ID C5QSL7_9STAP Unreviewed; 332 AA. AC C5QSL7; DT 01-SEP-2009, integrated into UniProtKB/TrEMBL. DT 01-SEP-2009, sequence version 1. DT 05-DEC-2018, entry version 61. DE RecName: Full=Glycerol-3-phosphate dehydrogenase [NAD(P)+] {ECO:0000256|HAMAP-Rule:MF_00394}; DE EC=1.1.1.94 {ECO:0000256|HAMAP-Rule:MF_00394}; DE AltName: Full=NAD(P)H-dependent glycerol-3-phosphate dehydrogenase {ECO:0000256|HAMAP-Rule:MF_00394}; GN Name=gpsA {ECO:0000256|HAMAP-Rule:MF_00394, GN ECO:0000313|EMBL:EES40120.1}; GN ORFNames=HMPREF0793_2223 {ECO:0000313|EMBL:EES40120.1}; OS Staphylococcus caprae M23864:W1. OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae; OC Staphylococcus. OX NCBI_TaxID=525378 {ECO:0000313|EMBL:EES40120.1, ECO:0000313|Proteomes:UP000003152}; RN [1] {ECO:0000313|EMBL:EES40120.1, ECO:0000313|Proteomes:UP000003152} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=M23864:W1 {ECO:0000313|EMBL:EES40120.1, RC ECO:0000313|Proteomes:UP000003152}; RA Qin X., Bachman B., Battles P., Bell A., Bess C., Bickham C., RA Chaboub L., Chen D., Coyle M., Deiros D.R., Dinh H., Forbes L., RA Fowler G., Francisco L., Fu Q., Gubbala S., Hale W., Han Y., RA Hemphill L., Highlander S.K., Hirani K., Hogues M., Jackson L., RA Jakkamsetti A., Javaid M., Jiang H., Korchina V., Kovar C., Lara F., RA Lee S., Mata R., Mathew T., Moen C., Morales K., Munidasa M., RA Nazareth L., Ngo R., Nguyen L., Okwuonu G., Ongeri F., Patil S., RA Petrosino J., Pham C., Pham P., Pu L.-L., Puazo M., Raj R., Reid J., RA Rouhana J., Saada N., Shang Y., Simmons D., Thornton R., Warren J., RA Weissenberger G., Zhang J., Zhang L., Zhou C., Zhu D., Muzny D., RA Worley K., Gibbs R.; RL Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: CC Reaction=NADP(+) + sn-glycerol 3-phosphate = dihydroxyacetone CC phosphate + H(+) + NADPH; Xref=Rhea:RHEA:11096, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57597, ChEBI:CHEBI:57642, CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.94; CC Evidence={ECO:0000256|HAMAP-Rule:MF_00394, CC ECO:0000256|RuleBase:RU000439, ECO:0000256|SAAS:SAAS01090081}; CC -!- PATHWAY: Membrane lipid metabolism; glycerophospholipid CC metabolism. {ECO:0000256|HAMAP-Rule:MF_00394, CC ECO:0000256|RuleBase:RU004280, ECO:0000256|SAAS:SAAS01090075}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00394, CC ECO:0000256|RuleBase:RU004280, ECO:0000256|SAAS:SAAS01090105}. CC -!- SIMILARITY: Belongs to the NAD-dependent glycerol-3-phosphate CC dehydrogenase family. {ECO:0000256|HAMAP-Rule:MF_00394, CC ECO:0000256|RuleBase:RU000437, ECO:0000256|SAAS:SAAS00567958}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EES40120.1}. 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; ACJB01000063; EES40120.1; -; Genomic_DNA. DR RefSeq; WP_002442972.1; NZ_GG696773.1. DR ProteinModelPortal; C5QSL7; -. DR STRING; 525378.HMPREF0793_2223; -. DR EnsemblBacteria; EES40120; EES40120; HMPREF0793_2223. DR eggNOG; ENOG4105CSF; Bacteria. DR eggNOG; COG0240; LUCA. DR OrthoDB; POG091H060E; -. DR UniPathway; UPA00940; -. DR Proteomes; UP000003152; Unassembled WGS sequence. DR GO; GO:0009331; C:glycerol-3-phosphate dehydrogenase complex; IEA:InterPro. DR GO; GO:0047952; F:glycerol-3-phosphate dehydrogenase [NAD(P)+] activity; IEA:UniProtKB-UniRule. DR GO; GO:0004367; F:glycerol-3-phosphate dehydrogenase [NAD+] activity; IEA:UniProtKB-EC. DR GO; GO:0051287; F:NAD binding; IEA:InterPro. DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro. DR GO; GO:0046167; P:glycerol-3-phosphate biosynthetic process; IEA:UniProtKB-UniRule. DR GO; GO:0046168; P:glycerol-3-phosphate catabolic process; IEA:InterPro. DR GO; GO:0006650; P:glycerophospholipid metabolic process; IEA:UniProtKB-UniPathway. DR GO; GO:0008654; P:phospholipid biosynthetic process; IEA:UniProtKB-UniRule. DR Gene3D; 1.10.1040.10; -; 1. DR HAMAP; MF_00394; NAD_Glyc3P_dehydrog; 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; 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 PROSITE; PS00957; NAD_G3PDH; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000003152}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00394, KW ECO:0000256|SAAS:SAAS01090070}; KW Lipid biosynthesis {ECO:0000256|HAMAP-Rule:MF_00394, KW ECO:0000256|SAAS:SAAS01090084}; KW Lipid metabolism {ECO:0000256|HAMAP-Rule:MF_00394, KW ECO:0000256|SAAS:SAAS01090080}; KW NAD {ECO:0000256|HAMAP-Rule:MF_00394, ECO:0000256|PIRSR:PIRSR000114-3, KW ECO:0000256|RuleBase:RU000437, ECO:0000256|SAAS:SAAS01090086}; KW Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_00394, KW ECO:0000256|RuleBase:RU000437, ECO:0000256|SAAS:SAAS00445907, KW ECO:0000313|EMBL:EES40120.1}; KW Phospholipid biosynthesis {ECO:0000256|HAMAP-Rule:MF_00394, KW ECO:0000256|RuleBase:RU004280, ECO:0000256|SAAS:SAAS01090074}; KW Phospholipid metabolism {ECO:0000256|HAMAP-Rule:MF_00394, KW ECO:0000256|SAAS:SAAS01090066}. FT DOMAIN 3 160 NAD_Gly3P_dh_N. {ECO:0000259|Pfam: FT PF01210}. FT DOMAIN 181 321 NAD_Gly3P_dh_C. {ECO:0000259|Pfam: FT PF07479}. FT NP_BIND 8 13 NAD. {ECO:0000256|HAMAP-Rule:MF_00394, FT ECO:0000256|PIRSR:PIRSR000114-3}. FT REGION 256 257 Substrate binding. {ECO:0000256|HAMAP- FT Rule:MF_00394, ECO:0000256|PIRSR: FT PIRSR000114-2}. FT ACT_SITE 192 192 Proton acceptor. {ECO:0000256|HAMAP-Rule: FT MF_00394, ECO:0000256|PIRSR:PIRSR000114- FT 1}. FT BINDING 106 106 NAD; via amide nitrogen. FT {ECO:0000256|HAMAP-Rule:MF_00394}. FT BINDING 106 106 Substrate. {ECO:0000256|HAMAP-Rule: FT MF_00394, ECO:0000256|PIRSR:PIRSR000114- FT 2}. FT BINDING 141 141 NAD; via amide nitrogen. FT {ECO:0000256|HAMAP-Rule:MF_00394, FT ECO:0000256|PIRSR:PIRSR000114-3}. FT BINDING 256 256 NAD. {ECO:0000256|HAMAP-Rule:MF_00394, FT ECO:0000256|PIRSR:PIRSR000114-3}. FT BINDING 282 282 NAD. {ECO:0000256|HAMAP-Rule:MF_00394}. SQ SEQUENCE 332 AA; 36070 MW; 7A7022EB471E869F CRC64; MTKITVFGMG SFGTALANVL AQNGHDVLMW GKNNDSVEEL NTHHMNKNYL KEAKLEESIQ ATTDLKQATQ FSDIFLMALP TKAMREVASN IDEMLESKKT FIHVAKGIEN GTFKRVSEML EDSISPEHNA GIGVLSGPSH AEEVVIKQPT TVAASSKDKK ISALIQDLFM NDYLRVYTNN DLVGVELGGA LKNIIAVASG IVAGMGFGDN AKAALMTRGL AEISRLGEKL GADPMTFLGL GGIGDLIVTC TSTHSRNFTL GYKLGQGKTM DDALKEMNMV VEGVYTTKSV YHLAKEENVD MPITSALYRV LFEDIPVKDS VKELMGRDKK AE //