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Database: UniProt
Entry: KPRS_METJA
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Original site: KPRS_METJA 
ID   KPRS_METJA              Reviewed;         284 AA.
AC   Q58761;
DT   25-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT   25-OCT-2002, sequence version 2.
DT   27-MAR-2024, entry version 132.
DE   RecName: Full=Ribose-phosphate pyrophosphokinase {ECO:0000255|HAMAP-Rule:MF_00583, ECO:0000303|PubMed:16288921};
DE            Short=RPPK {ECO:0000255|HAMAP-Rule:MF_00583, ECO:0000303|PubMed:16288921};
DE            EC=2.7.6.1 {ECO:0000255|HAMAP-Rule:MF_00583, ECO:0000269|PubMed:16288921};
DE   AltName: Full=5-phospho-D-ribosyl alpha-1-diphosphate synthase {ECO:0000255|HAMAP-Rule:MF_00583};
DE   AltName: Full=Phosphoribosyl diphosphate synthase {ECO:0000255|HAMAP-Rule:MF_00583, ECO:0000303|PubMed:16288921};
DE   AltName: Full=Phosphoribosyl pyrophosphate synthase {ECO:0000255|HAMAP-Rule:MF_00583, ECO:0000303|PubMed:16288921};
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:16288921};
DE            Short=PRPPase {ECO:0000255|HAMAP-Rule:MF_00583};
GN   Name=prs {ECO:0000255|HAMAP-Rule:MF_00583, ECO:0000303|PubMed:16288921};
GN   OrderedLocusNames=MJ1366;
OS   Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM
OS   10045 / NBRC 100440) (Methanococcus jannaschii).
OC   Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC   Methanocaldococcaceae; Methanocaldococcus.
OX   NCBI_TaxID=243232;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440;
RX   PubMed=8688087; DOI=10.1126/science.273.5278.1058;
RA   Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., Sutton G.G.,
RA   Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., Kerlavage A.R.,
RA   Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., Overbeek R.,
RA   Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., Scott J.L.,
RA   Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., Utterback T.R.,
RA   Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., Cotton M.D.,
RA   Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., Klenk H.-P.,
RA   Fraser C.M., Smith H.O., Woese C.R., Venter J.C.;
RT   "Complete genome sequence of the methanogenic archaeon, Methanococcus
RT   jannaschii.";
RL   Science 273:1058-1073(1996).
RN   [2]
RP   REVIEW, AND COFACTOR.
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 (2.65 ANGSTROMS) IN COMPLEX WITH SUBSTRATES,
RP   FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR,
RP   SUBSTRATE SPECIFICITY, ACTIVITY REGULATION, SUBUNIT, AND PATHWAY.
RC   STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440;
RX   PubMed=16288921; DOI=10.1016/j.jmb.2005.10.001;
RA   Kadziola A., Jepsen C.H., Johansson E., McGuire J., Larsen S.,
RA   Hove-Jensen B.;
RT   "Novel class III phosphoribosyl diphosphate synthase: structure and
RT   properties of the tetrameric, phosphate-activated, non-allosterically
RT   inhibited enzyme from Methanocaldococcus jannaschii.";
RL   J. Mol. Biol. 354:815-828(2005).
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). It can also use dATP as diphosphoryl donor. {ECO:0000255|HAMAP-
CC       Rule:MF_00583, ECO:0000269|PubMed:16288921}.
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, ECO:0000269|PubMed:16288921};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00583,
CC         ECO:0000269|PubMed:16288921};
CC       Note=Binds 2 Mg(2+) ions per subunit (PubMed:28031352). Mn(2+) is also
CC       accepted, but the activity is less than 15% of that obtained with
CC       Mg(2+), when assayed at pH 9.5 (PubMed:16288921). {ECO:0000255|HAMAP-
CC       Rule:MF_00583, ECO:0000269|PubMed:16288921,
CC       ECO:0000303|PubMed:28031352};
CC   -!- ACTIVITY REGULATION: Activated by inorganic phosphate, with a maximal
CC       activity at 190 mM. Above this concentration inorganic phosphate
CC       progressively inhibits the kinase. Completely inhibited by ADP, and
CC       partially inhibited by alpha,beta-methylene ATP (mATP). Lack of
CC       allosteric regulation. {ECO:0000269|PubMed:16288921}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=2.6 mM for ATP (at pH 9 and 85 degrees Celsius)
CC         {ECO:0000269|PubMed:16288921};
CC         KM=2.8 mM for ribose 5-phosphate (at pH 9 and 85 degrees Celsius)
CC         {ECO:0000269|PubMed:16288921};
CC         Vmax=2.2 mmol/min/mg enzyme (at pH 9 and 85 degrees Celsius)
CC         {ECO:0000269|PubMed:16288921};
CC       pH dependence:
CC         Optimum pH is 9.5. The activity declines strongly above pH 10.
CC         {ECO:0000269|PubMed:16288921};
CC       Temperature dependence:
CC         Optimum temperature is 85 degrees Celsius. 70% of maximal activity at
CC         72 and 95 degrees Celsius. {ECO:0000269|PubMed:16288921};
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, ECO:0000305|PubMed:16288921}.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:16288921}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00583}.
CC   -!- MISCELLANEOUS: M.jannaschii PRPP synthase is more compact than the PRPP
CC       synthase in the B.subtilis subunit. This is mainly due to truncations
CC       of eight residues at the N terminus, 14 residues at the C-terminus and
CC       to a seven-residue shorter loop. {ECO:0000305|PubMed:16288921}.
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, ECO:0000305|PubMed:16288921}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAB99374.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; L77117; AAB99374.1; ALT_INIT; Genomic_DNA.
DR   PIR; E64470; E64470.
DR   PDB; 1U9Y; X-ray; 2.65 A; A/B/C/D=1-284.
DR   PDB; 1U9Z; X-ray; 2.80 A; A/B/C/D=1-284.
DR   PDBsum; 1U9Y; -.
DR   PDBsum; 1U9Z; -.
DR   AlphaFoldDB; Q58761; -.
DR   SMR; Q58761; -.
DR   STRING; 243232.MJ_1366; -.
DR   PaxDb; 243232-MJ_1366; -.
DR   EnsemblBacteria; AAB99374; AAB99374; MJ_1366.
DR   KEGG; mja:MJ_1366; -.
DR   eggNOG; arCOG00067; Archaea.
DR   HOGENOM; CLU_033546_2_2_2; -.
DR   InParanoid; Q58761; -.
DR   OrthoDB; 371997at2157; -.
DR   PhylomeDB; Q58761; -.
DR   BRENDA; 2.7.6.1; 3260.
DR   SABIO-RK; Q58761; -.
DR   UniPathway; UPA00087; UER00172.
DR   EvolutionaryTrace; Q58761; -.
DR   Proteomes; UP000000805; 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   NCBIfam; TIGR01251; ribP_PPkin; 1.
DR   PANTHER; PTHR10210:SF32; RIBOSE-PHOSPHATE DIPHOSPHOKINASE; 1.
DR   PANTHER; PTHR10210; RIBOSE-PHOSPHATE DIPHOSPHOKINASE FAMILY MEMBER; 1.
DR   Pfam; PF00156; Pribosyltran; 1.
DR   Pfam; PF13793; Pribosyltran_N; 1.
DR   SMART; SM01400; Pribosyltran_N; 1.
DR   SUPFAM; SSF53271; PRTase-like; 2.
PE   1: Evidence at protein level;
KW   3D-structure; ATP-binding; Cytoplasm; Kinase; Magnesium; Manganese;
KW   Metal-binding; Nucleotide biosynthesis; Nucleotide-binding;
KW   Reference proteome; Transferase.
FT   CHAIN           1..284
FT                   /note="Ribose-phosphate pyrophosphokinase"
FT                   /id="PRO_0000141238"
FT   ACT_SITE        186
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:0000269|PubMed:16288921, ECO:0007744|PDB:1U9Z"
FT   BINDING         92..93
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00583,
FT                   ECO:0000305|PubMed:16288921, ECO:0007744|PDB:1U9Z"
FT   BINDING         125
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00583"
FT   BINDING         163
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00583"
FT   BINDING         188
FT                   /ligand="D-ribose 5-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:78346"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00583"
FT   BINDING         212
FT                   /ligand="D-ribose 5-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:78346"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00583,
FT                   ECO:0000269|PubMed:16288921, ECO:0007744|PDB:1U9Z"
FT   BINDING         216..220
FT                   /ligand="D-ribose 5-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:78346"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00583,
FT                   ECO:0000269|PubMed:16288921, ECO:0007744|PDB:1U9Z"
FT   STRAND          2..5
FT                   /evidence="ECO:0007829|PDB:1U9Y"
FT   HELIX           7..9
FT                   /evidence="ECO:0007829|PDB:1U9Z"
FT   HELIX           10..19
FT                   /evidence="ECO:0007829|PDB:1U9Y"
FT   STRAND          27..31
FT                   /evidence="ECO:0007829|PDB:1U9Y"
FT   STRAND          37..41
FT                   /evidence="ECO:0007829|PDB:1U9Y"
FT   STRAND          47..53
FT                   /evidence="ECO:0007829|PDB:1U9Y"
FT   HELIX           59..74
FT                   /evidence="ECO:0007829|PDB:1U9Y"
FT   TURN            75..77
FT                   /evidence="ECO:0007829|PDB:1U9Y"
FT   STRAND          80..84
FT                   /evidence="ECO:0007829|PDB:1U9Y"
FT   TURN            89..92
FT                   /evidence="ECO:0007829|PDB:1U9Z"
FT   HELIX           104..115
FT                   /evidence="ECO:0007829|PDB:1U9Y"
FT   STRAND          117..123
FT                   /evidence="ECO:0007829|PDB:1U9Y"
FT   HELIX           127..132
FT                   /evidence="ECO:0007829|PDB:1U9Y"
FT   STRAND          137..140
FT                   /evidence="ECO:0007829|PDB:1U9Y"
FT   HELIX           143..150
FT                   /evidence="ECO:0007829|PDB:1U9Y"
FT   TURN            151..153
FT                   /evidence="ECO:0007829|PDB:1U9Y"
FT   STRAND          158..163
FT                   /evidence="ECO:0007829|PDB:1U9Y"
FT   HELIX           164..166
FT                   /evidence="ECO:0007829|PDB:1U9Y"
FT   HELIX           167..177
FT                   /evidence="ECO:0007829|PDB:1U9Y"
FT   STRAND          181..184
FT                   /evidence="ECO:0007829|PDB:1U9Y"
FT   STRAND          198..200
FT                   /evidence="ECO:0007829|PDB:1U9Y"
FT   STRAND          208..214
FT                   /evidence="ECO:0007829|PDB:1U9Y"
FT   STRAND          216..218
FT                   /evidence="ECO:0007829|PDB:1U9Y"
FT   HELIX           219..230
FT                   /evidence="ECO:0007829|PDB:1U9Y"
FT   STRAND          235..242
FT                   /evidence="ECO:0007829|PDB:1U9Y"
FT   HELIX           249..256
FT                   /evidence="ECO:0007829|PDB:1U9Y"
FT   STRAND          259..264
FT                   /evidence="ECO:0007829|PDB:1U9Y"
FT   STRAND          272..274
FT                   /evidence="ECO:0007829|PDB:1U9Y"
FT   HELIX           277..281
FT                   /evidence="ECO:0007829|PDB:1U9Y"
SQ   SEQUENCE   284 AA;  31395 MW;  9EAE9805785B1127 CRC64;
     MIVVSGSQSQ NLAFKVAKLL NTKLTRVEYK RFPDNEIYVR IVDEINDDEA VIINTQKNQN
     DAIVETILLC DALRDEGVKK ITLVAPYLAY ARQDKKFNPG EAISIRALAK IYSNIVDKLI
     TINPHETHIK DFFTIPFIYG DAVPKLAEYV KDKLNDPIVL APDKGALEFA KTASKILNAE
     YDYLEKTRLS PTEIQIAPKT LDAKDRDVFI VDDIISTGGT MATAVKLLKE QGAKKIIAAC
     VHPVLIGDAL NKLYSAGVEE VVGTDTYLSE VSKVSVAEVI VDLL
//
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