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Database: UniProt
Entry: D7I8D4_9BACE
LinkDB: D7I8D4_9BACE
Original site: D7I8D4_9BACE 
ID   D7I8D4_9BACE            Unreviewed;       274 AA.
AC   D7I8D4;
DT   10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT   10-AUG-2010, sequence version 1.
DT   24-JAN-2024, entry version 49.
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=HMPREF9007_00441 {ECO:0000313|EMBL:EFI06345.1};
OS   Bacteroides sp. 1_1_14.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC   Bacteroides.
OX   NCBI_TaxID=469585 {ECO:0000313|EMBL:EFI06345.1, ECO:0000313|Proteomes:UP000003951};
RN   [1] {ECO:0000313|EMBL:EFI06345.1, ECO:0000313|Proteomes:UP000003951}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1_1_14 {ECO:0000313|EMBL:EFI06345.1,
RC   ECO:0000313|Proteomes:UP000003951};
RG   The Broad Institute Genome Sequencing Platform;
RA   Ward D., Earl A., Feldgarden M., Gevers D., Young S.K., Zeng Q.,
RA   Koehrsen M., Alvarado L., Berlin A., Bochicchio J., Borenstein D.,
RA   Chapman S.B., Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J.,
RA   Griggs A., Gujja S., Heilman E., Heiman D., Hepburn T., Howarth C., Jen D.,
RA   Larson L., Mehta T., Park D., Pearson M., Roberts A., Saif S., Shea T.,
RA   Shenoy N., Sisk P., Stolte C., Sykes S., Thomson T., Walk T., White J.,
RA   Yandava C., Strauss J., Daigneault M., McDonald J., Ambrose C.E.,
RA   Allen-Vercoe E., Haas B., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Bacteroides sp. strain 1_1_14.";
RL   Submitted (MAR-2010) 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; GG774702; EFI06345.1; -; Genomic_DNA.
DR   RefSeq; WP_008759883.1; NZ_GG774702.1.
DR   AlphaFoldDB; D7I8D4; -.
DR   SMR; D7I8D4; -.
DR   GeneID; 60925382; -.
DR   HOGENOM; CLU_060704_1_0_10; -.
DR   UniPathway; UPA00070; UER00120.
DR   Proteomes; UP000003951; 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; 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.
PE   3: Inferred from homology;
KW   Decarboxylase {ECO:0000256|HAMAP-Rule:MF_01215};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|HAMAP-Rule:MF_01215};
KW   Pyrimidine biosynthesis {ECO:0000256|HAMAP-Rule:MF_01215}.
FT   DOMAIN          16..255
FT                   /note="Orotidine 5'-phosphate decarboxylase"
FT                   /evidence="ECO:0000259|SMART:SM00934"
FT   ACT_SITE        96
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01215"
SQ   SEQUENCE   274 AA;  30880 MW;  DB4A532D4C38A7BC CRC64;
     MNKQQLFENI KRKKSFLCVG LDTDIKKIPE HLLKEEDPIF AFNKAIIDAT ADLCIAYKPN
     LAFYESMGVK GWIAFEKTVK YIKENYPDQF IIADAKRGDI GNTSAMYART FFEELEIDSV
     TVAPYMGEDS VTPFLTYEGK WVILLALTSN KGSHDFQLTE DANGERLFEK VLRKSQEWAN
     DERMMYVVGA TQGRAFEDIR KIVPNHFLLV PGVGAQGGSL EEVCKYGMNS TCGLIVNSSR
     GIIYVDKTEK FAEAARLAAQ EVQVQMAEQL KAIL
//
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