ID   KPRS_BACSU              Reviewed;         317 AA.
AC   P14193;
DT   01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1990, sequence version 1.
DT   27-MAR-2024, entry version 174.
DE   RecName: Full=Ribose-phosphate pyrophosphokinase {ECO:0000255|HAMAP-Rule:MF_00583, ECO:0000303|PubMed:10742175};
DE            Short=RPPK {ECO:0000255|HAMAP-Rule:MF_00583, ECO:0000303|PubMed:10742175};
DE            EC=2.7.6.1 {ECO:0000255|HAMAP-Rule:MF_00583, ECO:0000269|PubMed:16008562, ECO:0000269|PubMed:2169413};
DE   AltName: Full=5-phospho-D-ribosyl alpha-1-diphosphate synthase {ECO:0000255|HAMAP-Rule:MF_00583, ECO:0000303|PubMed:11790837};
DE   AltName: Full=Phosphoribosyl diphosphate synthase {ECO:0000255|HAMAP-Rule:MF_00583, ECO:0000303|PubMed:2169413};
DE   AltName: Full=Phosphoribosyl pyrophosphate synthase {ECO:0000255|HAMAP-Rule:MF_00583, ECO:0000303|PubMed:10742175};
DE            Short=P-Rib-PP synthase {ECO:0000255|HAMAP-Rule:MF_00583, ECO:0000303|PubMed:16008562};
DE            Short=PPRibP synthase {ECO:0000303|PubMed:2169413};
DE            Short=PRPP synthase {ECO:0000255|HAMAP-Rule:MF_00583, ECO:0000303|PubMed:11790837};
DE            Short=PRPPase {ECO:0000255|HAMAP-Rule:MF_00583, ECO:0000303|PubMed:11790837};
GN   Name=prs {ECO:0000255|HAMAP-Rule:MF_00583,
GN   ECO:0000303|PubMed:3038693}; OrderedLocusNames=BSU00510;
OS   Bacillus subtilis (strain 168).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=224308;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2555671; DOI=10.1007/bf00332425;
RA   Nilsson D., Hove-Jensen B., Arnvig K.;
RT   "Primary structure of the tms and prs genes of Bacillus subtilis.";
RL   Mol. Gen. Genet. 218:565-571(1989).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=7584024; DOI=10.1093/dnares/1.1.1;
RA   Ogasawara N., Nakai S., Yoshikawa H.;
RT   "Systematic sequencing of the 180 kilobase region of the Bacillus subtilis
RT   chromosome containing the replication origin.";
RL   DNA Res. 1:1-14(1994).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=9384377; DOI=10.1038/36786;
RA   Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA   Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA   Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA   Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA   Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA   Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA   Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA   Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA   Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA   Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA   Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA   Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA   Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA   Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA   Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA   Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA   Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA   Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA   Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA   Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA   Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA   Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA   Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA   Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA   Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA   Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA   Yoshikawa H., Danchin A.;
RT   "The complete genome sequence of the Gram-positive bacterium Bacillus
RT   subtilis.";
RL   Nature 390:249-256(1997).
RN   [4]
RP   PROTEIN SEQUENCE OF 2-15, FUNCTION, CATALYTIC ACTIVITY, COFACTOR,
RP   BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION, AND PATHWAY.
RX   PubMed=2169413; DOI=10.1111/j.1432-1033.1990.tb19214.x;
RA   Arnvig K., Hove-Jensen B., Switzer R.L.;
RT   "Purification and properties of phosphoribosyl-diphosphate synthetase from
RT   Bacillus subtilis.";
RL   Eur. J. Biochem. 192:195-200(1990).
RN   [5]
RP   FUNCTION, AND NOMENCLATURE.
RX   PubMed=3038693; DOI=10.1016/0378-1119(87)90013-8;
RA   Nilsson D., Hove-Jensen B.;
RT   "Phosphoribosylpyrophosphate synthetase of Bacillus subtilis. Cloning,
RT   characterization and chromosomal mapping of the prs gene.";
RL   Gene 53:247-255(1987).
RN   [6]
RP   FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF LYS-198; ARG-200; ARG-202;
RP   ASN-204 AND GLU-207, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION,
RP   PATHWAY, AND ACTIVE SITE.
RX   PubMed=16008562; DOI=10.1111/j.1742-4658.2005.04785.x;
RA   Hove-Jensen B., Bentsen A.K., Harlow K.W.;
RT   "Catalytic residues Lys197 and Arg199 of Bacillus subtilis phosphoribosyl
RT   diphosphate synthase. Alanine-scanning mutagenesis of the flexible
RT   catalytic loop.";
RL   FEBS J. 272:3631-3639(2005).
RN   [7]
RP   REVIEW, COFACTOR, SUBUNIT, AND ACTIVE SITE.
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   [8]
RP   X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) IN COMPLEX WITH ATP ANALOGS AND
RP   ALLOSTERIC INHIBITOR, FUNCTION, AND SUBUNIT.
RX   PubMed=10742175; DOI=10.1038/74069;
RA   Eriksen T.A., Kadziola A., Bentsen A.-K., Harlow K.W., Larsen S.;
RT   "Structural basis for the function of Bacillus subtilis phosphoribosyl-
RT   pyrophosphate synthetase.";
RL   Nat. Struct. Biol. 7:303-308(2000).
RN   [9]
RP   X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOGS;
RP   ALLOSTERIC INHIBITOR AND CADMIUM IONS, FUNCTION, COFACTOR, AND SUBUNIT.
RX   PubMed=11790837; DOI=10.1110/ps.28502;
RA   Eriksen T.A., Kadziola A., Larsen S.;
RT   "Binding of cations in Bacillus subtilis phosphoribosyldiphosphate
RT   synthetase and their role in catalysis.";
RL   Protein Sci. 11:271-279(2002).
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:0000269|PubMed:11790837,
CC       ECO:0000269|PubMed:16008562, ECO:0000269|PubMed:2169413,
CC       ECO:0000269|PubMed:3038693, ECO:0000305|PubMed:10742175}.
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:16008562,
CC         ECO:0000269|PubMed:2169413};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_00583, ECO:0000269|PubMed:2169413,
CC         ECO:0000303|PubMed:28031352};
CC       Note=Binds 2 Mg(2+) ions per subunit. Each Mg(2+) binds only one
CC       residue (His-136 and Asp-175, respectively) of this protein, however
CC       the magnesium ions also bind substrates and water molecules to complete
CC       their coordination spheres (PubMed:2169413, PubMed:11790837). Can also
CC       use Mn(2+) and Cd(2+) ions, but the activity is less than that obtained
CC       with Mg(2+) ions (PubMed:2169413, PubMed:11790837).
CC       {ECO:0000269|PubMed:11790837, ECO:0000269|PubMed:2169413,
CC       ECO:0000303|PubMed:28031352};
CC   -!- ACTIVITY REGULATION: Activated by inorganic phosphate, and to a lesser
CC       extent by sulfate ions (PubMed:2169413). In addition to form a complex
CC       with ATP, Mg(2+) also acts as a cofactor (PubMed:2169413). Strongly
CC       inhibited by ADP through competitive binding at the activation site and
CC       at a specific allosteric site (PubMed:2169413, PubMed:16008562). Less
CC       strongly inhibited by alpha,beta-methylene ATP (mADP), AMP, GDP, GMP
CC       and UTP (PubMed:2169413, PubMed:16008562).
CC       {ECO:0000269|PubMed:16008562, ECO:0000269|PubMed:2169413}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=191 uM for ATP (at pH 8 and 37 degrees Celsius)
CC         {ECO:0000269|PubMed:16008562};
CC         KM=230 uM for Rib-5-P (at pH 8 and 37 degrees Celsius)
CC         {ECO:0000269|PubMed:16008562};
CC         KM=480 uM for Rib-5-P (at pH 8.2 and 37 degrees Celsius)
CC         {ECO:0000269|PubMed:2169413};
CC         KM=660 uM for ATP (at pH 8.2 and 37 degrees Celsius)
CC         {ECO:0000269|PubMed:2169413};
CC         Vmax=108 umol/min/mg enzyme (at pH 8 and 37 degrees Celsius)
CC         {ECO:0000269|PubMed:16008562};
CC         Vmax=250 umol/min/mg enzyme (at pH 8.2 and 37 degrees Celsius)
CC         {ECO:0000269|PubMed:2169413};
CC       pH dependence:
CC         Optimum pH is 8-8.5. Activities at pH 7 and pH 9.5 are 35% and 85% of
CC         the maximal activity, respectively. {ECO:0000269|PubMed:2169413};
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:16008562,
CC       ECO:0000305|PubMed:2169413}.
CC   -!- SUBUNIT: Homohexamer; trimer of dimers. {ECO:0000269|PubMed:10742175,
CC       ECO:0000269|PubMed:11790837, ECO:0000303|PubMed:28031352}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00583}.
CC   -!- MISCELLANEOUS: This enzyme uses a steady state ordered mechanism, where
CC       Mg(2+) binds first, followed by Mg-ATP and lastly, ribose 5-phosphate.
CC       {ECO:0000269|PubMed:16008562}.
CC   -!- SIMILARITY: Belongs to the ribose-phosphate pyrophosphokinase family.
CC       Class I subfamily. {ECO:0000255|HAMAP-Rule:MF_00583,
CC       ECO:0000303|PubMed:28031352}.
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DR   EMBL; X16518; CAA34523.1; -; Genomic_DNA.
DR   EMBL; D26185; BAA05286.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB11827.1; -; Genomic_DNA.
DR   PIR; S05372; KIBSRS.
DR   RefSeq; NP_387932.1; NC_000964.3.
DR   RefSeq; WP_003218353.1; NZ_JNCM01000028.1.
DR   PDB; 1DKR; X-ray; 2.30 A; A/B=1-317.
DR   PDB; 1DKU; X-ray; 2.20 A; A/B=1-317.
DR   PDB; 1IBS; X-ray; 2.80 A; A/B=1-317.
DR   PDBsum; 1DKR; -.
DR   PDBsum; 1DKU; -.
DR   PDBsum; 1IBS; -.
DR   AlphaFoldDB; P14193; -.
DR   SMR; P14193; -.
DR   IntAct; P14193; 2.
DR   MINT; P14193; -.
DR   STRING; 224308.BSU00510; -.
DR   DrugBank; DB03148; Adenosine 5'-methylenediphosphate.
DR   DrugBank; DB02798; Alpha-Methylene Adenosine Monophosphate.
DR   jPOST; P14193; -.
DR   PaxDb; 224308-BSU00510; -.
DR   EnsemblBacteria; CAB11827; CAB11827; BSU_00510.
DR   GeneID; 83883262; -.
DR   GeneID; 936985; -.
DR   KEGG; bsu:BSU00510; -.
DR   PATRIC; fig|224308.179.peg.51; -.
DR   eggNOG; COG0462; Bacteria.
DR   InParanoid; P14193; -.
DR   OrthoDB; 9777067at2; -.
DR   PhylomeDB; P14193; -.
DR   BioCyc; BSUB:BSU00510-MONOMER; -.
DR   SABIO-RK; P14193; -.
DR   UniPathway; UPA00087; UER00172.
DR   EvolutionaryTrace; P14193; -.
DR   PRO; PR:P14193; -.
DR   Proteomes; UP000001570; 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_B; RibP_PPkinase_B; 1.
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   InterPro; IPR037515; Rib-P_diPkinase_bac.
DR   NCBIfam; TIGR01251; ribP_PPkin; 1.
DR   PANTHER; PTHR10210; RIBOSE-PHOSPHATE DIPHOSPHOKINASE FAMILY MEMBER; 1.
DR   PANTHER; PTHR10210:SF119; RIBOSE-PHOSPHATE PYROPHOSPHOKINASE; 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.
DR   PROSITE; PS00114; PRPP_SYNTHASE; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Allosteric enzyme; ATP-binding; Cytoplasm;
KW   Direct protein sequencing; Kinase; Magnesium; Metal-binding;
KW   Nucleotide biosynthesis; Nucleotide-binding; Reference proteome;
KW   Transferase.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:2169413"
FT   CHAIN           2..317
FT                   /note="Ribose-phosphate pyrophosphokinase"
FT                   /id="PRO_0000141110"
FT   ACT_SITE        198
FT                   /evidence="ECO:0000303|PubMed:28031352,
FT                   ECO:0000305|PubMed:16008562"
FT   BINDING         43..45
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00583,
FT                   ECO:0000305|PubMed:10742175"
FT   BINDING         102..103
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00583,
FT                   ECO:0000269|PubMed:11790837, ECO:0000305|PubMed:10742175,
FT                   ECO:0007744|PDB:1DKU, ECO:0007744|PDB:1IBS"
FT   BINDING         106
FT                   /ligand="ADP"
FT                   /ligand_id="ChEBI:CHEBI:456216"
FT                   /ligand_note="allosteric inhibitor"
FT                   /evidence="ECO:0000305|PubMed:10742175,
FT                   ECO:0007744|PDB:1DKU"
FT   BINDING         110
FT                   /ligand="ADP"
FT                   /ligand_id="ChEBI:CHEBI:456216"
FT                   /ligand_note="allosteric inhibitor"
FT                   /evidence="ECO:0000305|PubMed:10742175,
FT                   ECO:0007744|PDB:1DKU"
FT   BINDING         136
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00583,
FT                   ECO:0000303|PubMed:28031352, ECO:0000305|PubMed:11790837,
FT                   ECO:0007744|PDB:1IBS"
FT   BINDING         141
FT                   /ligand="ADP"
FT                   /ligand_id="ChEBI:CHEBI:456216"
FT                   /ligand_note="allosteric inhibitor"
FT                   /evidence="ECO:0000305|PubMed:10742175,
FT                   ECO:0007744|PDB:1DKU"
FT   BINDING         149..150
FT                   /ligand="ADP"
FT                   /ligand_id="ChEBI:CHEBI:456216"
FT                   /ligand_note="allosteric inhibitor"
FT                   /evidence="ECO:0000305|PubMed:10742175,
FT                   ECO:0007744|PDB:1DKU"
FT   BINDING         175
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00583,
FT                   ECO:0000303|PubMed:28031352, ECO:0000305|PubMed:11790837,
FT                   ECO:0007744|PDB:1IBS"
FT   BINDING         200
FT                   /ligand="D-ribose 5-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:78346"
FT                   /evidence="ECO:0000250|UniProtKB:Q97CA5, ECO:0000255|HAMAP-
FT                   Rule:MF_00583"
FT   BINDING         224
FT                   /ligand="D-ribose 5-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:78346"
FT                   /evidence="ECO:0000250|UniProtKB:Q97CA5, ECO:0000255|HAMAP-
FT                   Rule:MF_00583"
FT   BINDING         228..232
FT                   /ligand="D-ribose 5-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:78346"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00583,
FT                   ECO:0000269|PubMed:10742175, ECO:0000269|PubMed:11790837,
FT                   ECO:0007744|PDB:1DKR, ECO:0007744|PDB:1IBS"
FT   BINDING         311..313
FT                   /ligand="ADP"
FT                   /ligand_id="ChEBI:CHEBI:456216"
FT                   /ligand_note="allosteric inhibitor"
FT                   /evidence="ECO:0000305|PubMed:10742175,
FT                   ECO:0007744|PDB:1DKU"
FT   MUTAGEN         198
FT                   /note="K->A: Strong decrease of the Vmax value compared to
FT                   that of the wild-type. The affinity binding for ATP and
FT                   Rib-5-P are slightly altered compared to the wild-type. The
FT                   cooperativity of ADP binding is reduced."
FT                   /evidence="ECO:0000269|PubMed:16008562"
FT   MUTAGEN         200
FT                   /note="R->A: Strong decrease of the Vmax value compared to
FT                   that of the wild-type enzyme. The affinity binding for ATP
FT                   and Rib-5-P are slightly altered compared to the
FT                   wild-type."
FT                   /evidence="ECO:0000269|PubMed:16008562"
FT   MUTAGEN         202
FT                   /note="R->A: 3-fold decrease in the affinity binding for
FT                   ATP. Slight decrease of the Vmax value."
FT                   /evidence="ECO:0000269|PubMed:16008562"
FT   MUTAGEN         204
FT                   /note="N->A: 4.5-fold decrease in the affinity binding for
FT                   ATP. Slight decrease of the Vmax value."
FT                   /evidence="ECO:0000269|PubMed:16008562"
FT   MUTAGEN         207
FT                   /note="E->A: 2.5-fold decrease in the affinity binding for
FT                   ATP. Slight decrease of the Vmax value."
FT                   /evidence="ECO:0000269|PubMed:16008562"
FT   STRAND          10..14
FT                   /evidence="ECO:0007829|PDB:1DKU"
FT   HELIX           19..29
FT                   /evidence="ECO:0007829|PDB:1DKU"
FT   STRAND          36..40
FT                   /evidence="ECO:0007829|PDB:1DKU"
FT   STRAND          42..44
FT                   /evidence="ECO:0007829|PDB:1IBS"
FT   STRAND          46..50
FT                   /evidence="ECO:0007829|PDB:1DKU"
FT   STRAND          58..62
FT                   /evidence="ECO:0007829|PDB:1DKU"
FT   HELIX           69..85
FT                   /evidence="ECO:0007829|PDB:1DKU"
FT   STRAND          89..97
FT                   /evidence="ECO:0007829|PDB:1DKU"
FT   TURN            99..102
FT                   /evidence="ECO:0007829|PDB:1DKU"
FT   HELIX           114..125
FT                   /evidence="ECO:0007829|PDB:1DKU"
FT   STRAND          129..134
FT                   /evidence="ECO:0007829|PDB:1DKU"
FT   HELIX           138..143
FT                   /evidence="ECO:0007829|PDB:1DKU"
FT   STRAND          148..151
FT                   /evidence="ECO:0007829|PDB:1DKU"
FT   HELIX           154..162
FT                   /evidence="ECO:0007829|PDB:1DKU"
FT   TURN            163..165
FT                   /evidence="ECO:0007829|PDB:1DKU"
FT   STRAND          168..175
FT                   /evidence="ECO:0007829|PDB:1DKU"
FT   HELIX           176..178
FT                   /evidence="ECO:0007829|PDB:1DKU"
FT   HELIX           179..188
FT                   /evidence="ECO:0007829|PDB:1DKU"
FT   STRAND          193..197
FT                   /evidence="ECO:0007829|PDB:1DKU"
FT   STRAND          210..213
FT                   /evidence="ECO:0007829|PDB:1DKU"
FT   STRAND          219..223
FT                   /evidence="ECO:0007829|PDB:1DKU"
FT   STRAND          225..229
FT                   /evidence="ECO:0007829|PDB:1DKU"
FT   HELIX           231..242
FT                   /evidence="ECO:0007829|PDB:1DKU"
FT   STRAND          246..251
FT                   /evidence="ECO:0007829|PDB:1DKU"
FT   STRAND          253..255
FT                   /evidence="ECO:0007829|PDB:1DKU"
FT   HELIX           261..266
FT                   /evidence="ECO:0007829|PDB:1DKU"
FT   STRAND          268..276
FT                   /evidence="ECO:0007829|PDB:1DKU"
FT   STRAND          288..293
FT                   /evidence="ECO:0007829|PDB:1DKU"
FT   HELIX           296..308
FT                   /evidence="ECO:0007829|PDB:1DKU"
FT   HELIX           313..315
FT                   /evidence="ECO:0007829|PDB:1DKU"
SQ   SEQUENCE   317 AA;  34868 MW;  0D37FC81668111EB CRC64;
     MSNQYGDKNL KIFSLNSNPE LAKEIADIVG VQLGKCSVTR FSDGEVQINI EESIRGCDCY
     IIQSTSDPVN EHIMELLIMV DALKRASAKT INIVIPYYGY ARQDRKARSR EPITAKLFAN
     LLETAGATRV IALDLHAPQI QGFFDIPIDH LMGVPILGEY FEGKNLEDIV IVSPDHGGVT
     RARKLADRLK APIAIIDKRR PRPNVAEVMN IVGNIEGKTA ILIDDIIDTA GTITLAANAL
     VENGAKEVYA CCTHPVLSGP AVERINNSTI KELVVTNSIK LPEEKKIERF KQLSVGPLLA
     EAIIRVHEQQ SVSYLFS
//