ID   PGK_PROM0               Reviewed;         402 AA.
AC   A3PAR3;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   03-APR-2007, sequence version 1.
DT   27-MAR-2024, entry version 95.
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=P9301_02151;
OS   Prochlorococcus marinus (strain MIT 9301).
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales;
OC   Prochlorococcaceae; Prochlorococcus.
OX   NCBI_TaxID=167546;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MIT 9301;
RX   PubMed=18159947; DOI=10.1371/journal.pgen.0030231;
RA   Kettler G.C., Martiny A.C., Huang K., Zucker J., Coleman M.L., Rodrigue S.,
RA   Chen F., Lapidus A., Ferriera S., Johnson J., Steglich C., Church G.M.,
RA   Richardson P., Chisholm S.W.;
RT   "Patterns and implications of gene gain and loss in the evolution of
RT   Prochlorococcus.";
RL   PLoS Genet. 3:2515-2528(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; CP000576; ABO16838.1; -; Genomic_DNA.
DR   RefSeq; WP_011862240.1; NC_009091.1.
DR   AlphaFoldDB; A3PAR3; -.
DR   SMR; A3PAR3; -.
DR   STRING; 167546.P9301_02151; -.
DR   KEGG; pmg:P9301_02151; -.
DR   eggNOG; COG0126; Bacteria.
DR   HOGENOM; CLU_025427_0_2_3; -.
DR   OrthoDB; 9808460at2; -.
DR   UniPathway; UPA00109; UER00185.
DR   Proteomes; UP000001430; 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   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..402
FT                   /note="Phosphoglycerate kinase"
FT                   /id="PRO_1000058025"
FT   BINDING         24..26
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00145"
FT   BINDING         40
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00145"
FT   BINDING         63..66
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00145"
FT   BINDING         122
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00145"
FT   BINDING         155
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00145"
FT   BINDING         206
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00145"
FT   BINDING         297
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00145"
FT   BINDING         328
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;  42748 MW;  9EE3B5F072F56316 CRC64;
     MSKLSLSSLD KTHLEGKKVL VRVDFNVPLN EDGQITDDTR IRAAIPTIEY LVNHSAKVIL
     AAHFGRPKGQ VNEKMRLTPV AARLSELLGQ SVALTNSCIG DEAVAKSNSL SNRDVLLLEN
     VRFFGEEEKN DLEFAQKLAS HADMYVNDAF GAAHRAHAST QGVTNYLSPS VAGFLLEKEL
     KYLQGAVDSP NRPLAAIVGG SKVSSKIGVL DSLLDKCDKI MIGGGMIFTF YKARGLDVGK
     SLVEEDKLEL AKDLEAKAKA KGVELLLPTD VVLANEFSPD AESKISQIDS ISGNWMGLDI
     GPDSIKVFQN ALAECKTIIW NGPMGVFEFD KFADGTNAIA TTLADLSAFS EVCTIIGGGD
     SVAAVEKAGL AEKMSHISTG GGASLELLEG KILPGVAALN DA
//