ID   PGK_HAEIG               Reviewed;         386 AA.
AC   A5UH30;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   10-JUL-2007, sequence version 1.
DT   27-MAR-2024, entry version 82.
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};
GN   OrderedLocusNames=CGSHiGG_05875;
OS   Haemophilus influenzae (strain PittGG).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Haemophilus.
OX   NCBI_TaxID=374931;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PittGG;
RX   PubMed=17550610; DOI=10.1186/gb-2007-8-6-r103;
RA   Hogg J.S., Hu F.Z., Janto B., Boissy R., Hayes J., Keefe R., Post J.C.,
RA   Ehrlich G.D.;
RT   "Characterization and modeling of the Haemophilus influenzae core and
RT   supragenomes based on the complete genomic sequences of Rd and 12 clinical
RT   nontypeable strains.";
RL   Genome Biol. 8:R103.1-R103.18(2007).
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}.
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; CP000672; ABR00086.1; -; Genomic_DNA.
DR   AlphaFoldDB; A5UH30; -.
DR   SMR; A5UH30; -.
DR   KEGG; hiq:CGSHiGG_05875; -.
DR   HOGENOM; CLU_025427_0_2_6; -.
DR   UniPathway; UPA00109; UER00185.
DR   Proteomes; UP000001990; Chromosome.
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   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   Transferase.
FT   CHAIN           1..386
FT                   /note="Phosphoglycerate kinase"
FT                   /id="PRO_1000058001"
FT   BINDING         21..23
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00145"
FT   BINDING         36
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00145"
FT   BINDING         59..62
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00145"
FT   BINDING         112
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00145"
FT   BINDING         145
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00145"
FT   BINDING         196
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00145"
FT   BINDING         313
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00145"
FT   BINDING         339..342
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00145"
SQ   SEQUENCE   386 AA;  40985 MW;  373CDC37E3A600B9 CRC64;
     MSVIKMTDLD LAGKRVFIRA DLNVPVKDGK VTSDARIRAT IPTLKLALEK GAKVMVTSHL
     GRPTEGEFKP EDSLQPVVDY LKNAGFNVRL EQDYLNGVDV KDGEIVVLEN VRVNKGEKKN
     DPELGKKYAA LCDVFVMDAF GTAHRAQAST YGVAEFAPIA CAGPLLAAEL DALGKALKEP
     ARPMVAIVGG SKVSTKLEVL NSLSKIADQI IVGGGIANTF IAAAGHNVGK SLYEADLIPV
     AKELAANTDI PVPVDVRVGL EFSETATATE KAVNEVKDDE SIFDIGDKSA EQLAEIIKNA
     KTVLWNGPVG VFEFPHFRKG TEIISHAIAN SDAFSIAGGG DTLAAIDLFG IADKISYIST
     GGGAFLEFVE GKVLPAVEIL EKRAKN
//