ID B8CW98_HALOH Unreviewed; 503 AA. AC B8CW98; DT 03-MAR-2009, integrated into UniProtKB/TrEMBL. DT 03-MAR-2009, sequence version 1. DT 27-MAR-2024, entry version 61. DE SubName: Full=Glycerol-3-phosphate dehydrogenase {ECO:0000313|EMBL:ACL69567.1}; DE EC=1.1.5.3 {ECO:0000313|EMBL:ACL69567.1}; GN OrderedLocusNames=Hore_08100 {ECO:0000313|EMBL:ACL69567.1}; OS Halothermothrix orenii (strain H 168 / OCM 544 / DSM 9562). OC Bacteria; Bacillota; Clostridia; Halanaerobiales; Halothermotrichaceae; OC Halothermothrix. OX NCBI_TaxID=373903 {ECO:0000313|EMBL:ACL69567.1, ECO:0000313|Proteomes:UP000000719}; RN [1] {ECO:0000313|EMBL:ACL69567.1, ECO:0000313|Proteomes:UP000000719} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=H 168 / OCM 544 / DSM 9562 {ECO:0000313|Proteomes:UP000000719}; RX PubMed=19145256; DOI=10.1371/journal.pone.0004192; RA Mavromatis K., Ivanova N., Anderson I., Lykidis A., Hooper S.D., Sun H., RA Kunin V., Lapidus A., Hugenholtz P., Patel B., Kyrpides N.C.; RT "Genome analysis of the anaerobic thermohalophilic bacterium RT Halothermothrix orenii."; RL PLoS ONE 4:E4192-E4192(2009). 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; CP001098; ACL69567.1; -; Genomic_DNA. DR RefSeq; WP_012635755.1; NC_011899.1. DR AlphaFoldDB; B8CW98; -. DR STRING; 373903.Hore_08100; -. DR KEGG; hor:Hore_08100; -. DR eggNOG; COG0579; Bacteria. DR HOGENOM; CLU_024775_3_1_9; -. DR OrthoDB; 9801699at2; -. DR Proteomes; UP000000719; Chromosome. DR GO; GO:0004368; F:glycerol-3-phosphate dehydrogenase (quinone) activity; IEA:UniProtKB-EC. DR CDD; cd19946; GlpA-like_Fer2_BFD-like; 1. DR Gene3D; 1.10.10.1100; BFD-like [2Fe-2S]-binding 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; IPR007419; BFD-like_2Fe2S-bd_dom. DR InterPro; IPR041854; BFD-like_2Fe2S-bd_dom_sf. DR InterPro; IPR006076; FAD-dep_OxRdtase. DR InterPro; IPR036188; FAD/NAD-bd_sf. DR PANTHER; PTHR42720:SF1; GLYCEROL 3-PHOSPHATE OXIDASE; 1. DR PANTHER; PTHR42720; GLYCEROL-3-PHOSPHATE DEHYDROGENASE; 1. DR Pfam; PF01266; DAO; 1. DR Pfam; PF04324; Fer2_BFD; 1. DR SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 1. DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1. PE 4: Predicted; KW Oxidoreductase {ECO:0000313|EMBL:ACL69567.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000719}. FT DOMAIN 4..352 FT /note="FAD dependent oxidoreductase" FT /evidence="ECO:0000259|Pfam:PF01266" FT DOMAIN 408..462 FT /note="BFD-like [2Fe-2S]-binding" FT /evidence="ECO:0000259|Pfam:PF04324" SQ SEQUENCE 503 AA; 54885 MW; 1FF9EE312A460F0D CRC64; MRADVIIIGS GVVGSAIARR LARYNLDIIL LEKEHDVAMG TSKANSGIIH AGYNAPYDSL KGRLNVKSNP EFDKLCRDLR VPFKRIGSLV VGFDDKDLKI LKEEKENGEK AGIKDLEIVK GKRLFEIEPN LNPEAMYALY APTAGIISPH QFTIALADSA ALNGVKVMLL TEARNIKTEN GMITGVETNR GFIAAKVVIN AAGVYAGNIA SLAGDSSISI TPRKGEYHLL DKEWGDKVNH VLFPIPSTVS KGILVTPTVH GNLLIGPNSY NVEDPEDVST TTSGLDEVYN GARRLVPSIN RRDVIASFAG LRAAASGEDF IIGSSSHIKG LIHAAGIQSP GLSSAPAIAE KVEEIFKDIA DEFSLEISYK DDFKETLPEY PCFSEKLEKS HEQEWNNLVR ENPDFGEIVC RCERVTKGEI IAAIHRPVPA LSLDAIKRRT RAGMGRCQGG FCGHRVLEIL SEELNISPLE VTKKGGESKI LMRKTKDTEH QYEQMEVGVG ENV //