ID K9XIM3_9CHRO Unreviewed; 83 AA.
AC K9XIM3;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 24-JAN-2024, entry version 37.
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 ORFNames=Glo7428_3918 {ECO:0000313|EMBL:AFZ32373.1};
OS Gloeocapsa sp. PCC 7428.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae;
OC Chroococcales; Chroococcaceae; Gloeocapsa.
OX NCBI_TaxID=1173026 {ECO:0000313|EMBL:AFZ32373.1, ECO:0000313|Proteomes:UP000010476};
RN [1] {ECO:0000313|EMBL:AFZ32373.1, ECO:0000313|Proteomes:UP000010476}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 7428 {ECO:0000313|EMBL:AFZ32373.1,
RC ECO:0000313|Proteomes:UP000010476};
RG US DOE Joint Genome Institute;
RA Gugger M., Coursin T., Rippka R., Tandeau De Marsac N., Huntemann M.,
RA Wei C.-L., Han J., Detter J.C., Han C., Tapia R., Davenport K.,
RA Daligault H., Erkkila T., Gu W., Munk A.C.C., Teshima H., Xu Y., Chain P.,
RA Chen A., Krypides N., Mavromatis K., Markowitz V., Szeto E., Ivanova N.,
RA Mikhailova N., Ovchinnikova G., Pagani I., Pati A., Goodwin L., Peters L.,
RA Pitluck S., Woyke T., Kerfeld C.;
RT "Finished chromosome of genome of Gloeocapsa sp. PCC 7428.";
RL Submitted (JUN-2012) 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}.
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DR EMBL; CP003646; AFZ32373.1; -; Genomic_DNA.
DR AlphaFoldDB; K9XIM3; -.
DR STRING; 1173026.Glo7428_3918; -.
DR KEGG; glp:Glo7428_3918; -.
DR eggNOG; ENOG5032ZM4; Bacteria.
DR HOGENOM; CLU_171077_0_0_3; -.
DR Proteomes; UP000010476; 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:UP000010476};
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 14..41
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01355"
FT TRANSMEM 53..72
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01355"
SQ SEQUENCE 83 AA; 9774 MW; 580850B1045B23E9 CRC64;
MDSLLEYLNQ NQPIAIALLY LVLAGAYLLV VPLAIMLYLK LRWYNATSFE RGFMYFLVFF
FFPGLLLLAP FMNFRPQRRQ ISS
//
