ID G3P_PYRFU Reviewed; 334 AA. AC P61879; P20286; DT 07-JUN-2004, integrated into UniProtKB/Swiss-Prot. DT 07-JUN-2004, sequence version 1. DT 02-SEP-2026, entry version 123. 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; Synonyms=gapDH; OrderedLocusNames=PF1874; OS Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1). OC Archaea; Methanobacteriati; Methanobacteriota; Thermococci; Thermococcales; OC Thermococcaceae; Pyrococcus. OX NCBI_TaxID=186497; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43587 / DSM 3638 / JCM 8422 / Vc1; RX PubMed=10430560; DOI=10.1093/genetics/152.4.1299; RA Maeder D.L., Weiss R.B., Dunn D.M., Cherry J.L., Gonzalez J.M., RA DiRuggiero J., Robb F.T.; RT "Divergence of the hyperthermophilic archaea Pyrococcus furiosus and P. RT horikoshii inferred from complete genomic sequences."; RL Genetics 152:1299-1305(1999). RN [2] RP PUTATIVE SUBCELLULAR LOCATION. RX PubMed=34362927; DOI=10.1038/s41467-021-25071-y; RA Andreas M.P., Giessen T.W.; RT "Large-scale computational discovery and analysis of virus-derived RT microbial nanocompartments."; RL Nat. Commun. 12:4748-4748(2021). CC -!- FUNCTION: Possible cargo protein of a type 4B encapsulin CC nanocompartment (Probable). Active in the presence of NAD and NADP, CC prefers NADP (By similarity). {ECO:0000250|UniProtKB:P61880, CC ECO:0000305|PubMed:34362927}. CC -!- CATALYTIC ACTIVITY: CC Reaction=D-glyceraldehyde 3-phosphate + phosphate + NADP(+) = (2R)-3- CC phospho-glyceroyl phosphate + NADPH + H(+); 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:0000250|UniProtKB:P61880}; CC -!- CATALYTIC ACTIVITY: CC Reaction=D-glyceraldehyde 3-phosphate + phosphate + NAD(+) = (2R)-3- CC phospho-glyceroyl phosphate + NADH + H(+); 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:0000250|UniProtKB:P61880}; CC -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D- CC glyceraldehyde 3-phosphate: step 1/5. CC -!- SUBUNIT: Homotetramer. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Encapsulin nanocompartment CC {ECO:0000305|PubMed:34362927}. Note=Its location in a locus with a type CC 4B encapsulin shell protein suggests it might be located in an CC encapsulin nanocompartment. {ECO:0000305|PubMed:34362927}. CC -!- SIMILARITY: Belongs to the glyceraldehyde-3-phosphate dehydrogenase CC family. {ECO:0000305}. 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; AE009950; AAL81998.1; -; Genomic_DNA. DR RefSeq; WP_011013013.1; NC_003413.1. DR AlphaFoldDB; P61879; -. DR SMR; P61879; -. DR STRING; 186497.PF1874; -. DR PaxDb; 186497-PF1874; -. DR GeneID; 13301306; -. DR KEGG; pfu:PF1874; -. DR PATRIC; fig|186497.12.peg.1945; -. DR eggNOG; arCOG00493; Archaea. DR HOGENOM; CLU_069533_0_0_2; -. DR OrthoDB; 295712at2157; -. DR PhylomeDB; P61879; -. DR BRENDA; 1.2.1.59; 5243. DR UniPathway; UPA00109; UER00184. DR Proteomes; UP000001013; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-UniRule. DR GO; GO:0140737; C:encapsulin nanocompartment; IEA:UniProtKB-SubCell. DR GO; GO:0008839; F:4-hydroxy-tetrahydrodipicolinate reductase activity; IEA:InterPro. DR GO; GO:0004365; F:glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity; ISS:UniProtKB. DR GO; GO:0047100; F:glyceraldehyde-3-phosphate dehydrogenase (NADP+) (phosphorylating) activity; ISS:UniProtKB. DR GO; GO:0051287; F:NAD binding; IEA:InterPro. DR GO; GO:0050661; F:NADP binding; IEA:InterPro. DR GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-UniRule. DR CDD; cd18127; GAPDH_II_C; 1. DR CDD; cd02278; GAPDH_II_N; 1. DR Gene3D; 3.30.360.10; Dihydrodipicolinate Reductase, domain 2; 1. 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 NCBIfam; NF003251; PRK04207.1; 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 Encapsulin nanocompartment; Glycolysis; NAD; NADP; Oxidoreductase; KW Reference proteome. FT CHAIN 1..334 FT /note="Glyceraldehyde-3-phosphate dehydrogenase" FT /id="PRO_0000145730" FT ACT_SITE 141 FT /note="Nucleophile" FT /evidence="ECO:0000250" FT BINDING 12..13 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000250" FT BINDING 111 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000250" FT BINDING 140..142 FT /ligand="D-glyceraldehyde 3-phosphate" FT /ligand_id="ChEBI:CHEBI:59776" FT /evidence="ECO:0000250" FT BINDING 167 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000250" FT BINDING 192..193 FT /ligand="D-glyceraldehyde 3-phosphate" FT /ligand_id="ChEBI:CHEBI:59776" FT /evidence="ECO:0000250" FT BINDING 298 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000250" SQ SEQUENCE 334 AA; 37436 MW; 224E0626923AFC66 CRC64; MKIKVGINGY GTIGKRVAYA VTKQDDMELI GVTKTKPDFE AYRAKELGIP VYAASEEFLP RFEKAGFEVE GTLNDLLEKV DIIVDATPGG MGEKNKQLYE KAGVKAIFQG GEKAEVAQVS FVAQANYEAA LGKDYVRVVS CNTTGLVRTL NAIKDYVDYV YAVMIRRAAD PNDIKRGPIN AIKPSVTIPS HHGPDVQTVI PINIETSAFV VPTTIMHVHS IMVELKKPLT REDVIDIFEN TTRVLLFEKE KGFESTAQLI EFARDLHREW NNLYEIAVWK ESINVKGNRL FYIQAVHQES DVIPENIDAI RAMFEIAEKW ESIKKTNKSL GILK //