ID   PGKP_CUPNH              Reviewed;         412 AA.
AC   P50320;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   27-MAR-2024, entry version 135.
DE   RecName: Full=Phosphoglycerate kinase, plasmid;
DE            EC=2.7.2.3;
GN   Name=cbbKP; OrderedLocusNames=PHG417;
OS   Cupriavidus necator (strain ATCC 17699 / DSM 428 / KCTC 22496 / NCIMB 10442
OS   / H16 / Stanier 337) (Ralstonia eutropha).
OG   Plasmid megaplasmid pHG1.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Cupriavidus.
OX   NCBI_TaxID=381666;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=7763137; DOI=10.1007/bf00393383;
RA   Schaeferfohann J., Yoo J.-G., Bowien B.;
RT   "Analysis of the genes forming the distal parts of the two cbb CO2 fixation
RT   operons from Alcaligenes eutrophus.";
RL   Arch. Microbiol. 163:291-299(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 17699 / DSM 428 / KCTC 22496 / NCIMB 10442 / H16 / Stanier
RC   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).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2R)-3-phosphoglycerate + ATP = (2R)-3-phospho-glyceroyl
CC         phosphate + ADP; Xref=Rhea:RHEA:14801, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:57604, ChEBI:CHEBI:58272, ChEBI:CHEBI:456216; EC=2.7.2.3;
CC   -!- PATHWAY: Carbohydrate biosynthesis; Calvin cycle.
CC   -!- SUBUNIT: Monomer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the phosphoglycerate kinase family.
CC       {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; U12423; AAC43447.1; -; Genomic_DNA.
DR   EMBL; AY305378; AAP86166.1; -; Genomic_DNA.
DR   PIR; I39554; I39554.
DR   AlphaFoldDB; P50320; -.
DR   SMR; P50320; -.
DR   KEGG; reh:PHG417; -.
DR   eggNOG; COG0126; Bacteria.
DR   HOGENOM; CLU_025427_0_2_4; -.
DR   OrthoDB; 9808460at2; -.
DR   UniPathway; UPA00116; -.
DR   Proteomes; UP000008210; Plasmid megaplasmid pHG1.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004618; F:phosphoglycerate kinase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   GO; GO:0019253; P:reductive pentose-phosphate cycle; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.40.50.1260; Phosphoglycerate kinase, N-terminal domain; 2.
DR   HAMAP; MF_00145; Phosphoglyc_kinase; 1.
DR   InterPro; IPR001576; Phosphoglycerate_kinase.
DR   InterPro; IPR015911; Phosphoglycerate_kinase_CS.
DR   InterPro; IPR015824; Phosphoglycerate_kinase_N.
DR   InterPro; IPR036043; Phosphoglycerate_kinase_sf.
DR   PANTHER; PTHR11406; PHOSPHOGLYCERATE KINASE; 1.
DR   PANTHER; PTHR11406:SF23; PHOSPHOGLYCERATE KINASE 1, CHLOROPLASTIC-RELATED; 1.
DR   Pfam; PF00162; PGK; 1.
DR   PIRSF; PIRSF000724; Pgk; 1.
DR   PRINTS; PR00477; PHGLYCKINASE.
DR   SUPFAM; SSF53748; Phosphoglycerate kinase; 1.
DR   PROSITE; PS00111; PGLYCERATE_KINASE; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Calvin cycle; Cytoplasm; Kinase; Nucleotide-binding; Plasmid;
KW   Reference proteome; Transferase.
FT   CHAIN           1..412
FT                   /note="Phosphoglycerate kinase, plasmid"
FT                   /id="PRO_0000145896"
FT   BINDING         39..41
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         55
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         78..81
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         133
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         166
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         217
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         339
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         365..368
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   412 AA;  42299 MW;  9E84C666859E7274 CRC64;
     MMSLSHASVP HTNPTAPHTL AALLAAGGLA GKRVFIRADL NVPQDAAGDI TDDTRIRASV
     PAIAACLQAG AAVMVTSHLG RPQEGAPDPR HSLAPVGRRL SELLGRQVPL LSGWTEGGFQ
     VPPGQVVLLE NCRMNTGEKK NSDELAQKMA ALCDVYVNDA FGTAHRAEAT THGIARYAPV
     ACAGPLLAAE IDALGKALGQ PARPLVAIVA GSKVSTKLTI LKSLADKVDN LVVGGGIANT
     FMLAAGLKIG KSLAEPDLLA DARAIIDIMA ARGASVPIPV DVVCAKEFSA TAAAAVKDVR
     DVADDDMILD IGPKTAAMLA DQLKAAGTIV WNGPVGVFEF DQFGNGTRVL AQAIAESKAF
     SIAGGGDTLA AIAKYGIADR VGYISTGGGA FLEFLEGKKL PALDVLEQRA AS
//