ID E8U3R4_DEIML Unreviewed; 539 AA. AC E8U3R4; DT 05-APR-2011, integrated into UniProtKB/TrEMBL. DT 05-APR-2011, sequence version 1. DT 27-MAR-2024, entry version 52. DE SubName: Full=Glycerol-3-phosphate dehydrogenase {ECO:0000313|EMBL:ADV68757.1}; DE EC=1.1.5.3 {ECO:0000313|EMBL:ADV68757.1}; GN OrderedLocusNames=Deima_3128 {ECO:0000313|EMBL:ADV68757.1}; OS Deinococcus maricopensis (strain DSM 21211 / LMG 22137 / NRRL B-23946 / OS LB-34). OC Bacteria; Deinococcota; Deinococci; Deinococcales; Deinococcaceae; OC Deinococcus. OX NCBI_TaxID=709986 {ECO:0000313|EMBL:ADV68757.1, ECO:0000313|Proteomes:UP000008635}; RN [1] {ECO:0000313|EMBL:ADV68757.1, ECO:0000313|Proteomes:UP000008635} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 21211 / LMG 22137 / NRRL B-23946 / LB-34 RC {ECO:0000313|Proteomes:UP000008635}; RX PubMed=21677853; DOI=10.4056/sigs.1633949; RA Pukall R., Zeytun A., Lucas S., Lapidus A., Hammon N., Deshpande S., RA Nolan M., Cheng J.F., Pitluck S., Liolios K., Pagani I., Mikhailova N., RA Ivanova N., Mavromatis K., Pati A., Tapia R., Han C., Goodwin L., Chen A., RA Palaniappan K., Land M., Hauser L., Chang Y.J., Jeffries C.D., RA Brambilla E.M., Rohde M., Goker M., Detter J.C., Woyke T., Bristow J., RA Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.; RT "Complete genome sequence of Deinococcus maricopensis type strain (LB- RT 34)."; RL Stand. Genomic Sci. 4:163-172(2011). RN [2] {ECO:0000313|Proteomes:UP000008635} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 21211 / LMG 22137 / NRRL B-23946 / LB-34 RC {ECO:0000313|Proteomes:UP000008635}; RG US DOE Joint Genome Institute (JGI-PGF); RA Lucas S., Copeland A., Lapidus A., Goodwin L., Pitluck S., Kyrpides N., RA Mavromatis K., Pagani I., Ivanova N., Ovchinnikova G., Zeytun A., RA Detter J.C., Han C., Land M., Hauser L., Markowitz V., Cheng J.-F., RA Hugenholtz P., Woyke T., Wu D., Pukall R., Gehrich-Schroeter G., RA Brambilla E., Klenk H.-P., Eisen J.A.; RT "The complete genome of Deinococcus maricopensis DSM 21211."; RL Submitted (JAN-2011) 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; CP002454; ADV68757.1; -; Genomic_DNA. DR RefSeq; WP_013558260.1; NC_014958.1. DR AlphaFoldDB; E8U3R4; -. DR STRING; 709986.Deima_3128; -. DR KEGG; dmr:Deima_3128; -. DR eggNOG; COG0578; Bacteria. DR HOGENOM; CLU_015740_5_1_0; -. DR OrthoDB; 9801699at2; -. DR Proteomes; UP000008635; Chromosome. DR GO; GO:0009331; C:glycerol-3-phosphate dehydrogenase complex; IEA:InterPro. DR GO; GO:0004368; F:glycerol-3-phosphate dehydrogenase (quinone) activity; IEA:UniProtKB-EC. 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:SF37; AEROBIC GLYCEROL-3-PHOSPHATE DEHYDROGENASE; 1. DR PANTHER; PTHR11985; GLYCEROL-3-PHOSPHATE DEHYDROGENASE; 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. PE 3: Inferred from homology; KW FAD {ECO:0000256|ARBA:ARBA00022827}; KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630}; KW Glycerol metabolism {ECO:0000256|ARBA:ARBA00022798}; KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, KW ECO:0000313|EMBL:ADV68757.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008635}. FT DOMAIN 17..364 FT /note="FAD dependent oxidoreductase" FT /evidence="ECO:0000259|Pfam:PF01266" FT DOMAIN 408..500 FT /note="Alpha-glycerophosphate oxidase C-terminal" FT /evidence="ECO:0000259|Pfam:PF16901" SQ SEQUENCE 539 AA; 59095 MW; DC957D0FDAF37627 CRC64; MLDRDARFSA LRGQTFDLLI VGGGITGAGL LREATRAGLH AALVEARDYA WGSSSRSSKM VHGGLRYLQH AQFRVTLDSV RERERLLREA PGLIEPLGFL MAVYDDHPER RPLYAAGLTL YDLLARRRSH QYHAAPDFAL LAPHLRRAGL TGGFRYADAA TDDARLVLRV LRDATRDGAL ALNYAPVTKL HLNRGEVRGA SVRDAETGDE HLVRARIVIN ATGAHTDALR GELGCPPALR PLRGSHLVFP QTRFPASQAI AFQHPLDGRN VFVSPWQGHV LVGTTDLDHL TALTDDPRIT PQETSYLMAG VTHAFPTLGL TLRDATAAWA GVRPVIGHGH ADPSREARDT LIREERGLLS VTGGKLTTFR ATAHAALRVA TRRLGLPLHL PDTPFFDPVD EAALPGTLSV AQRRRLAGTY GPDAVELLRG AQPGDLHPMP GTHTLWAEVR HAARHEDVRG LSDLLLRRAR VGFTLGTSSL ALLPRVRDVT RDALGWSSER WNAEERAYEA LIRAAYSVPD ENDVPDWRLA LARAQHARA //