ID   H5YQJ4_9BRAD            Unreviewed;       492 AA.
AC   H5YQJ4;
DT   18-APR-2012, integrated into UniProtKB/TrEMBL.
DT   18-APR-2012, sequence version 1.
DT   27-MAR-2024, entry version 42.
DE   SubName: Full=FAD/FMN-dependent dehydrogenase {ECO:0000313|EMBL:EHR04826.1};
GN   ORFNames=Bra471DRAFT_05631 {ECO:0000313|EMBL:EHR04826.1};
OS   Bradyrhizobium sp. WSM471.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Nitrobacteraceae; Bradyrhizobium.
OX   NCBI_TaxID=319017 {ECO:0000313|EMBL:EHR04826.1};
RN   [1] {ECO:0000313|EMBL:EHR04826.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WSM471 {ECO:0000313|EMBL:EHR04826.1};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Peters L., Lu M., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA   Kyrpides N., Ivanova N., Pagani I., Brau L., Yates R., O'Hara G., Rui T.,
RA   Howieson J., Reeve W., Woyke T.;
RT   "The Noncontiguous Finished sequence of Bradyrhizobium sp. WSM471.";
RL   Submitted (NOV-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-binding oxidoreductase/transferase type
CC       4 family. {ECO:0000256|ARBA:ARBA00008000}.
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DR   EMBL; CM001442; EHR04826.1; -; Genomic_DNA.
DR   RefSeq; WP_007612993.1; NZ_CM001442.1.
DR   AlphaFoldDB; H5YQJ4; -.
DR   HOGENOM; CLU_017779_4_1_5; -.
DR   OrthoDB; 9809290at2; -.
DR   Proteomes; UP000005774; Chromosome.
DR   GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR   GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR   GO; GO:0008152; P:metabolic process; IEA:UniProt.
DR   Gene3D; 3.30.465.10; -; 1.
DR   Gene3D; 3.30.70.2190; -; 1.
DR   Gene3D; 3.30.70.2740; -; 1.
DR   Gene3D; 3.30.43.10; Uridine Diphospho-n-acetylenolpyruvylglucosamine Reductase, domain 2; 1.
DR   InterPro; IPR004113; FAD-bd_oxidored_4_C.
DR   InterPro; IPR016166; FAD-bd_PCMH.
DR   InterPro; IPR036318; FAD-bd_PCMH-like_sf.
DR   InterPro; IPR016167; FAD-bd_PCMH_sub1.
DR   InterPro; IPR016169; FAD-bd_PCMH_sub2.
DR   InterPro; IPR016164; FAD-linked_Oxase-like_C.
DR   InterPro; IPR006094; Oxid_FAD_bind_N.
DR   InterPro; IPR016171; Vanillyl_alc_oxidase_C-sub2.
DR   PANTHER; PTHR43716; D-2-HYDROXYGLUTARATE DEHYDROGENASE, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR43716:SF1; D-2-HYDROXYGLUTARATE DEHYDROGENASE, MITOCHONDRIAL; 1.
DR   Pfam; PF02913; FAD-oxidase_C; 1.
DR   Pfam; PF01565; FAD_binding_4; 1.
DR   SUPFAM; SSF56176; FAD-binding/transporter-associated domain-like; 1.
DR   SUPFAM; SSF55103; FAD-linked oxidases, C-terminal domain; 1.
DR   PROSITE; PS51387; FAD_PCMH; 1.
PE   3: Inferred from homology;
KW   FAD {ECO:0000256|ARBA:ARBA00022827};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022827}.
FT   DOMAIN          52..233
FT                   /note="FAD-binding PCMH-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51387"
SQ   SEQUENCE   492 AA;  52569 MW;  21550B9CA8850658 CRC64;
     MPGAALPTAP SIPTAPVTSA VLDRLRAIVG GKGLILDEQD KLPFVTDWRG TLAGQAAAVV
     RPASTAEVSA VVKLCYDNGI AIVPQGGNTG LMGGATPWPM HRGIVLSLGR MNQVLNVDPV
     GYAMTVEAGC ILETLQDTAA RHDRLFPLSL GAQGSCMIGG NLSTNAGGVQ VLRYGNARNL
     VLGLEVVLAN GDVWDGLRAL KKDNTGYDLK HLFMGAEGTL GIITKAVLKL WPAPKDVCTA
     WLAIRDPKAA IDLLSEAHAA SDDNVGSCEL VSRACTDMVL RHIPGTQDPL KAETEWYLLL
     EWSSARPRQD GGTGMSDRME QFLADQLEAG RVLDAVIAQT EAQSRNMWRI RESVAEASRT
     EGPGLSYDVS VAVSRIPEFI DSGLEAVLAI LPTIRPYPLG HIGDGNVHFS FMGPKGMDLD
     TLSQYSAAIT RAVNDLITSM GGSISAEHGI GIEKLDELQH YRSRAELDIM RTIKRALDPK
     NIMNPGKVLR LG
//