ID D5BJ81_ZUNPS Unreviewed; 451 AA.
AC D5BJ81;
DT 15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT 15-JUN-2010, sequence version 1.
DT 27-MAR-2024, entry version 64.
DE RecName: Full=NADH:ubiquinone reductase (non-electrogenic) {ECO:0000256|ARBA:ARBA00012637};
DE EC=1.6.5.9 {ECO:0000256|ARBA:ARBA00012637};
GN OrderedLocusNames=ZPR_3398 {ECO:0000313|EMBL:ADF53714.1};
OS Zunongwangia profunda (strain DSM 18752 / CCTCC AB 206139 / SM-A87) (Wangia
OS profunda).
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Zunongwangia.
OX NCBI_TaxID=655815 {ECO:0000313|EMBL:ADF53714.1, ECO:0000313|Proteomes:UP000001654};
RN [1] {ECO:0000313|EMBL:ADF53714.1, ECO:0000313|Proteomes:UP000001654}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 18752 / CCTCC AB 206139 / SM-A87
RC {ECO:0000313|Proteomes:UP000001654};
RX PubMed=20398413; DOI=10.1186/1471-2164-11-247;
RA Qin Q.L., Zhang X.Y., Wang X.M., Liu G.M., Chen X.L., Xie B.B., Dang H.Y.,
RA Zhou B.C., Yu J., Zhang Y.Z.;
RT "The complete genome of Zunongwangia profunda SM-A87 reveals its adaptation
RT to the deep-sea environment and ecological role in sedimentary organic
RT nitrogen degradation.";
RL BMC Genomics 11:247-247(2010).
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}.
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DR EMBL; CP001650; ADF53714.1; -; Genomic_DNA.
DR RefSeq; WP_013072804.1; NC_014041.1.
DR AlphaFoldDB; D5BJ81; -.
DR STRING; 655815.ZPR_3398; -.
DR KEGG; zpr:ZPR_3398; -.
DR eggNOG; COG1252; Bacteria.
DR HOGENOM; CLU_021377_7_1_10; -.
DR OrthoDB; 9781621at2; -.
DR Proteomes; UP000001654; 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: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 Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT DOMAIN 30..348
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
SQ SEQUENCE 451 AA; 50400 MW; 1A8A997A5EC11A84 CRC64;
MKEKQTHSIP LESTCKITDE ICLPDTKLPR VVIVGGGFAG LALVEKLKHK EVQVVLLDKN
NFHQFQPLLY QVATSALEPD SIVFPFRKQI NGYKNVFFRL AEVEEIQPDS NTILTNKGSV
SYDYLVLATG TTTNFFGMDS VAENSLRMKD IRDSLNIRHM MLQNLEQAAI TCDDKERDAL
TNFVIVGGGP AGVEMAGALA EFCKYILPKD YPEYPSSIMN IYLIEAIDEL LGTMSDKASS
KTLKYLEDLN VKVLLNEAVS NYDGNEVTTK SGKTILAKNL IWTAGVKGQF PNGIDEKHIV
RGNRIKTDAN LKVEGYENIF AIGDIAALIS KETPKGHPQV AQTAIQQGKY LGDSILNIIN
NKSIKPFKYK DKGSLATVGK RKAVADLGKF KFAGYFAWLL WSVVHLMSIS GFRNRLMVGF
NWAVSYFTYE KSNRLIIRNF KPKSSIKNRE K
//
