ID   F7Y8A0_MESOW            Unreviewed;       508 AA.
AC   F7Y8A0;
DT   21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT   21-SEP-2011, sequence version 1.
DT   24-JAN-2024, entry version 45.
DE   RecName: Full=Glycerol-3-phosphate dehydrogenase {ECO:0000256|RuleBase:RU361217};
DE            EC=1.1.5.3 {ECO:0000256|RuleBase:RU361217};
GN   OrderedLocusNames=Mesop_4203 {ECO:0000313|EMBL:AEH88636.1};
OS   Mesorhizobium opportunistum (strain LMG 24607 / HAMBI 3007 / WSM2075).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Phyllobacteriaceae; Mesorhizobium.
OX   NCBI_TaxID=536019 {ECO:0000313|EMBL:AEH88636.1, ECO:0000313|Proteomes:UP000001623};
RN   [1] {ECO:0000313|EMBL:AEH88636.1, ECO:0000313|Proteomes:UP000001623}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LMG 24607 / HAMBI 3007 / WSM2075
RC   {ECO:0000313|Proteomes:UP000001623};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA   Pitluck S., Chertkov O., Misra M., Detter J.C., Han C., Tapia R., Land M.,
RA   Hauser L., Kyrpides N., Ovchinnikova G., Mavrommatis K.M., Tiwari R.P.,
RA   Howieson J.G., O'Hara G.W., Nandasena K.G., Woyke T.;
RT   "Complete sequence of Mesorhizobium opportunistum WSM2075.";
RL   Submitted (OCT-2010) to the EMBL/GenBank/DDBJ databases.
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}.
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DR   EMBL; CP002279; AEH88636.1; -; Genomic_DNA.
DR   RefSeq; WP_013895312.1; NC_015675.1.
DR   AlphaFoldDB; F7Y8A0; -.
DR   STRING; 536019.Mesop_4203; -.
DR   KEGG; mop:Mesop_4203; -.
DR   eggNOG; COG0578; Bacteria.
DR   HOGENOM; CLU_015740_5_0_5; -.
DR   Proteomes; UP000001623; 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.
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..363
FT                   /note="FAD dependent oxidoreductase"
FT                   /evidence="ECO:0000259|Pfam:PF01266"
FT   DOMAIN          387..496
FT                   /note="Alpha-glycerophosphate oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF16901"
SQ   SEQUENCE   508 AA;  56382 MW;  3155A74B27002D7C CRC64;
     MDASSIRDIF VIGGGINGCG IARDAVGRGF SVFLAEMNDL ASGTSSGSTK LIHGGLRYLE
     FYEFRLVREA LMEREVLWKN APHIIWPMRF VLPYAKGLRP AWLIRLGLFL YDHIGGRKLL
     PATRTLDMAS DPAGKPLKPL FKKAFEYSDG WVNDARLVAL NARDAADRGA TIRTRTKVVE
     ARREGGIWAI KIENLQTGAT EEIKARLLVN AAGPWVDHVL SGVVGQNDVH NVRLVQGSHI
     VIAKKFDDPR AYFFQNRDGR IIFAIPYEEE FTLIGTTDRD YPGDPHDVKI SDTEIDYLCA
     AASEYFAQPV KRSDIVWTYS AVRPLYDDGA SKAQEATRDY VLKADGGDGA APIVNAFGGK
     ITTYRRLSES MLEKIEGFLG KRGKPWTANA PLPGGDFPAT GFDAQVAKLK AAYAFLDARL
     ARRLTRLYGT RAQVLLGLAK SNADLGRNFG GDLYEAEVRY LVENEWAITA EDVLWRRTKR
     GLHLGREQVS ALDEFMRGIS RRHVAAAE
//