G3PC_TRYBB
ID G3PC_TRYBB Reviewed; 331 AA.
AC P10097;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Glyceraldehyde-3-phosphate dehydrogenase, cytosolic;
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 [GENOMIC DNA].
RC STRAIN=427;
RX PubMed=2040303; DOI=10.1111/j.1432-1033.1991.tb16031.x;
RA Michels P.A.M., Marchand M., Kohl L., Allert S., Wierenga R.K.,
RA Opperdoes F.R.;
RT "The cytosolic and glycosomal isoenzymes of glyceraldehyde-3-phosphate
RT dehydrogenase in Trypanosoma brucei have a distant evolutionary
RT relationship.";
RL Eur. J. Biochem. 198:421-428(1991).
RN [2]
RP PRELIMINARY PROTEIN SEQUENCE OF 2-86.
RX PubMed=3830153; DOI=10.1111/j.1432-1033.1987.tb10668.x;
RA Misset O., van Beeumen J., Lambeir A.-M., van der Meer R., Opperdoes F.R.;
RT "Glyceraldehyde-phosphate dehydrogenase from Trypanosoma brucei. Comparison
RT of the glycosomal and cytosolic isoenzymes.";
RL Eur. J. Biochem. 162:501-507(1987).
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; X53472; CAA37568.1; -; Genomic_DNA.
DR PIR; S16091; DEUTGC.
DR AlphaFoldDB; P10097; -.
DR SMR; P10097; -.
DR SABIO-RK; P10097; -.
DR UniPathway; UPA00109; UER00184.
DR GO; GO:0005737; C:cytoplasm; IDA:GeneDB.
DR GO; GO:0005829; C:cytosol; TAS:GeneDB.
DR GO; GO:0004365; F:glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity; ISM:GeneDB.
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 Cytoplasm; Direct protein sequencing; Glycolysis; NAD; Oxidoreductase.
FT INIT_MET 1
FT /note="Removed"
FT CHAIN 2..331
FT /note="Glyceraldehyde-3-phosphate dehydrogenase, cytosolic"
FT /id="PRO_0000145530"
FT ACT_SITE 150
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:0000250"
FT BINDING 34
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 78
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 149..151
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000250"
FT BINDING 180
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000250"
FT BINDING 209..210
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000250"
FT BINDING 232
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000250"
FT BINDING 314
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT SITE 177
FT /note="Activates thiol group during catalysis"
FT /evidence="ECO:0000250"
FT VARIANT 73
FT /note="R -> I"
FT CONFLICT 57
FT /note="A -> T (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 61
FT /note="Q -> K (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 331 AA; 35635 MW; 4F754ECE9D1A3D1C CRC64;
MVIRVGINGF GRIGRVVFRA AQRRNDIEIV GINDLLDADY MAYMLKYDST HGRFEGAVEV
QGGALVVNGK KIRVTSERDP ANLKWNEINV DVVVESTGLF LSDDTARKHI QAGAKKVVIT
GPSKDDTPMF VMGVNHTTYK GEAIVSNASC TTNCLAPLAK VLNDKFGIVE GLMTTVHATT
ATQKTVDGPS QKDWRGGRGA AQNIIPSSTG AAKAVGKIIP SLNGKLTGMA FRVPTPNVSV
VDLTVRLERP ATYKQICDAI KAASEGELKG ILGYVDEEIV SSDINGIPLT SVFDARAGIS
LNDNFVKLVS WYDNETGYSN KVHDLIAHIT K
