ID A0LP17_SYNFM Unreviewed; 432 AA. AC A0LP17; DT 12-DEC-2006, integrated into UniProtKB/TrEMBL. DT 12-DEC-2006, sequence version 1. DT 27-MAR-2024, entry version 82. DE SubName: Full=Fumarate reductase/succinate dehydrogenase flavoprotein domain protein {ECO:0000313|EMBL:ABK19169.1}; GN OrderedLocusNames=Sfum_3498 {ECO:0000313|EMBL:ABK19169.1}; OS Syntrophobacter fumaroxidans (strain DSM 10017 / MPOB). OC Bacteria; Thermodesulfobacteriota; Syntrophobacteria; Syntrophobacterales; OC Syntrophobacteraceae; Syntrophobacter. OX NCBI_TaxID=335543 {ECO:0000313|EMBL:ABK19169.1, ECO:0000313|Proteomes:UP000001784}; RN [1] {ECO:0000313|EMBL:ABK19169.1, ECO:0000313|Proteomes:UP000001784} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 10017 / MPOB {ECO:0000313|Proteomes:UP000001784}; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., RA Glavina del Rio T., Hammon N., Israni S., Pitluck S., Goltsman E.G., RA Martinez M., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., RA Kim E., Boone D.R., Brockman F., Culley D., Ferry J., Gunsalus R., RA McInerney M.J., Morrison M., Plugge C., Rohlin L., Scholten J., Sieber J., RA Stams A.J.M., Worm P., Henstra A.M., Richardson P.; RT "Complete sequence of Syntrophobacter fumaroxidans MPOB."; RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases. 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; CP000478; ABK19169.1; -; Genomic_DNA. DR RefSeq; WP_011700294.1; NC_008554.1. DR AlphaFoldDB; A0LP17; -. DR STRING; 335543.Sfum_3498; -. DR KEGG; sfu:Sfum_3498; -. DR eggNOG; COG3075; Bacteria. DR HOGENOM; CLU_047793_1_0_7; -. DR InParanoid; A0LP17; -. DR OrthoDB; 140595at2; -. DR Proteomes; UP000001784; Chromosome. DR GO; GO:0004368; F:glycerol-3-phosphate dehydrogenase (quinone) activity; IEA:InterPro. DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1. DR InterPro; IPR003953; FAD-binding_2. DR InterPro; IPR036188; FAD/NAD-bd_sf. DR InterPro; IPR009158; G3P_DH_GlpB_su. DR NCBIfam; TIGR03378; glycerol3P_GlpB; 1. DR Pfam; PF00890; FAD_binding_2; 1. DR PIRSF; PIRSF000141; Anaerobic_G3P_dh; 1. DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1. DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1. PE 4: Predicted; KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630}; KW FMN {ECO:0000256|ARBA:ARBA00022643}; KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}; KW Reference proteome {ECO:0000313|Proteomes:UP000001784}. FT DOMAIN 10..413 FT /note="FAD-dependent oxidoreductase 2 FAD binding" FT /evidence="ECO:0000259|Pfam:PF00890" SQ SEQUENCE 432 AA; 46273 MW; 946B969D623BB406 CRC64; MKSRPDSRLD LIVIGGGLAG TAAACLATTR GLSVARVAAN AGGLAFAGGP LDLLGVYPPR EQMVRDDPWE GISALIEGSP RHPYAVLGVD AVRRAMGEFL AFADSAGLRY CGMAERNVTI ATAVGTLKTA YRVPRSMWRG VTALQDRLPT LIVDFEGMKD FSAAAMVEVL RSRWPRLQAL RVTFPVRFPG IDRHNPLLAE ALESSEIRAK LAEAIRPHLS GVLMVGMPAV LGIRAGDRVV ADLEERLGVG IFEIPTMPPS VPGIRLQSAM EEALRKRGVQ IFDGRRVLCA RTEERLCAGI TVGGAGEWHE TMEAQGIILA TGRFLGGGLS ASRDGISEAL FGLPVVQPPS RDRWHRGSFL DPRGHPVNEA GLAIDDRFRP LGEDGSFAFE NVFAAGSILA HQDWVRTKSG AGLAVSTAHG AVEGFLRYRS GK //