ID A0A2A3N2D7_CAPSP Unreviewed; 424 AA.
AC A0A2A3N2D7;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 14.
DE RecName: Full=NADH:ubiquinone reductase (non-electrogenic) {ECO:0000256|ARBA:ARBA00012637};
DE EC=1.6.5.9 {ECO:0000256|ARBA:ARBA00012637};
GN ORFNames=CDC50_07820 {ECO:0000313|EMBL:PBN45924.1};
OS Capnocytophaga sputigena.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Capnocytophaga.
OX NCBI_TaxID=1019 {ECO:0000313|EMBL:PBN45924.1, ECO:0000313|Proteomes:UP000218560};
RN [1] {ECO:0000313|EMBL:PBN45924.1, ECO:0000313|Proteomes:UP000218560}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=H6490 {ECO:0000313|EMBL:PBN45924.1,
RC ECO:0000313|Proteomes:UP000218560};
RA Gulvik C.A.;
RT "Capnocytophaga spp. assemblies.";
RL Submitted (JUN-2017) 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:PBN45924.1}.
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DR EMBL; NIBW01000002; PBN45924.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2A3N2D7; -.
DR Proteomes; UP000218560; 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; 2.
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 369..391
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 6..328
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
SQ SEQUENCE 424 AA; 47880 MW; C2509FDA862D3320 CRC64;
MENKKHIVIV GGGFAGLELV KELNRSGKYK ITLVDMNNYN FFPPLLYQLA AGFMEPSSIS
YPFRRLFRKY KNARFRMATL QEVVPSENKI ILSNGELQYD ILVMATGAES NFFGNKNVEE
KAMPMKTVGD ALMLRNLVYT RLERATRTKD KELRRKLLSF AIAGAGPTGV ELSGIFAEMK
QNIMRKDYPE LTYDDLGDIY LIDGQDTVLA PMSKKAQAYT EKSLLKKGVK LKLGVLVTDF
VNDEVHLSDG TILDARNLIW AAGISAKAFK GIDDKQYLGR GRRMKTDAYN KMEGFDNIYA
VGDSSIMTAD PNFPEGHPQL AQVALQQANN LGKNFNKDFI NPTPFSYVDK GSMAIIGRNQ
AVADLPKNIF LKGFIAWAIW AFIHIMSLVN FRNKMRALYN WVGYYISKDQ SYRMVLRPNE
KAKG
//
