ID E8R9H3_DESM0 Unreviewed; 356 AA. AC E8R9H3; DT 05-APR-2011, integrated into UniProtKB/TrEMBL. DT 05-APR-2011, sequence version 1. DT 27-MAR-2024, entry version 73. 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=Desmu_0845 {ECO:0000313|EMBL:ADV65149.1}; OS Desulfurococcus mucosus (strain ATCC 35584 / DSM 2162 / JCM 9187 / O7/1). OC Archaea; Thermoproteota; Thermoprotei; Desulfurococcales; OC Desulfurococcaceae; Desulfurococcus. OX NCBI_TaxID=765177 {ECO:0000313|EMBL:ADV65149.1, ECO:0000313|Proteomes:UP000001068}; RN [1] {ECO:0000313|Proteomes:UP000001068} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 35584 / DSM 2162 / JCM 9187 / O7/1 RC {ECO:0000313|Proteomes:UP000001068}; RG US DOE Joint Genome Institute (JGI-PGF); RA Lucas S., Copeland A., Lapidus A., Bruce D., Goodwin L., Pitluck S., RA Kyrpides N., Mavromatis K., Pagani I., Ivanova N., Ovchinnikova G., RA Chertkov O., Held B., Brettin T., Detter J.C., Tapia R., Han C., Land M., RA Hauser L., Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T., Wu D., RA Wirth R., Bilek Y., Hader T., Klenk H.-P., Eisen J.A.; RT "The complete genome of Desulfurococcus mucosus DSM 2162."; RL Submitted (NOV-2010) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:ADV65149.1, ECO:0000313|Proteomes:UP000001068} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 35584 / DSM 2162 / JCM 9187 / O7/1 RC {ECO:0000313|Proteomes:UP000001068}; RX PubMed=21677854; DOI=10.4056/sigs.1644004; RA Wirth R., Chertkov O., Held B., Lapidus A., Nolan M., Lucas S., Hammon N., RA Deshpande S., Cheng J.F., Tapia R., Han C., Goodwin L., Pitluck S., RA Liolios K., Ioanna P., Ivanova N., Mavromatis K., Mikhailova N., Pati A., RA Chen A., Palaniappan K., Land M., Hauser L., Chang Y.J., Jeffries C.D., RA Bilek Y., Hader T., Rohde M., Spring S., Sikorski J., Goker M., Woyke T., RA Bristow J., Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C., RA Klenk H.P.; RT "Complete genome sequence of Desulfurococcus mucosus type strain (O7/1)."; RL Stand. Genomic Sci. 4:173-182(2011). 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; CP002363; ADV65149.1; -; Genomic_DNA. DR RefSeq; WP_013562371.1; NC_014961.1. DR AlphaFoldDB; E8R9H3; -. DR STRING; 765177.Desmu_0845; -. DR GeneID; 10153542; -. DR KEGG; dmu:Desmu_0845; -. DR eggNOG; arCOG00493; Archaea. DR HOGENOM; CLU_069533_0_0_2; -. DR OrthoDB; 295712at2157; -. DR UniPathway; UPA00109; UER00184. DR Proteomes; UP000001068; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. 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 Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1. DR HAMAP; MF_00559; G3P_dehdrog_arch; 1. 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; 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|HAMAP-Rule:MF_00559, KW ECO:0000256|RuleBase:RU003388}; 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:UP000001068}. FT DOMAIN 3..140 FT /note="Glyceraldehyde 3-phosphate dehydrogenase NAD(P) FT binding" FT /evidence="ECO:0000259|SMART:SM00846" FT ACT_SITE 140 FT /note="Nucleophile" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00559, FT ECO:0000256|PIRSR:PIRSR000149-1" FT BINDING 12..13 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00559" FT BINDING 110 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00559" FT BINDING 139..141 FT /ligand="D-glyceraldehyde 3-phosphate" FT /ligand_id="ChEBI:CHEBI:59776" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00559" FT BINDING 168 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00559" FT BINDING 194..195 FT /ligand="D-glyceraldehyde 3-phosphate" FT /ligand_id="ChEBI:CHEBI:59776" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00559" FT BINDING 302 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00559" SQ SEQUENCE 356 AA; 39090 MW; 6384484C0E4929EA CRC64; MPVKIAVNGY GTIGKRIVDA VLSNKDFRLV GIAKYRVDYS AYLAARKGIP IYVPRERASE FREAGLEPHG YVDYLFEEAD LIYDASPGGK GAGNKKIYES YGKPGVFQGG EEPGVAELSY STLCNFEEAL NKKYVRVVSC NTTGMLRLLC TLHREYGVKR ALSVIIRRAA DPKEDQRGPV NSILLDPPSI PSHHGLDART VAPWLDIVTA AAVVPTTLMH MQFIEVELST QVNRGDVVEL LDGINRFLLV ESASTGIDST SKVMELARDS GRPRGDIYEN IVFIDSLSIN ASRLYLFQGI HQESIVIPEN IDVAYAMLGI ESDPLKVMER VDSTLGIGGL RRFISPHGYI QIGGAP //