ID   G3P_SULAC               Reviewed;         343 AA.
AC   Q4J940;
DT   27-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT   02-AUG-2005, sequence version 1.
DT   16-JUN-2009, entry version 36.
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=Saci_1356;
OS   Sulfolobus acidocaldarius.
OC   Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC   Sulfolobus.
OX   NCBI_TaxID=2285;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33909 / DSM 639 / IFO 15157 / JCM 8929 / NCIB 11770;
RX   PubMed=15995215; DOI=10.1128/JB.187.14.4992-4999.2005;
RA   Chen L., Bruegger K., Skovgaard M., Redder P., She Q., Torarinsson E.,
RA   Greve B., Awayez M., Zibat A., Klenk H.-P., Garrett R.A.;
RT   "The genome of Sulfolobus acidocaldarius, a model organism of the
RT   Crenarchaeota.";
RL   J. Bacteriol. 187:4992-4999(2005).
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; CP000077; AAY80691.1; -; Genomic_DNA.
DR   RefSeq; YP_255984.1; -.
DR   GeneID; 3473469; -.
DR   GenomeReviews; CP000077_GR; Saci_1356.
DR   KEGG; sai:Saci_1356; -.
DR   NMPDR; fig|330779.3.peg.122; -.
DR   HOGENOM; Q4J940; -.
DR   OMA; Q4J940; AIFQGGE.
DR   BioCyc; SACI330779:SACI_1356-MON; -.
DR   BRENDA; 1.2.1.59; 434.
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    343       Glyceraldehyde-3-phosphate dehydrogenase.
FT                                /FTId=PRO_0000145734.
FT   NP_BIND      13     14       NAD (By similarity).
FT   REGION      140    142       Glyceraldehyde 3-phosphate binding (By
FT                                similarity).
FT   REGION      195    196       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     303    303       NAD; via carbonyl oxygen (By similarity).
SQ   SEQUENCE   343 AA;  37957 MW;  D0F30CB7AAF27CD2 CRC64;
     MVKVKVAING YGTIGKRVAD AIRLQPDMEL IGVAKTSPNY EAFTAMRKGY KLYTTKENIQ
     KFQNSGINVA GSIEDMIKDS DIIIDATPGG VGANYKKIYQ EYGKKAIFQG GEKSDVADVS
     FSALCNYNDA INKNYIRVVS CNTTGILRVL CTINNFDKIE KVRGTIVRRA ADPKEVKKGP
     INSIVADPAR IPSHHAKDVL TVLKGIDIIT SALVAPTTLM HLHTLFITTR NKVSKEDLLN
     ILSNTPRILL LNTEKADAES TAEIMEIARD LGRYRNDVPE TVIFEDSIYT NGNEIFLMYG
     VHQESIVVPE NIDAIRASLN IMSRDESIRL TNETLKIGKG YLI
//