NDHJ_THEVB
ID NDHJ_THEVB Reviewed; 168 AA.
AC Q8DJ01;
DT 16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 102.
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=tlr1430;
OS Thermosynechococcus vestitus (strain NIES-2133 / IAM M-273 / BP-1).
OC Bacteria; Cyanobacteria; Pseudanabaenales; Thermosynechococcaceae;
OC Thermosynechococcus.
OX NCBI_TaxID=197221;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIES-2133 / IAM M-273 / BP-1;
RX PubMed=12240834; DOI=10.1093/dnares/9.4.123;
RA Nakamura Y., Kaneko T., Sato S., Ikeuchi M., Katoh H., Sasamoto S.,
RA Watanabe A., Iriguchi M., Kawashima K., Kimura T., Kishida Y., Kiyokawa C.,
RA Kohara M., Matsumoto M., Matsuno A., Nakazaki N., Shimpo S., Sugimoto M.,
RA Takeuchi C., Yamada M., Tabata S.;
RT "Complete genome structure of the thermophilic cyanobacterium
RT Thermosynechococcus elongatus BP-1.";
RL DNA Res. 9:123-130(2002).
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; BA000039; BAC08982.1; -; Genomic_DNA.
DR RefSeq; NP_682220.1; NC_004113.1.
DR RefSeq; WP_011057270.1; NC_004113.1.
DR PDB; 6HUM; EM; 3.34 A; J=1-168.
DR PDB; 6KHI; EM; 3.00 A; J=1-168.
DR PDB; 6KHJ; EM; 3.00 A; J=1-168.
DR PDB; 6L7O; EM; 3.20 A; J=1-168.
DR PDB; 6L7P; EM; 3.60 A; J=1-168.
DR PDB; 6NBQ; EM; 3.10 A; J=1-168.
DR PDB; 6NBX; EM; 3.50 A; J=1-168.
DR PDB; 6NBY; EM; 3.10 A; J=1-168.
DR PDB; 6TJV; EM; 3.20 A; J=1-168.
DR PDBsum; 6HUM; -.
DR PDBsum; 6KHI; -.
DR PDBsum; 6KHJ; -.
DR PDBsum; 6L7O; -.
DR PDBsum; 6L7P; -.
DR PDBsum; 6NBQ; -.
DR PDBsum; 6NBX; -.
DR PDBsum; 6NBY; -.
DR PDBsum; 6TJV; -.
DR AlphaFoldDB; Q8DJ01; -.
DR SMR; Q8DJ01; -.
DR IntAct; Q8DJ01; 1.
DR STRING; 197221.22295154; -.
DR TCDB; 3.D.1.8.2; the h(+) or na(+)-translocating nadh dehydrogenase (ndh) family.
DR EnsemblBacteria; BAC08982; BAC08982; BAC08982.
DR KEGG; tel:tlr1430; -.
DR PATRIC; fig|197221.4.peg.1501; -.
DR eggNOG; COG0852; Bacteria.
DR OMA; YELQDAY; -.
DR OrthoDB; 1735902at2; -.
DR Proteomes; UP000000440; 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 1: Evidence at protein level;
KW 3D-structure; Membrane; NAD; NADP; Plastoquinone; Quinone;
KW Reference proteome; Thylakoid; Translocase; Transport.
FT CHAIN 1..168
FT /note="NAD(P)H-quinone oxidoreductase subunit J"
FT /id="PRO_0000358204"
FT TURN 14..23
FT /evidence="ECO:0007829|PDB:6KHI"
FT STRAND 27..31
FT /evidence="ECO:0007829|PDB:6NBQ"
FT STRAND 33..35
FT /evidence="ECO:0007829|PDB:6KHI"
FT STRAND 37..41
FT /evidence="ECO:0007829|PDB:6KHI"
FT STRAND 43..45
FT /evidence="ECO:0007829|PDB:6KHI"
FT HELIX 46..54
FT /evidence="ECO:0007829|PDB:6KHI"
FT TURN 55..57
FT /evidence="ECO:0007829|PDB:6KHI"
FT STRAND 60..62
FT /evidence="ECO:0007829|PDB:6KHI"
FT STRAND 66..68
FT /evidence="ECO:0007829|PDB:6TJV"
FT STRAND 69..73
FT /evidence="ECO:0007829|PDB:6KHJ"
FT STRAND 80..82
FT /evidence="ECO:0007829|PDB:6KHI"
FT STRAND 93..100
FT /evidence="ECO:0007829|PDB:6KHI"
FT STRAND 102..104
FT /evidence="ECO:0007829|PDB:6KHI"
FT STRAND 106..108
FT /evidence="ECO:0007829|PDB:6KHJ"
FT TURN 111..113
FT /evidence="ECO:0007829|PDB:6KHI"
FT TURN 115..118
FT /evidence="ECO:0007829|PDB:6KHI"
FT HELIX 119..128
FT /evidence="ECO:0007829|PDB:6KHI"
FT STRAND 131..134
FT /evidence="ECO:0007829|PDB:6KHJ"
FT STRAND 141..143
FT /evidence="ECO:0007829|PDB:6KHI"
FT STRAND 153..155
FT /evidence="ECO:0007829|PDB:6L7O"
FT HELIX 162..164
FT /evidence="ECO:0007829|PDB:6KHI"
SQ SEQUENCE 168 AA; 19344 MW; 618C5809ABE6312C CRC64;
MSDTPEAPIV EAGPVGRLLQ SQNLSVESLG RDASGVEMIK VDRDRLLAVC QTLYADGFNY
LRCQAAYDSG PGQDLVSTYH LIKLSDNADR PPEVRIKVFV PRDDPRVPSV YWIWKTADWQ
ERESYDMFGI VYEGHPNLKR ILMPEDWVGW PLRKDYITPD FYELQEAY
