ID   B1LI35_ECOSM            Unreviewed;       434 AA.
AC   B1LI35;
DT   29-APR-2008, integrated into UniProtKB/TrEMBL.
DT   29-APR-2008, sequence version 1.
DT   27-MAR-2024, entry version 74.
DE   SubName: Full=NADH dehydrogenase {ECO:0000313|EMBL:ACB19543.1};
DE            EC=1.6.99.3 {ECO:0000313|EMBL:ACB19543.1};
GN   Name=ndh {ECO:0000313|EMBL:ACB19543.1};
GN   OrderedLocusNames=EcSMS35_2017 {ECO:0000313|EMBL:ACB19543.1};
OS   Escherichia coli (strain SMS-3-5 / SECEC).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=439855 {ECO:0000313|EMBL:ACB19543.1, ECO:0000313|Proteomes:UP000007011};
RN   [1] {ECO:0000313|EMBL:ACB19543.1, ECO:0000313|Proteomes:UP000007011}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SMS-3-5 / SECEC {ECO:0000313|Proteomes:UP000007011};
RX   PubMed=18708504; DOI=10.1128/JB.00661-08;
RA   Fricke W.F., Wright M.S., Lindell A.H., Harkins D.M., Baker-Austin C.,
RA   Ravel J., Stepanauskas R.;
RT   "Insights into the environmental resistance gene pool from the genome
RT   sequence of the multidrug-resistant environmental isolate Escherichia coli
RT   SMS-3-5.";
RL   J. Bacteriol. 190:6779-6794(2008).
CC   -!- SIMILARITY: Belongs to the NADH dehydrogenase family.
CC       {ECO:0000256|ARBA:ARBA00005272}.
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DR   EMBL; CP000970; ACB19543.1; -; Genomic_DNA.
DR   RefSeq; WP_012311941.1; NC_010498.1.
DR   AlphaFoldDB; B1LI35; -.
DR   KEGG; ecm:EcSMS35_2017; -.
DR   HOGENOM; CLU_021377_7_0_6; -.
DR   Proteomes; UP000007011; 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:ACB19543.1}.
FT   DOMAIN          6..338
FT                   /note="FAD/NAD(P)-binding"
FT                   /evidence="ECO:0000259|Pfam:PF07992"
SQ   SEQUENCE   434 AA;  47320 MW;  9FCC6207D81A37EE CRC64;
     MTTPLKKIVI VGGGAGGLEM ATQLGHKQGR KKKAKITLVD RNHSHLWKPL LHEVATGSLD
     EGVDALSYLA HARNHGFQFQ LGSVIDIDRE AKTITIAELR DEKGELLVPE RKIAYDTLVM
     ALGSTSNDFN TPGVKENCIF LDNPHQARRF HQEMLNLFLK YSANLGANGK VNIAIVGGGA
     TGVELSAELH NAVKQLHSYG YKGLTNEALN VTLVEAGERI LPALPPRISA AAHSELTKLG
     VRVLTQTMVT SADEGGLHTK DGEYIEADLM VWAAGIKAPD FLKDIGGLET NRINQLVVEP
     TLQTTRDPDI YAIGDCASCP RPEGGFVPPR AQAAHQMATC AMNNILAQMN GKPLKSYQYK
     DHGSLVSLSN FSTVGSLMGN LTRGSMMIEG RIARFVYISL YRMHQIALHG YFKTGLMMLV
     GSINRVIRPR LKLH
//