ID   PGKC_CUPNH              Reviewed;         413 AA.
AC   P50319; Q0K1F0;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   03-AUG-2022, entry version 126.
DE   RecName: Full=Phosphoglycerate kinase, chromosomal;
DE            EC=2.7.2.3;
GN   Name=cbbKC; Synonyms=cbbK2; OrderedLocusNames=H16_B1385;
OS   Cupriavidus necator (strain ATCC 17699 / DSM 428 / KCTC 22496 / NCIMB 10442
OS   / H16 / Stanier 337) (Ralstonia eutropha).
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=16964242; DOI=10.1038/nbt1244;
RA   Pohlmann A., Fricke W.F., Reinecke F., Kusian B., Liesegang H., Cramm R.,
RA   Eitinger T., Ewering C., Poetter M., Schwartz E., Strittmatter A., Voss I.,
RA   Gottschalk G., Steinbuechel A., Friedrich B., Bowien B.;
RT   "Genome sequence of the bioplastic-producing 'Knallgas' bacterium Ralstonia
RT   eutropha H16.";
RL   Nat. Biotechnol. 24:1257-1262(2006).
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.
CC   -!- SIMILARITY: Belongs to the phosphoglycerate kinase family.
CC       {ECO:0000305}.
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DR   EMBL; U12422; AAC43444.1; -; Genomic_DNA.
DR   EMBL; AM260480; CAJ96174.1; -; Genomic_DNA.
DR   PIR; I39551; I39551.
DR   AlphaFoldDB; P50319; -.
DR   SMR; P50319; -.
DR   STRING; 381666.H16_B1385; -.
DR   EnsemblBacteria; CAJ96174; CAJ96174; H16_B1385.
DR   KEGG; reh:H16_B1385; -.
DR   eggNOG; COG0126; Bacteria.
DR   HOGENOM; CLU_025427_0_2_4; -.
DR   OMA; YVNDAYS; -.
DR   UniPathway; UPA00116; -.
DR   Proteomes; UP000008210; Chromosome 2.
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;
KW   Reference proteome; Transferase.
FT   CHAIN           1..413
FT                   /note="Phosphoglycerate kinase, chromosomal"
FT                   /id="PRO_0000145895"
FT   BINDING         40..42
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         56
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         79..82
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         134
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         167
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         218
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         340
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         366..369
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   413 AA;  42284 MW;  6B4C9D195566A90D CRC64;
     MMSLSHATNP QPKPAAAPHT LAALLAAGGL AGKRVFIRAD LNVPQDAAGA ITDDTRIRAS
     VPAIAACLQA GAAVMVTSHL GRPQEGAPDP RHSLAPVGRR LSELLGRQVP LLSGWTEGGF
     QVPPGQVVLL ENCRMNTGEK KNSDELAQKM AALCDVYVND AFGTAHRAEA TTHGIARYAP
     IACAGPLLAA EIDALGKALG QPARPLVAIV AGSKVSTKLT ILKSLADKVD NLIVGGGIAN
     TFMLAAGLKI GKSLAEPDLL ADARAIIDIM ARRGASVPIP VDVVCAKEFS ATAAATVKDV
     KDVADDDMIL DIGPKTAAML AEQLKAAGTI VWNGPVGVFE FDQFGNGTRV LAQAIAESKA
     FSIAGGGDTL AAIAKHGIAD RVGYISTGGG AFLEFLEGKT LPALAVLAQR AAA