ID A0A1M6HIY1_9FIRM Unreviewed; 305 AA.
AC A0A1M6HIY1;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 24-JAN-2024, entry version 20.
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=SAMN02745691_01546 {ECO:0000313|EMBL:SHJ22166.1};
OS Parasporobacterium paucivorans DSM 15970.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC Parasporobacterium.
OX NCBI_TaxID=1122934 {ECO:0000313|EMBL:SHJ22166.1, ECO:0000313|Proteomes:UP000184342};
RN [1] {ECO:0000313|EMBL:SHJ22166.1, ECO:0000313|Proteomes:UP000184342}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15970 {ECO:0000313|EMBL:SHJ22166.1,
RC ECO:0000313|Proteomes:UP000184342};
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-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}.
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DR EMBL; FQYT01000015; SHJ22166.1; -; Genomic_DNA.
DR RefSeq; WP_073993785.1; NZ_FQYT01000015.1.
DR AlphaFoldDB; A0A1M6HIY1; -.
DR STRING; 1122934.SAMN02745691_01546; -.
DR OrthoDB; 9808470at2; -.
DR UniPathway; UPA00070; UER00120.
DR Proteomes; UP000184342; 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:UP000184342}.
FT DOMAIN 15..281
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 305 AA; 33761 MW; 0254CE04D274B50B CRC64;
MINKLIEKIK ETQAPIVVGL DPMLDYIPEQ VKEKAYEEFG ETLEGAAWAA WEFNKNIIDT
TYDLIPAVKP QIAMYEQFGL PGLLSYQKTI DYARSKGLVI IGDVKRGDIG STSQAYATAH
IGRIKIGSNE FRAFDEDFAT INPYFGTDGI KPFLDVAKEE NTGMFILVKT SNKSSGEFQD
RLVDGRPLYE IVGEQVSKWG EEHMGNEYSY VGAVVGATYP QMAVTLRKLM PKTYFLVPGY
GAQGGTAADL KPCFNEDGLG AIVNSSRGII AAYKNEKYAE FGEENYADAS RQAVIDMIND
IKSVF
//
