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NUON_NITMU
ID   NUON_NITMU              Reviewed;         507 AA.
AC   Q2YA93;
DT   09-FEB-2010, integrated into UniProtKB/Swiss-Prot.
DT   20-DEC-2005, sequence version 1.
DT   25-MAY-2022, entry version 91.
DE   RecName: Full=NADH-quinone oxidoreductase subunit N {ECO:0000255|HAMAP-Rule:MF_00445};
DE            EC=7.1.1.- {ECO:0000255|HAMAP-Rule:MF_00445};
DE   AltName: Full=NADH dehydrogenase I subunit N {ECO:0000255|HAMAP-Rule:MF_00445};
DE   AltName: Full=NDH-1 subunit N {ECO:0000255|HAMAP-Rule:MF_00445};
GN   Name=nuoN {ECO:0000255|HAMAP-Rule:MF_00445}; OrderedLocusNames=Nmul_A1025;
OS   Nitrosospira multiformis (strain ATCC 25196 / NCIMB 11849 / C 71).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Nitrosomonadales;
OC   Nitrosomonadaceae; Nitrosospira.
OX   NCBI_TaxID=323848;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25196 / NCIMB 11849 / C 71;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Chain P., Malfatti S., Shin M.,
RA   Vergez L., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Lykidis A., Richardson P.;
RT   "Complete sequence of chromosome 1 of Nitrosospira multiformis ATCC
RT   25196.";
RL   Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
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. {ECO:0000255|HAMAP-Rule:MF_00445}.
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_00445};
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_00445}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC       Rule:MF_00445}; Multi-pass membrane protein {ECO:0000255|HAMAP-
CC       Rule:MF_00445}.
CC   -!- SIMILARITY: Belongs to the complex I subunit 2 family.
CC       {ECO:0000255|HAMAP-Rule:MF_00445}.
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DR   EMBL; CP000103; ABB74328.1; -; Genomic_DNA.
DR   RefSeq; WP_011380373.1; NZ_FNVK01000002.1.
DR   AlphaFoldDB; Q2YA93; -.
DR   SMR; Q2YA93; -.
DR   STRING; 323848.Nmul_A1025; -.
DR   EnsemblBacteria; ABB74328; ABB74328; Nmul_A1025.
DR   KEGG; nmu:Nmul_A1025; -.
DR   eggNOG; COG1007; Bacteria.
DR   HOGENOM; CLU_007100_1_5_4; -.
DR   OMA; NAWAPDA; -.
DR   OrthoDB; 1664448at2; -.
DR   Proteomes; UP000002718; 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   GO; GO:0042773; P:ATP synthesis coupled electron transport; IEA:InterPro.
DR   HAMAP; MF_00445; NDH1_NuoN_1; 1.
DR   InterPro; IPR010096; NADH-Q_OxRdtase_suN/2.
DR   InterPro; IPR001750; ND/Mrp_mem.
DR   Pfam; PF00361; Proton_antipo_M; 1.
DR   TIGRFAMs; TIGR01770; NDH_I_N; 1.
PE   3: Inferred from homology;
KW   Cell inner membrane; Cell membrane; Membrane; NAD; Quinone;
KW   Reference proteome; Translocase; Transmembrane; Transmembrane helix;
KW   Transport; Ubiquinone.
FT   CHAIN           1..507
FT                   /note="NADH-quinone oxidoreductase subunit N"
FT                   /id="PRO_0000391190"
FT   TRANSMEM        17..37
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT   TRANSMEM        46..66
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT   TRANSMEM        81..101
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT   TRANSMEM        113..133
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT   TRANSMEM        134..154
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT   TRANSMEM        168..188
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT   TRANSMEM        190..210
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT   TRANSMEM        211..231
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT   TRANSMEM        245..265
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT   TRANSMEM        279..299
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT   TRANSMEM        307..327
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT   TRANSMEM        334..354
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT   TRANSMEM        392..412
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT   TRANSMEM        425..445
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT   TRANSMEM        478..498
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
SQ   SEQUENCE   507 AA;  53746 MW;  75AAE0EE7543D508 CRC64;
     MNPMPSALPS DFLHVDLVTL SPLILLAAAA VVVMLTAAFY RHPRPVMILT LAGLVLSFMA
     LFLSQGTASS QVTTLLILDQ YALFFIGLIV VATFVVAILC YRYFGGGESR HEALYILLLL
     AALGGGVLVA SSHFASFLLG LELLSISLFA LIAYPRFTEH PLEAGIKYLI LAGFSSGLLL
     FGMALVYAQL GTMQFVKIGT MLAAPGAALE LYGLAGLALI VTGVGFKLAL VPFHMWTPDV
     YEGAPVPITA FIATASKGAM LVLLLRYFLM AGAHQSHSIT FALSLIAVAT ILVGNLLALL
     QNNIKRILAY SSIAQLGYLL VGFLAFDQLA IEAVAYFLTA YFVTMLGAFG VVTVLSEGFN
     GGSAGEFHDA GEKDSDRLAD YAGLFWHRPW LAGVFTAMLL SLAGIPLTMG FIGKFYIVTA
     GVEASLWMPV ITLVIGSIIG LFYYMRIIAV MYGWGPEAAG EAIMLRAASP SFAESATLAA
     LALLLIWLGI FPAQLIGVLE GAGGGLT
 
 
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