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Database: UniProt
Entry: P10618
LinkDB: P10618
Original site: P10618 
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   01-OCT-2014, entry version 108.
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. {ECO:0000269|PubMed:10715215}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the glyceraldehyde-3-phosphate
CC       dehydrogenase family. {ECO:0000305}.
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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   SABIO-RK; P10618; -.
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:UniProtKB-EC.
DR   GO; GO:0004365; F:glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity; IEA:UniProtKB-HAMAP.
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-HAMAP.
DR   Gene3D; 3.40.50.720; -; 1.
DR   HAMAP; MF_00559; G3P_dehdrog_arch; 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; 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. {ECO:0000269|PubMed:10715215}.
FT   NP_BIND      34     35       NADP. {ECO:0000269|PubMed:10715215}.
FT   REGION      139    141       Glyceraldehyde 3-phosphate binding.
FT                                {ECO:0000250}.
FT   REGION      194    195       Glyceraldehyde 3-phosphate binding.
FT                                {ECO:0000250}.
FT   ACT_SITE    140    140       Nucleophile. {ECO:0000250}.
FT   BINDING     110    110       NADP; via amide nitrogen.
FT                                {ECO:0000269|PubMed:10715215}.
FT   BINDING     171    171       NADP. {ECO:0000269|PubMed:10715215}.
FT   BINDING     300    300       NADP; via carbonyl oxygen. {ECO:0000250}.
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
//
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