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Database: UniProt
Entry: K9QVN7_NOSS7
LinkDB: K9QVN7_NOSS7
Original site: K9QVN7_NOSS7 
ID   K9QVN7_NOSS7            Unreviewed;       240 AA.
AC   K9QVN7;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   24-JAN-2024, entry version 59.
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   OrderedLocusNames=Nos7524_3906 {ECO:0000313|EMBL:AFY49680.1};
OS   Nostoc sp. (strain ATCC 29411 / PCC 7524).
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Nostocaceae; Nostoc.
OX   NCBI_TaxID=28072 {ECO:0000313|EMBL:AFY49680.1, ECO:0000313|Proteomes:UP000010378};
RN   [1] {ECO:0000313|Proteomes:UP000010378}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29411 / PCC 7524 {ECO:0000313|Proteomes:UP000010378};
RX   PubMed=23277585; DOI=10.1073/pnas.1217107110;
RA   Shih P.M., Wu D., Latifi A., Axen S.D., Fewer D.P., Talla E., Calteau A.,
RA   Cai F., Tandeau de Marsac N., Rippka R., Herdman M., Sivonen K.,
RA   Coursin T., Laurent T., Goodwin L., Nolan M., Davenport K.W., Han C.S.,
RA   Rubin E.M., Eisen J.A., Woyke T., Gugger M., Kerfeld C.A.;
RT   "Improving the coverage of the cyanobacterial phylum using diversity-driven
RT   genome sequencing.";
RL   Proc. Natl. Acad. Sci. U.S.A. 110:1053-1058(2013).
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; CP003552; AFY49680.1; -; Genomic_DNA.
DR   RefSeq; WP_015140100.1; NC_019684.1.
DR   AlphaFoldDB; K9QVN7; -.
DR   STRING; 28072.Nos7524_3906; -.
DR   KEGG; nop:Nos7524_3906; -.
DR   PATRIC; fig|28072.8.peg.4270; -.
DR   eggNOG; COG0284; Bacteria.
DR   HOGENOM; CLU_067069_1_0_3; -.
DR   OMA; FWKVGLE; -.
DR   OrthoDB; 9806203at2; -.
DR   UniPathway; UPA00070; UER00120.
DR   Proteomes; UP000010378; Chromosome.
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}; Reference proteome {ECO:0000313|Proteomes:UP000010378}.
FT   DOMAIN          8..233
FT                   /note="Orotidine 5'-phosphate decarboxylase"
FT                   /evidence="ECO:0000259|SMART:SM00934"
FT   ACT_SITE        64
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01200"
FT   BINDING         14
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01200"
FT   BINDING         35
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01200"
FT   BINDING         62..71
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01200"
FT   BINDING         126
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01200"
FT   BINDING         188
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01200"
FT   BINDING         197
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01200"
FT   BINDING         217
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01200"
FT   BINDING         218
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01200"
SQ   SEQUENCE   240 AA;  25625 MW;  380210A6E1CB9032 CRC64;
     MGNGIEQRII VPLDVADEKS AIALIDKLEA VSFWKVGLEL FTSVGPKILE VLKSRNKQIF
     LDLKFHDIPN TVAGACRAAA GYGVDLLTIH ATGGRNALKA ATEAIQEGAA QAGVKPPKLI
     AVTVLTSISA RQLSCDLKIP IELPEYALEM ALMAKEAGLD GAVCSPQEVA QLRQTCGDDF
     LFVCPGVRPT WAEPGDQKRS LTPAQAIQVG ADYLVIGRPI TAAAEPELAW KRIVQELTTT
//
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