ID   KPPR_SINMW              Reviewed;         289 AA.
AC   P56887; A6UGF1;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   13-NOV-2007, sequence version 2.
DT   03-AUG-2022, entry version 95.
DE   RecName: Full=Phosphoribulokinase;
DE            Short=PRK;
DE            Short=PRKase;
DE            EC=2.7.1.19;
DE   AltName: Full=Phosphopentokinase;
GN   Name=cbbP; OrderedLocusNames=Smed_3921;
OS   Sinorhizobium medicae (strain WSM419) (Ensifer medicae).
OG   Plasmid pSMED01.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX   NCBI_TaxID=366394;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Fenner B.J., Tiwari R.P., Dilworth M.J.;
RT   "Genetic regulation of C1 metabolism in Sinorhizobium meliloti.";
RL   Submitted (DEC-1999) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WSM419;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Reeve W.G.,
RA   Richardson P.;
RT   "Complete sequence of Sinorhizobium medicae WSM419 plasmid pSMED01.";
RL   Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
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   -!- PATHWAY: Carbohydrate biosynthesis; Calvin cycle.
CC   -!- SIMILARITY: Belongs to the phosphoribulokinase family. {ECO:0000305}.
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DR   EMBL; AF211846; AAF25376.1; -; Genomic_DNA.
DR   EMBL; CP000739; ABR62731.1; -; Genomic_DNA.
DR   RefSeq; WP_011969553.1; NC_009620.1.
DR   RefSeq; YP_001312664.1; NC_009620.1.
DR   AlphaFoldDB; P56887; -.
DR   SMR; P56887; -.
DR   EnsemblBacteria; ABR62731; ABR62731; Smed_3921.
DR   GeneID; 61612434; -.
DR   KEGG; smd:Smed_3921; -.
DR   PATRIC; fig|366394.8.peg.367; -.
DR   HOGENOM; CLU_962223_0_0_5; -.
DR   OMA; TDILFYE; -.
DR   OrthoDB; 1793376at2; -.
DR   UniPathway; UPA00116; -.
DR   Proteomes; UP000001108; Plasmid pSMED01.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0008974; F:phosphoribulokinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   GO; GO:0019253; P:reductive pentose-phosphate cycle; IEA:UniProtKB-UniPathway.
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; Calvin cycle; Kinase; Nucleotide-binding; Plasmid;
KW   Transferase.
FT   CHAIN           1..289
FT                   /note="Phosphoribulokinase"
FT                   /id="PRO_0000201956"
FT   BINDING         12..20
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        77
FT                   /note="E -> D (in Ref. 1; AAF25376)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        80
FT                   /note="E -> Q (in Ref. 1; AAF25376)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        279
FT                   /note="H -> N (in Ref. 1; AAF25376)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        282
FT                   /note="L -> I (in Ref. 1; AAF25376)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   289 AA;  32970 MW;  A74ED5CCEAD465F9 CRC64;
     MSAKYPIISI TGSSGAGTTT VKDTFEKIFK RENISASFIE GDAFHRYDRE TMRSKIAEEK
     ARGVDFTHFS AEANELEILE SVFAEYGRRG VGRTRHYVHD DAEAVKFGSD PGTFTDWEEF
     RDSDLLFYEG LHGCAVTDTI NLAQHCDLKI GVVPVINLEW IQKIHRDKAT RGYSTEAVTD
     TILRRMPDYV HYICPQFSLT DINFQRVPIV DTSNPFIARW IPTPAESILV IRFAKPQSID
     FPYLLSMLHN SYMSRANSIV VPGDKLDLAM QLIFTPLIHK LLERKHRMS