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Database: UniProt
Entry: Q8LLS8_AEGSP
LinkDB: Q8LLS8_AEGSP
Original site: Q8LLS8_AEGSP 
ID   Q8LLS8_AEGSP            Unreviewed;       298 AA.
AC   Q8LLS8;
DT   01-OCT-2002, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2002, sequence version 1.
DT   24-JAN-2024, entry version 75.
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=Pgk-1 {ECO:0000313|EMBL:AAM51716.1};
OS   Aegilops speltoides var. ligustica.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Pooideae; Triticodae; Triticeae; Triticinae; Aegilops.
OX   NCBI_TaxID=58532 {ECO:0000313|EMBL:AAM51716.1};
RN   [1] {ECO:0000313|EMBL:AAM51716.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=11999851; DOI=10.1023/A:1014868320552;
RA   Huang S., Sirikhachornkit A., Faris J.D., Su X., Gill B.S., Haselkorn R.,
RA   Gornicki P.;
RT   "Phylogenetic analysis of the acetyl-CoA carboxylase and 3-phosphoglycerate
RT   kinase loci in wheat and other grasses.";
RL   Plant Mol. Biol. 48:805-820(2002).
RN   [2] {ECO:0000313|EMBL:AAM51716.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=12060759; DOI=10.1073/pnas.072223799;
RA   Huang S., Sirikhachornkit A., Su X., Faris J., Gill B., Haselkorn R.,
RA   Gornicki P.;
RT   "Genes encoding plastid acetyl-CoA carboxylase and 3-phosphoglycerate
RT   kinase of the Triticum/Aegilops complex and the evolutionary history of
RT   polyploid wheat.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:8133-8138(2002).
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,
CC         ECO:0000256|RuleBase:RU000532};
CC   -!- PATHWAY: Carbohydrate biosynthesis; Calvin cycle.
CC       {ECO:0000256|ARBA:ARBA00005215}.
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; AF343490; AAM51716.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q8LLS8; -.
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; 2.
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:SF23; PHOSPHOGLYCERATE KINASE 1, CHLOROPLASTIC-RELATED; 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:AAM51716.1"
FT   NON_TER         298
FT                   /evidence="ECO:0000313|EMBL:AAM51716.1"
SQ   SEQUENCE   298 AA;  31421 MW;  AA3F032A89923E20 CRC64;
     FSLAPLVPRL SELLGIAVKK AEDVIGPEVE KLVADLENGA VLLLENVRFY KEEEKNDPEF
     AKKLASLADL FVNDAFGTAH RAHASTEGVT KFLKPSVAGF LLQKELDYLD GAVSNPKRPF
     AAIVGGSKVS SKIGVIESLL EKCDILLLGG GMIFTFYKAQ GLSVGSSLVE EDKLELATSL
     LAKAKAKGVS LLLPSDVIIA DKFAPDANSQ TVPASAIPDG WMGLDIGPDS VKTFNDALDT
     TQTIIWNGPM GVFEFDKFAV GTESIAKKLA ELSKKGVTTI IGGGDSVAAV EKVGVADV
//
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