(data stored in ACNUC1104 zone)

SWISSPROT: NUOD_NOCSJ

ID   NUOD_NOCSJ              Reviewed;         446 AA.
AC   A1SE30;
DT   16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   08-MAY-2019, entry version 83.
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=Noca_0523;
OS   Nocardioides sp. (strain ATCC BAA-499 / JS614).
OC   Bacteria; Actinobacteria; Propionibacteriales; Nocardioidaceae;
OC   Nocardioides.
OX   NCBI_TaxID=196162;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-499 / JS614;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H.,
RA   Pitluck S., Thompson L.S., Brettin T., Bruce D., Han C., Tapia R.,
RA   Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E.,
RA   Mattes T., Gossett J., Richardson P.;
RT   "Complete sequence of chromosome 1 of Nocardioides sp. JS614.";
RL   Submitted (DEC-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 a menaquinone. 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 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; CP000509; ABL80065.1; -; Genomic_DNA.
DR   RefSeq; WP_011754015.1; NC_008699.1.
DR   SMR; A1SE30; -.
DR   STRING; 196162.Noca_0523; -.
DR   PRIDE; A1SE30; -.
DR   EnsemblBacteria; ABL80065; ABL80065; Noca_0523.
DR   KEGG; nca:Noca_0523; -.
DR   eggNOG; ENOG4105CQV; Bacteria.
DR   eggNOG; COG0649; LUCA.
DR   HOGENOM; HOG000228264; -.
DR   KO; K00333; -.
DR   OMA; KKIAWPA; -.
DR   OrthoDB; 473681at2; -.
DR   Proteomes; UP000000640; 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; IPR014029; NADH_UbQ_OxRdtase_49kDa_CS.
DR   InterPro; IPR022885; NDH1_su_D/H.
DR   InterPro; IPR029014; NiFe-Hase_large.
DR   Pfam; PF00346; Complex1_49kDa; 1.
DR   SUPFAM; SSF56762; SSF56762; 1.
DR   TIGRFAMs; TIGR01962; NuoD; 1.
DR   PROSITE; PS00535; COMPLEX1_49K; 1.
PE   3: Inferred from homology;
DR   PRODOM; A1SE30.
DR   SWISS-2DPAGE; A1SE30.
KW   Cell membrane; Complete proteome; Membrane; NAD; Quinone;
KW   Reference proteome; Translocase; Transport.
FT   CHAIN         1    446       NADH-quinone oxidoreductase subunit D.
FT                                /FTId=PRO_0000357876.
SQ   SEQUENCE   446 AA;  49335 MW;  4A088F7A10951E13 CRC64;
     MADQDLYSGS SETTEGRVFT VTGQDWDSIA EGLAEDEAQE RIVVNMGPQH PSTHGVLRLI
     LELEGETVTE ARAGIGYLHT GIEKNMEYRT WTQGVTFCTR MDYLSPFFNE MTYVLGIERL
     LDIEDRVPEK AQVMRVLLME LNRISSHLVA IATGGMELGA LTVMTIGFRE RELVLDLFEL
     ITGLRMNHAF IRPGGVAQDM PPGALDEIRG FVALMKKRLP EYADLCNANP IFKGRLEGIG
     HLDLAGCLAL GLTGPVLRST GYPWDLRKTQ PYCGYETYDF DVQTWDTSDS YGRFRIRLNE
     MWESLRIIEQ AADRLAGLDG APVMIEDKKI GWPSQLAIGS DGMGNSLDHI RHIMGESMEA
     LIHHFKLVTE GFRVPPGQAY VPVESPRGEL GAHVVSDGGT RPFRAHFRDP SFTNLQATSV
     MAEGGMVADV IVAIASIDPV MGGVDR
//

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