ID   U5DBW2_AMBTC            Unreviewed;       401 AA.
AC   U5DBW2;
DT   11-DEC-2013, integrated into UniProtKB/TrEMBL.
DT   11-DEC-2013, sequence version 1.
DT   27-MAR-2024, entry version 52.
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};
GN   ORFNames=AMTR_s00062p00191350 {ECO:0000313|EMBL:ERN19700.1};
OS   Amborella trichopoda.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Amborellales; Amborellaceae; Amborella.
OX   NCBI_TaxID=13333 {ECO:0000313|EMBL:ERN19700.1, ECO:0000313|Proteomes:UP000017836};
RN   [1] {ECO:0000313|Proteomes:UP000017836}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=24357323;
RG   Amborella Genome Project;
RT   "The Amborella genome and the evolution of flowering plants.";
RL   Science 342:1241089-1241089(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|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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; KI392068; ERN19700.1; -; Genomic_DNA.
DR   RefSeq; XP_006858233.1; XM_006858171.2.
DR   AlphaFoldDB; U5DBW2; -.
DR   STRING; 13333.U5DBW2; -.
DR   EnsemblPlants; ERN19700; ERN19700; AMTR_s00062p00191350.
DR   GeneID; 18448095; -.
DR   Gramene; ERN19700; ERN19700; AMTR_s00062p00191350.
DR   KEGG; atr:18448095; -.
DR   eggNOG; KOG1367; Eukaryota.
DR   HOGENOM; CLU_025427_0_1_1; -.
DR   OMA; VNEMITG; -.
DR   OrthoDB; 5477183at2759; -.
DR   Proteomes; UP000017836; Unassembled WGS sequence.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0043531; F:ADP binding; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IBA:GO_Central.
DR   GO; GO:0004618; F:phosphoglycerate kinase activity; IBA:GO_Central.
DR   GO; GO:0006094; P:gluconeogenesis; IBA:GO_Central.
DR   GO; GO:0006096; P:glycolytic process; IBA:GO_Central.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   CDD; cd00318; Phosphoglycerate_kinase; 1.
DR   Gene3D; 3.40.50.1260; Phosphoglycerate kinase, N-terminal domain; 2.
DR   HAMAP; MF_00145; Phosphoglyc_kinase; 1.
DR   InterPro; IPR001576; Phosphoglycerate_kinase.
DR   InterPro; IPR015911; Phosphoglycerate_kinase_CS.
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   PIRSF; PIRSF000724; Pgk; 1.
DR   PRINTS; PR00477; PHGLYCKINASE.
DR   SUPFAM; SSF53748; Phosphoglycerate kinase; 1.
DR   PROSITE; PS00111; PGLYCERATE_KINASE; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PIRSR:PIRSR000724-
KW   2}; Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|RuleBase:RU000532};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000017836};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU000532}.
FT   BINDING         25..27
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000724-1"
FT   BINDING         41
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000724-1"
FT   BINDING         64..67
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000724-1"
FT   BINDING         122
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000724-1"
FT   BINDING         155
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000724-1"
FT   BINDING         206
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000724-2"
FT   BINDING         328
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000724-2"
FT   BINDING         357..360
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000724-2"
SQ   SEQUENCE   401 AA;  42486 MW;  4C645CB2B2AF1A70 CRC64;
     MARKKSVGDL SPSDLKGKRV FVRVDLNVPL DDNQKITDDT RIRAAVPTIK YLMENGAKVI
     LASHLGRPKG VTPKYSLKPL VPRLSELLGV PVLTADDCIG EAVEKLVASL TEGGVLLLEN
     VRFYKEEEKN DPEFSKKLAA LADLYVNDAF GTAHRAHAST EGIAKFLRPA VAGFLMQKEL
     DYLVGAVSNP KRPFAAIVGG SKVSTKIGVI ESLLEKCDIL LMGGGMIFTF YEAQGFSVGS
     SLVEEDKLDL ATSLLEKAKA KGVALLLPTD VVVADKFAPD AESKVVPASE IPEGWMGLDI
     GPDSIKTFND ALEPAKTIIW NGPMGVFEFE KFAAGTKAIA KKLAELSEKG VTTIIGGGDS
     VAAVEQAGLA DKMSHISTGG GASLELLEGK PLPGVLALDD A
//