G3P1_KLUMA
ID G3P1_KLUMA Reviewed; 329 AA.
AC P84998;
DT 17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 72.
DE RecName: Full=Glyceraldehyde-3-phosphate dehydrogenase 1;
DE Short=GAPDH 1;
DE EC=1.2.1.12;
GN Name=GAP1 {ECO:0000303|PubMed:7668042};
OS Kluyveromyces marxianus (Yeast) (Candida kefyr).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
OX NCBI_TaxID=4911;
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], CATALYTIC ACTIVITY, AND PATHWAY.
RC STRAIN=ATCC 10022 / CBS 6432 / NCTC 2303 / NRRL Y-665
RC {ECO:0000269|PubMed:7668042};
RX PubMed=7668042; DOI=10.1002/yea.320110804;
RA Fernandes P.A., Sena-Esteves M., Moradas-Ferreira P.;
RT "Characterization of the glyceraldehyde-3-phosphate dehydrogenase gene
RT family from Kluyveromyces marxianus -- polymerase chain reaction-single-
RT strand conformation polymorphism as a tool for the study of multigenic
RT families.";
RL Yeast 11:725-733(1995).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
RC STRAIN=ATCC 10022 / CBS 6432 / NCTC 2303 / NRRL Y-665;
RX PubMed=16963457; DOI=10.1074/jbc.m605267200;
RA Ferreira-da-Silva F., Pereira P.J.B., Gales L., Roessle M., Svergun D.I.,
RA Moradas-Ferreira P., Damas A.M.;
RT "The crystal and solution structures of glyceraldehyde-3-phosphate
RT dehydrogenase reveal different quaternary structures.";
RL J. Biol. Chem. 281:33433-33440(2006).
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 ECO:0000269|PubMed:7668042};
CC -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
CC glyceraldehyde 3-phosphate: step 1/5. {ECO:0000269|PubMed:7668042}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000250|UniProtKB:P22513}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P00359}.
CC -!- SIMILARITY: Belongs to the glyceraldehyde-3-phosphate dehydrogenase
CC family. {ECO:0000255}.
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DR PIR; S57279; S57279.
DR PDB; 2I5P; X-ray; 2.30 A; O/P=1-329.
DR PDBsum; 2I5P; -.
DR AlphaFoldDB; P84998; -.
DR SASBDB; P84998; -.
DR SMR; P84998; -.
DR PRIDE; P84998; -.
DR UniPathway; UPA00109; UER00184.
DR EvolutionaryTrace; P84998; -.
DR GO; GO:0005829; C:cytosol; IEA:UniProt.
DR GO; GO:0030312; C:external encapsulating structure; IEA:UniProt.
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 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Glycolysis; NAD; Oxidoreductase; Phosphoprotein.
FT CHAIN 1..329
FT /note="Glyceraldehyde-3-phosphate dehydrogenase 1"
FT /id="PRO_0000253990"
FT ACT_SITE 149
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:P22513,
FT ECO:0000255|PROSITE-ProRule:PRU10009"
FT BINDING 11..12
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P22513"
FT BINDING 33
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P22513"
FT BINDING 77
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P22513"
FT BINDING 148..150
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000250|UniProtKB:P22513"
FT BINDING 179
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000250|UniProtKB:P22513"
FT BINDING 208..209
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000250|UniProtKB:P22513"
FT BINDING 231
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000250|UniProtKB:P22513"
FT BINDING 313
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P22513"
FT SITE 176
FT /note="Activates thiol group during catalysis"
FT /evidence="ECO:0000250|UniProtKB:P22513"
FT MOD_RES 148
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P00359"
FT MOD_RES 177
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P00359"
FT MOD_RES 200
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P00359"
FT STRAND 2..7
FT /evidence="ECO:0007829|PDB:2I5P"
FT HELIX 11..20
FT /evidence="ECO:0007829|PDB:2I5P"
FT STRAND 26..32
FT /evidence="ECO:0007829|PDB:2I5P"
FT HELIX 38..46
FT /evidence="ECO:0007829|PDB:2I5P"
FT TURN 49..51
FT /evidence="ECO:0007829|PDB:2I5P"
FT STRAND 58..60
FT /evidence="ECO:0007829|PDB:2I5P"
FT STRAND 62..67
FT /evidence="ECO:0007829|PDB:2I5P"
FT STRAND 70..75
FT /evidence="ECO:0007829|PDB:2I5P"
FT HELIX 80..82
FT /evidence="ECO:0007829|PDB:2I5P"
FT TURN 85..89
FT /evidence="ECO:0007829|PDB:2I5P"
FT STRAND 91..95
FT /evidence="ECO:0007829|PDB:2I5P"
FT STRAND 97..100
FT /evidence="ECO:0007829|PDB:2I5P"
FT HELIX 103..111
FT /evidence="ECO:0007829|PDB:2I5P"
FT STRAND 115..121
FT /evidence="ECO:0007829|PDB:2I5P"
FT STRAND 124..126
FT /evidence="ECO:0007829|PDB:2I5P"
FT TURN 131..133
FT /evidence="ECO:0007829|PDB:2I5P"
FT HELIX 135..137
FT /evidence="ECO:0007829|PDB:2I5P"
FT STRAND 142..145
FT /evidence="ECO:0007829|PDB:2I5P"
FT HELIX 149..164
FT /evidence="ECO:0007829|PDB:2I5P"
FT STRAND 167..176
FT /evidence="ECO:0007829|PDB:2I5P"
FT STRAND 204..207
FT /evidence="ECO:0007829|PDB:2I5P"
FT TURN 210..213
FT /evidence="ECO:0007829|PDB:2I5P"
FT HELIX 214..217
FT /evidence="ECO:0007829|PDB:2I5P"
FT HELIX 219..221
FT /evidence="ECO:0007829|PDB:2I5P"
FT STRAND 224..231
FT /evidence="ECO:0007829|PDB:2I5P"
FT STRAND 236..248
FT /evidence="ECO:0007829|PDB:2I5P"
FT HELIX 252..264
FT /evidence="ECO:0007829|PDB:2I5P"
FT TURN 265..270
FT /evidence="ECO:0007829|PDB:2I5P"
FT STRAND 271..274
FT /evidence="ECO:0007829|PDB:2I5P"
FT HELIX 280..283
FT /evidence="ECO:0007829|PDB:2I5P"
FT STRAND 288..293
FT /evidence="ECO:0007829|PDB:2I5P"
FT TURN 294..296
FT /evidence="ECO:0007829|PDB:2I5P"
FT STRAND 298..301
FT /evidence="ECO:0007829|PDB:2I5P"
FT STRAND 304..314
FT /evidence="ECO:0007829|PDB:2I5P"
FT HELIX 315..328
FT /evidence="ECO:0007829|PDB:2I5P"
SQ SEQUENCE 329 AA; 35253 MW; 4C5C08D5C7858672 CRC64;
MVSIAINGFG RIGRLVLRIA LERKNIDVVA INDPFISVDY AAYMFKYDST HGKYKGEVSH
DGSNLIINGK KVAVFQEKDP ATLPWGKLGV DIAVDSTGVF KELDSAQKHI DAGAKKVVIT
APSKTAPMFV VGVNEDKYNG EKIVSNASCT TNCLAPIAKI INDEFGIEEG LMTTVHSITA
TQKTVDGPSH KDWRGGRTAS GNIIPSSTGA AKAVGKVLPE LQGKLTGMAF RVPTTDVSVV
DLTVKLVKAA TYDEIKAAVK KVSEGKLKDV VGYTEDAVVS SDFLGDTHST IFDAAAGIQL
SPKFVKLVAW YDNEYGYSTR VVDLVEHVA
