ID A0A1Z4QAH8_9CYAN Unreviewed; 231 AA. AC A0A1Z4QAH8; DT 27-SEP-2017, integrated into UniProtKB/TrEMBL. DT 27-SEP-2017, sequence version 1. DT 07-APR-2021, entry version 13. DE RecName: Full=NAD(P)H-quinone oxidoreductase subunit K {ECO:0000256|HAMAP-Rule:MF_01356}; DE EC=7.1.1.- {ECO:0000256|HAMAP-Rule:MF_01356}; DE AltName: Full=NAD(P)H dehydrogenase I subunit K {ECO:0000256|HAMAP-Rule:MF_01356}; DE AltName: Full=NDH-1 subunit K {ECO:0000256|HAMAP-Rule:MF_01356}; DE Short=NDH-K {ECO:0000256|HAMAP-Rule:MF_01356}; GN Name=ndhK {ECO:0000256|HAMAP-Rule:MF_01356}; GN ORFNames=NIES4073_81290 {ECO:0000313|EMBL:BAZ27212.1}; OS Scytonema sp. NIES-4073. OC Bacteria; Cyanobacteria; Nostocales; Scytonemataceae; Scytonema; OC unclassified Scytonema. OX NCBI_TaxID=2005464 {ECO:0000313|EMBL:BAZ27212.1, ECO:0000313|Proteomes:UP000218871}; RN [1] {ECO:0000313|EMBL:BAZ27212.1, ECO:0000313|Proteomes:UP000218871} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NIES-4073 {ECO:0000313|EMBL:BAZ27212.1, RC ECO:0000313|Proteomes:UP000218871}; RA Hirose Y., Shimura Y., Fujisawa T., Nakamura Y., Kawachi M.; RT "Genome sequencing of cyanobaciteial culture collection at National RT Institute for Environmental Studies (NIES)."; RL Submitted (JUN-2017) to the EMBL/GenBank/DDBJ databases. 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:0000256|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:0000256|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:0000256|HAMAP-Rule:MF_01356}; CC -!- COFACTOR: CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; CC Evidence={ECO:0000256|HAMAP-Rule:MF_01356}; CC Note=Binds 1 [4Fe-4S] cluster. {ECO:0000256|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:0000256|HAMAP- CC Rule:MF_01356}. CC -!- SUBCELLULAR LOCATION: Cellular thylakoid membrane {ECO:0000256|HAMAP- CC Rule:MF_01356}; Peripheral membrane protein {ECO:0000256|HAMAP- CC Rule:MF_01356}; Cytoplasmic side {ECO:0000256|HAMAP-Rule:MF_01356}. CC -!- SIMILARITY: Belongs to the complex I 20 kDa subunit family. CC {ECO:0000256|HAMAP-Rule:MF_01356, ECO:0000256|RuleBase:RU004464}. 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; AP018268; BAZ27212.1; -; Genomic_DNA. DR EnsemblBacteria; BAZ27212; BAZ27212; NIES4073_81290. DR Proteomes; UP000218871; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. 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 {ECO:0000256|HAMAP-Rule:MF_01356, ECO:0000256|RuleBase:RU004464}; KW Iron {ECO:0000256|HAMAP-Rule:MF_01356, ECO:0000256|RuleBase:RU004464}; KW Iron-sulfur {ECO:0000256|HAMAP-Rule:MF_01356, KW ECO:0000256|RuleBase:RU004464}; KW Membrane {ECO:0000256|HAMAP-Rule:MF_01356, ECO:0000256|SAM:Phobius}; KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_01356, KW ECO:0000256|RuleBase:RU004464}; KW NAD {ECO:0000256|HAMAP-Rule:MF_01356, ECO:0000256|RuleBase:RU004464}; KW NADP {ECO:0000256|HAMAP-Rule:MF_01356}; KW Plastoquinone {ECO:0000256|HAMAP-Rule:MF_01356}; KW Quinone {ECO:0000256|HAMAP-Rule:MF_01356}; KW Thylakoid {ECO:0000256|HAMAP-Rule:MF_01356}; KW Translocase {ECO:0000256|HAMAP-Rule:MF_01356}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}; KW Transport {ECO:0000256|HAMAP-Rule:MF_01356}. FT TRANSMEM 38..57 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT DOMAIN 47..157 FT /note="Oxidored_q6" FT /evidence="ECO:0000259|Pfam:PF01058" FT METAL 47 FT /note="Iron-sulfur (4Fe-4S)" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01356" FT METAL 48 FT /note="Iron-sulfur (4Fe-4S)" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01356" FT METAL 112 FT /note="Iron-sulfur (4Fe-4S)" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01356" FT METAL 143 FT /note="Iron-sulfur (4Fe-4S)" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01356" SQ SEQUENCE 231 AA; 25983 MW; 18BCBC18DD9D3900 CRC64; MTNVINPIER PQVTQQLSEN IILTTLDDLY NWAKMSSLYP MMFGTACCFM EFMAAYASRF DMERYGMIPR ATPRQADLMI TAGTITMKYA PNLVRLYEQM AEPKYVIAMG ACTITGGMFS VDSPTTVRGV DKLIPVDVYI PGCPPRPEAV IDAIIKLRKK IGNQSIQELP QLQQSHRYYS IPHKMKAVPP INDGKYLKSP TREAPSKEIA EATGLPLPLA LQQQKMEVEF Q //