(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
//
If you have problems or comments...
Back to PBIL home page