NDHN_CROS5
ID NDHN_CROS5 Reviewed; 158 AA.
AC B1WYX9;
DT 14-OCT-2008, integrated into UniProtKB/Swiss-Prot.
DT 20-MAY-2008, sequence version 1.
DT 25-MAY-2022, entry version 64.
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=cce_3395;
OS Crocosphaera subtropica (strain ATCC 51142 / BH68) (Cyanothece sp. (strain
OS ATCC 51142)).
OC Bacteria; Cyanobacteria; Oscillatoriophycideae; Chroococcales;
OC Aphanothecaceae; Crocosphaera; Crocosphaera subtropica.
OX NCBI_TaxID=43989;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51142 / BH68;
RX PubMed=18812508; DOI=10.1073/pnas.0805418105;
RA Welsh E.A., Liberton M., Stoeckel J., Loh T., Elvitigala T., Wang C.,
RA Wollam A., Fulton R.S., Clifton S.W., Jacobs J.M., Aurora R., Ghosh B.K.,
RA Sherman L.A., Smith R.D., Wilson R.K., Pakrasi H.B.;
RT "The genome of Cyanothece 51142, a unicellular diazotrophic cyanobacterium
RT important in the marine nitrogen cycle.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:15094-15099(2008).
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; CP000806; ACB52743.1; -; Genomic_DNA.
DR RefSeq; WP_009545435.1; NC_010546.1.
DR AlphaFoldDB; B1WYX9; -.
DR SMR; B1WYX9; -.
DR STRING; 43989.cce_3395; -.
DR EnsemblBacteria; ACB52743; ACB52743; cce_3395.
DR KEGG; cyt:cce_3395; -.
DR eggNOG; ENOG502ZBMI; Bacteria.
DR HOGENOM; CLU_087432_0_0_3; -.
DR OMA; HGIRPPH; -.
DR OrthoDB; 1804108at2; -.
DR Proteomes; UP000001203; Chromosome circular.
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..158
FT /note="NAD(P)H-quinone oxidoreductase subunit N"
FT /id="PRO_0000352215"
SQ SEQUENCE 158 AA; 17242 MW; BA5F097B7D7F104E CRC64;
MALLTTGKGF VRALEKSGAL GVYAPLEGGF EGRYQRRLRT NGYDSLSLTA RGLGDVSAYL
MGVHGVRPPH LGKKNIGQGA AVGPIYFVPP IAAYQLESLS PQSKGLVLWI LEGYILSKAE
LEYLVSLPQQ EPRIKVVVEL GGERYFRWEP LENLIAVA
