KPPR1_CERSP
ID KPPR1_CERSP Reviewed; 290 AA.
AC P12033;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1992, sequence version 2.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=Phosphoribulokinase 1;
DE Short=PRK I;
DE Short=PRKase 1;
DE EC=2.7.1.19;
DE AltName: Full=Phosphopentokinase 1;
GN Name=prkA;
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=1907281; DOI=10.1016/s0021-9258(18)98734-x;
RA Gibson J.L., Falcone D.L., Tabita F.R.;
RT "Nucleotide sequence, transcriptional analysis, and expression of genes
RT encoded within the form I CO2 fixation operon of Rhodobacter sphaeroides.";
RL J. Biol. Chem. 266:14646-14653(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-28.
RX PubMed=3038847; DOI=10.1128/jb.169.8.3669-3678.1987;
RA Hallenbeck P.L., Kaplan S.;
RT "Cloning of the gene for phosphoribulokinase activity from Rhodobacter
RT sphaeroides and its expression in Escherichia coli.";
RL J. Bacteriol. 169:3669-3678(1987).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
RX PubMed=9548738; DOI=10.1021/bi972805y;
RA Harrison D.H., Runquist J.A., Holub A., Miziorko H.M.;
RT "The crystal structure of phosphoribulokinase from Rhodobacter sphaeroides
RT reveals a fold similar to that of adenylate kinase.";
RL Biochemistry 37:5074-5085(1998).
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 -!- ACTIVITY REGULATION: Activated by NADH and inhibited by
CC phosphoenolpyruvate.
CC -!- PATHWAY: Carbohydrate biosynthesis; Calvin cycle.
CC -!- SUBUNIT: Homooctamer.
CC -!- MISCELLANEOUS: Is not found in cells cultured chemoheterotrophically
CC and only low levels of activities are found in those grown
CC photoheterotrophically on oxidized organic acids.
CC -!- SIMILARITY: Belongs to the phosphoribulokinase family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; M64624; AAA26113.1; -; Genomic_DNA.
DR EMBL; M28006; AAA26153.1; -; Genomic_DNA.
DR PIR; C40767; KIRFAS.
DR PDB; 1A7J; X-ray; 2.50 A; A=1-290.
DR PDBsum; 1A7J; -.
DR AlphaFoldDB; P12033; -.
DR SMR; P12033; -.
DR UniPathway; UPA00116; -.
DR EvolutionaryTrace; P12033; -.
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 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Calvin cycle; Kinase; Nucleotide-binding;
KW Photosynthesis; Transferase.
FT CHAIN 1..290
FT /note="Phosphoribulokinase 1"
FT /id="PRO_0000201957"
FT BINDING 12..20
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT STRAND 7..12
FT /evidence="ECO:0007829|PDB:1A7J"
FT HELIX 21..32
FT /evidence="ECO:0007829|PDB:1A7J"
FT STRAND 36..40
FT /evidence="ECO:0007829|PDB:1A7J"
FT HELIX 41..44
FT /evidence="ECO:0007829|PDB:1A7J"
FT HELIX 49..62
FT /evidence="ECO:0007829|PDB:1A7J"
FT HELIX 72..74
FT /evidence="ECO:0007829|PDB:1A7J"
FT HELIX 77..90
FT /evidence="ECO:0007829|PDB:1A7J"
FT STRAND 126..133
FT /evidence="ECO:0007829|PDB:1A7J"
FT HELIX 145..147
FT /evidence="ECO:0007829|PDB:1A7J"
FT STRAND 149..156
FT /evidence="ECO:0007829|PDB:1A7J"
FT HELIX 158..168
FT /evidence="ECO:0007829|PDB:1A7J"
FT STRAND 170..172
FT /evidence="ECO:0007829|PDB:1A7J"
FT HELIX 180..194
FT /evidence="ECO:0007829|PDB:1A7J"
FT HELIX 196..200
FT /evidence="ECO:0007829|PDB:1A7J"
FT STRAND 203..212
FT /evidence="ECO:0007829|PDB:1A7J"
FT HELIX 217..219
FT /evidence="ECO:0007829|PDB:1A7J"
FT HELIX 226..228
FT /evidence="ECO:0007829|PDB:1A7J"
FT STRAND 229..237
FT /evidence="ECO:0007829|PDB:1A7J"
FT HELIX 243..249
FT /evidence="ECO:0007829|PDB:1A7J"
FT STRAND 254..257
FT /evidence="ECO:0007829|PDB:1A7J"
FT STRAND 260..264
FT /evidence="ECO:0007829|PDB:1A7J"
FT HELIX 265..267
FT /evidence="ECO:0007829|PDB:1A7J"
FT HELIX 268..284
FT /evidence="ECO:0007829|PDB:1A7J"
FT TURN 285..288
FT /evidence="ECO:0007829|PDB:1A7J"
SQ SEQUENCE 290 AA; 32664 MW; 6899EFB1D780640F CRC64;
MSKKHPIISV TGSSGAGTST VKHTFDQIFR REGVKAVSIE GDAFHRFNRA DMKAELDRRY
AAGDATFSHF SYEANELKEL ERVFREYGET GQGRTRTYVH DDAEAARTGV APGNFTDWRD
FDSDSHLLFY EGLHGAVVNS EVNIAGLADL KIGVVPVINL EWIQKIHRDR ATRGYTTEAV
TDVILRRMHA YVHCIVPQFS QTDINFQRVP VVDTSNPFIA RWIPTADESV VVIRFRNPRG
IDFPYLTSMI HGSWMSRANS IVVPGNKLDL AMQLILTPLI DRVVRESKVA
