ID   PGK_SYNY3               Reviewed;         401 AA.
AC   P74421;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 2.
DT   03-AUG-2022, entry version 122.
DE   RecName: Full=Phosphoglycerate kinase;
DE            EC=2.7.2.3;
GN   Name=pgk; OrderedLocusNames=slr0394;
OS   Synechocystis sp. (strain PCC 6803 / Kazusa).
OC   Bacteria; Cyanobacteria; Synechococcales; Merismopediaceae; Synechocystis;
OC   unclassified Synechocystis.
OX   NCBI_TaxID=1111708;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 6803 / Kazusa;
RX   PubMed=8905231; DOI=10.1093/dnares/3.3.109;
RA   Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y.,
RA   Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T.,
RA   Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S.,
RA   Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT   "Sequence analysis of the genome of the unicellular cyanobacterium
RT   Synechocystis sp. strain PCC6803. II. Sequence determination of the entire
RT   genome and assignment of potential protein-coding regions.";
RL   DNA Res. 3:109-136(1996).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAA18521.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; BA000022; BAA18521.1; ALT_INIT; Genomic_DNA.
DR   PIR; S76392; S76392.
DR   AlphaFoldDB; P74421; -.
DR   SMR; P74421; -.
DR   IntAct; P74421; 5.
DR   STRING; 1148.1653609; -.
DR   PaxDb; P74421; -.
DR   EnsemblBacteria; BAA18521; BAA18521; BAA18521.
DR   KEGG; syn:slr0394; -.
DR   eggNOG; COG0126; Bacteria.
DR   InParanoid; P74421; -.
DR   OMA; DMIFDIG; -.
DR   PhylomeDB; P74421; -.
DR   UniPathway; UPA00109; UER00185.
DR   Proteomes; UP000001425; 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   CDD; cd00318; Phosphoglycerate_kinase; 1.
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..401
FT                   /note="Phosphoglycerate kinase"
FT                   /id="PRO_0000146024"
FT   BINDING         25..27
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         40
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         63..66
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         122
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         155
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         206
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         297
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         328
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   401 AA;  41784 MW;  74905FDBBCF81B7D CRC64;
     MLSKQSIANL TEADLAGKRV FVRVDFNVPL DNGSITDDTR IRAALPTIKD LLSKGAKVIL
     GSHFGRPKGK VVDSMRLTPV GDRLGELLGQ PVVKCDDCIG AEVTAKIASL PNGGVALLEN
     LRFHAGEEGN DAEFAKALAA NADLYVNDAF GTAHRAHAST EGVTHFLSPN VAGYLIEKEL
     QFLQGAIEAP KRPLVAIVGG SKVSSKIGVI ETLLDKCDKL IIGGGMIFTF YKAQGLNTGK
     SLVEEDKLDL AKSLMAKAKE KGVEFLLPTD VVVADNFAPD ANAQTVGVDA IPDGWMGLDI
     GPDSVKTFQD ALAGCGTVIW NGPMGVFEFD KFAVGTEAIA CSLAELTASG TVTIIGGGDS
     VAAVEKVGVA EKMSHISTGG GASLELLEGK VLPGIAALDD R