NDHK2_SYNY3
ID NDHK2_SYNY3 Reviewed; 219 AA.
AC P17062; Q6ZE61;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1990, sequence version 1.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=NAD(P)H-quinone oxidoreductase subunit K 2 {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 2 {ECO:0000255|HAMAP-Rule:MF_01356};
DE AltName: Full=NDH-1 subunit K 2 {ECO:0000255|HAMAP-Rule:MF_01356};
DE Short=NDH-K 2 {ECO:0000255|HAMAP-Rule:MF_01356};
GN Name=ndhK2 {ECO:0000255|HAMAP-Rule:MF_01356}; Synonyms=psbG2;
GN OrderedLocusNames=sll8031;
OS Synechocystis sp. (strain PCC 6803 / Kazusa).
OG Plasmid pSYSG.
OC Bacteria; Cyanobacteria; Synechococcales; Merismopediaceae; Synechocystis;
OC unclassified Synechocystis.
OX NCBI_TaxID=1111708;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2108054; DOI=10.1016/0014-5793(90)80151-8;
RA Mayes S.R., Cook K.M., Barber J.;
RT "Nucleotide sequence of the second psbG gene in Synechocystis 6803.
RT Possible implications for psbG function as a NAD(P)H dehydrogenase subunit
RT gene.";
RL FEBS Lett. 262:49-54(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 6803 / Kazusa;
RX PubMed=14686584; DOI=10.1093/dnares/10.5.221;
RA Kaneko T., Nakamura Y., Sasamoto S., Watanabe A., Kohara M., Matsumoto M.,
RA Shimpo S., Yamada M., Tabata S.;
RT "Structural analysis of four large plasmids harboring in a unicellular
RT cyanobacterium, Synechocystis sp. PCC 6803.";
RL DNA Res. 10:221-228(2003).
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.
CC -!- SUBCELLULAR LOCATION: Cellular thylakoid membrane {ECO:0000305};
CC Peripheral membrane protein {ECO:0000305}; Cytoplasmic side
CC {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the complex I 20 kDa subunit family.
CC {ECO:0000255|HAMAP-Rule:MF_01356}.
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DR EMBL; X17359; CAA35236.1; -; Genomic_DNA.
DR EMBL; AP004312; BAD02039.1; -; Genomic_DNA.
DR PIR; S09199; F2YBG2.
DR AlphaFoldDB; P17062; -.
DR SMR; P17062; -.
DR EnsemblBacteria; BAD02039; BAD02039; BAD02039.
DR KEGG; syn:sll8031; -.
DR InParanoid; P17062; -.
DR OMA; TACCFME; -.
DR PhylomeDB; P17062; -.
DR Proteomes; UP000001425; Plasmid pSYSG.
DR GO; GO:0045272; C:plasma membrane respiratory chain complex I; IBA:GO_Central.
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; IBA:GO_Central.
DR GO; GO:0048038; F:quinone binding; IEA:UniProtKB-KW.
DR GO; GO:0009060; P:aerobic respiration; IBA:GO_Central.
DR GO; GO:0015990; P:electron transport coupled proton transport; IBA:GO_Central.
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; Plasmid;
KW Plastoquinone; Quinone; Reference proteome; Thylakoid; Translocase;
KW Transport.
FT CHAIN 1..219
FT /note="NAD(P)H-quinone oxidoreductase subunit K 2"
FT /id="PRO_0000118761"
FT BINDING 53
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01356"
FT BINDING 54
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01356"
FT BINDING 118
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01356"
FT BINDING 149
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01356"
SQ SEQUENCE 219 AA; 24541 MW; 97E469317E971436 CRC64;
MSTSTHALTL QNPIQAPQVT KELSENVILT CLDDIYNWAR LSTLYPMMFG TACCFMEFMA
AFGPRFDLER FGSIPRATPR QADLMITAGT ITMKYAPALV QLYEQIPEPK YVIAMGACTI
TAGMFSADSP TAVRGVDKLI PVDVYIPGCP PRPEAVIDGI IKLRKKVAGE SRQDYTEDLQ
THRFHAVRHR MKPVSPILTG QYLRHHEDLT PHHDPLLIK
