KPR1_SCHPO
ID KPR1_SCHPO Reviewed; 409 AA.
AC P41831;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Ribose-phosphate pyrophosphokinase 1;
DE EC=2.7.6.1;
DE AltName: Full=Phosphoribosyl pyrophosphate synthase 1;
GN ORFNames=SPAC4A8.14;
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]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RA Hilti N.;
RL Submitted (JAN-1995) to the EMBL/GenBank/DDBJ databases.
RN [2]
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).
RN [3]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
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 -!- 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 -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}.
CC -!- SIMILARITY: Belongs to the ribose-phosphate pyrophosphokinase family.
CC {ECO:0000305}.
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; X83866; CAA58747.1; -; Genomic_DNA.
DR EMBL; CU329670; CAB11484.1; -; Genomic_DNA.
DR PIR; S51326; S51326.
DR RefSeq; NP_593826.1; NM_001019255.2.
DR AlphaFoldDB; P41831; -.
DR SMR; P41831; -.
DR BioGRID; 279943; 29.
DR STRING; 4896.SPAC4A8.14.1; -.
DR iPTMnet; P41831; -.
DR MaxQB; P41831; -.
DR PaxDb; P41831; -.
DR PRIDE; P41831; -.
DR EnsemblFungi; SPAC4A8.14.1; SPAC4A8.14.1:pep; SPAC4A8.14.
DR GeneID; 2543525; -.
DR KEGG; spo:SPAC4A8.14; -.
DR PomBase; SPAC4A8.14; -.
DR VEuPathDB; FungiDB:SPAC4A8.14; -.
DR eggNOG; KOG1448; Eukaryota.
DR HOGENOM; CLU_033546_1_0_1; -.
DR InParanoid; P41831; -.
DR OMA; CKMKKHR; -.
DR PhylomeDB; P41831; -.
DR Reactome; R-SPO-73843; 5-Phosphoribose 1-diphosphate biosynthesis.
DR UniPathway; UPA00087; UER00172.
DR PRO; PR:P41831; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005634; C:nucleus; HDA: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; 2.
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; 2.
DR TIGRFAMs; TIGR01251; ribP_PPkin; 1.
DR PROSITE; PS00114; PRPP_SYNTHASE; 1.
PE 3: Inferred from homology;
KW ATP-binding; Cytoplasm; Kinase; Magnesium; Metal-binding;
KW Nucleotide biosynthesis; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Transferase.
FT CHAIN 1..409
FT /note="Ribose-phosphate pyrophosphokinase 1"
FT /id="PRO_0000141091"
FT BINDING 128
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255"
FT BINDING 130
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255"
FT BINDING 143
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255"
FT MOD_RES 199
FT /note="Phosphoserine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 409 AA; 45353 MW; 08157F6E93F2BFC6 CRC64;
MKSATIIGGG SHPELLHLIS NRLGITPCDV SLKRFANGET SVEIRESVRD KDVFILQSGS
STVNDSLMEL LIIISACKGG SAKRITAVMP YFPYSKQSKM RKYRDAITAR MVANLLTVAG
VDHIITLDLH ASQMQGFFTR PVDNLYAEPN IAEWIRRNVD DWEEAVVVSK NPGGAKRVTS
LADTLNLDFA LINTDRQRSS HFSQNFEDSI MDETEATETH VTNCSVYLDR PRIHTAKYLL
GHIIDDEEII TTPASVCSED YAQEVNLYSQ GGCPSDDDEE ENIMSASIYA ERMITLVGDV
NGKTALLIDD TIENPTAFIV ASEHLVKRCG AKRVIVIGTH GIFQNKCLKD LQSCEYIEQI
VVTNTYPIKP QAVLECDKLT VIDISGVLAE AIRRTHNGES ISFLFKKAF
