ID   G3P_GLOMM               Reviewed;         333 AA.
AC   Q4U3L0;
DT   26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2005, sequence version 1.
DT   03-AUG-2022, entry version 69.
DE   RecName: Full=Glyceraldehyde-3-phosphate dehydrogenase;
DE            Short=GAPDH;
DE            EC=1.2.1.12;
GN   Name=Gapdh;
OS   Glossina morsitans morsitans (Savannah tsetse fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Hippoboscoidea;
OC   Glossinidae; Glossina.
OX   NCBI_TaxID=37546;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=16689795; DOI=10.1111/j.1365-2958.2006.05180.x;
RA   Hu C., Aksoy S.;
RT   "Innate immune responses regulate trypanosome parasite infection of the
RT   tsetse fly Glossina morsitans morsitans.";
RL   Mol. Microbiol. 60:1194-1204(2006).
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:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the glyceraldehyde-3-phosphate dehydrogenase
CC       family. {ECO:0000305}.
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DR   EMBL; DQ016434; AAY41178.1; -; mRNA.
DR   AlphaFoldDB; Q4U3L0; -.
DR   SMR; Q4U3L0; -.
DR   STRING; 37546.Q4U3L0; -.
DR   PRIDE; Q4U3L0; -.
DR   VEuPathDB; VectorBase:GMOY000473; -.
DR   PhylomeDB; Q4U3L0; -.
DR   UniPathway; UPA00109; UER00184.
DR   Proteomes; UP000092444; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0015630; C:microtubule cytoskeleton; ISS:UniProtKB.
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   2: Evidence at transcript level;
KW   Cytoplasm; Glycolysis; NAD; Oxidoreductase.
FT   CHAIN           1..333
FT                   /note="Glyceraldehyde-3-phosphate dehydrogenase"
FT                   /id="PRO_0000291647"
FT   ACT_SITE        149
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10009"
FT   BINDING         11..12
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         32
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         77
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         148..150
FT                   /ligand="D-glyceraldehyde 3-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:59776"
FT                   /evidence="ECO:0000250"
FT   BINDING         179
FT                   /ligand="D-glyceraldehyde 3-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:59776"
FT                   /evidence="ECO:0000250"
FT   BINDING         208..209
FT                   /ligand="D-glyceraldehyde 3-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:59776"
FT                   /evidence="ECO:0000250"
FT   BINDING         231
FT                   /ligand="D-glyceraldehyde 3-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:59776"
FT                   /evidence="ECO:0000250"
FT   BINDING         313
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   SITE            176
FT                   /note="Activates thiol group during catalysis"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   333 AA;  35663 MW;  25EEB473B1741327 CRC64;
     MSKIGINGFG RIGRLVLRAA LDKGAEVVAV NDPFIDVNYM VYLFKYDSTH GRFKGTVAAD
     GGFLVVNGKK ITVFCERDPT NINWASAGAE YIVESTGVFT TIDKASAHFK GGAKKVVISA
     PSADAPMFVC GVNLEAYSPD MKVVSNASCT TNCLAPLAKV IHDNFEIVEG LMTTVHATTA
     TQKTVDGPSG KLWRDGRGAA QNIIPASTGA AKAVGKVIPE LNGKLTGMAF RVPTPNVSVV
     DLTVRLGKSA TYDEIKAKVL EASQGPMKGI LDYTEEEVVS TDFVGDTHSS VFDAKAGIPL
     NDKFVKLISW YDNEFGYSNR VIDLIKYMQS KDA