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Database: UniProt
Entry: E2EHU7_9NEOP
LinkDB: E2EHU7_9NEOP
Original site: E2EHU7_9NEOP 
ID   E2EHU7_9NEOP            Unreviewed;       214 AA.
AC   E2EHU7;
DT   30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT   30-NOV-2010, sequence version 1.
DT   24-JAN-2024, entry version 32.
DE   RecName: Full=glyceraldehyde-3-phosphate dehydrogenase (phosphorylating) {ECO:0000256|ARBA:ARBA00013119};
DE            EC=1.2.1.12 {ECO:0000256|ARBA:ARBA00013119};
DE   Flags: Fragment;
GN   Name=GAPDH {ECO:0000313|EMBL:ADN82758.1};
OS   Bucculatrix maritima.
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Tineoidea;
OC   Bucculatricidae; Bucculatrix.
OX   NCBI_TaxID=753138 {ECO:0000313|EMBL:ADN82758.1};
RN   [1] {ECO:0000313|EMBL:ADN82758.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=20444718; DOI=10.1098/rspb.2010.0392;
RA   Mutanen M., Wahlberg N., Kaila L.;
RT   "Comprehensive gene and taxon coverage elucidates radiation patterns in
RT   moths and butterflies.";
RL   Proc. R. Soc. B 277:2839-2848(2010).
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   -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
CC       glyceraldehyde 3-phosphate: step 1/5. {ECO:0000256|ARBA:ARBA00004869}.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000256|ARBA:ARBA00011881}.
CC   -!- SIMILARITY: Belongs to the glyceraldehyde-3-phosphate dehydrogenase
CC       family. {ECO:0000256|ARBA:ARBA00007406}.
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DR   EMBL; GU829901; ADN82758.1; -; Genomic_DNA.
DR   AlphaFoldDB; E2EHU7; -.
DR   GO; GO:0016620; F:oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor; IEA:InterPro.
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; 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   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   Glycolysis {ECO:0000256|ARBA:ARBA00023152};
KW   NAD {ECO:0000256|ARBA:ARBA00023027};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT   DOMAIN          46..203
FT                   /note="Glyceraldehyde 3-phosphate dehydrogenase catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF02800"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:ADN82758.1"
FT   NON_TER         214
FT                   /evidence="ECO:0000313|EMBL:ADN82758.1"
SQ   SEQUENCE   214 AA;  22609 MW;  D2135E32CD88C339 CRC64;
     LEGGAKKVII SAPSADAPMF VVGVNLESYD PSHKVISNAS CTTNCLAPLA KVIHDNFEII
     EGLMTTVHAT TATQKTVDGP SGKLWRDGRG AQQNIIPAST GAAKAVGKVI PALNGKLTGM
     AFRVPVPNVS VVDLTVRLGK PATYDAIKQK VKEASEGPMK GILGYTEDQV VSTDFVGDTH
     SSIFDAAAGI SLNDNFVKLI SWYDNEYGYS SRVI
//
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