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}.
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; 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