G3P1_YEAST
ID G3P1_YEAST Reviewed; 332 AA.
AC P00360; D6VWD1;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 213.
DE RecName: Full=Glyceraldehyde-3-phosphate dehydrogenase 1;
DE Short=GAPDH 1;
DE EC=1.2.1.12;
GN Name=TDH1; Synonyms=GPD1, SSS2; OrderedLocusNames=YJL052W; ORFNames=J1154;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=6833300; DOI=10.1016/s0021-9258(18)32570-5;
RA Holland J.P., Labieniec L., Swimmer C., Holland M.J.;
RT "Homologous nucleotide sequences at the 5' termini of messenger RNAs
RT synthesized from the yeast enolase and glyceraldehyde-3-phosphate
RT dehydrogenase gene families. The primary structure of a third yeast
RT glyceraldehyde-3-phosphate dehydrogenase gene.";
RL J. Biol. Chem. 258:5291-5299(1983).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8641269; DOI=10.1002/j.1460-2075.1996.tb00557.x;
RA Galibert F., Alexandraki D., Baur A., Boles E., Chalwatzis N., Chuat J.-C.,
RA Coster F., Cziepluch C., de Haan M., Domdey H., Durand P., Entian K.-D.,
RA Gatius M., Goffeau A., Grivell L.A., Hennemann A., Herbert C.J.,
RA Heumann K., Hilger F., Hollenberg C.P., Huang M.-E., Jacq C.,
RA Jauniaux J.-C., Katsoulou C., Kirchrath L., Kleine K., Kordes E.,
RA Koetter P., Liebl S., Louis E.J., Manus V., Mewes H.-W., Miosga T.,
RA Obermaier B., Perea J., Pohl T.M., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rasmussen S.W., Rose M., Rossau R.,
RA Schaaff-Gerstenschlaeger I., Smits P.H.M., Scarcez T., Soriano N.,
RA To Van D., Tzermia M., Van Broekhoven A., Vandenbol M., Wedler H.,
RA von Wettstein D., Wambutt R., Zagulski M., Zollner A., Karpfinger-Hartl L.;
RT "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome X.";
RL EMBO J. 15:2031-2049(1996).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [5]
RP PROTEIN SEQUENCE OF 64-70 AND 218-225.
RC STRAIN=ATCC 44827 / SKQ2N;
RX PubMed=9509572;
RX DOI=10.1002/(sici)1097-0061(199712)13:16<1519::aid-yea211>3.0.co;2-u;
RA Norbeck J., Blomberg A.;
RT "Two-dimensional electrophoretic separation of yeast proteins using a non-
RT linear wide range (pH 3-10) immobilized pH gradient in the first dimension;
RT reproducibility and evidence for isoelectric focusing of alkaline (pI > 7)
RT proteins.";
RL Yeast 13:1519-1534(1997).
RN [6]
RP PROTEIN SEQUENCE OF N-TERMINUS.
RX PubMed=10930071; DOI=10.1016/s0723-2020(00)80005-3;
RA Kadokura T., Ito T., Takano S., Nakazato A., Hara H., Watanabe S., Kudo T.,
RA Takeda M., Kaneko T.;
RT "Divergence of glyceraldehyde-3-phosphate dehydrogenase isozymes in
RT Saccharomyces cerevisiae complex.";
RL Syst. Appl. Microbiol. 23:198-205(2000).
RN [7]
RP SUBCELLULAR LOCATION.
RX PubMed=11502169; DOI=10.1021/bi010277r;
RA Grandier-Vazeille X., Bathany K., Chaignepain S., Camougrand N., Manon S.,
RA Schmitter J.-M.;
RT "Yeast mitochondrial dehydrogenases are associated in a supramolecular
RT complex.";
RL Biochemistry 40:9758-9769(2001).
RN [8]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
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.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11502169}.
CC -!- MISCELLANEOUS: There are three genes for G3PDH in yeast.
CC -!- MISCELLANEOUS: Present with 120000 molecules/cell in log phase SD
CC medium. {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the glyceraldehyde-3-phosphate dehydrogenase
CC family. {ECO:0000305}.
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DR EMBL; V01302; CAA24609.1; -; Genomic_DNA.
DR EMBL; Z49327; CAA89343.1; -; Genomic_DNA.
DR EMBL; AY693001; AAT93020.1; -; Genomic_DNA.
DR EMBL; BK006943; DAA08747.1; -; Genomic_DNA.
DR PIR; S56824; DEBYG3.
DR RefSeq; NP_012483.3; NM_001181485.3.
DR AlphaFoldDB; P00360; -.
DR SMR; P00360; -.
DR BioGRID; 33703; 108.
DR DIP; DIP-4304N; -.
DR IntAct; P00360; 67.
DR MINT; P00360; -.
DR STRING; 4932.YJL052W; -.
DR MoonDB; P00360; Curated.
DR iPTMnet; P00360; -.
DR SWISS-2DPAGE; P00360; -.
DR MaxQB; P00360; -.
DR PaxDb; P00360; -.
DR PRIDE; P00360; -.
DR TopDownProteomics; P00360; -.
DR EnsemblFungi; YJL052W_mRNA; YJL052W; YJL052W.
DR GeneID; 853395; -.
DR KEGG; sce:YJL052W; -.
DR SGD; S000003588; TDH1.
DR VEuPathDB; FungiDB:YJL052W; -.
DR eggNOG; KOG0657; Eukaryota.
DR GeneTree; ENSGT00940000153298; -.
DR HOGENOM; CLU_030140_0_3_1; -.
DR InParanoid; P00360; -.
DR OMA; HETYKGE; -.
DR BioCyc; YEAST:YJL052W-MON; -.
DR Reactome; R-SCE-70171; Glycolysis.
DR Reactome; R-SCE-70263; Gluconeogenesis.
DR SABIO-RK; P00360; -.
DR UniPathway; UPA00109; UER00184.
DR ChiTaRS; GPD1; yeast.
DR PRO; PR:P00360; -.
DR Proteomes; UP000002311; Chromosome X.
DR RNAct; P00360; protein.
DR GO; GO:0005829; C:cytosol; IDA:SGD.
DR GO; GO:0009277; C:fungal-type cell wall; IDA:SGD.
DR GO; GO:0005811; C:lipid droplet; IDA:SGD.
DR GO; GO:0005739; C:mitochondrion; IDA:SGD.
DR GO; GO:0005886; C:plasma membrane; HDA:SGD.
DR GO; GO:0004365; F:glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity; IDA:SGD.
DR GO; GO:1904408; F:melatonin binding; IDA:SGD.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR GO; GO:0006094; P:gluconeogenesis; IEP:SGD.
DR GO; GO:0006096; P:glycolytic process; IEP:SGD.
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 1: Evidence at protein level;
KW Cytoplasm; Direct protein sequencing; Glycolysis; NAD; Oxidoreductase;
KW Reference proteome.
FT CHAIN 1..332
FT /note="Glyceraldehyde-3-phosphate dehydrogenase 1"
FT /id="PRO_0000145589"
FT ACT_SITE 150
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10009"
FT BINDING 11..12
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 33
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 78
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 149..151
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000250"
FT BINDING 180
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000250"
FT BINDING 209..210
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000250"
FT BINDING 232
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000250"
FT BINDING 314
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT SITE 177
FT /note="Activates thiol group during catalysis"
FT /evidence="ECO:0000250"
FT CONFLICT 248
FT /note="E -> A (in Ref. 1; CAA24609)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 332 AA; 35750 MW; 4C116C86EAF3DB70 CRC64;
MIRIAINGFG RIGRLVLRLA LQRKDIEVVA VNDPFISNDY AAYMVKYDST HGRYKGTVSH
DDKHIIIDGV KIATYQERDP ANLPWGSLKI DVAVDSTGVF KELDTAQKHI DAGAKKVVIT
APSSSAPMFV VGVNHTKYTP DKKIVSNASC TTNCLAPLAK VINDAFGIEE GLMTTVHSMT
ATQKTVDGPS HKDWRGGRTA SGNIIPSSTG AAKAVGKVLP ELQGKLTGMA FRVPTVDVSV
VDLTVKLEKE ATYDQIKKAV KAAAEGPMKG VLGYTEDAVV SSDFLGDTHA SIFDASAGIQ
LSPKFVKLIS WYDNEYGYSA RVVDLIEYVA KA
