ID   G3P_METBR               Reviewed;         338 AA.
AC   P19314;
DT   01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 2.
DT   04-NOV-2026, entry version 119.
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;
OS   Methanobacterium bryantii.
OC   Archaea; Methanobacteriati; Methanobacteriota; Methanomada group;
OC   Methanobacteria; Methanobacteriales; Methanobacteriaceae; Methanobacterium.
OX   NCBI_TaxID=2161;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=DSM 862;
RX   PubMed=2492940; DOI=10.1111/j.1432-1033.1989.tb14568.x;
RA   Fabry S., Lang J., Niermann T., Vingron M., Hensel R.;
RT   "Nucleotide sequence of the glyceraldehyde-3-phosphate dehydrogenase gene
RT   from the mesophilic methanogenic archaebacteria Methanobacterium bryantii
RT   and Methanobacterium formicicum. Comparison with the respective gene
RT   structure of the closely related extreme thermophile Methanothermus
RT   fervidus.";
RL   Eur. J. Biochem. 179:405-413(1989).
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   -!- 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   -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
CC       glyceraldehyde 3-phosphate: step 1/5.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the glyceraldehyde-3-phosphate dehydrogenase
CC       family. {ECO:0000305}.
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DR   EMBL; X14631; CAA32780.1; -; Genomic_DNA.
DR   PIR; S02804; S02804.
DR   AlphaFoldDB; P19314; -.
DR   SMR; P19314; -.
DR   UniPathway; UPA00109; UER00184.
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   GO; GO:0009085; P:L-lysine biosynthetic process; IEA:InterPro.
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.
FT   CHAIN           1..338
FT                   /note="Glyceraldehyde-3-phosphate dehydrogenase"
FT                   /id="PRO_0000145720"
FT   ACT_SITE        141
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   BINDING         11..12
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         169
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         195..196
FT                   /ligand="D-glyceraldehyde 3-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:59776"
FT                   /evidence="ECO:0000250"
FT   BINDING         302
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   338 AA;  37013 MW;  6E8B7529688D63A5 CRC64;
     MKSVGINGYG TIGKRVADAV SAQDDMKIVG VTKRSPDFEA RMAVENGYDL YISVPERESS
     FEEAGIKVTG TADELLEKLD IVVDCTPEGI GAKNKEGTYE KMGLKAIFQG GEKHDQIGLS
     FNSFSNYNDV IGKDYARVVS CNTTGLCRTL NPINDLCGIK KVRAVMVRRG ADPGQVKKGP
     INAIVPNPPT VPSHHGPDVQ TVMYDLNITT MALLVPTTLM HQHNLMVELE SSVSVDDIKE
     KLNETPRVLL LKAGEGLTST AGFMEYAKDL GRSRNDLFEI GVWEESLNIV DGELYYMQAI
     HQESDVVPEN VDAIRAMLEM ENDPSKSIQK TNKAMGIL
//