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NUON2_ACICJ
ID   NUON2_ACICJ             Reviewed;         486 AA.
AC   A5FXI8;
DT   09-FEB-2010, integrated into UniProtKB/Swiss-Prot.
DT   12-JUN-2007, sequence version 1.
DT   25-MAY-2022, entry version 75.
DE   RecName: Full=NADH-quinone oxidoreductase subunit N 2 {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 2 {ECO:0000255|HAMAP-Rule:MF_00445};
DE   AltName: Full=NDH-1 subunit N 2 {ECO:0000255|HAMAP-Rule:MF_00445};
GN   Name=nuoN2 {ECO:0000255|HAMAP-Rule:MF_00445}; OrderedLocusNames=Acry_1108;
OS   Acidiphilium cryptum (strain JF-5).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC   Acetobacteraceae; Acidiphilium.
OX   NCBI_TaxID=349163;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JF-5;
RG   US DOE Joint Genome Institute;
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., Pitluck S.,
RA   Sims D., Brettin T., Bruce D., Han C., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Kim E., Magnuson T., Richardson P.;
RT   "Complete sequence of chromosome of Acidiphilium cryptum JF-5.";
RL   Submitted (MAY-2007) 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; CP000697; ABQ30320.1; -; Genomic_DNA.
DR   RefSeq; WP_011941994.1; NC_009484.1.
DR   AlphaFoldDB; A5FXI8; -.
DR   SMR; A5FXI8; -.
DR   STRING; 349163.Acry_1108; -.
DR   EnsemblBacteria; ABQ30320; ABQ30320; Acry_1108.
DR   KEGG; acr:Acry_1108; -.
DR   eggNOG; COG1007; Bacteria.
DR   HOGENOM; CLU_007100_1_5_5; -.
DR   OMA; NAWAPDA; -.
DR   OrthoDB; 1664448at2; -.
DR   Proteomes; UP000000245; 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..486
FT                   /note="NADH-quinone oxidoreductase subunit N 2"
FT                   /id="PRO_0000391084"
FT   TRANSMEM        11..31
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT   TRANSMEM        39..59
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT   TRANSMEM        76..96
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT   TRANSMEM        108..128
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT   TRANSMEM        129..149
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT   TRANSMEM        165..185
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT   TRANSMEM        208..228
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT   TRANSMEM        239..259
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT   TRANSMEM        275..295
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        329..349
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT   TRANSMEM        375..395
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT   TRANSMEM        398..418
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT   TRANSMEM        419..439
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT   TRANSMEM        456..476
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
SQ   SEQUENCE   486 AA;  50181 MW;  D742A7961E114AA9 CRC64;
     MTAPAFTAKA FAAFAPFTLL GAVTILVMLL IAVRRDHRLV ALSTIAGLLL CCIALPLAAP
     ASPVAVTKLF VIDGAALFYA GLVLVSALVV AALSWVYLDR VGEGPREEYY LLLLTATLGA
     AILPASVHFA SFFLGIETLG ISLLGLIAYA GPRGSAAEAG TKYLILSGAA SAFLLFGMAL
     IYAAFGSMSF ARIGALAHQA GPADLYRLAG IALILSGVAF KLSLVPFHMW TPDVYEGAPA
     PVTAFIAVVS KIAVFAVILR FFALAGAHAD ASLRAGIAAV AILSMLAGNL LALLQTNVKR
     LLAYSSIAHL GYLLVAFLAA PALGVDAAAY YLAAYAVTSL GAFGIVALLS APGAGRDADR
     IEDYRGLFRT RPFLAASLAL MLLSLAGMPP TMGFIAKFYL VVAGVGTALF WPVAALLLGS
     VIGLYYYLRI LVAMALPAPG DEEARHPNAV PPLGNAVIGA LLVLLVVLGA YPAPALALIR
     MTIGHG
 
 
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