ID D5U0C7_THEAM Unreviewed; 343 AA. AC D5U0C7; DT 13-JUL-2010, integrated into UniProtKB/TrEMBL. DT 13-JUL-2010, sequence version 1. DT 27-MAR-2024, entry version 80. DE RecName: Full=Glyceraldehyde-3-phosphate dehydrogenase {ECO:0000256|HAMAP-Rule:MF_00559, ECO:0000256|RuleBase:RU003388}; DE Short=GAPDH {ECO:0000256|HAMAP-Rule:MF_00559}; DE EC=1.2.1.59 {ECO:0000256|HAMAP-Rule:MF_00559, ECO:0000256|RuleBase:RU003388}; DE AltName: Full=NAD(P)-dependent glyceraldehyde-3-phosphate dehydrogenase {ECO:0000256|HAMAP-Rule:MF_00559}; GN Name=gap {ECO:0000256|HAMAP-Rule:MF_00559}; GN OrderedLocusNames=Tagg_0301 {ECO:0000313|EMBL:ADG90577.1}; OS Thermosphaera aggregans (strain DSM 11486 / M11TL). OC Archaea; Thermoproteota; Thermoprotei; Desulfurococcales; OC Desulfurococcaceae; Thermosphaera. OX NCBI_TaxID=633148 {ECO:0000313|EMBL:ADG90577.1, ECO:0000313|Proteomes:UP000002376}; RN [1] {ECO:0000313|EMBL:ADG90577.1, ECO:0000313|Proteomes:UP000002376} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 11486 / M11TL {ECO:0000313|Proteomes:UP000002376}; RX PubMed=21304709; RA Spring S., Rachel R., Lapidus A., Davenport K., Tice H., Copeland A., RA Cheng J.F., Lucas S., Chen F., Nolan M., Bruce D., Goodwin L., Pitluck S., RA Ivanova N., Mavromatis K., Ovchinnikova G., Pati A., Chen A., RA Palaniappan K., Land M., Hauser L., Chang Y.J., Jeffries C.C., Brettin T., RA Detter J.C., Tapia R., Han C., Heimerl T., Weikl F., Brambilla E., RA Goker M., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P., RA Kyrpides N.C., Klenk H.P.; RT "Complete genome sequence of Thermosphaera aggregans type strain (M11TL)."; RL Stand. Genomic Sci. 2:245-259(2010). RN [2] {ECO:0000313|Proteomes:UP000002376} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 11486 / M11TL {ECO:0000313|Proteomes:UP000002376}; RX DOI=10.4056/sigs.821804; RA Spring S., Rachel R., Lapidus A., Davenport K., Tice H., Copeland A., RA Cheng J.-F., Lucas S., Chen F., Nolan M., Bruce D., Goodwin L., Pitluck S., RA Ivanova N., Mavromatis K., Ovchinnikova G., Pati A., Chen A., RA Palaniappan K., Land M., Hauser L., Chang Y.-J., Jeffries C.C., Brettin T., RA Detter J.C., Tapia R., Han C., Heimerl T., Weikl F., Brambilla E., RA Goker M., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P., RA Kyrpides N.C., Klenk H.-P.; RT "Complete genome sequence of Thermosphaera aggregans type strain RT (M11TLT)."; RL Stand. Genomic Sci. 2:245-259(2010). RN [3] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 11486; RG US DOE Joint Genome Institute (JGI-PGF); RA Spring S., Lapidus A., Munk C., Schroeder M., Glavina Del Rio T., Tice H., RA Copeland A., Cheng J.-F., Lucas S., Chen F., Nolan M., Bruce D., RA Goodwin L., Pitluck S., Ivanova N., Mavromatis K., Ovchinnikova G., RA Pati A., Chen A., Palaniappan K., Land M., Hauser L., Chang Y.-J., RA Jeffries C.C., Brettin T., Detter J.C., Tapia R., Han C., Chain P., RA Heimerl T., Weik F., Goker M., Rachel R., Bristow J., Eisen J.A., RA Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.-P.; RT "Complete genome sequence of Thermosphaera aggregans type strain (M11TL)."; RL Submitted (FEB-2010) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: CC Reaction=D-glyceraldehyde 3-phosphate + NAD(+) + phosphate = (2R)-3- CC phospho-glyceroyl phosphate + H(+) + NADH; Xref=Rhea:RHEA:10300, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:57540, CC ChEBI:CHEBI:57604, ChEBI:CHEBI:57945, ChEBI:CHEBI:59776; EC=1.2.1.59; CC Evidence={ECO:0000256|ARBA:ARBA00001820, ECO:0000256|HAMAP- CC Rule:MF_00559, ECO:0000256|RuleBase:RU003388}; CC -!- CATALYTIC ACTIVITY: CC Reaction=D-glyceraldehyde 3-phosphate + NADP(+) + phosphate = (2R)-3- CC phospho-glyceroyl phosphate + H(+) + NADPH; Xref=Rhea:RHEA:10296, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:57604, CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:59776; EC=1.2.1.59; CC Evidence={ECO:0000256|ARBA:ARBA00001295, ECO:0000256|HAMAP- CC Rule:MF_00559, ECO:0000256|RuleBase:RU003388}; CC -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D- CC glyceraldehyde 3-phosphate: step 1/5. {ECO:0000256|ARBA:ARBA00004869, CC ECO:0000256|HAMAP-Rule:MF_00559, ECO:0000256|RuleBase:RU003388}. CC -!- SUBUNIT: Homotetramer. {ECO:0000256|ARBA:ARBA00011881, CC ECO:0000256|HAMAP-Rule:MF_00559, ECO:0000256|RuleBase:RU003388}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00559, CC ECO:0000256|RuleBase:RU003388}. CC -!- SIMILARITY: Belongs to the glyceraldehyde-3-phosphate dehydrogenase CC family. {ECO:0000256|HAMAP-Rule:MF_00559, CC ECO:0000256|RuleBase:RU003388}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CP001939; ADG90577.1; -; Genomic_DNA. DR AlphaFoldDB; D5U0C7; -. DR STRING; 633148.Tagg_0301; -. DR KEGG; tag:Tagg_0301; -. DR eggNOG; arCOG00493; Archaea. DR HOGENOM; CLU_069533_0_0_2; -. DR UniPathway; UPA00109; UER00184. DR Proteomes; UP000002376; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0008839; F:4-hydroxy-tetrahydrodipicolinate reductase; IEA:InterPro. DR GO; GO:0004365; F:glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity; IEA:UniProtKB-UniRule. DR GO; GO:0047100; F:glyceraldehyde-3-phosphate dehydrogenase (NADP+) (phosphorylating) activity; IEA:RHEA. DR GO; GO:0051287; F:NAD binding; IEA:UniProtKB-UniRule. DR GO; GO:0050661; F:NADP binding; IEA:UniProtKB-UniRule. DR GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-UniRule. DR GO; GO:0009089; P:lysine biosynthetic process via diaminopimelate; IEA:InterPro. DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1. DR HAMAP; MF_00559; G3P_dehdrog_arch; 1. DR InterPro; IPR000846; DapB_N. DR InterPro; IPR020831; GlycerAld/Erythrose_P_DH. DR InterPro; IPR020830; GlycerAld_3-P_DH_AS. DR InterPro; IPR020829; GlycerAld_3-P_DH_cat. DR InterPro; IPR020828; GlycerAld_3-P_DH_NAD(P)-bd. DR InterPro; IPR006436; Glyceraldehyde-3-P_DH_2_arc. DR InterPro; IPR036291; NAD(P)-bd_dom_sf. DR NCBIfam; TIGR01546; GAPDH-II_archae; 1. DR Pfam; PF01113; DapB_N; 1. DR Pfam; PF02800; Gp_dh_C; 1. DR PIRSF; PIRSF000149; GAP_DH; 1. DR SMART; SM00846; Gp_dh_N; 1. DR SUPFAM; SSF55347; Glyceraldehyde-3-phosphate dehydrogenase-like, C-terminal domain; 1. DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1. DR PROSITE; PS00071; GAPDH; 1. PE 3: Inferred from homology; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00559, ECO:0000256|RuleBase:RU003388}; KW Glycolysis {ECO:0000256|ARBA:ARBA00023152, ECO:0000256|HAMAP- KW Rule:MF_00559}; KW NAD {ECO:0000256|HAMAP-Rule:MF_00559, ECO:0000256|RuleBase:RU003388}; KW NADP {ECO:0000256|ARBA:ARBA00022857, ECO:0000256|HAMAP-Rule:MF_00559}; KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, ECO:0000256|HAMAP- KW Rule:MF_00559}; Reference proteome {ECO:0000313|Proteomes:UP000002376}. FT DOMAIN 2..139 FT /note="Glyceraldehyde 3-phosphate dehydrogenase NAD(P) FT binding" FT /evidence="ECO:0000259|SMART:SM00846" FT ACT_SITE 139 FT /note="Nucleophile" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00559, FT ECO:0000256|PIRSR:PIRSR000149-1" FT BINDING 11..12 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00559" FT BINDING 109 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00559" FT BINDING 138..140 FT /ligand="D-glyceraldehyde 3-phosphate" FT /ligand_id="ChEBI:CHEBI:59776" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00559" FT BINDING 167 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00559" FT BINDING 193..194 FT /ligand="D-glyceraldehyde 3-phosphate" FT /ligand_id="ChEBI:CHEBI:59776" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00559" FT BINDING 301 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00559" SQ SEQUENCE 343 AA; 37975 MW; 356D92B0171D6F33 CRC64; MVKVGVNGYG TIGKRVADAI LKNPRFQLVG IVKYNPDYSS KIAFKKGINI YVPQDKWRDF ESTGITPKGT IQEFLEESSI IIDASPNGKG AANLSLYKGA GKPAIFQGGE KPEVAELSYS TYCNYDEAFG RKYLRVVSCN TTGILRVLCA LHREFNVKRA RVLVIRRGAD PKEDARGPIN SIKLESFEDV SHHGKDAMLV LPSVKIISQA VVVPTTLMHV QYLDIDVASP VTRSQVIEAL SKHARILLVN PKKTGIDSTS KLIEAARDFL RSRNDIYENI VFENTIIVSD NNISLIQAIH QESIVVPENM DALYAIANIR LPFEKVVEET DRLLGVGGLK DVF //