NDHK_THEVB
ID NDHK_THEVB Reviewed; 237 AA.
AC Q8DKZ4;
DT 16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 105.
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=tlr0705;
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).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY, CHARACTERIZATION AS A MEMBER OF THE
RP NAD(P)H-QUINONE OXIDOREDUCTASE COMPLEX, AND SUBCOMPLEXES OF NDH-1.
RX PubMed=15910282; DOI=10.1042/bj20050390;
RA Zhang P., Battchikova N., Paakkarinen V., Katoh H., Iwai M., Ikeuchi M.,
RA Pakrasi H.B., Ogawa T., Aro E.-M.;
RT "Isolation, subunit composition and interaction of the NDH-1 complexes from
RT Thermosynechococcus elongatus BP-1.";
RL Biochem. J. 390:513-520(2005).
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; BA000039; BAC08256.1; -; Genomic_DNA.
DR RefSeq; NP_681494.1; NC_004113.1.
DR RefSeq; WP_011056552.1; NC_004113.1.
DR PDB; 6HUM; EM; 3.34 A; K=1-237.
DR PDB; 6KHI; EM; 3.00 A; K=1-237.
DR PDB; 6KHJ; EM; 3.00 A; K=1-237.
DR PDB; 6L7O; EM; 3.20 A; K=1-237.
DR PDB; 6L7P; EM; 3.60 A; K=1-237.
DR PDB; 6NBQ; EM; 3.10 A; K=1-237.
DR PDB; 6NBX; EM; 3.50 A; K=1-237.
DR PDB; 6NBY; EM; 3.10 A; K=1-237.
DR PDB; 6TJV; EM; 3.20 A; K=1-237.
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; Q8DKZ4; -.
DR SMR; Q8DKZ4; -.
DR IntAct; Q8DKZ4; 1.
DR STRING; 197221.22294426; -.
DR TCDB; 3.D.1.8.2; the h(+) or na(+)-translocating nadh dehydrogenase (ndh) family.
DR EnsemblBacteria; BAC08256; BAC08256; BAC08256.
DR KEGG; tel:tlr0705; -.
DR PATRIC; fig|197221.4.peg.745; -.
DR eggNOG; COG0377; Bacteria.
DR OMA; TMKMAPQ; -.
DR OrthoDB; 1904620at2; -.
DR Proteomes; UP000000440; 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 1: Evidence at protein level;
KW 3D-structure; 4Fe-4S; Iron; Iron-sulfur; Membrane; Metal-binding; NAD;
KW NADP; Plastoquinone; Quinone; Reference proteome; Thylakoid; Translocase;
KW Transport.
FT CHAIN 1..237
FT /note="NAD(P)H-quinone oxidoreductase subunit K"
FT /id="PRO_0000358489"
FT BINDING 52
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01356"
FT BINDING 53
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01356"
FT BINDING 117
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01356"
FT BINDING 148
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01356"
FT STRAND 8..11
FT /evidence="ECO:0007829|PDB:6KHI"
FT HELIX 26..40
FT /evidence="ECO:0007829|PDB:6KHI"
FT STRAND 45..47
FT /evidence="ECO:0007829|PDB:6L7O"
FT STRAND 49..51
FT /evidence="ECO:0007829|PDB:6HUM"
FT HELIX 53..61
FT /evidence="ECO:0007829|PDB:6KHI"
FT STRAND 62..65
FT /evidence="ECO:0007829|PDB:6KHI"
FT HELIX 68..70
FT /evidence="ECO:0007829|PDB:6KHI"
FT STRAND 75..77
FT /evidence="ECO:0007829|PDB:6KHI"
FT HELIX 78..80
FT /evidence="ECO:0007829|PDB:6KHI"
FT STRAND 82..86
FT /evidence="ECO:0007829|PDB:6KHI"
FT HELIX 94..103
FT /evidence="ECO:0007829|PDB:6KHI"
FT STRAND 110..115
FT /evidence="ECO:0007829|PDB:6KHI"
FT HELIX 116..119
FT /evidence="ECO:0007829|PDB:6KHI"
FT HELIX 122..124
FT /evidence="ECO:0007829|PDB:6KHI"
FT STRAND 125..127
FT /evidence="ECO:0007829|PDB:6KHI"
FT STRAND 129..131
FT /evidence="ECO:0007829|PDB:6KHI"
FT HELIX 135..137
FT /evidence="ECO:0007829|PDB:6KHI"
FT STRAND 142..145
FT /evidence="ECO:0007829|PDB:6KHI"
FT STRAND 147..149
FT /evidence="ECO:0007829|PDB:6KHJ"
FT HELIX 152..166
FT /evidence="ECO:0007829|PDB:6KHI"
FT TURN 172..175
FT /evidence="ECO:0007829|PDB:6KHI"
FT STRAND 176..178
FT /evidence="ECO:0007829|PDB:6KHI"
FT STRAND 183..187
FT /evidence="ECO:0007829|PDB:6NBQ"
FT STRAND 201..204
FT /evidence="ECO:0007829|PDB:6KHI"
FT STRAND 207..209
FT /evidence="ECO:0007829|PDB:6NBQ"
FT TURN 212..216
FT /evidence="ECO:0007829|PDB:6NBQ"
SQ SEQUENCE 237 AA; 25742 MW; F25839B9F65C06CE CRC64;
MTNTTSPAIL NPIARPEVPQ ELAENIILTS LNDVYDWARL SSLWPLMYGT ACCFIEFAAM
IGSRFDFDRF GLVPRNSPRQ ADLIITSGTI TMKMAPALVR LYEQMPSPKY VIAMGACTIT
GGMFSSDSYS AVRGVDKLIP VDVYLPGCPP RPEAIMDAIV KLRKKIANEH INERGNLAQT
HRLFTAKHKM KPVPPILTGQ YLNAPSRQAP PPALAAAMGI AVPALGEAVS ETTSVAE
