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Database: UniProt
Entry: E5YG95_9ENTR
LinkDB: E5YG95_9ENTR
Original site: E5YG95_9ENTR 
ID   E5YG95_9ENTR            Unreviewed;       241 AA.
AC   E5YG95;
DT   08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT   08-MAR-2011, sequence version 1.
DT   24-JAN-2024, entry version 63.
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=HMPREF0864_01549 {ECO:0000313|EMBL:EFV41025.1};
OS   Enterobacteriaceae bacterium 9_2_54FAA.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae.
OX   NCBI_TaxID=469613 {ECO:0000313|EMBL:EFV41025.1, ECO:0000313|Proteomes:UP000004908};
RN   [1] {ECO:0000313|EMBL:EFV41025.1, ECO:0000313|Proteomes:UP000004908}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=9_2_54FAA {ECO:0000313|EMBL:EFV41025.1,
RC   ECO:0000313|Proteomes:UP000004908};
RG   The Broad Institute Genome Sequencing Platform;
RA   Ward D., Earl A., Feldgarden M., Young S.K., Gargeya S., Zeng Q.,
RA   Alvarado L., Berlin A., Bochicchio J., Chapman S.B., Chen Z., Freedman E.,
RA   Gellesch M., Goldberg J., Griggs A., Gujja S., Heilman E., Heiman D.,
RA   Howarth C., Mehta T., Neiman D., Pearson M., Roberts A., Saif S., Shea T.,
RA   Shenoy N., Sisk P., Stolte C., Sykes S., White J., Yandava C.,
RA   Allen-Vercoe E., Ambrose C., Strauss J., Sibley C., Haas B., Nusbaum C.,
RA   Birren B.;
RL   Submitted (OCT-2010) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:EFV41025.1, ECO:0000313|Proteomes:UP000004908}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=9_2_54FAA {ECO:0000313|EMBL:EFV41025.1,
RC   ECO:0000313|Proteomes:UP000004908};
RG   The Broad Institute Genomics Platform;
RA   Earl A., Ward D., Feldgarden M., Gevers D., Allen-Vercoe E., Ambrose C.,
RA   Strauss J., Sibley C., Walker B., Young S.K., Zeng Q., Gargeya S.,
RA   Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA   Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA   Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA   Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA   Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA   Birren B.;
RT   "The Genome Sequence of Enterobacteriaceae bacterium 9_2_54FAA.";
RL   Submitted (MAR-2013) 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:EFV41025.1}.
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DR   EMBL; ADCU02000001; EFV41025.1; -; Genomic_DNA.
DR   AlphaFoldDB; E5YG95; -.
DR   UniPathway; UPA00070; UER00120.
DR   Proteomes; UP000004908; 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          15..236
FT                   /note="Orotidine 5'-phosphate decarboxylase"
FT                   /evidence="ECO:0000259|SMART:SM00934"
FT   ACT_SITE        72
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01200"
FT   BINDING         21
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01200"
FT   BINDING         43
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01200"
FT   BINDING         70..79
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01200"
FT   BINDING         130
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01200"
FT   BINDING         191
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01200"
FT   BINDING         200
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01200"
FT   BINDING         220
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01200"
FT   BINDING         221
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01200"
SQ   SEQUENCE   241 AA;  25566 MW;  ADBF550B8737B991 CRC64;
     MSISTPSQAN ATSSPILVAL DYADKNAALA FVDNIDPLDC RLKVGKEMFT LYGPQLVSEL
     QQRGFEIFLD LKFHDIPNTA AHAVAAAAEL GVWMVNVHAS GGARMMSAAR EALVPFGKDA
     PLLIAVTVLT SMEAEDLRGI GIEQSPADYA ERLAKLTKAC GLDGVVCSAH EATRLKNSCG
     KDFKLVTPGI RPEGSAAGDQ RRIMTPVEAV QAGVDYMVIG RPITQSATPA ETLRSILNSL
     A
//
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