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Database: UniProt
Entry: Q05VI9_9SYNE
LinkDB: Q05VI9_9SYNE
Original site: Q05VI9_9SYNE 
ID   Q05VI9_9SYNE            Unreviewed;       401 AA.
AC   Q05VI9;
DT   14-NOV-2006, integrated into UniProtKB/TrEMBL.
DT   14-NOV-2006, sequence version 1.
DT   24-JAN-2024, entry version 92.
DE   RecName: Full=Phosphoglycerate kinase {ECO:0000256|ARBA:ARBA00013061, ECO:0000256|HAMAP-Rule:MF_00145};
DE            EC=2.7.2.3 {ECO:0000256|ARBA:ARBA00013061, ECO:0000256|HAMAP-Rule:MF_00145};
GN   Name=pgk {ECO:0000256|HAMAP-Rule:MF_00145};
GN   ORFNames=RS9916_36362 {ECO:0000313|EMBL:EAU75098.1};
OS   Synechococcus sp. RS9916.
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales; Synechococcaceae;
OC   Synechococcus.
OX   NCBI_TaxID=221359 {ECO:0000313|EMBL:EAU75098.1, ECO:0000313|Proteomes:UP000004972};
RN   [1] {ECO:0000313|EMBL:EAU75098.1, ECO:0000313|Proteomes:UP000004972}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RS9916 {ECO:0000313|EMBL:EAU75098.1,
RC   ECO:0000313|Proteomes:UP000004972};
RA   Scanlan D., Ferriera S., Johnson J., Kravitz S., Halpern A., Remington K.,
RA   Beeson K., Tran B., Rogers Y.-H., Friedman R., Venter J.C.;
RL   Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
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:0000256|ARBA:ARBA00000642, ECO:0000256|HAMAP-
CC         Rule:MF_00145, ECO:0000256|RuleBase:RU000532};
CC   -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
CC       glyceraldehyde 3-phosphate: step 2/5. {ECO:0000256|HAMAP-
CC       Rule:MF_00145}.
CC   -!- SUBUNIT: Monomer. {ECO:0000256|HAMAP-Rule:MF_00145}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00145}.
CC   -!- SIMILARITY: Belongs to the phosphoglycerate kinase family.
CC       {ECO:0000256|HAMAP-Rule:MF_00145, ECO:0000256|RuleBase:RU000532}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EAU75098.1}.
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DR   EMBL; AAUA01000001; EAU75098.1; -; Genomic_DNA.
DR   RefSeq; WP_007099195.1; NZ_DS022299.1.
DR   AlphaFoldDB; Q05VI9; -.
DR   STRING; 221359.RS9916_36362; -.
DR   eggNOG; COG0126; Bacteria.
DR   HOGENOM; CLU_025427_0_2_3; -.
DR   OrthoDB; 9808460at2; -.
DR   UniPathway; UPA00109; UER00185.
DR   Proteomes; UP000004972; Unassembled WGS sequence.
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 {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW   Rule:MF_00145}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00145};
KW   Glycolysis {ECO:0000256|HAMAP-Rule:MF_00145};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|HAMAP-Rule:MF_00145};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_00145}; Reference proteome {ECO:0000313|Proteomes:UP000004972};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_00145}.
FT   BINDING         24..26
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00145,
FT                   ECO:0000256|PIRSR:PIRSR000724-1"
FT   BINDING         40
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00145,
FT                   ECO:0000256|PIRSR:PIRSR000724-1"
FT   BINDING         63..66
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00145,
FT                   ECO:0000256|PIRSR:PIRSR000724-1"
FT   BINDING         122
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00145,
FT                   ECO:0000256|PIRSR:PIRSR000724-1"
FT   BINDING         155
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00145,
FT                   ECO:0000256|PIRSR:PIRSR000724-1"
FT   BINDING         206
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00145,
FT                   ECO:0000256|PIRSR:PIRSR000724-2"
FT   BINDING         297
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00145,
FT                   ECO:0000256|PIRSR:PIRSR000724-2"
FT   BINDING         328
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00145,
FT                   ECO:0000256|PIRSR:PIRSR000724-2"
FT   BINDING         357..360
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00145,
FT                   ECO:0000256|PIRSR:PIRSR000724-2"
SQ   SEQUENCE   401 AA;  41546 MW;  CA289772CE0A6FD8 CRC64;
     MAKRSLASLT GADLSGKRVL VRVDFNVPLN DAGAITDDTR IRAALPTIND LIGKGAKVIL
     SAHFGRPKGQ VNDSMRLTPV AARLSELLGK PVVKTDSCIG PDAEAKVGAM ADGDVVLLEN
     VRFFAEEEKN DAGFAEKLAG LAEVYVNDAF GAAHRAHAST EGVTKFLKPS VGGFLMEKEL
     QYLQGAIDAP KRPLAAIVGG SKVSSKIGVL EALMDKCDKI LVGGGMIFTF YKARGLAVGK
     SLVEEDKLEL AKELEAKAKA KGVELLLPTD VVLADNFAPD ANSQTAPVTA IPDGWMGLDI
     GPDSVKVFQN ALADCQTVIW NGPMGVFEFD KFAAGTNAIA TTLADLSGKG CCTIIGGGDS
     VAAVEKAGLA DKMSHISTGG GASLELLEGK VLPGVAALDA A
//
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