(data stored in ACNUC7421 zone)

SWISSPROT: PGK_ASHGO

ID   PGK_ASHGO               Reviewed;         416 AA.
AC   Q757Q0;
DT   27-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT   09-JAN-2013, sequence version 3.
DT   11-DEC-2019, entry version 85.
DE   RecName: Full=Phosphoglycerate kinase;
DE            EC=2.7.2.3;
GN   Name=PGK1; OrderedLocusNames=AEL038C;
OS   Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS   (Yeast) (Eremothecium gossypii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX   NCBI_TaxID=284811;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX   PubMed=15001715; DOI=10.1126/science.1095781;
RA   Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA   Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA   Gaffney T.D., Philippsen P.;
RT   "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT   cerevisiae genome.";
RL   Science 304:304-307(2004).
RN   [2]
RP   GENOME REANNOTATION, AND SEQUENCE REVISION TO 94-100.
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX   PubMed=23749448; DOI=10.1534/g3.112.002881;
RA   Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT   "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT   loci, numerous translocations, lack of transposons, and distinct gene
RT   duplications.";
RL   G3 (Bethesda) 3:1225-1239(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   -!- SUBUNIT: Monomer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the phosphoglycerate kinase family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAS52647.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
DR   EMBL; AE016818; AAS52647.2; ALT_INIT; Genomic_DNA.
DR   RefSeq; NP_984823.2; NM_210177.2.
DR   SMR; Q757Q0; -.
DR   STRING; 33169.AAS52647; -.
DR   PRIDE; Q757Q0; -.
DR   GeneID; 4621019; -.
DR   KEGG; ago:AGOS_AEL038C; -.
DR   HOGENOM; HOG000227107; -.
DR   InParanoid; Q757Q0; -.
DR   KO; K00927; -.
DR   Proteomes; UP000000591; Chromosome V.
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:1903862; P:positive regulation of oxidative phosphorylation; IBA:GO_Central.
DR   CDD; cd00318; Phosphoglycerate_kinase; 1.
DR   Gene3D; 3.40.50.1260; -; 3.
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;
DR   PRODOM; Q757Q0.
DR   SWISS-2DPAGE; Q757Q0.
KW   ATP-binding; Cytoplasm; Glycolysis; Kinase; Nucleotide-binding;
KW   Reference proteome; Transferase.
FT   CHAIN           1..416
FT                   /note="Phosphoglycerate kinase"
FT                   /id="PRO_0000145874"
FT   NP_BIND         371..374
FT                   /note="ATP"
FT                   /evidence="ECO:0000250"
FT   REGION          24..26
FT                   /note="Substrate binding"
FT                   /evidence="ECO:0000250"
FT   REGION          63..66
FT                   /note="Substrate binding"
FT                   /evidence="ECO:0000250"
FT   BINDING         39
FT                   /note="Substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         122
FT                   /note="Substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         169
FT                   /note="Substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         218
FT                   /note="ATP"
FT                   /evidence="ECO:0000250"
FT   BINDING         311
FT                   /note="ATP; via carbonyl oxygen"
FT                   /evidence="ECO:0000250"
FT   BINDING         342
FT                   /note="ATP"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   416 AA;  44219 MW;  C53E920FEFEFC3CD CRC64;
     MSLSSKLTVK DLSLAGKRVF IRVDFNVPLD GKTITSNQRI VAALPTIKYV LEQGPKAVVL
     ASHLGRPNGE RNEKYSLAPV AAELEKLLGQ KVNFLDDCVG EHVTAAVNGA AAGSVFLLEN
     LRFHIEEEGS RKVDGEKVKA SAEDVQKFRQ GLMSLADVYV NDAFGTAHRA HSSMVGFELP
     ERAGGFLLSR ELEYFSKALE NPTRPFLAIL GGAKVADKIQ LIDNLLDKVD SIVIGGGMAF
     TFKKVLENME IGNSIYDKAG AEIVPKLAEK AKKNGVKIVL PVDFVIGDDF SQDANTKIVS
     ASEGIPSGWE GLDCGPESRK LFSETIASAK TIVWNGPPGV FEIPKFSEGT QAMLAAAVKA
     SEAGSTVIIG GGDTATVAKK YGVVEKISHV STGGGASLEL LEGKDLPGVT FLSSKQ
//

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