KPRS_SACS2
ID KPRS_SACS2 Reviewed; 291 AA.
AC Q97Z86;
DT 25-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2002, sequence version 2.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Ribose-phosphate pyrophosphokinase {ECO:0000255|HAMAP-Rule:MF_00583};
DE Short=RPPK {ECO:0000255|HAMAP-Rule:MF_00583};
DE EC=2.7.6.1 {ECO:0000255|HAMAP-Rule:MF_00583};
DE AltName: Full=5-phospho-D-ribosyl alpha-1-diphosphate {ECO:0000255|HAMAP-Rule:MF_00583, ECO:0000303|PubMed:25605536};
DE AltName: Full=Phosphoribosyl diphosphate synthase {ECO:0000255|HAMAP-Rule:MF_00583};
DE AltName: Full=Phosphoribosyl pyrophosphate synthase {ECO:0000255|HAMAP-Rule:MF_00583};
DE Short=P-Rib-PP synthase {ECO:0000255|HAMAP-Rule:MF_00583};
DE Short=PRPP synthase {ECO:0000255|HAMAP-Rule:MF_00583, ECO:0000303|PubMed:25605536};
DE Short=PRPPase {ECO:0000255|HAMAP-Rule:MF_00583};
GN Name=prs {ECO:0000255|HAMAP-Rule:MF_00583, ECO:0000303|PubMed:25605536};
GN OrderedLocusNames=SSO1045;
OS Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
OS (Sulfolobus solfataricus).
OC Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC Saccharolobus.
OX NCBI_TaxID=273057;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35092 / DSM 1617 / JCM 11322 / P2;
RX PubMed=11427726; DOI=10.1073/pnas.141222098;
RA She Q., Singh R.K., Confalonieri F., Zivanovic Y., Allard G., Awayez M.J.,
RA Chan-Weiher C.C.-Y., Clausen I.G., Curtis B.A., De Moors A., Erauso G.,
RA Fletcher C., Gordon P.M.K., Heikamp-de Jong I., Jeffries A.C., Kozera C.J.,
RA Medina N., Peng X., Thi-Ngoc H.P., Redder P., Schenk M.E., Theriault C.,
RA Tolstrup N., Charlebois R.L., Doolittle W.F., Duguet M., Gaasterland T.,
RA Garrett R.A., Ragan M.A., Sensen C.W., Van der Oost J.;
RT "The complete genome of the crenarchaeon Sulfolobus solfataricus P2.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:7835-7840(2001).
RN [2]
RP REVIEW, AND SUBUNIT.
RX PubMed=28031352; DOI=10.1128/mmbr.00040-16;
RA Hove-Jensen B., Andersen K.R., Kilstrup M., Martinussen J., Switzer R.L.,
RA Willemoes M.;
RT "Phosphoribosyl diphosphate (PRPP): biosynthesis, enzymology, utilization,
RT and metabolic significance.";
RL Microbiol. Mol. Biol. Rev. 81:E00040-E00040(2017).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS) IN COMPLEX WITH ATP ANALOG,
RP FUNCTION, AND SUBUNIT.
RX PubMed=25605536; DOI=10.1007/s00792-014-0726-x;
RA Andersen R.W., Leggio L.L., Hove-Jensen B., Kadziola A.;
RT "Structure of dimeric, recombinant Sulfolobus solfataricus phosphoribosyl
RT diphosphate synthase: a bent dimer defining the adenine specificity of the
RT substrate ATP.";
RL Extremophiles 19:407-415(2015).
CC -!- FUNCTION: Involved in the biosynthesis of the central metabolite
CC phospho-alpha-D-ribosyl-1-pyrophosphate (PRPP) via the transfer of
CC pyrophosphoryl group from ATP to 1-hydroxyl of ribose-5-phosphate (Rib-
CC 5-P). {ECO:0000255|HAMAP-Rule:MF_00583, ECO:0000305|PubMed:25605536}.
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; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_00583};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00583};
CC Note=Binds 2 Mg(2+) ions per subunit. {ECO:0000255|HAMAP-
CC Rule:MF_00583};
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. {ECO:0000255|HAMAP-
CC Rule:MF_00583}.
CC -!- SUBUNIT: Homodimer. {ECO:0000303|PubMed:28031352,
CC ECO:0000305|PubMed:25605536}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00583}.
CC -!- SIMILARITY: Belongs to the ribose-phosphate pyrophosphokinase family.
CC Class III (archaeal) subfamily. {ECO:0000255|HAMAP-Rule:MF_00583,
CC ECO:0000303|PubMed:28031352}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAK41307.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={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; AE006641; AAK41307.1; ALT_INIT; Genomic_DNA.
DR PIR; D90256; D90256.
DR RefSeq; WP_009989183.1; NC_002754.1.
DR PDB; 4TWB; X-ray; 2.80 A; A/B/C/D/E/F=1-291.
DR PDBsum; 4TWB; -.
DR AlphaFoldDB; Q97Z86; -.
DR SMR; Q97Z86; -.
DR STRING; 273057.SSO1045; -.
DR EnsemblBacteria; AAK41307; AAK41307; SSO1045.
DR GeneID; 44129974; -.
DR KEGG; sso:SSO1045; -.
DR PATRIC; fig|273057.12.peg.1039; -.
DR eggNOG; arCOG00067; Archaea.
DR HOGENOM; CLU_033546_2_2_2; -.
DR InParanoid; Q97Z86; -.
DR OMA; FGWARQD; -.
DR PhylomeDB; Q97Z86; -.
DR BRENDA; 2.7.6.1; 6163.
DR UniPathway; UPA00087; UER00172.
DR Proteomes; UP000001974; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
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:UniProtKB-UniRule.
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: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:UniProtKB-UniRule.
DR CDD; cd06223; PRTases_typeI; 1.
DR Gene3D; 3.40.50.2020; -; 2.
DR HAMAP; MF_00583_A; RibP_PPkinase_A; 1.
DR InterPro; IPR029099; Pribosyltran_N.
DR InterPro; IPR000836; PRibTrfase_dom.
DR InterPro; IPR029057; PRTase-like.
DR InterPro; IPR005946; Rib-P_diPkinase.
DR InterPro; IPR037514; Rib-P_diPkinase_arc.
DR PANTHER; PTHR10210; PTHR10210; 1.
DR Pfam; PF00156; Pribosyltran; 1.
DR Pfam; PF13793; Pribosyltran_N; 1.
DR SUPFAM; SSF53271; SSF53271; 1.
DR TIGRFAMs; TIGR01251; ribP_PPkin; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Cytoplasm; Kinase; Magnesium; Metal-binding;
KW Nucleotide biosynthesis; Nucleotide-binding; Reference proteome;
KW Transferase.
FT CHAIN 1..291
FT /note="Ribose-phosphate pyrophosphokinase"
FT /id="PRO_0000141248"
FT ACT_SITE 188
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00583"
FT BINDING 34..36
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00583,
FT ECO:0000305|PubMed:25605536, ECO:0007744|PDB:4TWB"
FT BINDING 93..94
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00583,
FT ECO:0000305|PubMed:25605536, ECO:0007744|PDB:4TWB"
FT BINDING 127
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00583"
FT BINDING 165
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00583"
FT BINDING 190
FT /ligand="D-ribose 5-phosphate"
FT /ligand_id="ChEBI:CHEBI:78346"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00583"
FT BINDING 216
FT /ligand="D-ribose 5-phosphate"
FT /ligand_id="ChEBI:CHEBI:78346"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00583"
FT BINDING 220..224
FT /ligand="D-ribose 5-phosphate"
FT /ligand_id="ChEBI:CHEBI:78346"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00583,
FT ECO:0000269|PubMed:25605536, ECO:0007744|PDB:4TWB"
FT STRAND 2..5
FT /evidence="ECO:0007829|PDB:4TWB"
FT HELIX 12..20
FT /evidence="ECO:0007829|PDB:4TWB"
FT STRAND 24..26
FT /evidence="ECO:0007829|PDB:4TWB"
FT STRAND 28..31
FT /evidence="ECO:0007829|PDB:4TWB"
FT STRAND 37..40
FT /evidence="ECO:0007829|PDB:4TWB"
FT STRAND 49..53
FT /evidence="ECO:0007829|PDB:4TWB"
FT HELIX 60..76
FT /evidence="ECO:0007829|PDB:4TWB"
FT STRAND 80..88
FT /evidence="ECO:0007829|PDB:4TWB"
FT HELIX 105..114
FT /evidence="ECO:0007829|PDB:4TWB"
FT TURN 115..117
FT /evidence="ECO:0007829|PDB:4TWB"
FT STRAND 120..125
FT /evidence="ECO:0007829|PDB:4TWB"
FT HELIX 131..134
FT /evidence="ECO:0007829|PDB:4TWB"
FT STRAND 137..142
FT /evidence="ECO:0007829|PDB:4TWB"
FT HELIX 145..155
FT /evidence="ECO:0007829|PDB:4TWB"
FT STRAND 157..165
FT /evidence="ECO:0007829|PDB:4TWB"
FT HELIX 166..168
FT /evidence="ECO:0007829|PDB:4TWB"
FT HELIX 169..178
FT /evidence="ECO:0007829|PDB:4TWB"
FT STRAND 183..185
FT /evidence="ECO:0007829|PDB:4TWB"
FT TURN 206..209
FT /evidence="ECO:0007829|PDB:4TWB"
FT STRAND 210..221
FT /evidence="ECO:0007829|PDB:4TWB"
FT HELIX 223..233
FT /evidence="ECO:0007829|PDB:4TWB"
FT TURN 234..236
FT /evidence="ECO:0007829|PDB:4TWB"
FT STRAND 240..247
FT /evidence="ECO:0007829|PDB:4TWB"
FT HELIX 253..259
FT /evidence="ECO:0007829|PDB:4TWB"
FT STRAND 262..268
FT /evidence="ECO:0007829|PDB:4TWB"
FT STRAND 279..281
FT /evidence="ECO:0007829|PDB:4TWB"
FT HELIX 284..289
FT /evidence="ECO:0007829|PDB:4TWB"
SQ SEQUENCE 291 AA; 32179 MW; A18743D629CF60A6 CRC64;
MIIIGGSATN GIDESLSKIL SIPLVKVENK IFPDGESYIR VPSSIRDEEV LLVQTTDYPQ
DKHLIELFLI AETIRDLGAK KLTAIVPYLA YSRQDRRFKD GEAISIKTIL HILSEVGVNT
LVVVEPHKPE ELSYFKGELK IVHPYHQIAR KIKEIIEDPF ILAPDRGALD RARKIAEEIN
APYSYIEKER DRTTGEVRIK EAPNINLKGK DVVIIDDIIS TGGTIVQATR LAYSLGAKSV
TAAAIHLLLV GGAKERLREV GVKTLIGTNT INVNDKDIIT IDVSQSIALS L
