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Database: UniProt
Entry: Q89NV7_BRADU
LinkDB: Q89NV7_BRADU
Original site: Q89NV7_BRADU 
ID   Q89NV7_BRADU            Unreviewed;       440 AA.
AC   Q89NV7;
DT   01-JUN-2003, integrated into UniProtKB/TrEMBL.
DT   01-JUN-2003, sequence version 1.
DT   27-MAR-2024, entry version 120.
DE   SubName: Full=NADH dehydrogenase {ECO:0000313|EMBL:BAC48992.1};
DE            EC=1.6.99.3 {ECO:0000313|EMBL:BAC48992.1};
GN   OrderedLocusNames=blr3727 {ECO:0000313|EMBL:BAC48992.1};
OS   Bradyrhizobium diazoefficiens (strain JCM 10833 / BCRC 13528 / IAM 13628 /
OS   NBRC 14792 / USDA 110).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Nitrobacteraceae; Bradyrhizobium.
OX   NCBI_TaxID=224911 {ECO:0000313|EMBL:BAC48992.1, ECO:0000313|Proteomes:UP000002526};
RN   [1] {ECO:0000313|Proteomes:UP000002526}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 10833 / BCRC 13528 / IAM 13628 / NBRC 14792 / USDA 110
RC   {ECO:0000313|Proteomes:UP000002526};
RX   PubMed=12597275; DOI=10.1093/dnares/9.6.189;
RA   Kaneko T., Nakamura Y., Sato S., Minamisawa K., Uchiumi T., Sasamoto S.,
RA   Watanabe A., Idesawa K., Iriguchi M., Kawashima K., Kohara M.,
RA   Matsumoto M., Shimpo S., Tsuruoka H., Wada T., Yamada M., Tabata S.;
RT   "Complete genomic sequence of nitrogen-fixing symbiotic bacterium
RT   Bradyrhizobium japonicum USDA110.";
RL   DNA Res. 9:189-197(2002).
CC   -!- SIMILARITY: Belongs to the NADH dehydrogenase family.
CC       {ECO:0000256|ARBA:ARBA00005272}.
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DR   EMBL; BA000040; BAC48992.1; -; Genomic_DNA.
DR   RefSeq; NP_770367.1; NC_004463.1.
DR   RefSeq; WP_011086508.1; NZ_CP011360.1.
DR   AlphaFoldDB; Q89NV7; -.
DR   STRING; 224911.AAV28_15605; -.
DR   EnsemblBacteria; BAC48992; BAC48992; BAC48992.
DR   GeneID; 64023451; -.
DR   KEGG; bja:blr3727; -.
DR   PATRIC; fig|224911.44.peg.3390; -.
DR   eggNOG; COG1252; Bacteria.
DR   HOGENOM; CLU_021377_7_0_5; -.
DR   InParanoid; Q89NV7; -.
DR   OrthoDB; 9781621at2; -.
DR   PhylomeDB; Q89NV7; -.
DR   Proteomes; UP000002526; Chromosome.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0003954; F:NADH dehydrogenase activity; IEA:InterPro.
DR   GO; GO:0006116; P:NADH oxidation; IEA:InterPro.
DR   Gene3D; 3.50.50.100; -; 1.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR023753; FAD/NAD-binding_dom.
DR   InterPro; IPR045024; NDH-2.
DR   PANTHER; PTHR43706; NADH DEHYDROGENASE; 1.
DR   PANTHER; PTHR43706:SF9; TYPE II NADH:QUINONE OXIDOREDUCTASE; 1.
DR   Pfam; PF07992; Pyr_redox_2; 1.
DR   PRINTS; PR00368; FADPNR.
DR   PRINTS; PR00411; PNDRDTASEI.
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   Membrane {ECO:0000256|SAM:Phobius};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000313|EMBL:BAC48992.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002526};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        380..399
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          10..344
FT                   /note="FAD/NAD(P)-binding"
FT                   /evidence="ECO:0000259|Pfam:PF07992"
SQ   SEQUENCE   440 AA;  48196 MW;  EC1A530DEE131396 CRC64;
     MSEAQAGKPR VVIVGGGAGG LELATRLGDK YGRKGRLDVT LIERNRTHVW KPKLHEIAAG
     SMDIAAHEVD YLAQSYWHGF RYRIGEMIGI DRERRQVLVA PYLDAEGREV TPKRSFDYDV
     LVIAVGSQNN DFGTPGVAEH AIKLESQADA KRFHERMVNA CIRAHAQSSP LGEHQLKVAI
     IGAGATGVEL AAELHRTTRE VVAHGLDQVD PQKDIRITLI EAADRVLPAL PERVSKETEK
     LLVRLGVNVL VGAKVSVVGS DHVSLTDGRT IPAELIVWAA GVKAPDSLKE IAGLETNRIN
     QLVVRPTLQA TRDDNIFAIG DCSACSWGDR GNVPPRAQAA HQQASHLYSQ IPRHLRGEAL
     KDYRYRDFGS LVSLGEFSTV GSMMGALVGG SLVFEGLFAR MMYLSLYKMH EHALHGSVKV
     ALDTLARLIT RRTEPHVKLH
//
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