PYRF_PICKU
ID PYRF_PICKU Reviewed; 262 AA.
AC Q6IUR4;
DT 31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 62.
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 Pichia kudriavzevii (Yeast) (Issatchenkia orientalis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Pichiaceae; Pichia.
OX NCBI_TaxID=4909;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Li Y., Shen W., Rao Z., Fang H., Zhuge J.;
RT "Isolation and sequence analysis of the gene URA3 encoding the orotidine-
RT 5'-monophosphate decarboxylase from the yeast Candida glycerinogenes.";
RL Submitted (MAY-2004) 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; AY623794; AAT39474.1; -; mRNA.
DR AlphaFoldDB; Q6IUR4; -.
DR SMR; Q6IUR4; -.
DR VEuPathDB; FungiDB:C5L36_0B05730; -.
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 2: Evidence at transcript level;
KW Decarboxylase; Lyase; Pyrimidine biosynthesis.
FT CHAIN 1..262
FT /note="Orotidine 5'-phosphate decarboxylase"
FT /id="PRO_0000134650"
FT ACT_SITE 91
FT /note="Proton donor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10110"
FT BINDING 35
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 57..59
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 89..98
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 215
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 233
FT /ligand="substrate"
FT /evidence="ECO:0000250"
SQ SEQUENCE 262 AA; 29130 MW; B0F0012C0A5B980A CRC64;
MASYKERSES HTSPVARRLF SIMEEKKSNL CASLDITETE KLLSILDTIG PYICLVKTHI
DIVSDFTYEG TVLPLKELAK KHNFMIFEDR KFADIGNTVK NQYKSGVFRI AEWADITNAH
GVTGAGIVSG LKEAAQETTS EPRGLLMLAE LSSKGSLAYG EYTEKTVEIA KSDKEFVIGF
IAQHDMGGRE EGFDWIIMTP GVGLDDKGDA LGQQYRTVDE VVKTGTDIII VGRGLYGQGR
DPIEQAKRYQ QAGWNAYLNR FK