NDHN_THEVB
ID NDHN_THEVB Reviewed; 150 AA.
AC Q8DJU2;
DT 14-OCT-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 N;
DE EC=7.1.1.-;
DE AltName: Full=NAD(P)H dehydrogenase I subunit N;
DE Short=NDH-1 subunit N;
DE Short=NDH-N;
GN Name=ndhN; OrderedLocusNames=tlr1130;
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 IDENTIFICATION BY MASS SPECTROMETRY, 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};
CC Peripheral membrane protein {ECO:0000305}; Cytoplasmic side
CC {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the complex I NdhN subunit family.
CC {ECO:0000305}.
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DR EMBL; BA000039; BAC08682.1; -; Genomic_DNA.
DR RefSeq; NP_681920.1; NC_004113.1.
DR RefSeq; WP_011056972.1; NC_004113.1.
DR PDB; 6HUM; EM; 3.34 A; N=1-150.
DR PDB; 6KHI; EM; 3.00 A; N=1-150.
DR PDB; 6KHJ; EM; 3.00 A; N=1-150.
DR PDB; 6L7O; EM; 3.20 A; N=1-150.
DR PDB; 6L7P; EM; 3.60 A; N=1-150.
DR PDB; 6NBQ; EM; 3.10 A; N=1-150.
DR PDB; 6NBX; EM; 3.50 A; N=1-150.
DR PDB; 6NBY; EM; 3.10 A; N=1-150.
DR PDB; 6TJV; EM; 3.20 A; N=1-150.
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; Q8DJU2; -.
DR SMR; Q8DJU2; -.
DR IntAct; Q8DJU2; 1.
DR STRING; 197221.22294853; -.
DR TCDB; 3.D.1.8.2; the h(+) or na(+)-translocating nadh dehydrogenase (ndh) family.
DR EnsemblBacteria; BAC08682; BAC08682; BAC08682.
DR KEGG; tel:tlr1130; -.
DR PATRIC; fig|197221.4.peg.1186; -.
DR eggNOG; ENOG502ZBMI; Bacteria.
DR OMA; HGIRPPH; -.
DR OrthoDB; 1804108at2; -.
DR Proteomes; UP000000440; 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_01353; NDH1_NDH1N; 1.
DR InterPro; IPR020874; NAD(P)H-quinone_OxRdtase_su_N.
DR PANTHER; PTHR35515; PTHR35515; 1.
DR Pfam; PF11909; NdhN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Membrane; NAD; NADP; Plastoquinone; Quinone;
KW Reference proteome; Thylakoid; Translocase; Transport.
FT CHAIN 1..150
FT /note="NAD(P)H-quinone oxidoreductase subunit N"
FT /id="PRO_0000352232"
FT HELIX 8..16
FT /evidence="ECO:0007829|PDB:6KHI"
FT STRAND 17..22
FT /evidence="ECO:0007829|PDB:6KHI"
FT STRAND 28..30
FT /evidence="ECO:0007829|PDB:6NBQ"
FT HELIX 31..38
FT /evidence="ECO:0007829|PDB:6KHI"
FT TURN 39..41
FT /evidence="ECO:0007829|PDB:6KHI"
FT STRAND 43..47
FT /evidence="ECO:0007829|PDB:6KHI"
FT HELIX 49..51
FT /evidence="ECO:0007829|PDB:6KHI"
FT HELIX 55..58
FT /evidence="ECO:0007829|PDB:6KHI"
FT STRAND 63..65
FT /evidence="ECO:0007829|PDB:6NBQ"
FT STRAND 71..73
FT /evidence="ECO:0007829|PDB:6KHI"
FT STRAND 78..80
FT /evidence="ECO:0007829|PDB:6NBQ"
FT HELIX 83..89
FT /evidence="ECO:0007829|PDB:6KHI"
FT STRAND 93..95
FT /evidence="ECO:0007829|PDB:6NBQ"
FT STRAND 98..103
FT /evidence="ECO:0007829|PDB:6KHI"
FT HELIX 105..107
FT /evidence="ECO:0007829|PDB:6NBQ"
FT HELIX 110..122
FT /evidence="ECO:0007829|PDB:6KHI"
FT STRAND 123..128
FT /evidence="ECO:0007829|PDB:6KHI"
FT STRAND 139..142
FT /evidence="ECO:0007829|PDB:6KHI"
FT HELIX 143..146
FT /evidence="ECO:0007829|PDB:6KHI"
SQ SEQUENCE 150 AA; 16636 MW; 6ED2F8EE6E024909 CRC64;
MGLLAGYQFV KDLESAGALA LFVPPEGGFE GRYQRRLRSK GYTTLPMSAP GLGDLAAYLT
QEHGIRPAHT GKEDIRVYFQ PPLVTYHLEN LPPNAKGLVL WLIDGKRLSK QEFAYLAQLT
QTLPKFKVVV EVGGDRVVRW EPLADWVAAA
