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Database: UniProt
Entry: Q386K8_TRYB2
LinkDB: Q386K8_TRYB2
Original site: Q386K8_TRYB2 
ID   Q386K8_TRYB2            Unreviewed;       441 AA.
AC   Q386K8;
DT   22-NOV-2005, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2005, sequence version 1.
DT   27-MAR-2024, entry version 96.
DE   SubName: Full=Phosphoribosylpyrophosphate synthetase, putative {ECO:0000313|EMBL:EAN79273.1};
DE            EC=2.7.6.1 {ECO:0000313|EMBL:EAN79273.1};
GN   ORFNames=Tb11.02.0530 {ECO:0000313|EMBL:EAN79273.1};
OS   Trypanosoma brucei brucei (strain 927/4 GUTat10.1).
OC   Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC   Trypanosomatida; Trypanosomatidae; Trypanosoma.
OX   NCBI_TaxID=185431 {ECO:0000313|EMBL:EAN79273.1, ECO:0000313|Proteomes:UP000008524};
RN   [1] {ECO:0000313|EMBL:EAN79273.1, ECO:0000313|Proteomes:UP000008524}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=927/4 GUTat10.1 {ECO:0000313|EMBL:EAN79273.1,
RC   ECO:0000313|Proteomes:UP000008524};
RX   PubMed=16020726; DOI=10.1126/science.1112642;
RA   Berriman M., Ghedin E., Hertz-Fowler C., Blandin G., Renauld H.,
RA   Bartholomeu D.C., Lennard N.J., Caler E., Hamlin N.E., Haas B., Bohme U.,
RA   Hannick L., Aslett M.A., Shallom J., Marcello L., Hou L., Wickstead B.,
RA   Alsmark U.C., Arrowsmith C., Atkin R.J., Barron A.J., Bringaud F.,
RA   Brooks K., Carrington M., Cherevach I., Chillingworth T.J., Churcher C.,
RA   Clark L.N., Corton C.H., Cronin A., Davies R.M., Doggett J., Djikeng A.,
RA   Feldblyum T., Field M.C., Fraser A., Goodhead I., Hance Z., Harper D.,
RA   Harris B.R., Hauser H., Hostetler J., Ivens A., Jagels K., Johnson D.,
RA   Johnson J., Jones K., Kerhornou A.X., Koo H., Larke N., Landfear S.,
RA   Larkin C., Leech V., Line A., Lord A., Macleod A., Mooney P.J., Moule S.,
RA   Martin D.M., Morgan G.W., Mungall K., Norbertczak H., Ormond D., Pai G.,
RA   Peacock C.S., Peterson J., Quail M.A., Rabbinowitsch E., Rajandream M.A.,
RA   Reitter C., Salzberg S.L., Sanders M., Schobel S., Sharp S., Simmonds M.,
RA   Simpson A.J., Tallon L., Turner C.M., Tait A., Tivey A.R., Van Aken S.,
RA   Walker D., Wanless D., Wang S., White B., White O., Whitehead S.,
RA   Woodward J., Wortman J., Adams M.D., Embley T.M., Gull K., Ullu E.,
RA   Barry J.D., Fairlamb A.H., Opperdoes F., Barrell B.G., Donelson J.E.,
RA   Hall N., Fraser C.M., Melville S.E., El-Sayed N.M.;
RT   "The genome of the African trypanosome Trypanosoma brucei.";
RL   Science 309:416-422(2005).
CC   -!- SIMILARITY: Belongs to the ribose-phosphate pyrophosphokinase family.
CC       {ECO:0000256|ARBA:ARBA00006478}.
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DR   EMBL; CH464491; EAN79273.1; -; Genomic_DNA.
DR   RefSeq; XP_828385.1; XM_823292.1.
DR   AlphaFoldDB; Q386K8; -.
DR   STRING; 185431.Q386K8; -.
DR   PaxDb; 5691-EAN79273; -.
DR   GeneID; 3664028; -.
DR   KEGG; tbr:Tb11.02.0530; -.
DR   eggNOG; KOG1448; Eukaryota.
DR   InParanoid; Q386K8; -.
DR   OrthoDB; 276387at2759; -.
DR   Proteomes; UP000008524; Chromosome 11 Scaffold 1.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0020015; C:glycosome; IDA:GeneDB.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0002189; C:ribose phosphate diphosphokinase complex; IBA:GO_Central.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0004749; F:ribose phosphate diphosphokinase activity; IBA:GO_Central.
DR   GO; GO:0006015; P:5-phosphoribose 1-diphosphate biosynthetic process; IBA:GO_Central.
DR   GO; GO:0006164; P:purine nucleotide biosynthetic process; IBA:GO_Central.
DR   CDD; cd06223; PRTases_typeI; 1.
DR   Gene3D; 3.40.50.2020; -; 2.
DR   InterPro; IPR029099; Pribosyltran_N.
DR   InterPro; IPR000836; PRibTrfase_dom.
DR   InterPro; IPR029057; PRTase-like.
DR   InterPro; IPR005946; Rib-P_diPkinase.
DR   NCBIfam; TIGR01251; ribP_PPkin; 1.
DR   PANTHER; PTHR10210; RIBOSE-PHOSPHATE DIPHOSPHOKINASE FAMILY MEMBER; 1.
DR   PANTHER; PTHR10210:SF117; SYNTHETASE, PUTATIVE-RELATED; 1.
DR   Pfam; PF14572; Pribosyl_synth; 1.
DR   Pfam; PF13793; Pribosyltran_N; 1.
DR   SMART; SM01400; Pribosyltran_N; 1.
DR   SUPFAM; SSF53271; PRTase-like; 1.
PE   3: Inferred from homology;
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Nucleotide biosynthesis {ECO:0000256|ARBA:ARBA00022727};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008524};
KW   Transferase {ECO:0000313|EMBL:EAN79273.1};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        31..62
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          123..242
FT                   /note="Ribose-phosphate pyrophosphokinase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF13793"
SQ   SEQUENCE   441 AA;  49243 MW;  E26FF4F140C9D8AD CRC64;
     MGCAMHFARL YLSFSFRSPT YFQCDSCFCP FALYAFFAVT CVLSSPAYPI WFLPLLIINF
     VYRLDRCDNK KLGYVRQSPS RAISNMQGQA DALTPKAQRV AAGETYFYRE HRKPQVETSY
     RIRVISGTAN YALSESVAKY LKVDLCRTEI KRFANGELNI KVVDDVRGDD CFILQPIAAN
     EHTDINTAMM ELLLLVHTLK LSSAKRITAI VPYFAYSRQD RKTEPRVPIS ASAVAQLLQC
     MGVDRVVTVD LHCGQIQGFF RNMPVDNLLM FPEFATYVMR QPWFDRERTV VVSPDAGGVE
     RANVLADRIG ASHIVTILKR RSGPGKVDSM QTVGNVEGYT CVIVDDIVDT AGTLCKACEL
     LRDMGALRLV ACATHGILTD PACERISQCD ALTELVVSDS IAQNINSQKC NKLTVLTIAP
     LLVQAIYNLH FECSLSSLFR T
//
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