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KPPR2_CERSP
ID   KPPR2_CERSP             Reviewed;         292 AA.
AC   P23010;
DT   01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 2.
DT   03-AUG-2022, entry version 75.
DE   RecName: Full=Phosphoribulokinase 2;
DE            Short=PRKase 2;
DE            EC=2.7.1.19;
DE   AltName: Full=PRK II;
DE   AltName: Full=Phosphopentokinase 2;
GN   Name=prkB;
OS   Cereibacter sphaeroides (Rhodobacter sphaeroides).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Cereibacter.
OX   NCBI_TaxID=1063;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2175647; DOI=10.1021/bi00487a014;
RA   Gibson J.L., Chen J.-H., Tower P.A., Tabita F.R.;
RT   "The form II fructose 1,6-bisphosphatase and phosphoribulokinase genes form
RT   part of a large operon in Rhodobacter sphaeroides: primary structure and
RT   insertional mutagenesis analysis.";
RL   Biochemistry 29:8085-8093(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 259-292.
RX   PubMed=1939098; DOI=10.1016/s0021-9258(18)54944-9;
RA   Chen J.-H., Gibson J.L., McCue L.A., Tabita F.R.;
RT   "Identification, expression, and deduced primary structure of transketolase
RT   and other enzymes encoded within the form II CO2 fixation operon of
RT   Rhodobacter sphaeroides.";
RL   J. Biol. Chem. 266:20447-20452(1991).
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; J02922; AAA26106.1; -; Genomic_DNA.
DR   EMBL; M68914; AAA26154.1; -; Genomic_DNA.
DR   PIR; B35819; B35819.
DR   AlphaFoldDB; P23010; -.
DR   SMR; P23010; -.
DR   UniPathway; UPA00116; -.
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; Photosynthesis;
KW   Transferase.
FT   CHAIN           1..292
FT                   /note="Phosphoribulokinase 2"
FT                   /id="PRO_0000201958"
FT   BINDING         12..20
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   292 AA;  33177 MW;  BFA8CEB5F68BC021 CRC64;
     MSKKYPIISV VGSSGAGTST VKNTFEQIFR REGVKSVSIE GDAFHRFNRA DMKAELERRY
     AAGDATFSHF SYEANELKEL ERVFREYGET GRGRTRTYVH DDAEAARTGV APGNFTQWAP
     FEDNSDLLFY EGLHGCVVND EVNLVRHADL KLGVAPVINL EWIQKIHRDR AQRGYTTEAV
     TDVILRRMYA YVHCIVPQFS ETDINFQRVP VVDTSNPFIA RWIPTPDESL IVIRFKNPRG
     IDCPYLTSMI AGSWMSRANS IVVPGNKQDL AMQLILTPLI ERMVREARRA RA
 
 
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