ID A8M5P0_SALAI Unreviewed; 507 AA. AC A8M5P0; DT 04-DEC-2007, integrated into UniProtKB/TrEMBL. DT 04-DEC-2007, sequence version 1. DT 27-MAR-2024, entry version 80. DE SubName: Full=FAD dependent oxidoreductase {ECO:0000313|EMBL:ABV98608.1}; GN OrderedLocusNames=Sare_2773 {ECO:0000313|EMBL:ABV98608.1}; OS Salinispora arenicola (strain CNS-205). OC Bacteria; Actinomycetota; Actinomycetes; Micromonosporales; OC Micromonosporaceae; Salinispora. OX NCBI_TaxID=391037 {ECO:0000313|EMBL:ABV98608.1}; RN [1] {ECO:0000313|EMBL:ABV98608.1} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CNS-205 {ECO:0000313|EMBL:ABV98608.1}; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E., RA Tice H., Pitluck S., Foster B., Schmutz J., Larimer F., Land M., Hauser L., RA Kyrpides N., Ivanova N., Jensen P.R., Moore B.S., Penn K., Jenkins C., RA Udwary D., Xiang L., Gontang E., Richardson P.; RT "Complete sequence of Salinispora arenicola CNS-205."; RL Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases. CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000256|ARBA:ARBA00001974}; CC -!- SIMILARITY: Belongs to the FAD-dependent glycerol-3-phosphate CC dehydrogenase family. {ECO:0000256|ARBA:ARBA00007330}. 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; CP000850; ABV98608.1; -; Genomic_DNA. DR AlphaFoldDB; A8M5P0; -. DR STRING; 391037.Sare_2773; -. DR KEGG; saq:Sare_2773; -. DR PATRIC; fig|391037.6.peg.2810; -. DR eggNOG; COG0578; Bacteria. DR HOGENOM; CLU_015740_5_1_11; -. DR OrthoDB; 9766796at2; -. DR GO; GO:0009331; C:glycerol-3-phosphate dehydrogenase complex; IEA:InterPro. DR GO; GO:0004368; F:glycerol-3-phosphate dehydrogenase (quinone) activity; IEA:InterPro. DR GO; GO:0006071; P:glycerol metabolic process; IEA:UniProtKB-KW. DR GO; GO:0006072; P:glycerol-3-phosphate metabolic process; IEA:InterPro. DR Gene3D; 1.10.8.870; Alpha-glycerophosphate oxidase, cap domain; 1. DR Gene3D; 3.30.9.10; D-Amino Acid Oxidase, subunit A, domain 2; 1. DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1. DR InterPro; IPR031656; DAO_C. DR InterPro; IPR038299; DAO_C_sf. DR InterPro; IPR006076; FAD-dep_OxRdtase. DR InterPro; IPR036188; FAD/NAD-bd_sf. DR InterPro; IPR000447; G3P_DH_FAD-dep. DR PANTHER; PTHR11985; GLYCEROL-3-PHOSPHATE DEHYDROGENASE; 1. DR PANTHER; PTHR11985:SF38; GLYCEROL-3-PHOSPHATE DEHYDROGENASE 1; 1. DR Pfam; PF01266; DAO; 1. DR Pfam; PF16901; DAO_C; 1. DR PRINTS; PR01001; FADG3PDH. DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1. DR PROSITE; PS00978; FAD_G3PDH_2; 1. PE 3: Inferred from homology; KW FAD {ECO:0000256|ARBA:ARBA00022827}; KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630}; KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}. FT DOMAIN 24..352 FT /note="FAD dependent oxidoreductase" FT /evidence="ECO:0000259|Pfam:PF01266" FT DOMAIN 403..504 FT /note="Alpha-glycerophosphate oxidase C-terminal" FT /evidence="ECO:0000259|Pfam:PF16901" SQ SEQUENCE 507 AA; 53597 MW; 5A39F335F14223B3 CRC64; MNSALTGPRR DRELAELAGG KVVDVLVVGL GVTGAGVALD AASRGLSVAA VDAHDLAHGT SRWSSKLVHG GLRYLAHGRV RIAYESAVER HVLMTRTAPH LARALPMLLP ATGYTAGWQD RAAAAGLHAG DLLRACAGTS RRTLPSTRRL RPAEVSAMVP ALRPAGLRGA RLSWDGQLCD DARLVVGLAR AAAARSARIL PGCRVVDLRR DGATVEDART GETLHLTARA VINATGVWAG DLTPHVRLRP SRGTHIVLSA ASLGGLWAGL TIPVPGEFSR YVLALPQTDG LVYVGLTDEP VDGPIPDVPE PTEADIAFLL DVLNSALDRP LRRTDVLGAY AGLRPLLADA DDRTADLSRR HAVIEDPDGV ISVVGGKLTT YRRMAEDAVD TAVRRRALTA GACRTRRLPL PGAGSGADLA RVPAPRRLVA RYGVEAVDVL AEAPAHLHRP IGPDIPVTGA ELLWAVRHEL ALTVDDLLDR RTRLGLVPAY RDAALPVARE VLAVAGR //