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NUOH_BRADU
ID   NUOH_BRADU              Reviewed;         355 AA.
AC   Q89KJ5;
DT   11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   25-MAY-2022, entry version 106.
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}; OrderedLocusNames=bll4910;
OS   Bradyrhizobium diazoefficiens (strain JCM 10833 / BCRC 13528 / IAM 13628 /
OS   NBRC 14792 / USDA 110).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Bradyrhizobiaceae; Bradyrhizobium.
OX   NCBI_TaxID=224911;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 10833 / BCRC 13528 / IAM 13628 / NBRC 14792 / USDA 110;
RX   PubMed=12597275; DOI=10.1093/dnares/9.6.189;
RA   Kaneko T., Nakamura Y., Sato S., Minamisawa K., Uchiumi T., Sasamoto S.,
RA   Watanabe A., Idesawa K., Iriguchi M., Kawashima K., Kohara M.,
RA   Matsumoto M., Shimpo S., Tsuruoka H., Wada T., Yamada M., Tabata S.;
RT   "Complete genomic sequence of nitrogen-fixing symbiotic bacterium
RT   Bradyrhizobium japonicum USDA110.";
RL   DNA Res. 9:189-197(2002).
CC   -!- FUNCTION: NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur
CC       (Fe-S) centers, to quinones in the respiratory chain. The immediate
CC       electron acceptor for the enzyme in this species is believed to be
CC       ubiquinone. Couples the redox reaction to proton translocation (for
CC       every two electrons transferred, four hydrogen ions are translocated
CC       across the cytoplasmic membrane), and thus conserves the redox energy
CC       in a proton gradient. This subunit may bind ubiquinone.
CC       {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, ChEBI:CHEBI:24646,
CC         ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:132124;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01350};
CC   -!- SUBUNIT: NDH-1 is composed of 14 different subunits. Subunits NuoA, H,
CC       J, K, L, M, N constitute the membrane sector of the complex.
CC       {ECO:0000255|HAMAP-Rule:MF_01350}.
CC   -!- SUBCELLULAR LOCATION: Cell inner 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}.
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DR   EMBL; BA000040; BAC50175.1; -; Genomic_DNA.
DR   RefSeq; NP_771550.1; NC_004463.1.
DR   RefSeq; WP_011087676.1; NC_004463.1.
DR   AlphaFoldDB; Q89KJ5; -.
DR   SMR; Q89KJ5; -.
DR   STRING; 224911.27353175; -.
DR   EnsemblBacteria; BAC50175; BAC50175; BAC50175.
DR   GeneID; 64024666; -.
DR   KEGG; bja:bll4910; -.
DR   PATRIC; fig|224911.5.peg.4995; -.
DR   eggNOG; COG1005; Bacteria.
DR   HOGENOM; CLU_015134_0_1_5; -.
DR   InParanoid; Q89KJ5; -.
DR   OMA; WSGWASN; -.
DR   PhylomeDB; Q89KJ5; -.
DR   Proteomes; UP000002526; 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   GO; GO:0009060; P:aerobic respiration; IBA:GO_Central.
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; PS00668; COMPLEX1_ND1_2; 1.
PE   3: Inferred from homology;
KW   Cell inner membrane; Cell membrane; Membrane; NAD; Quinone;
KW   Reference proteome; Translocase; Transmembrane; Transmembrane helix;
KW   Ubiquinone.
FT   CHAIN           1..355
FT                   /note="NADH-quinone oxidoreductase subunit H"
FT                   /id="PRO_0000244900"
FT   TRANSMEM        17..37
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01350"
FT   TRANSMEM        86..106
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01350"
FT   TRANSMEM        119..139
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01350"
FT   TRANSMEM        165..185
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01350"
FT   TRANSMEM        204..224
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01350"
FT   TRANSMEM        262..282
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01350"
FT   TRANSMEM        291..311
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01350"
FT   TRANSMEM        332..352
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01350"
SQ   SEQUENCE   355 AA;  39194 MW;  DDAC08C56180826B CRC64;
     MEFFESAFWT GFLWPLIIMV AESVLVLVVL LVAIAYILLA DRKIWAAVQI RRGPNVVGPW
     GLLQSFADLL KFVLKEPIIP AGANKGVFLL APLVSCVLAL AAWAVIPTNL GWVISDINVG
     ILFIFAISSL SIYGIIMAGW SSNSKYPFLA ALRSAAQMVS YEVSIGFVII TVLLCAGTLN
     LSAVVEAQHV RGLASLIGLP QLTILNWYVW PLFPMFVVFY VSALAETNRP PFDLVEAESE
     LVAGFMVEYG STPYLLFMLG EYVAIVTMCA MATILFLGGW LPPVDLPPFN WVPGIIWFLL
     KVFFMFFLFA MAKAIVPRYR YDQLMRLGWK VFLPLSLAMV IVVAGVLHFA GIAPK
 
 
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