ID PYRF_DEIRA Reviewed; 272 AA.
AC Q9RSC5;
DT 23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2002, sequence version 2.
DT 27-MAR-2024, entry version 123.
DE RecName: Full=Orotidine 5'-phosphate decarboxylase;
DE EC=4.1.1.23;
DE AltName: Full=OMP decarboxylase;
DE Short=OMPDCase;
DE Short=OMPdecase;
GN Name=pyrF; OrderedLocusNames=DR_2200;
OS Deinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / CCUG
OS 27074 / LMG 4051 / NBRC 15346 / NCIMB 9279 / VKM B-1422 / R1).
OC Bacteria; Deinococcota; Deinococci; Deinococcales; Deinococcaceae;
OC Deinococcus.
OX NCBI_TaxID=243230;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 13939 / DSM 20539 / JCM 16871 / CCUG 27074 / LMG 4051 / NBRC
RC 15346 / NCIMB 9279 / VKM B-1422 / R1;
RX PubMed=10567266; DOI=10.1126/science.286.5444.1571;
RA White O., Eisen J.A., Heidelberg J.F., Hickey E.K., Peterson J.D.,
RA Dodson R.J., Haft D.H., Gwinn M.L., Nelson W.C., Richardson D.L.,
RA Moffat K.S., Qin H., Jiang L., Pamphile W., Crosby M., Shen M.,
RA Vamathevan J.J., Lam P., McDonald L.A., Utterback T.R., Zalewski C.,
RA Makarova K.S., Aravind L., Daly M.J., Minton K.W., Fleischmann R.D.,
RA Ketchum K.A., Nelson K.E., Salzberg S.L., Smith H.O., Venter J.C.,
RA Fraser C.M.;
RT "Genome sequence of the radioresistant bacterium Deinococcus radiodurans
RT R1.";
RL Science 286:1571-1577(1999).
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 -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo pathway;
CC UMP from orotate: step 2/2.
CC -!- SIMILARITY: Belongs to the OMP decarboxylase family. Type 2 subfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF11749.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AE000513; AAF11749.1; ALT_INIT; Genomic_DNA.
DR PIR; G75302; G75302.
DR RefSeq; NP_295922.1; NC_001263.1.
DR RefSeq; WP_027479917.1; NZ_JMLF01000004.1.
DR AlphaFoldDB; Q9RSC5; -.
DR SMR; Q9RSC5; -.
DR STRING; 243230.DR_2200; -.
DR PaxDb; 243230-DR_2200; -.
DR EnsemblBacteria; AAF11749; AAF11749; DR_2200.
DR GeneID; 69518447; -.
DR KEGG; dra:DR_2200; -.
DR PATRIC; fig|243230.17.peg.2426; -.
DR eggNOG; COG0284; Bacteria.
DR HOGENOM; CLU_450357_0_0_0; -.
DR InParanoid; Q9RSC5; -.
DR OrthoDB; 9808470at2; -.
DR UniPathway; UPA00070; UER00120.
DR Proteomes; UP000002524; Chromosome I.
DR GO; GO:0004590; F:orotidine-5'-phosphate decarboxylase activity; IEA:UniProtKB-UniRule.
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 CDD; cd04725; OMP_decarboxylase_like; 1.
DR Gene3D; 3.20.20.70; Aldolase class I; 1.
DR HAMAP; MF_01215; OMPdecase_type2; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR018089; OMPdecase_AS.
DR InterPro; IPR011995; OMPdecase_type-2.
DR InterPro; IPR001754; OMPdeCOase_dom.
DR InterPro; IPR011060; RibuloseP-bd_barrel.
DR NCBIfam; TIGR02127; pyrF_sub2; 1.
DR PANTHER; PTHR43375; OROTIDINE 5'-PHOSPHATE DECARBOXYLASE; 1.
DR PANTHER; PTHR43375:SF1; OROTIDINE 5'-PHOSPHATE DECARBOXYLASE; 1.
DR Pfam; PF00215; OMPdecase; 1.
DR SMART; SM00934; OMPdecase; 1.
DR SUPFAM; SSF51366; Ribulose-phoshate binding barrel; 1.
DR PROSITE; PS00156; OMPDECASE; 1.
PE 3: Inferred from homology;
KW Decarboxylase; Lyase; Pyrimidine biosynthesis; Reference proteome.
FT CHAIN 1..272
FT /note="Orotidine 5'-phosphate decarboxylase"
FT /id="PRO_0000134626"
FT ACT_SITE 92
FT /note="Proton donor"
FT /evidence="ECO:0000250"
SQ SEQUENCE 272 AA; 28066 MW; 79CB125491ECEBA2 CRC64;
MTPTFAQAVT ERTLSRRTRL CVGLDPRLGE YRDVAQLRQN TLDVLEASAP YAACVKPQLA
FFEALGLPGF TLLEEVCAAA RTLGLPVLLD GKRGDIGTTA AAYAQGWLGG THAGDALTVN
PFLGFQTLTP FVQAARENGG AIFVLVKTSN PDQQDLQGQG VSERIAVEIA RLGDEEGLGD
GDYASVGAVV GATHPGDLAT FRALMPKALL LLPGLGAQGA QARDLAGAFH AGGTGALASA
SRAVQYARGL DVGAAREAAL ALRDELNGAL GV
//
