NDHK1_SYNY3
ID NDHK1_SYNY3 Reviewed; 248 AA.
AC P19050;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1990, sequence version 1.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=NAD(P)H-quinone oxidoreductase subunit K 1 {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 1 {ECO:0000255|HAMAP-Rule:MF_01356};
DE AltName: Full=NDH-1 subunit K 1 {ECO:0000255|HAMAP-Rule:MF_01356};
DE Short=NDH-K 1 {ECO:0000255|HAMAP-Rule:MF_01356};
DE Flags: Precursor;
GN Name=ndhK1 {ECO:0000255|HAMAP-Rule:MF_01356}; Synonyms=psbG;
GN OrderedLocusNames=slr1280;
OS Synechocystis sp. (strain PCC 6803 / Kazusa).
OC Bacteria; Cyanobacteria; Synechococcales; Merismopediaceae; Synechocystis;
OC unclassified Synechocystis.
OX NCBI_TaxID=1111708;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2499764; DOI=10.1007/bf00332231;
RA Steinmueller K., Ley A.C., Steinmetz A.A., Sayre R.T., Bogorad L.;
RT "Characterization of the ndhC-psbG-ORF157/159 operon of maize plastid DNA
RT and of the cyanobacterium Synechocystis sp. PCC6803.";
RL Mol. Gen. Genet. 216:60-69(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 6803 / Kazusa;
RX PubMed=8905231; DOI=10.1093/dnares/3.3.109;
RA Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y.,
RA Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T.,
RA Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S.,
RA Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence analysis of the genome of the unicellular cyanobacterium
RT Synechocystis sp. strain PCC6803. II. Sequence determination of the entire
RT genome and assignment of potential protein-coding regions.";
RL DNA Res. 3:109-136(1996).
RN [3]
RP PROTEIN SEQUENCE OF 2-10, CHARACTERIZATION AS A MEMBER OF THE
RP NAD(P)H-QUINONE OXIDOREDUCTASE COMPLEX, AND SUBCOMPLEXES OF NDH-1.
RX PubMed=15102833; DOI=10.1074/jbc.m401107200;
RA Prommeenate P., Lennon A.M., Markert C., Hippler M., Nixon P.J.;
RT "Subunit composition of NDH-1 complexes of Synechocystis sp. PCC 6803:
RT identification of two new ndh gene products with nuclear-encoded homologues
RT in the chloroplast Ndh complex.";
RL J. Biol. Chem. 279:28165-28173(2004).
RN [4]
RP PROTEIN SEQUENCE OF 2-8, AND CHARACTERIZATION AS A MEMBER OF THE
RP NAD(P)H-QUINONE OXIDOREDUCTASE COMPLEX.
RX PubMed=8325373; DOI=10.1016/0014-5793(93)81800-f;
RA Berger S., Ellersiek U., Kinzelt D., Steinmueller K.;
RT "Immunopurification of a subcomplex of the NAD(P)H-plastoquinone-
RT oxidoreductase from the cyanobacterium Synechocystis sp. PCC6803.";
RL FEBS Lett. 326:246-250(1993).
RN [5]
RP PROTEIN SEQUENCE OF 90-119, CHARACTERIZATION AS A MEMBER OF THE
RP NAD(P)H-QUINONE OXIDOREDUCTASE COMPLEX, AND SUBCOMPLEXES OF NDH-1.
RX PubMed=15548534; DOI=10.1074/jbc.m410914200;
RA Battchikova N., Zhang P., Rudd S., Ogawa T., Aro E.-M.;
RT "Identification of NdhL and Ssl1690 (NdhO) in NDH-1L and NDH-1M complexes
RT of Synechocystis sp. PCC 6803.";
RL J. Biol. Chem. 280:2587-2595(2005).
RN [6]
RP SUBCELLULAR LOCATION IN THYLAKOID.
RX PubMed=16287171; DOI=10.1002/pmic.200500111;
RA Srivastava R., Pisareva T., Norling B.;
RT "Proteomic studies of the thylakoid membrane of Synechocystis sp. PCC
RT 6803.";
RL Proteomics 5:4905-4916(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.
CC -!- SUBCELLULAR LOCATION: Cellular thylakoid membrane
CC {ECO:0000305|PubMed:16287171}; Peripheral membrane protein
CC {ECO:0000305|PubMed:16287171}; Cytoplasmic side
CC {ECO:0000305|PubMed:16287171}.
CC -!- SIMILARITY: Belongs to the complex I 20 kDa subunit family.
CC {ECO:0000255|HAMAP-Rule:MF_01356}.
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DR EMBL; X17439; CAA35485.1; -; Genomic_DNA.
DR EMBL; BA000022; BAA18284.1; -; Genomic_DNA.
DR PIR; S04437; S04437.
DR AlphaFoldDB; P19050; -.
DR SMR; P19050; -.
DR IntAct; P19050; 7.
DR STRING; 1148.1653370; -.
DR PaxDb; P19050; -.
DR EnsemblBacteria; BAA18284; BAA18284; BAA18284.
DR KEGG; syn:slr1280; -.
DR eggNOG; COG0377; Bacteria.
DR InParanoid; P19050; -.
DR OMA; TMKMAPQ; -.
DR PhylomeDB; P19050; -.
DR Proteomes; UP000001425; Chromosome.
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 1: Evidence at protein level;
KW 4Fe-4S; Direct protein sequencing; Iron; Iron-sulfur; Membrane;
KW Metal-binding; NAD; NADP; Plastoquinone; Quinone; Reference proteome;
KW Thylakoid; Translocase; Transport.
FT PROPEP 1..2
FT /id="PRO_0000358500"
FT CHAIN 3..248
FT /note="NAD(P)H-quinone oxidoreductase subunit K 1"
FT /id="PRO_0000118760"
FT REGION 228..248
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 234..248
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 62
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01356"
FT BINDING 63
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01356"
FT BINDING 127
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01356"
FT BINDING 158
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01356"
SQ SEQUENCE 248 AA; 27346 MW; FF68BEA64B92F6E7 CRC64;
MSPNPANPTD LERVATAKIL NPASRSQVTQ DLSENVILTT VDDLYNWAKL SSLWPLLYGT
ACCFIEFAAL IGSRFDFDRF GLVPRSSPRQ ADLIITAGTI TMKMAPALVR LYEEMPEPKY
VIAMGACTIT GGMFSSDSTT AVRGVDKLIP VDVYIPGCPP RPEAIFDAII KLRKKVANES
IQERAITQQT HRYYSTSHQM KVVAPILDGK YLQQGTRSAP PRELQEAMGM PVPPALTTSQ
QKEQLNRG
