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 27-MAR-2024, entry version 115.
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; Cyanobacteriota; Cyanophyceae; Nostocales; Nostocaceae;
OC 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 KEGG; ava:Ava_1860; -.
DR eggNOG; COG0852; Bacteria.
DR HOGENOM; CLU_042628_9_1_3; -.
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; NADH:ubiquinone oxidoreductase, 30kDa subunit; 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 PANTHER; PTHR10884:SF14; NADH DEHYDROGENASE [UBIQUINONE] IRON-SULFUR PROTEIN 3, MITOCHONDRIAL; 1.
DR PANTHER; PTHR10884; NADH DEHYDROGENASE UBIQUINONE IRON-SULFUR PROTEIN 3; 1.
DR Pfam; PF00329; Complex1_30kDa; 1.
DR SUPFAM; SSF143243; Nqo5-like; 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
//
