 3513211; -.
DR KEGG; afm:AFUA_2G08360; -.
DR VEuPathDB; FungiDB:Afu2g08360; -.
DR eggNOG; KOG1377; Eukaryota.
DR HOGENOM; CLU_030821_0_0_1; -.
DR InParanoid; O13410; -.
DR OMA; KNFVMGF; -.
DR OrthoDB; 1303452at2759; -.
DR UniPathway; UPA00070; UER00120.
DR Proteomes; UP000002530; Chromosome 2.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0004590; F:orotidine-5'-phosphate decarboxylase activity; IBA:GO_Central.
DR GO; GO:0006207; P:'de novo' pyrimidine nucleobase biosynthetic process; IBA:GO_Central.
DR GO; GO:0044205; P:'de novo' UMP biosynthetic process; 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..278
FT /note="Orotidine 5'-phosphate decarboxylase"
FT /id="PRO_0000134641"
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 229
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 247
FT /ligand="substrate"
FT /evidence="ECO:0000250"
SQ SEQUENCE 278 AA; 30267 MW; F4CFF6703CFD0803 CRC64;
MSSKSQLTYG ARASKHPNPL AKRLFEIAEA KKTNVTVSAD VTTTRELLDL ADRLGPYIAV
IKTHIDILTD FSVDTINGLN VLAQKHNFLI FEDRKFIDIG NTVQKQYHGG ALRISEWAHI
INCSVLPGEG IVEALAQTAS AQDFPYGPER GLLVLAEMTS KGSLATGEYT KASVDYARKY
KNFVMGFVST RALTEVQSDV SSASEDEDFV VFTTGVNLSS KGDKLGQQYQ TPASAIGRGA
DFIIAGRGIY AAPDPVEAAQ RYQKEGWEAY MARVCGKS
