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Database: UniProt
Entry: J0DGM8_9BIFI
LinkDB: J0DGM8_9BIFI
Original site: J0DGM8_9BIFI 
ID   J0DGM8_9BIFI            Unreviewed;       342 AA.
AC   J0DGM8;
DT   03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   03-OCT-2012, sequence version 1.
DT   27-MAR-2024, entry version 51.
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=HMPREF9156_00227 {ECO:0000313|EMBL:EJD65463.1};
OS   Scardovia wiggsiae F0424.
OC   Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC   Bifidobacteriaceae; Scardovia.
OX   NCBI_TaxID=857290 {ECO:0000313|EMBL:EJD65463.1, ECO:0000313|Proteomes:UP000006415};
RN   [1] {ECO:0000313|EMBL:EJD65463.1, ECO:0000313|Proteomes:UP000006415}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=F0424 {ECO:0000313|EMBL:EJD65463.1,
RC   ECO:0000313|Proteomes:UP000006415};
RG   The Broad Institute Genome Sequencing Platform;
RA   Earl A., Ward D., Feldgarden M., Gevers D., Izard J., Ganesan A.,
RA   Baranova O.V., Blanton J.M., Tanner A.C., Mathney J., Dewhirst F.E.,
RA   Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A.,
RA   Alvarado L., Arachchi H.M., Berlin A., Chapman S.B., Gearin G.,
RA   Goldberg J., Griggs A., Gujja S., Hansen M., Heiman D., Howarth C.,
RA   Larimer J., Lui A., MacDonald P.J.P., McCowen C., Montmayeur A., Murphy C.,
RA   Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T., Sisk P.,
RA   Stolte C., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Scardovia wiggsiae F0424.";
RL   Submitted (JAN-2012) 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:EJD65463.1}.
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DR   EMBL; AGZS01000001; EJD65463.1; -; Genomic_DNA.
DR   RefSeq; WP_007147295.1; NZ_JH719939.1.
DR   AlphaFoldDB; J0DGM8; -.
DR   STRING; 857290.HMPREF9156_00227; -.
DR   GeneID; 84815166; -.
DR   eggNOG; COG0284; Bacteria.
DR   HOGENOM; CLU_060704_1_1_11; -.
DR   OrthoDB; 9808470at2; -.
DR   UniPathway; UPA00070; UER00120.
DR   Proteomes; UP000006415; 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:UP000006415}.
FT   DOMAIN          14..290
FT                   /note="Orotidine 5'-phosphate decarboxylase"
FT                   /evidence="ECO:0000259|SMART:SM00934"
FT   ACT_SITE        99
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01215"
SQ   SEQUENCE   342 AA;  35797 MW;  77122721324080B6 CRC64;
     MDRLATAIEK MHSPCVVGLD PRPEVIPRQV LEDVSSAESL AEAYADFSRV IIDAVSDIVP
     AVKPQIAMYE ALGPAGISAY CRTTRYAQER GLYVIGDIKR GDIGSTAQAY AAHLSGIPGI
     SGQGADVWHE DAVTVNPYLG IDGIRPFIEA AERNDKDIFV LCRTSNPSSA QLQDLDIKDA
     KEAAGTADAR IVQGPATVGM YVAGLIAQWG EEHCGASGYS RVGAVVGATH IQDAAGFRSR
     MPHTMFLVPG YGVQGGTAAD AAALFNADGT GAVINSSRGI IAAWKKDPQY SPSLTRGQAL
     DCAAASAHRA AAAMRADIIG SLKPGSMEAH TAVSHNHQKK GS
//
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