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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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
//