ID A3LU81_PICST Unreviewed; 391 AA. AC A3LU81; DT 03-APR-2007, integrated into UniProtKB/TrEMBL. DT 24-JUL-2007, sequence version 2. DT 27-MAR-2024, entry version 106. DE RecName: Full=Glycerol-3-phosphate dehydrogenase [NAD(+)] {ECO:0000256|RuleBase:RU361243}; DE EC=1.1.1.8 {ECO:0000256|RuleBase:RU361243}; GN Name=GPD2 {ECO:0000313|EMBL:ABN66537.2}; GN ORFNames=PICST_83071 {ECO:0000313|EMBL:ABN66537.2}; OS Scheffersomyces stipitis (strain ATCC 58785 / CBS 6054 / NBRC 10063 / NRRL OS Y-11545) (Yeast) (Pichia stipitis). OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; OC Saccharomycetales; Debaryomycetaceae; Scheffersomyces. OX NCBI_TaxID=322104 {ECO:0000313|EMBL:ABN66537.2, ECO:0000313|Proteomes:UP000002258}; RN [1] {ECO:0000313|EMBL:ABN66537.2, ECO:0000313|Proteomes:UP000002258} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 58785 / CBS 6054 / NBRC 10063 / NRRL Y-11545 RC {ECO:0000313|Proteomes:UP000002258}; RX PubMed=17334359; DOI=10.1038/nbt1290; RA Jeffries T.W., Grigoriev I.V., Grimwood J., Laplaza J.M., Aerts A., RA Salamov A., Schmutz J., Lindquist E., Dehal P., Shapiro H., Jin Y.S., RA Passoth V., Richardson P.M.; RT "Genome sequence of the lignocellulose-bioconverting and xylose-fermenting RT yeast Pichia stipitis."; RL Nat. Biotechnol. 25:319-326(2007). 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; CP000498; ABN66537.2; -; Genomic_DNA. DR RefSeq; XP_001384566.2; XM_001384529.1. DR AlphaFoldDB; A3LU81; -. DR STRING; 322104.A3LU81; -. DR GeneID; 4838862; -. DR KEGG; pic:PICST_83071; -. DR eggNOG; KOG2711; Eukaryota. DR HOGENOM; CLU_033449_2_4_1; -. DR InParanoid; A3LU81; -. DR OMA; YDTPPMD; -. DR OrthoDB; 3675564at2759; -. DR Proteomes; UP000002258; Chromosome 4. 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:UP000002258}. FT DOMAIN 42..206 FT /note="Glycerol-3-phosphate dehydrogenase NAD-dependent N- FT terminal" FT /evidence="ECO:0000259|Pfam:PF01210" FT DOMAIN 239..383 FT /note="Glycerol-3-phosphate dehydrogenase NAD-dependent C- FT terminal" FT /evidence="ECO:0000259|Pfam:PF07479" FT ACT_SITE 250 FT /note="Proton acceptor" FT /evidence="ECO:0000256|PIRSR:PIRSR000114-1" FT BINDING 46..51 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|PIRSR:PIRSR000114-3" FT BINDING 134 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|PIRSR:PIRSR000114-3" FT BINDING 157 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR000114-2" FT BINDING 190 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|PIRSR:PIRSR000114-3" FT BINDING 315..316 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR000114-2" FT BINDING 315 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|PIRSR:PIRSR000114-3" FT BINDING 344 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|PIRSR:PIRSR000114-3" SQ SEQUENCE 391 AA; 42235 MW; 53F144EACAEFFF2C CRC64; MSTPVARLAQ LANILAPNPT AAYAAHSHHP EASLSPEHPF RVAVIGSGNW GTTIAKVIAE NAAARPRLFR HQVNMWVHDE IIDGEKLTHI INTRHENVKY LPGVILPRNI RAEADIGNVV HDADLIVFNL PHQFLPRVVK SLKGKIKHGA RAISCLKGLE VTPEGCKLLS TYITEELGIV CGALSGANIA PEVARCKWSE TTVAYKLPED FRGAGKDIDK FVLRACFHRP YFHVNVIEDV AGVSVAGALK NVVALAVGFV EGLGWGDNAK AAVMRVGLLE TIKFSETFFP ESIASTFTAE SAGVADLITS CSGGRNVKVG RYMAQTGSSA ENAEKMLLNG QSSQGIVTVR EVHDLLTNVG MLDKFPLFEA TYQIIYGSES IENLPLLLVG E //