ID A0A1H9BRS9_9FIRM Unreviewed; 307 AA.
AC A0A1H9BRS9;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 17.
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=SAMN02910369_00845 {ECO:0000313|EMBL:SEP91273.1};
OS Lachnospiraceae bacterium NE2001.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae.
OX NCBI_TaxID=1520823 {ECO:0000313|EMBL:SEP91273.1, ECO:0000313|Proteomes:UP000199680};
RN [1] {ECO:0000313|EMBL:SEP91273.1, ECO:0000313|Proteomes:UP000199680}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NE2001 {ECO:0000313|EMBL:SEP91273.1,
RC ECO:0000313|Proteomes:UP000199680};
RA de Groot N.N.;
RL Submitted (OCT-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; FOEK01000005; SEP91273.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H9BRS9; -.
DR STRING; 1520823.SAMN02910369_00845; -.
DR OrthoDB; 9808470at2; -.
DR UniPathway; UPA00070; UER00120.
DR Proteomes; UP000199680; 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:UP000199680}.
FT DOMAIN 15..283
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 307 AA; 33245 MW; 301CD6D174B46369 CRC64;
MINNLIKLIK EKNAPIVVGL DPQLGFIPEQ ILSKWYKELG NNLEAVGEAI FEYNVGLLDA
TYDLIPAVKP QIAMYEQFGI PGLAAFKKTV DYAHEKGLVV IGDIKRGDIG STSEAYALGH
IGTVSIGENE FQPFDEDIVT VNPYLGSDGV MPFVKVCEQC NRGIFVLVKT SNPSSGEFQD
RLIDGKPLYE IVAEKVNEWG ATSVDDEYGY SEVGAVVGAT YPEMGAKLRK LMPKSYILVP
GYGAQGGSGK DLKGFFNEDG LGAIVNSSRG IIAAYKNDKY SSFGAAGYAD ASRAAVEDMI
KDIRENI
//
