ID A0A143ZUP5_9FIRM Unreviewed; 310 AA.
AC A0A143ZUP5;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 24-JAN-2024, entry version 24.
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=BN3661_02075 {ECO:0000313|EMBL:CZT57569.1};
OS Eubacteriaceae bacterium CHKCI005.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Eubacteriaceae.
OX NCBI_TaxID=1780381 {ECO:0000313|EMBL:CZT57569.1, ECO:0000313|Proteomes:UP000199521};
RN [1] {ECO:0000313|EMBL:CZT57569.1, ECO:0000313|Proteomes:UP000199521}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CHKC5 {ECO:0000313|EMBL:CZT57569.1};
RA Oliw E.H.;
RL Submitted (JAN-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; FJVJ01000036; CZT57569.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A143ZUP5; -.
DR STRING; 1780381.BN3661_02075; -.
DR UniPathway; UPA00070; UER00120.
DR Proteomes; UP000199521; 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; IPR018089; OMPdecase_AS.
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.
DR PROSITE; PS00156; OMPDECASE; 1.
PE 3: Inferred from homology;
KW Decarboxylase {ECO:0000256|ARBA:ARBA00022793, ECO:0000256|HAMAP-
KW Rule:MF_01215};
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|HAMAP-Rule:MF_01215};
KW Pyrimidine biosynthesis {ECO:0000256|ARBA:ARBA00022975, ECO:0000256|HAMAP-
KW Rule:MF_01215}; Reference proteome {ECO:0000313|Proteomes:UP000199521}.
FT DOMAIN 16..288
FT /note="Orotidine 5'-phosphate decarboxylase"
FT /evidence="ECO:0000259|SMART:SM00934"
FT ACT_SITE 106
FT /note="Proton donor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01215"
SQ SEQUENCE 310 AA; 33666 MW; 2B58C6427FD0FFA2 CRC64;
MSLDRLIEGI ARTNNPTVAG LDPKLEYIPD CILKPCIDQY GRTLEAAAEA IFTYNQGLID
ALCDIVPAVK PQCAYYEMYG WQGVRALERT IRYAKEKGMF VITDGKRNDI GSTMDAYAAA
HLGVTDVAGN GIEAFGGDAL TVNGYLGSDG IDPVIKVCRQ RDKGMFVLVK TSNPSSEELQ
DQDINEDTVY LMMGRQCEKW GEQLPGKYGY TGVGAVVGAT WPQQLNELRY ELPHTFFLVP
GYGAQGGSAE SVAGAFDKRG LGAIVNSSRA ILCAWKKEGC PGEDYAQAAR REAIRMRDAI
AAVIPAITLE
//