G3P2_DROSU
ID G3P2_DROSU Reviewed; 304 AA.
AC O44105;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=Glyceraldehyde-3-phosphate dehydrogenase 2;
DE EC=1.2.1.12;
DE AltName: Full=Glyceraldehyde-3-phosphate dehydrogenase II;
DE Short=GAPDH II;
DE Flags: Fragment;
GN Name=Gapdh2;
OS Drosophila subobscura (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7241;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=9720289; DOI=10.1023/a:1017035109224;
RA Zeng L.-W., Comeron J.M., Chen B., Kreitman M.;
RT "The molecular clock revisited: the rate of synonymous vs. replacement
RT change in Drosophila.";
RL Genetica 102:369-382(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.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- SIMILARITY: Belongs to the glyceraldehyde-3-phosphate dehydrogenase
CC family. {ECO:0000305}.
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DR EMBL; AF025810; AAB87895.1; -; mRNA.
DR AlphaFoldDB; O44105; -.
DR SMR; O44105; -.
DR FlyBase; FBgn0012937; Dsub\Gapdh2.
DR UniPathway; UPA00109; UER00184.
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 2: Evidence at transcript level;
KW Cytoplasm; Glycolysis; NAD; Oxidoreductase.
FT CHAIN <1..>304
FT /note="Glyceraldehyde-3-phosphate dehydrogenase 2"
FT /id="PRO_0000145525"
FT ACT_SITE 139
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10009"
FT BINDING 1..2
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 22
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 67
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 138..140
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000250"
FT BINDING 169
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000250"
FT BINDING 198..199
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000250"
FT BINDING 221
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000250"
FT BINDING 303
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT SITE 166
FT /note="Activates thiol group during catalysis"
FT /evidence="ECO:0000250"
FT NON_TER 1
FT NON_TER 304
SQ SEQUENCE 304 AA; 32176 MW; 9BE9C70576089D1C CRC64;
RIGRLVLRAA IDKGASVVAV NDPFIDVNYM VYLFKFDSTH GRFKGTVVAE GGFLVVNGQK
ITVFSERDPA NINWASAGAE YVVESTGVFT TIEKASTHLK GGAKKVVISA PSADAPMFVC
GVNLDAYKPD MKVVSNASCT TNCLAPLAKV INDNFEIVEG LMTTVHATTA TQKTVDGPSG
KLWRDGRGAA QNIIPAATGA AKAVGKVIPA LNGKLTGMAF RVPTPNVSVV DLTVRLGKGA
SYDEIKAKVQ EAANGPLKGI LGYTDEEVVS TDFLSDTHSS VFDAKAGISL NDKFVKLISW
YDNE
