ID A0A1G7M8G6_9EURY Unreviewed; 279 AA.
AC A0A1G7M8G6;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 25.
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=SAMN05216218_107173 {ECO:0000313|EMBL:SDF58011.1};
OS Halorientalis regularis.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC Haloarculaceae; Halorientalis.
OX NCBI_TaxID=660518 {ECO:0000313|EMBL:SDF58011.1, ECO:0000313|Proteomes:UP000199076};
RN [1] {ECO:0000313|EMBL:SDF58011.1, ECO:0000313|Proteomes:UP000199076}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IBRC-M 10760 {ECO:0000313|EMBL:SDF58011.1,
RC ECO:0000313|Proteomes:UP000199076};
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; FNBK01000007; SDF58011.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G7M8G6; -.
DR STRING; 660518.SAMN05216218_107173; -.
DR OrthoDB; 94124at2157; -.
DR UniPathway; UPA00070; UER00120.
DR Proteomes; UP000199076; 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}.
FT DOMAIN 17..260
FT /note="Orotidine 5'-phosphate decarboxylase"
FT /evidence="ECO:0000259|SMART:SM00934"
FT ACT_SITE 93
FT /note="Proton donor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01215"
SQ SEQUENCE 279 AA; 30494 MW; 9E547000461D1FA8 CRC64;
MTFFDRLADR IDAVDSVVSV GLDPDMDRLP EHLLDRDLPR WAFNRRIIDA THEHAACYKP
NAAFYEDPDG WRALEETIAY AHGKDVPVLL DAKRGDIGNT ARQYADLLDR ADAITANPYM
GRDSLEPFLE RTDSGVFLLC RTSNPGGADI QNLELASGEP VYERVAALAD TWNRNGNVGL
VVGATQPDEL AEIREIVPDL PFLVPGVGAQ GGDAEAAVEH GLAELDERSS PNRSRSGIGV
GLVNSSRGII FAGEDQGEDF HKASGQAAKQ LKQRLNQYR
//
