ID D7H9X4_VIBCL Unreviewed; 231 AA.
AC D7H9X4;
DT 10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT 10-AUG-2010, sequence version 1.
DT 24-JAN-2024, entry version 64.
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=VCRC385_02217 {ECO:0000313|EMBL:EFH75855.1};
OS Vibrio cholerae RC385.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=345074 {ECO:0000313|EMBL:EFH75855.1, ECO:0000313|Proteomes:UP000004696};
RN [1] {ECO:0000313|Proteomes:UP000004696}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RC385 {ECO:0000313|Proteomes:UP000004696};
RA Heidelberg J.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:EFH75855.1, ECO:0000313|Proteomes:UP000004696}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RC385 {ECO:0000313|EMBL:EFH75855.1,
RC ECO:0000313|Proteomes:UP000004696};
RG The Broad Institute Genome Sequencing Platform;
RA Colwell R., Grim C.J., Young S., Zeng Q., Koehrsen M., Alvarado L.,
RA Berlin A., Borenstein D., Chapman S.B., Chen Z., Engels R., Freedman E.,
RA Gellesch M., Goldberg J., Griggs A., Gujja S., Heilman E.R., Heiman D.,
RA Hepburn T., Howarth C., Jen D., Larson L., Lewis B., Mehta T., Park D.,
RA Pearson M., Richards J., Roberts A., Saif S., Shea T., Shenoy N., Sisk P.,
RA Stolte C., Sykes S., Walk T., White J., Yandava C., Borodovsky M.,
RA Heidelberg J., Haas B., Nusbaum C., Birren B.;
RT "The genome sequence of Vibrio cholerae RC385.";
RL Submitted (OCT-2009) 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}.
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DR EMBL; GG774555; EFH75855.1; -; Genomic_DNA.
DR RefSeq; WP_000999557.1; NZ_GG774555.1.
DR AlphaFoldDB; D7H9X4; -.
DR PATRIC; fig|345074.23.peg.3817; -.
DR HOGENOM; CLU_067069_0_0_6; -.
DR UniPathway; UPA00070; UER00120.
DR Proteomes; UP000004696; 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..226
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 120
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01200"
FT BINDING 181
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01200"
FT BINDING 190
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01200"
FT BINDING 210
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01200"
FT BINDING 211
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01200"
SQ SEQUENCE 231 AA; 24989 MW; EA9E84AA980B582C CRC64;
MNDPKVIVAL DYDNLADALA FVDKIDPSTC RLKVGKEMFT LFGPDFVREL HKRGFSVFLD
LKFHDIPNTC SKAVKAAAEL GVWMVNVHAS GGERMMAASR EILEPYGKDR PLLIGVTVLT
SMESADLQGI GILSAPQDHV LRLATLTKNA GLDGVVCSAQ EASLLKQHLG REFKLVTPGI
RPAGSEQGDQ RRIMTPAQAI ASGSDYLVIG RPITQAAHPE VVLEEINSSL V
//
