NDHN_SYNS3
ID NDHN_SYNS3 Reviewed; 153 AA.
AC Q0ID04;
DT 14-OCT-2008, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2006, sequence version 1.
DT 25-MAY-2022, entry version 77.
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}; OrderedLocusNames=sync_0438;
OS Synechococcus sp. (strain CC9311).
OC Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus;
OC unclassified Synechococcus.
OX NCBI_TaxID=64471;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CC9311;
RX PubMed=16938853; DOI=10.1073/pnas.0602963103;
RA Palenik B., Ren Q., Dupont C.L., Myers G.S., Heidelberg J.F., Badger J.H.,
RA Madupu R., Nelson W.C., Brinkac L.M., Dodson R.J., Durkin A.S.,
RA Daugherty S.C., Sullivan S.A., Khouri H., Mohamoud Y., Halpin R.,
RA Paulsen I.T.;
RT "Genome sequence of Synechococcus CC9311: insights into adaptation to a
RT coastal environment.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:13555-13559(2006).
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; CP000435; ABI47819.1; -; Genomic_DNA.
DR RefSeq; WP_011618400.1; NC_008319.1.
DR AlphaFoldDB; Q0ID04; -.
DR SMR; Q0ID04; -.
DR STRING; 64471.sync_0438; -.
DR EnsemblBacteria; ABI47819; ABI47819; sync_0438.
DR KEGG; syg:sync_0438; -.
DR eggNOG; ENOG502ZBMI; Bacteria.
DR HOGENOM; CLU_087432_0_0_3; -.
DR OMA; HGIRPPH; -.
DR OrthoDB; 1804108at2; -.
DR Proteomes; UP000001961; 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..153
FT /note="NAD(P)H-quinone oxidoreductase subunit N"
FT /id="PRO_0000352235"
SQ SEQUENCE 153 AA; 16767 MW; 36A2BE5928BA04C9 CRC64;
MPLLLSGRGF RRELESAGCM AVFAPLEGGA ETRLLRRLRG AGYRTQLSSA RGLGDPEVFL
FQKHGIRPPH LGHQSVGRGA AVGEVQEVMP LLGESMLGTK PVVLWLLEGQ VLSRSELSAL
CDLCRREPRL KVVVEMGGAR SLRWQPLKEL LSN
