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Database: UniProt
Entry: J8B794_BACCE
LinkDB: J8B794_BACCE
Original site: J8B794_BACCE 
ID   J8B794_BACCE            Unreviewed;       238 AA.
AC   J8B794;
DT   31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   31-OCT-2012, sequence version 1.
DT   24-JAN-2024, entry version 51.
DE   RecName: Full=Orotidine 5'-phosphate decarboxylase {ECO:0000256|HAMAP-Rule:MF_01200};
DE            EC=4.1.1.23 {ECO:0000256|HAMAP-Rule:MF_01200};
DE   AltName: Full=OMP decarboxylase {ECO:0000256|HAMAP-Rule:MF_01200};
DE            Short=OMPDCase {ECO:0000256|HAMAP-Rule:MF_01200};
DE            Short=OMPdecase {ECO:0000256|HAMAP-Rule:MF_01200};
GN   Name=pyrF {ECO:0000256|HAMAP-Rule:MF_01200};
GN   ORFNames=IEE_01557 {ECO:0000313|EMBL:EJQ46934.1};
OS   Bacillus cereus BAG5X1-1.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=1053189 {ECO:0000313|EMBL:EJQ46934.1, ECO:0000313|Proteomes:UP000006600};
RN   [1] {ECO:0000313|EMBL:EJQ46934.1, ECO:0000313|Proteomes:UP000006600}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BAG5X1-1 {ECO:0000313|EMBL:EJQ46934.1,
RC   ECO:0000313|Proteomes:UP000006600};
RG   The Broad Institute Genome Sequencing Platform;
RG   The Broad Institute Genome Sequencing Center for Infectious Disease;
RA   Feldgarden M., Van der Auwera G.A., Mahillon J., Duprez V., Timmery S.,
RA   Mattelet C., Dierick K., Sun M., Yu Z., Zhu L., Hu X., Shank E.B.,
RA   Swiecicka I., Hansen B.M., Andrup L., Young S.K., Zeng Q., Gargeya S.,
RA   Fitzgerald M., Haas B., Abouelleil A., Alvarado L., Arachchi H.M.,
RA   Berlin A., Chapman S.B., Goldberg J., Griggs A., Gujja S., Hansen M.,
RA   Howarth C., Imamovic A., Larimer J., McCowen C., Montmayeur A., Murphy C.,
RA   Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T., Sisk P.,
RA   Sykes S., Wortman J., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Bacillus cereus BAG5X1-1.";
RL   Submitted (APR-2012) 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, ECO:0000256|HAMAP-Rule:MF_01200}.
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_01200, ECO:0000256|RuleBase:RU000512};
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_01200, ECO:0000256|RuleBase:RU000512}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_01200}.
CC   -!- SIMILARITY: Belongs to the OMP decarboxylase family. Type 1 subfamily.
CC       {ECO:0000256|HAMAP-Rule:MF_01200}.
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:EJQ46934.1}.
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DR   EMBL; AHDJ01000019; EJQ46934.1; -; Genomic_DNA.
DR   RefSeq; WP_002199520.1; NZ_JH791996.1.
DR   AlphaFoldDB; J8B794; -.
DR   PATRIC; fig|1053189.3.peg.1578; -.
DR   HOGENOM; CLU_067069_1_1_9; -.
DR   UniPathway; UPA00070; UER00120.
DR   Proteomes; UP000006600; 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_01200_B; OMPdecase_type1_B; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR014732; OMPdecase.
DR   InterPro; IPR018089; OMPdecase_AS.
DR   InterPro; IPR047596; OMPdecase_bac.
DR   InterPro; IPR001754; OMPdeCOase_dom.
DR   InterPro; IPR011060; RibuloseP-bd_barrel.
DR   NCBIfam; TIGR01740; pyrF; 1.
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   3: Inferred from homology;
KW   Decarboxylase {ECO:0000256|ARBA:ARBA00022793, ECO:0000256|HAMAP-
KW   Rule:MF_01200};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|HAMAP-Rule:MF_01200};
KW   Pyrimidine biosynthesis {ECO:0000256|ARBA:ARBA00022975, ECO:0000256|HAMAP-
KW   Rule:MF_01200}.
FT   DOMAIN          4..229
FT                   /note="Orotidine 5'-phosphate decarboxylase"
FT                   /evidence="ECO:0000259|SMART:SM00934"
FT   ACT_SITE        61
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01200"
FT   BINDING         10
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01200"
FT   BINDING         32
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01200"
FT   BINDING         59..68
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01200"
FT   BINDING         122
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01200"
FT   BINDING         184
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01200"
FT   BINDING         193
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01200"
FT   BINDING         213
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01200"
FT   BINDING         214
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01200"
SQ   SEQUENCE   238 AA;  26171 MW;  102B32F21359C884 CRC64;
     MSQSLIVALD FPGKQEVEQF LHHFEGEELF VKVGMELFYK EGPAIITYLK EKGHKIFLDL
     KLHDIPNTVK SAMRSLASLD VDMVNVHAAG GSSMMKAAIE GLEEGKQEGK ERPICIAVTQ
     LTSTSEAMMK KEIGIEKTLE EAVAHYAKLT KESGLDGVVC STLEVPKLRE VCGNELVTVT
     PGIRLASDDV NDQVRVATPK RARELGSSYI VVGRSITKAE NPLEAYKIVK QQWEGVTV
//
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