PYRF_MUCCL
ID PYRF_MUCCL Reviewed; 265 AA.
AC P32431;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1993, sequence version 1.
DT 03-AUG-2022, entry version 83.
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;
OS Mucor circinelloides f. lusitanicus (Mucor racemosus var. lusitanicus).
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC Mucoromycetes; Mucorales; Mucorineae; Mucoraceae; Mucor.
OX NCBI_TaxID=29924;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 1216b / BCRC 32522 / CBS 277.49 / NRRL 3631;
RX PubMed=1628845; DOI=10.1016/0378-1119(92)90629-4;
RA Benito E.P., Diaz-Minguez J.M., Iturriaga E.A., Campuzano V., Eslava A.P.;
RT "Cloning and sequence analysis of the Mucor circinelloides pyrG gene
RT encoding orotidine-5'-monophosphate decarboxylase: use of pyrG for
RT homologous transformation.";
RL Gene 116:59-67(1992).
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; M69112; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; P32431; -.
DR SMR; P32431; -.
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..265
FT /note="Orotidine 5'-phosphate decarboxylase"
FT /id="PRO_0000134679"
FT ACT_SITE 93
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 91..100
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 213
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 232
FT /ligand="substrate"
FT /evidence="ECO:0000250"
SQ SEQUENCE 265 AA; 29514 MW; 10BF511627BCEA14 CRC64;
MNTYKTYSER GQQHPNACAR SLFELMERNE SNLSVAVDVT TKKELLSIAD AVGPFVCVLK
THIDIVEDFD HDLVAQLEQL AKKHDFLIFE DRKFADIGNT VKHQYANGIY KIASWSHITN
AHTVPGEGII KGLGEVGLPL GRGLLLLAEM SSKGALTKGS YTSESVEMAR RNKDFVFGFI
AQHKMNEHDD EDFVVMSPGV GLDVKGDGLG QQYRTPHEVI VESGGDIIIV GRGIYGNPDQ
VEAQAKRYRQ AGWDAYLERV RLHKK
