ID Q2S2J4_SALRD Unreviewed; 524 AA. AC Q2S2J4; DT 24-JAN-2006, integrated into UniProtKB/TrEMBL. DT 24-JAN-2006, sequence version 1. DT 27-MAR-2024, entry version 101. DE SubName: Full=Glycerol-3-phosphate dehydrogenase, anaerobic {ECO:0000313|EMBL:ABC44790.1}; DE EC=1.1.5.3 {ECO:0000313|EMBL:ABC44790.1}; GN Name=glpA {ECO:0000313|EMBL:ABC44790.1}; GN OrderedLocusNames=SRU_1463 {ECO:0000313|EMBL:ABC44790.1}; OS Salinibacter ruber (strain DSM 13855 / M31). OC Bacteria; Rhodothermota; Rhodothermia; Rhodothermales; Salinibacteraceae; OC Salinibacter. OX NCBI_TaxID=309807 {ECO:0000313|EMBL:ABC44790.1, ECO:0000313|Proteomes:UP000008674}; RN [1] {ECO:0000313|EMBL:ABC44790.1, ECO:0000313|Proteomes:UP000008674} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 13855 / CECT 5946 / M31 RC {ECO:0000313|Proteomes:UP000008674}; RX PubMed=16330755; DOI=10.1073/pnas.0509073102; RA Mongodin E.F., Nelson K.E., Daugherty S., Deboy R.T., Wister J., Khouri H., RA Weidman J., Walsh D.A., Papke R.T., Sanchez Perez G., Sharma A.K., RA Nesbo C.L., MacLeod D., Bapteste E., Doolittle W.F., Charlebois R.L., RA Legault B., Rodriguez-Valera F.; RT "The genome of Salinibacter ruber: convergence and gene exchange among RT hyperhalophilic bacteria and archaea."; RL Proc. Natl. Acad. Sci. U.S.A. 102:18147-18152(2005). 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; CP000159; ABC44790.1; -; Genomic_DNA. DR RefSeq; WP_011404213.1; NC_007677.1. DR RefSeq; YP_445587.1; NC_007677.1. DR AlphaFoldDB; Q2S2J4; -. DR STRING; 309807.SRU_1463; -. DR EnsemblBacteria; ABC44790; ABC44790; SRU_1463. DR KEGG; sru:SRU_1463; -. DR PATRIC; fig|309807.25.peg.1518; -. DR eggNOG; COG0578; Bacteria. DR HOGENOM; CLU_015740_4_1_10; -. DR OrthoDB; 9766796at2; -. DR Proteomes; UP000008674; 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; GLYCEROL-3-PHOSPHATE DEHYDROGENASE; 1. DR PANTHER; PTHR11985:SF15; GLYCEROL-3-PHOSPHATE DEHYDROGENASE, MITOCHONDRIAL; 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. DR PROSITE; PS00978; FAD_G3PDH_2; 1. DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 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 ECO:0000313|EMBL:ABC44790.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008674}. FT DOMAIN 18..374 FT /note="FAD dependent oxidoreductase" FT /evidence="ECO:0000259|Pfam:PF01266" FT DOMAIN 417..495 FT /note="Alpha-glycerophosphate oxidase C-terminal" FT /evidence="ECO:0000259|Pfam:PF16901" SQ SEQUENCE 524 AA; 57763 MW; 907A5FB866B2E598 CRC64; MDRTQGIEAL QSRQTPWDFV IIGGGATGLG CAVDAAARGY DTLLLEMHDF AKATSSRSTK LVHGGVRYLE QGNVSLVFEA LKERERLQDN APHLVSNLPF VVPSYKWWEA PYYGIGMKVY DLLAGSQNFG RSQYLDRNQT IERLPTVETD GLRGGILYFD GQFDDTRLAV NMAQTADEQG GVLLNYMKAT DLKKTNGAVD GVVAECQETG ATFDIEARSV INATGIFTDT IRQMDDPSAG TTLRPSRGTH IVLDKSFLPG DSAIMVPKTD DGRVLFAIPW HDRVVVGTTE AEVDEVSMEP TPGHEELDFL LTHAQRYLAK DPGPEDVRSV YAGIRPLVAP PGSNGDTSDI SREHQLNVSD SGLVTISGGK WTTYRKMAED TIDRAARHAE LARRPSQTDD LRLHGWHQNP EQFGDLALYG ADAEALGGLM EEHPHLQTPL DERLPIRAGQ VVWAARHEMA RTVEDVLARR TRCLLLDAQA SIDVAPRVAE LMAEERDLPP SWVDDQVEAF TEVARNYLMP SIPA //