ID A0A0Q3LKL4_BRADI Unreviewed; 446 AA.
AC A0A0Q3LKL4;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 44.
DE RecName: Full=Glyceraldehyde-3-phosphate dehydrogenase {ECO:0000256|RuleBase:RU361160};
DE EC=1.2.1.- {ECO:0000256|RuleBase:RU361160};
GN Name=100829538 {ECO:0000313|EnsemblPlants:KQK23841};
GN ORFNames=BRADI_1g76470v3 {ECO:0000313|EMBL:KQK23841.1};
OS Brachypodium distachyon (Purple false brome) (Trachynia distachya).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Pooideae; Stipodae; Brachypodieae; Brachypodium.
OX NCBI_TaxID=15368 {ECO:0000313|EMBL:KQK23841.1};
RN [1] {ECO:0000313|EMBL:KQK23841.1, ECO:0000313|EnsemblPlants:KQK23841}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bd21 {ECO:0000313|EMBL:KQK23841.1,
RC ECO:0000313|EnsemblPlants:KQK23841};
RX PubMed=20148030; DOI=10.1038/nature08747;
RG International Brachypodium Initiative;
RT "Genome sequencing and analysis of the model grass Brachypodium
RT distachyon.";
RL Nature 463:763-768(2010).
RN [2] {ECO:0000313|EMBL:KQK23841.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Bd21 {ECO:0000313|EMBL:KQK23841.1};
RG The International Brachypodium Initiative;
RA Lucas S., Harmon-Smith M., Lail K., Tice H., Grimwood J., Bruce D.,
RA Barry K., Shu S., Lindquist E., Wang M., Pitluck S., Vogel J.P.,
RA Garvin D.F., Mockler T.C., Schmutz J., Rokhsar D., Bevan M.W.;
RT "WGS assembly of Brachypodium distachyon.";
RL Submitted (JUN-2017) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EnsemblPlants:KQK23841}
RP IDENTIFICATION.
RC STRAIN=cv. Bd21 {ECO:0000313|EnsemblPlants:KQK23841};
RG EnsemblPlants;
RL Submitted (AUG-2018) to UniProtKB.
CC -!- FUNCTION: Key enzyme in glycolysis that catalyzes the first step of the
CC pathway by converting D-glyceraldehyde 3-phosphate (G3P) into 3-
CC phospho-D-glyceroyl phosphate. Essential for the maintenance of
CC cellular ATP levels and carbohydrate metabolism.
CC {ECO:0000256|ARBA:ARBA00025350}.
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; CM000880; KQK23841.1; -; Genomic_DNA.
DR RefSeq; XP_003558903.2; XM_003558855.3.
DR AlphaFoldDB; A0A0Q3LKL4; -.
DR STRING; 15368.A0A0Q3LKL4; -.
DR EnsemblPlants; KQK23841; KQK23841; BRADI_1g76470v3.
DR GeneID; 100829538; -.
DR Gramene; KQK23841; KQK23841; BRADI_1g76470v3.
DR KEGG; bdi:100829538; -.
DR InParanoid; A0A0Q3LKL4; -.
DR OrthoDB; 3165299at2759; -.
DR Proteomes; UP000008810; Chromosome 1.
DR ExpressionAtlas; A0A0Q3LKL4; baseline.
DR GO; GO:0004365; F:glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity; IBA:GO_Central.
DR GO; GO:0051287; F:NAD binding; IBA:GO_Central.
DR GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR GO; GO:0006006; P:glucose metabolic process; IBA:GO_Central.
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:SF17; GLYCERALDEHYDE-3-PHOSPHATE DEHYDROGENASE; 1.
DR PANTHER; PTHR43148; GLYCERALDEHYDE-3-PHOSPHATE DEHYDROGENASE 2; 1.
DR Pfam; PF02672; CP12; 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 3: Inferred from homology;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU361160};
KW Reference proteome {ECO:0000313|Proteomes:UP000008810}.
FT DOMAIN 81..234
FT /note="Glyceraldehyde 3-phosphate dehydrogenase NAD(P)
FT binding"
FT /evidence="ECO:0000259|SMART:SM00846"
SQ SEQUENCE 446 AA; 47227 MW; C9E7A1D2AAAEEAB4 CRC64;
MAAHAALAAS RIPTGRLQHG KAASSKLQRL DLADFSGLRP GSCSVSVAAT REASFSDVLG
AQLVARASGE NAVRAPAEAK LKVAINGFGR IGRNFLRCWH GRENSPLEVV VINDSGGVRN
ASHLLKYDSM LGTFKADVKI VDNETISVDG KNIQVVSNRD PLKLPWAELG IDIVIEGTGV
FVDGPGAGKH IQAGAKKVII TAPAKGADIP TYVLGVNEEG YDHDVANIVS NASCTTNCLA
PFVKVLDEEF GIVKGTMTTT HSYTGDQRLL DASHRDLRRA RAAALNIVPT STGAAKAVAL
VLPQLKGKLN GIALRVPTPN VSVVDLVINT AKTGITADDV NAAFRKAAAG PLNGILDVCD
EPLVSVDFRC SDVSSTIDAS LTMVMGDDMV KVVAWYDNEW GYSQRVVDLA HLVASKWPGS
EVKGTGDPLE DYCKTNPETD ECKVYD
//
