KPPR1_CUPNH
ID KPPR1_CUPNH Reviewed; 292 AA.
AC P19924;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Phosphoribulokinase, plasmid;
DE Short=PRK;
DE Short=PRKase;
DE EC=2.7.1.19;
DE AltName: Full=Phosphopentokinase;
GN Name=cfxP; Synonyms=cbbPP; OrderedLocusNames=PHG421;
OS Cupriavidus necator (strain ATCC 17699 / DSM 428 / KCTC 22496 / NCIMB 10442
OS / H16 / Stanier 337) (Ralstonia eutropha).
OG Plasmid megaplasmid pHG1.
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Cupriavidus.
OX NCBI_TaxID=381666;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2559876; DOI=10.1016/0378-1119(89)90490-3;
RA Kossmann J., Klintworth R., Bowien B.;
RT "Sequence analysis of the chromosomal and plasmid genes encoding
RT phosphoribulokinase from Alcaligenes eutrophus.";
RL Gene 85:247-252(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 17699 / DSM 428 / KCTC 22496 / NCIMB 10442 / H16 / Stanier 337;
RX PubMed=12948488; DOI=10.1016/s0022-2836(03)00894-5;
RA Schwartz E., Henne A., Cramm R., Eitinger T., Friedrich B., Gottschalk G.;
RT "Complete nucleotide sequence of pHG1: a Ralstonia eutropha H16 megaplasmid
RT encoding key enzymes of H(2)-based lithoautotrophy and anaerobiosis.";
RL J. Mol. Biol. 332:369-383(2003).
RN [3]
RP PROTEIN SEQUENCE OF 2-18.
RX PubMed=2997141; DOI=10.1128/jb.164.2.954-956.1985;
RA Klintworth R., Husemann M., Salnikow J., Bowien B.;
RT "Chromosomal and plasmid locations for phosphoribulokinase genes in
RT Alcaligenes eutrophus.";
RL J. Bacteriol. 164:954-956(1985).
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 -!- SUBUNIT: Homooctamer.
CC -!- SIMILARITY: Belongs to the phosphoribulokinase family. {ECO:0000305}.
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DR EMBL; M33562; AAA21957.1; -; Genomic_DNA.
DR EMBL; AY305378; AAP86170.1; -; Genomic_DNA.
DR PIR; JQ0400; JQ0400.
DR RefSeq; WP_011154333.1; NZ_CP039289.1.
DR AlphaFoldDB; P19924; -.
DR SMR; P19924; -.
DR STRING; 381666.PHG421; -.
DR EnsemblBacteria; AAP86170; AAP86170; PHG421.
DR GeneID; 39976769; -.
DR KEGG; reh:PHG421; -.
DR PATRIC; fig|381666.6.peg.349; -.
DR eggNOG; COG3954; Bacteria.
DR HOGENOM; CLU_962223_0_0_4; -.
DR OMA; HYIHAED; -.
DR OrthoDB; 1793376at2; -.
DR UniPathway; UPA00116; -.
DR Proteomes; UP000008210; Plasmid megaplasmid pHG1.
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 ATP-binding; Calvin cycle; Direct protein sequencing; Kinase;
KW Nucleotide-binding; Plasmid; Reference proteome; Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:2997141"
FT CHAIN 2..292
FT /note="Phosphoribulokinase, plasmid"
FT /id="PRO_0000201950"
FT BINDING 12..20
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
SQ SEQUENCE 292 AA; 33161 MW; 045FAC49329F5BC9 CRC64;
MSERYPIIAI TGSSGAGTTS VTRTFENIFC REGVKSVVIE GDSFHRYDRA EMKVKMAEAE
RTGNMNFSHF GAENNLFGDL ESLFRSYAES GTGMRRRYLH STEEAAPFGQ QPGTFTAWEP
LPADTDLLFY EGLHGGVVTD EVNVAQYPNL LIGVVPVINL EWIQKLWRDK KQRGYSTEAV
TDTILRRMPD YVNYICPQFS RTHVNFQRVP CVDTSNPFIS REIPAPDESM VVIRFANPKG
IDFQYLLSMI HDSFMSRANT IVVPGGKMEL AMQLIFTPFV LRMMERRKRA AL