(data stored in ACNUC7421 zone)

SWISSPROT: NUOD_SYNFM

ID   NUOD_SYNFM              Reviewed;         373 AA.
AC   A0LEQ1;
DT   16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT   12-DEC-2006, sequence version 1.
DT   08-MAY-2019, entry version 80.
DE   RecName: Full=NADH-quinone oxidoreductase subunit D {ECO:0000255|HAMAP-Rule:MF_01358};
DE            EC=7.1.1.- {ECO:0000255|HAMAP-Rule:MF_01358};
DE   AltName: Full=NADH dehydrogenase I subunit D {ECO:0000255|HAMAP-Rule:MF_01358};
DE   AltName: Full=NDH-1 subunit D {ECO:0000255|HAMAP-Rule:MF_01358};
GN   Name=nuoD {ECO:0000255|HAMAP-Rule:MF_01358};
GN   OrderedLocusNames=Sfum_0202;
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_01358}.
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_01358};
CC   -!- SUBUNIT: NDH-1 is composed of 14 different subunits. Subunits
CC       NuoB, C, D, E, F, and G constitute the peripheral sector of the
CC       complex. {ECO:0000255|HAMAP-Rule:MF_01358}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC       Rule:MF_01358}; Peripheral membrane protein {ECO:0000255|HAMAP-
CC       Rule:MF_01358}; Cytoplasmic side {ECO:0000255|HAMAP-
CC       Rule:MF_01358}.
CC   -!- SIMILARITY: Belongs to the complex I 49 kDa subunit family.
CC       {ECO:0000255|HAMAP-Rule:MF_01358}.
DR   EMBL; CP000478; ABK15903.1; -; Genomic_DNA.
DR   RefSeq; WP_011697076.1; NC_008554.1.
DR   SMR; A0LEQ1; -.
DR   STRING; 335543.Sfum_0202; -.
DR   EnsemblBacteria; ABK15903; ABK15903; Sfum_0202.
DR   KEGG; sfu:Sfum_0202; -.
DR   eggNOG; ENOG4105CQV; Bacteria.
DR   eggNOG; COG0649; LUCA.
DR   HOGENOM; HOG000228263; -.
DR   KO; K00333; -.
DR   OMA; RDSHTIW; -.
DR   OrthoDB; 473681at2; -.
DR   BioCyc; SFUM335543:G1G7I-205-MONOMER; -.
DR   Proteomes; UP000001784; Chromosome.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR   GO; GO:0050136; F:NADH dehydrogenase (quinone) activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0048038; F:quinone binding; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.645.20; -; 1.
DR   HAMAP; MF_01358; NDH1_NuoD; 1.
DR   InterPro; IPR001135; NADH_Q_OxRdtase_suD.
DR   InterPro; IPR038290; NADH_Q_OxRdtase_suD_sf.
DR   InterPro; IPR022885; NDH1_su_D/H.
DR   InterPro; IPR029014; NiFe-Hase_large.
DR   Pfam; PF00346; Complex1_49kDa; 1.
DR   SUPFAM; SSF56762; SSF56762; 1.
PE   3: Inferred from homology;
DR   PRODOM; A0LEQ1.
DR   SWISS-2DPAGE; A0LEQ1.
KW   Cell inner membrane; Cell membrane; Complete proteome; Membrane; NAD;
KW   Quinone; Reference proteome; Translocase; Transport; Ubiquinone.
FT   CHAIN         1    373       NADH-quinone oxidoreductase subunit D.
FT                                /FTId=PRO_0000357946.
SQ   SEQUENCE   373 AA;  42531 MW;  389F59DE8A0444C9 CRC64;
     MPKRFLAPVT EQIYTLNLGP QHPSTHGVLR VLLDLDGEFI VKADPVIGYG HRGHEKMGEN
     RLFKQFLPNT SRLDYLSGFL FNHGYVLAVE KLAGIPVPPR AQFIRTICSE FNRIASHLLW
     FGTYVMDLGG FTPFLYAFDD RERILDILDW VTGSRLTYSY CRFGGVDRDI DTRFTDMARD
     FIKRLRSRWP DYHNLVTRNI IFIHRTRGVG VITPEQARQF GVTGPNLRAC GIAFDTRKAE
     PYEVYDQFDF EIPVGSDGDA LDRYRVRFEE MEQSLRIIEQ ALDRLPGGPF MNDSVPTRLK
     PPKGEVYFAF ESARGQAAYY LVSDGTPSPY RCHIRVPSFG NLHVLTEVLR GTLVADAISI
     LGSVDLVIPE IDR
//

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