ID A0A1Z4QAH8_9CYAN Unreviewed; 231 AA. AC A0A1Z4QAH8; DT 27-SEP-2017, integrated into UniProtKB/TrEMBL. DT 27-SEP-2017, sequence version 1. DT 22-NOV-2017, entry version 3. DE RecName: Full=NAD(P)H-quinone oxidoreductase subunit K {ECO:0000256|HAMAP-Rule:MF_01356}; DE EC=1.6.5.- {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. OX NCBI_TaxID=2005464 {ECO:0000313|EMBL:BAZ27212.1}; RN [1] {ECO:0000313|EMBL:BAZ27212.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=NIES-4073 {ECO:0000313|EMBL:BAZ27212.1}; 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, CC via FMN and iron-sulfur (Fe-S) centers, to quinones in the CC respiratory and/or the photosynthetic chain. The immediate CC electron acceptor for the enzyme in this species is believed to be CC plastoquinone. Couples the redox reaction to proton translocation, CC and thus conserves the redox energy in a proton gradient. CC Cyanobacterial NDH-1 also plays a role in inorganic carbon- CC concentration. {ECO:0000256|HAMAP-Rule:MF_01356}. CC -!- CATALYTIC ACTIVITY: NAD(P)H + plastoquinone = NAD(P)(+) + CC plastoquinol. {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 CC identified which probably have different functions. CC {ECO:0000256|HAMAP-Rule:MF_01356}. CC -!- SUBCELLULAR LOCATION: Cellular thylakoid membrane CC {ECO:0000256|HAMAP-Rule:MF_01356}; Peripheral membrane protein CC {ECO:0000256|HAMAP-Rule:MF_01356}; Cytoplasmic side CC {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 GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042651; C: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 GO; GO:0006810; P:transport; IEA:UniProtKB-KW. DR Gene3D; 3.40.50.700; -; 1. DR HAMAP; MF_01356; NDH1_NuoB; 1. DR InterPro; IPR037024; NADH_UbQ_OxR-like_20kDa_sf. 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, KW 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 Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_01356, KW ECO:0000256|RuleBase:RU004464}; 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 Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}; KW Transport {ECO:0000256|HAMAP-Rule:MF_01356}. FT TRANSMEM 38 57 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 47 157 Oxidored_q6. {ECO:0000259|Pfam:PF01058}. FT METAL 47 47 Iron-sulfur (4Fe-4S). {ECO:0000256|HAMAP- FT Rule:MF_01356}. FT METAL 48 48 Iron-sulfur (4Fe-4S). {ECO:0000256|HAMAP- FT Rule:MF_01356}. FT METAL 112 112 Iron-sulfur (4Fe-4S). {ECO:0000256|HAMAP- FT Rule:MF_01356}. FT METAL 143 143 Iron-sulfur (4Fe-4S). {ECO:0000256|HAMAP- FT 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 //