G3P_HOMAM
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 03-AUG-2022, entry version 121.
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; Crustacea; Multicrustacea;
OC Malacostraca; Eumalacostraca; Eucarida; Decapoda; Pleocyemata; Astacidea;
OC 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 + 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=1.2.1.12;
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}.
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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 PDBsum; 1GPD; -.
DR PDBsum; 4GPD; -.
DR AlphaFoldDB; P00357; -.
DR SMR; P00357; -.
DR iPTMnet; P00357; -.
DR PRIDE; P00357; -.
DR UniPathway; UPA00109; UER00184.
DR EvolutionaryTrace; P00357; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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:0006096; P:glycolytic process; IEA:UniProtKB-UniPathway.
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 PANTHER; PTHR10836; PTHR10836; 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; SSF51735; SSF51735; 1.
DR TIGRFAMs; TIGR01534; GAPDH-I; 1.
DR PROSITE; PS00071; GAPDH; 1.
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:4GPD"
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 HELIX 192..194
FT /evidence="ECO:0007829|PDB:4GPD"
FT STRAND 197..200
FT /evidence="ECO:0007829|PDB:1GPD"
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
