PYRF_RHIOR
ID PYRF_RHIOR Reviewed; 265 AA.
AC Q71HN5;
DT 31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 66.
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 Rhizopus oryzae (Mucormycosis agent) (Rhizopus arrhizus var. delemar).
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC Mucoromycetes; Mucorales; Mucorineae; Rhizopodaceae; Rhizopus.
OX NCBI_TaxID=64495;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 9363 / NRRL 395;
RX PubMed=12436261; DOI=10.1007/s00438-002-0760-8;
RA Skory C.D.;
RT "Homologous recombination and double-strand break repair in the
RT transformation of Rhizopus oryzae.";
RL Mol. Genet. Genomics 268:397-406(2002).
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; AF497632; AAN78311.1; -; Genomic_DNA.
DR AlphaFoldDB; Q71HN5; -.
DR SMR; Q71HN5; -.
DR OMA; KNFVMGF; -.
DR PhylomeDB; Q71HN5; -.
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_0000134677"
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; 29611 MW; 87FE1AA5900494FE CRC64;
MNTYKPYSER AKQHSNACAR SLLELMERKQ TNLSVAVDVT TKKELISIAD AIGPYICVLK
THIDIVEDFD ADLIQQLQEL AKKHDFLFFE DRKFADIGNT VKHQYANGIY KIASWSHITN
AHTVPGEGII KGLAEVGLPL GRGLLLLAEM SSKGALTKGS YTTDSVEMAR RNKDFVFGFI
AQNKMNQYDD EDFIVMSPGV GLDVKGDGLG QQYRTPREVI VESGADVIIV GRGIYGQPDK
LVEQAQRYRQ AGWDAYLERL ALHNK