ID   J7JQ43_9NEOP            Unreviewed;       230 AA.
AC   J7JQ43;
DT   31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   31-OCT-2012, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   SubName: Full=Glyceraldhyde-3-phosphate dehydrogenase {ECO:0000313|EMBL:AFQ55333.1};
DE   Flags: Fragment;
GN   Name=GAPDH {ECO:0000313|EMBL:AFQ55333.1};
OS   Hemerophila sp. 2 JR-2011.
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Sesioidea;
OC   Choreutidae; Choreutinae; Hemerophila.
OX   NCBI_TaxID=1001003 {ECO:0000313|EMBL:AFQ55333.1};
RN   [1] {ECO:0000313|EMBL:AFQ55333.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Rota J., Wahlberg N.;
RT   "Exploration of data partitioning in an eight-gene dataset: phylogeny of
RT   metalmark moths (Lepidoptera, Choreutidae).";
RL   Zool. Scr. 41:536-546(2012).
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:0000256|ARBA:ARBA00001810};
CC   -!- SIMILARITY: Belongs to the glyceraldehyde-3-phosphate dehydrogenase
CC       family. {ECO:0000256|ARBA:ARBA00007406}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; JQ958444; AFQ55333.1; -; Genomic_DNA.
DR   AlphaFoldDB; J7JQ43; -.
DR   GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR   GO; GO:0016620; F:oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor; IEA:InterPro.
DR   GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
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; IPR036291; NAD(P)-bd_dom_sf.
DR   PANTHER; PTHR10836; GLYCERALDEHYDE 3-PHOSPHATE DEHYDROGENASE; 1.
DR   PANTHER; PTHR10836:SF76; GLYCERALDEHYDE-3-PHOSPHATE DEHYDROGENASE-RELATED; 1.
DR   Pfam; PF02800; Gp_dh_C; 1.
DR   PRINTS; PR00078; G3PDHDRGNASE.
DR   SMART; SM00846; Gp_dh_N; 1.
DR   SUPFAM; SSF55347; Glyceraldehyde-3-phosphate dehydrogenase-like, C-terminal domain; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR   PROSITE; PS00071; GAPDH; 1.
PE   3: Inferred from homology;
KW   NAD {ECO:0000256|ARBA:ARBA00023027};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT   DOMAIN          1..57
FT                   /note="Glyceraldehyde 3-phosphate dehydrogenase NAD(P)
FT                   binding"
FT                   /evidence="ECO:0000259|SMART:SM00846"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:AFQ55333.1"
FT   NON_TER         230
FT                   /evidence="ECO:0000313|EMBL:AFQ55333.1"
SQ   SEQUENCE   230 AA;  24147 MW;  77114F811D7E1EB0 CRC64;
     IESTGVFTTI DKASAHLEGG AKKVIISAPS ADAPMFVVGV NLESYDPSHK VISNASCTTN
     CLAPLAKVIH DNFEIVEGLM TTVHATTATQ KTVDGPSGKL WRDGRGAQQN IIPAATGAAK
     AVGKVIPALN GKLTGMAFRV PVANVSVVDL TVRLGKPASY DAIKQKVKEA AEGPLKGILG
     YTEDQVVSSD FIGDTHSSIF DAAAGISLND NFVKLISWYD NEFGYSSRVI
//