ID G3P_METB6 Reviewed; 343 AA. AC A7IB57; DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot. DT 11-SEP-2007, sequence version 1. DT 02-SEP-2026, entry version 103. DE RecName: Full=Glyceraldehyde-3-phosphate dehydrogenase {ECO:0000255|HAMAP-Rule:MF_00559}; DE Short=GAPDH {ECO:0000255|HAMAP-Rule:MF_00559}; DE EC=1.2.1.59 {ECO:0000255|HAMAP-Rule:MF_00559}; DE AltName: Full=NAD(P)-dependent glyceraldehyde-3-phosphate dehydrogenase {ECO:0000255|HAMAP-Rule:MF_00559}; GN Name=gap {ECO:0000255|HAMAP-Rule:MF_00559}; GN OrderedLocusNames=Mboo_2454; OS Methanoregula boonei (strain DSM 21154 / JCM 14090 / 6A8). OC Archaea; Methanobacteriati; Methanobacteriota; Stenosarchaea group; OC Methanomicrobia; Methanomicrobiales; Methanoregulaceae; Methanoregula. OX NCBI_TaxID=456442; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 21154 / JCM 14090 / 6A8; RX PubMed=25998264; DOI=10.1099/mic.0.000117; RA Braeuer S., Cadillo-Quiroz H., Kyrpides N., Woyke T., Goodwin L., RA Detter C., Podell S., Yavitt J.B., Zinder S.H.; RT "Genome of Methanoregula boonei 6A8 reveals adaptations to oligotrophic RT peatland environments."; RL Microbiology 161:1572-1581(2015). 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:0000255|HAMAP-Rule:MF_00559}; 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:0000255|HAMAP-Rule:MF_00559}; CC -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D- CC glyceraldehyde 3-phosphate: step 1/5. {ECO:0000255|HAMAP- CC Rule:MF_00559}. CC -!- SUBUNIT: Homotetramer. {ECO:0000255|HAMAP-Rule:MF_00559}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00559}. CC -!- SIMILARITY: Belongs to the glyceraldehyde-3-phosphate dehydrogenase CC family. {ECO:0000255|HAMAP-Rule:MF_00559}. 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; CP000780; ABS56968.1; -; Genomic_DNA. DR RefSeq; WP_012108032.1; NC_009712.1. DR AlphaFoldDB; A7IB57; -. DR SMR; A7IB57; -. DR STRING; 456442.Mboo_2454; -. DR GeneID; 5412014; -. DR KEGG; mbn:Mboo_2454; -. DR eggNOG; arCOG00493; Archaea. DR HOGENOM; CLU_069533_0_0_2; -. DR OrthoDB; 295712at2157; -. DR UniPathway; UPA00109; UER00184. DR Proteomes; UP000002408; Chromosome. DR GO; GO:0005737; C:cytoplasm; 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; 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: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 Cytoplasm; Glycolysis; NAD; NADP; Oxidoreductase; Reference proteome. FT CHAIN 1..343 FT /note="Glyceraldehyde-3-phosphate dehydrogenase" FT /id="PRO_1000061116" FT ACT_SITE 140 FT /note="Nucleophile" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00559" FT BINDING 11..12 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00559" FT BINDING 110 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00559" FT BINDING 139..141 FT /ligand="D-glyceraldehyde 3-phosphate" FT /ligand_id="ChEBI:CHEBI:59776" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00559" FT BINDING 168 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00559" FT BINDING 194..195 FT /ligand="D-glyceraldehyde 3-phosphate" FT /ligand_id="ChEBI:CHEBI:59776" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00559" FT BINDING 301 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00559" SQ SEQUENCE 343 AA; 37403 MW; 5FC38818621545B8 CRC64; MIKVAINGYG TIGKRVADAV AAQKDMKVIG VSKTRPNAEA FIAKQRGYPL YIADLSKKAA FEKAGLTVAG SVEDMCKAAD VIVDATPGDI GVTNKPLYEK LGKKALWQGG EDHEVAGFSF NSSCNFKDAI GRQFIRVVSC NTTGLCRIIN EVDKAFGVEH VHAIMVRRGS DPGEIKKGPI DAVVLDPVTV PSHHGPDVQT VLPHISITTM AMIVPTTMMH MHAVRITTKK EVNREKVIEL IKNHPRLGLV KKSAGIKSTA ELKEFAMDLG RQRADLYENC IFEDSIYANK NELCFFQAIH QEADVVVENV DAIRAMTSLA NDGTASIKLT NDALHFVPIQ NNH //