PGKP_CUPNH
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 03-AUG-2022, entry version 130.
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; Proteobacteria; 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 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}.
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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 STRING; 381666.PHG417; -.
DR EnsemblBacteria; AAP86166; AAP86166; PHG417.
DR KEGG; reh:PHG417; -.
DR eggNOG; COG0126; Bacteria.
DR HOGENOM; CLU_025427_0_2_4; -.
DR OMA; MGDGYKV; -.
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:0019253; P:reductive pentose-phosphate cycle; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.40.50.1260; -; 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; PTHR11406; 1.
DR Pfam; PF00162; PGK; 1.
DR PIRSF; PIRSF000724; Pgk; 1.
DR PRINTS; PR00477; PHGLYCKINASE.
DR SUPFAM; SSF53748; SSF53748; 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