ID   PGK_AQUAE               Reviewed;         397 AA.
AC   O66519;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   27-MAR-2024, entry version 119.
DE   RecName: Full=Phosphoglycerate kinase;
DE            EC=2.7.2.3;
GN   Name=pgk; OrderedLocusNames=aq_118;
OS   Aquifex aeolicus (strain VF5).
OC   Bacteria; Aquificota; Aquificae; Aquificales; Aquificaceae; Aquifex.
OX   NCBI_TaxID=224324;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VF5;
RX   PubMed=9537320; DOI=10.1038/32831;
RA   Deckert G., Warren P.V., Gaasterland T., Young W.G., Lenox A.L.,
RA   Graham D.E., Overbeek R., Snead M.A., Keller M., Aujay M., Huber R.,
RA   Feldman R.A., Short J.M., Olsen G.J., Swanson R.V.;
RT   "The complete genome of the hyperthermophilic bacterium Aquifex aeolicus.";
RL   Nature 392:353-358(1998).
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   -!- 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; AE000657; AAC06475.1; -; Genomic_DNA.
DR   PIR; D70311; D70311.
DR   RefSeq; NP_213079.1; NC_000918.1.
DR   RefSeq; WP_010880017.1; NC_000918.1.
DR   AlphaFoldDB; O66519; -.
DR   SMR; O66519; -.
DR   STRING; 224324.aq_118; -.
DR   EnsemblBacteria; AAC06475; AAC06475; aq_118.
DR   KEGG; aae:aq_118; -.
DR   PATRIC; fig|224324.8.peg.102; -.
DR   eggNOG; COG0126; Bacteria.
DR   HOGENOM; CLU_025427_0_2_0; -.
DR   InParanoid; O66519; -.
DR   OrthoDB; 9808460at2; -.
DR   UniPathway; UPA00109; UER00185.
DR   Proteomes; UP000000798; 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   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   CDD; cd00318; 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..397
FT                   /note="Phosphoglycerate kinase"
FT                   /id="PRO_0000145898"
FT   BINDING         22..24
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         38
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         61..64
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         119
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         152
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         203
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         294
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         325
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         351..354
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   397 AA;  43956 MW;  BF66BA208A8EBC57 CRC64;
     MLRKKTLRDV DVKGKRVLVR VDYNVPLDEQ GNIVDDTRIR ASLPTVEYLL DANAKVILMS
     HLGRPKNRDP KYSLAPVAKR LSRYINKEVK LAPDCVGEEV KRIVNSMKEG DVVLLENLRF
     HKEETECDEN FARELASLGE VYVADAFGTC HRKHASVYLV PKFLKPAVMG FLLEKEITYF
     EKAMVAPQRP VVAILGGAKV SSKLEVIKNL IRRVDKLFIG GAMAFTFLKA MGYKVGNSLV
     EDDLQDVARD LIDVAKKLEI KLYLPVDFVI GQEVSENTPT KVVPWQEIPD GWMGLDIGPV
     SVELVKEIIS DAQTIVWNGP MGVFEIDKFK HGTIEVAKLL AQSSALTIAG GGDTDHAIHK
     AGVYHAFDFV STGGGAFLEL LAGKELPCLV NLDDKEA
//