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
//