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Database: UniProt
Entry: Q4KQX9_SOLCI
LinkDB: Q4KQX9_SOLCI
Original site: Q4KQX9_SOLCI 
ID   Q4KQX9_SOLCI            Unreviewed;       224 AA.
AC   Q4KQX9;
DT   02-AUG-2005, integrated into UniProtKB/TrEMBL.
DT   02-AUG-2005, sequence version 1.
DT   03-MAY-2023, entry version 59.
DE   RecName: Full=Phosphoglycerate kinase {ECO:0000256|ARBA:ARBA00013061, ECO:0000256|RuleBase:RU000532};
DE            EC=2.7.2.3 {ECO:0000256|ARBA:ARBA00013061, ECO:0000256|RuleBase:RU000532};
DE   Flags: Fragment;
GN   Name=CT114 {ECO:0000313|EMBL:AAX57312.1};
OS   Solanum chilense (Tomato) (Lycopersicon chilense).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; Solanum;
OC   Solanum subgen. Lycopersicon.
OX   NCBI_TaxID=4083 {ECO:0000313|EMBL:AAX57312.1};
RN   [1] {ECO:0000313|EMBL:AAX57312.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=LA2884 {ECO:0000313|EMBL:AAX57312.1};
RX   PubMed=16050103; DOI=10.1554/04-722;
RA   Stadler T., Roselius K., Stephan W.;
RT   "Genealogical footprints of speciation processes in wild tomatoes:
RT   demography and evidence for historical gene flow.";
RL   Evolution 59:1268-1279(2005).
RN   [2] {ECO:0000313|EMBL:AAX57312.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=LA2884 {ECO:0000313|EMBL:AAX57312.1};
RA   Staedler T., Roselius K., Stephan W.;
RL   Submitted (FEB-2005) 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|RuleBase:RU000532};
CC   -!- SUBUNIT: Monomer. {ECO:0000256|RuleBase:RU000696}.
CC   -!- SIMILARITY: Belongs to the phosphoglycerate kinase family.
CC       {ECO:0000256|ARBA:ARBA00008982, ECO:0000256|RuleBase:RU000532}.
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DR   EMBL; AY941646; AAX57312.1; -; Genomic_DNA.
DR   EMBL; AY941647; AAX57313.1; -; Genomic_DNA.
DR   EMBL; AY941648; AAX57314.1; -; Genomic_DNA.
DR   EMBL; AY941649; AAX57315.1; -; Genomic_DNA.
DR   EMBL; AY941650; AAX57316.1; -; Genomic_DNA.
DR   EMBL; AY941651; AAX57317.1; -; Genomic_DNA.
DR   EMBL; AY941652; AAX57318.1; -; Genomic_DNA.
DR   EMBL; AY941653; AAX57319.1; -; Genomic_DNA.
DR   EMBL; AY941654; AAX57320.1; -; Genomic_DNA.
DR   EMBL; AY941655; AAX57321.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q4KQX9; -.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004618; F:phosphoglycerate kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006096; P:glycolytic process; IEA:InterPro.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.1260; Phosphoglycerate kinase, N-terminal domain; 1.
DR   InterPro; IPR001576; Phosphoglycerate_kinase.
DR   InterPro; IPR015824; Phosphoglycerate_kinase_N.
DR   InterPro; IPR036043; Phosphoglycerate_kinase_sf.
DR   PANTHER; PTHR11406; PHOSPHOGLYCERATE KINASE; 1.
DR   PANTHER; PTHR11406:SF27; PHOSPHOGLYCERATE KINASE 3, CYTOSOLIC; 1.
DR   Pfam; PF00162; PGK; 1.
DR   PRINTS; PR00477; PHGLYCKINASE.
DR   SUPFAM; SSF53748; Phosphoglycerate kinase; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|RuleBase:RU000532};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU000532}.
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:AAX57312.1"
FT   NON_TER         224
FT                   /evidence="ECO:0000313|EMBL:AAX57312.1"
SQ   SEQUENCE   224 AA;  23149 MW;  357D4A7E921F4A37 CRC64;
     FLMQKELDYL VGAVSNPQKP FAAIVGGSKV SSKIGVIESL LEKVDVLLLG GGMIFTFYKA
     QGYAVGSSLV EEDKLDLATS LMEKAKTKGV SLLLPTDVVI ADKFAADANS KIVPASEIPD
     GWMGLDIGPD AIKSFGSALD TTKTIIWNGP MGVFEFDKFA AGTEAIAKKL AELSGKGVTT
     IIGGGDSVAA VEKVGLAEKM SHISTGGGAS LELLEGKQLP GVLA
//
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