ID   PGK_AERPE               Reviewed;         415 AA.
AC   Q9YFS7;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   26-JUN-2007, sequence version 2.
DT   28-JUN-2023, entry version 109.
DE   RecName: Full=Phosphoglycerate kinase;
DE            EC=2.7.2.3;
GN   Name=pgk; OrderedLocusNames=APE_0173.1;
OS   Aeropyrum pernix (strain ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 /
OS   K1).
OC   Archaea; Thermoproteota; Thermoprotei; Desulfurococcales;
OC   Desulfurococcaceae; Aeropyrum.
OX   NCBI_TaxID=272557;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1;
RX   PubMed=10382966; DOI=10.1093/dnares/6.2.83;
RA   Kawarabayasi Y., Hino Y., Horikawa H., Yamazaki S., Haikawa Y., Jin-no K.,
RA   Takahashi M., Sekine M., Baba S., Ankai A., Kosugi H., Hosoyama A.,
RA   Fukui S., Nagai Y., Nishijima K., Nakazawa H., Takamiya M., Masuda S.,
RA   Funahashi T., Tanaka T., Kudoh Y., Yamazaki J., Kushida N., Oguchi A.,
RA   Aoki K., Kubota K., Nakamura Y., Nomura N., Sako Y., Kikuchi H.;
RT   "Complete genome sequence of an aerobic hyper-thermophilic crenarchaeon,
RT   Aeropyrum pernix K1.";
RL   DNA Res. 6:83-101(1999).
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 {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the phosphoglycerate kinase family.
CC       {ECO:0000305}.
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DR   EMBL; BA000002; BAA79084.2; -; Genomic_DNA.
DR   PIR; B72773; B72773.
DR   AlphaFoldDB; Q9YFS7; -.
DR   SMR; Q9YFS7; -.
DR   STRING; 272557.APE_0173.1; -.
DR   EnsemblBacteria; BAA79084; BAA79084; APE_0173.1.
DR   KEGG; ape:APE_0173.1; -.
DR   PATRIC; fig|272557.25.peg.123; -.
DR   eggNOG; arCOG00496; Archaea.
DR   UniPathway; UPA00109; UER00185.
DR   Proteomes; UP000002518; Chromosome.
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   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
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:SF23; PHOSPHOGLYCERATE KINASE 1, CHLOROPLASTIC-RELATED; 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; Cytoplasm; Glycolysis; Kinase; Nucleotide-binding;
KW   Reference proteome; Transferase.
FT   CHAIN           1..415
FT                   /note="Phosphoglycerate kinase"
FT                   /id="PRO_0000146049"
FT   BINDING         28..30
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         44
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         67..70
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         124
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         164
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         336
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         362..365
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   415 AA;  44902 MW;  710CBF57112A82CF CRC64;
     MPLEYMGGRL ATLDDVDVRG KKVIVRFDLN SPVGNGGEIL DDSRIAEAAG TLRELCDRGA
     AVVALSHQGR PLESDFVSLE RHASLLSRYS GVEVRFVMDV IGPEALRTVA SLRPGEAVLL
     DNTRIISEDF IEAEGTVHAR GIMVTRLSKL ANMYVNEAFS ASHRSQASIV GFPYVLPSAG
     GRVLEKEIRS LNRAVSSGER PKVVVLGGAK LKDAVRIVDY LSSSGVADEV LTTGLVGLLF
     LYARGYRLPR DVTKLLEKKG GEEAIAKARR IVEEGRRVRT PIDFVVEVGD KIYIKPADEL
     TEGVPKDIGP STVEYFRAKM RGARVIVMRG PAGVIEDPRF RRGTVELVKA ALSSGAYTVF
     GGGHFRAILR DLPEHLSSKV GHLSTGGGAL LYYLSGRPLP GVKALVDSAR IFNLV
//