ID   G3P_METST               Reviewed;         337 AA.
AC   Q2NEN0;
DT   04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT   07-FEB-2006, sequence version 1.
DT   16-JUN-2009, entry version 28.
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; OrderedLocusNames=Msp_1346;
OS   Methanosphaera stadtmanae (strain DSM 3091).
OC   Archaea; Euryarchaeota; Methanobacteria; Methanobacteriales;
OC   Methanobacteriaceae; Methanosphaera.
OX   NCBI_TaxID=339860;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16385054; DOI=10.1128/JB.188.2.642-658.2006;
RA   Fricke W.F., Seedorf H., Henne A., Kruer M., Liesegang H.,
RA   Hedderich R., Gottschalk G., Thauer R.K.;
RT   "The genome sequence of Methanosphaera stadtmanae reveals why this
RT   human intestinal archaeon is restricted to methanol and H2 for methane
RT   formation and ATP synthesis.";
RL   J. Bacteriol. 188:642-658(2006).
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 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- SIMILARITY: Belongs to the glyceraldehyde-3-phosphate
CC       dehydrogenase family.
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DR   EMBL; CP000102; ABC57723.1; -; Genomic_DNA.
DR   RefSeq; YP_448366.1; -.
DR   GeneID; 3855085; -.
DR   GenomeReviews; CP000102_GR; Msp_1346.
DR   KEGG; mst:Msp_1346; -.
DR   NMPDR; fig|339860.6.peg.1292; -.
DR   HOGENOM; Q2NEN0; -.
DR   OMA; Q2NEN0; AIFQGGE.
DR   BioCyc; MSTA339860:MSP_1346-MON; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0043891; F:glyceraldehyde-3-phosphate dehydrogenase (N...; IEA:EC.
DR   GO; GO:0004365; F:glyceraldehyde-3-phosphate dehydrogenase (p...; IEA:HAMAP.
DR   GO; GO:0051287; F:NAD or NADH binding; IEA:InterPro.
DR   GO; GO:0050661; F:NADP or NADPH binding; IEA:InterPro.
DR   GO; GO:0006096; P:glycolysis; IEA:HAMAP.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   HAMAP; MF_00559; -; 1.
DR   InterPro; IPR000173; GlycerAld_3-P_DH.
DR   InterPro; IPR006436; Glyceraldehyde-3-P_DH_2_arc.
DR   Pfam; PF02800; Gp_dh_C; 1.
DR   Pfam; PF00044; Gp_dh_N; 1.
DR   PIRSF; PIRSF000149; GAP_DH; 1.
DR   ProDom; PD007761; GAPDH_like; 1.
DR   TIGRFAMs; TIGR01546; GAPDH-II_archae; 1.
DR   PROSITE; PS00071; GAPDH; 1.
PE   3: Inferred from homology;
KW   Complete proteome; Cytoplasm; Glycolysis; NAD; NADP; Oxidoreductase.
FT   CHAIN         1    337       Glyceraldehyde-3-phosphate dehydrogenase.
FT                                /FTId=PRO_0000232392.
FT   NP_BIND      11     12       NAD (By similarity).
FT   REGION      140    142       Glyceraldehyde 3-phosphate binding (By
FT                                similarity).
FT   REGION      194    195       Glyceraldehyde 3-phosphate binding (By
FT                                similarity).
FT   ACT_SITE    141    141       Nucleophile (By similarity).
FT   BINDING     111    111       NAD; via amide nitrogen (By similarity).
FT   BINDING     169    169       NAD (By similarity).
FT   BINDING     301    301       NAD; via carbonyl oxygen (By similarity).
SQ   SEQUENCE   337 AA;  36910 MW;  71F5CD8AAECC35BF CRC64;
     MKSIGINGYG TIGKRVADAV SAQDDMKIVG VTKRTPDYEA KAAVEKGYDL YISVPERESQ
     FEEAGIEVAG TADELFEKLD LVVDCTPGGI GAQNKTDIYE KIGLKAIFEG GEDHDAIGSS
     FNAEANYADN IGEDYVRVVS CNTTGLCRTL KPIYDISGIK KVRAVMVRRG ADPSDVKKGP
     INSIVPTTEV PSHHGPDVQT IIDDINVMTM ALLVPTTLMH THNIMVELED KITTDDVLDA
     FENAHRVLPV QKSLKLGSTA EIMEYAKDLG RSRGDMYEIP VWKESVNIEN GELFYMQAVH
     QESDVVPENV DAIRAMLELE EDGEKSILKT NKAMGIL
//