ID   PYRF_MYCS2              Reviewed;         276 AA.
AC   O08323; A0QWS6; I7FL41;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1997, sequence version 1.
DT   27-MAR-2024, entry version 126.
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=MSMEG_3048, MSMEI_2974;
OS   Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium
OS   smegmatis).
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC   Mycolicibacterium.
OX   NCBI_TaxID=246196;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=9169204; DOI=10.1006/plas.1997.1286;
RA   Knipfer N., Seth A., Shrader T.E.;
RT   "Unmarked gene integration into the chromosome of Mycobacterium smegmatis
RT   via precise replacement of the pyrF gene.";
RL   Plasmid 37:129-140(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700084 / mc(2)155;
RA   Fleischmann R.D., Dodson R.J., Haft D.H., Merkel J.S., Nelson W.C.,
RA   Fraser C.M.;
RL   Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700084 / mc(2)155;
RX   PubMed=17295914; DOI=10.1186/gb-2007-8-2-r20;
RA   Deshayes C., Perrodou E., Gallien S., Euphrasie D., Schaeffer C.,
RA   Van-Dorsselaer A., Poch O., Lecompte O., Reyrat J.-M.;
RT   "Interrupted coding sequences in Mycobacterium smegmatis: authentic
RT   mutations or sequencing errors?";
RL   Genome Biol. 8:R20.1-R20.9(2007).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700084 / mc(2)155;
RX   PubMed=18955433; DOI=10.1101/gr.081901.108;
RA   Gallien S., Perrodou E., Carapito C., Deshayes C., Reyrat J.-M.,
RA   Van Dorsselaer A., Poch O., Schaeffer C., Lecompte O.;
RT   "Ortho-proteogenomics: multiple proteomes investigation through orthology
RT   and a new MS-based protocol.";
RL   Genome Res. 19:128-135(2009).
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}.
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DR   EMBL; U91572; AAB50157.1; -; Genomic_DNA.
DR   EMBL; CP000480; ABK73017.1; -; Genomic_DNA.
DR   EMBL; CP001663; AFP39438.1; -; Genomic_DNA.
DR   RefSeq; WP_003894432.1; NZ_SIJM01000002.1.
DR   RefSeq; YP_887364.1; NC_008596.1.
DR   AlphaFoldDB; O08323; -.
DR   SMR; O08323; -.
DR   STRING; 246196.MSMEG_3048; -.
DR   PaxDb; 246196-MSMEI_2974; -.
DR   GeneID; 66734455; -.
DR   KEGG; msg:MSMEI_2974; -.
DR   KEGG; msm:MSMEG_3048; -.
DR   PATRIC; fig|246196.19.peg.3010; -.
DR   eggNOG; COG0284; Bacteria.
DR   OrthoDB; 9808470at2; -.
DR   UniPathway; UPA00070; UER00120.
DR   Proteomes; UP000000757; Chromosome.
DR   Proteomes; UP000006158; Chromosome.
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..276
FT                   /note="Orotidine 5'-phosphate decarboxylase"
FT                   /id="PRO_0000134629"
FT   ACT_SITE        95
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   276 AA;  27816 MW;  41437843A3E2A896 CRC64;
     MTGFGQRLDA AVSARGPLCP GIDPHPELLN AWGLTVDAEG LRAFCDICVA AFAGFAIVKP
     QVAFFEAYGS AGFAVLEDTI AALRAEGVLV LADAKRGDIG STMAAYAAAW AGDSPLAADA
     VTASPYLGFG SLRPLLDTAV ANGRGVFVLA ATSNPEGVGL QRAVAGDVTV AQSIVDAVAQ
     ANREADPAAR DGDPVGPFGV VVGATVADPP DLHMLGGPVL VPGVGAQGGR PEALGGLGNA
     RRLLPAVSRE VLRAGPAVDD VRAAAERLRD QVAYLA
//