PYRF_WICAN
ID PYRF_WICAN Reviewed; 267 AA.
AC P78724;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 03-AUG-2022, entry version 75.
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=URA3;
OS Wickerhamomyces anomalus (strain ATCC 8168 / CBS 5759 / DSM 6766 / JCM 3585
OS / IAM 12210 / NCYC 432 / NBRC 10213 / NRRL Y-366 / AJ 5027) (Yeast) (Pichia
OS anomala).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Phaffomycetaceae; Wickerhamomyces.
OX NCBI_TaxID=885923;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 8168 / CBS 5759 / DSM 6766 / JCM 3585 / IAM 12210 / NCYC 432 /
RC NBRC 10213 / NRRL Y-366 / AJ 5027;
RA Perez J.A., Rodriguez J., Ruiz T., Rodriguez L.;
RL Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
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; Y09221; CAA70421.1; -; Genomic_DNA.
DR AlphaFoldDB; P78724; -.
DR SMR; P78724; -.
DR UniPathway; UPA00070; UER00120.
DR GO; GO:0004590; F:orotidine-5'-phosphate decarboxylase activity; IEA:UniProtKB-EC.
DR GO; GO:0006207; P:'de novo' pyrimidine nucleobase biosynthetic process; IEA:InterPro.
DR GO; GO:0044205; P:'de novo' UMP biosynthetic process; IEA:UniProtKB-UniPathway.
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.
FT CHAIN 1..267
FT /note="Orotidine 5'-phosphate decarboxylase"
FT /id="PRO_0000134661"
FT ACT_SITE 94
FT /note="Proton donor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10110"
FT BINDING 38
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 60..62
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 92..101
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 218
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 236
FT /ligand="substrate"
FT /evidence="ECO:0000250"
SQ SEQUENCE 267 AA; 29152 MW; A0F416956D8355FB CRC64;
MVQTLTYPQR AEAHPSPLAK RLFGVMESKK SNLCASIDVR TTKEFLELVD TLGPYICLVK
THIDIIDDFS IEGTIEPLKK LASKHNFLIF EDRKFADIGN TVKAQYSGGA FKIATWSDIT
NAHGVTGEGI VRGLKEAASE VSQEPRGLLM LAELSSKGSL AKGEYTKQTV DIAKTDKDFV
IGFIAQNDMG GRDEGFDWLI MTPGVGLDDK GDGLGQQYRS VSEVVAGGSD IIIVGRGLFG
KGRDPKVEGE RYRSAGWNAY LKRTSQI
