ID   KPPR_ECOLI              Reviewed;         289 AA.
AC   P0AEX5; P37307; P76684; Q2M721;
DT   20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   20-DEC-2005, sequence version 1.
DT   03-AUG-2022, entry version 106.
DE   RecName: Full=Probable phosphoribulokinase;
DE            Short=PRK;
DE            Short=PRKase;
DE            EC=2.7.1.19;
DE   AltName: Full=Phosphopentokinase;
GN   Name=prkB; Synonyms=yhfF; OrderedLocusNames=b3355, JW3318;
OS   Escherichia coli (strain K12).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83333;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA   Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA   Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA   Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA   Shao Y.;
RT   "The complete genome sequence of Escherichia coli K-12.";
RL   Science 277:1453-1462(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=16738553; DOI=10.1038/msb4100049;
RA   Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA   Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT   "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT   and W3110.";
RL   Mol. Syst. Biol. 2:E1-E5(2006).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 228-289.
RC   STRAIN=K12;
RX   PubMed=1756168; DOI=10.1016/0167-4781(91)90222-8;
RA   Bhasin R., Freundlich M.;
RT   "The nucleotide sequence of the Escherichia coli crp divergent RNA and an
RT   overlapping ORF.";
RL   Biochim. Biophys. Acta 1129:109-111(1991).
RN   [4]
RP   IDENTIFICATION.
RX   PubMed=7940673; DOI=10.1016/0968-0004(94)90067-1;
RA   Borodovsky M., Koonin E.V., Rudd K.E.;
RT   "New genes in old sequence: a strategy for finding genes in the bacterial
RT   genome.";
RL   Trends Biochem. Sci. 19:309-313(1994).
RN   [5]
RP   IDENTIFICATION.
RX   PubMed=7984428; DOI=10.1093/nar/22.22.4756;
RA   Borodovsky M., Rudd K.E., Koonin E.V.;
RT   "Intrinsic and extrinsic approaches for detecting genes in a bacterial
RT   genome.";
RL   Nucleic Acids Res. 22:4756-4767(1994).
RN   [6]
RP   IDENTIFICATION.
RX   PubMed=7920643; DOI=10.1038/ng0694-205;
RA   Robison K., Gilbert W., Church G.M.;
RT   "Large scale bacterial gene discovery by similarity search.";
RL   Nat. Genet. 7:205-214(1994).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + D-ribulose 5-phosphate = ADP + D-ribulose 1,5-
CC         bisphosphate + H(+); Xref=Rhea:RHEA:19365, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:57870, ChEBI:CHEBI:58121,
CC         ChEBI:CHEBI:456216; EC=2.7.1.19;
CC   -!- SIMILARITY: Belongs to the phosphoribulokinase family. {ECO:0000305}.
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DR   EMBL; U18997; AAA58152.1; ALT_FRAME; Genomic_DNA.
DR   EMBL; U00096; AAC76380.1; -; Genomic_DNA.
DR   EMBL; AP009048; BAE77935.1; -; Genomic_DNA.
DR   EMBL; X61919; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   PIR; F65129; F65129.
DR   RefSeq; NP_417814.1; NC_000913.3.
DR   RefSeq; WP_001274680.1; NZ_STEB01000004.1.
DR   AlphaFoldDB; P0AEX5; -.
DR   SMR; P0AEX5; -.
DR   BioGRID; 4259590; 23.
DR   DIP; DIP-10565N; -.
DR   IntAct; P0AEX5; 4.
DR   STRING; 511145.b3355; -.
DR   jPOST; P0AEX5; -.
DR   PaxDb; P0AEX5; -.
DR   PRIDE; P0AEX5; -.
DR   EnsemblBacteria; AAC76380; AAC76380; b3355.
DR   EnsemblBacteria; BAE77935; BAE77935; BAE77935.
DR   GeneID; 66672764; -.
DR   GeneID; 947862; -.
DR   KEGG; ecj:JW3318; -.
DR   KEGG; eco:b3355; -.
DR   PATRIC; fig|1411691.4.peg.3375; -.
DR   EchoBASE; EB2268; -.
DR   eggNOG; COG3954; Bacteria.
DR   HOGENOM; CLU_962223_0_0_6; -.
DR   InParanoid; P0AEX5; -.
DR   OMA; TDILFYE; -.
DR   PhylomeDB; P0AEX5; -.
DR   BioCyc; EcoCyc:EG12365-MON; -.
DR   PRO; PR:P0AEX5; -.
DR   Proteomes; UP000000318; Chromosome.
DR   Proteomes; UP000000625; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0008974; F:phosphoribulokinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.300; -; 1.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR006082; PRK.
DR   InterPro; IPR006083; PRK/URK.
DR   Pfam; PF00485; PRK; 1.
DR   PRINTS; PR00478; PHRIBLKINASE.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   PROSITE; PS00567; PHOSPHORIBULOKINASE; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Kinase; Nucleotide-binding; Reference proteome; Transferase.
FT   CHAIN           1..289
FT                   /note="Probable phosphoribulokinase"
FT                   /id="PRO_0000201952"
FT   BINDING         12..20
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        250
FT                   /note="Q -> L (in Ref. 3)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   289 AA;  32344 MW;  A98EE1A322148DAE CRC64;
     MSAKHPVIAV TGSSGAGTTT TSLAFRKIFA QLNLHAAEVE GDSFHRYTRP EMDMAIRKAR
     DAGRHISYFG PEANDFGLLE QTFIEYGQSG KGKSRKYLHT YDEAVPWNQV PGTFTPWQPL
     PEPTDVLFYE GLHGGVVTPQ HNVAQHVDLL VGVVPIVNLE WIQKLIRDTS ERGHSREAVM
     DSVVRSMEDY INYITPQFSR THLNFQRVPT VDTSNPFAAK GIPSLDESFV VIHFRNLEGI
     DFPWLLAMLQ GSFISHINTL VVPGGKMGLA MELIMLPLVQ RLMEGKKIE