ID D7MJ57_ARALL Unreviewed; 366 AA. AC D7MJ57; DT 10-AUG-2010, integrated into UniProtKB/TrEMBL. DT 10-AUG-2010, sequence version 1. DT 24-JAN-2024, entry version 72. DE RecName: Full=Glycerol-3-phosphate dehydrogenase [NAD(+)] {ECO:0000256|RuleBase:RU361243}; DE EC=1.1.1.8 {ECO:0000256|RuleBase:RU361243}; GN ORFNames=ARALYDRAFT_493921 {ECO:0000313|EMBL:EFH44903.1}; OS Arabidopsis lyrata subsp. lyrata (Lyre-leaved rock-cress). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae; OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis. OX NCBI_TaxID=81972 {ECO:0000313|Proteomes:UP000008694}; RN [1] {ECO:0000313|Proteomes:UP000008694} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. MN47 {ECO:0000313|Proteomes:UP000008694}; RX PubMed=21478890; DOI=10.1038/ng.807; RA Hu T.T., Pattyn P., Bakker E.G., Cao J., Cheng J.-F., Clark R.M., RA Fahlgren N., Fawcett J.A., Grimwood J., Gundlach H., Haberer G., RA Hollister J.D., Ossowski S., Ottilar R.P., Salamov A.A., Schneeberger K., RA Spannagl M., Wang X., Yang L., Nasrallah M.E., Bergelson J., RA Carrington J.C., Gaut B.S., Schmutz J., Mayer K.F.X., Van de Peer Y., RA Grigoriev I.V., Nordborg M., Weigel D., Guo Y.-L.; RT "The Arabidopsis lyrata genome sequence and the basis of rapid genome size RT change."; RL Nat. Genet. 43:476-481(2011). CC -!- CATALYTIC ACTIVITY: CC Reaction=NAD(+) + sn-glycerol 3-phosphate = dihydroxyacetone phosphate CC + H(+) + NADH; Xref=Rhea:RHEA:11092, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57597, ChEBI:CHEBI:57642, CC ChEBI:CHEBI:57945; EC=1.1.1.8; CC Evidence={ECO:0000256|ARBA:ARBA00001662, CC ECO:0000256|RuleBase:RU361243}; CC -!- SIMILARITY: Belongs to the NAD-dependent glycerol-3-phosphate CC dehydrogenase family. {ECO:0000256|ARBA:ARBA00011009, CC ECO:0000256|RuleBase:RU000437}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; GL348719; EFH44903.1; -; Genomic_DNA. DR RefSeq; XP_002868644.1; XM_002868598.1. DR AlphaFoldDB; D7MJ57; -. DR STRING; 81972.D7MJ57; -. DR EnsemblPlants; fgenesh2_kg.7__3354__AT5G40610.1; fgenesh2_kg.7__3354__AT5G40610.1; fgenesh2_kg.7__3354__AT5G40610.1. DR GeneID; 9306762; -. DR Gramene; fgenesh2_kg.7__3354__AT5G40610.1; fgenesh2_kg.7__3354__AT5G40610.1; fgenesh2_kg.7__3354__AT5G40610.1. DR KEGG; aly:9306762; -. DR eggNOG; KOG2711; Eukaryota. DR HOGENOM; CLU_033449_2_2_1; -. DR OrthoDB; 3675564at2759; -. DR Proteomes; UP000008694; Unassembled WGS sequence. DR GO; GO:0009331; C:glycerol-3-phosphate dehydrogenase complex; IEA:UniProtKB-UniRule. DR GO; GO:0047952; F:glycerol-3-phosphate dehydrogenase [NAD(P)+] activity; IEA:UniProtKB-UniRule. DR GO; GO:0051287; F:NAD binding; IEA:UniProtKB-UniRule. DR GO; GO:0042803; F:protein homodimerization activity; IEA:InterPro. DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro. DR GO; GO:0046168; P:glycerol-3-phosphate catabolic process; IEA:UniProtKB-UniRule. DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1. DR InterPro; IPR008927; 6-PGluconate_DH-like_C_sf. DR InterPro; IPR013328; 6PGD_dom2. DR InterPro; IPR006168; G3P_DH_NAD-dep. DR InterPro; IPR006109; G3P_DH_NAD-dep_C. DR InterPro; IPR017751; G3P_DH_NAD-dep_euk. DR InterPro; IPR011128; G3P_DH_NAD-dep_N. DR InterPro; IPR036291; NAD(P)-bd_dom_sf. DR NCBIfam; TIGR03376; glycerol3P_DH; 1. DR PANTHER; PTHR11728; GLYCEROL-3-PHOSPHATE DEHYDROGENASE; 1. DR PANTHER; PTHR11728:SF8; GLYCEROL-3-PHOSPHATE DEHYDROGENASE [NAD(+)]-RELATED; 1. DR Pfam; PF07479; NAD_Gly3P_dh_C; 1. DR Pfam; PF01210; NAD_Gly3P_dh_N; 1. DR PIRSF; PIRSF000114; Glycerol-3-P_dh; 1. DR PRINTS; PR00077; GPDHDRGNASE. DR SUPFAM; SSF48179; 6-phosphogluconate dehydrogenase C-terminal domain-like; 1. DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1. DR PROSITE; PS00957; NAD_G3PDH; 1. PE 3: Inferred from homology; KW NAD {ECO:0000256|PIRSR:PIRSR000114-3, ECO:0000256|RuleBase:RU000437}; KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, KW ECO:0000256|RuleBase:RU000437}; KW Reference proteome {ECO:0000313|Proteomes:UP000008694}. FT DOMAIN 22..186 FT /note="Glycerol-3-phosphate dehydrogenase NAD-dependent N- FT terminal" FT /evidence="ECO:0000259|Pfam:PF01210" FT DOMAIN 212..360 FT /note="Glycerol-3-phosphate dehydrogenase NAD-dependent C- FT terminal" FT /evidence="ECO:0000259|Pfam:PF07479" FT ACT_SITE 223 FT /note="Proton acceptor" FT /evidence="ECO:0000256|PIRSR:PIRSR000114-1" FT BINDING 27..32 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|PIRSR:PIRSR000114-3" FT BINDING 58 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|PIRSR:PIRSR000114-3" FT BINDING 115 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|PIRSR:PIRSR000114-3" FT BINDING 138 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR000114-2" FT BINDING 171 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|PIRSR:PIRSR000114-3" FT BINDING 287..288 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR000114-2" FT BINDING 287 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|PIRSR:PIRSR000114-3" FT BINDING 316 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|PIRSR:PIRSR000114-3" FT BINDING 318 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|PIRSR:PIRSR000114-3" SQ SEQUENCE 366 AA; 39942 MW; 41D1E8DD47072ECC CRC64; MSPALEKSRQ GNGECNEVSK SKVTVVGSGN WGSVAAKLIA SNALKLPSFH DEVRMWVFEE VLPNGEKLTD VINKTNENVK YLPGVKLGRN VVADPDLENA VKEANMLVFV TPHQFMDGIC KKLDGKITGD VEAISLVKGM EVKKEGPCMI SSLISKQLGI NCCVLMGANI ANEIAVEKFS EATVGYRGSR EIADTWVQLF STPYFMVTPV HDVEGVELCG TLKNVVAIAA GFVDGLEMGN NTKAAIMRIG LREMKALSKL LFPSVKDSTF FESCGVADVI TTCLGGRNRR VAEAFAKSGG KRSFDELEAE MLQGQKLQGV STAREVYEVL NHCGWLEMFP LFSTVHQICT GHLQPEAIVQ YRENKL //