NDHL_SYNR3
ID NDHL_SYNR3 Reviewed; 83 AA.
AC A5GUE6;
DT 04-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 04-NOV-2008, sequence version 2.
DT 25-MAY-2022, entry version 64.
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};
GN OrderedLocusNames=SynRCC307_1602;
OS Synechococcus sp. (strain RCC307).
OC Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus;
OC unclassified Synechococcus.
OX NCBI_TaxID=316278;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RCC307;
RG Genoscope;
RL Submitted (MAY-2006) to the EMBL/GenBank/DDBJ databases.
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAK28505.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; CT978603; CAK28505.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_043738178.1; NC_009482.1.
DR AlphaFoldDB; A5GUE6; -.
DR SMR; A5GUE6; -.
DR STRING; 316278.SynRCC307_1602; -.
DR EnsemblBacteria; CAK28505; CAK28505; SynRCC307_1602.
DR KEGG; syr:SynRCC307_1602; -.
DR eggNOG; ENOG5032ZM4; Bacteria.
DR HOGENOM; CLU_171077_1_0_3; -.
DR OrthoDB; 2075884at2; -.
DR Proteomes; UP000001115; 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; Reference proteome; Thylakoid;
KW Translocase; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..83
FT /note="NAD(P)H-quinone oxidoreductase subunit L"
FT /id="PRO_0000353692"
FT TRANSMEM 17..37
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; 9291 MW; A62D0FBB868E093A CRC64;
MPFQQLLSQL PDQALPVLLA YGALGGAYLL VVPLALLLWM NKRWHQMGKI ERTAIYGMVF
LFFPGLILFA PFINLRMAGQ GEA
