G3PG_TRYBB
ID G3PG_TRYBB Reviewed; 359 AA.
AC P22512;
DT 01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Glyceraldehyde-3-phosphate dehydrogenase, glycosomal;
DE Short=GAPDH;
DE EC=1.2.1.12;
OS Trypanosoma brucei brucei.
OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC Trypanosomatida; Trypanosomatidae; Trypanosoma.
OX NCBI_TaxID=5702;
RN [1]
RP NUCLEOTIDE SEQUENCE, AND PROTEIN SEQUENCE OF 2-53.
RC STRAIN=427;
RX PubMed=3013612; DOI=10.1002/j.1460-2075.1986.tb04321.x;
RA Michels P.A.M., Poliszczak A., Osinga K.A., Misset O., van Beeumen J.,
RA Wiegenga R.K., Borst P., Opperdoes F.R.;
RT "Two tandemly linked identical genes code for the glycosomal
RT glyceraldehyde-phosphate dehydrogenase in Trypanosoma brucei.";
RL EMBO J. 5:1049-1056(1986).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS) IN COMPLEX WITH NAD, AND SUBUNIT.
RX PubMed=8460146; DOI=10.1073/pnas.90.6.2355;
RA Vellieux F.M., Hajdu J., Verlinde C.L., Groendijk H., Read R.J.,
RA Greenhough T.J., Campbell J.W., Kalk K.H., Littlechild J.A., Watson H.C.;
RT "Structure of glycosomal glyceraldehyde-3-phosphate dehydrogenase from
RT Trypanosoma brucei determined from Laue data.";
RL Proc. Natl. Acad. Sci. U.S.A. 90:2355-2359(1993).
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:8460146}.
CC -!- SUBCELLULAR LOCATION: Glycosome.
CC -!- MISCELLANEOUS: There are two identical genes that code for glycosomal
CC GAPDH.
CC -!- SIMILARITY: Belongs to the glyceraldehyde-3-phosphate dehydrogenase
CC family. {ECO:0000305}.
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DR EMBL; X59955; CAA42576.1; -; Genomic_DNA.
DR EMBL; X59955; CAA42577.1; -; Genomic_DNA.
DR EMBL; M26816; AAA30198.1; -; mRNA.
DR PIR; S18806; DEUT1B.
DR PDB; 2X0N; X-ray; 3.20 A; A/B/O/P/Q/R=1-359.
DR PDB; 3CVN; X-ray; 2.00 A; B=353-359.
DR PDBsum; 2X0N; -.
DR PDBsum; 3CVN; -.
DR AlphaFoldDB; P22512; -.
DR SMR; P22512; -.
DR PRIDE; P22512; -.
DR SABIO-RK; P22512; -.
DR UniPathway; UPA00109; UER00184.
DR EvolutionaryTrace; P22512; -.
DR GO; GO:0020015; C:glycosome; 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; Direct protein sequencing; Glycolysis; Glycosome; NAD;
KW Oxidoreductase; Peroxisome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:3013612"
FT CHAIN 2..359
FT /note="Glyceraldehyde-3-phosphate dehydrogenase,
FT glycosomal"
FT /id="PRO_0000145531"
FT MOTIF 357..359
FT /note="Microbody targeting signal"
FT /evidence="ECO:0000255"
FT ACT_SITE 166
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10009"
FT BINDING 12..13
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:8460146"
FT BINDING 38
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:8460146"
FT BINDING 91
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:8460146"
FT BINDING 165..167
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000250"
FT BINDING 197
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000250"
FT BINDING 226..227
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000250"
FT BINDING 249
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000250"
FT BINDING 335
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:8460146"
FT SITE 194
FT /note="Activates thiol group during catalysis"
FT /evidence="ECO:0000250"
FT STRAND 3..9
FT /evidence="ECO:0007829|PDB:2X0N"
FT HELIX 13..23
FT /evidence="ECO:0007829|PDB:2X0N"
FT TURN 28..30
FT /evidence="ECO:0007829|PDB:2X0N"
FT STRAND 31..39
FT /evidence="ECO:0007829|PDB:2X0N"
FT HELIX 43..51
FT /evidence="ECO:0007829|PDB:2X0N"
FT TURN 54..56
FT /evidence="ECO:0007829|PDB:2X0N"
FT STRAND 68..71
FT /evidence="ECO:0007829|PDB:2X0N"
FT STRAND 77..80
FT /evidence="ECO:0007829|PDB:2X0N"
FT STRAND 83..89
FT /evidence="ECO:0007829|PDB:2X0N"
FT HELIX 94..96
FT /evidence="ECO:0007829|PDB:2X0N"
FT HELIX 99..102
FT /evidence="ECO:0007829|PDB:2X0N"
FT STRAND 106..109
FT /evidence="ECO:0007829|PDB:2X0N"
FT STRAND 111..113
FT /evidence="ECO:0007829|PDB:2X0N"
FT HELIX 117..120
FT /evidence="ECO:0007829|PDB:2X0N"
FT HELIX 122..125
FT /evidence="ECO:0007829|PDB:2X0N"
FT STRAND 130..135
FT /evidence="ECO:0007829|PDB:2X0N"
FT STRAND 138..140
FT /evidence="ECO:0007829|PDB:2X0N"
FT TURN 146..148
FT /evidence="ECO:0007829|PDB:2X0N"
FT TURN 155..157
FT /evidence="ECO:0007829|PDB:2X0N"
FT STRAND 159..162
FT /evidence="ECO:0007829|PDB:2X0N"
FT HELIX 166..180
FT /evidence="ECO:0007829|PDB:2X0N"
FT STRAND 186..194
FT /evidence="ECO:0007829|PDB:2X0N"
FT STRAND 202..204
FT /evidence="ECO:0007829|PDB:2X0N"
FT HELIX 212..214
FT /evidence="ECO:0007829|PDB:2X0N"
FT HELIX 217..219
FT /evidence="ECO:0007829|PDB:2X0N"
FT STRAND 222..225
FT /evidence="ECO:0007829|PDB:2X0N"
FT HELIX 228..235
FT /evidence="ECO:0007829|PDB:2X0N"
FT HELIX 237..239
FT /evidence="ECO:0007829|PDB:2X0N"
FT STRAND 242..249
FT /evidence="ECO:0007829|PDB:2X0N"
FT STRAND 256..263
FT /evidence="ECO:0007829|PDB:2X0N"
FT HELIX 270..282
FT /evidence="ECO:0007829|PDB:2X0N"
FT TURN 283..288
FT /evidence="ECO:0007829|PDB:2X0N"
FT STRAND 289..292
FT /evidence="ECO:0007829|PDB:2X0N"
FT HELIX 298..301
FT /evidence="ECO:0007829|PDB:2X0N"
FT STRAND 307..311
FT /evidence="ECO:0007829|PDB:2X0N"
FT HELIX 312..316
FT /evidence="ECO:0007829|PDB:2X0N"
FT STRAND 324..333
FT /evidence="ECO:0007829|PDB:2X0N"
FT HELIX 337..353
FT /evidence="ECO:0007829|PDB:2X0N"
SQ SEQUENCE 359 AA; 39038 MW; DB0C62911A7D162C CRC64;
MTIKVGINGF GRIGRMVFQA LCDDGLLGNE IDVVAVVDMN TDARYFAYQM KYDSVHGKFK
HSVSTTKSKP SVAKDDTLVV NGHRILCVKA QRNPADLPWG KLGVEYVIES TGLFTVKSAA
EGHLRGGARK VVISAPASGG AKTFVMGVNH NNYNPREQHV VSNASCTTNC LAPLVHVLVK
EGFGISTGLM TTVHSYTATQ KTVDGVSVKD WRGGRAAALN IIPSTTGAAK AVGMVIPSTQ
GKLTGMAFRV PTADVSVVDL TFIATRDTSI KEIDAALKRA SKTYMKNILG YTDEELVSAD
FISDSRSSIY DSKATLQNNL PNERRFFKIV SWYDNEWGYS HRVVDLVRHM AARDRAAKL
