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Database: UniProt
Entry: D3J6M6_9NEOP
LinkDB: D3J6M6_9NEOP
Original site: D3J6M6_9NEOP 
ID   D3J6M6_9NEOP            Unreviewed;       230 AA.
AC   D3J6M6;
DT   23-MAR-2010, integrated into UniProtKB/TrEMBL.
DT   23-MAR-2010, sequence version 1.
DT   24-JAN-2024, entry version 39.
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:ADB93198.1};
OS   Lymanopoda caudalis.
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Papilionoidea;
OC   Nymphalidae; Satyrinae; Satyrini; Pronophilina; Lymanopoda.
OX   NCBI_TaxID=669553 {ECO:0000313|EMBL:ADB93198.1};
RN   [1] {ECO:0000313|EMBL:ADB93198.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=KA89 {ECO:0000313|EMBL:ADB93198.1};
RA   Casner K.L., Pyrcz T.W.;
RT   "Patterns and timing of diversification in a tropical montane butterfly
RT   genus, Lymanopoda (Nymphalidae, Satyrinae).";
RL   Ecography 33:251-259(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; GQ861884; ADB93198.1; -; Genomic_DNA.
DR   AlphaFoldDB; D3J6M6; -.
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   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   Glycolysis {ECO:0000256|ARBA:ARBA00023152};
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:ADB93198.1"
FT   NON_TER         230
FT                   /evidence="ECO:0000313|EMBL:ADB93198.1"
SQ   SEQUENCE   230 AA;  24161 MW;  F51D499C1EFB9B76 CRC64;
     VESTGVFTTI EKASAHLDGG AKKVIISAPS ADAPMFVVGV NLEAYDPSFK VISNASCTTN
     CLAPLAKVIH DNFEIIEGLM TTVHATTATQ KTVDGPSGKL WRDGRGAQQN IIPASTGAAK
     AVGKVIPALN GKLTGMAFRV PVANVSVVDL TVRLGKPASY DAIKQKVKEA AEGPLKGILA
     YTEDQVVSSD FIGDTHSSIF DAAAGISLND NFVKLISWYD NEYGYSSRVS
//
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