PYRF_ACRCH
ID PYRF_ACRCH Reviewed; 376 AA.
AC P14017;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1990, sequence version 1.
DT 03-AUG-2022, entry version 94.
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=PYR4;
OS Acremonium chrysogenum (Cephalosporium acremonium).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Hypocreales incertae sedis; Acremonium.
OX NCBI_TaxID=5044;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 11550 / CBS 779.69 / DSM 880 / IMI 49137;
RX PubMed=2587233; DOI=10.1093/nar/17.21.8874;
RA Vian A., Penalva M.A.;
RT "Nucleotide sequence of the Cephalosporium acremonium pyr4 gene.";
RL Nucleic Acids Res. 17:8874-8874(1989).
RN [2]
RP DISCUSSION OF SEQUENCE.
RX PubMed=2140299; DOI=10.1007/bf00312613;
RA Vian A., Penalva M.A.;
RT "Cloning of the pyr4 gene encoding orotidine-5'-phosphate decarboxylase in
RT Cephalosporium acremonium.";
RL Curr. Genet. 17:223-227(1990).
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; X15937; CAA34063.1; -; Genomic_DNA.
DR PIR; S06746; DCCEOC.
DR AlphaFoldDB; P14017; -.
DR SMR; P14017; -.
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; -; 2.
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 PROSITE; PS00156; OMPDECASE; 1.
PE 3: Inferred from homology;
KW Decarboxylase; Lyase; Pyrimidine biosynthesis.
FT CHAIN 1..376
FT /note="Orotidine 5'-phosphate decarboxylase"
FT /id="PRO_0000134655"
FT REGION 160..208
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 101
FT /note="Proton donor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10110"
FT BINDING 42
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 64..66
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 99..108
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 329
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 348
FT /ligand="substrate"
FT /evidence="ECO:0000250"
SQ SEQUENCE 376 AA; 41128 MW; 462A23AD21814FA7 CRC64;
MAPHPTLKST YSTRAETVTH PLSAYLYKLM DLKASNLCLS ADVANARELL HVADKVGPSI
VVLKTHYDMV AGWDFTPETG TGARLAKLAR KHGFLIFEDR KFGDIGNTVE LQYTQGAARI
IEWAHIVNVN MVPGKASVTS LANAAAKWLE RLPYEVKTSV TVGTPRNTDE DDDDEDDGNA
GEMERSHTFG LNGNNGVPIK ESSDGRKGSI VSVTTVTQQY ESAHSPRLTK TIAEEGDMLL
AGLEEPPLNR GLLILAQMSS AGNFMNAEYT QACVEAAREH KDFVMGFVSQ EALNSQPDDD
FIHMTPGCQL PPEHEEDAEL RGDGKGQQYN TPEKLIGVCG ADIVIVGRGI LKAGDLQHEA
ERYRSAAWKA YTERVR
