ID D3HXW0_9BACT Unreviewed; 432 AA.
AC D3HXW0;
DT 23-MAR-2010, integrated into UniProtKB/TrEMBL.
DT 23-MAR-2010, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE RecName: Full=NADH:ubiquinone reductase (non-electrogenic) {ECO:0000256|ARBA:ARBA00012637};
DE EC=1.6.5.9 {ECO:0000256|ARBA:ARBA00012637};
GN ORFNames=HMPREF0649_01092 {ECO:0000313|EMBL:EFC75941.1};
OS Segatella buccae D17.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae;
OC Segatella.
OX NCBI_TaxID=575611 {ECO:0000313|EMBL:EFC75941.1, ECO:0000313|Proteomes:UP000005080};
RN [1] {ECO:0000313|EMBL:EFC75941.1, ECO:0000313|Proteomes:UP000005080}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=D17 {ECO:0000313|EMBL:EFC75941.1,
RC ECO:0000313|Proteomes:UP000005080};
RG The Broad Institute Genome Sequencing Platform;
RA Ward D., Feldgarden M., Earl A., Young S.K., Zeng Q., Koehrsen M.,
RA Alvarado L., Berlin A., Bochicchio J., Borenstein D., Chapman S.B.,
RA Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A.,
RA Gujja S., Heilman E., Heiman D., Hepburn T., Howarth C., Jen D., Larson L.,
RA Lewis B., Mehta T., Park D., Pearson M., Roberts A., Saif S., Shea T.,
RA Shenoy N., Sisk P., Stolte C., Sykes S., Thomson T., Walk T., White J.,
RA Yandava C., Sibley C.D., White A., Allen-Vercoe E., Strauss J., Crowley S.,
RA Surette M.G., Haas B., Nusbaum C., Birren B.;
RT "The Genome Sequence of Prevotella buccae Oral Taxon 560 strain D17.";
RL Submitted (NOV-2009) 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 ---------------------------------------------------------------------------
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; GG739931; EFC75941.1; -; Genomic_DNA.
DR RefSeq; WP_004341715.1; NZ_GG739931.1.
DR AlphaFoldDB; D3HXW0; -.
DR HOGENOM; CLU_021377_7_1_10; -.
DR OrthoDB; 9781621at2; -.
DR Proteomes; UP000005080; 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: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 12..331
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
SQ SEQUENCE 432 AA; 48273 MW; 63488D5806BCE1D0 CRC64;
MRANIKRNNQ KRVVIVGGGL AGLQLALRLR HTDFQVVLVD KNNYNQFPPL IYQVASAGLE
PSSISFPFRR LFQNQRNFYF RMGEALSVDN DERVLHTSFG TLHYDYLVLA AGATTNFFGN
VNIEREALPM KTVTEAIKLR NTVLQNLEKA ETEDDEHHRQ SLLNIVIVGG GPSGVEIAGA
LAEMKRTVMP RDYPDLDADR MNIYLVNADR RLLKSMDSAS SARAEKDLRE MGVNVMPGYT
VVDCRGGQVM LSDGSSIDAR TVIWVSGIRA SAIGGIPQTS IGHAGRVLTD RFNNVKGMAG
VYAIGDQSLV EGDADYPLGH PQLAQVAIQQ ATNVAENLMR INRNEQPRPF TYRNLGTMAT
IGRKRAVAEI GRFKFGGLSA WLLWLVVHLR SILGVKNKTV IFLNWMWNYF NYKQSLRLIL
KSECKTIETN KK
//