(data stored in ACNUC1104 zone)

SWISSPROT: NUOH_NOCSJ

ID   NUOH_NOCSJ              Reviewed;         449 AA.
AC   A1SE34;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   08-MAY-2019, entry version 73.
DE   RecName: Full=NADH-quinone oxidoreductase subunit H {ECO:0000255|HAMAP-Rule:MF_01350};
DE            EC=7.1.1.- {ECO:0000255|HAMAP-Rule:MF_01350};
DE   AltName: Full=NADH dehydrogenase I subunit H {ECO:0000255|HAMAP-Rule:MF_01350};
DE   AltName: Full=NDH-1 subunit H {ECO:0000255|HAMAP-Rule:MF_01350};
GN   Name=nuoH {ECO:0000255|HAMAP-Rule:MF_01350};
GN   OrderedLocusNames=Noca_0527;
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 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. This subunit may
CC       bind ubiquinone. {ECO:0000255|HAMAP-Rule:MF_01350}.
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_01350};
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_01350}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP-
CC       Rule:MF_01350}; Multi-pass membrane protein {ECO:0000255|HAMAP-
CC       Rule:MF_01350}.
CC   -!- SIMILARITY: Belongs to the complex I subunit 1 family.
CC       {ECO:0000255|HAMAP-Rule:MF_01350}.
DR   EMBL; CP000509; ABL80069.1; -; Genomic_DNA.
DR   RefSeq; WP_011754019.1; NC_008699.1.
DR   STRING; 196162.Noca_0527; -.
DR   PRIDE; A1SE34; -.
DR   EnsemblBacteria; ABL80069; ABL80069; Noca_0527.
DR   KEGG; nca:Noca_0527; -.
DR   eggNOG; ENOG4105CMZ; Bacteria.
DR   eggNOG; COG1005; LUCA.
DR   HOGENOM; HOG000228276; -.
DR   KO; K00337; -.
DR   OMA; MKFALFY; -.
DR   OrthoDB; 1559067at2; -.
DR   Proteomes; UP000000640; 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:0016655; F:oxidoreductase activity, acting on NAD(P)H, quinone or similar compound as acceptor; IEA:UniProtKB-UniRule.
DR   GO; GO:0048038; F:quinone binding; IEA:UniProtKB-KW.
DR   HAMAP; MF_01350; NDH1_NuoH; 1.
DR   InterPro; IPR001694; NADH_UbQ_OxRdtase_su1/FPO.
DR   InterPro; IPR018086; NADH_UbQ_OxRdtase_su1_CS.
DR   PANTHER; PTHR11432; PTHR11432; 1.
DR   Pfam; PF00146; NADHdh; 1.
DR   PROSITE; PS00667; COMPLEX1_ND1_1; 1.
DR   PROSITE; PS00668; COMPLEX1_ND1_2; 1.
PE   3: Inferred from homology;
DR   PRODOM; A1SE34.
DR   SWISS-2DPAGE; A1SE34.
KW   Cell membrane; Complete proteome; Membrane; NAD; Quinone;
KW   Reference proteome; Translocase; Transmembrane; Transmembrane helix;
KW   Ubiquinone.
FT   CHAIN         1    449       NADH-quinone oxidoreductase subunit H.
FT                                /FTId=PRO_0000299945.
FT   TRANSMEM     23     43       Helical. {ECO:0000255|HAMAP-
FT                                Rule:MF_01350}.
FT   TRANSMEM     93    113       Helical. {ECO:0000255|HAMAP-
FT                                Rule:MF_01350}.
FT   TRANSMEM    137    157       Helical. {ECO:0000255|HAMAP-
FT                                Rule:MF_01350}.
FT   TRANSMEM    176    196       Helical. {ECO:0000255|HAMAP-
FT                                Rule:MF_01350}.
FT   TRANSMEM    209    229       Helical. {ECO:0000255|HAMAP-
FT                                Rule:MF_01350}.
FT   TRANSMEM    258    280       Helical. {ECO:0000255|HAMAP-
FT                                Rule:MF_01350}.
FT   TRANSMEM    300    320       Helical. {ECO:0000255|HAMAP-
FT                                Rule:MF_01350}.
FT   TRANSMEM    332    352       Helical. {ECO:0000255|HAMAP-
FT                                Rule:MF_01350}.
FT   TRANSMEM    368    388       Helical. {ECO:0000255|HAMAP-
FT                                Rule:MF_01350}.
SQ   SEQUENCE   449 AA;  48538 MW;  D8C4B9BCB58B6BC5 CRC64;
     MNTLTAPLPM ATDALSQFGH DAWWVIGLKA VLILVVLLLL TLFNIWFERR VVGRMQHRPG
     PNVNGPFGLL QSLADALKLI FKEGIIPKAA DKAVYLIAPV IAVIPSFITF SVIPFGPEVT
     IPFTDTRTPL QLTDMPVAVL FVMAIASIGI YGIVLGGWSS GSTYSLLGGL RSSAQMISYE
     VAMGLALVAV FLYAGSMSTS EIVAAQDNLW YGLILVPSFV IYLIAMVGET NRAPFDLPEA
     EGELVGGFHT EYSSMTFALF FLAEYINMAT VSAVATTLFL GGWHAPFWLD HAWAGANEGY
     WPLLWFLGKV LFFVFIFIWL RGTLPRLRYD QFMAFGWKRL IPVALVWIVA VATIRSISLD
     GGVDRRYLLI GIGALAVVFL VLFFIGGAAE EQPTTVPEAA PAGGYPVPPM PAGGPVRGAA
     VPLTFDRSSP IASSMPQPSA ATRSAGEEI
//

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