ID G3P_SULTO Reviewed; 343 AA. AC Q971K2; DT 27-MAY-2002, integrated into UniProtKB/Swiss-Prot. DT 01-DEC-2001, sequence version 1. DT 16-JUN-2009, entry version 55. 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=ST1356; OS Sulfolobus tokodaii. OC Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae; OC Sulfolobus. OX NCBI_TaxID=111955; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 16993 / JCM 10545 / NBRC 100140 / 7; RX MEDLINE=21456156; PubMed=11572479; DOI=10.1093/dnares/8.4.123; RA Kawarabayasi Y., Hino Y., Horikawa H., Jin-no K., Takahashi M., RA Sekine M., Baba S., Ankai A., Kosugi H., Hosoyama A., Fukui S., RA Nagai Y., Nishijima K., Otsuka R., Nakazawa H., Takamiya M., Kato Y., RA Yoshizawa T., Tanaka T., Kudoh Y., Yamazaki J., Kushida N., Oguchi A., RA Aoki K., Masuda S., Yanagii M., Nishimura M., Yamagishi A., Oshima T., RA Kikuchi H.; RT "Complete genome sequence of an aerobic thermoacidophilic RT Crenarchaeon, Sulfolobus tokodaii strain7."; RL DNA Res. 8:123-140(2001). 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; BA000023; BAB66418.1; -; Genomic_DNA. DR RefSeq; NP_377309.1; -. DR HSSP; P39460; 1B7G. DR GeneID; 1459378; -. DR GenomeReviews; BA000023_GR; ST1356. DR KEGG; sto:ST1356; -. DR NMPDR; fig|273063.1.peg.1477; -. DR HOGENOM; Q971K2; -. DR OMA; Q971K2; AIFQGGE. DR BRENDA; 1.2.1.59; 261167. 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_0000145736. 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; 37515 MW; F5620C2D7A673303 CRC64; MEKVKVAVNG YGTIGKRVAD AIRLQPDMEL IGVGKTSPNY EAIIADKKGI KIYTVKDNIG KFEKSGIRVA GTIEDMVKEA DIVVDTTPNG VGATYKPLYQ SLGKNALFQG GEKADVADIS FSALCNYDEA KGKKYIRVVS CNTTGMLRII CTMNKISKVE KVRATIVRRA ADPKEVKRGP INSIVPDPAS VPSHHAKDVL TVIKGIDIVT MAVIAPTTLM HLHTMVLTVK DKVNRDDIIN TFLNTPRIIL VNSSRTTVSS TAEIIEVSRD MGRVRYDIPE VVVFEDSIYT NGNEVFLMYG VHQESIVVPE NIDAIRASLG LMGKEESIKV TNDTLGIMKG YLL //