G3P_PANVR
ID G3P_PANVR Reviewed; 333 AA.
AC P56649;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 15-JUL-1999, sequence version 1.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=Glyceraldehyde-3-phosphate dehydrogenase;
DE Short=GAPDH;
DE EC=1.2.1.12;
OS Panulirus versicolor (Painted spiny lobster) (Palinurus versicolor).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Crustacea; Multicrustacea;
OC Malacostraca; Eumalacostraca; Eucarida; Decapoda; Pleocyemata; Achelata;
OC Palinuroidea; Palinuridae; Panulirus.
OX NCBI_TaxID=150436;
RN [1]
RP X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS).
RX PubMed=8470893; DOI=10.1006/abbi.1993.1194;
RA Lin Z.J., Li J., Zhang F.M., Song S.Y., Yang J., Liang S.J., Tsou C.L.;
RT "Structure of D-glyceraldehyde-3-phosphate dehydrogenase from Palinurus
RT versicolor carrying the fluorescent NAD derivatives at 2.7-A resolution.";
RL Arch. Biochem. Biophys. 302:161-166(1993).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.88 ANGSTROMS) IN COMPLEX WITH NAD.
RC TISSUE=Muscle;
RX PubMed=9761850; DOI=10.1107/s090744499701620x;
RA Song S.Y., Li J., Lin Z.J.;
RT "Structure of holo-glyceraldehyde-3-phosphate dehydrogenase from Palinurus
RT versicolor refined at 2-A resolution.";
RL Acta Crystallogr. D 54:558-569(1998).
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:9761850}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- SIMILARITY: Belongs to the glyceraldehyde-3-phosphate dehydrogenase
CC family. {ECO:0000305}.
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DR PDB; 1CRW; X-ray; 2.00 A; G/R=1-333.
DR PDB; 1DSS; X-ray; 1.88 A; G/R=1-333.
DR PDB; 1IHX; X-ray; 2.80 A; A/B/C/D=1-333.
DR PDB; 1IHY; X-ray; 3.00 A; A/B/C/D=1-333.
DR PDB; 1SZJ; X-ray; 2.00 A; G/R=1-333.
DR PDBsum; 1CRW; -.
DR PDBsum; 1DSS; -.
DR PDBsum; 1IHX; -.
DR PDBsum; 1IHY; -.
DR PDBsum; 1SZJ; -.
DR AlphaFoldDB; P56649; -.
DR SMR; P56649; -.
DR PRIDE; P56649; -.
DR BRENDA; 1.2.1.12; 4494.
DR SABIO-RK; P56649; -.
DR UniPathway; UPA00109; UER00184.
DR EvolutionaryTrace; P56649; -.
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; Glycolysis; NAD; Oxidoreductase.
FT CHAIN 1..333
FT /note="Glyceraldehyde-3-phosphate dehydrogenase"
FT /id="PRO_0000145506"
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:9761850"
FT BINDING 31
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:9761850"
FT BINDING 76
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
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:9761850"
FT SITE 175
FT /note="Activates thiol group during catalysis"
FT MOD_RES 1
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:P00357"
FT STRAND 3..6
FT /evidence="ECO:0007829|PDB:1DSS"
FT HELIX 10..22
FT /evidence="ECO:0007829|PDB:1DSS"
FT STRAND 26..30
FT /evidence="ECO:0007829|PDB:1DSS"
FT STRAND 32..34
FT /evidence="ECO:0007829|PDB:1CRW"
FT HELIX 36..44
FT /evidence="ECO:0007829|PDB:1DSS"
FT TURN 47..49
FT /evidence="ECO:0007829|PDB:1DSS"
FT STRAND 56..59
FT /evidence="ECO:0007829|PDB:1DSS"
FT STRAND 62..65
FT /evidence="ECO:0007829|PDB:1DSS"
FT STRAND 68..73
FT /evidence="ECO:0007829|PDB:1DSS"
FT HELIX 78..80
FT /evidence="ECO:0007829|PDB:1DSS"
FT HELIX 83..86
FT /evidence="ECO:0007829|PDB:1DSS"
FT STRAND 90..93
FT /evidence="ECO:0007829|PDB:1DSS"
FT STRAND 95..97
FT /evidence="ECO:0007829|PDB:1DSS"
FT HELIX 101..104
FT /evidence="ECO:0007829|PDB:1DSS"
FT HELIX 105..108
FT /evidence="ECO:0007829|PDB:1DSS"
FT TURN 109..111
FT /evidence="ECO:0007829|PDB:1DSS"
FT STRAND 113..119
FT /evidence="ECO:0007829|PDB:1DSS"
FT STRAND 122..124
FT /evidence="ECO:0007829|PDB:1DSS"
FT TURN 129..131
FT /evidence="ECO:0007829|PDB:1DSS"
FT HELIX 133..135
FT /evidence="ECO:0007829|PDB:1DSS"
FT STRAND 142..144
FT /evidence="ECO:0007829|PDB:1DSS"
FT HELIX 148..164
FT /evidence="ECO:0007829|PDB:1DSS"
FT STRAND 166..175
FT /evidence="ECO:0007829|PDB:1DSS"
FT STRAND 181..185
FT /evidence="ECO:0007829|PDB:1DSS"
FT HELIX 193..195
FT /evidence="ECO:0007829|PDB:1DSS"
FT TURN 198..200
FT /evidence="ECO:0007829|PDB:1DSS"
FT STRAND 203..205
FT /evidence="ECO:0007829|PDB:1DSS"
FT HELIX 209..216
FT /evidence="ECO:0007829|PDB:1DSS"
FT HELIX 218..220
FT /evidence="ECO:0007829|PDB:1DSS"
FT TURN 221..223
FT /evidence="ECO:0007829|PDB:1DSS"
FT STRAND 224..230
FT /evidence="ECO:0007829|PDB:1DSS"
FT STRAND 237..247
FT /evidence="ECO:0007829|PDB:1DSS"
FT HELIX 251..263
FT /evidence="ECO:0007829|PDB:1DSS"
FT TURN 264..269
FT /evidence="ECO:0007829|PDB:1DSS"
FT STRAND 270..273
FT /evidence="ECO:0007829|PDB:1DSS"
FT HELIX 279..282
FT /evidence="ECO:0007829|PDB:1DSS"
FT STRAND 288..292
FT /evidence="ECO:0007829|PDB:1DSS"
FT TURN 293..295
FT /evidence="ECO:0007829|PDB:1DSS"
FT STRAND 297..300
FT /evidence="ECO:0007829|PDB:1DSS"
FT STRAND 303..310
FT /evidence="ECO:0007829|PDB:1DSS"
FT HELIX 314..331
FT /evidence="ECO:0007829|PDB:1DSS"
SQ SEQUENCE 333 AA; 35724 MW; 818572106E294C19 CRC64;
SKIGINGFGR IGRLVLRAAL EMGAQVVAVN DPFIALEYMV YMFKYDSTHG MFKGEVKAED
GALVVDGKKI TVFNEMKPEN IPWSKAGAEY IVESTGVFTT IEKASAHFKG GAKKVIISAP
SADAPMFVCG VNLEKYSKDM KVVSNASCTT NCLAPVAKVL HENFEIVEGL MTTVHAVTAT
QKTVDGPSAK DWRGGRGAAQ NIIPSSTGAA KAVGKVIPEL DGKLTGMAFR VPTPNVSVVD
LTVRLGKECS YDDIKAAMKA ASEGPLQGVL GYTEDDVVSC DFTGDNRSSI FDAKAGIQLS
KTFVKVVSWY DNEFGYSQRV IDLIKHMQKV DSA
