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NDHL_CROS5
ID   NDHL_CROS5              Reviewed;          85 AA.
AC   B1WNP9;
DT   04-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT   20-MAY-2008, sequence version 1.
DT   25-MAY-2022, entry version 66.
DE   RecName: Full=NAD(P)H-quinone oxidoreductase subunit L {ECO:0000255|HAMAP-Rule:MF_01355};
DE            EC=7.1.1.- {ECO:0000255|HAMAP-Rule:MF_01355};
DE   AltName: Full=NAD(P)H dehydrogenase I subunit L {ECO:0000255|HAMAP-Rule:MF_01355};
DE   AltName: Full=NDH-1 subunit L;
DE   AltName: Full=NDH-L;
GN   Name=ndhL {ECO:0000255|HAMAP-Rule:MF_01355}; OrderedLocusNames=cce_2128;
OS   Crocosphaera subtropica (strain ATCC 51142 / BH68) (Cyanothece sp. (strain
OS   ATCC 51142)).
OC   Bacteria; Cyanobacteria; Oscillatoriophycideae; Chroococcales;
OC   Aphanothecaceae; Crocosphaera; Crocosphaera subtropica.
OX   NCBI_TaxID=43989;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51142 / BH68;
RX   PubMed=18812508; DOI=10.1073/pnas.0805418105;
RA   Welsh E.A., Liberton M., Stoeckel J., Loh T., Elvitigala T., Wang C.,
RA   Wollam A., Fulton R.S., Clifton S.W., Jacobs J.M., Aurora R., Ghosh B.K.,
RA   Sherman L.A., Smith R.D., Wilson R.K., Pakrasi H.B.;
RT   "The genome of Cyanothece 51142, a unicellular diazotrophic cyanobacterium
RT   important in the marine nitrogen cycle.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:15094-15099(2008).
CC   -!- FUNCTION: NDH-1 shuttles electrons from an unknown electron donor, via
CC       FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory
CC       and/or the photosynthetic chain. The immediate electron acceptor for
CC       the enzyme in this species is believed to be plastoquinone. Couples the
CC       redox reaction to proton translocation, and thus conserves the redox
CC       energy in a proton gradient. Cyanobacterial NDH-1 also plays a role in
CC       inorganic carbon-concentration. {ECO:0000255|HAMAP-Rule:MF_01355}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a plastoquinone + (n+1) H(+)(in) + NADH = a plastoquinol + n
CC         H(+)(out) + NAD(+); Xref=Rhea:RHEA:42608, Rhea:RHEA-COMP:9561,
CC         Rhea:RHEA-COMP:9562, ChEBI:CHEBI:15378, ChEBI:CHEBI:17757,
CC         ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:62192;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01355};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a plastoquinone + (n+1) H(+)(in) + NADPH = a plastoquinol + n
CC         H(+)(out) + NADP(+); Xref=Rhea:RHEA:42612, Rhea:RHEA-COMP:9561,
CC         Rhea:RHEA-COMP:9562, ChEBI:CHEBI:15378, ChEBI:CHEBI:17757,
CC         ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:62192;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01355};
CC   -!- SUBUNIT: NDH-1 can be composed of about 15 different subunits;
CC       different subcomplexes with different compositions have been identified
CC       which probably have different functions. {ECO:0000255|HAMAP-
CC       Rule:MF_01355}.
CC   -!- SUBCELLULAR LOCATION: Cellular thylakoid membrane {ECO:0000255|HAMAP-
CC       Rule:MF_01355}; Multi-pass membrane protein {ECO:0000255|HAMAP-
CC       Rule:MF_01355}.
CC   -!- SIMILARITY: Belongs to the complex I NdhL subunit family.
CC       {ECO:0000255|HAMAP-Rule:MF_01355}.
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DR   EMBL; CP000806; ACB51478.1; -; Genomic_DNA.
DR   RefSeq; WP_009546880.1; NC_010546.1.
DR   AlphaFoldDB; B1WNP9; -.
DR   SMR; B1WNP9; -.
DR   STRING; 43989.cce_2128; -.
DR   EnsemblBacteria; ACB51478; ACB51478; cce_2128.
DR   KEGG; cyt:cce_2128; -.
DR   eggNOG; ENOG5032ZM4; Bacteria.
DR   HOGENOM; CLU_171077_0_0_3; -.
DR   OMA; YWMNNRW; -.
DR   Proteomes; UP000001203; Chromosome circular.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0031676; C:plasma membrane-derived thylakoid 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   HAMAP; MF_01355; NDH1_NDH1L; 1.
DR   InterPro; IPR019654; NADH-quinone_OxRdatse_su_L.
DR   Pfam; PF10716; NdhL; 1.
PE   3: Inferred from homology;
KW   Membrane; NAD; NADP; Plastoquinone; Quinone; Reference proteome; Thylakoid;
KW   Translocase; Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..85
FT                   /note="NAD(P)H-quinone oxidoreductase subunit L"
FT                   /id="PRO_0000353668"
FT   TRANSMEM        17..37
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01355"
FT   TRANSMEM        54..74
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01355"
SQ   SEQUENCE   85 AA;  9973 MW;  C3CBB67396877E78 CRC64;
     MDTIIDAIAS LPQDTLIVAV LYLGLSLLYL LIIPGFVYFY LNSRWYVASS FERAFMYFLM
     FFFFPGVLLL SPFLNFRPKR RQVNS
 
 
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