NDHL_THEVB
ID NDHL_THEVB Reviewed; 76 AA.
AC Q8DKZ3;
DT 04-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 85.
DE RecName: Full=NAD(P)H-quinone oxidoreductase subunit L;
DE EC=7.1.1.-;
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; OrderedLocusNames=tsr0706;
OS Thermosynechococcus vestitus (strain NIES-2133 / IAM M-273 / BP-1).
OC Bacteria; Cyanobacteria; Pseudanabaenales; Thermosynechococcaceae;
OC Thermosynechococcus.
OX NCBI_TaxID=197221;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIES-2133 / IAM M-273 / BP-1;
RX PubMed=12240834; DOI=10.1093/dnares/9.4.123;
RA Nakamura Y., Kaneko T., Sato S., Ikeuchi M., Katoh H., Sasamoto S.,
RA Watanabe A., Iriguchi M., Kawashima K., Kimura T., Kishida Y., Kiyokawa C.,
RA Kohara M., Matsumoto M., Matsuno A., Nakazaki N., Shimpo S., Sugimoto M.,
RA Takeuchi C., Yamada M., Tabata S.;
RT "Complete genome structure of the thermophilic cyanobacterium
RT Thermosynechococcus elongatus BP-1.";
RL DNA Res. 9:123-130(2002).
RN [2]
RP PROTEIN SEQUENCE OF 36-44, CHARACTERIZATION AS A MEMBER OF THE
RP NAD(P)H-QUINONE OXIDOREDUCTASE COMPLEX, AND SUBCOMPLEXES OF NDH-1.
RX PubMed=15910282; DOI=10.1042/bj20050390;
RA Zhang P., Battchikova N., Paakkarinen V., Katoh H., Iwai M., Ikeuchi M.,
RA Pakrasi H.B., Ogawa T., Aro E.-M.;
RT "Isolation, subunit composition and interaction of the NDH-1 complexes from
RT Thermosynechococcus elongatus BP-1.";
RL Biochem. J. 390:513-520(2005).
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 (By similarity). {ECO:0000250}.
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.
CC -!- SUBCELLULAR LOCATION: Cellular thylakoid membrane {ECO:0000305}; Multi-
CC pass membrane protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the complex I NdhL subunit family.
CC {ECO:0000305}.
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DR EMBL; BA000039; BAC08257.1; -; Genomic_DNA.
DR RefSeq; NP_681495.1; NC_004113.1.
DR RefSeq; WP_011056553.1; NC_004113.1.
DR PDB; 6HUM; EM; 3.34 A; L=1-76.
DR PDB; 6KHI; EM; 3.00 A; L=1-76.
DR PDB; 6KHJ; EM; 3.00 A; L=1-76.
DR PDB; 6L7O; EM; 3.20 A; L=1-76.
DR PDB; 6L7P; EM; 3.60 A; L=1-76.
DR PDB; 6NBQ; EM; 3.10 A; L=1-76.
DR PDB; 6NBX; EM; 3.50 A; L=1-76.
DR PDB; 6NBY; EM; 3.10 A; L=1-76.
DR PDB; 6TJV; EM; 3.20 A; L=1-76.
DR PDBsum; 6HUM; -.
DR PDBsum; 6KHI; -.
DR PDBsum; 6KHJ; -.
DR PDBsum; 6L7O; -.
DR PDBsum; 6L7P; -.
DR PDBsum; 6NBQ; -.
DR PDBsum; 6NBX; -.
DR PDBsum; 6NBY; -.
DR PDBsum; 6TJV; -.
DR AlphaFoldDB; Q8DKZ3; -.
DR SMR; Q8DKZ3; -.
DR IntAct; Q8DKZ3; 1.
DR STRING; 197221.22294427; -.
DR TCDB; 3.D.1.8.2; the h(+) or na(+)-translocating nadh dehydrogenase (ndh) family.
DR EnsemblBacteria; BAC08257; BAC08257; BAC08257.
DR KEGG; tel:tsr0706; -.
DR PATRIC; fig|197221.4.peg.746; -.
DR eggNOG; ENOG5032ZM4; Bacteria.
DR OMA; YWMNNRW; -.
DR BRENDA; 7.1.1.10; 7763.
DR Proteomes; UP000000440; 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 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Membrane; NAD; NADP;
KW Plastoquinone; Quinone; Reference proteome; Thylakoid; Translocase;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..76
FT /note="NAD(P)H-quinone oxidoreductase subunit L"
FT /id="PRO_0000353684"
FT TRANSMEM 8..28
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 45..65
FT /note="Helical"
FT /evidence="ECO:0000255"
FT HELIX 6..21
FT /evidence="ECO:0007829|PDB:6KHI"
FT HELIX 23..34
FT /evidence="ECO:0007829|PDB:6KHI"
FT STRAND 35..38
FT /evidence="ECO:0007829|PDB:6KHI"
FT HELIX 41..53
FT /evidence="ECO:0007829|PDB:6KHI"
FT HELIX 55..61
FT /evidence="ECO:0007829|PDB:6KHI"
FT HELIX 62..64
FT /evidence="ECO:0007829|PDB:6KHI"
SQ SEQUENCE 76 AA; 8571 MW; 3FAA4D52E0CE3D25 CRC64;
MAVSTELLVL GVYGALAGLY LLVVPAIVYA YLNARWYVAS SFERAFMYFL VTFFFPGLLL
LAPFINFRPQ PRSLNS
