NDHN_SYNP2
ID NDHN_SYNP2 Reviewed; 157 AA.
AC B1XK97;
DT 14-OCT-2008, integrated into UniProtKB/Swiss-Prot.
DT 20-MAY-2008, sequence version 1.
DT 25-MAY-2022, entry version 80.
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=SYNPCC7002_A1143;
OS Synechococcus sp. (strain ATCC 27264 / PCC 7002 / PR-6) (Agmenellum
OS quadruplicatum).
OC Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus;
OC unclassified Synechococcus.
OX NCBI_TaxID=32049;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27264 / PCC 7002 / PR-6;
RA Li T., Zhao J., Zhao C., Liu Z., Zhao F., Marquardt J., Nomura C.T.,
RA Persson S., Detter J.C., Richardson P.M., Lanz C., Schuster S.C., Wang J.,
RA Li S., Huang X., Cai T., Yu Z., Luo J., Zhao J., Bryant D.A.;
RT "Complete sequence of Synechococcus sp. PCC 7002.";
RL Submitted (FEB-2008) 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; CP000951; ACA99143.1; -; Genomic_DNA.
DR RefSeq; WP_012306766.1; NC_010475.1.
DR AlphaFoldDB; B1XK97; -.
DR SMR; B1XK97; -.
DR STRING; 32049.SYNPCC7002_A1143; -.
DR EnsemblBacteria; ACA99143; ACA99143; SYNPCC7002_A1143.
DR KEGG; syp:SYNPCC7002_A1143; -.
DR eggNOG; ENOG502ZBMI; Bacteria.
DR HOGENOM; CLU_087432_0_0_3; -.
DR OMA; HGIRPPH; -.
DR Proteomes; UP000001688; 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 3: Inferred from homology;
KW Membrane; NAD; NADP; Plastoquinone; Quinone; Reference proteome; Thylakoid;
KW Translocase; Transport.
FT CHAIN 1..157
FT /note="NAD(P)H-quinone oxidoreductase subunit N"
FT /id="PRO_0000352234"
SQ SEQUENCE 157 AA; 17191 MW; 0E79D7FFB66202FD CRC64;
MALLTTGKSF IRTVEKSGAV AVYAPLEGGF EGRYVRRLRC SGYSVVNLTA RGLGDVAAYL
TQYHGIRPPH LGKKDIAGSG AAVGLRYYVP GIASYQLENL PQKSKGIILW IIEGFVLSRQ
EQEYLVSLTQ DNPQIKVVVE MGGDRQFSFK PLADLLV
