ID A0A2Z5T107_9CYAN Unreviewed; 81 AA.
AC A0A2Z5T107;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 24-JAN-2024, entry version 15.
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:BBA80261.1};
GN ORFNames=RGRSB_1895 {ECO:0000313|EMBL:BBA80261.1};
OS cyanobacterium endosymbiont of Rhopalodia gibberula.
OC Bacteria; Cyanobacteriota.
OX NCBI_TaxID=1763363 {ECO:0000313|EMBL:BBA80261.1, ECO:0000313|Proteomes:UP000264686};
RN [1] {ECO:0000313|EMBL:BBA80261.1, ECO:0000313|Proteomes:UP000264686}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RgSB {ECO:0000313|EMBL:BBA80261.1};
RX PubMed=29026213; DOI=10.1038/s41598-017-13578-8;
RA Nakayama T., Inagaki Y.;
RT "Genomic divergence within non-photosynthetic cyanobacterial endosymbionts
RT in rhopalodiacean diatoms.";
RL Sci. Rep. 7:13075-13075(2017).
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}.
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DR EMBL; AP018341; BBA80261.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2Z5T107; -.
DR KEGG; cer:RGRSB_1895; -.
DR OrthoDB; 517549at2; -.
DR Proteomes; UP000264686; Chromosome.
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 Reference proteome {ECO:0000313|Proteomes:UP000264686};
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 15..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; 9668 MW; 902DF76EC66530E3 CRC64;
MTIVDFLTND TLSVALLYLT LSILYLLIIP GMVYFYLNSR WYVASSFERV LMYFLMFFFF
PGMLVLSPFL NFRPKRRNIT T
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