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NDHJ_TRIV2
ID   NDHJ_TRIV2              Reviewed;         175 AA.
AC   Q9XBL6; Q3MC04;
DT   27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT   04-APR-2006, sequence version 4.
DT   25-MAY-2022, entry version 110.
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=Ava_1860;
OS   Trichormus variabilis (strain ATCC 29413 / PCC 7937) (Anabaena variabilis).
OC   Bacteria; Cyanobacteria; Nostocales; Nostocaceae; Trichormus.
OX   NCBI_TaxID=240292;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Happe T., Schiefer W., Boehme H.;
RT   "Isolation and characterisation of the ndhCKJ gene-cluster of Anabaena
RT   variabilis.";
RL   Submitted (OCT-1998) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29413 / PCC 7937;
RX   PubMed=25197444; DOI=10.4056/sigs.3899418;
RA   Thiel T., Pratte B.S., Zhong J., Goodwin L., Copeland A., Lucas S., Han C.,
RA   Pitluck S., Land M.L., Kyrpides N.C., Woyke T.;
RT   "Complete genome sequence of Anabaena variabilis ATCC 29413.";
RL   Stand. Genomic Sci. 9:562-573(2014).
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}.
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DR   EMBL; AJ012181; CAB45648.1; -; Genomic_DNA.
DR   EMBL; CP000117; ABA21482.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q9XBL6; -.
DR   SMR; Q9XBL6; -.
DR   STRING; 240292.Ava_1860; -.
DR   EnsemblBacteria; ABA21482; ABA21482; Ava_1860.
DR   KEGG; ava:Ava_1860; -.
DR   eggNOG; COG0852; Bacteria.
DR   HOGENOM; CLU_042628_9_1_3; -.
DR   OMA; YELQDAY; -.
DR   Proteomes; UP000002533; 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   PROSITE; PS00542; COMPLEX1_30K; 1.
PE   3: Inferred from homology;
KW   Membrane; NAD; NADP; Plastoquinone; Quinone; Thylakoid; Translocase;
KW   Transport.
FT   CHAIN           1..175
FT                   /note="NAD(P)H-quinone oxidoreductase subunit J"
FT                   /id="PRO_0000118666"
FT   CONFLICT        49
FT                   /note="E -> D (in Ref. 1; CAB45648)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        72..73
FT                   /note="GG -> RR (in Ref. 1; CAB45648)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        77
FT                   /note="G -> R (in Ref. 1; CAB45648)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        101
FT                   /note="V -> I (in Ref. 1; CAB45648)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        121
FT                   /note="W -> G (in Ref. 1; CAB45648)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        130
FT                   /note="E -> G (in Ref. 1; CAB45648)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        135
FT                   /note="F -> V (in Ref. 1; CAB45648)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        150
FT                   /note="M -> I (in Ref. 1; CAB45648)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   175 AA;  19920 MW;  7543107ACCF6C46F CRC64;
     MADEELKPVP AAAEAIVPSG PTSQWLTENG FAHESLAADK NGVEIIKVEP DFLLPIATAL
     YAYGFNYLQF QGGIDLGPGQ DLVSVYHLVK VSDNADKPEE VRVKVFLPRE NPVVPSVYWI
     WKTADWQERE SYDMFGIIYE GHPNLKRILM PEDWVGWPLR KDYISPDFYE LQDAY
 
 
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