ID   NDHL_SYNY3              Reviewed;          80 AA.
AC   P27372;
DT   01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1992, sequence version 1.
DT   27-MAR-2024, entry version 114.
DE   RecName: Full=NAD(P)H-quinone oxidoreductase subunit L;
DE            EC=7.1.1.-;
DE   AltName: Full=Inorganic carbon transport protein;
DE   AltName: Full=NAD(P)H dehydrogenase I subunit L;
DE   AltName: Full=NDH-1 subunit L;
DE   AltName: Full=NDH-L;
GN   Name=ndhL; Synonyms=ictA; OrderedLocusNames=ssr1386;
OS   Synechocystis sp. (strain PCC 6803 / Kazusa).
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales; Merismopediaceae;
OC   Synechocystis.
OX   NCBI_TaxID=1111708;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION IN INORGANIC CARBON
RP   TRANSPORT.
RX   PubMed=16668165; DOI=10.1104/pp.96.1.280;
RA   Ogawa T.;
RT   "Cloning and inactivation of a gene essential to inorganic carbon transport
RT   of Synechocystis PCC6803.";
RL   Plant Physiol. 96:280-284(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 6803 / Kazusa;
RX   PubMed=8905231; DOI=10.1093/dnares/3.3.109;
RA   Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y.,
RA   Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T.,
RA   Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S.,
RA   Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT   "Sequence analysis of the genome of the unicellular cyanobacterium
RT   Synechocystis sp. strain PCC6803. II. Sequence determination of the entire
RT   genome and assignment of potential protein-coding regions.";
RL   DNA Res. 3:109-136(1996).
RN   [3]
RP   PROTEIN SEQUENCE OF 42-50, AND SUBUNIT.
RX   PubMed=15548534; DOI=10.1074/jbc.m410914200;
RA   Battchikova N., Zhang P., Rudd S., Ogawa T., Aro E.-M.;
RT   "Identification of NdhL and Ssl1690 (NdhO) in NDH-1L and NDH-1M complexes
RT   of Synechocystis sp. PCC 6803.";
RL   J. Biol. Chem. 280:2587-2595(2005).
RN   [4]
RP   CHARACTERIZATION AS A MEMBER OF THE NAD(P)H-QUINONE OXIDOREDUCTASE COMPLEX,
RP   AND SUBCELLULAR LOCATION.
RX   PubMed=16669080; DOI=10.1104/pp.99.4.1604;
RA   Ogawa T.;
RT   "Identification and characterization of the ictA/ndhL gene product
RT   essential to inorganic carbon transport of Synechocystis PCC6803.";
RL   Plant Physiol. 99:1604-1608(1992).
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 (By similarity). Cyanobacterial NDH-1 also
CC       plays a role in inorganic carbon-concentration. {ECO:0000250,
CC       ECO:0000269|PubMed:16668165}.
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   -!- 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   -!- 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:0000269|PubMed:15548534}.
CC   -!- SUBCELLULAR LOCATION: Cellular thylakoid membrane
CC       {ECO:0000305|PubMed:16669080}; Multi-pass membrane protein
CC       {ECO:0000305|PubMed:16669080}.
CC   -!- SIMILARITY: Belongs to the complex I NdhL subunit family.
CC       {ECO:0000305}.
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DR   EMBL; M73833; AAA27290.1; -; Genomic_DNA.
DR   EMBL; BA000022; BAA18123.1; -; Genomic_DNA.
DR   PIR; JQ1959; JQ1959.
DR   AlphaFoldDB; P27372; -.
DR   SMR; P27372; -.
DR   IntAct; P27372; 7.
DR   STRING; 1148.gene:10498994; -.
DR   PaxDb; 1148-1653207; -.
DR   EnsemblBacteria; BAA18123; BAA18123; BAA18123.
DR   KEGG; syn:ssr1386; -.
DR   eggNOG; ENOG5032ZM4; Bacteria.
DR   InParanoid; P27372; -.
DR   Proteomes; UP000001425; 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   1: Evidence at protein level;
KW   Direct protein sequencing; Membrane; NAD; NADP; Plastoquinone; Quinone;
KW   Reference proteome; Thylakoid; Translocase; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN           1..80
FT                   /note="NAD(P)H-quinone oxidoreductase subunit L"
FT                   /id="PRO_0000084150"
FT   TRANSMEM        14..34
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        51..71
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   80 AA;  9252 MW;  311AD10FA3B6136D CRC64;
     MEDLLGLLLS ETGLLAIIYL GLSLAYLLVF PALLYWYLQK RWYVASSVER LVMYFLVFLF
     FPGLLVLSPV LNLRPRRQAA
//