(data stored in ACNUC6288 zone)

SWISSPROT: G3P_DEBHA

ID   G3P_DEBHA               Reviewed;         335 AA.
AC   Q6BMK0;
DT   11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   11-DEC-2019, entry version 101.
DE   RecName: Full=Glyceraldehyde-3-phosphate dehydrogenase;
DE            Short=GAPDH;
DE            EC=1.2.1.12;
GN   Name=GPD; OrderedLocusNames=DEHA2F04796g;
OS   Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / JCM 1990 / NBRC 0083 /
OS   IGC 2968) (Yeast) (Torulaspora hansenii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Debaryomyces.
OX   NCBI_TaxID=284592;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 36239 / CBS 767 / JCM 1990 / NBRC 0083 / IGC 2968;
RX   PubMed=15229592; DOI=10.1038/nature02579;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA   de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA   Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA   Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA   Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA   Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA   Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA   Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA   Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA   Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA   Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA   Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA   Weissenbach J., Wincker P., Souciet J.-L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(2004).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=D-glyceraldehyde 3-phosphate + NAD(+) + phosphate = (2R)-3-
CC         phospho-glyceroyl phosphate + H(+) + NADH; Xref=Rhea:RHEA:10300,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:57540,
CC         ChEBI:CHEBI:57604, ChEBI:CHEBI:57945, ChEBI:CHEBI:59776; EC=1.2.1.12;
CC         Evidence={ECO:0000255|PROSITE-ProRule:PRU10009};
CC   -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
CC       glyceraldehyde 3-phosphate: step 1/5.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the glyceraldehyde-3-phosphate dehydrogenase
CC       family. {ECO:0000305}.
DR   EMBL; CR382138; CAG88895.1; -; Genomic_DNA.
DR   RefSeq; XP_460571.1; XM_460571.1.
DR   SMR; Q6BMK0; -.
DR   STRING; 4959.XP_460571.1; -.
DR   PRIDE; Q6BMK0; -.
DR   EnsemblFungi; CAG88895; CAG88895; DEHA2F04796g.
DR   GeneID; 2903236; -.
DR   KEGG; dha:DEHA2F04796g; -.
DR   HOGENOM; HOG000071678; -.
DR   InParanoid; Q6BMK0; -.
DR   KO; K00134; -.
DR   OMA; NCVAPMA; -.
DR   OrthoDB; 945145at2759; -.
DR   UniPathway; UPA00109; UER00184.
DR   Proteomes; UP000000599; Chromosome F.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004365; F:glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity; IEA:UniProtKB-EC.
DR   GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR   GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR   GO; GO:0006006; P:glucose metabolic process; IEA:InterPro.
DR   GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-UniPathway.
DR   InterPro; IPR020831; GlycerAld/Erythrose_P_DH.
DR   InterPro; IPR020830; GlycerAld_3-P_DH_AS.
DR   InterPro; IPR020829; GlycerAld_3-P_DH_cat.
DR   InterPro; IPR020828; GlycerAld_3-P_DH_NAD(P)-bd.
DR   InterPro; IPR006424; Glyceraldehyde-3-P_DH_1.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   PANTHER; PTHR10836; PTHR10836; 1.
DR   Pfam; PF02800; Gp_dh_C; 1.
DR   Pfam; PF00044; Gp_dh_N; 1.
DR   PIRSF; PIRSF000149; GAP_DH; 1.
DR   PRINTS; PR00078; G3PDHDRGNASE.
DR   SMART; SM00846; Gp_dh_N; 1.
DR   SUPFAM; SSF51735; SSF51735; 1.
DR   TIGRFAMs; TIGR01534; GAPDH-I; 1.
DR   PROSITE; PS00071; GAPDH; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q6BMK0.
DR   SWISS-2DPAGE; Q6BMK0.
KW   Cytoplasm; Glycolysis; NAD; Oxidoreductase; Reference proteome.
FT   CHAIN           1..335
FT                   /note="Glyceraldehyde-3-phosphate dehydrogenase"
FT                   /id="PRO_0000145553"
FT   NP_BIND         12..13
FT                   /note="NAD"
FT                   /evidence="ECO:0000250"
FT   REGION          150..152
FT                   /note="Glyceraldehyde 3-phosphate binding"
FT                   /evidence="ECO:0000250"
FT   REGION          210..211
FT                   /note="Glyceraldehyde 3-phosphate binding"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        151
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10009"
FT   BINDING         34
FT                   /note="NAD"
FT                   /evidence="ECO:0000250"
FT   BINDING         79
FT                   /note="NAD; via carbonyl oxygen"
FT                   /evidence="ECO:0000250"
FT   BINDING         181
FT                   /note="Glyceraldehyde 3-phosphate"
FT                   /evidence="ECO:0000250"
FT   BINDING         233
FT                   /note="Glyceraldehyde 3-phosphate"
FT                   /evidence="ECO:0000250"
FT   BINDING         315
FT                   /note="NAD"
FT                   /evidence="ECO:0000250"
FT   SITE            178
FT                   /note="Activates thiol group during catalysis"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   335 AA;  35834 MW;  3EB63090B7B3A4D2 CRC64;
     MAITIGINGF GRIGRLVLRI ALQRSDIKVV AVNDPFIAPE YAAYMFKYDS THGRYKGEVT
     SKDDSLVIDG QSIKVFGEKD PASIPWGKAG VDYVIESTGV FTTTEGAQKH IDGGAKKVII
     TAPSSDAPMF VVGVNEQKYT PDLKIVSNAS CTTNCLAPLA KVINDKFGIE EGLMTTVHSI
     TATQKTVDGP SHKDWRGGRT ASGNIIPSST GAAKAVGKVI PELNGKLTGM SLRVPTVDVS
     VVDLTVRLKK SATYEEISEA IKAASNGELK GILGYTEDAV VSTDFLGSDY SSIFDQKAGI
     LLSPTFVKLI SWYDNEFGYS TRVVDLLEHV AKASN
//

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