ID   PGK_HALVA               Reviewed;         401 AA.
AC   P50315;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   03-AUG-2022, entry version 82.
DE   RecName: Full=Phosphoglycerate kinase;
DE            EC=2.7.2.3;
GN   Name=pgk;
OS   Haloarcula vallismortis (Halobacterium vallismortis).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC   Haloarculaceae; Haloarcula.
OX   NCBI_TaxID=28442;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 29715 / DSM 3756 / JCM 8877 / NBRC 14741 / NCIMB 2082;
RX   PubMed=8616244; DOI=10.1007/bf00017803;
RA   Brinkmann H., Martin W.;
RT   "Higher-plant chloroplast and cytosolic 3-phosphoglycerate kinases: a case
RT   of endosymbiotic gene replacement.";
RL   Plant Mol. Biol. 30:65-75(1996).
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   -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
CC       glyceraldehyde 3-phosphate: step 2/5.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the phosphoglycerate kinase family.
CC       {ECO:0000305}.
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DR   EMBL; L47295; AAB03731.1; -; Genomic_DNA.
DR   PIR; S65044; S65044.
DR   AlphaFoldDB; P50315; -.
DR   SMR; P50315; -.
DR   STRING; 28442.SAMN05443574_102192; -.
DR   UniPathway; UPA00109; UER00185.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004618; F:phosphoglycerate kinase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.40.50.1260; -; 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; PTHR11406; 1.
DR   Pfam; PF00162; PGK; 1.
DR   PIRSF; PIRSF000724; Pgk; 1.
DR   PRINTS; PR00477; PHGLYCKINASE.
DR   SUPFAM; SSF53748; SSF53748; 1.
DR   PROSITE; PS00111; PGLYCERATE_KINASE; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Cytoplasm; Glycolysis; Kinase; Nucleotide-binding;
KW   Transferase.
FT   CHAIN           1..401
FT                   /note="Phosphoglycerate kinase"
FT                   /id="PRO_0000146053"
FT   BINDING         21..23
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         36
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         59..62
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         116
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         156
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         331
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         357..360
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   401 AA;  44193 MW;  ACDD98F8856B490E CRC64;
     MMTFQTLDDL DDGQRVLVRL DLNSPVEDGT VQDNRRFDRH AETVKELADR GFEVAVLAHQ
     GRPGRDDFVS LDQHADILAD HIDRDVDFVD ETYGPQAIHD IADLDSGDVL VLENTRMCDD
     ELPEEDPEVK AQTEFVKTLA GEFDAYINDA YSAAHRSHAS LVGFPLVMDA YAGRVMETEY
     EANTAIAEKE FDGQVTMVVG GTKATDVIDV MTHLDEKVDD FLLGGIAGTV PAAAGHPVGY
     DIDDANLYDE QWEANSEKIE SMLEDHRDQI TLAVDLAYED ENDDRAEQAV DDIDEKRLSY
     LDVGSETLME YSPIIRESEA VFGEGRAGMF EDERFSVGTA GVLEAIADTD CFSVVGGGDT
     SRAIEMYGME EDEFGHVSIA GGAYIRALTR AQLVGVEVLQ R