ID A0A061LVM9_9MICO Unreviewed; 447 AA.
AC A0A061LVM9;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE SubName: Full=NADH dehydrogenase {ECO:0000313|EMBL:EYT51983.1};
GN ORFNames=H490_0113340 {ECO:0000313|EMBL:EYT51983.1};
OS Leucobacter sp. UCD-THU.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Leucobacter.
OX NCBI_TaxID=1292023 {ECO:0000313|EMBL:EYT51983.1, ECO:0000313|Proteomes:UP000026917};
RN [1] {ECO:0000313|EMBL:EYT51983.1, ECO:0000313|Proteomes:UP000026917}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UCD-THU {ECO:0000313|EMBL:EYT51983.1,
RC ECO:0000313|Proteomes:UP000026917};
RX PubMed=23792744; DOI=10.1128/genomeA.00325-13;
RA Holland-Moritz H.E., Bevans D.R., Lang J.M., Darling A.E., Eisen J.A.,
RA Coil D.A.;
RT "Draft Genome Sequence of Leucobacter sp. Strain UCD-THU (Phylum
RT Actinobacteria).";
RL Genome Announc. 1:S69-S82(2013).
CC -!- SIMILARITY: Belongs to the NADH dehydrogenase family.
CC {ECO:0000256|ARBA:ARBA00005272}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EYT51983.1}.
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; APJM01000027; EYT51983.1; -; Genomic_DNA.
DR RefSeq; WP_017885183.1; NZ_KB714605.1.
DR AlphaFoldDB; A0A061LVM9; -.
DR STRING; 1292023.H490_0113340; -.
DR HOGENOM; CLU_021377_7_1_11; -.
DR OrthoDB; 9781621at2; -.
DR Proteomes; UP000026917; Unassembled WGS sequence.
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:SF45; NADH DEHYDROGENASE-LIKE PROTEIN RV1812C; 1.
DR Pfam; PF07992; Pyr_redox_2; 1.
DR PRINTS; PR00368; FADPNR.
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 Reference proteome {ECO:0000313|Proteomes:UP000026917}.
FT DOMAIN 4..335
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
SQ SEQUENCE 447 AA; 48768 MW; C14D9F0AE024622A CRC64;
MAKKILIVGG GYAGFYTAWK LEKLLRAGEA EVTIVDPLPY MAYLPFLPEV AAGSIEPRHA
VVARRRHLQR THNIAGKVTG ISHATKTATV TPNEGEAFDF EYDHIVVTTG SVSRTFPIAG
IAENAIGMKT IEEAVAVRDR LVGNFERAAS LPAGSPERAR LLTVTVVGGG FAGIETIAEL
RSFATSLLRR YPEITFEETR FHLVEAMGRI MPEVTEALAD WVVKDQTRRG VDIHLDTQLS
SAVDGNIELS TGEKFESDLI VWTAGVMPRP FLRGTDLPIG PRGHVIGSPE LRITTEEGQA
LEGAWTAGDT SQTPDISSTP GPGGFCVPNA QHAVRQGRLL AKNIVADLRG EGVRQYNHKN
MGAVAGLGVN TGVFRSGGSF AMKGYFAWLA HRFYHGLAIP TWERKWRVFG GWVGHFFLGR
DIVNIEAVQE PRAIFEEFAS RPKPKTD
//