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NUOL_BUCAI
ID   NUOL_BUCAI              Reviewed;         614 AA.
AC   P57262;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2000, sequence version 1.
DT   25-MAY-2022, entry version 103.
DE   RecName: Full=NADH-quinone oxidoreductase subunit L;
DE            EC=7.1.1.-;
DE   AltName: Full=NADH dehydrogenase I subunit L;
DE   AltName: Full=NDH-1 subunit L;
GN   Name=nuoL; OrderedLocusNames=BU164;
OS   Buchnera aphidicola subsp. Acyrthosiphon pisum (strain APS) (Acyrthosiphon
OS   pisum symbiotic bacterium).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Buchnera.
OX   NCBI_TaxID=107806;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=APS;
RX   PubMed=10993077; DOI=10.1038/35024074;
RA   Shigenobu S., Watanabe H., Hattori M., Sakaki Y., Ishikawa H.;
RT   "Genome sequence of the endocellular bacterial symbiont of aphids Buchnera
RT   sp. APS.";
RL   Nature 407:81-86(2000).
CC   -!- FUNCTION: NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur
CC       (Fe-S) centers, to quinones in the respiratory chain. Couples the redox
CC       reaction to proton translocation (for every two electrons transferred,
CC       four hydrogen ions are translocated across the cytoplasmic membrane),
CC       and thus conserves the redox energy in a proton gradient (By
CC       similarity). {ECO:0000250}.
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   -!- SUBUNIT: Composed of 13 different subunits. Subunits NuoA, H, J, K, L,
CC       M, N constitute the membrane sector of the complex (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC       protein {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the complex I subunit 5 family. {ECO:0000305}.
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DR   EMBL; BA000003; BAB12882.1; -; Genomic_DNA.
DR   RefSeq; NP_239996.1; NC_002528.1.
DR   RefSeq; WP_010895980.1; NC_002528.1.
DR   AlphaFoldDB; P57262; -.
DR   SMR; P57262; -.
DR   STRING; 107806.10038847; -.
DR   EnsemblBacteria; BAB12882; BAB12882; BAB12882.
DR   KEGG; buc:BU164; -.
DR   PATRIC; fig|107806.10.peg.174; -.
DR   eggNOG; COG1009; Bacteria.
DR   HOGENOM; CLU_007100_6_2_6; -.
DR   OMA; GVGIMSF; -.
DR   Proteomes; UP000001806; 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   InterPro; IPR018393; NADHpl_OxRdtase_5_subgr.
DR   InterPro; IPR001750; ND/Mrp_mem.
DR   InterPro; IPR003945; NU5C-like.
DR   InterPro; IPR001516; Proton_antipo_N.
DR   PANTHER; PTHR42829; PTHR42829; 1.
DR   Pfam; PF00361; Proton_antipo_M; 1.
DR   Pfam; PF00662; Proton_antipo_N; 1.
DR   TIGRFAMs; TIGR01974; NDH_I_L; 1.
PE   3: Inferred from homology;
KW   Cell membrane; Membrane; NAD; Quinone; Reference proteome; Translocase;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..614
FT                   /note="NADH-quinone oxidoreductase subunit L"
FT                   /id="PRO_0000118214"
FT   TRANSMEM        1..21
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        33..53
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        79..99
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        136..156
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        168..188
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        207..227
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        247..267
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        271..291
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        327..347
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        372..392
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        410..430
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        455..475
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        492..512
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        533..553
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        593..613
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   614 AA;  70882 MW;  18CCC2DFC4FE27E0 CRC64;
     MSIIFFIILF PLIGFLFLST IQDFIFKRYT LNIGIFSIFI SFFITCFYGV SILKNNNQVF
     TQILWKWLSI NEFKIDFGFF LDGLSLSMLF VITGVGLLIH IFSSWYMRYK EGQSRFFAYT
     NLFIASMSVL VLADNFLFMY LGWEGVSVCS YLLIGFYYTE LKNNLCAFKA FILTRVSDVF
     LMIGMFLIYR EFNSFNFQEI KFLSSFLNVE NFYYLDYITL FLLLGVIGKS AQLPLQTWLS
     DAMVGPTPVS ALIHAATMVT AGVYLIARTH FLFLLTPGIL YLVGLIGTLT ILVSSISALV
     QKDIKRILAY STMSQIGYMF LALGVKAWSA AITHLIMHAI FKALLFLSAG SLIKSCKNEK
     NIFKMGGLRK QLPFLYISFI VGGASLVSFP LITAGFYSKG NILFSVLKSG CIDFFIIGLF
     CSFLTAIYTF RMIFVIFHGK NIHTADSSTN LQHNIPLFVL LLLSTVFGSY ISPPLSDVFP
     LSYTPIDHKF AFEIICSILS LSGIYLSYYI WIKNLYVLDK IFQFKFMRYL YYFFLKGWGF
     NWFYKISFVY FYLYISKRLS ADPLNKIINY FLKVTQIFNF YLLKTSNGYV RWYVASMILG
     INFIFLLMLF FYFN
 
 
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