ID A1X7A7_AEGSP Unreviewed; 234 AA.
AC A1X7A7;
DT 06-FEB-2007, integrated into UniProtKB/TrEMBL.
DT 06-FEB-2007, sequence version 1.
DT 24-JAN-2024, entry version 51.
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=pgk1 {ECO:0000313|EMBL:ABB99706.1};
OS Aegilops speltoides (Goatgrass) (Triticum speltoides).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Pooideae; Triticodae; Triticeae; Triticinae; Aegilops.
OX NCBI_TaxID=4573 {ECO:0000313|EMBL:ABB99706.1};
RN [1] {ECO:0000313|EMBL:ABB99706.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=A2IIK393 {ECO:0000313|EMBL:ABB99706.1};
RX PubMed=17053048; DOI=10.1093/molbev/msl151;
RA Kilian B., Ozkan H., Deusch O., Effgen S., Brandolini A., Kohl J.,
RA Martin W., Salamini F.;
RT "Independent wheat B and G genome origins in outcrossing Aegilops
RT progenitor haplotypes.";
RL Mol. Biol. Evol. 24:217-227(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: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; DQ290750; ABB99706.1; -; Genomic_DNA.
DR AlphaFoldDB; A1X7A7; -.
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:ABB99706.1"
FT NON_TER 234
FT /evidence="ECO:0000313|EMBL:ABB99706.1"
SQ SEQUENCE 234 AA; 24819 MW; 425EC882B89D7AE5 CRC64;
SELLGIEVKK AEDVIGPEVE KLVADLANGA VLLLENVRFY KEEEKNDPEF AKKLASLADL
FVNDAFGTAH RAHASTEGVT KFLKPSVAGF LLQKELDYLD GAVSNPKRPF AAIVGGSKVS
SKIGVIESLL EKCDILLLGG GMIFTFYKAQ GLSVGSSLVE EDKLELATSL LAKAKAKGVS
LLLPSDVIIA DKFAPDANSQ IVPASAIPDG WMGLDIGPDS VKTFNDALDT TQTI
//
