ID B6HGH0_PENRW Unreviewed; 409 AA. AC B6HGH0; DT 16-DEC-2008, integrated into UniProtKB/TrEMBL. DT 16-DEC-2008, sequence version 1. DT 27-MAR-2024, entry version 88. DE RecName: Full=Glycerol-3-phosphate dehydrogenase [NAD(+)] {ECO:0000256|RuleBase:RU361243}; DE EC=1.1.1.8 {ECO:0000256|RuleBase:RU361243}; GN ORFNames=Pc20g06370 {ECO:0000313|EMBL:CAP85966.1}, PCH_Pc20g06370 GN {ECO:0000313|EMBL:CAP85966.1}; OS Penicillium rubens (strain ATCC 28089 / DSM 1075 / NRRL 1951 / Wisconsin OS 54-1255) (Penicillium chrysogenum). OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes; OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium; OC Penicillium chrysogenum species complex. OX NCBI_TaxID=500485 {ECO:0000313|EMBL:CAP85966.1, ECO:0000313|Proteomes:UP000000724}; RN [1] {ECO:0000313|EMBL:CAP85966.1, ECO:0000313|Proteomes:UP000000724} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 28089 / DSM 1075 / NRRL 1951 / Wisconsin 54-1255 RC {ECO:0000313|Proteomes:UP000000724}; RX PubMed=18820685; DOI=10.1038/nbt.1498; RA van den Berg M.A., Albang R., Albermann K., Badger J.H., Daran J.-M., RA Driessen A.J.M., Garcia-Estrada C., Fedorova N.D., Harris D.M., RA Heijne W.H.M., Joardar V.S., Kiel J.A.K.W., Kovalchuk A., Martin J.F., RA Nierman W.C., Nijland J.G., Pronk J.T., Roubos J.A., van der Klei I.J., RA van Peij N.N.M.E., Veenhuis M., von Doehren H., Wagner C., Wortman J.R., RA Bovenberg R.A.L.; RT "Genome sequencing and analysis of the filamentous fungus Penicillium RT chrysogenum."; RL Nat. Biotechnol. 26:1161-1168(2008). 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; AM920435; CAP85966.1; -; Genomic_DNA. DR RefSeq; XP_002563166.1; XM_002563120.1. DR AlphaFoldDB; B6HGH0; -. DR STRING; 500485.B6HGH0; -. DR GeneID; 8310734; -. DR KEGG; pcs:Pc20g06370; -. DR VEuPathDB; FungiDB:PCH_Pc20g06370; -. DR eggNOG; KOG2711; Eukaryota. DR HOGENOM; CLU_033449_2_3_1; -. DR OMA; YDTPPMD; -. DR OrthoDB; 3675564at2759; -. DR BioCyc; PCHR:PC20G06370-MONOMER; -. DR Proteomes; UP000000724; Contig Pc00c20. 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:SF31; GLYCEROL-3-PHOSPHATE DEHYDROGENASE [NAD(+)]; 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:UP000000724}. FT DOMAIN 6..184 FT /note="Glycerol-3-phosphate dehydrogenase NAD-dependent N- FT terminal" FT /evidence="ECO:0000259|Pfam:PF01210" FT DOMAIN 251..396 FT /note="Glycerol-3-phosphate dehydrogenase NAD-dependent C- FT terminal" FT /evidence="ECO:0000259|Pfam:PF07479" FT ACT_SITE 262 FT /note="Proton acceptor" FT /evidence="ECO:0000256|PIRSR:PIRSR000114-1" FT BINDING 11..16 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|PIRSR:PIRSR000114-3" FT BINDING 43 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|PIRSR:PIRSR000114-3" FT BINDING 113 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|PIRSR:PIRSR000114-3" FT BINDING 136 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR000114-2" FT BINDING 169 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|PIRSR:PIRSR000114-3" FT BINDING 328..329 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR000114-2" FT BINDING 328 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|PIRSR:PIRSR000114-3" FT BINDING 355 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|PIRSR:PIRSR000114-3" FT BINDING 357 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|PIRSR:PIRSR000114-3" SQ SEQUENCE 409 AA; 44775 MW; 5640FAD6636CFFF0 CRC64; MTQKHKVVVI GSGNWGSTIG KILAENTREH SDIFEEDVSM WVFEEDVDVP DDGTLRDQLG DKPVKLTHAI NTAHQNIKYL PGIKLPDNLI ANPDLQDTVR GATILVFNLP HQFMSKTLEQ IKGHHLPYAR AISCVKGVDI SEGTVKLYSE LIMEKLGIYC GSLSGANIAS EVAAENLCET TIGYDGPPMD YKEPDGSSRD NLIKVDKQRQ SKSSPSQLSL HRVPQNYPHV DSALLEKLFG RPYFNVQVVR DVSGVALGGA LKNIVALAAG FVAGKGWGEN TKAAVIRIGI LEMVRFGCLW FPQSVDERTF TKESAGIADV IASTSAGRNF HSACHAVEQG VTVDEIEKKE LGGQKLQGTS TSRAVYEFLE KQGQLEKFPL FVFVHDILEE RTTMDALPGL LIKGSKVMA //