ID A0A1B8P1D2_HALEL Unreviewed; 95 AA.
AC A0A1B8P1D2;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=orotidine-5'-phosphate decarboxylase {ECO:0000256|ARBA:ARBA00012321};
DE EC=4.1.1.23 {ECO:0000256|ARBA:ARBA00012321};
GN Name=pyrF_1 {ECO:0000313|EMBL:OBX36052.1};
GN ORFNames=A8U91_00388 {ECO:0000313|EMBL:OBX36052.1};
OS Halomonas elongata.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Halomonadaceae; Halomonas.
OX NCBI_TaxID=2746 {ECO:0000313|EMBL:OBX36052.1, ECO:0000313|Proteomes:UP000092504};
RN [1] {ECO:0000313|EMBL:OBX36052.1, ECO:0000313|Proteomes:UP000092504}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HEK1 {ECO:0000313|EMBL:OBX36052.1,
RC ECO:0000313|Proteomes:UP000092504};
RA Gaba S., Singh R.N., Abrol S., Kaushik R., Saxena A.K.;
RT "Genome sequence of halotolerant plant growth promoting strain of Halomonas
RT elongata HEK1 isolated from salterns of Rann of Kutch, Gujarat, India.";
RL Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the decarboxylation of orotidine 5'-monophosphate
CC (OMP) to uridine 5'-monophosphate (UMP).
CC {ECO:0000256|ARBA:ARBA00002356}.
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 -!- 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:OBX36052.1}.
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DR EMBL; MAJD01000001; OBX36052.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1B8P1D2; -.
DR PATRIC; fig|2746.7.peg.400; -.
DR UniPathway; UPA00070; UER00120.
DR Proteomes; UP000092504; 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 Gene3D; 3.20.20.70; Aldolase class I; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR014732; OMPdecase.
DR InterPro; IPR018089; OMPdecase_AS.
DR InterPro; IPR001754; OMPdeCOase_dom.
DR InterPro; IPR011060; RibuloseP-bd_barrel.
DR PANTHER; PTHR32119; OROTIDINE 5'-PHOSPHATE DECARBOXYLASE; 1.
DR PANTHER; PTHR32119:SF2; 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 4: Predicted;
KW Decarboxylase {ECO:0000256|ARBA:ARBA00022793};
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000313|EMBL:OBX36052.1};
KW Pyrimidine biosynthesis {ECO:0000256|ARBA:ARBA00022975}.
FT DOMAIN 6..95
FT /note="Orotidine 5'-phosphate decarboxylase"
FT /evidence="ECO:0000259|SMART:SM00934"
SQ SEQUENCE 95 AA; 10135 MW; 31DEC9C202AD67AD CRC64;
MATASPLIIA LDYTSLDAAL CMADRLDPTR CRLKVGKELF TRSGPDVLEA LHGRGFEVFL
DLKFHDIPNT VAGAVQAAAE QGCGWSTCML PVVVG
//
