KPR5_SCHPO
ID KPR5_SCHPO Reviewed; 341 AA.
AC P87171;
DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Ribose-phosphate pyrophosphokinase 5;
DE EC=2.7.6.1;
DE AltName: Full=Phosphoribosyl pyrophosphate synthase 5;
GN ORFNames=SPBC3D6.06c;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1] {ECO:0000312|EMBL:CAB09126.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
CC -!- FUNCTION: 5-phosphoribose 1-diphosphate synthase involved in
CC nucleotide, histidine, and tryptophan biosynthesis. Active in
CC heteromultimeric complexes with other 5-phosphoribose 1-diphosphate
CC synthases (By similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + D-ribose 5-phosphate = 5-phospho-alpha-D-ribose 1-
CC diphosphate + AMP + H(+); Xref=Rhea:RHEA:15609, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:58017, ChEBI:CHEBI:78346,
CC ChEBI:CHEBI:456215; EC=2.7.6.1;
CC Evidence={ECO:0000250|UniProtKB:P38063};
CC -!- PATHWAY: Metabolic intermediate biosynthesis; 5-phospho-alpha-D-ribose
CC 1-diphosphate biosynthesis; 5-phospho-alpha-D-ribose 1-diphosphate from
CC D-ribose 5-phosphate (route I): step 1/1.
CC {ECO:0000250|UniProtKB:P38063}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P38063}.
CC -!- SIMILARITY: Belongs to the ribose-phosphate pyrophosphokinase family.
CC {ECO:0000255}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CU329671; CAB09126.1; -; Genomic_DNA.
DR PIR; T40366; T40366.
DR RefSeq; NP_595518.1; NM_001021427.2.
DR AlphaFoldDB; P87171; -.
DR SMR; P87171; -.
DR BioGRID; 277529; 7.
DR STRING; 4896.SPBC3D6.06c.1; -.
DR MaxQB; P87171; -.
DR PaxDb; P87171; -.
DR EnsemblFungi; SPBC3D6.06c.1; SPBC3D6.06c.1:pep; SPBC3D6.06c.
DR GeneID; 2541014; -.
DR KEGG; spo:SPBC3D6.06c; -.
DR PomBase; SPBC3D6.06c; -.
DR VEuPathDB; FungiDB:SPBC3D6.06c; -.
DR eggNOG; KOG1448; Eukaryota.
DR HOGENOM; CLU_033546_1_0_1; -.
DR InParanoid; P87171; -.
DR OMA; MMLVGDI; -.
DR PhylomeDB; P87171; -.
DR Reactome; R-SPO-73843; 5-Phosphoribose 1-diphosphate biosynthesis.
DR UniPathway; UPA00087; UER00172.
DR PRO; PR:P87171; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0005737; C:cytoplasm; ISO:PomBase.
DR GO; GO:0002189; C:ribose phosphate diphosphokinase complex; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0004749; F:ribose phosphate diphosphokinase activity; ISO:PomBase.
DR GO; GO:0006015; P:5-phosphoribose 1-diphosphate biosynthetic process; ISO:PomBase.
DR GO; GO:0031505; P:fungal-type cell wall organization; IEA:UniProt.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0006164; P:purine nucleotide biosynthetic process; IBA:GO_Central.
DR GO; GO:0009156; P:ribonucleoside monophosphate biosynthetic process; IEA:InterPro.
DR CDD; cd06223; PRTases_typeI; 1.
DR Gene3D; 3.40.50.2020; -; 2.
DR InterPro; IPR000842; PRib_PP_synth_CS.
DR InterPro; IPR029099; Pribosyltran_N.
DR InterPro; IPR000836; PRibTrfase_dom.
DR InterPro; IPR029057; PRTase-like.
DR InterPro; IPR005946; Rib-P_diPkinase.
DR PANTHER; PTHR10210; PTHR10210; 2.
DR Pfam; PF14572; Pribosyl_synth; 1.
DR Pfam; PF13793; Pribosyltran_N; 1.
DR SUPFAM; SSF53271; SSF53271; 1.
DR TIGRFAMs; TIGR01251; ribP_PPkin; 1.
DR PROSITE; PS00114; PRPP_SYNTHASE; 1.
DR PROSITE; PS00103; PUR_PYR_PR_TRANSFER; 1.
PE 3: Inferred from homology;
KW ATP-binding; Cytoplasm; Kinase; Magnesium; Metal-binding;
KW Nucleotide biosynthesis; Nucleotide-binding; Reference proteome;
KW Transferase.
FT CHAIN 1..341
FT /note="Ribose-phosphate pyrophosphokinase 5"
FT /id="PRO_0000309464"
FT BINDING 152
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P38063, ECO:0000255"
FT BINDING 154
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P38063, ECO:0000255"
FT BINDING 167
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P38063, ECO:0000255"
SQ SEQUENCE 341 AA; 37338 MW; 3D7348E9AA0F9DC7 CRC64;
MKNLVVFGTE SHPKLTESIC EHLCLDIGRV ELSKFSNGET SVRIKQSVRG CDVYIVSPAS
GQVNDHLMEL LIMISACKTA SAKKVTAVLP VFPYSRQPDQ KFSFSGAPLS DLQDAVVPCK
KQTGYHPWIA QSGTLVADLL MCSGADHIIT MDLHDPQFQG FFDIPVDNLF GRPLLKHYIS
LNIPNYHNAV IVSPDAGGAK RATAIADALG LDFALIHKNR RHEYGTSLML VGDVQNKVAI
LIDDLIDTAY TLVRAAEFVK EHGASKIYAL VTHCVLSGDA IERVKLSCID KLIVTNTAPQ
TITPSGCFDI IDVAPTFAEA IRRIHNGESI SILYDHNQVW V
