ID   G3P_PYRAR               Reviewed;         344 AA.
AC   A4WIW2;
DT   11-SEP-2007, 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=Pars_0743;
OS   Pyrobaculum arsenaticum (strain DSM 13514 / JCM 11321).
OC   Archaea; Crenarchaeota; Thermoprotei; Thermoproteales;
OC   Thermoproteaceae; Pyrobaculum.
OX   NCBI_TaxID=340102;
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., Chain P., Malfatti S., Shin M.,
RA   Vergez L., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Mikhailova N., Cozen A.E., Fitz-Gibbon S.T., House C.H., Saltikov C.,
RA   Lowe T.M., Richardson P.;
RT   "Complete sequence of Pyrobaculum arsenaticum DSM 13514.";
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; CP000660; ABP50329.1; -; Genomic_DNA.
DR   RefSeq; YP_001152981.1; -.
DR   GeneID; 5054487; -.
DR   GenomeReviews; CP000660_GR; Pars_0743.
DR   KEGG; pas:Pars_0743; -.
DR   OMA; A4WIW2; 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    344       Glyceraldehyde-3-phosphate dehydrogenase.
FT                                /FTId=PRO_0000300975.
FT   NP_BIND      11     12       NAD (By similarity).
FT   REGION      139    141       Glyceraldehyde 3-phosphate binding (By
FT                                similarity).
FT   REGION      195    196       Glyceraldehyde 3-phosphate binding (By
FT                                similarity).
FT   ACT_SITE    140    140       Nucleophile (By similarity).
FT   BINDING     110    110       NAD; via amide nitrogen (By similarity).
FT   BINDING     169    169       NAD (By similarity).
FT   BINDING     302    302       NAD; via carbonyl oxygen (By similarity).
SQ   SEQUENCE   344 AA;  37492 MW;  02B316F2B8F47E36 CRC64;
     MIRVGIVGFG TIGKRIADAV AAQGDMHVSG VLKVTPDYEV LVAAAKGFKV YTLPDRVEKF
     KKAGIEPAGT IEDLIKASDV IIDASPEDVG AENKEKYYSK FDKPVIFQGG EEAEVAEVSF
     NALANYDEAR GRRYVRVVSC NTTGITRVLT SLMLNGVGIK KARIFIARRG ADPKEYKKGP
     INDVVPNPAT VPSHHGPDVK TVLKNVDIVT MAVAVPVTIM HMHMAFLELD GAYPRDAVLE
     ALAKTPRIFL ADVGAGFQSL AQIIEYARDL GRPRGDFPEV AIFRDSVTVN GNELYLMYGV
     HQESIVVPEN VDAVRAVLGA MPKWESIKKT DTTLKLFTEG KRYG
//