PYRF_THEAC
ID PYRF_THEAC Reviewed; 214 AA.
AC O74110;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2000, sequence version 2.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=Orotidine 5'-phosphate decarboxylase {ECO:0000255|HAMAP-Rule:MF_01200};
DE EC=4.1.1.23 {ECO:0000255|HAMAP-Rule:MF_01200};
DE AltName: Full=OMP decarboxylase {ECO:0000255|HAMAP-Rule:MF_01200};
DE Short=OMPDCase {ECO:0000255|HAMAP-Rule:MF_01200};
DE Short=OMPdecase {ECO:0000255|HAMAP-Rule:MF_01200};
GN Name=pyrF {ECO:0000255|HAMAP-Rule:MF_01200}; OrderedLocusNames=Ta0073;
OS Thermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC
OS 15155 / AMRC-C165).
OC Archaea; Candidatus Thermoplasmatota; Thermoplasmata; Thermoplasmatales;
OC Thermoplasmataceae; Thermoplasma.
OX NCBI_TaxID=273075;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RX PubMed=10973825; DOI=10.1006/bbrc.2000.3401;
RA Yaoi T., Laksanalamai P., Jiemjit A., Kagawa H., Alton T., Trent J.D.;
RT "Cloning and characterization of ftsZ and pyrF from the archaeon
RT Thermoplasma acidophilum.";
RL Biochem. Biophys. Res. Commun. 275:936-945(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165;
RX PubMed=11029001; DOI=10.1038/35035069;
RA Ruepp A., Graml W., Santos-Martinez M.-L., Koretke K.K., Volker C.,
RA Mewes H.-W., Frishman D., Stocker S., Lupas A.N., Baumeister W.;
RT "The genome sequence of the thermoacidophilic scavenger Thermoplasma
RT acidophilum.";
RL Nature 407:508-513(2000).
CC -!- FUNCTION: Catalyzes the decarboxylation of orotidine 5'-monophosphate
CC (OMP) to uridine 5'-monophosphate (UMP). {ECO:0000255|HAMAP-
CC Rule:MF_01200, ECO:0000269|PubMed:10973825}.
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|HAMAP-Rule:MF_01200};
CC -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo pathway;
CC UMP from orotate: step 2/2. {ECO:0000255|HAMAP-Rule:MF_01200}.
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01200}.
CC -!- SIMILARITY: Belongs to the OMP decarboxylase family. Type 1 subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_01200}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAC11221.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AF038845; AAC24044.1; -; Genomic_DNA.
DR EMBL; AL445063; CAC11221.1; ALT_INIT; Genomic_DNA.
DR PIR; T37332; T37332.
DR RefSeq; WP_048161418.1; NC_002578.1.
DR AlphaFoldDB; O74110; -.
DR SMR; O74110; -.
DR STRING; 273075.Ta0073; -.
DR EnsemblBacteria; CAC11221; CAC11221; CAC11221.
DR GeneID; 1455733; -.
DR KEGG; tac:Ta0073; -.
DR eggNOG; arCOG00081; Archaea.
DR HOGENOM; CLU_067069_2_0_2; -.
DR OMA; EMSHPGA; -.
DR OrthoDB; 54384at2157; -.
DR BRENDA; 4.1.1.23; 6324.
DR UniPathway; UPA00070; UER00120.
DR Proteomes; UP000001024; 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_01200_A; OMPdecase_type1_A; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR014732; OMPdecase.
DR InterPro; IPR001754; OMPdeCOase_dom.
DR InterPro; IPR011060; RibuloseP-bd_barrel.
DR Pfam; PF00215; OMPdecase; 1.
DR SMART; SM00934; OMPdecase; 1.
DR SUPFAM; SSF51366; SSF51366; 1.
DR TIGRFAMs; TIGR01740; pyrF; 1.
DR PROSITE; PS00156; OMPDECASE; 1.
PE 3: Inferred from homology;
KW Decarboxylase; Lyase; Pyrimidine biosynthesis; Reference proteome.
FT CHAIN 1..214
FT /note="Orotidine 5'-phosphate decarboxylase"
FT /id="PRO_0000134620"
FT ACT_SITE 61
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01200"
FT BINDING 11
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01200"
FT BINDING 33
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01200"
FT BINDING 59..68
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01200"
FT BINDING 114
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01200"
FT BINDING 164..174
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01200"
FT BINDING 187
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01200"
FT BINDING 188
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01200"
FT CONFLICT 206
FT /note="E -> G (in Ref. 1; AAC24044)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 214 AA; 22890 MW; 1171F2C6AC058489 CRC64;
MSESRLVVAL DLTDKDRALE IARSIGRQVF AIKINWPLVL AGSGSIIGEI ARVSRVVCDF
KIADIPNTNS IIAKFARDQG AWGIISHSFT GLESLRSVVE ASGDTKVFSV VAMSHPGSDL
INDNYRKLMD ISERAGVYGY IAPGNKLSDL SEIRKRTKKT IMSPGIGSQG GRASDAIKAG
ADLVIVGRSI YESADPVTAA EAINEEIAKA VEQN
