ID   PGK_HELPY               Reviewed;         402 AA.
AC   P56154;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   03-AUG-2022, entry version 116.
DE   RecName: Full=Phosphoglycerate kinase;
DE            EC=2.7.2.3;
GN   Name=pgk; OrderedLocusNames=HP_1345;
OS   Helicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter pylori).
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Helicobacteraceae; Helicobacter.
OX   NCBI_TaxID=85962;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700392 / 26695;
RX   PubMed=9252185; DOI=10.1038/41483;
RA   Tomb J.-F., White O., Kerlavage A.R., Clayton R.A., Sutton G.G.,
RA   Fleischmann R.D., Ketchum K.A., Klenk H.-P., Gill S.R., Dougherty B.A.,
RA   Nelson K.E., Quackenbush J., Zhou L., Kirkness E.F., Peterson S.N.,
RA   Loftus B.J., Richardson D.L., Dodson R.J., Khalak H.G., Glodek A.,
RA   McKenney K., FitzGerald L.M., Lee N., Adams M.D., Hickey E.K., Berg D.E.,
RA   Gocayne J.D., Utterback T.R., Peterson J.D., Kelley J.M., Cotton M.D.,
RA   Weidman J.F., Fujii C., Bowman C., Watthey L., Wallin E., Hayes W.S.,
RA   Borodovsky M., Karp P.D., Smith H.O., Fraser C.M., Venter J.C.;
RT   "The complete genome sequence of the gastric pathogen Helicobacter
RT   pylori.";
RL   Nature 388:539-547(1997).
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 degradation; glycolysis; pyruvate from D-
CC       glyceraldehyde 3-phosphate: step 2/5.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the phosphoglycerate kinase family.
CC       {ECO:0000305}.
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DR   EMBL; AE000511; AAD08386.1; -; Genomic_DNA.
DR   PIR; A64688; A64688.
DR   RefSeq; NP_208137.1; NC_000915.1.
DR   RefSeq; WP_000880064.1; NC_018939.1.
DR   AlphaFoldDB; P56154; -.
DR   SMR; P56154; -.
DR   DIP; DIP-3617N; -.
DR   IntAct; P56154; 3.
DR   MINT; P56154; -.
DR   STRING; 85962.C694_06940; -.
DR   PaxDb; P56154; -.
DR   EnsemblBacteria; AAD08386; AAD08386; HP_1345.
DR   KEGG; hpy:HP_1345; -.
DR   PATRIC; fig|85962.47.peg.1440; -.
DR   eggNOG; COG0126; Bacteria.
DR   OMA; YVNDAYS; -.
DR   PhylomeDB; P56154; -.
DR   UniPathway; UPA00109; UER00185.
DR   Proteomes; UP000000429; Chromosome.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0043531; F:ADP binding; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IBA:GO_Central.
DR   GO; GO:0004618; F:phosphoglycerate kinase activity; IBA:GO_Central.
DR   GO; GO:0006094; P:gluconeogenesis; IBA:GO_Central.
DR   GO; GO:0006096; P:glycolytic process; IBA:GO_Central.
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; Cytoplasm; Glycolysis; Kinase; Nucleotide-binding;
KW   Reference proteome; Transferase.
FT   CHAIN           1..402
FT                   /note="Phosphoglycerate kinase"
FT                   /id="PRO_0000145950"
FT   BINDING         29..31
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         45
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         69..72
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         125
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         158
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         209
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         331
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         357..360
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   402 AA;  44772 MW;  D74B63DBAF4465D7 CRC64;
     MLAKMSFMQN VKNIQEVEVS HKRVLIRVDF NVPLDENLNI TDDTRIRESL PTIQYCIDNK
     AKDIILVSHL GRPKGVEEKL SLKPFLKRLE RLLNHEVVFS QNIVQLKQAL NENAPTRIFL
     LENIRFLRGE EENDENLAKD LASLCDVFVN DAFGTSHRKH ASTYGTAKFA PIKVSGFLLK
     KEIDSFYQAF NHPLRPLLLI VGGAKVSSKL TLLKNILDLI DKLIIAGAMS NTFLKALGYD
     VQDSSVEDAL INDALELLQS AKEKKVKVYL PIDAVTTDDI LNPKHIKISP VQDIEPKHKI
     ADIGPASLKL FSEVIESAPT ILWNGPLGVH EKQEFARGTT FLAHKIADTY AFSLIGGGDT
     IDAINRAGEK DNMSFISTGG GASLELLEGK ILPCFEVLDK RH