ID C5QSL7_9STAP Unreviewed; 332 AA. AC C5QSL7; DT 01-SEP-2009, integrated into UniProtKB/TrEMBL. DT 01-SEP-2009, sequence version 1. DT 19-JAN-2022, entry version 73. 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., Chaboub L., RA Chen D., Coyle M., Deiros D.R., Dinh H., Forbes L., Fowler G., RA Francisco L., Fu Q., Gubbala S., Hale W., Han Y., Hemphill L., RA Highlander S.K., Hirani K., Hogues M., Jackson L., Jakkamsetti A., RA Javaid M., Jiang H., Korchina V., Kovar C., Lara F., Lee S., Mata R., RA Mathew T., Moen C., Morales K., Munidasa M., Nazareth L., Ngo R., RA Nguyen L., Okwuonu G., Ongeri F., Patil S., Petrosino J., Pham C., Pham P., RA Pu L.-L., Puazo M., Raj R., Reid J., Rouhana J., Saada N., Shang Y., RA Simmons D., Thornton R., Warren J., Weissenberger G., Zhang J., Zhang L., RA Zhou C., Zhu D., Muzny D., Worley K., Gibbs R.; RL Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: CC Reaction=6-phospho-D-gluconate + NADP(+) = CO2 + D-ribulose 5-phosphate CC + NADPH; Xref=Rhea:RHEA:10116, ChEBI:CHEBI:16526, ChEBI:CHEBI:57783, CC ChEBI:CHEBI:58121, ChEBI:CHEBI:58349, ChEBI:CHEBI:58759; EC=1.1.1.44; CC Evidence={ECO:0000256|ARBA:ARBA00000530}; 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=1.1.1.94; Evidence={ECO:0000256|HAMAP- CC Rule:MF_00394}; CC -!- CATALYTIC ACTIVITY: CC Reaction=NADP(+) + sn-glycerol 3-phosphate = dihydroxyacetone phosphate CC + H(+) + NADPH; Xref=Rhea:RHEA:11096, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:57597, ChEBI:CHEBI:57642, ChEBI:CHEBI:57783, CC ChEBI:CHEBI:58349; EC=1.1.1.94; Evidence={ECO:0000256|HAMAP- CC Rule:MF_00394, ECO:0000256|RuleBase:RU000439}; CC -!- PATHWAY: Membrane lipid metabolism; glycerophospholipid metabolism. CC {ECO:0000256|HAMAP-Rule:MF_00394, ECO:0000256|RuleBase:RU004280}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00394, CC ECO:0000256|RuleBase:RU004280}. CC -!- SIMILARITY: Belongs to the NAD-dependent glycerol-3-phosphate CC dehydrogenase family. {ECO:0000256|ARBA:ARBA00011009, CC ECO:0000256|HAMAP-Rule:MF_00394, ECO:0000256|RuleBase:RU000437}. CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ CC whole genome shotgun (WGS) entry which is preliminary data. CC {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 STRING; 525378.HMPREF0793_2223; -. DR EnsemblBacteria; EES40120; EES40120; HMPREF0793_2223. DR GeneID; 58051172; -. DR eggNOG; COG0240; Bacteria. DR HOGENOM; CLU_033449_0_2_9; -. DR UniPathway; UPA00940; -. DR Proteomes; UP000003152; Unassembled WGS sequence. DR GO; GO:0009331; C:glycerol-3-phosphate dehydrogenase complex; IEA:InterPro. DR GO; GO:0004367; F:glycerol-3-phosphate dehydrogenase [NAD+] activity; IEA:InterPro. DR GO; GO:0106257; F:glycerol-3-phosphate dehydrogenase [NADP+] activity; IEA:RHEA. DR GO; GO:0051287; F:NAD binding; IEA:InterPro. DR GO; GO:0004616; F:phosphogluconate dehydrogenase (decarboxylating) activity; IEA:UniProtKB-EC. 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 PANTHER; PTHR11728; PTHR11728; 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; SSF48179; 1. DR SUPFAM; SSF51735; SSF51735; 1. DR PROSITE; PS00957; NAD_G3PDH; 1. PE 3: Inferred from homology; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00394}; KW Lipid biosynthesis {ECO:0000256|ARBA:ARBA00022516, ECO:0000256|HAMAP- KW Rule:MF_00394}; KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098, ECO:0000256|HAMAP- KW Rule:MF_00394}; KW NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|HAMAP-Rule:MF_00394}; KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, ECO:0000256|HAMAP- KW Rule:MF_00394}; KW Phospholipid biosynthesis {ECO:0000256|ARBA:ARBA00023209, KW ECO:0000256|HAMAP-Rule:MF_00394}; KW Phospholipid metabolism {ECO:0000256|ARBA:ARBA00023264, ECO:0000256|HAMAP- KW Rule:MF_00394}. FT DOMAIN 3..160 FT /note="NAD_Gly3P_dh_N" FT /evidence="ECO:0000259|Pfam:PF01210" FT DOMAIN 181..321 FT /note="NAD_Gly3P_dh_C" FT /evidence="ECO:0000259|Pfam:PF07479" FT NP_BIND 8..13 FT /note="NAD" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00394, FT ECO:0000256|PIRSR:PIRSR000114-3" FT REGION 256..257 FT /note="Substrate binding" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00394, FT ECO:0000256|PIRSR:PIRSR000114-2" FT ACT_SITE 192 FT /note="Proton acceptor" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00394, FT ECO:0000256|PIRSR:PIRSR000114-1" FT BINDING 106 FT /note="NAD; via amide nitrogen" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00394" FT BINDING 106 FT /note="Substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00394, FT ECO:0000256|PIRSR:PIRSR000114-2" FT BINDING 141 FT /note="NAD; via amide nitrogen" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00394, FT ECO:0000256|PIRSR:PIRSR000114-3" FT BINDING 256 FT /note="NAD" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00394, FT ECO:0000256|PIRSR:PIRSR000114-3" FT BINDING 282 FT /note="NAD" FT /evidence="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 //