ID NDHK_PROM3 Reviewed; 250 AA. AC A2CCP6; DT 16-DEC-2008, integrated into UniProtKB/Swiss-Prot. DT 20-FEB-2007, sequence version 1. DT 27-MAR-2024, entry version 95. 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}; GN OrderedLocusNames=P9303_25251; OS Prochlorococcus marinus (strain MIT 9303). OC Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales; OC Prochlorococcaceae; Prochlorococcus. OX NCBI_TaxID=59922; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MIT 9303; RX PubMed=18159947; DOI=10.1371/journal.pgen.0030231; RA Kettler G.C., Martiny A.C., Huang K., Zucker J., Coleman M.L., Rodrigue S., RA Chen F., Lapidus A., Ferriera S., Johnson J., Steglich C., Church G.M., RA Richardson P., Chisholm S.W.; RT "Patterns and implications of gene gain and loss in the evolution of RT Prochlorococcus."; RL PLoS Genet. 3:2515-2528(2007). 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CP000554; ABM79256.1; -; Genomic_DNA. DR AlphaFoldDB; A2CCP6; -. DR SMR; A2CCP6; -. DR STRING; 59922.P9303_25251; -. DR KEGG; pmf:P9303_25251; -. DR HOGENOM; CLU_055737_2_0_3; -. DR BioCyc; PMAR59922:G1G80-2216-MONOMER; -. DR Proteomes; UP000002274; 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 Gene3D; 3.40.50.12280; -; 1. DR HAMAP; MF_01356; NDH1_NuoB; 1. DR InterPro; IPR006137; NADH_UbQ_OxRdtase-like_20kDa. DR InterPro; IPR006138; NADH_UQ_OxRdtase_20Kd_su. DR NCBIfam; TIGR01957; nuoB_fam; 1. DR PANTHER; PTHR11995; NADH DEHYDROGENASE; 1. DR PANTHER; PTHR11995:SF14; NADH DEHYDROGENASE [UBIQUINONE] IRON-SULFUR PROTEIN 7, MITOCHONDRIAL; 1. DR Pfam; PF01058; Oxidored_q6; 1. DR SUPFAM; SSF56770; HydA/Nqo6-like; 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; Thylakoid; Translocase; Transport. FT CHAIN 1..250 FT /note="NAD(P)H-quinone oxidoreductase subunit K" FT /id="PRO_0000358453" FT REGION 230..250 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 235..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; 26879 MW; 37A2BD06379B2017 CRC64; MSVTPSIDAV RDLRAASCGP VGAPSVTSEL SENIILTSLD DLHNWARLSS LWPLLYGTAC CFIEFAALIG SRFDFDRFGL VPRSSPRQAD LLIVAGTVTM KMAPALVRLY EQMPEPKYVI AMGACTITGG MFSADSTTAV RGVDKLIPVD LYLPGCPPRP EAIFDAVIKL RKKVGDESVS ERIKIAQTHR YFTVPHQMKR VEPIVTGAYL SADTQKAALS PGAGLPMAAE LNTSEIDASP ASQPSSTYES //