ID A0A0C1YP14_9CYAN Unreviewed; 81 AA.
AC A0A0C1YP14;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 24-JAN-2024, entry version 30.
DE RecName: Full=NAD(P)H-quinone oxidoreductase subunit L {ECO:0000256|HAMAP-Rule:MF_01355};
DE EC=7.1.1.- {ECO:0000256|HAMAP-Rule:MF_01355};
DE AltName: Full=NAD(P)H dehydrogenase I subunit L {ECO:0000256|HAMAP-Rule:MF_01355};
DE Short=NDH-1 subunit L {ECO:0000256|HAMAP-Rule:MF_01355};
DE Short=NDH-L {ECO:0000256|HAMAP-Rule:MF_01355};
GN Name=ndhL {ECO:0000256|HAMAP-Rule:MF_01355,
GN ECO:0000313|EMBL:NEV65848.1};
GN ORFNames=QQ91_001815 {ECO:0000313|EMBL:NEV65848.1};
OS Lyngbya confervoides BDU141951.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae;
OC Oscillatoriales; Oscillatoriaceae; Lyngbya.
OX NCBI_TaxID=1574623 {ECO:0000313|EMBL:NEV65848.1, ECO:0000313|Proteomes:UP000031561};
RN [1] {ECO:0000313|EMBL:NEV65848.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=BDU141951 {ECO:0000313|EMBL:NEV65848.1};
RA Malar M.C., Sen D., Tripathy S.;
RL Submitted (NOV-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:NEV65848.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=BDU141951 {ECO:0000313|EMBL:NEV65848.1};
RX PubMed=25745003;
RA Chandrababunaidu M.M., Sen D., Tripathy S.;
RT "Draft Genome Sequence of Filamentous Marine Cyanobacterium Lyngbya
RT confervoides Strain BDU141951.";
RL Genome Announc. 3:e00066-e00015(2015).
RN [3] {ECO:0000313|EMBL:NEV65848.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=BDU141951 {ECO:0000313|EMBL:NEV65848.1};
RA Sarangi A.N., Ghosh S., Mukherjee M., Tripathy S.;
RL Submitted (FEB-2020) 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:0000256|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:0000256|ARBA:ARBA00001230, ECO:0000256|HAMAP-
CC 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:0000256|ARBA:ARBA00001558, ECO:0000256|HAMAP-
CC 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:0000256|HAMAP-
CC Rule:MF_01355}.
CC -!- SUBCELLULAR LOCATION: Cellular thylakoid membrane {ECO:0000256|HAMAP-
CC Rule:MF_01355}; Multi-pass membrane protein {ECO:0000256|HAMAP-
CC Rule:MF_01355}. Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass
CC membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the complex I NdhL subunit family.
CC {ECO:0000256|HAMAP-Rule:MF_01355}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:NEV65848.1}.
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DR EMBL; JTHE02000002; NEV65848.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0C1YP14; -.
DR Proteomes; UP000031561; Unassembled WGS sequence.
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 PANTHER; PTHR36727; NAD(P)H-QUINONE OXIDOREDUCTASE SUBUNIT L, CHLOROPLASTIC; 1.
DR PANTHER; PTHR36727:SF2; NAD(P)H-QUINONE OXIDOREDUCTASE SUBUNIT L, CHLOROPLASTIC; 1.
DR Pfam; PF10716; NdhL; 1.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_01355};
KW NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|HAMAP-Rule:MF_01355};
KW NADP {ECO:0000256|ARBA:ARBA00022857, ECO:0000256|HAMAP-Rule:MF_01355};
KW Plastoquinone {ECO:0000256|ARBA:ARBA00022957, ECO:0000256|HAMAP-
KW Rule:MF_01355};
KW Quinone {ECO:0000256|ARBA:ARBA00022719, ECO:0000256|HAMAP-Rule:MF_01355};
KW Thylakoid {ECO:0000256|ARBA:ARBA00023078, ECO:0000256|HAMAP-Rule:MF_01355};
KW Translocase {ECO:0000256|ARBA:ARBA00022967, ECO:0000256|HAMAP-
KW Rule:MF_01355};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|HAMAP-
KW Rule:MF_01355};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, ECO:0000256|HAMAP-
KW Rule:MF_01355}; Transport {ECO:0000256|HAMAP-Rule:MF_01355}.
FT TRANSMEM 12..38
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01355"
FT TRANSMEM 50..70
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01355"
SQ SEQUENCE 81 AA; 9122 MW; 2DA4D34C1D9735E2 CRC64;
MLETLPLSLD TLISLGLYGG LAIAYLLVIP AAILFYLKAK WHKVGSVERF VLYGLMFVFF
PGMLLMSPFL NFRPQPRSLN S
//
