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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   26-NOV-2014, entry version 110.
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-HAMAP.
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       {ECO:0000244|PDB:1CF2}.
FT   HELIX        13     21       {ECO:0000244|PDB:1CF2}.
FT   STRAND       23     35       {ECO:0000244|PDB:1CF2}.
FT   HELIX        38     45       {ECO:0000244|PDB:1CF2}.
FT   STRAND       50     54       {ECO:0000244|PDB:1CF2}.
FT   HELIX        55     57       {ECO:0000244|PDB:1CF2}.
FT   HELIX        58     63       {ECO:0000244|PDB:1CF2}.
FT   HELIX        72     77       {ECO:0000244|PDB:1CF2}.
FT   STRAND       80     84       {ECO:0000244|PDB:1CF2}.
FT   HELIX        90    101       {ECO:0000244|PDB:1CF2}.
FT   STRAND      105    107       {ECO:0000244|PDB:1CF2}.
FT   HELIX       113    116       {ECO:0000244|PDB:1CF2}.
FT   HELIX       122    125       {ECO:0000244|PDB:1CF2}.
FT   HELIX       126    129       {ECO:0000244|PDB:1CF2}.
FT   STRAND      133    137       {ECO:0000244|PDB:1CF2}.
FT   HELIX       140    156       {ECO:0000244|PDB:1CF2}.
FT   STRAND      158    170       {ECO:0000244|PDB:1CF2}.
FT   STRAND      184    191       {ECO:0000244|PDB:1CF2}.
FT   HELIX       194    199       {ECO:0000244|PDB:1CF2}.
FT   STRAND      206    214       {ECO:0000244|PDB:1CF2}.
FT   STRAND      219    229       {ECO:0000244|PDB:1CF2}.
FT   HELIX       233    242       {ECO:0000244|PDB:1CF2}.
FT   STRAND      246    249       {ECO:0000244|PDB:1CF2}.
FT   TURN        251    254       {ECO:0000244|PDB:1CF2}.
FT   HELIX       258    268       {ECO:0000244|PDB:1CF2}.
FT   HELIX       271    273       {ECO:0000244|PDB:1CF2}.
FT   STRAND      277    281       {ECO:0000244|PDB:1CF2}.
FT   HELIX       282    284       {ECO:0000244|PDB:1CF2}.
FT   STRAND      286    288       {ECO:0000244|PDB:1CF2}.
FT   STRAND      291    298       {ECO:0000244|PDB:1CF2}.
FT   TURN        300    303       {ECO:0000244|PDB:1CF2}.
FT   HELIX       304    315       {ECO:0000244|PDB:1CF2}.
FT   HELIX       322    333       {ECO:0000244|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
//
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