G3P_METFE
ID G3P_METFE Reviewed; 337 AA.
AC P10618;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1989, sequence version 1.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Glyceraldehyde-3-phosphate dehydrogenase;
DE Short=GAPDH;
DE EC=1.2.1.59;
DE AltName: Full=NAD(P)-dependent glyceraldehyde-3-phosphate dehydrogenase;
GN Name=gap;
OS Methanothermus fervidus.
OC Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC Methanobacteriales; Methanothermaceae; Methanothermus.
OX NCBI_TaxID=2180;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2841192; DOI=10.1016/0378-1119(88)90334-4;
RA Fabry S., Hensel R.;
RT "Primary structure of glyceraldehyde-3-phosphate dehydrogenase deduced from
RT the nucleotide sequence of the thermophilic archaebacterium Methanothermus
RT fervidus.";
RL Gene 64:189-197(1988).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) IN COMPLEX WITH NADP, AND SUBUNIT.
RX PubMed=10715215; DOI=10.1006/jmbi.2000.3565;
RA Charron C., Talfournier F., Isupov M.N., Littlechild J.A., Branlant G.,
RA Vitoux B., Aubry A.;
RT "The crystal structure of D-glyceraldehyde-3-phosphate dehydrogenase from
RT the hyperthermophilic archaeon Methanothermus fervidus in the presence of
RT NADP(+) at 2.1 A resolution.";
RL J. Mol. Biol. 297:481-500(2000).
CC -!- FUNCTION: Exhibits a dual-cofactor specificity, with a marked
CC preference for NADP(+) over NAD(+).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-glyceraldehyde 3-phosphate + NADP(+) + phosphate = (2R)-3-
CC phospho-glyceroyl phosphate + H(+) + NADPH; Xref=Rhea:RHEA:10296,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:57604,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:59776; EC=1.2.1.59;
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=1.2.1.59;
CC -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
CC glyceraldehyde 3-phosphate: step 1/5.
CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:10715215}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- SIMILARITY: Belongs to the glyceraldehyde-3-phosphate dehydrogenase
CC family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; M19980; AAA88227.1; -; Genomic_DNA.
DR PIR; JT0286; JT0286.
DR RefSeq; WP_013413357.1; NC_014658.1.
DR PDB; 1CF2; X-ray; 2.10 A; O/P/Q/R=1-337.
DR PDBsum; 1CF2; -.
DR AlphaFoldDB; P10618; -.
DR SMR; P10618; -.
DR GeneID; 9961991; -.
DR OMA; NAIVPNP; -.
DR SABIO-RK; P10618; -.
DR UniPathway; UPA00109; UER00184.
DR EvolutionaryTrace; P10618; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0008839; F:4-hydroxy-tetrahydrodipicolinate reductase; IEA:InterPro.
DR GO; GO:0004365; F:glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity; IEA:UniProtKB-UniRule.
DR GO; GO:0047100; F:glyceraldehyde-3-phosphate dehydrogenase (NADP+) (phosphorylating) activity; IMP:CACAO.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-UniRule.
DR GO; GO:0009089; P:lysine biosynthetic process via diaminopimelate; IEA:InterPro.
DR HAMAP; MF_00559; G3P_dehdrog_arch; 1.
DR InterPro; IPR000846; DapB_N.
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; IPR006436; Glyceraldehyde-3-P_DH_2_arc.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR Pfam; PF01113; DapB_N; 1.
DR Pfam; PF02800; Gp_dh_C; 1.
DR PIRSF; PIRSF000149; GAP_DH; 1.
DR SMART; SM00846; Gp_dh_N; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
DR TIGRFAMs; TIGR01546; GAPDH-II_archae; 1.
DR PROSITE; PS00071; GAPDH; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Glycolysis; NAD; NADP; Oxidoreductase.
FT CHAIN 1..337
FT /note="Glyceraldehyde-3-phosphate dehydrogenase"
FT /id="PRO_0000145722"
FT ACT_SITE 140
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT BINDING 11..12
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:10715215"
FT BINDING 34..35
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:10715215"
FT BINDING 110
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:10715215"
FT BINDING 139..141
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000250"
FT BINDING 171
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:10715215"
FT BINDING 194..195
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000250"
FT BINDING 300
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT STRAND 2..7
FT /evidence="ECO:0007829|PDB:1CF2"
FT HELIX 13..21
FT /evidence="ECO:0007829|PDB:1CF2"
FT STRAND 23..35
FT /evidence="ECO:0007829|PDB:1CF2"
FT HELIX 38..45
FT /evidence="ECO:0007829|PDB:1CF2"
FT STRAND 50..54
FT /evidence="ECO:0007829|PDB:1CF2"
FT HELIX 55..57
FT /evidence="ECO:0007829|PDB:1CF2"
FT HELIX 58..63
FT /evidence="ECO:0007829|PDB:1CF2"
FT HELIX 72..77
FT /evidence="ECO:0007829|PDB:1CF2"
FT STRAND 80..84
FT /evidence="ECO:0007829|PDB:1CF2"
FT HELIX 90..101
FT /evidence="ECO:0007829|PDB:1CF2"
FT STRAND 105..107
FT /evidence="ECO:0007829|PDB:1CF2"
FT HELIX 113..116
FT /evidence="ECO:0007829|PDB:1CF2"
FT HELIX 122..125
FT /evidence="ECO:0007829|PDB:1CF2"
FT HELIX 126..129
FT /evidence="ECO:0007829|PDB:1CF2"
FT STRAND 133..137
FT /evidence="ECO:0007829|PDB:1CF2"
FT HELIX 140..156
FT /evidence="ECO:0007829|PDB:1CF2"
FT STRAND 158..170
FT /evidence="ECO:0007829|PDB:1CF2"
FT STRAND 184..191
FT /evidence="ECO:0007829|PDB:1CF2"
FT HELIX 194..199
FT /evidence="ECO:0007829|PDB:1CF2"
FT STRAND 206..214
FT /evidence="ECO:0007829|PDB:1CF2"
FT STRAND 219..229
FT /evidence="ECO:0007829|PDB:1CF2"
FT HELIX 233..242
FT /evidence="ECO:0007829|PDB:1CF2"
FT STRAND 246..249
FT /evidence="ECO:0007829|PDB:1CF2"
FT TURN 251..254
FT /evidence="ECO:0007829|PDB:1CF2"
FT HELIX 258..268
FT /evidence="ECO:0007829|PDB:1CF2"
FT HELIX 271..273
FT /evidence="ECO:0007829|PDB:1CF2"
FT STRAND 277..281
FT /evidence="ECO:0007829|PDB:1CF2"
FT HELIX 282..284
FT /evidence="ECO:0007829|PDB:1CF2"
FT STRAND 286..288
FT /evidence="ECO:0007829|PDB:1CF2"
FT STRAND 291..298
FT /evidence="ECO:0007829|PDB:1CF2"
FT TURN 300..303
FT /evidence="ECO:0007829|PDB:1CF2"
FT HELIX 304..315
FT /evidence="ECO:0007829|PDB:1CF2"
FT HELIX 322..333
FT /evidence="ECO:0007829|PDB:1CF2"
SQ SEQUENCE 337 AA; 37408 MW; D83CBA88AAE5B0B8 CRC64;
MKAVAINGYG TVGKRVADAI AQQDDMKVIG VSKTRPDFEA RMALKKGYDL YVAIPERVKL
FEKAGIEVAG TVDDMLDEAD IVIDCTPEGI GAKNLKMYKE KGIKAIFQGG EKHEDIGLSF
NSLSNYEESY GKDYTRVVSC NTTGLCRTLK PLHDSFGIKK VRAVIVRRGA DPAQVSKGPI
NAIIPNPPKL PSHHGPDVKT VLDINIDTMA VIVPTTLMHQ HNVMVEVEET PTVDDIIDVF
EDTPRVILIS AEDGLTSTAE IMEYAKELGR SRNDLFEIPV WRESITVVDN EIYYMQAVHQ
ESDIVPENVD AVRAILEMEE DKYKSINKTN KAMNILQ
