ID E8N143_ANATU Unreviewed; 386 AA. AC E8N143; DT 05-APR-2011, integrated into UniProtKB/TrEMBL. DT 05-APR-2011, sequence version 1. DT 27-MAR-2024, entry version 57. DE SubName: Full=FAD dependent oxidoreductase family protein {ECO:0000313|EMBL:BAJ64786.1}; GN OrderedLocusNames=ANT_27600 {ECO:0000313|EMBL:BAJ64786.1}; OS Anaerolinea thermophila (strain DSM 14523 / JCM 11388 / NBRC 100420 / OS UNI-1). OC Bacteria; Chloroflexota; Anaerolineae; Anaerolineales; Anaerolineaceae; OC Anaerolinea. OX NCBI_TaxID=926569 {ECO:0000313|EMBL:BAJ64786.1, ECO:0000313|Proteomes:UP000008922}; RN [1] {ECO:0000313|EMBL:BAJ64786.1, ECO:0000313|Proteomes:UP000008922} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 14523 / JCM 11388 / NBRC 100420 / UNI-1 RC {ECO:0000313|Proteomes:UP000008922}; RA Narita-Yamada S., Kishi E., Watanabe Y., Takasaki K., Ankai A., Oguchi A., RA Fukui S., Takahashi M., Yashiro I., Hosoyama A., Sekiguchi Y., Hanada S., RA Fujita N.; RT "Whole genome sequence of Anaerolinea thermophila UNI-1."; RL Submitted (DEC-2010) 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; AP012029; BAJ64786.1; -; Genomic_DNA. DR RefSeq; WP_013561134.1; NC_014960.1. DR AlphaFoldDB; E8N143; -. DR STRING; 926569.ANT_27600; -. DR GeneID; 78351027; -. DR KEGG; atm:ANT_27600; -. DR eggNOG; COG0578; Bacteria. DR HOGENOM; CLU_015740_0_1_0; -. DR InParanoid; E8N143; -. DR OrthoDB; 9801699at2; -. DR Proteomes; UP000008922; 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:InterPro. DR GO; GO:0006072; P:glycerol-3-phosphate metabolic process; IEA:InterPro. DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 3. DR InterPro; IPR006076; FAD-dep_OxRdtase. DR InterPro; IPR036188; FAD/NAD-bd_sf. DR InterPro; IPR000447; G3P_DH_FAD-dep. DR PANTHER; PTHR11985:SF36; ANAEROBIC GLYCEROL-3-PHOSPHATE DEHYDROGENASE SUBUNIT A; 1. DR PANTHER; PTHR11985; GLYCEROL-3-PHOSPHATE DEHYDROGENASE; 1. DR Pfam; PF01266; DAO; 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 Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}; KW Reference proteome {ECO:0000313|Proteomes:UP000008922}. FT DOMAIN 6..347 FT /note="FAD dependent oxidoreductase" FT /evidence="ECO:0000259|Pfam:PF01266" SQ SEQUENCE 386 AA; 42018 MW; 3E3F4B5F8A665A45 CRC64; MTKPHAIVIG AGFTGVAIAW DLTQRGFRVS VVERGPIANG TSGRTHGLLH SGARYAVNDQ ESAIECIQEN LILRRIVPDA IEPNGGLFVA VQEEDLAYRE KFIEGCAACG IPIRELTPQE VLRLEPNLNP RLLTAFTVPD ATFDPLRLAL AFAASAKAGG AQFYLYTDVV DLLRDGRGNV CGVKAWNRAA DQRFHLPAEV VINATGAWVG QITAMAGVQV PITPTPGVMV AYDKRLTQRA INLLNEPGDG DIVLPQRRMM VVGTTSFTIE DPDYVPVYED HVALMMERGA ALIPALRQTR ERGAYMATRP LIGATAPGRS ISRTFKAYDH AETDGIEGLV TITGGKATTL RLMAEKTVDV VCRKFGIEVP CRTAETPLLS YRKFYQ //