NDHN_PROMS
ID NDHN_PROMS Reviewed; 158 AA.
AC A2BTD8;
DT 14-OCT-2008, integrated into UniProtKB/Swiss-Prot.
DT 20-FEB-2007, sequence version 1.
DT 25-MAY-2022, entry version 69.
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=A9601_17661;
OS Prochlorococcus marinus (strain AS9601).
OC Bacteria; Cyanobacteria; Synechococcales; Prochlorococcaceae;
OC Prochlorococcus.
OX NCBI_TaxID=146891;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AS9601;
RX PubMed=18159947; DOI=10.1371/journal.pgen.0030231;
RA Kettler G.C., Martiny A.C., Huang K., Zucker J., Coleman M.L., Rodrigue S.,
RA Chen F., Lapidus A., Ferriera S., Johnson J., Steglich C., Church G.M.,
RA Richardson P., Chisholm S.W.;
RT "Patterns and implications of gene gain and loss in the evolution of
RT Prochlorococcus.";
RL PLoS Genet. 3:2515-2528(2007).
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; CP000551; ABM71049.1; -; Genomic_DNA.
DR RefSeq; WP_011819171.1; NC_008816.1.
DR AlphaFoldDB; A2BTD8; -.
DR SMR; A2BTD8; -.
DR STRING; 146891.A9601_17661; -.
DR EnsemblBacteria; ABM71049; ABM71049; A9601_17661.
DR KEGG; pmb:A9601_17661; -.
DR eggNOG; ENOG5033TWM; Bacteria.
DR HOGENOM; CLU_087432_0_0_3; -.
DR OMA; HGIRPPH; -.
DR OrthoDB; 1804108at2; -.
DR Proteomes; UP000002590; 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; Thylakoid; Translocase;
KW Transport.
FT CHAIN 1..158
FT /note="NAD(P)H-quinone oxidoreductase subunit N"
FT /id="PRO_0000352220"
SQ SEQUENCE 158 AA; 17772 MW; 6C30E9087DA527A5 CRC64;
MPLLLSGKKF HNDLKTNKCL AIFAPLEGGY ETRLLRRMRA KGFKTFITSA RGLGDPEVFL
LKLHGVRPPH LGHQSVGRNG ALGEVQQVIP QASELFNEND KNKLLWLLEG QVLSQSELES
LIEICTNDNK LTIVVEMGGS RKLEWKPLSN YILDEFES
