NDHJ_NOSS1
ID NDHJ_NOSS1 Reviewed; 175 AA.
AC Q44241; Q9WWN0;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2002, sequence version 3.
DT 25-MAY-2022, entry version 118.
DE RecName: Full=NAD(P)H-quinone oxidoreductase subunit J {ECO:0000255|HAMAP-Rule:MF_01357};
DE EC=7.1.1.- {ECO:0000255|HAMAP-Rule:MF_01357};
DE AltName: Full=NAD(P)H dehydrogenase subunit J;
DE AltName: Full=NADH-plastoquinone oxidoreductase subunit J {ECO:0000255|HAMAP-Rule:MF_01357};
DE AltName: Full=NDH-1 subunit J {ECO:0000255|HAMAP-Rule:MF_01357};
DE Short=NDH-J {ECO:0000255|HAMAP-Rule:MF_01357};
GN Name=ndhJ {ECO:0000255|HAMAP-Rule:MF_01357}; OrderedLocusNames=all3840;
OS Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576).
OC Bacteria; Cyanobacteria; Nostocales; Nostocaceae; Nostoc.
OX NCBI_TaxID=103690;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Happe T., Schiefer W., Boehme H.;
RT "Isolation and characterisation of the ndhCKJ-cluster of the cyanobacteria
RT Anabaena sp. PCC 7120.";
RL Submitted (OCT-1998) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 7120 / SAG 25.82 / UTEX 2576;
RX PubMed=11759840; DOI=10.1093/dnares/8.5.205;
RA Kaneko T., Nakamura Y., Wolk C.P., Kuritz T., Sasamoto S., Watanabe A.,
RA Iriguchi M., Ishikawa A., Kawashima K., Kimura T., Kishida Y., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakazaki N., Shimpo S., Sugimoto M.,
RA Takazawa M., Yamada M., Yasuda M., Tabata S.;
RT "Complete genomic sequence of the filamentous nitrogen-fixing
RT cyanobacterium Anabaena sp. strain PCC 7120.";
RL DNA Res. 8:205-213(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-155.
RX PubMed=8797851; DOI=10.1111/j.1432-1033.1996.0173h.x;
RA Howitt C.A., Whelan J., Price G.D., Day D.A.;
RT "Cloning, analysis and inactivation of the ndhK gene encoding a subunit of
RT NADH quinone oxidoreductase from Anabaena PCC 7120.";
RL Eur. J. Biochem. 240:173-180(1996).
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_01357}.
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_01357};
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_01357};
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_01357}.
CC -!- SUBCELLULAR LOCATION: Cellular thylakoid membrane {ECO:0000255|HAMAP-
CC Rule:MF_01357}; Peripheral membrane protein {ECO:0000255|HAMAP-
CC Rule:MF_01357}; Cytoplasmic side {ECO:0000255|HAMAP-Rule:MF_01357}.
CC -!- SIMILARITY: Belongs to the complex I 30 kDa subunit family.
CC {ECO:0000255|HAMAP-Rule:MF_01357}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC44354.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AJ012180; CAB45641.1; -; Genomic_DNA.
DR EMBL; BA000019; BAB75539.1; -; Genomic_DNA.
DR EMBL; U31208; AAC44354.1; ALT_INIT; Genomic_DNA.
DR PIR; AI2285; AI2285.
DR PIR; S74217; S74217.
DR RefSeq; WP_010997981.1; NZ_RSCN01000011.1.
DR AlphaFoldDB; Q44241; -.
DR SMR; Q44241; -.
DR STRING; 103690.17132974; -.
DR EnsemblBacteria; BAB75539; BAB75539; BAB75539.
DR KEGG; ana:all3840; -.
DR eggNOG; COG0852; Bacteria.
DR OMA; YELQDAY; -.
DR OrthoDB; 1735902at2; -.
DR Proteomes; UP000002483; Chromosome.
DR GO; GO:0031676; C:plasma membrane-derived thylakoid membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0008137; F:NADH dehydrogenase (ubiquinone) activity; IEA:InterPro.
DR GO; GO:0048038; F:quinone binding; IEA:UniProtKB-KW.
DR GO; GO:0019684; P:photosynthesis, light reaction; IEA:UniProtKB-UniRule.
DR Gene3D; 3.30.460.80; -; 1.
DR HAMAP; MF_01357; NDH1_NuoC; 1.
DR InterPro; IPR010218; NADH_DH_suC.
DR InterPro; IPR037232; NADH_quin_OxRdtase_su_C/D-like.
DR InterPro; IPR001268; NADH_UbQ_OxRdtase_30kDa_su.
DR InterPro; IPR020396; NADH_UbQ_OxRdtase_CS.
DR Pfam; PF00329; Complex1_30kDa; 1.
DR SUPFAM; SSF143243; SSF143243; 1.
DR TIGRFAMs; TIGR01961; NuoC_fam; 1.
DR PROSITE; PS00542; COMPLEX1_30K; 1.
PE 3: Inferred from homology;
KW Membrane; NAD; NADP; Plastoquinone; Quinone; Reference proteome; Thylakoid;
KW Translocase; Transport.
FT CHAIN 1..175
FT /note="NAD(P)H-quinone oxidoreductase subunit J"
FT /id="PRO_0000118665"
FT CONFLICT 7
FT /note="Q -> K (in Ref. 3)"
FT /evidence="ECO:0000305"
FT CONFLICT 13..14
FT /note="EA -> AE (in Ref. 3)"
FT /evidence="ECO:0000305"
FT CONFLICT 50
FT /note="A -> P (in Ref. 3; AAC44354)"
FT /evidence="ECO:0000305"
FT CONFLICT 53
FT /note="L -> M (in Ref. 3; AAC44354)"
FT /evidence="ECO:0000305"
FT CONFLICT 74
FT /note="V -> I (in Ref. 3; AAC44354)"
FT /evidence="ECO:0000305"
FT CONFLICT 101
FT /note="I -> V (in Ref. 3; AAC44354)"
FT /evidence="ECO:0000305"
FT CONFLICT 152
FT /note="E -> G (in Ref. 3; AAC44354)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 175 AA; 19893 MW; FA257DBD9F76D3A4 CRC64;
MADEELQPVP AAEAAIVPSG PTSQWLTENG FAHESLAADK NGVEIIKVEA DFLLPIATAL
YAYGFNYLQF QGGVDLGPGQ DLVSVYHLVK VSDNADKPEE IRVKVFLPRE NPVVPSVYWI
WKTADWQERE SYDMFGIIYE GHPNLKRILM PEDWVGWPLR KDYISPDFYE LQDAY
