PYRF_BACTN
ID PYRF_BACTN Reviewed; 274 AA.
AC Q8A012;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=Orotidine 5'-phosphate decarboxylase {ECO:0000255|HAMAP-Rule:MF_01215};
DE EC=4.1.1.23 {ECO:0000255|HAMAP-Rule:MF_01215};
DE AltName: Full=OMP decarboxylase {ECO:0000255|HAMAP-Rule:MF_01215};
DE Short=OMPDCase {ECO:0000255|HAMAP-Rule:MF_01215};
DE Short=OMPdecase {ECO:0000255|HAMAP-Rule:MF_01215};
GN Name=pyrF {ECO:0000255|HAMAP-Rule:MF_01215}; OrderedLocusNames=BT_4209;
OS Bacteroides thetaiotaomicron (strain ATCC 29148 / DSM 2079 / JCM 5827 /
OS CCUG 10774 / NCTC 10582 / VPI-5482 / E50).
OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC Bacteroides.
OX NCBI_TaxID=226186;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29148 / DSM 2079 / JCM 5827 / CCUG 10774 / NCTC 10582 /
RC VPI-5482 / E50;
RX PubMed=12663928; DOI=10.1126/science.1080029;
RA Xu J., Bjursell M.K., Himrod J., Deng S., Carmichael L.K., Chiang H.C.,
RA Hooper L.V., Gordon J.I.;
RT "A genomic view of the human-Bacteroides thetaiotaomicron symbiosis.";
RL Science 299:2074-2076(2003).
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_01215};
CC -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo pathway;
CC UMP from orotate: step 2/2. {ECO:0000255|HAMAP-Rule:MF_01215}.
CC -!- SIMILARITY: Belongs to the OMP decarboxylase family. Type 2 subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_01215}.
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DR EMBL; AE015928; AAO79314.1; -; Genomic_DNA.
DR RefSeq; NP_813120.1; NC_004663.1.
DR RefSeq; WP_008759883.1; NZ_UYXG01000012.1.
DR AlphaFoldDB; Q8A012; -.
DR SMR; Q8A012; -.
DR STRING; 226186.BT_4209; -.
DR PaxDb; Q8A012; -.
DR PRIDE; Q8A012; -.
DR EnsemblBacteria; AAO79314; AAO79314; BT_4209.
DR GeneID; 60925382; -.
DR KEGG; bth:BT_4209; -.
DR PATRIC; fig|226186.12.peg.4276; -.
DR eggNOG; COG0284; Bacteria.
DR HOGENOM; CLU_060704_1_0_10; -.
DR InParanoid; Q8A012; -.
DR OMA; QSAFFER; -.
DR UniPathway; UPA00070; UER00120.
DR Proteomes; UP000001414; 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; 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.
PE 3: Inferred from homology;
KW Decarboxylase; Lyase; Pyrimidine biosynthesis; Reference proteome.
FT CHAIN 1..274
FT /note="Orotidine 5'-phosphate decarboxylase"
FT /id="PRO_1000138945"
FT ACT_SITE 96
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01215"
SQ SEQUENCE 274 AA; 30880 MW; DB4A532D4C38A7BC CRC64;
MNKQQLFENI KRKKSFLCVG LDTDIKKIPE HLLKEEDPIF AFNKAIIDAT ADLCIAYKPN
LAFYESMGVK GWIAFEKTVK YIKENYPDQF IIADAKRGDI GNTSAMYART FFEELEIDSV
TVAPYMGEDS VTPFLTYEGK WVILLALTSN KGSHDFQLTE DANGERLFEK VLRKSQEWAN
DERMMYVVGA TQGRAFEDIR KIVPNHFLLV PGVGAQGGSL EEVCKYGMNS TCGLIVNSSR
GIIYVDKTEK FAEAARLAAQ EVQVQMAEQL KAIL
