ID B7LSP8_ESCF3 Unreviewed; 434 AA.
AC B7LSP8;
DT 10-FEB-2009, integrated into UniProtKB/TrEMBL.
DT 10-FEB-2009, sequence version 1.
DT 27-MAR-2024, entry version 68.
DE SubName: Full=Respiratory NADH dehydrogenase 2/cupric reductase {ECO:0000313|EMBL:CAQ89334.1};
DE EC=1.16.1.- {ECO:0000313|EMBL:CAQ89334.1};
DE EC=1.6.99.3 {ECO:0000313|EMBL:CAQ89334.1};
GN Name=ndh {ECO:0000313|EMBL:CAQ89334.1};
GN OrderedLocusNames=EFER_1819 {ECO:0000313|EMBL:CAQ89334.1};
OS Escherichia fergusonii (strain ATCC 35469 / DSM 13698 / CCUG 18766 / IAM
OS 14443 / JCM 21226 / LMG 7866 / NBRC 102419 / NCTC 12128 / CDC 0568-73).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=585054 {ECO:0000313|EMBL:CAQ89334.1, ECO:0000313|Proteomes:UP000000745};
RN [1] {ECO:0000313|Proteomes:UP000000745}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35469 / DSM 13698 / BCRC 15582 / CCUG 18766 / IAM 14443 /
RC JCM 21226 / LMG 7866 / NBRC 102419 / NCTC 12128 / CDC 0568-73
RC {ECO:0000313|Proteomes:UP000000745};
RX PubMed=19165319; DOI=10.1371/journal.pgen.1000344;
RA Touchon M., Hoede C., Tenaillon O., Barbe V., Baeriswyl S., Bidet P.,
RA Bingen E., Bonacorsi S., Bouchier C., Bouvet O., Calteau A., Chiapello H.,
RA Clermont O., Cruveiller S., Danchin A., Diard M., Dossat C., Karoui M.E.,
RA Frapy E., Garry L., Ghigo J.M., Gilles A.M., Johnson J., Le Bouguenec C.,
RA Lescat M., Mangenot S., Martinez-Jehanne V., Matic I., Nassif X., Oztas S.,
RA Petit M.A., Pichon C., Rouy Z., Ruf C.S., Schneider D., Tourret J.,
RA Vacherie B., Vallenet D., Medigue C., Rocha E.P.C., Denamur E.;
RT "Organised genome dynamics in the Escherichia coli species results in
RT highly diverse adaptive paths.";
RL PLoS Genet. 5:E1000344-E1000344(2009).
CC -!- SIMILARITY: Belongs to the NADH dehydrogenase family.
CC {ECO:0000256|ARBA:ARBA00005272}.
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DR EMBL; CU928158; CAQ89334.1; -; Genomic_DNA.
DR RefSeq; WP_002431502.1; NC_011740.1.
DR AlphaFoldDB; B7LSP8; -.
DR GeneID; 75057143; -.
DR KEGG; efe:EFER_1819; -.
DR HOGENOM; CLU_021377_7_0_6; -.
DR OrthoDB; 9781621at2; -.
DR Proteomes; UP000000745; Chromosome.
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 Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000313|EMBL:CAQ89334.1}.
FT DOMAIN 7..338
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
SQ SEQUENCE 434 AA; 47262 MW; F9C0A1D5DA55E37D CRC64;
MTTPLKRIVI VGGGAGGLEL ATQLGHKLGR KKKAKVTLVD RNHSHLWKPL LHEVATGSLD
EGVDALSYLA HARNHGFEFQ LGSVKDIDRE AKTITIAELR DEKGELLVPE RKIAYDTLVM
ALGSTSNDFN TPGVKENCIF LDNPHQARRF HQEMLNLFLK YSANLGSNGK VNIAIVGGGA
TGVELSAELH NAVKQLHSYG YKGLTNEALN VTLVEAGERI LPALPPRISS AAHNELTKLG
VRVLTQTMVT SADAGGLHTK DGEYIEADLM VWAAGIKAPD FLKDIGGLET NRINQLVVEP
TLQTTRDADI YAIGDCASCA RPEGGFVPPR AQAAHQMATC ALQNILAQMN GKPLKSYRYK
DHGSLVSLSN FSTVGSLMGN LTKGSMMIEG RIARFVYISL YRMHQIALHG YFKTGLMMLV
GSINRVIRPR LKLH
//
