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Database: UniProt
Entry: A0A0R0CK83_9GAMM
LinkDB: A0A0R0CK83_9GAMM
Original site: A0A0R0CK83_9GAMM 
ID   A0A0R0CK83_9GAMM        Unreviewed;       431 AA.
AC   A0A0R0CK83;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 35.
DE   RecName: Full=NADH:ubiquinone reductase (non-electrogenic) {ECO:0000256|ARBA:ARBA00012637};
DE            EC=1.6.5.9 {ECO:0000256|ARBA:ARBA00012637};
GN   ORFNames=ABB26_03390 {ECO:0000313|EMBL:KRG65603.1};
OS   Stenotrophomonas humi.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Stenotrophomonas.
OX   NCBI_TaxID=405444 {ECO:0000313|EMBL:KRG65603.1, ECO:0000313|Proteomes:UP000050864};
RN   [1] {ECO:0000313|EMBL:KRG65603.1, ECO:0000313|Proteomes:UP000050864}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 18929 {ECO:0000313|EMBL:KRG65603.1,
RC   ECO:0000313|Proteomes:UP000050864};
RA   Patil P.P., Midha S., Patil P.B.;
RT   "Genome sequencing and analysis of members of genus Stenotrophomonas.";
RL   Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a quinone + H(+) + NADH = a quinol + NAD(+);
CC         Xref=Rhea:RHEA:46160, ChEBI:CHEBI:15378, ChEBI:CHEBI:24646,
CC         ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:132124; EC=1.6.5.9;
CC         Evidence={ECO:0000256|ARBA:ARBA00000864};
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:KRG65603.1}.
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DR   EMBL; LDJI01000006; KRG65603.1; -; Genomic_DNA.
DR   RefSeq; WP_057632168.1; NZ_LDJI01000006.1.
DR   AlphaFoldDB; A0A0R0CK83; -.
DR   STRING; 405444.ABB26_03390; -.
DR   PATRIC; fig|405444.3.peg.3345; -.
DR   OrthoDB; 9781621at2; -.
DR   Proteomes; UP000050864; Unassembled WGS sequence.
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:SF3; EXTERNAL NADH-UBIQUINONE OXIDOREDUCTASE 1, MITOCHONDRIAL-RELATED; 1.
DR   PANTHER; PTHR43706; NADH DEHYDROGENASE; 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   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        373..390
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          8..325
FT                   /note="FAD/NAD(P)-binding"
FT                   /evidence="ECO:0000259|Pfam:PF07992"
SQ   SEQUENCE   431 AA;  46908 MW;  3976ADFEEF60C5F1 CRC64;
     MPHDPVPHLV IVGGGFAGLW ATRALANAPL RITLIDRRNH HLFQPLLYQV ATAGLSSPDI
     AAPLRHILRR QHNVDVRLGE VVSIDKQQRR VLLGDATYVD YDLLVVASGA THAYFGHDEW
     AKDAPGLKTL DDALLLRRKL LLAFERAEAE SDPDKKAAWL SFAVVGGGPT GVELAGTLAE
     IARHTLKNEF RHIDPASAKV RLVEAGPRVL SSFPDTLSLK ARQQLERLGV EVLTGTPVNN
     IDAQGFQLGD TFVPARTVVW AAGVAASPLG RTLEVPLDRA GRVQVLPDLT VPGHPEIFVA
     GDLASLMQDD GRPVPGVAPA AKQMGAHIAD SIRARLHGKP APPPFRYNDQ GNLATIGRMA
     AIVHVGKLQL SGLLAWWFWL AAHVFFLIGF RNRLVVLLNW GVAYWSYQRS ARIILGSPYE
     SRKPVAPEST Q
//
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