ID R4S2T3_9POAL Unreviewed; 298 AA.
AC R4S2T3;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 24-JAN-2024, entry version 25.
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:AGL91128.1};
OS Anthosachne rectiseta.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Pooideae; Triticodae; Triticeae; Hordeinae; Anthosachne.
OX NCBI_TaxID=129752 {ECO:0000313|EMBL:AGL91128.1};
RN [1] {ECO:0000313|EMBL:AGL91128.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=23816902; DOI=10.1016/j.ympev.2013.06.012;
RA Fan X., Sha L.N., Dong Z.Z., Zhang H.Q., Kang H.Y., Wang Y., Wang X.L.,
RA Zhang L., Ding C.B., Yang R.W., Zheng Y.L., Zhou Y.H.;
RT "Phylogenetic relationships and Y genome origin in Elymus L. sensu lato
RT (Triticeae; Poaceae) based on single-copy nuclear Acc1 and Pgk1 gene
RT sequences.";
RL Mol. Phylogenet. Evol. 69:919-928(2013).
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; KC131226; AGL91128.1; -; Genomic_DNA.
DR AlphaFoldDB; R4S2T3; -.
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:AGL91128.1"
FT NON_TER 298
FT /evidence="ECO:0000313|EMBL:AGL91128.1"
SQ SEQUENCE 298 AA; 31352 MW; 2CC793563A8AACC1 CRC64;
FSLAPLVPRL SELLGIEVKK ADDVIGPEVE KLVADLANGA VLLLENVRFY KEEEKNDPEF
AKKLASLADL FVTDAFGTAH RAHASTEGVT KFLKPSVAGF LLRKELDYLD GAVSNPKRPF
AAIVGGSKVS SKIGVIESLL EKCDILLLGG GMIFTFYKAQ GLSVGSSLVE EDKLELATSL
LAKAKAKGVS LLLPSDVVIA DKFAPDANSQ TVAASAIPDG WMGLDIGPDS VKTFNDALDT
TQTIIWNGPM GVFEFDKFAV GTEAVAKKLA ELSKKGVTTI IGGGDSVAAV EKVGVADV
//