ID Q7T1E0_DANRE Unreviewed; 350 AA. AC Q7T1E0; DT 01-OCT-2003, integrated into UniProtKB/TrEMBL. DT 01-OCT-2003, sequence version 1. DT 16-JAN-2019, entry version 132. DE RecName: Full=Glycerol-3-phosphate dehydrogenase [NAD(+)] {ECO:0000256|RuleBase:RU361243}; DE EC=1.1.1.8 {ECO:0000256|RuleBase:RU361243}; GN Name=gpd1b {ECO:0000313|EMBL:AAH55382.1, GN ECO:0000313|ZFIN:ZDB-GENE-030131-3906}; GN Synonyms=gpd1h {ECO:0000313|EMBL:ABG78033.1}; OS Danio rerio (Zebrafish) (Brachydanio rerio). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes; OC Cyprinidae; Danio. OX NCBI_TaxID=7955 {ECO:0000313|EMBL:AAH55382.1}; RN [1] {ECO:0000313|EMBL:AAH55382.1} RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Kidney {ECO:0000313|EMBL:AAH55382.1}; RG NIH - Zebrafish Gene Collection (ZGC) project; RL Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:AAH67596.1} RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Kidney {ECO:0000313|EMBL:AAH67596.1}; RG NIH - Zebrafish Gene Collection (ZGC) project; RL Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases. RN [3] {ECO:0000313|EMBL:ABG78033.1} RP NUCLEOTIDE SEQUENCE. RA Smith A.H., Chopra S.S., Roden D.M.; RT "Cloning gpd1h in adult zebrafish myocardium."; RL Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: CC Reaction=NAD(+) + sn-glycerol 3-phosphate = dihydroxyacetone CC phosphate + H(+) + NADH; Xref=Rhea:RHEA:11092, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57597, CC ChEBI:CHEBI:57642, ChEBI:CHEBI:57945; EC=1.1.1.8; CC Evidence={ECO:0000256|RuleBase:RU361243}; CC -!- SIMILARITY: Belongs to the NAD-dependent glycerol-3-phosphate CC dehydrogenase family. {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; BC055382; AAH55382.1; -; mRNA. DR EMBL; BC067596; AAH67596.1; -; mRNA. DR EMBL; DQ677583; ABG78033.1; -; mRNA. DR RefSeq; NP_956000.1; NM_199706.1. DR UniGene; Dr.79210; -. DR GeneID; 325181; -. DR KEGG; dre:325181; -. DR CTD; 325181; -. DR ZFIN; ZDB-GENE-030131-3906; gpd1b. DR eggNOG; KOG2711; Eukaryota. DR eggNOG; COG0240; LUCA. DR HOGENOM; HOG000246855; -. DR HOVERGEN; HBG003669; -. DR KO; K00006; -. DR OrthoDB; 476066at2759; -. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0009331; C:glycerol-3-phosphate dehydrogenase complex; IEA:UniProtKB-UniRule. DR GO; GO:0004368; F:glycerol-3-phosphate dehydrogenase (quinone) activity; IBA:GO_Central. DR GO; GO:0047952; F:glycerol-3-phosphate dehydrogenase [NAD(P)+] activity; IBA:GO_Central. DR GO; GO:0004367; F:glycerol-3-phosphate dehydrogenase [NAD+] activity; IBA:GO_Central. DR GO; GO:0051287; F:NAD binding; IBA:GO_Central. 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 GO; GO:0006072; P:glycerol-3-phosphate metabolic process; IBA:GO_Central. DR Gene3D; 1.10.1040.10; -; 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 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; SSF48179; 1. DR SUPFAM; SSF51735; SSF51735; 1. DR TIGRFAMs; TIGR03376; glycerol3P_DH; 1. DR PROSITE; PS00957; NAD_G3PDH; 1. PE 2: Evidence at transcript level; KW NAD {ECO:0000256|PIRSR:PIRSR000114-3, ECO:0000256|RuleBase:RU000437}; KW Oxidoreductase {ECO:0000256|RuleBase:RU000437}. FT DOMAIN 5 171 NAD_Gly3P_dh_N. {ECO:0000259|Pfam: FT PF01210}. FT DOMAIN 197 340 NAD_Gly3P_dh_C. {ECO:0000259|Pfam: FT PF07479}. FT NP_BIND 10 15 NAD. {ECO:0000256|PIRSR:PIRSR000114-3}. FT REGION 270 271 Substrate binding. {ECO:0000256|PIRSR: FT PIRSR000114-2}. FT ACT_SITE 204 204 Proton acceptor. {ECO:0000256|PIRSR: FT PIRSR000114-1}. FT BINDING 41 41 NAD. {ECO:0000256|PIRSR:PIRSR000114-3}. FT BINDING 97 97 NAD. {ECO:0000256|PIRSR:PIRSR000114-3}. FT BINDING 120 120 Substrate. {ECO:0000256|PIRSR: FT PIRSR000114-2}. FT BINDING 153 153 NAD; via amide nitrogen. FT {ECO:0000256|PIRSR:PIRSR000114-3}. FT BINDING 270 270 NAD. {ECO:0000256|PIRSR:PIRSR000114-3}. FT BINDING 297 297 NAD; via amide nitrogen. FT {ECO:0000256|PIRSR:PIRSR000114-3}. FT BINDING 299 299 NAD. {ECO:0000256|PIRSR:PIRSR000114-3}. SQ SEQUENCE 350 AA; 38194 MW; 6A124D0095BFFCD5 CRC64; MAAKKICIIG SGNWGSAIAK IVGANAAKYN TFENTVNMWV FEEMINGRKL TEIINTEHEN VKYLPGHKLP PNVLAVPDLL ESVKGADILI FVIPHQFVSR ICDTIKGHIK PDAVGMSLIK GVDEGPDGLK LISDVIREKL GITMTVLMGA NLANEVADEK FCETTIGCKS KPHGPLLKEL MQTQNFRVTV VEEADVVEIC GALKNIVAVG AGFCDGLSFG DNTKAAVIRL GLMEMIAFAR LFCTASPVSP ATFLESCGVA DLITTCYGGR NRKVGEAFAR TGKSIEELEK EMLNGQKLQG PATAAEVHQI LKHKNLVEKF PLFNAVYQIC FQNHPVKEFI MCLQNHPEHM //