ID PYRF_CLOAB Reviewed; 286 AA.
AC Q97FS5;
DT 23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2001, sequence version 1.
DT 27-MAR-2024, entry version 110.
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=CA_C2652;
OS Clostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / LMG 5710
OS / VKM B-1787).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=272562;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787;
RX PubMed=11466286; DOI=10.1128/jb.183.16.4823-4838.2001;
RA Noelling J., Breton G., Omelchenko M.V., Makarova K.S., Zeng Q., Gibson R.,
RA Lee H.M., Dubois J., Qiu D., Hitti J., Wolf Y.I., Tatusov R.L., Sabathe F.,
RA Doucette-Stamm L.A., Soucaille P., Daly M.J., Bennett G.N., Koonin E.V.,
RA Smith D.R.;
RT "Genome sequence and comparative analysis of the solvent-producing
RT bacterium Clostridium acetobutylicum.";
RL J. Bacteriol. 183:4823-4838(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; AE001437; AAK80599.1; -; Genomic_DNA.
DR PIR; D97226; D97226.
DR RefSeq; NP_349259.1; NC_003030.1.
DR RefSeq; WP_010965940.1; NC_003030.1.
DR AlphaFoldDB; Q97FS5; -.
DR SMR; Q97FS5; -.
DR STRING; 272562.CA_C2652; -.
DR DNASU; 1118835; -.
DR GeneID; 44999120; -.
DR KEGG; cac:CA_C2652; -.
DR PATRIC; fig|272562.8.peg.2841; -.
DR eggNOG; COG0284; Bacteria.
DR HOGENOM; CLU_060704_1_1_9; -.
DR OrthoDB; 9808470at2; -.
DR UniPathway; UPA00070; UER00120.
DR Proteomes; UP000000814; 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..286
FT /note="Orotidine 5'-phosphate decarboxylase"
FT /id="PRO_0000134622"
FT ACT_SITE 97
FT /note="Proton donor"
FT /evidence="ECO:0000250"
SQ SEQUENCE 286 AA; 32241 MW; 5BC7E3ACBD5FF2A4 CRC64;
MIIDRLFDSV EKKGHVCLGL DTDITYVPEE FCKKFNSIED AIFNFNKKII DATLDVVSCY
KVQIAYYEAY GLKGLLAYKR TLEYLREKKA IAIADIKRGD IAKTAEMYAK AHFEGDFEAD
FVTLNPYMGL DGIEPYMPYI EKMEKGLFIL LRTSNKGAYD IQYIKTQGGK NVYDEVGEKI
YDLGQKATGR SKYSSIGAVV GCTHVEEGVE IRNKFKNMFF LIPGYGAQGG TAKEVSLYLR
EGNGGVVNSS RGILLAYKKE ENGEKIFDEC ARLAAINMRD EIRKTL
//
