ID A9WN08_RENSM Unreviewed; 146 AA. AC A9WN08; DT 05-FEB-2008, integrated into UniProtKB/TrEMBL. DT 05-FEB-2008, sequence version 1. DT 28-JAN-2026, entry version 67. DE SubName: Full=Glycerol-3-phosphate dehydrogenase {ECO:0000313|EMBL:ABY23497.1}; DE EC=1.1.5.3 {ECO:0000313|EMBL:ABY23497.1}; GN OrderedLocusNames=RSal33209_1762 {ECO:0000313|EMBL:ABY23497.1}; OS Renibacterium salmoninarum (strain ATCC 33209 / DSM 20767 / JCM 11484 / OS NBRC 15589 / NCIMB 2235). OC Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales; OC Micrococcaceae; Renibacterium. OX NCBI_TaxID=288705 {ECO:0000313|EMBL:ABY23497.1, ECO:0000313|Proteomes:UP000002007}; RN [1] {ECO:0000313|Proteomes:UP000002007} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33209 / DSM 20767 / JCM 11484 / NBRC 15589 / NCIMB 2235 RC {ECO:0000313|Proteomes:UP000002007}; RX PubMed=18723615; DOI=10.1128/JB.00721-08; RA Wiens G.D., Rockey D.D., Wu Z., Chang J., Levy R., Crane S., Chen D.S., RA Capri G.R., Burnett J.R., Sudheesh P.S., Schipma M.J., Burd H., RA Bhattacharyya A., Rhodes L.D., Kaul R., Strom M.S.; RT "Genome sequence of the fish pathogen Renibacterium salmoninarum suggests RT reductive evolution away from an environmental Arthrobacter ancestor."; RL J. Bacteriol. 190:6970-6982(2008). 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; CP000910; ABY23497.1; -; Genomic_DNA. DR AlphaFoldDB; A9WN08; -. DR STRING; 288705.RSal33209_1762; -. DR KEGG; rsa:RSal33209_1762; -. DR eggNOG; COG0578; Bacteria. DR HOGENOM; CLU_1775901_0_0_11; -. DR Proteomes; UP000002007; Chromosome. DR GO; GO:0004368; F:glycerol-3-phosphate dehydrogenase (quinone) activity; IEA:UniProtKB-EC. DR GO; GO:0046168; P:glycerol-3-phosphate catabolic process; IEA:TreeGrafter. 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; IPR036188; FAD/NAD-bd_sf. DR InterPro; IPR000447; G3P_DH_FAD-dep. DR PANTHER; PTHR11985; GLYCEROL-3-PHOSPHATE DEHYDROGENASE; 1. DR PANTHER; PTHR11985:SF31; GLYCEROL-3-PHOSPHATE DEHYDROGENASE 2; 1. DR SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 1. DR PROSITE; PS00978; FAD_G3PDH_2; 1. PE 4: Predicted; KW FAD {ECO:0000256|ARBA:ARBA00022827}; KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630}; KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, KW ECO:0000313|EMBL:ABY23497.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000002007}. SQ SEQUENCE 146 AA; 16173 MW; 33B2ABEA0D440C52 CRC64; MVTDRGQLKV RASKGIHLVV PRDRFQSTVG LILRTEKSVL FVIPWGRHWI IGTTDTDWKL DKAHPAASAA DIDYVLEHVK KVLKRPLTRE DVEGVYAGLR PLLAGENDST AKLSREHVVA HPVPGLVVVA GGKYTTYRVM AKDAID //