ID   G3P_METS5               Reviewed;         340 AA.
AC   A4YHA5;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   29-MAY-2007, sequence version 1.
DT   16-JUN-2009, entry version 17.
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=Msed_1652;
OS   Metallosphaera sedula (strain ATCC 51363 / DSM 5348).
OC   Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC   Metallosphaera.
OX   NCBI_TaxID=399549;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T.,
RA   Dalin E., Tice H., Pitluck S., Chertkov O., Brettin T., Han C.,
RA   Detter J.C., Bruce D., Schmutz J., Larimer F., Land M., Hauser L.,
RA   Kyrpides N., Mikhailova N., Maezato Y., Auernik K.S., Kelly R.M.,
RA   Blum P., Richardson P.;
RT   "Complete sequence of Metallosphaera sedula DSM 5348.";
RL   Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
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; CP000682; ABP95807.1; -; Genomic_DNA.
DR   RefSeq; YP_001191731.1; -.
DR   GeneID; 5104857; -.
DR   GenomeReviews; CP000682_GR; Msed_1652.
DR   KEGG; mse:Msed_1652; -.
DR   OMA; A4YHA5; AIFQGGE.
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   InterPro; IPR016040; NAD(P)-bd_dom.
DR   Gene3D; G3DSA:3.40.50.720; NAD(P)-bd; 1.
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    340       Glyceraldehyde-3-phosphate dehydrogenase.
FT                                /FTId=PRO_1000072562.
FT   NP_BIND      11     12       NAD (By similarity).
FT   REGION      138    140       Glyceraldehyde 3-phosphate binding (By
FT                                similarity).
FT   REGION      193    194       Glyceraldehyde 3-phosphate binding (By
FT                                similarity).
FT   ACT_SITE    139    139       Nucleophile (By similarity).
FT   BINDING     109    109       NAD; via amide nitrogen (By similarity).
FT   BINDING     167    167       NAD (By similarity).
FT   BINDING     300    300       NAD; via carbonyl oxygen (By similarity).
SQ   SEQUENCE   340 AA;  36648 MW;  997600B78F9101A1 CRC64;
     MIKVAVNGYG TIGKRVASAI LAQPDMTLVG VSKTSPNYEA YQAQKMGINL YVTKESLKEF
     EEAGIKVKGV LEDMIKEADV VVDATPNGVG AQYKQVYSSM GKRALFQGGE KANVADVSFS
     ALCNYDEAVD KRYVRVVSCN TTGLLRTLCT LNRVSKIAKV RGTIVRRAAD PKEVKKGPIN
     SLVPDPASIP SHHAKDVNTV LKDLDIVTMA VVAPTTLMHV HLLDVTVSSP VTKEDVLSVL
     SSTPRILLAS GKSKVSSTAE IVEVARDMGR PRNDLYELVV FEDSVSVRGN EVFLMYAVHQ
     ESIVVPENVD AIRAVSGFAD GRKSIEMTNA SMGIGKGYLV
//