G3P2_YEAST
ID G3P2_YEAST Reviewed; 332 AA.
AC P00358; D6VWI4;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 217.
DE RecName: Full=Glyceraldehyde-3-phosphate dehydrogenase 2;
DE Short=GAPDH 2;
DE EC=1.2.1.12;
GN Name=TDH2; Synonyms=GPD2; OrderedLocusNames=YJR009C; ORFNames=J1433;
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].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=1789010; DOI=10.1002/yea.320070814;
RA Mountain H.A., Korch C.;
RT "TDH2 is linked to MET3 on chromosome X of Saccharomyces cerevisiae.";
RL Yeast 7:873-880(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=6244283; DOI=10.1016/s0021-9258(19)85934-3;
RA Holland J.P., Holland M.J.;
RT "Structural comparison of two nontandemly repeated yeast glyceraldehyde-3-
RT phosphate dehydrogenase genes.";
RL J. Biol. Chem. 255:2596-2605(1980).
RN [3]
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 [4]
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 [5]
RP PROTEIN SEQUENCE OF 24-37; 72-77; 81-86; 199-213; 226-232 AND 322-331.
RC STRAIN=ATCC 38531 / Y41;
RX PubMed=7737086; DOI=10.1002/elps.1150160124;
RA Norbeck J., Blomberg A.;
RT "Gene linkage of two-dimensional polyacrylamide gel electrophoresis
RT resolved proteins from isogene families in Saccharomyces cerevisiae by
RT microsequencing of in-gel trypsin generated peptides.";
RL Electrophoresis 16:149-156(1995).
RN [6]
RP PROTEIN SEQUENCE OF 2-13.
RC STRAIN=ATCC 26786 / X2180-1A;
RA Frutiger S., Hughes G.J., Sanchez J.-C., Hochstrasser D.F.;
RL Submitted (FEB-1996) to UniProtKB.
RN [7]
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).
RN [8]
RP UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-63, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22106047; DOI=10.1002/pmic.201100166;
RA Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.;
RT "Sites of ubiquitin attachment in Saccharomyces cerevisiae.";
RL Proteomics 12:236-240(2012).
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 -!- INTERACTION:
CC P00358; P0CG63: UBI4; NbExp=2; IntAct=EBI-7212, EBI-7000452;
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- MISCELLANEOUS: There are three genes for G3PDH in yeast.
CC -!- MISCELLANEOUS: Present with 121000 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; X60157; CAA42725.1; -; Genomic_DNA.
DR EMBL; V01301; CAA24608.1; ALT_SEQ; Genomic_DNA.
DR EMBL; X87611; CAA60931.1; -; Genomic_DNA.
DR EMBL; Z49509; CAA89531.1; -; Genomic_DNA.
DR EMBL; BK006943; DAA08800.1; -; Genomic_DNA.
DR PIR; S57024; DEBYG1.
DR RefSeq; NP_012542.1; NM_001181666.1.
DR AlphaFoldDB; P00358; -.
DR SMR; P00358; -.
DR BioGRID; 33765; 137.
DR DIP; DIP-1951N; -.
DR IntAct; P00358; 61.
DR MINT; P00358; -.
DR STRING; 4932.YJR009C; -.
DR MoonDB; P00358; Curated.
DR CarbonylDB; P00358; -.
DR iPTMnet; P00358; -.
DR SWISS-2DPAGE; P00358; -.
DR MaxQB; P00358; -.
DR PaxDb; P00358; -.
DR PRIDE; P00358; -.
DR TopDownProteomics; P00358; -.
DR EnsemblFungi; YJR009C_mRNA; YJR009C; YJR009C.
DR GeneID; 853465; -.
DR KEGG; sce:YJR009C; -.
DR SGD; S000003769; TDH2.
DR VEuPathDB; FungiDB:YJR009C; -.
DR eggNOG; KOG0657; Eukaryota.
DR GeneTree; ENSGT00940000153298; -.
DR HOGENOM; CLU_030140_0_3_1; -.
DR InParanoid; P00358; -.
DR OMA; NAKVLAW; -.
DR BioCyc; YEAST:YJR009C-MON; -.
DR Reactome; R-SCE-70171; Glycolysis.
DR Reactome; R-SCE-70263; Gluconeogenesis.
DR SABIO-RK; P00358; -.
DR UniPathway; UPA00109; UER00184.
DR PRO; PR:P00358; -.
DR Proteomes; UP000002311; Chromosome X.
DR RNAct; P00358; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
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:0005634; C:nucleus; HDA: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:1990841; F:promoter-specific chromatin binding; IDA:SGD.
DR GO; GO:0006915; P:apoptotic process; IMP:SGD.
DR GO; GO:0006094; P:gluconeogenesis; IEP:SGD.
DR GO; GO:0006096; P:glycolytic process; IEP:SGD.
DR GO; GO:0072593; P:reactive oxygen species metabolic process; IMP: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; Isopeptide bond; NAD;
KW Oxidoreductase; Phosphoprotein; Reference proteome; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|Ref.6"
FT CHAIN 2..332
FT /note="Glyceraldehyde-3-phosphate dehydrogenase 2"
FT /id="PRO_0000145590"
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 MOD_RES 302
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P00359"
FT CROSSLNK 46
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:P00359"
FT CROSSLNK 63
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0007744|PubMed:22106047"
FT CONFLICT 77
FT /note="E -> A (in Ref. 5; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 332 AA; 35847 MW; 9A99DCB26672541E CRC64;
MVRVAINGFG RIGRLVMRIA LQRKNVEVVA LNDPFISNDY SAYMFKYDST HGRYAGEVSH
DDKHIIVDGH KIATFQERDP ANLPWASLNI DIAIDSTGVF KELDTAQKHI DAGAKKVVIT
APSSTAPMFV MGVNEEKYTS DLKIVSNASC TTNCLAPLAK VINDAFGIEE GLMTTVHSMT
ATQKTVDGPS HKDWRGGRTA SGNIIPSSTG AAKAVGKVLP ELQGKLTGMA FRVPTVDVSV
VDLTVKLNKE TTYDEIKKVV KAAAEGKLKG VLGYTEDAVV SSDFLGDSNS SIFDAAAGIQ
LSPKFVKLVS WYDNEYGYST RVVDLVEHVA KA
