ID   G3P_PYRIL               Reviewed;         344 AA.
AC   A1RV79;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   25-NOV-2008, entry version 18.
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=Pisl_1710;
OS   Pyrobaculum islandicum (strain DSM 4184 / JCM 9189).
OC   Archaea; Crenarchaeota; Thermoprotei; Thermoproteales;
OC   Thermoproteaceae; Pyrobaculum.
OX   NCBI_TaxID=384616;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Dalin E., Tice H., Pitluck S., Meincke L.,
RA   Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Lowe T.,
RA   Richardson P.;
RT   "Complete sequence of Pyrobaculum islandicum DSM 4184.";
RL   Submitted (DEC-2006) 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.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; CP000504; ABL88861.1; -; Genomic_DNA.
DR   RefSeq; YP_931204.1; -.
DR   GeneID; 4617093; -.
DR   GenomeReviews; CP000504_GR; Pisl_1710.
DR   KEGG; pis:Pisl_1710; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:HAMAP.
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 binding; IEA:InterPro.
DR   GO; GO:0050661; F:NADP 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_DHase.
DR   InterPro; IPR006436; Glyceraldehyde-3-P_DHase_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    344       Glyceraldehyde-3-phosphate dehydrogenase.
FT                                /FTId=PRO_0000300977.
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;  38074 MW;  0157B44F43030CD8 CRC64;
     MIKVGIIGYG TIGKRIADAV AMQDDMKVVG VLKVTPDYEA KIALARGFPI YTYSDRFDKF
     KKAGIEPAGT IEDLIKASDI IIDASPEDVG RENKEKYYQR YDKPVIFQGG EEADVADVSF
     NALANYEEAK GRRYVRVVSC NTTGITRVLT SLILNGIGIK KARIFIARRG ADPKEHKKGP
     INDVVPNPAT VPSHHGPDVQ TILKDIDIVT MAIAVPVTIM HMHMAYIELS STYTKDAVIE
     AFVKTPRIFL ADVGSGFQSL AHVIEYARDL GRSRSDFPEV AIFRDSVTIR GNELYLMYGV
     HQESIVVPEN VDAIRAVLGI LPKWRSIEKT DKTLKLITEG KVYG
//