ID Q7T3H5_DANRE Unreviewed; 349 AA. AC Q7T3H5; A0A8M1PHK3; DT 01-OCT-2003, integrated into UniProtKB/TrEMBL. DT 01-OCT-2003, sequence version 1. DT 27-MAR-2024, entry version 151. DE RecName: Full=Glycerol-3-phosphate dehydrogenase [NAD(+)] {ECO:0000256|RuleBase:RU361243}; DE EC=1.1.1.8 {ECO:0000256|RuleBase:RU361243}; GN Name=gpd1c {ECO:0000313|Ensembl:ENSDARP00000113739, GN ECO:0000313|RefSeq:NP_999918.1, GN ECO:0000313|ZFIN:ZDB-GENE-040426-2576}; GN Synonyms=fc30a07 {ECO:0000313|RefSeq:NP_999918.1}, gpd1 GN {ECO:0000313|EMBL:AAH53116.1, ECO:0000313|RefSeq:NP_999918.1}, GN wu:fc30a07 {ECO:0000313|RefSeq:NP_999918.1}, zgc:63859 GN {ECO:0000313|RefSeq:NP_999918.1}; OS Danio rerio (Zebrafish) (Brachydanio rerio). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes; OC Danionidae; Danioninae; Danio. OX NCBI_TaxID=7955 {ECO:0000313|EMBL:AAH53116.1}; RN [1] {ECO:0000313|EMBL:AAH53116.1} RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Embryo {ECO:0000313|EMBL:AAH53116.1}; RG NIH - Zebrafish Gene Collection (ZGC) project; RL Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|RefSeq:NP_999918.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=Tuebingen {ECO:0000313|RefSeq:NP_999918.1}; RX PubMed=16109975; RA Woods I.G., Wilson C., Friedlander B., Chang P., Reyes D.K., Nix R., RA Kelly P.D., Chu F., Postlethwait J.H., Talbot W.S.; RT "The zebrafish gene map defines ancestral vertebrate chromosomes."; RL Genome Res. 15:1307-1314(2005). RN [3] {ECO:0000313|RefSeq:NP_999918.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=Tuebingen {ECO:0000313|RefSeq:NP_999918.1}; RX PubMed=18803863; RA Kolmakov N.N., Kube M., Reinhardt R., Canario A.V.; RT "Analysis of the goldfish Carassius auratus olfactory epithelium RT transcriptome reveals the presence of numerous non-olfactory GPCR and RT putative receptors for progestin pheromones."; RL BMC Genomics 9:429-429(2008). RN [4] {ECO:0000313|Ensembl:ENSDARP00000113739} RP IDENTIFICATION. RC STRAIN=Tuebingen {ECO:0000313|Ensembl:ENSDARP00000113739}; RG Ensembl; RL Submitted (FEB-2012) to UniProtKB. RN [5] {ECO:0000313|Ensembl:ENSDARP00000113739, ECO:0000313|Proteomes:UP000000437} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Tuebingen {ECO:0000313|Ensembl:ENSDARP00000113739}; RX PubMed=23594743; DOI=10.1038/nature12111; RG Genome Reference Consortium Zebrafish; RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M., RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I., RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J., RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y., RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B., RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S., RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M., RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J., RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Eliott D., RA Threadgold G., Harden G., Ware D., Begum S., Mortimore B., Mortimer B., RA Kerry G., Heath P., Phillimore B., Tracey A., Corby N., Dunn M., RA Johnson C., Wood J., Clark S., Pelan S., Griffiths G., Smith M., RA Glithero R., Howden P., Barker N., Lloyd C., Stevens C., Harley J., RA Holt K., Panagiotidis G., Lovell J., Beasley H., Henderson C., Gordon D., RA Auger K., Wright D., Collins J., Raisen C., Dyer L., Leung K., RA Robertson L., Ambridge K., Leongamornlert D., McGuire S., Gilderthorp R., RA Griffiths C., Manthravadi D., Nichol S., Barker G., Whitehead S., Kay M., RA Brown J., Murnane C., Gray E., Humphries M., Sycamore N., Barker D., RA Saunders D., Wallis J., Babbage A., Hammond S., Mashreghi-Mohammadi M., RA Barr L., Martin S., Wray P., Ellington A., Matthews N., Ellwood M., RA Woodmansey R., Clark G., Cooper J., Cooper J., Tromans A., Grafham D., RA Skuce C., Pandian R., Andrews R., Harrison E., Kimberley A., Garnett J., RA Fosker N., Hall R., Garner P., Kelly D., Bird C., Palmer S., Gehring I., RA Berger A., Dooley C.M., Ersan-Urun Z., Eser C., Geiger H., Geisler M., RA Karotki L., Kirn A., Konantz J., Konantz M., Oberlander M., RA Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G., Osoegawa K., Zhu B., RA Rapp A., Widaa S., Langford C., Yang F., Schuster S.C., Carter N.P., RA Harrow J., Ning Z., Herrero J., Searle S.M., Enright A., Geisler R., RA Plasterk R.H., Lee C., Westerfield M., de Jong P.J., Zon L.I., RA Postlethwait J.H., Nusslein-Volhard C., Hubbard T.J., Roest Crollius H., RA Rogers J., Stemple D.L.; RT "The zebrafish reference genome sequence and its relationship to the human RT genome."; RL Nature 496:498-503(2013). RN [6] {ECO:0000313|RefSeq:NP_999918.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=Tuebingen {ECO:0000313|RefSeq:NP_999918.1}; RX PubMed=26469318; RA Elkon R., Milon B., Morrison L., Shah M., Vijayakumar S., Racherla M., RA Leitch C.C., Silipino L., Hadi S., Weiss-Gayet M., Barras E., Schmid C.D., RA Ait-Lounis A., Barnes A., Song Y., Eisenman D.J., Eliyahu E., RA Frolenkov G.I., Strome S.E., Durand B., Zaghloul N.A., Jones S.M., RA Reith W., Hertzano R.; RT "RFX transcription factors are essential for hearing in mice."; RL Nat. Commun. 6:8549-8549(2015). RN [7] {ECO:0000313|RefSeq:NP_999918.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=Tuebingen {ECO:0000313|RefSeq:NP_999918.1}; RX PubMed=27189481; RA Pasquier J., Cabau C., Nguyen T., Jouanno E., Severac D., Braasch I., RA Journot L., Pontarotti P., Klopp C., Postlethwait J.H., Guiguen Y., RA Bobe J.; RT "Gene evolution and gene expression after whole genome duplication in fish: RT the PhyloFish database."; RL BMC Genomics 17:368-368(2016). RN [8] {ECO:0000313|RefSeq:NP_999918.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=Tuebingen {ECO:0000313|RefSeq:NP_999918.1}; RX PubMed=28252024; RA Bayes A., Collins M.O., Reig-Viader R., Gou G., Goulding D., Izquierdo A., RA Choudhary J.S., Emes R.D., Grant S.G.; RT "Evolution of complexity in the zebrafish synapse proteome."; RL Nat. Commun. 8:14613-14613(2017). RN [9] {ECO:0000313|RefSeq:NP_999918.1} RP IDENTIFICATION. RC STRAIN=Tuebingen {ECO:0000313|RefSeq:NP_999918.1}; RG RefSeq; RL Submitted (NOV-2023) to UniProtKB. 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:ARBA00001343}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11093; CC Evidence={ECO:0000256|ARBA:ARBA00001343}; 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; CR548627; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC053116; AAH53116.1; -; mRNA. DR RefSeq; NP_999918.1; NM_214753.2. DR STRING; 7955.ENSDARP00000113739; -. DR PaxDb; 7955-ENSDARP00000113739; -. DR Ensembl; ENSDART00000134266.2; ENSDARP00000113739.1; ENSDARG00000036942.8. DR GeneID; 406615; -. DR KEGG; dre:406615; -. DR AGR; ZFIN:ZDB-GENE-040426-2576; -. DR CTD; 406615; -. DR ZFIN; ZDB-GENE-040426-2576; gpd1c. DR eggNOG; KOG2711; Eukaryota. DR HOGENOM; CLU_033449_2_2_1; -. DR OMA; ICYEGRS; -. DR OrthoDB; 3675564at2759; -. DR TreeFam; TF300836; -. DR Proteomes; UP000000437; Chromosome 19. DR Bgee; ENSDARG00000036942; Expressed in zone of skin and 23 other cell types or tissues. 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: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 GO; GO:0006072; P:glycerol-3-phosphate metabolic process; IBA:GO_Central. DR GO; GO:0006116; P:NADH oxidation; IBA:GO_Central. 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:SF42; 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 1: Evidence at protein level; KW NAD {ECO:0000256|PIRSR:PIRSR000114-3, ECO:0000256|RuleBase:RU000437}; KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, KW ECO:0000256|RuleBase:RU000437}; KW Proteomics identification {ECO:0007829|PeptideAtlas:Q7T3H5}; KW Reference proteome {ECO:0000313|Proteomes:UP000000437}. FT DOMAIN 5..172 FT /note="Glycerol-3-phosphate dehydrogenase NAD-dependent N- FT terminal" FT /evidence="ECO:0000259|Pfam:PF01210" FT DOMAIN 196..339 FT /note="Glycerol-3-phosphate dehydrogenase NAD-dependent C- FT terminal" FT /evidence="ECO:0000259|Pfam:PF07479" FT ACT_SITE 204 FT /note="Proton acceptor" FT /evidence="ECO:0000256|PIRSR:PIRSR000114-1" FT BINDING 10..15 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|PIRSR:PIRSR000114-3" FT BINDING 97 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|PIRSR:PIRSR000114-3" FT BINDING 120 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR000114-2" FT BINDING 153 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|PIRSR:PIRSR000114-3" FT BINDING 269..270 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR000114-2" FT BINDING 269 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|PIRSR:PIRSR000114-3" FT BINDING 296 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|PIRSR:PIRSR000114-3" FT BINDING 298 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|PIRSR:PIRSR000114-3" SQ SEQUENCE 349 AA; 38179 MW; 43EFE27743393D0E CRC64; MPGKKVCIIG SGNWGSAIAK IVGHNVKSSN RFEPLVKMWV YEEMIDGRKL TEIINTEHEN VKYLPGHKLP KTVVAVPDVT EAASGADFLI FVIPHQFIVR VCDQMKPHIK PGAIGISLIK GIDEGPDGLT LISDIIRAKL EIEVCVLMGA NIASEVADEK FCETTIGATN EASGKLFKEL LQTPNFRITV VKESDTVELC GALKNIVAVG AGFCDGLGFG DNTKAAVIRL GLMEMVAFSK LFCKSSVSSA TFLESCGVAD LITTCYGGRN RRVAEAFART QKSIVELEAE MLNGQKLQGP QTSAEVYKIL HKRNITDKFP LFVSVYQICF EGRQVKDFIN CLQNHPEHM //