NDHK_NOSS1
ID NDHK_NOSS1 Reviewed; 245 AA.
AC Q44240; Q9R6Y5;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2002, sequence version 2.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=NAD(P)H-quinone oxidoreductase subunit K {ECO:0000255|HAMAP-Rule:MF_01356};
DE EC=7.1.1.- {ECO:0000255|HAMAP-Rule:MF_01356};
DE AltName: Full=NAD(P)H dehydrogenase I subunit K {ECO:0000255|HAMAP-Rule:MF_01356};
DE AltName: Full=NDH-1 subunit K {ECO:0000255|HAMAP-Rule:MF_01356};
DE Short=NDH-K {ECO:0000255|HAMAP-Rule:MF_01356};
GN Name=ndhK {ECO:0000255|HAMAP-Rule:MF_01356}; OrderedLocusNames=all3841;
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].
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).
RN [2]
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 [3]
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).
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_01356}.
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_01356};
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_01356};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01356};
CC Note=Binds 1 [4Fe-4S] cluster. {ECO:0000255|HAMAP-Rule:MF_01356};
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_01356}.
CC -!- SUBCELLULAR LOCATION: Cellular thylakoid membrane {ECO:0000255|HAMAP-
CC Rule:MF_01356}; Peripheral membrane protein {ECO:0000255|HAMAP-
CC Rule:MF_01356}; Cytoplasmic side {ECO:0000255|HAMAP-Rule:MF_01356}.
CC -!- SIMILARITY: Belongs to the complex I 20 kDa subunit family.
CC {ECO:0000255|HAMAP-Rule:MF_01356}.
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DR EMBL; U31208; AAC44353.1; -; Genomic_DNA.
DR EMBL; AJ012180; CAB45640.1; -; Genomic_DNA.
DR EMBL; BA000019; BAB75540.1; -; Genomic_DNA.
DR PIR; AB2286; AB2286.
DR PIR; S74216; S74216.
DR RefSeq; WP_010997982.1; NZ_RSCN01000011.1.
DR AlphaFoldDB; Q44240; -.
DR SMR; Q44240; -.
DR STRING; 103690.17132975; -.
DR EnsemblBacteria; BAB75540; BAB75540; BAB75540.
DR KEGG; ana:all3841; -.
DR eggNOG; COG0377; Bacteria.
DR OMA; TMKMAPQ; -.
DR OrthoDB; 1904620at2; -.
DR Proteomes; UP000002483; Chromosome.
DR GO; GO:0031676; C:plasma membrane-derived thylakoid membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-UniRule.
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 HAMAP; MF_01356; NDH1_NuoB; 1.
DR InterPro; IPR006137; NADH_UbQ_OxRdtase-like_20kDa.
DR InterPro; IPR006138; NADH_UQ_OxRdtase_20Kd_su.
DR Pfam; PF01058; Oxidored_q6; 1.
DR TIGRFAMs; TIGR01957; nuoB_fam; 1.
DR PROSITE; PS01150; COMPLEX1_20K; 1.
PE 3: Inferred from homology;
KW 4Fe-4S; Iron; Iron-sulfur; Membrane; Metal-binding; NAD; NADP;
KW Plastoquinone; Quinone; Reference proteome; Thylakoid; Translocase;
KW Transport.
FT CHAIN 1..245
FT /note="NAD(P)H-quinone oxidoreductase subunit K"
FT /id="PRO_0000118758"
FT BINDING 58
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01356"
FT BINDING 59
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01356"
FT BINDING 123
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01356"
FT BINDING 154
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01356"
FT CONFLICT 12
FT /note="K -> I (in Ref. 1; AAC44353)"
FT /evidence="ECO:0000305"
FT CONFLICT 24
FT /note="I -> V (in Ref. 1; AAC44353)"
FT /evidence="ECO:0000305"
FT CONFLICT 104
FT /note="L -> M (in Ref. 1; AAC44353)"
FT /evidence="ECO:0000305"
FT CONFLICT 110
FT /note="Q -> K (in Ref. 1; AAC44353)"
FT /evidence="ECO:0000305"
FT CONFLICT 133
FT /note="D -> E (in Ref. 1; AAC44353)"
FT /evidence="ECO:0000305"
FT CONFLICT 165
FT /note="I -> M (in Ref. 1 and 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 200..201
FT /note="PD -> AE (in Ref. 1 and 2)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 245 AA; 27493 MW; AAD00A315C7A7CC0 CRC64;
MVLNSDLTTQ DKERIINPIE RPTITQDLSE NVILTTVDDL YNWARLSSLW PLLFGTACCF
IEFAALIGSR FDFDRFGLIP RSSPRQADLI ITAGTITMKM APQLVRLYEQ MPEPKYVIAM
GACTITGGMF SVDSPTAVRG VDKLIPVDVY LPGCPPRPEA IIDAIIKLRK KIANDSMQER
SLIRQTHRFY STTHNLKPVP DILTGKYMQS ETRFNPPKEL TEAIGLPVPP ALLTSQTQKE
EQKRG
