ID   PGK_SYNJB               Reviewed;         412 AA.
AC   Q2JKX6;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   07-MAR-2006, sequence version 1.
DT   03-AUG-2022, entry version 91.
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=CYB_1693;
OS   Synechococcus sp. (strain JA-2-3B'a(2-13)) (Cyanobacteria bacterium
OS   Yellowstone B-Prime).
OC   Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus;
OC   unclassified Synechococcus.
OX   NCBI_TaxID=321332;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JA-2-3B'a(2-13);
RX   PubMed=18059494; DOI=10.1038/ismej.2007.46;
RA   Bhaya D., Grossman A.R., Steunou A.-S., Khuri N., Cohan F.M., Hamamura N.,
RA   Melendrez M.C., Bateson M.M., Ward D.M., Heidelberg J.F.;
RT   "Population level functional diversity in a microbial community revealed by
RT   comparative genomic and metagenomic analyses.";
RL   ISME J. 1:703-713(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}.
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DR   EMBL; CP000240; ABD02652.1; -; Genomic_DNA.
DR   RefSeq; WP_011433296.1; NC_007776.1.
DR   AlphaFoldDB; Q2JKX6; -.
DR   SMR; Q2JKX6; -.
DR   STRING; 321332.CYB_1693; -.
DR   KEGG; cyb:CYB_1693; -.
DR   eggNOG; COG0126; Bacteria.
DR   HOGENOM; CLU_025427_0_2_3; -.
DR   OMA; DMIFDIG; -.
DR   OrthoDB; 462069at2; -.
DR   UniPathway; UPA00109; UER00185.
DR   Proteomes; UP000001938; 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   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..412
FT                   /note="Phosphoglycerate kinase"
FT                   /id="PRO_1000058076"
FT   BINDING         26..28
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00145"
FT   BINDING         42
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00145"
FT   BINDING         65..68
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00145"
FT   BINDING         133
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00145"
FT   BINDING         166
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00145"
FT   BINDING         217
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00145"
FT   BINDING         308
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00145"
FT   BINDING         339
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00145"
FT   BINDING         368..371
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00145"
SQ   SEQUENCE   412 AA;  43532 MW;  53269D11F35DFFEA CRC64;
     MAKQTLGSLL SSGFDLAGKR VLVRADFNVP LDAQGNITDD TRIRAALPTV QALTQAGAKV
     ILTSHLGRPV KKDKETGAVK VAREGNSLAP VATRLSQLLG QPVAFAPDCI GPEAEAVVNR
     LENGQVALLE NVRFYPEEED NDPEFARKLA SLADLFVNDA FGSAHRAHAS TAGVTAYLQP
     AVAGYLVERE LQFLSGAIED PRRPLAAIIG GSKVSTKIGV IERLLEKVDK LLLGGGMIFT
     FYQAQGIQTG KSLVETDKLD LARSLMEKAK ERGVELLLPV DVVVADRFDK DAQAQTVSIH
     AIPEDWMGLD IGPESVKAFQ SALQGCQTVV WNGPMGVFEF DRFALGTEAI ARTLADLTQA
     GATTIIGGGD SVAAVEKVGL ADKMTHISTG GGASLELLEG KVLPGIAALT EA