ID F8UX79_ARAHY Unreviewed; 405 AA.
AC F8UX79;
DT 21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT 21-SEP-2011, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE RecName: Full=Glyceraldehyde-3-phosphate dehydrogenase {ECO:0000256|RuleBase:RU361160};
DE EC=1.2.1.- {ECO:0000256|RuleBase:RU361160};
OS Arachis hypogaea (Peanut).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC dalbergioids sensu lato; Dalbergieae; Pterocarpus clade; Arachis.
OX NCBI_TaxID=3818 {ECO:0000313|EMBL:AEH04452.1};
RN [1] {ECO:0000313|EMBL:AEH04452.1}
RP NUCLEOTIDE SEQUENCE.
RA Xie H.F., Chi Y.C., Xu M.L., Fan T.Q., Yu S.L.;
RT "In silico cloning and sequence analysis of glyceraldehyde-3-phosphate
RT dehydrogenase from peanut.";
RL Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-glyceraldehyde 3-phosphate + NADP(+) + phosphate = (2R)-3-
CC phospho-glyceroyl phosphate + H(+) + NADPH; Xref=Rhea:RHEA:10296,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:57604,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:59776; EC=1.2.1.13;
CC Evidence={ECO:0000256|ARBA:ARBA00035876};
CC -!- PATHWAY: Carbohydrate biosynthesis; Calvin cycle.
CC {ECO:0000256|ARBA:ARBA00005215}.
CC -!- SIMILARITY: Belongs to the glyceraldehyde-3-phosphate dehydrogenase
CC family. {ECO:0000256|ARBA:ARBA00007406, ECO:0000256|RuleBase:RU000397}.
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DR EMBL; JF957835; AEH04452.1; -; mRNA.
DR AlphaFoldDB; F8UX79; -.
DR OrthoDB; 3165299at2759; -.
DR SABIO-RK; F8UX79; -.
DR GO; GO:0047100; F:glyceraldehyde-3-phosphate dehydrogenase (NADP+) (phosphorylating) activity; IEA:RHEA.
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 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; IPR006424; Glyceraldehyde-3-P_DH_1.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR NCBIfam; TIGR01534; GAPDH-I; 1.
DR PANTHER; PTHR43148; GLYCERALDEHYDE-3-PHOSPHATE DEHYDROGENASE 2; 1.
DR PANTHER; PTHR43148:SF2; GLYCERALDEHYDE-3-PHOSPHATE DEHYDROGENASE 2; 1.
DR Pfam; PF02800; Gp_dh_C; 1.
DR Pfam; PF00044; Gp_dh_N; 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 2: Evidence at transcript level;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU361160}.
FT DOMAIN 71..222
FT /note="Glyceraldehyde 3-phosphate dehydrogenase NAD(P)
FT binding"
FT /evidence="ECO:0000259|SMART:SM00846"
SQ SEQUENCE 405 AA; 43179 MW; 15C8D62CD62ADD6E CRC64;
MASATLSVAK PALQGNGGKG FSEFSGLRNS SSSYLPFSRK TSDDFHSIIS FQTSAVGSSG
GYRKGVTEAK LKVAINGFGR IGRNFLRCWH GRKDSPLDVI AINDTGGVKQ ASHLLKYDST
LGIFDADVKP VGEDAISVDG KVIKVVSNRN PANLPWKELG VDLVIEGTGV FVDREGAGKH
IQAGAKKVLI TAPGKGDIPT YVVGVNADAY SPDEPIISNA SCTTNCLAPF VKVLDQKFGI
IKGTMTTTHS YTGDQRLLDA SHRDLRRARA AALNIVPTST GAAKAVALVL PTLKGKLNGI
ALRVPTPNVS VVDLVVQVSK KTFAEEVNAA FRESAEKELN GILSVCDEPL VSVDFRCTDV
SSTVDSSLTM VMGDDMVKVI AWYDNEWGYS QRVVDLADIV ANSWK
//
