ID   E8TCB8_MESCW            Unreviewed;       570 AA.
AC   E8TCB8;
DT   05-APR-2011, integrated into UniProtKB/TrEMBL.
DT   05-APR-2011, sequence version 1.
DT   27-MAR-2024, entry version 59.
DE   SubName: Full=FAD dependent oxidoreductase {ECO:0000313|EMBL:ADV14426.1};
GN   OrderedLocusNames=Mesci_5328 {ECO:0000313|EMBL:ADV14426.1};
OS   Mesorhizobium ciceri biovar biserrulae (strain HAMBI 2942 / LMG 23838 /
OS   WSM1271).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Phyllobacteriaceae; Mesorhizobium.
OX   NCBI_TaxID=765698 {ECO:0000313|EMBL:ADV14426.1, ECO:0000313|Proteomes:UP000007471};
RN   [1] {ECO:0000313|Proteomes:UP000007471}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HAMBI 2942 / LMG 23838 / WSM1271
RC   {ECO:0000313|Proteomes:UP000007471};
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Teshima H., Detter J.C., Han C., Tapia R., Land M., Hauser L., Kyrpides N.,
RA   Ivanova N., Nandasena K., Reeve W.G., Howieson J.G., O'Hara G.,
RA   Tiwari R.P., Woyke T.;
RT   "Complete sequence of chromosome of Mesorhizobium ciceri bv. biserrulae
RT   WSM1271.";
RL   Submitted (JAN-2011) to the EMBL/GenBank/DDBJ databases.
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}.
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DR   EMBL; CP002447; ADV14426.1; -; Genomic_DNA.
DR   RefSeq; YP_004144476.1; NC_014923.1.
DR   AlphaFoldDB; E8TCB8; -.
DR   STRING; 765698.Mesci_5328; -.
DR   KEGG; mci:Mesci_5328; -.
DR   PATRIC; fig|765698.3.peg.5863; -.
DR   eggNOG; COG0578; Bacteria.
DR   HOGENOM; CLU_015740_5_1_5; -.
DR   OrthoDB; 9766796at2; -.
DR   Proteomes; UP000007471; 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:InterPro.
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.
PE   3: Inferred from homology;
KW   FAD {ECO:0000256|ARBA:ARBA00022827};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT   DOMAIN          26..371
FT                   /note="FAD dependent oxidoreductase"
FT                   /evidence="ECO:0000259|Pfam:PF01266"
FT   DOMAIN          426..548
FT                   /note="Alpha-glycerophosphate oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF16901"
SQ   SEQUENCE   570 AA;  61038 MW;  B3545C5FE0357C54 CRC64;
     MSSSEAKFTE NPAGRLAAMA GTGEVDVVIL GAGINGAGLF RDLCAQGVSC LIVDKADFGS
     GTSAAPSRLI HGGLKYLETG EFGLVAQSTL ERNLLLKNAP HYVSPLPTVI PIFSWSKGML
     AALRTLFGST SAPRSRGAVL IKIGLMIYDF YGSRNQVMPR HRMVGRRQAL SGMPALNPSI
     VATGTYYDAK ISHPERLVLE LILDGRQANA ASASANYTAL VKSADGVLTF QPENGAAFSV
     RPKLVVNAAG PWIDDVNELL GAPSKMIGGT KGSHVLLKHD ELVKSLAGRM LYFEADDGRI
     CLIYDYLGLA LVGSTDIKAD NPDAVRCEPD EVEYLLDSVR TLLPGMAFER GQIVYAYSGI
     RPLPASDASL PGLISRDHSA PVTEPDRNRP FAVISLVGGK WTTFRGFAEE VADTVLGRLQ
     RSRKVTTQAM PIGGGRDFPT NAAARASWLA LAHSKTGAEE RRLDALLSRY GTRATQIATH
     GSGDEGRLPD SESYSKSEID YIVRNEFVEH LADIVMRRST LAISASLTGR DLQAIAAIAG
     QALGWSAGRL AREVEAAIVE LEDRNLMRLG
//