ID A0A1S9CID7_9FIRM Unreviewed; 304 AA.
AC A0A1S9CID7;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE RecName: Full=Orotidine 5'-phosphate decarboxylase {ECO:0000256|HAMAP-Rule:MF_01215};
DE EC=4.1.1.23 {ECO:0000256|HAMAP-Rule:MF_01215};
DE AltName: Full=OMP decarboxylase {ECO:0000256|HAMAP-Rule:MF_01215};
DE Short=OMPDCase {ECO:0000256|HAMAP-Rule:MF_01215};
DE Short=OMPdecase {ECO:0000256|HAMAP-Rule:MF_01215};
GN Name=pyrF {ECO:0000256|HAMAP-Rule:MF_01215};
GN ORFNames=ATN31_09550 {ECO:0000313|EMBL:OON96587.1};
OS Epulopiscium sp. AS2M-Bin001.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC Candidatus Epulonipiscium.
OX NCBI_TaxID=1764958 {ECO:0000313|EMBL:OON96587.1, ECO:0000313|Proteomes:UP000190284};
RN [1] {ECO:0000313|EMBL:OON96587.1, ECO:0000313|Proteomes:UP000190284}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AS2M-Bin001 {ECO:0000313|EMBL:OON96587.1};
RA Seilhamer J.J.;
RL Submitted (AUG-2016) to the EMBL/GenBank/DDBJ databases.
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:0000256|ARBA:ARBA00001419, ECO:0000256|HAMAP-
CC Rule:MF_01215};
CC -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo pathway;
CC UMP from orotate: step 2/2. {ECO:0000256|ARBA:ARBA00004861,
CC ECO:0000256|HAMAP-Rule:MF_01215}.
CC -!- SIMILARITY: Belongs to the OMP decarboxylase family. Type 2 subfamily.
CC {ECO:0000256|ARBA:ARBA00008847, ECO:0000256|HAMAP-Rule:MF_01215}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OON96587.1}.
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DR EMBL; LNZM01000032; OON96587.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1S9CID7; -.
DR STRING; 1764958.ATN31_09550; -.
DR UniPathway; UPA00070; UER00120.
DR Proteomes; UP000190284; Unassembled WGS sequence.
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; 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.
PE 3: Inferred from homology;
KW Decarboxylase {ECO:0000256|HAMAP-Rule:MF_01215};
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|HAMAP-Rule:MF_01215};
KW Pyrimidine biosynthesis {ECO:0000256|HAMAP-Rule:MF_01215};
KW Reference proteome {ECO:0000313|Proteomes:UP000190284}.
FT DOMAIN 15..282
FT /note="Orotidine 5'-phosphate decarboxylase"
FT /evidence="ECO:0000259|SMART:SM00934"
FT ACT_SITE 105
FT /note="Proton donor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01215"
SQ SEQUENCE 304 AA; 34215 MW; F85A28344797BE99 CRC64;
MIDRLIEQIK LKQNPTVVGL DPTLEMIPNF LKEKCFKKWG KTPKAVGKMF YKFNKEIIDY
SYDLIPAVKP QIAMYERYGV EGLKSYIKTI KYAKKKNLLV IGDIKRGDIF STAEAYSAHI
SGTNIEGEFF DLWQEDAVTL NPYMGYDAIE PFMDACKNKD KGLFILVKTS NKSGEEIQDL
VVDGKPVYDY IADFVKNWGR SLIGKYGYSN IGAVVGATYK EQGEELRERM PQTFFLVPGY
GAQGATASNI SGYFDERGLG AIVNSSRGII AAYKKQGAND KDFAKASREA VVMMREDLRK
AIKL
//
