GenomeNet

Database: UniProt
Entry: K4R529_STRDJ
LinkDB: K4R529_STRDJ
Original site: K4R529_STRDJ 
ID   K4R529_STRDJ            Unreviewed;       119 AA.
AC   K4R529;
DT   09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT   09-JAN-2013, sequence version 1.
DT   10-APR-2019, entry version 36.
DE   RecName: Full=NADH-quinone oxidoreductase subunit A {ECO:0000256|HAMAP-Rule:MF_01394};
DE            EC=7.1.1.- {ECO:0000256|HAMAP-Rule:MF_01394};
DE   AltName: Full=NADH dehydrogenase I subunit A {ECO:0000256|HAMAP-Rule:MF_01394};
DE   AltName: Full=NDH-1 subunit A {ECO:0000256|HAMAP-Rule:MF_01394};
DE   AltName: Full=NUO1 {ECO:0000256|HAMAP-Rule:MF_01394};
GN   Name=nuoA {ECO:0000256|HAMAP-Rule:MF_01394};
GN   ORFNames=BN159_3816 {ECO:0000313|EMBL:CCK28195.1};
OS   Streptomyces davaonensis (strain DSM 101723 / JCM 4913 / KCC S-0913 /
OS   768).
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=1214101 {ECO:0000313|EMBL:CCK28195.1, ECO:0000313|Proteomes:UP000008043};
RN   [1] {ECO:0000313|EMBL:CCK28195.1, ECO:0000313|Proteomes:UP000008043}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 101723 / JCM 4913 / KCC S-0913 / 768
RC   {ECO:0000313|Proteomes:UP000008043};
RX   PubMed=23043000; DOI=10.1128/JB.01592-12;
RA   Jankowitsch F., Schwarz J., Ruckert C., Gust B., Szczepanowski R.,
RA   Blom J., Pelzer S., Kalinowski J., Mack M.;
RT   "Genome sequence of the bacterium Streptomyces davawensis JCM 4913 and
RT   heterologous production of the unique antibiotic roseoflavin.";
RL   J. Bacteriol. 194:6818-6827(2012).
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:0000256|HAMAP-Rule:MF_01394}.
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:0000256|HAMAP-Rule:MF_01394,
CC         ECO:0000256|RuleBase:RU003639};
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:0000256|HAMAP-Rule:MF_01394}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|HAMAP-
CC       Rule:MF_01394, ECO:0000256|RuleBase:RU003639}; Multi-pass membrane
CC       protein {ECO:0000256|HAMAP-Rule:MF_01394,
CC       ECO:0000256|RuleBase:RU003639}.
CC   -!- SIMILARITY: Belongs to the complex I subunit 3 family.
CC       {ECO:0000256|HAMAP-Rule:MF_01394, ECO:0000256|RuleBase:RU003639}.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   -----------------------------------------------------------------------
DR   EMBL; HE971709; CCK28195.1; -; Genomic_DNA.
DR   RefSeq; WP_003992243.1; NC_020504.1.
DR   STRING; 1214101.BN159_3816; -.
DR   EnsemblBacteria; CCK28195; CCK28195; BN159_3816.
DR   GeneID; 34228293; -.
DR   KEGG; sdv:BN159_3816; -.
DR   PATRIC; fig|1214101.3.peg.3873; -.
DR   KO; K00330; -.
DR   OrthoDB; 1748431at2; -.
DR   Proteomes; UP000008043; 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   Gene3D; 1.20.58.1610; -; 1.
DR   HAMAP; MF_01394; NDH1_NuoA; 1.
DR   InterPro; IPR023043; NAD(P)H_OxRDtase_bac/plastid.
DR   InterPro; IPR000440; NADH_UbQ/plastoQ_OxRdtase_su3.
DR   InterPro; IPR038430; NDAH_ubi_oxred_su3_sf.
DR   PANTHER; PTHR11058; PTHR11058; 1.
DR   Pfam; PF00507; Oxidored_q4; 1.
PE   3: Inferred from homology;
KW   Cell membrane {ECO:0000256|HAMAP-Rule:MF_01394};
KW   Complete proteome {ECO:0000313|Proteomes:UP000008043};
KW   Membrane {ECO:0000256|HAMAP-Rule:MF_01394};
KW   NAD {ECO:0000256|HAMAP-Rule:MF_01394, ECO:0000256|RuleBase:RU003639};
KW   Quinone {ECO:0000256|HAMAP-Rule:MF_01394,
KW   ECO:0000256|RuleBase:RU003639};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008043};
KW   Translocase {ECO:0000256|HAMAP-Rule:MF_01394};
KW   Transmembrane {ECO:0000256|HAMAP-Rule:MF_01394,
KW   ECO:0000256|RuleBase:RU003639};
KW   Transmembrane helix {ECO:0000256|HAMAP-Rule:MF_01394};
KW   Transport {ECO:0000256|HAMAP-Rule:MF_01394};
KW   Ubiquinone {ECO:0000313|EMBL:CCK28195.1}.
FT   TRANSMEM      6     28       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01394}.
FT   TRANSMEM     61     82       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01394}.
FT   TRANSMEM     88    110       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01394}.
SQ   SEQUENCE   119 AA;  13242 MW;  5665B543A609BC8B CRC64;
     MNAYAPILVL GALGAGFAIF SVVMATLIGP KRYNRAKLEA YECGIEPTPT PAGGGRFPIK
     YYLTAMLFIV FDIEIVFLYP WAVTFDALGI FGLVEMLLFV LTVFVAYAYV WRRGGLEWD
//
DBGET integrated database retrieval system