ID E6YI00_BARC7 Unreviewed; 501 AA. AC E6YI00; DT 08-MAR-2011, integrated into UniProtKB/TrEMBL. DT 08-MAR-2011, sequence version 1. DT 27-MAR-2024, entry version 65. DE RecName: Full=Glycerol-3-phosphate dehydrogenase {ECO:0000256|RuleBase:RU361217}; DE EC=1.1.5.3 {ECO:0000256|RuleBase:RU361217}; GN Name=glpD {ECO:0000313|EMBL:CBI76488.1}; GN OrderedLocusNames=BARCL_0807 {ECO:0000313|EMBL:CBI76488.1}; OS Bartonella clarridgeiae (strain CCUG 45776 / CIP 104772 / 73). OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales; OC Bartonellaceae; Bartonella. OX NCBI_TaxID=696125 {ECO:0000313|EMBL:CBI76488.1, ECO:0000313|Proteomes:UP000009101}; RN [1] {ECO:0000313|Proteomes:UP000009101} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CIP 104772 / 73 {ECO:0000313|Proteomes:UP000009101}; RA Engel P., Salzburger W., Marius L., Chao-Chin C., Soichi M., Christa L., RA Alexandra C., Aurelie L., Claudine M., Stephan S.C., Christoph D.; RT "Genome sequencing of Bartonella species and comparative genomics."; RL Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:CBI76488.1, ECO:0000313|Proteomes:UP000009101} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CIP 104772 / 73 {ECO:0000313|Proteomes:UP000009101}; RX PubMed=21347280; DOI=10.1371/journal.pgen.1001296; RA Engel P., Salzburger W., Liesch M., Chang C.C., Maruyama S., Lanz C., RA Calteau A., Lajus A., Medigue C., Schuster S.C., Dehio C.; RT "Parallel evolution of a type IV secretion system in radiating lineages of RT the host-restricted bacterial pathogen Bartonella."; RL PLoS Genet. 7:E1001296-E1001296(2011). CC -!- CATALYTIC ACTIVITY: CC Reaction=a quinone + sn-glycerol 3-phosphate = a quinol + CC dihydroxyacetone phosphate; Xref=Rhea:RHEA:18977, ChEBI:CHEBI:24646, CC ChEBI:CHEBI:57597, ChEBI:CHEBI:57642, ChEBI:CHEBI:132124; EC=1.1.5.3; CC Evidence={ECO:0000256|RuleBase:RU361217}; CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000256|ARBA:ARBA00001974, CC ECO:0000256|RuleBase:RU361217}; CC -!- SIMILARITY: Belongs to the FAD-dependent glycerol-3-phosphate CC dehydrogenase family. {ECO:0000256|ARBA:ARBA00007330, CC ECO:0000256|RuleBase:RU361217}. 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; FN645454; CBI76488.1; -; Genomic_DNA. DR RefSeq; WP_013545126.1; NC_014932.1. DR AlphaFoldDB; E6YI00; -. DR STRING; 696125.BARCL_0807; -. DR KEGG; bcd:BARCL_0807; -. DR eggNOG; COG0578; Bacteria. DR HOGENOM; CLU_015740_5_0_5; -. DR OrthoDB; 9766796at2; -. DR Proteomes; UP000009101; Chromosome. DR GO; GO:0009331; C:glycerol-3-phosphate dehydrogenase complex; IEA:UniProtKB-UniRule. DR GO; GO:0004368; F:glycerol-3-phosphate dehydrogenase (quinone) activity; IEA:UniProtKB-EC. DR GO; GO:0006072; P:glycerol-3-phosphate metabolic process; IEA:UniProtKB-UniRule. DR Gene3D; 6.10.250.1890; -; 1. 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; SSF54373; FAD-linked reductases, C-terminal domain; 1. DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1. DR PROSITE; PS00977; FAD_G3PDH_1; 1. DR PROSITE; PS00978; FAD_G3PDH_2; 1. PE 3: Inferred from homology; KW FAD {ECO:0000256|ARBA:ARBA00022827}; KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630, KW ECO:0000256|RuleBase:RU361217}; KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, KW ECO:0000256|RuleBase:RU361217}. FT DOMAIN 8..335 FT /note="FAD dependent oxidoreductase" FT /evidence="ECO:0000259|Pfam:PF01266" FT DOMAIN 387..489 FT /note="Alpha-glycerophosphate oxidase C-terminal" FT /evidence="ECO:0000259|Pfam:PF16901" SQ SEQUENCE 501 AA; 57562 MW; ACB546CB5D5F44DF CRC64; MKATTHYDLF IIGGGINGCG VARDAAGRGF SVGLAEMNDL ASGTSSASTK LIHGGLRYLE HYEFRLVRKA LKEREIIWRM APHIVHPLRF ILPYHKKLRS SWILRFGLFI YDYLGGWNQI FQRTKMIDLS KNFGTFFKEN YRKGFEYSDA IVDDARLVIA NARDAKKWGA DIKVRTEVLS LKIEEKKWFI TLHDKLNDKK YCVTASYIAN MVGPWINQVL ANVLNSKELP PMRLVKGSHI LVPKLDIHNR AYILQNSDNR IIFAIPYQEK FTLIGTTDCD YQGDPASVSI SDEEIDYICA IANEYFRKPI LRESIIWTYS GVRPLYDDGS SIAQDITRDY VLKEIGIEDK PKILNLYGGK ITTYRILAED VMKFIEKALG SKKGPWTLNS VLPGGDFPYN RLDIIENRIA VLLPDLDAFT CRRLARSYGS ETFTIFANGN VDKGKYFGHG LYEIEVKWLM EKEWAKTCED ILWRRSKLGL FFNKQETDSL TAYIEDKRGR E //