NDHN_SYNE7
ID NDHN_SYNE7 Reviewed; 158 AA.
AC Q31L05;
DT 14-OCT-2008, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 74.
DE RecName: Full=NAD(P)H-quinone oxidoreductase subunit N {ECO:0000255|HAMAP-Rule:MF_01353};
DE EC=7.1.1.- {ECO:0000255|HAMAP-Rule:MF_01353};
DE AltName: Full=NAD(P)H dehydrogenase I subunit N {ECO:0000255|HAMAP-Rule:MF_01353};
DE Short=NDH-1 subunit N {ECO:0000255|HAMAP-Rule:MF_01353};
DE Short=NDH-N {ECO:0000255|HAMAP-Rule:MF_01353};
GN Name=ndhN {ECO:0000255|HAMAP-Rule:MF_01353};
GN OrderedLocusNames=Synpcc7942_2234;
OS Synechococcus elongatus (strain PCC 7942 / FACHB-805) (Anacystis nidulans
OS R2).
OC Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus.
OX NCBI_TaxID=1140;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 7942 / FACHB-805;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA Hammon N., Israni S., Pitluck S., Schmutz J., Larimer F., Land M.,
RA Kyrpides N., Lykidis A., Richardson P.;
RT "Complete sequence of chromosome 1 of Synechococcus elongatus PCC 7942.";
RL Submitted (AUG-2005) 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:0000255|HAMAP-Rule:MF_01353}.
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:0000255|HAMAP-Rule:MF_01353};
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:0000255|HAMAP-Rule:MF_01353};
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:0000255|HAMAP-
CC Rule:MF_01353}.
CC -!- SUBCELLULAR LOCATION: Cellular thylakoid membrane {ECO:0000255|HAMAP-
CC Rule:MF_01353}; Peripheral membrane protein {ECO:0000255|HAMAP-
CC Rule:MF_01353}; Cytoplasmic side {ECO:0000255|HAMAP-Rule:MF_01353}.
CC -!- SIMILARITY: Belongs to the complex I NdhN subunit family.
CC {ECO:0000255|HAMAP-Rule:MF_01353}.
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DR EMBL; CP000100; ABB58264.1; -; Genomic_DNA.
DR RefSeq; WP_011244174.1; NC_007604.1.
DR AlphaFoldDB; Q31L05; -.
DR SMR; Q31L05; -.
DR STRING; 1140.Synpcc7942_2234; -.
DR PRIDE; Q31L05; -.
DR EnsemblBacteria; ABB58264; ABB58264; Synpcc7942_2234.
DR KEGG; syf:Synpcc7942_2234; -.
DR eggNOG; ENOG502ZBMI; Bacteria.
DR HOGENOM; CLU_087432_0_0_3; -.
DR OMA; HGIRPPH; -.
DR OrthoDB; 1804108at2; -.
DR BioCyc; MetaCyc:SYNPCC7942_2234-MON; -.
DR BioCyc; SYNEL:SYNPCC7942_2234-MON; -.
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 3: Inferred from homology;
KW Membrane; NAD; NADP; Plastoquinone; Quinone; Thylakoid; Translocase;
KW Transport.
FT CHAIN 1..158
FT /note="NAD(P)H-quinone oxidoreductase subunit N"
FT /id="PRO_0000352231"
SQ SEQUENCE 158 AA; 17145 MW; 51225D2F0C78A7E2 CRC64;
MALITTGSKF LRALEQEGAL AVYAPLEGGY EGRYLRRLRS KGYSALTYSA RGLGDPAQFL
MDIHGVRPPH LGKQTIGNEA AVGRVEYVLP LVGYPLQNLP ANAKGLVLWL LEGHVLSPQE
LSYFVTLPQA EPRLKVVIEM GGDRGFSWQP LAAVAEAA
