ID   H2D2N2_9NEOP            Unreviewed;       149 AA.
AC   H2D2N2;
DT   21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT   21-MAR-2012, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   SubName: Full=Glyceraldhyde-3-phosphate dehydrogenase {ECO:0000313|EMBL:AEY63530.1};
DE   Flags: Fragment;
GN   Name=GAPDH {ECO:0000313|EMBL:AEY63530.1};
OS   Peridrome orbicularis.
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Noctuoidea;
OC   Erebidae; Aganainae; Peridrome.
OX   NCBI_TaxID=1126784 {ECO:0000313|EMBL:AEY63530.1};
RN   [1] {ECO:0000313|EMBL:AEY63530.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Zahiri R., Holloway J.D., Kitching I.J., Lafontaine J.D., Mutanen M.,
RA   Wahlberg N.;
RT   "Molecular phylogenetics of Erebidae (Lepidoptera, Noctuoidea).";
RL   Syst. Entomol. 37:102-124(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}.
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DR   EMBL; JN401607; AEY63530.1; -; Genomic_DNA.
DR   AlphaFoldDB; H2D2N2; -.
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   InterPro; IPR020831; GlycerAld/Erythrose_P_DH.
DR   InterPro; IPR020829; GlycerAld_3-P_DH_cat.
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   SUPFAM; SSF55347; Glyceraldehyde-3-phosphate dehydrogenase-like, C-terminal domain; 1.
PE   3: Inferred from homology;
KW   NAD {ECO:0000256|ARBA:ARBA00023027};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT   DOMAIN          6..148
FT                   /note="Glyceraldehyde 3-phosphate dehydrogenase catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF02800"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:AEY63530.1"
FT   NON_TER         149
FT                   /evidence="ECO:0000313|EMBL:AEY63530.1"
SQ   SEQUENCE   149 AA;  15509 MW;  065A6EBC836D4BB0 CRC64;
     CTTNCLAPLA KVIHDNFEIV EGLMTTVHAT TATQKTVDGP SGKLWRDGRG AQQNIIPAST
     GAAKAVGKVI PALTGKLTGM AFRVPVANVS VVDLTVRLGK PASYDAFKLK VKEAAEGPLK
     GILDYTEEQV VSSDFIGDAH SSIFDAAAG
//