ID G3P_HOMAM Reviewed; 333 AA. AC P00357; DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot. DT 15-JUL-1999, sequence version 2. DT 02-SEP-2026, entry version 131. DE RecName: Full=Glyceraldehyde-3-phosphate dehydrogenase; DE Short=GAPDH; DE EC=1.2.1.12; OS Homarus americanus (American lobster). OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Altocrustacea; Communostraca; OC Malacostraca; Eumalacostraca; Stomatocarida; Decapoda; Pleocyemata; OC Astacidea; Nephropoidea; Nephropidae; Homarus. OX NCBI_TaxID=6706; RN [1] RP PROTEIN SEQUENCE, AND ACETYLATION AT SER-1. RX PubMed=4294736; DOI=10.1038/2161181a0; RA Davidson B.E., Sajgo M., Noller H.F., Harris J.I.; RT "Amino-acid sequence of glyceraldehyde 3-phosphate dehydrogenase from RT lobster muscle."; RL Nature 216:1181-1185(1967). RN [2] RP X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) IN COMPLEX WITH NAD AND INORGANIC RP PHOSPHATE, SUBUNIT, AND SEQUENCE REVISION TO 6. RX PubMed=127793; DOI=10.2210/pdb1gpd/pdb; RA Moras D., Olsen K.W., Sabesan M.N., Buehner M., Ford G.C., Rossmann M.G.; RT "Studies of asymmetry in the three-dimensional structure of lobster D- RT glyceraldehyde-3-phosphate dehydrogenase."; RL J. Biol. Chem. 250:9137-9162(1975). 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=1.2.1.12; CC Evidence={ECO:0000255|PROSITE-ProRule:PRU10009}; CC -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D- CC glyceraldehyde 3-phosphate: step 1/5. CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:127793}. CC -!- SUBCELLULAR LOCATION: Cytoplasm. 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 PIR; A00369; DELOG3. DR PDB; 1GPD; X-ray; 2.90 A; G/R=1-333. DR PDB; 4GPD; X-ray; 2.80 A; 1/2/3/4=1-333. DR AlphaFoldDB; P00357; -. DR SMR; P00357; -. DR iPTMnet; P00357; -. DR EnsemblMetazoa; XM_042356887.1; XP_042212821.1; LOC121859928. DR OrthoDB; 1152826at2759; -. DR UniPathway; UPA00109; UER00184. DR EvolutionaryTrace; P00357; -. DR GO; GO:0005829; C:cytosol; IEA:TreeGrafter. DR GO; GO:0004365; F:glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity; IEA:UniProtKB-EC. DR GO; GO:0051287; F:NAD binding; IEA:InterPro. DR GO; GO:0050661; F:NADP binding; IEA:InterPro. DR GO; GO:0006006; P:glucose metabolic process; IEA:InterPro. DR GO; GO:0019682; P:glyceraldehyde-3-phosphate metabolic process; IEA:UniProtKB-ARBA. DR GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-UniPathway. DR CDD; cd18126; GAPDH_I_C; 1. DR CDD; cd05214; GAPDH_I_N; 1. DR FunFam; 3.30.360.10:FF:000001; Glyceraldehyde-3-phosphate dehydrogenase; 1. DR FunFam; 3.40.50.720:FF:000266; Glyceraldehyde-3-phosphate dehydrogenase; 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 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; IPR006424; Glyceraldehyde-3-P_DH_1. DR InterPro; IPR036291; NAD(P)-bd_dom_sf. DR NCBIfam; TIGR01534; GAPDH-I; 1. DR PANTHER; PTHR10836; GLYCERALDEHYDE 3-PHOSPHATE DEHYDROGENASE; 1. DR PANTHER; PTHR10836:SF76; GLYCERALDEHYDE-3-PHOSPHATE DEHYDROGENASE-RELATED; 1. DR Pfam; PF02800; Gp_dh_C; 1. DR Pfam; PF00044; Gp_dh_N; 1. DR PIRSF; PIRSF000149; GAP_DH; 1. DR PRINTS; PR00078; G3PDHDRGNASE. 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. DR PDBsum; 1GPD; -. DR PDBsum; 4GPD; -. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Cytoplasm; Direct protein sequencing; KW Glycolysis; NAD; Oxidoreductase. FT CHAIN 1..333 FT /note="Glyceraldehyde-3-phosphate dehydrogenase" FT /id="PRO_0000145505" FT ACT_SITE 148 FT /note="Nucleophile" FT BINDING 10..11 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000269|PubMed:127793" FT BINDING 31 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000269|PubMed:127793" FT BINDING 118 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000269|PubMed:127793" FT BINDING 147..149 FT /ligand="D-glyceraldehyde 3-phosphate" FT /ligand_id="ChEBI:CHEBI:59776" FT /evidence="ECO:0000250" FT BINDING 178 FT /ligand="D-glyceraldehyde 3-phosphate" FT /ligand_id="ChEBI:CHEBI:59776" FT /evidence="ECO:0000250" FT BINDING 207..208 FT /ligand="D-glyceraldehyde 3-phosphate" FT /ligand_id="ChEBI:CHEBI:59776" FT /evidence="ECO:0000250" FT BINDING 230 FT /ligand="D-glyceraldehyde 3-phosphate" FT /ligand_id="ChEBI:CHEBI:59776" FT /evidence="ECO:0000250" FT BINDING 312 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000269|PubMed:127793" FT SITE 175 FT /note="Activates thiol group during catalysis" FT MOD_RES 1 FT /note="N-acetylserine" FT /evidence="ECO:0000269|PubMed:4294736" FT CONFLICT 6 FT /note="N -> D (in Ref. 1; AA sequence)" FT /evidence="ECO:0000305" FT STRAND 3..6 FT /evidence="ECO:0007829|PDB:1GPD" FT HELIX 10..14 FT /evidence="ECO:0007829|PDB:4GPD" FT HELIX 16..19 FT /evidence="ECO:0007829|PDB:4GPD" FT TURN 20..23 FT /evidence="ECO:0007829|PDB:4GPD" FT HELIX 36..44 FT /evidence="ECO:0007829|PDB:4GPD" FT STRAND 47..49 FT /evidence="ECO:0007829|PDB:4GPD" FT STRAND 56..59 FT /evidence="ECO:0007829|PDB:4GPD" FT STRAND 62..67 FT /evidence="ECO:0007829|PDB:4GPD" FT STRAND 68..70 FT /evidence="ECO:0007829|PDB:1GPD" FT HELIX 78..80 FT /evidence="ECO:0007829|PDB:4GPD" FT TURN 84..87 FT /evidence="ECO:0007829|PDB:1GPD" FT STRAND 90..93 FT /evidence="ECO:0007829|PDB:4GPD" FT STRAND 95..97 FT /evidence="ECO:0007829|PDB:4GPD" FT HELIX 101..105 FT /evidence="ECO:0007829|PDB:4GPD" FT HELIX 106..110 FT /evidence="ECO:0007829|PDB:4GPD" FT STRAND 114..119 FT /evidence="ECO:0007829|PDB:4GPD" FT STRAND 122..124 FT /evidence="ECO:0007829|PDB:4GPD" FT HELIX 129..135 FT /evidence="ECO:0007829|PDB:4GPD" FT STRAND 141..145 FT /evidence="ECO:0007829|PDB:1GPD" FT HELIX 148..164 FT /evidence="ECO:0007829|PDB:4GPD" FT STRAND 165..176 FT /evidence="ECO:0007829|PDB:4GPD" FT STRAND 179..181 FT /evidence="ECO:0007829|PDB:4GPD" FT TURN 189..191 FT /evidence="ECO:0007829|PDB:4GPD" FT HELIX 192..194 FT /evidence="ECO:0007829|PDB:4GPD" FT TURN 198..200 FT /evidence="ECO:0007829|PDB:4GPD" FT STRAND 203..207 FT /evidence="ECO:0007829|PDB:1GPD" FT HELIX 209..214 FT /evidence="ECO:0007829|PDB:4GPD" FT STRAND 217..223 FT /evidence="ECO:0007829|PDB:1GPD" FT STRAND 227..232 FT /evidence="ECO:0007829|PDB:4GPD" FT STRAND 237..247 FT /evidence="ECO:0007829|PDB:4GPD" FT HELIX 251..263 FT /evidence="ECO:0007829|PDB:4GPD" FT TURN 264..269 FT /evidence="ECO:0007829|PDB:4GPD" FT STRAND 283..285 FT /evidence="ECO:0007829|PDB:1GPD" FT STRAND 288..292 FT /evidence="ECO:0007829|PDB:4GPD" FT STRAND 298..300 FT /evidence="ECO:0007829|PDB:4GPD" FT STRAND 303..309 FT /evidence="ECO:0007829|PDB:4GPD" FT HELIX 314..331 FT /evidence="ECO:0007829|PDB:4GPD" SQ SEQUENCE 333 AA; 35716 MW; 6EEB5577D06D756A CRC64; SKIGINGFGR IGRLVLRAAL SCGAQVVAVN DPFIALEYMV YMFKYDSTHG VFKGEVKMED GALVVDGKKI TVFNEMKPEN IPWSKAGAEY IVESTGVFTT IEKASAHFKG GAKKVVISAP SADAPMFVCG VNLEKYSKDM TVVSNASCTT NCLAPVAKVL HENFEIVEGL MTTVHAVTAT QKTVDGPSAK DWRGGRGAAQ NIIPSSTGAA KAVGKVIPEL DGKLTGMAFR VPTPDVSVVD LTVRLGKECS YDDIKAAMKT ASEGPLQGFL GYTEDDVVSS DFIGDNRSSI FDAKAGIQLS KTFVKVVSWY DNEFGYSQRV IDLLKHMQKV DSA //