ID G3P_METMJ Reviewed; 341 AA.
AC A3CYG8;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 20-MAR-2007, sequence version 1.
DT 27-MAR-2024, entry version 101.
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}; OrderedLocusNames=Memar_2497;
OS Methanoculleus marisnigri (strain ATCC 35101 / DSM 1498 / JR1).
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanomicrobiales; Methanomicrobiaceae; Methanoculleus.
OX NCBI_TaxID=368407;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35101 / DSM 1498 / JR1;
RX PubMed=21304656; DOI=10.4056/sigs.32535;
RA Anderson I.J., Sieprawska-Lupa M., Lapidus A., Nolan M., Copeland A.,
RA Glavina Del Rio T., Tice H., Dalin E., Barry K., Saunders E., Han C.,
RA Brettin T., Detter J.C., Bruce D., Mikhailova N., Pitluck S., Hauser L.,
RA Land M., Lucas S., Richardson P., Whitman W.B., Kyrpides N.C.;
RT "Complete genome sequence of Methanoculleus marisnigri Romesser et al. 1981
RT type strain JR1.";
RL Stand. Genomic Sci. 1:189-196(2009).
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:0000255|HAMAP-Rule:MF_00559};
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: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}.
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DR EMBL; CP000562; ABN58418.1; -; Genomic_DNA.
DR RefSeq; WP_011845327.1; NC_009051.1.
DR AlphaFoldDB; A3CYG8; -.
DR SMR; A3CYG8; -.
DR STRING; 368407.Memar_2497; -.
DR GeneID; 76730578; -.
DR KEGG; mem:Memar_2497; -.
DR eggNOG; arCOG00493; Archaea.
DR HOGENOM; CLU_069533_0_0_2; -.
DR OrthoDB; 295712at2157; -.
DR UniPathway; UPA00109; UER00184.
DR Proteomes; UP000002146; 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:InterPro.
DR GO; GO:0050661; F:NADP binding; IEA:InterPro.
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; 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.
PE 3: Inferred from homology;
KW Cytoplasm; Glycolysis; NAD; NADP; Oxidoreductase.
FT CHAIN 1..341
FT /note="Glyceraldehyde-3-phosphate dehydrogenase"
FT /id="PRO_0000300973"
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 302
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00559"
SQ SEQUENCE 341 AA; 37212 MW; FBFCE0F69EA81953 CRC64;
MIKVAINGYG TIGKRVADAV AAQPDMEVIG VSKTSVSAEA YIAKERGYPL YIADLGKKPA
FEKAGIEVAG DVEAMLKAAD IVVDATPGGV GEKNRPIYEK LGKKAIFQGG EDHEVAGFSF
NAHANYNEAE NHQFARVVSC NSTGLVRIIH ALDQAFGVAR VRAVMVRRGA DPDDVKRGPI
DAIVLNPASI PSHHGPDVNT VLPHINIVTL AMIVPTTFMH MHSIQMDLKK ETTREEVLKV
FENHSRIGLV RKTMGIKSNA QLREYTQDLG RPRTDLWENG VFEESVSILD GKEFYCFQAI
HQEADVVPEN IDCIRALMGT VKDPQESIRM TNEALGLVAI G
//
