NDHL_PARMW
ID NDHL_PARMW Reviewed; 83 AA.
AC Q7U620;
DT 04-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 89.
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=SYNW1521;
OS Parasynechococcus marenigrum (strain WH8102).
OC Bacteria; Cyanobacteria; Synechococcales; Prochlorococcaceae;
OC Parasynechococcus; Parasynechococcus marenigrum.
OX NCBI_TaxID=84588;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WH8102;
RX PubMed=12917641; DOI=10.1038/nature01943;
RA Palenik B., Brahamsha B., Larimer F.W., Land M.L., Hauser L., Chain P.,
RA Lamerdin J.E., Regala W., Allen E.E., McCarren J., Paulsen I.T.,
RA Dufresne A., Partensky F., Webb E.A., Waterbury J.;
RT "The genome of a motile marine Synechococcus.";
RL Nature 424:1037-1042(2003).
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; BX569693; CAE08036.1; -; Genomic_DNA.
DR RefSeq; WP_011128385.1; NC_005070.1.
DR AlphaFoldDB; Q7U620; -.
DR SMR; Q7U620; -.
DR STRING; 84588.SYNW1521; -.
DR EnsemblBacteria; CAE08036; CAE08036; SYNW1521.
DR KEGG; syw:SYNW1521; -.
DR eggNOG; ENOG5032ZM4; Bacteria.
DR HOGENOM; CLU_171077_1_0_3; -.
DR OMA; YWMNNRW; -.
DR OrthoDB; 2075884at2; -.
DR BioCyc; MetaCyc:TX72_RS07640-MON; -.
DR Proteomes; UP000001422; Chromosome.
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; Thylakoid; Translocase;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..83
FT /note="NAD(P)H-quinone oxidoreductase subunit L"
FT /id="PRO_0000353694"
FT TRANSMEM 18..38
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01355"
FT TRANSMEM 53..73
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01355"
SQ SEQUENCE 83 AA; 9387 MW; 91659677ECAD4CBB CRC64;
MDLQSLASSI PQDTLLVILA YALLGGLYLL VVPLALFFWM NSRWTRMGKI ERLLVYGLVF
LFFPGMVVFA PFLNFRLSGQ GDN
