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Database: UniProt
Entry: A0A3P7P0W1_9FIRM
LinkDB: A0A3P7P0W1_9FIRM
Original site: A0A3P7P0W1_9FIRM 
ID   A0A3P7P0W1_9FIRM        Unreviewed;       637 AA.
AC   A0A3P7P0W1;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   27-MAR-2024, entry version 16.
DE   RecName: Full=NADH:ubiquinone reductase (non-electrogenic) {ECO:0000256|ARBA:ARBA00012637};
DE            EC=1.6.5.9 {ECO:0000256|ARBA:ARBA00012637};
GN   ORFNames=PATL70BA_3095 {ECO:0000313|EMBL:VDN49014.1};
OS   Petrocella atlantisensis.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Vallitaleaceae; Petrocella.
OX   NCBI_TaxID=2173034 {ECO:0000313|EMBL:VDN49014.1, ECO:0000313|Proteomes:UP000279029};
RN   [1] {ECO:0000313|EMBL:VDN49014.1, ECO:0000313|Proteomes:UP000279029}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=70B-A {ECO:0000313|EMBL:VDN49014.1};
RA   Postec A.;
RL   Submitted (SEP-2018) 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}.
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DR   EMBL; LR130778; VDN49014.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3P7P0W1; -.
DR   KEGG; cbar:PATL70BA_3095; -.
DR   OrthoDB; 9781621at2; -.
DR   Proteomes; UP000279029; Chromosome 1.
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   Reference proteome {ECO:0000313|Proteomes:UP000279029};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        556..582
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        594..617
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          6..326
FT                   /note="FAD/NAD(P)-binding"
FT                   /evidence="ECO:0000259|Pfam:PF07992"
SQ   SEQUENCE   637 AA;  71440 MW;  849EB11F35B181EF CRC64;
     MGNEKHIVVL GAGYGGILTA KKLARKFKKK EDIKITLIDK NTYHTMLTEL HEVAAGRVPE
     ESIRIDLDKI FEGRNVDVVL DEIKNIDFEK KELTGDLNTY AYDYLVLGTG SKPTFYGCKG
     AEENALTLWS YEDALKIKYH ILEAFGKASV EKTPDKRAHL LTFVVVGCGF TGIEMIGELA
     EWTDKLCFNF NIPREEVKLM VVDLLPRVLP MFKDKLIHKT EKRLEKLGVE VLTRSNIIEV
     NKNSISIEGK EPIPTYTTIW AAGVEGSDLM GTLKKEHFSK GPRNRVQTDQ YLRSESHDDV
     FVVGDNIFFI PEGEEQPVPQ MVENAEHSSA LVAGNIIATI KKEPLKPYKP KFHGAMVSIG
     GKYGVAQVGT PKNQMVYSGF LAMLIKHMIN MVYFLQVSGF NKAWTYMMHE FFHVEDRRSF
     LGGHFSKRSP NFFLVPLRLF LGLKWLLEGL AKLPRIMENP NDIFLIPAKL PTSGASEEWV
     EEATEVIVWT TSLPLPQFVE DIVSWMLNLS HGAALPVPEF VTNMVDASMD MVFYTSTGDF
     TAMASIFQTG MVLGEIAVGG ALIIGLFTAL ASIGSIIMGI MIWSSNMAPV EMLWYLAAGF
     ALIGGSGSTF GLDYYVLPFL KKQWMKLKVV KKWYLFT
//
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