NDHK_PROMM
ID NDHK_PROMM Reviewed; 250 AA.
AC Q7V4Q5;
DT 16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 103.
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=PMT_1892;
OS Prochlorococcus marinus (strain MIT 9313).
OC Bacteria; Cyanobacteria; Synechococcales; Prochlorococcaceae;
OC Prochlorococcus.
OX NCBI_TaxID=74547;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MIT 9313;
RX PubMed=12917642; DOI=10.1038/nature01947;
RA Rocap G., Larimer F.W., Lamerdin J.E., Malfatti S., Chain P., Ahlgren N.A.,
RA Arellano A., Coleman M., Hauser L., Hess W.R., Johnson Z.I., Land M.L.,
RA Lindell D., Post A.F., Regala W., Shah M., Shaw S.L., Steglich C.,
RA Sullivan M.B., Ting C.S., Tolonen A., Webb E.A., Zinser E.R.,
RA Chisholm S.W.;
RT "Genome divergence in two Prochlorococcus ecotypes reflects oceanic niche
RT differentiation.";
RL Nature 424:1042-1047(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. {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; BX548175; CAE22067.1; -; Genomic_DNA.
DR RefSeq; WP_011131258.1; NC_005071.1.
DR AlphaFoldDB; Q7V4Q5; -.
DR SMR; Q7V4Q5; -.
DR STRING; 74547.PMT_1892; -.
DR EnsemblBacteria; CAE22067; CAE22067; PMT_1892.
DR KEGG; pmt:PMT_1892; -.
DR eggNOG; COG0377; Bacteria.
DR HOGENOM; CLU_055737_2_0_3; -.
DR OMA; TMKMAPQ; -.
DR OrthoDB; 1904620at2; -.
DR Proteomes; UP000001423; 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..250
FT /note="NAD(P)H-quinone oxidoreductase subunit K"
FT /id="PRO_0000358455"
FT REGION 230..250
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 236..250
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 60
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01356"
FT BINDING 61
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01356"
FT BINDING 125
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01356"
FT BINDING 156
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01356"
SQ SEQUENCE 250 AA; 26927 MW; 0CFEFA3D9B181E23 CRC64;
MSVTPSIDAV RDLRAASCGP VGAPSVTSDL SENIILTSLD DLHNWARLSS LWPLLYGTAC
CFIEFAALIG SRFDFDRFGL VPRSSPRQAD LLIVAGTVTM KMAPALVRLY EQMPEPKYVI
AMGACTITGG MFSADSTTAV RGVDKLIPVD LYLPGCPPRP EAIFDAVIKL RKKVGDESVA
ERIKIAQTHR YFTVPHHMKR VEPIVTGAYL SADTQKAALK PGAGLPMAAE LNTPEIDVSP
ASQSSSTYES
