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Database: UniProt
Entry: W3Y0B0_9FIRM
LinkDB: W3Y0B0_9FIRM
Original site: W3Y0B0_9FIRM 
ID   W3Y0B0_9FIRM            Unreviewed;       239 AA.
AC   W3Y0B0;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   24-JAN-2024, entry version 48.
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   ECO:0000313|EMBL:ETS91668.1};
GN   ORFNames=HMPREF1521_1155 {ECO:0000313|EMBL:ETS91668.1};
OS   Veillonella sp. AS16.
OC   Bacteria; Bacillota; Negativicutes; Veillonellales; Veillonellaceae;
OC   Veillonella.
OX   NCBI_TaxID=936589 {ECO:0000313|EMBL:ETS91668.1, ECO:0000313|Proteomes:UP000019042};
RN   [1] {ECO:0000313|EMBL:ETS91668.1, ECO:0000313|Proteomes:UP000019042}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AS16 {ECO:0000313|EMBL:ETS91668.1,
RC   ECO:0000313|Proteomes:UP000019042};
RA   Durkin A.S., McCorrison J., Torralba M., Gillis M., Haft D.H., Methe B.,
RA   Sutton G., Nelson K.E.;
RL   Submitted (JAN-2014) 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:ETS91668.1}.
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DR   EMBL; AZYX01000022; ETS91668.1; -; Genomic_DNA.
DR   RefSeq; WP_038118010.1; NZ_AZYX01000022.1.
DR   AlphaFoldDB; W3Y0B0; -.
DR   PATRIC; fig|936589.3.peg.1600; -.
DR   eggNOG; COG0284; Bacteria.
DR   UniPathway; UPA00070; UER00120.
DR   Proteomes; UP000019042; 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          5..230
FT                   /note="Orotidine 5'-phosphate decarboxylase"
FT                   /evidence="ECO:0000259|SMART:SM00934"
FT   ACT_SITE        62
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01200"
FT   BINDING         11
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01200"
FT   BINDING         33
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01200"
FT   BINDING         60..69
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01200"
FT   BINDING         124
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01200"
FT   BINDING         185
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01200"
FT   BINDING         194
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"
FT   BINDING         215
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01200"
SQ   SEQUENCE   239 AA;  25855 MW;  67A192522B55614C CRC64;
     MADDRLIVAL DVSTMDEVKA IVTSLGDSVS FYKVGMELFY AEGEKTIRYL QEQGKHVFLD
     LKLHDIPNTV AHGVSTLTYV GANLITIHGQ GGPVMMKAAV QAARESAEKL GVERPKLLAI
     TVLTSFDEEA WTATGGQLPI SDQVIRLAKL AKECGMDGVV CSALEAKMIR QACGEDFLIV
     TPGIRPSFAT TDDQKRIATP ASALQDGASR LVIGRPITQA KKPREAVRLI IEEMESLSK
//
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