PYRF_MYCLE
ID PYRF_MYCLE Reviewed; 282 AA.
AC Q9CCR1;
DT 23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 25-MAY-2022, entry version 99.
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=ML0537;
OS Mycobacterium leprae (strain TN).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=272631;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TN;
RX PubMed=11234002; DOI=10.1038/35059006;
RA Cole S.T., Eiglmeier K., Parkhill J., James K.D., Thomson N.R.,
RA Wheeler P.R., Honore N., Garnier T., Churcher C.M., Harris D.E.,
RA Mungall K.L., Basham D., Brown D., Chillingworth T., Connor R.,
RA Davies R.M., Devlin K., Duthoy S., Feltwell T., Fraser A., Hamlin N.,
RA Holroyd S., Hornsby T., Jagels K., Lacroix C., Maclean J., Moule S.,
RA Murphy L.D., Oliver K., Quail M.A., Rajandream M.A., Rutherford K.M.,
RA Rutter S., Seeger K., Simon S., Simmonds M., Skelton J., Squares R.,
RA Squares S., Stevens K., Taylor K., Whitehead S., Woodward J.R.,
RA Barrell B.G.;
RT "Massive gene decay in the leprosy bacillus.";
RL Nature 409:1007-1011(2001).
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; AL583918; CAC30045.1; -; Genomic_DNA.
DR PIR; A86976; A86976.
DR RefSeq; NP_301456.1; NC_002677.1.
DR RefSeq; WP_010907780.1; NC_002677.1.
DR AlphaFoldDB; Q9CCR1; -.
DR SMR; Q9CCR1; -.
DR STRING; 272631.ML0537; -.
DR EnsemblBacteria; CAC30045; CAC30045; CAC30045.
DR KEGG; mle:ML0537; -.
DR PATRIC; fig|272631.5.peg.938; -.
DR Leproma; ML0537; -.
DR eggNOG; COG0284; Bacteria.
DR HOGENOM; CLU_060704_0_0_11; -.
DR OMA; QSAFFER; -.
DR UniPathway; UPA00070; UER00120.
DR Proteomes; UP000000806; 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 Gene3D; 3.20.20.70; -; 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 PANTHER; PTHR43375; PTHR43375; 1.
DR Pfam; PF00215; OMPdecase; 1.
DR SMART; SM00934; OMPdecase; 1.
DR SUPFAM; SSF51366; SSF51366; 1.
DR TIGRFAMs; TIGR02127; pyrF_sub2; 1.
DR PROSITE; PS00156; OMPDECASE; 1.
PE 3: Inferred from homology;
KW Decarboxylase; Lyase; Pyrimidine biosynthesis; Reference proteome.
FT CHAIN 1..282
FT /note="Orotidine 5'-phosphate decarboxylase"
FT /id="PRO_0000134628"
FT ACT_SITE 95
FT /note="Proton donor"
FT /evidence="ECO:0000250"
SQ SEQUENCE 282 AA; 28678 MW; 89DE23C44B227BA5 CRC64;
MTGFGARLVE ATSRRGQLCL GIDPHPELLR AWDLPTTADG LAAFCDICVE AFSGFAIVKP
QVAFFEAYGA AGFAVLEYTI AALRSVGVLV LADAKRGDIG STMAAYAAAW AGNSPLAADA
VTASPYLGFG SLRPLLEVAA AHDRGVFVLA STSNLEGATV QRATFDGRIV AQLIVDQAAF
VNREMNRSFH RSEPGCLGYV GVVVGATVFG APDVSALGGP VLVPGVGAQG GHPEALGGLG
GAAPGQLLPA VSRAVLRAGP GVSELRAAGE QMRDAVAYLA AV
