ID   PGK_HELHP               Reviewed;         402 AA.
AC   Q7VJB6;
DT   26-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   02-SEP-2026, entry version 113.
DE   RecName: Full=Phosphoglycerate kinase {ECO:0000255|HAMAP-Rule:MF_00145};
DE            EC=2.7.2.3 {ECO:0000255|HAMAP-Rule:MF_00145};
GN   Name=pgk {ECO:0000255|HAMAP-Rule:MF_00145}; OrderedLocusNames=HH_0327;
OS   Helicobacter hepaticus (strain ATCC 51449 / 3B1).
OC   Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
OC   Campylobacterales; Helicobacteraceae; Helicobacter.
OX   NCBI_TaxID=235279;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51449 / 3B1;
RX   PubMed=12810954; DOI=10.1073/pnas.1332093100;
RA   Suerbaum S., Josenhans C., Sterzenbach T., Drescher B., Brandt P., Bell M.,
RA   Droege M., Fartmann B., Fischer H.-P., Ge Z., Hoerster A., Holland R.,
RA   Klein K., Koenig J., Macko L., Mendz G.L., Nyakatura G., Schauer D.B.,
RA   Shen Z., Weber J., Frosch M., Fox J.G.;
RT   "The complete genome sequence of the carcinogenic bacterium Helicobacter
RT   hepaticus.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:7901-7906(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         Evidence={ECO:0000255|HAMAP-Rule:MF_00145};
CC   -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
CC       glyceraldehyde 3-phosphate: step 2/5. {ECO:0000255|HAMAP-
CC       Rule:MF_00145}.
CC   -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_00145}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00145}.
CC   -!- SIMILARITY: Belongs to the phosphoglycerate kinase family.
CC       {ECO:0000255|HAMAP-Rule:MF_00145}.
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DR   EMBL; AE017125; AAP76924.1; -; Genomic_DNA.
DR   RefSeq; WP_011115170.1; NC_004917.1.
DR   AlphaFoldDB; Q7VJB6; -.
DR   SMR; Q7VJB6; -.
DR   STRING; 235279.HH_0327; -.
DR   KEGG; hhe:HH_0327; -.
DR   eggNOG; COG0126; Bacteria.
DR   HOGENOM; CLU_025427_0_2_7; -.
DR   OrthoDB; 9808460at2; -.
DR   UniPathway; UPA00109; UER00185.
DR   Proteomes; UP000002495; Chromosome.
DR   GO; GO:0005829; C:cytosol; IEA:TreeGrafter.
DR   GO; GO:0043531; F:ADP binding; IEA:TreeGrafter.
DR   GO; GO:0005524; F:ATP binding; IEA:TreeGrafter.
DR   GO; GO:0004618; F:phosphoglycerate kinase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006094; P:gluconeogenesis; IEA:TreeGrafter.
DR   GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-UniRule.
DR   FunFam; 3.40.50.1260:FF:000006; Phosphoglycerate kinase; 1.
DR   FunFam; 3.40.50.1260:FF:000012; Phosphoglycerate kinase; 1.
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; Cytoplasm; Glycolysis; Kinase; Nucleotide-binding;
KW   Reference proteome; Transferase.
FT   CHAIN           1..402
FT                   /note="Phosphoglycerate kinase"
FT                   /id="PRO_0000145949"
FT   BINDING         30..32
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00145"
FT   BINDING         46
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00145"
FT   BINDING         70..73
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00145"
FT   BINDING         126
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00145"
FT   BINDING         159
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00145"
FT   BINDING         210
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00145"
FT   BINDING         332
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00145"
FT   BINDING         358..361
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00145"
SQ   SEQUENCE   402 AA;  44464 MW;  7C5BDBF24113F8D6 CRC64;
     MKETGIELMK NTKSVRDIDV KDKRVLIRVD FNVPMDEDFD ISDDTRIREA LPTINYCIDN
     HAQNIVLVSH LGRPKGRNAE FSLKHVLKRV ERLLGRDIAF AETIENVENL QQQSKSGSVI
     LLENIRFYEG EEKNDEELST KLASICDVYI NDAFGTSHRA HSSTCGIAKY AKECVAGLLL
     KKEIDSFAKA MANPLKPVLL IVGGSKVSSK LALLYNILDV VDKIIIGGAM SNTFLKARGF
     DMQKSLVEDD LVSEARKILD KAKEKKVKIY LPVDVVSTDD IKEHRHIKIT PAQDIPEGFM
     AVDMGPATSK LFSEVVRDSQ TIIWNGPLGI YEIQAFSRGT FNLAHAVSDT YAFSLIGGGD
     TADAIDKAGE RDNMSFISTG GGASLELLEG KILPAFEVLE RK
//