ID A0A087AS25_9BIFI Unreviewed; 323 AA.
AC A0A087AS25;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 38.
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 ECO:0000313|EMBL:HJG42213.1};
GN ORFNames=BIGA_0093 {ECO:0000313|EMBL:KFI61575.1}, K8U73_07525
GN {ECO:0000313|EMBL:HJG42213.1};
OS Bifidobacterium pullorum subsp. gallinarum.
OC Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC Bifidobacteriaceae; Bifidobacterium.
OX NCBI_TaxID=78344 {ECO:0000313|EMBL:KFI61575.1, ECO:0000313|Proteomes:UP000029046};
RN [1] {ECO:0000313|EMBL:KFI61575.1, ECO:0000313|Proteomes:UP000029046}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 11586 {ECO:0000313|EMBL:KFI61575.1,
RC ECO:0000313|Proteomes:UP000029046};
RA Ventura M., Milani C., Lugli G.A.;
RT "Genomics of Bifidobacteria.";
RL Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:HJG42213.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ChiBcolR7-4860 {ECO:0000313|EMBL:HJG42213.1};
RX PubMed=33868800;
RA Gilroy R., Ravi A., Getino M., Pursley I., Horton D.L., Alikhan N.F.,
RA Baker D., Gharbi K., Hall N., Watson M., Adriaenssens E.M.,
RA Foster-Nyarko E., Jarju S., Secka A., Antonio M., Oren A., Chaudhuri R.R.,
RA La Ragione R., Hildebrand F., Pallen M.J.;
RT "Extensive microbial diversity within the chicken gut microbiome revealed
RT by metagenomics and culture.";
RL PeerJ 9:0-0(2021).
RN [3] {ECO:0000313|EMBL:HJG42213.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ChiBcolR7-4860 {ECO:0000313|EMBL:HJG42213.1};
RA Gilroy R.;
RL Submitted (SEP-2021) 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}.
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:KFI61575.1}.
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DR EMBL; DYUX01000025; HJG42213.1; -; Genomic_DNA.
DR EMBL; JGYX01000001; KFI61575.1; -; Genomic_DNA.
DR RefSeq; WP_033505586.1; NZ_JGYX01000001.1.
DR AlphaFoldDB; A0A087AS25; -.
DR eggNOG; COG0284; Bacteria.
DR OrthoDB; 9808470at2; -.
DR UniPathway; UPA00070; UER00120.
DR Proteomes; UP000029046; Unassembled WGS sequence.
DR Proteomes; UP000786560; 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:UP000029046}.
FT DOMAIN 52..293
FT /note="Orotidine 5'-phosphate decarboxylase"
FT /evidence="ECO:0000259|SMART:SM00934"
FT ACT_SITE 112
FT /note="Proton donor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01215"
SQ SEQUENCE 323 AA; 33833 MW; 86C204518465EFCE CRC64;
MDRLIEAIAA TQNPSVVGLD PTEALVPAQV VASFADEIAD EVEDAADRPA AQLAVAYFEY
NRAIIDAIAD IVPAVKPQIA MYEALGPAGV DAYTMTCEYA QSHGLYVIGD IKRGDIGSTA
AAYAGHLGGV AFGAGESGPY DPWHEDAVTV NPYLGTDGIT PFVEAATAAD KDIFALVRTS
NPSSSEIQEL ELAGGCRVYE HVADLVERWG QGTVGQHRYS RVGAVVGATH PEEGRALRAR
MPHTFFLVPG YGAQGGTARD VAGMFDDAGS GAIVNSSRGI IGAWRKTGAY SETMSAESAL
DLVADAARNA AIAMRDDLRA VMP
//
