ID B5RIM9_DROME Unreviewed; 360 AA. AC B5RIM9; DT 04-NOV-2008, integrated into UniProtKB/TrEMBL. DT 04-NOV-2008, sequence version 1. DT 24-JAN-2024, entry version 119. DE RecName: Full=Glycerol-3-phosphate dehydrogenase [NAD(+)] {ECO:0000256|RuleBase:RU361243}; DE EC=1.1.1.8 {ECO:0000256|RuleBase:RU361243}; GN Name=Gpdh1 {ECO:0000313|EMBL:AGB92648.1, GN ECO:0000313|FlyBase:FBgn0001128}; GN Synonyms=alpha-GPD {ECO:0000313|EMBL:AGB92648.1}, alpha-GPDH GN {ECO:0000313|EMBL:AGB92648.1}, alpha-Gpdh GN {ECO:0000313|EMBL:AGB92648.1}, alpha-GPDH-1 GN {ECO:0000313|EMBL:AGB92648.1}, alphaGpd {ECO:0000313|EMBL:AGB92648.1}, GN alphaGPDH {ECO:0000313|EMBL:AGB92648.1}, alphaGpdh GN {ECO:0000313|EMBL:AGB92648.1}, alphaGpdh-1 GN {ECO:0000313|EMBL:AGB92648.1}, dGpdh {ECO:0000313|EMBL:AGB92648.1}, GN Dmel\CG9042 {ECO:0000313|EMBL:AGB92648.1}, DmG3PDH GN {ECO:0000313|EMBL:AGB92648.1}, DROGPDHA {ECO:0000313|EMBL:AGB92648.1}, GN G3PDH {ECO:0000313|EMBL:AGB92648.1}, G3pdh GN {ECO:0000313|EMBL:AGB92648.1}, GAPDH {ECO:0000313|EMBL:AGB92648.1}, GN Gdh {ECO:0000313|EMBL:AGB92648.1}, GPD {ECO:0000313|EMBL:AGB92648.1}, GN Gpd {ECO:0000313|EMBL:AGB92648.1}, GPDA {ECO:0000313|EMBL:AGB92648.1}, GN GPDH {ECO:0000313|EMBL:AGB92648.1}, Gpdh GN {ECO:0000313|EMBL:AGB92648.1}, gpdh {ECO:0000313|EMBL:AGB92648.1}, GN GPDH-1 {ECO:0000313|EMBL:AGB92648.1}, gpdh-1 GN {ECO:0000313|EMBL:AGB92648.1}, sn-Gpdh {ECO:0000313|EMBL:AGB92648.1}; GN ORFNames=CG9042 {ECO:0000313|EMBL:AGB92648.1, GN ECO:0000313|FlyBase:FBgn0001128}, Dmel_CG9042 GN {ECO:0000313|EMBL:AGB92648.1}; OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea; OC Drosophilidae; Drosophila; Sophophora. OX NCBI_TaxID=7227 {ECO:0000313|EMBL:ACH92218.1}; RN [1] {ECO:0000313|EMBL:AGB92648.1, ECO:0000313|Proteomes:UP000000803} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803}; RX PubMed=10731132; DOI=10.1126/science.287.5461.2185; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C., RA Rogers Y.H., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., RA Baxter E.G., Helt G., Nelson C.R., Gabor G.L., Abril J.F., Agbayani A., RA An H.J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D., Heiman T.J., Hernandez J.R., Houck J., Hostin D., RA Houston K.A., Howland T.J., Wei M.H., Ibegwam C., Jalali M., Kalush F., RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., RA Kraft C., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., RA Li J., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., RA Reese M.G., Reinert K., Remington K., Saunders R.D., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., Spier E., RA Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., RA Turner R., Venter E., Wang A.H., Wang X., Wang Z.Y., Wassarman D.A., RA Weinstock G.M., Weissenbach J., Williams S.M., WoodageT, Worley K.C., RA Wu D., Yang S., Yao Q.A., Ye J., Yeh R.F., Zaveri J.S., Zhan M., Zhang G., RA Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., RA Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [2] {ECO:0000313|Proteomes:UP000000803} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803}; RX PubMed=12537568; RA Celniker S.E., Wheeler D.A., Kronmiller B., Carlson J.W., Halpern A., RA Patel S., Adams M., Champe M., Dugan S.P., Frise E., Hodgson A., RA George R.A., Hoskins R.A., Laverty T., Muzny D.M., Nelson C.R., RA Pacleb J.M., Park S., Pfeiffer B.D., Richards S., Sodergren E.J., RA Svirskas R., Tabor P.E., Wan K., Stapleton M., Sutton G.G., Venter C., RA Weinstock G., Scherer S.E., Myers E.W., Gibbs R.A., Rubin G.M.; RT "Finishing a whole-genome shotgun: release 3 of the Drosophila melanogaster RT euchromatic genome sequence."; RL Genome Biol. 3:RESEARCH0079-RESEARCH0079(2002). RN [3] {ECO:0000313|Proteomes:UP000000803} RP GENOME REANNOTATION. RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803}; RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M., RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic RT review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [4] {ECO:0000313|Proteomes:UP000000803} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803}; RX PubMed=12537573; RA Kaminker J.S., Bergman C.M., Kronmiller B., Carlson J., Svirskas R., RA Patel S., Frise E., Wheeler D.A., Lewis S.E., Rubin G.M., Ashburner M., RA Celniker S.E.; RT "The transposable elements of the Drosophila melanogaster euchromatin: a RT genomics perspective."; RL Genome Biol. 3:RESEARCH0084.1-RESEARCH0084.20(2002). RN [5] {ECO:0000313|EMBL:AGB92648.1, ECO:0000313|Proteomes:UP000000803} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803}; RX PubMed=12537574; RA Hoskins R.A., Smith C.D., Carlson J.W., Carvalho A.B., Halpern A., RA Kaminker J.S., Kennedy C., Mungall C.J., Sullivan B.A., Sutton G.G., RA Yasuhara J.C., Wakimoto B.T., Myers E.W., Celniker S.E., Rubin G.M., RA Karpen G.H.; RT "Heterochromatic sequences in a Drosophila whole-genome shotgun assembly."; RL Genome Biol. 3:RESEARCH0085-RESEARCH0085(2002). RN [6] {ECO:0000313|EMBL:AGB92648.1, ECO:0000313|Proteomes:UP000000803} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803}; RX PubMed=16110336; DOI=10.1371/journal.pcbi.0010022; RA Quesneville H., Bergman C.M., Andrieu O., Autard D., Nouaud D., RA Ashburner M., Anxolabehere D.; RT "Combined evidence annotation of transposable elements in genome RT sequences."; RL PLoS Comput. Biol. 1:166-175(2005). RN [7] {ECO:0000313|EMBL:AGB92648.1} RP NUCLEOTIDE SEQUENCE. RA Celniker S., Carlson J., Wan K., Frise E., Hoskins R., Park S., RA Svirskas R., Rubin G.; RL Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases. RN [8] {ECO:0000313|EMBL:AGB92648.1, ECO:0000313|Proteomes:UP000000803} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803}; RX PubMed=17569856; DOI=10.1126/science.1139815; RA Smith C.D., Shu S., Mungall C.J., Karpen G.H.; RT "The Release 5.1 annotation of Drosophila melanogaster heterochromatin."; RL Science 316:1586-1591(2007). RN [9] {ECO:0000313|EMBL:AGB92648.1, ECO:0000313|Proteomes:UP000000803} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803}; RX PubMed=17569867; DOI=10.1126/science.1139816; RA Hoskins R.A., Carlson J.W., Kennedy C., Acevedo D., Evans-Holm M., RA Frise E., Wan K.H., Park S., Mendez-Lago M., Rossi F., Villasante A., RA Dimitri P., Karpen G.H., Celniker S.E.; RT "Sequence finishing and mapping of Drosophila melanogaster RT heterochromatin."; RL Science 316:1625-1628(2007). RN [10] {ECO:0000313|EMBL:ACH92218.1} RP NUCLEOTIDE SEQUENCE. RA Carlson J., Booth B., Frise E., Park S., Wan K., Yu C., Celniker S.; RL Submitted (SEP-2008) to the EMBL/GenBank/DDBJ databases. RN [11] {ECO:0000313|EMBL:AGB92648.1} RP NUCLEOTIDE SEQUENCE. RX PubMed=26109357; DOI=.1534/g3.115.018929; RG FlyBase Consortium; RA Matthews B.B., Dos Santos G., Crosby M.A., Emmert D.B., St Pierre S.E., RA Gramates L.S., Zhou P., Schroeder A.J., Falls K., Strelets V., Russo S.M., RA Gelbart W.M., null; RT "Gene Model Annotations for Drosophila melanogaster: Impact of High- RT Throughput Data."; RL G3 (Bethesda) 5:1721-1736(2015). RN [12] {ECO:0000313|EMBL:AGB92648.1} RP NUCLEOTIDE SEQUENCE. RX PubMed=26109356; DOI=.1534/g3.115.018937; RG FlyBase Consortium; RA Crosby M.A., Gramates L.S., Dos Santos G., Matthews B.B., St Pierre S.E., RA Zhou P., Schroeder A.J., Falls K., Emmert D.B., Russo S.M., Gelbart W.M., RA null; RT "Gene Model Annotations for Drosophila melanogaster: The Rule-Benders."; RL G3 (Bethesda) 5:1737-1749(2015). RN [13] {ECO:0000313|EMBL:AGB92648.1} RP NUCLEOTIDE SEQUENCE. RX PubMed=25589440; RA Hoskins R.A., Carlson J.W., Wan K.H., Park S., Mendez I., Galle S.E., RA Booth B.W., Pfeiffer B.D., George R.A., Svirskas R., Krzywinski M., RA Schein J., Accardo M.C., Damia E., Messina G., Mendez-Lago M., RA de Pablos B., Demakova O.V., Andreyeva E.N., Boldyreva L.V., Marra M., RA Carvalho A.B., Dimitri P., Villasante A., Zhimulev I.F., Rubin G.M., RA Karpen G.H., Celniker S.E.; RT "The Release 6 reference sequence of the Drosophila melanogaster genome."; RL Genome Res. 25:445-458(2015). RN [14] {ECO:0000313|EMBL:AGB92648.1} RP NUCLEOTIDE SEQUENCE. RG Berkeley Drosophila Genome Project; RA Celniker S., Carlson J., Wan K., Pfeiffer B., Frise E., George R., RA Hoskins R., Stapleton M., Pacleb J., Park S., Svirskas R., Smith E., Yu C., RA Rubin G.; RT "Drosophila melanogaster release 4 sequence."; RL Submitted (NOV-2022) to the EMBL/GenBank/DDBJ databases. RN [15] {ECO:0000313|EMBL:AGB92648.1} RP NUCLEOTIDE SEQUENCE. RG FlyBase; RL Submitted (NOV-2022) to the EMBL/GenBank/DDBJ databases. 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 -!- PATHWAY: Lipid metabolism. {ECO:0000256|ARBA:ARBA00005189}. CC -!- PATHWAY: Phospholipid metabolism; alpha-glycerophosphate cycle. CC {ECO:0000256|ARBA:ARBA00005192}. CC -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}. 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; BT044153; ACH92218.1; -; mRNA. DR EMBL; AE014134; AGB92648.1; -; Genomic_DNA. DR RefSeq; NP_001260112.1; NM_001273183.2. DR RefSeq; NP_476565.1; NM_057217.4. DR SMR; B5RIM9; -. DR DNASU; 33824; -. DR EnsemblMetazoa; FBtr0079146; FBpp0078777; FBgn0001128. DR EnsemblMetazoa; FBtr0333229; FBpp0305431; FBgn0001128. DR GeneID; 33824; -. DR KEGG; dme:Dmel_CG9042; -. DR AGR; FB:FBgn0001128; -. DR CTD; 33824; -. DR FlyBase; FBgn0001128; Gpdh1. DR VEuPathDB; VectorBase:FBgn0001128; -. DR OMA; NRMFGNM; -. DR OrthoDB; 3675564at2759; -. DR UniPathway; UPA00086; -. DR BioGRID-ORCS; 33824; 1 hit in 3 CRISPR screens. DR ChiTaRS; Gpdh; fly. DR GenomeRNAi; 33824; -. DR Proteomes; UP000000803; Chromosome 2L. DR Bgee; FBgn0001128; Expressed in capitellum (Drosophila) and 24 other cell types or tissues. DR ExpressionAtlas; B5RIM9; baseline and differential. 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:0006650; P:glycerophospholipid metabolic process; IEA:UniProtKB-UniPathway. 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 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:B5RIM9}; KW Reference proteome {ECO:0000313|Proteomes:UP000000803}. FT DOMAIN 7..174 FT /note="Glycerol-3-phosphate dehydrogenase NAD-dependent N- FT terminal" FT /evidence="ECO:0000259|Pfam:PF01210" FT DOMAIN 195..340 FT /note="Glycerol-3-phosphate dehydrogenase NAD-dependent C- FT terminal" FT /evidence="ECO:0000259|Pfam:PF07479" FT ACT_SITE 206 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 98 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|PIRSR:PIRSR000114-3" FT BINDING 121 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR000114-2" FT BINDING 155 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|PIRSR:PIRSR000114-3" FT BINDING 270..271 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR000114-2" FT BINDING 270 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|PIRSR:PIRSR000114-3" FT BINDING 297 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|PIRSR:PIRSR000114-3" FT BINDING 299 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|PIRSR:PIRSR000114-3" SQ SEQUENCE 360 AA; 39329 MW; 7E7FB6FDF432CDD0 CRC64; MADKVNVCIV GSGNWGSAIA KIVGANAAAL PEFEERVTMF VYEELIDGKK LTEIINETHE NVKYLKGHKL PPNVVAVPDL VEAAKNADIL IFVVPHQFIP NFCKQLLGKI KPNAIAISLI KGFDKAEGGG IDLISHIITR HLKIPCAVLM GANLANEVAE GNFCETTIGC TDKKYGKVLR DLFQANHFRV VVVDDADAVE VCGALKNIVA CGAGFVDGLK LGDNTKAAVI RLGLMEMIRF VDVFYPGSKL STFFESCGVA DLITTCYGGR NRRVSEAFVT SGKTIEELEK EMLNGQKLQG PPTAEEVNYM LKNKGLEDKF PLFTAIHKIC TNQLKPNDLI DCIRNHPEHM DTSIMPSPKL //