ID A0A1F7JIS2_9BACT Unreviewed; 257 AA.
AC A0A1F7JIS2;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 13-SEP-2023, entry version 18.
DE RecName: Full=orotidine-5'-phosphate decarboxylase {ECO:0000256|ARBA:ARBA00012321};
DE EC=4.1.1.23 {ECO:0000256|ARBA:ARBA00012321};
GN ORFNames=A3H78_05015 {ECO:0000313|EMBL:OGK55499.1};
OS Candidatus Roizmanbacteria bacterium RIFCSPLOWO2_02_FULL_36_11.
OC Bacteria; Candidatus Roizmanbacteria.
OX NCBI_TaxID=1802071 {ECO:0000313|EMBL:OGK55499.1, ECO:0000313|Proteomes:UP000177418};
RN [1] {ECO:0000313|EMBL:OGK55499.1, ECO:0000313|Proteomes:UP000177418}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27774985; DOI=10.1038/ncomms13219;
RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA Williams K.H., Hubbard S.S., Banfield J.F.;
RT "Thousands of microbial genomes shed light on interconnected biogeochemical
RT processes in an aquifer system.";
RL Nat. Commun. 7:13219-13219(2016).
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};
CC -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo pathway;
CC UMP from orotate: step 2/2. {ECO:0000256|ARBA:ARBA00004861}.
CC -!- SIMILARITY: Belongs to the OMP decarboxylase family. Type 2 subfamily.
CC {ECO:0000256|ARBA:ARBA00008847}.
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:OGK55499.1}.
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DR EMBL; MGAV01000002; OGK55499.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F7JIS2; -.
DR UniPathway; UPA00070; UER00120.
DR Proteomes; UP000177418; Unassembled WGS sequence.
DR GO; GO:0004590; F:orotidine-5'-phosphate decarboxylase activity; IEA:UniProtKB-EC.
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 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};
KW Lyase {ECO:0000256|ARBA:ARBA00023239};
KW Pyrimidine biosynthesis {ECO:0000256|ARBA:ARBA00022975}.
FT DOMAIN 17..248
FT /note="Orotidine 5'-phosphate decarboxylase"
FT /evidence="ECO:0000259|SMART:SM00934"
SQ SEQUENCE 257 AA; 28253 MW; 92026BC7E559AF7E CRC64;
MTFQQKLDSA ILKNNSLLCI NLDPDEKTSD LFEFNKKIID ETHGLVCCYK PNSAFYEAQG
APGIEALKRT IDYIHRVTSG LPVILDAKRG DIGNTNRGYV RYAFEYLNAD GIVVNPYMGG
EALSLFFDQK EKGIVVMCRT SNPGAGELQN LISDGKPLFQ HVAEKVATAW NKNGNLMVVV
GATYPEELQK VREIVGDMTI LVPGIGAQGG DLEKTLKVGL NSKKAGLIIA VGRSIIYSEN
VKKETEKLRN QINLLKS
//