ID   G3P3_YEAST              Reviewed;         332 AA.
AC   P00359; D6VUX4; Q6Q5P9;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   27-MAR-2024, entry version 230.
DE   RecName: Full=Glyceraldehyde-3-phosphate dehydrogenase 3 {ECO:0000303|PubMed:2999100};
DE            Short=GAPDH 3 {ECO:0000303|PubMed:2999100};
DE            EC=1.2.1.12 {ECO:0000269|PubMed:3905788};
DE   AltName: Full=Triose-phosphate dehydrogenase 1 {ECO:0000303|PubMed:2999100};
GN   Name=TDH3 {ECO:0000303|PubMed:2999100}; Synonyms=GPD3;
GN   OrderedLocusNames=YGR192C; ORFNames=G7576;
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=385592; DOI=10.1016/s0021-9258(19)83593-7;
RA   Holland J.P., Holland M.J.;
RT   "The primary structure of a glyceraldehyde-3-phosphate dehydrogenase gene
RT   from Saccharomyces cerevisiae.";
RL   J. Biol. Chem. 254:9839-9845(1979).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=7645350; DOI=10.1002/yea.320110609;
RA   Arroyo J., Garcia-Gonzalez M., Garcia-Saez M.I., Sanchez M., Nombela C.;
RT   "The complete sequence of a 9037 bp DNA fragment of the right arm of
RT   Saccharomyces cerevisiae chromosome VII.";
RL   Yeast 11:587-591(1995).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169869;
RA   Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J.,
RA   Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M.,
RA   Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L.,
RA   Coblenz A., Coglievina M., Coissac E., Defoor E., Del Bino S., Delius H.,
RA   Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P.,
RA   Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M.,
RA   Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A.,
RA   Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K.,
RA   Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P.,
RA   Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E.,
RA   Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K.,
RA   Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A.,
RA   Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S.,
RA   Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M.,
RA   Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C.,
RA   Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M.,
RA   Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M.,
RA   Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y.,
RA   Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L.,
RA   Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D.,
RA   Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F.,
RA   Zaccaria P., Zimmermann M., Zollner A., Kleine K.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII.";
RL   Nature 387:81-84(1997).
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   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   [6]
RP   PARTIAL PROTEIN SEQUENCE OF 2-332, AND CLEAVAGE OF INITIATOR METHIONINE.
RX   PubMed=11946592; DOI=10.1016/0014-5793(72)80040-1;
RA   Jones G.M., Harris J.I.;
RT   "Glyceraldehyde 3-phosphate dehydrogenase: Amino acid sequence of enzyme
RT   from baker's yeast.";
RL   FEBS Lett. 22:185-189(1972).
RN   [7]
RP   PROTEIN SEQUENCE OF 47-58.
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=7895733; DOI=10.1002/elps.11501501210;
RA   Garrels J.I., Futcher B., Kobayashi R., Latter G.I., Schwender B.,
RA   Volpe T., Warner J.R., McLaughlin C.S.;
RT   "Protein identifications for a Saccharomyces cerevisiae protein database.";
RL   Electrophoresis 15:1466-1486(1994).
RN   [8]
RP   PARTIAL PROTEIN SEQUENCE.
RC   STRAIN=ATCC 38531 / Y41, and ATCC 44827 / SKQ2N;
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   [9]
RP   FUNCTION, AND CATALYTIC ACTIVITY.
RX   PubMed=13174589; DOI=10.1016/s0021-9258(18)65605-4;
RA   Rafter G.W., Chaykin S., Krebs E.G.;
RT   "The action of glyceraldehyde-3-phosphate dehydrogenase on reduced
RT   diphosphopyridine nucleotide.";
RL   J. Biol. Chem. 208:799-811(1954).
RN   [10]
RP   FUNCTION, AND CATALYTIC ACTIVITY.
RX   PubMed=4371815; DOI=10.1021/bi00720a002;
RA   Oppenheimer N.J., Kaplan N.O.;
RT   "Glyceraldehyde-3-phosphate dehydrogenase catalyzed hydration of the 5-6
RT   double bond of reduced beta-nicotinamide adenine dinucleotide (betaNADH).
RT   Formation of beta-6-hydroxy-1,4,5,6-tetrahydronicotinamide adenine
RT   dinucleotide.";
RL   Biochemistry 13:4685-4694(1974).
RN   [11]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=2999100; DOI=10.1016/s0021-9258(18)95695-4;
RA   McAlister L., Holland M.J.;
RT   "Isolation and characterization of yeast strains carrying mutations in the
RT   glyceraldehyde-3-phosphate dehydrogenase genes.";
RL   J. Biol. Chem. 260:15013-15018(1985).
RN   [12]
RP   FUNCTION, SUBUNIT, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX   PubMed=3905788; DOI=10.1016/s0021-9258(18)95696-6;
RA   McAlister L., Holland M.J.;
RT   "Differential expression of the three yeast glyceraldehyde-3-phosphate
RT   dehydrogenase genes.";
RL   J. Biol. Chem. 260:15019-15027(1985).
RN   [13]
RP   INDUCTION.
RX   PubMed=7875559; DOI=10.1111/j.1574-6968.1995.tb07348.x;
RA   Boucherie H., Bataille N., Fitch I.T., Perrot M., Tuite M.F.;
RT   "Differential synthesis of glyceraldehyde-3-phosphate dehydrogenase
RT   polypeptides in stressed yeast cells.";
RL   FEMS Microbiol. Lett. 125:127-133(1995).
RN   [14]
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   [15]
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   [16]
RP   SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
RP   SPECTROMETRY.
RX   PubMed=16823961; DOI=10.1021/pr050477f;
RA   Reinders J., Zahedi R.P., Pfanner N., Meisinger C., Sickmann A.;
RT   "Toward the complete yeast mitochondrial proteome: multidimensional
RT   separation techniques for mitochondrial proteomics.";
RL   J. Proteome Res. 5:1543-1554(2006).
RN   [17]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=17287358; DOI=10.1073/pnas.0607084104;
RA   Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,
RA   Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
RT   "Analysis of phosphorylation sites on proteins from Saccharomyces
RT   cerevisiae by electron transfer dissociation (ETD) mass spectrometry.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
RN   [18]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-302, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA   Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT   "A multidimensional chromatography technology for in-depth phosphoproteome
RT   analysis.";
RL   Mol. Cell. Proteomics 7:1389-1396(2008).
RN   [19]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19779198; DOI=10.1126/science.1172867;
RA   Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT   "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT   into evolution.";
RL   Science 325:1682-1686(2009).
RN   [20]
RP   UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-46 AND LYS-63, AND
RP   IDENTIFICATION BY MASS 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).
RN   [21] {ECO:0007744|PDB:3PYM}
RP   X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) IN COMPLEX WITH NAD(+).
RA   Garcia-Saez I., Kozielski F., Job D., Boscheron C.;
RT   "Structure of GAPDH 3 from S.cerevisiae at 2.0 A resolution.";
RL   Submitted (DEC-2010) to the PDB data bank.
RN   [22] {ECO:0007744|PDB:4IQ8}
RP   X-RAY CRYSTALLOGRAPHY (2.49 ANGSTROMS), AND SUBUNIT.
RX   PubMed=22869137; DOI=10.1107/s1744309112028989;
RA   Liu Q., Wang H., Liu H., Teng M., Li X.;
RT   "Preliminary crystallographic analysis of glyceraldehyde-3-phosphate
RT   dehydrogenase 3 from Saccharomyces cerevisiae.";
RL   Acta Crystallogr. F 68:978-980(2012).
CC   -!- FUNCTION: Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) involved in
CC       glycolysis and gluconeogenesis (PubMed:2999100). Catalyzes the reaction
CC       of glyceraldehyde-3-phosphate to 1,3 bis-phosphoglycerate
CC       (PubMed:3905788). The contribution of the TDH1, TDH2, and TDH3 to the
CC       total glyceraldehyde-3-phosphate dehydrogenase activity is 10-15, 25-
CC       30, and 50-60%, respectively (PubMed:3905788).
CC       {ECO:0000269|PubMed:2999100, ECO:0000269|PubMed:3905788}.
CC   -!- FUNCTION: As a side activity, catalyzes the hydration of the
CC       nicotinamide ring of NADH or NADPH at the C6 position to give the
CC       corresponding hydrates, NADHX and NADPHX, which exist as R and S
CC       epimers, that cannot act as electron donors or acceptors and inhibit
CC       several dehydrogenases, making them toxic.
CC       {ECO:0000269|PubMed:13174589, ECO:0000269|PubMed:4371815}.
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:0000269|PubMed:3905788};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10301;
CC         Evidence={ECO:0000269|PubMed:3905788};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + NADH = (6R)-NADHX; Xref=Rhea:RHEA:57360,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:57945, ChEBI:CHEBI:64075;
CC         Evidence={ECO:0000269|PubMed:13174589, ECO:0000269|PubMed:4371815};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:57361;
CC         Evidence={ECO:0000269|PubMed:13174589, ECO:0000269|PubMed:4371815};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + NADH = (6S)-NADHX; Xref=Rhea:RHEA:57364,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:57945, ChEBI:CHEBI:64074;
CC         Evidence={ECO:0000269|PubMed:13174589, ECO:0000269|PubMed:4371815};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:57365;
CC         Evidence={ECO:0000269|PubMed:13174589, ECO:0000269|PubMed:4371815};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + NADPH = (6R)-NADPHX; Xref=Rhea:RHEA:57368,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:57783, ChEBI:CHEBI:64077;
CC         Evidence={ECO:0000269|PubMed:13174589, ECO:0000269|PubMed:4371815};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:57369;
CC         Evidence={ECO:0000269|PubMed:13174589, ECO:0000269|PubMed:4371815};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + NADPH = (6S)-NADPHX; Xref=Rhea:RHEA:57372,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:57783, ChEBI:CHEBI:64076;
CC         Evidence={ECO:0000269|PubMed:13174589, ECO:0000269|PubMed:4371815};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:57373;
CC         Evidence={ECO:0000269|PubMed:13174589, ECO:0000269|PubMed:4371815};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=0.32 uM for NAD(+) {ECO:0000303|PubMed:3905788};
CC   -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
CC       glyceraldehyde 3-phosphate: step 1/5. {ECO:0000269|PubMed:3905788}.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:22869137,
CC       ECO:0000269|PubMed:3905788}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11502169}.
CC       Mitochondrion {ECO:0000269|PubMed:16823961}.
CC   -!- INDUCTION: Expression is not affected by a heat shock.
CC       {ECO:0000269|PubMed:7875559}.
CC   -!- DISRUPTION PHENOTYPE: Does not affect growth when ethanol is used as
CC       carbon source but reduces growth when glucose is used as carbon source.
CC       {ECO:0000269|PubMed:2999100}.
CC   -!- MISCELLANEOUS: Present with 169000 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; V01300; CAA24607.1; -; Genomic_DNA.
DR   EMBL; J01324; AAA88714.1; -; Genomic_DNA.
DR   EMBL; X82408; CAA57803.1; -; Genomic_DNA.
DR   EMBL; Z72977; CAA97218.1; -; Genomic_DNA.
DR   EMBL; AY557831; AAS56157.1; -; Genomic_DNA.
DR   EMBL; BK006941; DAA08285.1; -; Genomic_DNA.
DR   PIR; S55870; DEBYG2.
DR   RefSeq; NP_011708.3; NM_001181321.3.
DR   PDB; 3PYM; X-ray; 2.00 A; A/B=1-332.
DR   PDB; 4IQ8; X-ray; 2.49 A; A=1-332.
DR   PDBsum; 3PYM; -.
DR   PDBsum; 4IQ8; -.
DR   AlphaFoldDB; P00359; -.
DR   SMR; P00359; -.
DR   BioGRID; 33445; 326.
DR   DIP; DIP-4309N; -.
DR   IntAct; P00359; 102.
DR   MINT; P00359; -.
DR   STRING; 4932.YGR192C; -.
DR   MoonDB; P00359; Curated.
DR   MoonProt; P00359; -.
DR   CarbonylDB; P00359; -.
DR   iPTMnet; P00359; -.
DR   MaxQB; P00359; -.
DR   PaxDb; 4932-YGR192C; -.
DR   PeptideAtlas; P00359; -.
DR   TopDownProteomics; P00359; -.
DR   EnsemblFungi; YGR192C_mRNA; YGR192C; YGR192C.
DR   GeneID; 853106; -.
DR   KEGG; sce:YGR192C; -.
DR   AGR; SGD:S000003424; -.
DR   SGD; S000003424; TDH3.
DR   VEuPathDB; FungiDB:YGR192C; -.
DR   eggNOG; KOG0657; Eukaryota.
DR   GeneTree; ENSGT00940000153298; -.
DR   HOGENOM; CLU_030140_0_3_1; -.
DR   InParanoid; P00359; -.
DR   OMA; YGYTCNM; -.
DR   OrthoDB; 275384at2759; -.
DR   BioCyc; YEAST:YGR192C-MONOMER; -.
DR   BRENDA; 1.2.1.12; 984.
DR   Reactome; R-SCE-70171; Glycolysis.
DR   Reactome; R-SCE-70263; Gluconeogenesis.
DR   SABIO-RK; P00359; -.
DR   UniPathway; UPA00109; UER00184.
DR   BioGRID-ORCS; 853106; 2 hits in 10 CRISPR screens.
DR   PRO; PR:P00359; -.
DR   Proteomes; UP000002311; Chromosome VII.
DR   RNAct; P00359; 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:0003723; F:RNA 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:0015886; P:heme transport; IMP:SGD.
DR   GO; GO:0072593; P:reactive oxygen species metabolic process; IMP:SGD.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
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   NCBIfam; TIGR01534; GAPDH-I; 1.
DR   PANTHER; PTHR10836; GLYCERALDEHYDE 3-PHOSPHATE DEHYDROGENASE; 1.
DR   PANTHER; PTHR10836:SF76; GLYCERALDEHYDE-3-PHOSPHATE DEHYDROGENASE-RELATED; 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; SSF55347; Glyceraldehyde-3-phosphate dehydrogenase-like, C-terminal domain; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR   PROSITE; PS00071; GAPDH; 1.
DR   COMPLUYEAST-2DPAGE; P00359; -.
DR   SWISS-2DPAGE; P00359; -.
PE   1: Evidence at protein level;
KW   3D-structure; Cytoplasm; Direct protein sequencing; Glycolysis;
KW   Isopeptide bond; Mitochondrion; NAD; Oxidoreductase; Phosphoprotein;
KW   Reference proteome; Ubl conjugation.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:11946592"
FT   CHAIN           2..332
FT                   /note="Glyceraldehyde-3-phosphate dehydrogenase 3"
FT                   /id="PRO_0000145591"
FT   ACT_SITE        150
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10009"
FT   BINDING         11
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0007744|PDB:3PYM"
FT   BINDING         12
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0007744|PDB:3PYM"
FT   BINDING         33
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0007744|PDB:3PYM"
FT   BINDING         120
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0007744|PDB:3PYM"
FT   BINDING         149..151
FT                   /ligand="D-glyceraldehyde 3-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:59776"
FT                   /evidence="ECO:0000250|UniProtKB:P22513"
FT   BINDING         180
FT                   /ligand="D-glyceraldehyde 3-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:59776"
FT                   /evidence="ECO:0000250|UniProtKB:P22513"
FT   BINDING         209..210
FT                   /ligand="D-glyceraldehyde 3-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:59776"
FT                   /evidence="ECO:0000250|UniProtKB:P22513"
FT   BINDING         232
FT                   /ligand="D-glyceraldehyde 3-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:59776"
FT                   /evidence="ECO:0000250|UniProtKB:P22513"
FT   BINDING         314
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0007744|PDB:3PYM"
FT   BINDING         318
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0007744|PDB:3PYM"
FT   SITE            177
FT                   /note="Activates thiol group during catalysis"
FT                   /evidence="ECO:0000250|UniProtKB:P04406"
FT   MOD_RES         302
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18407956"
FT   CROSSLNK        46
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin)"
FT                   /evidence="ECO:0007744|PubMed:22106047"
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        136
FT                   /note="E -> V (in Ref. 1; CAA24607/AAA88714)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        248
FT                   /note="N -> D (in Ref. 1; CAA24607/AAA88714)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        287
FT                   /note="D -> G (in Ref. 5; AAS56157)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        329
FT                   /note="V -> I (in Ref. 1; CAA24607/AAA88714)"
FT                   /evidence="ECO:0000305"
FT   STRAND          3..7
FT                   /evidence="ECO:0007829|PDB:3PYM"
FT   HELIX           11..22
FT                   /evidence="ECO:0007829|PDB:3PYM"
FT   STRAND          27..32
FT                   /evidence="ECO:0007829|PDB:3PYM"
FT   HELIX           38..46
FT                   /evidence="ECO:0007829|PDB:3PYM"
FT   TURN            49..51
FT                   /evidence="ECO:0007829|PDB:3PYM"
FT   STRAND          58..60
FT                   /evidence="ECO:0007829|PDB:3PYM"
FT   STRAND          62..67
FT                   /evidence="ECO:0007829|PDB:3PYM"
FT   STRAND          70..75
FT                   /evidence="ECO:0007829|PDB:3PYM"
FT   HELIX           80..82
FT                   /evidence="ECO:0007829|PDB:3PYM"
FT   TURN            85..89
FT                   /evidence="ECO:0007829|PDB:3PYM"
FT   STRAND          91..95
FT                   /evidence="ECO:0007829|PDB:3PYM"
FT   STRAND          97..100
FT                   /evidence="ECO:0007829|PDB:3PYM"
FT   HELIX           103..111
FT                   /evidence="ECO:0007829|PDB:3PYM"
FT   STRAND          115..121
FT                   /evidence="ECO:0007829|PDB:3PYM"
FT   STRAND          124..126
FT                   /evidence="ECO:0007829|PDB:3PYM"
FT   TURN            131..133
FT                   /evidence="ECO:0007829|PDB:3PYM"
FT   HELIX           135..137
FT                   /evidence="ECO:0007829|PDB:3PYM"
FT   STRAND          144..146
FT                   /evidence="ECO:0007829|PDB:3PYM"
FT   HELIX           150..166
FT                   /evidence="ECO:0007829|PDB:3PYM"
FT   STRAND          168..178
FT                   /evidence="ECO:0007829|PDB:3PYM"
FT   STRAND          183..187
FT                   /evidence="ECO:0007829|PDB:3PYM"
FT   HELIX           195..197
FT                   /evidence="ECO:0007829|PDB:3PYM"
FT   HELIX           200..202
FT                   /evidence="ECO:0007829|PDB:3PYM"
FT   STRAND          205..208
FT                   /evidence="ECO:0007829|PDB:3PYM"
FT   HELIX           211..218
FT                   /evidence="ECO:0007829|PDB:3PYM"
FT   HELIX           220..222
FT                   /evidence="ECO:0007829|PDB:3PYM"
FT   STRAND          225..234
FT                   /evidence="ECO:0007829|PDB:3PYM"
FT   STRAND          239..249
FT                   /evidence="ECO:0007829|PDB:3PYM"
FT   HELIX           253..265
FT                   /evidence="ECO:0007829|PDB:3PYM"
FT   TURN            266..271
FT                   /evidence="ECO:0007829|PDB:3PYM"
FT   STRAND          272..275
FT                   /evidence="ECO:0007829|PDB:3PYM"
FT   HELIX           281..284
FT                   /evidence="ECO:0007829|PDB:3PYM"
FT   STRAND          290..294
FT                   /evidence="ECO:0007829|PDB:3PYM"
FT   HELIX           295..297
FT                   /evidence="ECO:0007829|PDB:3PYM"
FT   STRAND          299..302
FT                   /evidence="ECO:0007829|PDB:3PYM"
FT   STRAND          305..312
FT                   /evidence="ECO:0007829|PDB:3PYM"
FT   HELIX           316..331
FT                   /evidence="ECO:0007829|PDB:3PYM"
SQ   SEQUENCE   332 AA;  35747 MW;  6CFFFEE7061BC36F CRC64;
     MVRVAINGFG RIGRLVMRIA LSRPNVEVVA LNDPFITNDY AAYMFKYDST HGRYAGEVSH
     DDKHIIVDGK KIATYQERDP ANLPWGSSNV DIAIDSTGVF KELDTAQKHI DAGAKKVVIT
     APSSTAPMFV MGVNEEKYTS DLKIVSNASC TTNCLAPLAK VINDAFGIEE GLMTTVHSLT
     ATQKTVDGPS HKDWRGGRTA SGNIIPSSTG AAKAVGKVLP ELQGKLTGMA FRVPTVDVSV
     VDLTVKLNKE TTYDEIKKVV KAAAEGKLKG VLGYTEDAVV SSDFLGDSHS SIFDASAGIQ
     LSPKFVKLVS WYDNEYGYST RVVDLVEHVA KA
//