(data stored in ACNUC7421 zone)

SWISSPROT: NUON1_SYNFM

ID   NUON1_SYNFM             Reviewed;         473 AA.
AC   A0LEQ8;
DT   09-FEB-2010, integrated into UniProtKB/Swiss-Prot.
DT   12-DEC-2006, sequence version 1.
DT   16-JAN-2019, entry version 75.
DE   RecName: Full=NADH-quinone oxidoreductase subunit N 1 {ECO:0000255|HAMAP-Rule:MF_00445};
DE            EC=7.1.1.- {ECO:0000255|HAMAP-Rule:MF_00445};
DE   AltName: Full=NADH dehydrogenase I subunit N 1 {ECO:0000255|HAMAP-Rule:MF_00445};
DE   AltName: Full=NDH-1 subunit N 1 {ECO:0000255|HAMAP-Rule:MF_00445};
GN   Name=nuoN1 {ECO:0000255|HAMAP-Rule:MF_00445};
GN   OrderedLocusNames=Sfum_0209;
OS   Syntrophobacter fumaroxidans (strain DSM 10017 / MPOB).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Syntrophobacterales;
OC   Syntrophobacteraceae; Syntrophobacter.
OX   NCBI_TaxID=335543;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 10017 / MPOB;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Pitluck S., Goltsman E.G.,
RA   Martinez M., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Kim E., Boone D.R., Brockman F., Culley D., Ferry J., Gunsalus R.,
RA   McInerney M.J., Morrison M., Plugge C., Rohlin L., Scholten J.,
RA   Sieber J., Stams A.J.M., Worm P., Henstra A.M., Richardson P.;
RT   "Complete sequence of Syntrophobacter fumaroxidans MPOB.";
RL   Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: NDH-1 shuttles electrons from NADH, via FMN and iron-
CC       sulfur (Fe-S) centers, to quinones in the respiratory chain. The
CC       immediate electron acceptor for the enzyme in this species is
CC       believed to be ubiquinone. Couples the redox reaction to proton
CC       translocation (for every two electrons transferred, four hydrogen
CC       ions are translocated across the cytoplasmic membrane), and thus
CC       conserves the redox energy in a proton gradient.
CC       {ECO:0000255|HAMAP-Rule:MF_00445}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a quinone + 5 H(+)(in) + NADH = a quinol + 4 H(+)(out) +
CC         NAD(+); Xref=Rhea:RHEA:57888, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:24646, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945,
CC         ChEBI:CHEBI:132124; Evidence={ECO:0000255|HAMAP-Rule:MF_00445};
CC   -!- SUBUNIT: NDH-1 is composed of 14 different subunits. Subunits
CC       NuoA, H, J, K, L, M, N constitute the membrane sector of the
CC       complex. {ECO:0000255|HAMAP-Rule:MF_00445}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC       Rule:MF_00445}; Multi-pass membrane protein {ECO:0000255|HAMAP-
CC       Rule:MF_00445}.
CC   -!- SIMILARITY: Belongs to the complex I subunit 2 family.
CC       {ECO:0000255|HAMAP-Rule:MF_00445}.
DR   EMBL; CP000478; ABK15910.1; -; Genomic_DNA.
DR   RefSeq; WP_011697083.1; NC_008554.1.
DR   STRING; 335543.Sfum_0209; -.
DR   EnsemblBacteria; ABK15910; ABK15910; Sfum_0209.
DR   KEGG; sfu:Sfum_0209; -.
DR   eggNOG; ENOG4105CNR; Bacteria.
DR   eggNOG; COG1007; LUCA.
DR   HOGENOM; HOG000100795; -.
DR   KO; K00343; -.
DR   OMA; NILMICA; -.
DR   OrthoDB; 1664448at2; -.
DR   BioCyc; SFUM335543:G1G7I-212-MONOMER; -.
DR   Proteomes; UP000001784; Chromosome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0008137; F:NADH dehydrogenase (ubiquinone) activity; IEA:InterPro.
DR   GO; GO:0048038; F:quinone binding; IEA:UniProtKB-KW.
DR   GO; GO:0042773; P:ATP synthesis coupled electron transport; IEA:InterPro.
DR   HAMAP; MF_00445; NDH1_NuoN_1; 1.
DR   InterPro; IPR010096; NADH-Q_OxRdtase_suN/2.
DR   InterPro; IPR001750; ND/Mrp_mem.
DR   Pfam; PF00361; Proton_antipo_M; 1.
DR   TIGRFAMs; TIGR01770; NDH_I_N; 1.
PE   3: Inferred from homology;
DR   PRODOM; A0LEQ8.
DR   SWISS-2DPAGE; A0LEQ8.
KW   Cell inner membrane; Cell membrane; Complete proteome; Membrane; NAD;
KW   Quinone; Reference proteome; Translocase; Transmembrane;
KW   Transmembrane helix; Transport; Ubiquinone.
FT   CHAIN         1    473       NADH-quinone oxidoreductase subunit N 1.
FT                                /FTId=PRO_0000391237.
FT   TRANSMEM      5     25       Helical. {ECO:0000255|HAMAP-
FT                                Rule:MF_00445}.
FT   TRANSMEM     33     53       Helical. {ECO:0000255|HAMAP-
FT                                Rule:MF_00445}.
FT   TRANSMEM     66     86       Helical. {ECO:0000255|HAMAP-
FT                                Rule:MF_00445}.
FT   TRANSMEM    102    122       Helical. {ECO:0000255|HAMAP-
FT                                Rule:MF_00445}.
FT   TRANSMEM    157    177       Helical. {ECO:0000255|HAMAP-
FT                                Rule:MF_00445}.
FT   TRANSMEM    199    219       Helical. {ECO:0000255|HAMAP-
FT                                Rule:MF_00445}.
FT   TRANSMEM    226    248       Helical. {ECO:0000255|HAMAP-
FT                                Rule:MF_00445}.
FT   TRANSMEM    265    285       Helical. {ECO:0000255|HAMAP-
FT                                Rule:MF_00445}.
FT   TRANSMEM    292    312       Helical. {ECO:0000255|HAMAP-
FT                                Rule:MF_00445}.
FT   TRANSMEM    318    338       Helical. {ECO:0000255|HAMAP-
FT                                Rule:MF_00445}.
FT   TRANSMEM    362    382       Helical. {ECO:0000255|HAMAP-
FT                                Rule:MF_00445}.
FT   TRANSMEM    399    419       Helical. {ECO:0000255|HAMAP-
FT                                Rule:MF_00445}.
FT   TRANSMEM    445    465       Helical. {ECO:0000255|HAMAP-
FT                                Rule:MF_00445}.
SQ   SEQUENCE   473 AA;  52334 MW;  761B65B42450C1A0 CRC64;
     MMKWVLFIPE LYYLLMAVVF FACSLSRRLQ SGVLYRWAVI LAGGGLLATV LAVNQNGFIF
     FDCYRVDLYS QLFKILLALG TFWVIFSCSE LQGIDSRYHA EFFLLTTVCT LGMMMLVSAN
     ELLTVYVSIE LSSYSLYLLV PMRKQTEIYV ETGIKYFMIG VTASAFMLFG ISFIFGVAHT
     TYVPDLVKTL PSLIKEPAAI IGLVLTLCGF FFKQALFPFH SWAPDVYMGA ANQVTTYIAT
     ASKMAAAAMV IRFVNLSGGE SPLFTQVLVG LAVLSMTFGN LVAIIQKDLK RLLAYSSIAH
     AGYMMIGILT MSEHGVASAI YYSAAYLVMN FACFMVIMKV ADDGRNLQIK ELAGLHKRSP
     LLAMTLMLGL FGLAGIPPTV GFTGKFLVFA AALRKGYLIL VIIGMINATI SLYYYLIVIK
     AAYLLEPERP YPDVRVDTWT RALSYGLIVL MIYLGVFPDQ FVALTEAAAR SLP
//

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