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-APR-2013, entry version 102.
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; Methanobacteria; Methanobacteriales;
OC 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
RT from the nucleotide sequence of the thermophilic archaebacterium
RT Methanothermus fervidus.";
RL Gene 64:189-197(1988).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) IN COMPLEX WITH NADP, AND
RP SUBUNIT.
RX PubMed=10715215; DOI=10.1006/jmbi.2000.3565;
RA Charron C., Talfournier F., Isupov M.N., Littlechild J.A.,
RA Branlant G., Vitoux B., Aubry A.;
RT "The crystal structure of D-glyceraldehyde-3-phosphate dehydrogenase
RT from the hyperthermophilic archaeon Methanothermus fervidus in the
RT presence of 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: D-glyceraldehyde 3-phosphate + phosphate +
CC NAD(P)(+) = 3-phospho-D-glyceroyl phosphate + NAD(P)H.
CC -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
CC glyceraldehyde 3-phosphate: step 1/5.
CC -!- SUBUNIT: Homotetramer.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- SIMILARITY: Belongs to the glyceraldehyde-3-phosphate
CC dehydrogenase family.
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DR EMBL; M19980; AAA88227.1; -; Genomic_DNA.
DR PIR; JT0286; JT0286.
DR RefSeq; YP_004003841.1; NC_014658.1.
DR PDB; 1CF2; X-ray; 2.10 A; O/P/Q/R=1-337.
DR PDBsum; 1CF2; -.
DR ProteinModelPortal; P10618; -.
DR SMR; P10618; 1-336.
DR GeneID; 9961991; -.
DR KEGG; mfv:Mfer_0276; -.
DR KO; K00150; -.
DR UniPathway; UPA00109; UER00184.
DR EvolutionaryTrace; P10618; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0043891; F:glyceraldehyde-3-phosphate dehydrogenase (NAD(P)+) (phosphorylating) activity; IEA:EC.
DR GO; GO:0004365; F:glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity; IEA:HAMAP.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR GO; GO:0006096; P:glycolysis; IEA:HAMAP.
DR Gene3D; 3.40.50.720; -; 1.
DR HAMAP; MF_00559; G3P_dehdrog_arch; 1; atypical.
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; IPR016040; NAD(P)-bd_dom.
DR Pfam; PF02800; Gp_dh_C; 1.
DR Pfam; PF00044; Gp_dh_N; 1.
DR PIRSF; PIRSF000149; GAP_DH; 1.
DR SMART; SM00846; Gp_dh_N; 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 Glyceraldehyde-3-phosphate dehydrogenase.
FT /FTId=PRO_0000145722.
FT NP_BIND 11 12 NADP.
FT NP_BIND 34 35 NADP.
FT REGION 139 141 Glyceraldehyde 3-phosphate binding (By
FT similarity).
FT REGION 194 195 Glyceraldehyde 3-phosphate binding (By
FT similarity).
FT ACT_SITE 140 140 Nucleophile (By similarity).
FT BINDING 110 110 NADP; via amide nitrogen.
FT BINDING 171 171 NADP.
FT BINDING 300 300 NADP; via carbonyl oxygen (By
FT similarity).
FT STRAND 2 7
FT HELIX 13 21
FT STRAND 23 35
FT HELIX 38 45
FT STRAND 50 54
FT HELIX 55 57
FT HELIX 58 63
FT HELIX 72 77
FT STRAND 80 84
FT HELIX 90 101
FT STRAND 105 107
FT HELIX 113 116
FT HELIX 122 125
FT HELIX 126 129
FT STRAND 133 137
FT HELIX 140 156
FT STRAND 158 170
FT STRAND 184 191
FT HELIX 194 199
FT STRAND 206 214
FT STRAND 219 229
FT HELIX 233 242
FT STRAND 246 249
FT TURN 251 254
FT HELIX 258 268
FT HELIX 271 273
FT STRAND 277 281
FT HELIX 282 284
FT STRAND 286 288
FT STRAND 291 298
FT TURN 300 303
FT HELIX 304 315
FT HELIX 322 333
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
//
