ID   F7YE33_MESOW            Unreviewed;       505 AA.
AC   F7YE33;
DT   21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT   21-SEP-2011, sequence version 1.
DT   24-JAN-2024, entry version 50.
DE   RecName: Full=Glycerol-3-phosphate dehydrogenase {ECO:0000256|RuleBase:RU361217};
DE            EC=1.1.5.3 {ECO:0000256|RuleBase:RU361217};
GN   OrderedLocusNames=Mesop_5788 {ECO:0000313|EMBL:AEH90197.1};
OS   Mesorhizobium opportunistum (strain LMG 24607 / HAMBI 3007 / WSM2075).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Phyllobacteriaceae; Mesorhizobium.
OX   NCBI_TaxID=536019 {ECO:0000313|EMBL:AEH90197.1, ECO:0000313|Proteomes:UP000001623};
RN   [1] {ECO:0000313|EMBL:AEH90197.1, 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; AEH90197.1; -; Genomic_DNA.
DR   RefSeq; WP_013896831.1; NC_015675.1.
DR   AlphaFoldDB; F7YE33; -.
DR   STRING; 536019.Mesop_5788; -.
DR   KEGG; mop:Mesop_5788; -.
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; 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; 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   PRINTS; PR01001; FADG3PDH.
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          9..330
FT                   /note="FAD dependent oxidoreductase"
FT                   /evidence="ECO:0000259|Pfam:PF01266"
SQ   SEQUENCE   505 AA;  56404 MW;  2A643ED454E52B74 CRC64;
     MSGGTEIVDL FVVGGGVNGA GIARDAAGRG LSVILCEKDD LAEGTSSRSG KLVHGGLRYL
     EYYEFRLVRE ALIEREVLLE SAPHIIWPMR FVLPHSPDDR PAWLVRLGLF LYDHLGGRKR
     LPPTRTLDLR TAPEGAPIKD AFKRGFEYSD CWVDDARLVV INALDAAERG AKVFTRTACT
     AARRENGLWV VEMRDGGTGA RTTVRARALI NAAGPWVNDI VNRVAGQNSK RNVRLVKGSH
     IVVPKFWEGR HAYLVQNSDK RVIFINPYQN DLALIGTTDI PYEGRPEDVT ADESEIDYLI
     RVINRYFKRG LARSDVVYSF SGVRPLYDDN ADNPSAVTRD YIFELDAPDA QAPLLSVFGG
     KITTFRKLAE HALDRIAPFF PRMGKPWTAK EHLPGGDIAN ADFEQFLGDL GREYPWMPAS
     LIKHYGRLYG TRTRLLVGAT GSLAGLGRCF GKDFFEREAN YLFEQEWAAT SADILERRTK
     HGLHLSAEER AAFEHWCANR LARAG
//