G3P_BRUMA
ID G3P_BRUMA Reviewed; 339 AA.
AC P48812;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=Glyceraldehyde-3-phosphate dehydrogenase;
DE Short=GAPDH;
DE EC=1.2.1.12;
GN Name=G3PD;
OS Brugia malayi (Filarial nematode worm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Spirurina; Spiruromorpha; Filarioidea; Onchocercidae; Brugia.
OX NCBI_TaxID=6279;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Scott A.L., Yenbutr P.;
RL Submitted (DEC-1994) to the EMBL/GenBank/DDBJ databases.
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.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- SIMILARITY: Belongs to the glyceraldehyde-3-phosphate dehydrogenase
CC family. {ECO:0000305}.
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DR EMBL; U18137; AAA57337.1; -; mRNA.
DR PDB; 4K9D; X-ray; 2.10 A; A/B/C/D/E/F/G/H=1-339.
DR PDBsum; 4K9D; -.
DR AlphaFoldDB; P48812; -.
DR SMR; P48812; -.
DR STRING; 6279.P48812; -.
DR UniPathway; UPA00109; UER00184.
DR Proteomes; UP000006672; Unassembled WGS sequence.
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; Cytoplasm; Glycolysis; NAD; Oxidoreductase;
KW Reference proteome.
FT CHAIN 1..339
FT /note="Glyceraldehyde-3-phosphate dehydrogenase"
FT /id="PRO_0000145507"
FT ACT_SITE 157
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10009"
FT BINDING 13..14
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 35
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 84
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 156..158
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000250"
FT BINDING 187
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000250"
FT BINDING 216..217
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000250"
FT BINDING 239
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000250"
FT BINDING 321
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT SITE 184
FT /note="Activates thiol group during catalysis"
FT /evidence="ECO:0000250"
FT STRAND 5..9
FT /evidence="ECO:0007829|PDB:4K9D"
FT HELIX 13..25
FT /evidence="ECO:0007829|PDB:4K9D"
FT STRAND 27..34
FT /evidence="ECO:0007829|PDB:4K9D"
FT HELIX 40..48
FT /evidence="ECO:0007829|PDB:4K9D"
FT TURN 51..53
FT /evidence="ECO:0007829|PDB:4K9D"
FT STRAND 57..63
FT /evidence="ECO:0007829|PDB:4K9D"
FT STRAND 66..70
FT /evidence="ECO:0007829|PDB:4K9D"
FT STRAND 75..81
FT /evidence="ECO:0007829|PDB:4K9D"
FT HELIX 86..88
FT /evidence="ECO:0007829|PDB:4K9D"
FT HELIX 91..94
FT /evidence="ECO:0007829|PDB:4K9D"
FT STRAND 98..101
FT /evidence="ECO:0007829|PDB:4K9D"
FT STRAND 103..105
FT /evidence="ECO:0007829|PDB:4K9D"
FT HELIX 109..112
FT /evidence="ECO:0007829|PDB:4K9D"
FT HELIX 114..117
FT /evidence="ECO:0007829|PDB:4K9D"
FT STRAND 121..127
FT /evidence="ECO:0007829|PDB:4K9D"
FT STRAND 130..132
FT /evidence="ECO:0007829|PDB:4K9D"
FT TURN 137..139
FT /evidence="ECO:0007829|PDB:4K9D"
FT HELIX 141..143
FT /evidence="ECO:0007829|PDB:4K9D"
FT TURN 146..148
FT /evidence="ECO:0007829|PDB:4K9D"
FT STRAND 150..153
FT /evidence="ECO:0007829|PDB:4K9D"
FT HELIX 157..173
FT /evidence="ECO:0007829|PDB:4K9D"
FT STRAND 175..185
FT /evidence="ECO:0007829|PDB:4K9D"
FT STRAND 190..194
FT /evidence="ECO:0007829|PDB:4K9D"
FT HELIX 201..204
FT /evidence="ECO:0007829|PDB:4K9D"
FT TURN 207..209
FT /evidence="ECO:0007829|PDB:4K9D"
FT STRAND 212..215
FT /evidence="ECO:0007829|PDB:4K9D"
FT HELIX 218..225
FT /evidence="ECO:0007829|PDB:4K9D"
FT HELIX 227..229
FT /evidence="ECO:0007829|PDB:4K9D"
FT TURN 230..232
FT /evidence="ECO:0007829|PDB:4K9D"
FT STRAND 233..241
FT /evidence="ECO:0007829|PDB:4K9D"
FT STRAND 246..256
FT /evidence="ECO:0007829|PDB:4K9D"
FT HELIX 260..272
FT /evidence="ECO:0007829|PDB:4K9D"
FT TURN 273..278
FT /evidence="ECO:0007829|PDB:4K9D"
FT STRAND 279..282
FT /evidence="ECO:0007829|PDB:4K9D"
FT HELIX 288..291
FT /evidence="ECO:0007829|PDB:4K9D"
FT STRAND 297..301
FT /evidence="ECO:0007829|PDB:4K9D"
FT HELIX 302..304
FT /evidence="ECO:0007829|PDB:4K9D"
FT STRAND 306..309
FT /evidence="ECO:0007829|PDB:4K9D"
FT STRAND 312..319
FT /evidence="ECO:0007829|PDB:4K9D"
FT HELIX 323..337
FT /evidence="ECO:0007829|PDB:4K9D"
SQ SEQUENCE 339 AA; 36155 MW; 01F9F8BFDE3F075E CRC64;
MSKPKVGING FGRIGRLVLR AAVEKDTVDV VAVNDPFINI DYMVYMFKYD STHGRFKGSV
SAEGGKLIVT NGKTTHHISV HNSKDPAEIP WGVDGAEYVV ESTGVFTTTD KASAHLKGGA
KKVIISAPSA DAPMFVMGVN NDMYDKANNH IISNASCTTN CLAPLAKVIH DKFGIIEGLM
TTVHATTATQ KTVDGPSGKL WRDGRGAGQN IIPASTGAAK AVGKVIPGLN GKLTGMANRV
PTPDVSVVDL TCRLQKGATM DEIKAAVKEA ANGPMKGILE YTEDQVVSTD FTGDTHSSIF
DSLACISLNP NFVKLIAWYD NEYGYSNRVV DLISYIASR
