ID A0A2K8SR27_9NOSO Unreviewed; 562 AA. AC A0A2K8SR27; DT 25-APR-2018, integrated into UniProtKB/TrEMBL. DT 25-APR-2018, sequence version 1. DT 20-JUN-2018, entry version 3. DE RecName: Full=NAD(P)H-quinone oxidoreductase chain 4 {ECO:0000256|HAMAP-Rule:MF_00491}; DE EC=1.6.5.- {ECO:0000256|HAMAP-Rule:MF_00491}; DE AltName: Full=NAD(P)H dehydrogenase I, chain 4 {ECO:0000256|HAMAP-Rule:MF_00491}; DE AltName: Full=NDH-1, chain 4 {ECO:0000256|HAMAP-Rule:MF_00491}; GN Name=ndhD {ECO:0000256|HAMAP-Rule:MF_00491}; GN ORFNames=COO91_03875 {ECO:0000313|EMBL:AUB37924.1}; OS Nostoc flagelliforme CCNUN1. OC Bacteria; Cyanobacteria; Nostocales; Nostocaceae; Nostoc. OX NCBI_TaxID=2038116 {ECO:0000313|EMBL:AUB37924.1, ECO:0000313|Proteomes:UP000232003}; RN [1] {ECO:0000313|EMBL:AUB37924.1, ECO:0000313|Proteomes:UP000232003} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CCNUN1 {ECO:0000313|EMBL:AUB37924.1, RC ECO:0000313|Proteomes:UP000232003}; RA Shang J.; RT "Complete genome of a free-living desiccation-tolerant cyanobacterium RT and its photosynthetic adaptation to extreme terrestrial habitat."; RL Submitted (NOV-2017) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: NDH-1 shuttles electrons from NAD(P)H, via FMN and iron- CC sulfur (Fe-S) centers, to quinones in the respiratory chain. The CC immediate electron acceptor for the enzyme in this species is CC believed to be plastoquinone. Couples the redox reaction to proton CC translocation (for every two electrons transferred, four hydrogen CC ions are translocated across the cytoplasmic membrane), and thus CC conserves the redox energy in a proton gradient. CC {ECO:0000256|HAMAP-Rule:MF_00491}. CC -!- CATALYTIC ACTIVITY: NAD(P)H + plastoquinone = NAD(P)(+) + CC plastoquinol. {ECO:0000256|HAMAP-Rule:MF_00491}. CC -!- SUBCELLULAR LOCATION: Cellular thylakoid membrane CC {ECO:0000256|HAMAP-Rule:MF_00491}; Multi-pass membrane protein CC {ECO:0000256|HAMAP-Rule:MF_00491}. CC -!- SIMILARITY: Belongs to the complex I subunit 4 family. CC {ECO:0000256|HAMAP-Rule:MF_00491}. 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; CP024785; AUB37924.1; -; Genomic_DNA. DR Proteomes; UP000232003; Chromosome. 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:0008137; F:NADH dehydrogenase (ubiquinone) activity; IEA:InterPro. DR GO; GO:0048038; F:quinone binding; IEA:UniProtKB-KW. DR GO; GO:0042773; P:ATP synthesis coupled electron transport; IEA:InterPro. DR HAMAP; MF_00491; NDH1_NuoM; 1. DR InterPro; IPR022997; NADH_Q_OxRdtase_chain4. DR InterPro; IPR010227; NADH_Q_OxRdtase_chainM/4. DR InterPro; IPR003918; NADH_UbQ_OxRdtase. DR InterPro; IPR001750; ND/Mrp_mem. DR PANTHER; PTHR43507; PTHR43507; 2. DR PANTHER; PTHR43507:SF3; PTHR43507:SF3; 2. DR Pfam; PF00361; Proton_antipo_M; 1. DR PRINTS; PR01437; NUOXDRDTASE4. DR TIGRFAMs; TIGR01972; NDH_I_M; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000232003}; KW Membrane {ECO:0000256|HAMAP-Rule:MF_00491}; KW NAD {ECO:0000256|HAMAP-Rule:MF_00491}; KW NADP {ECO:0000256|HAMAP-Rule:MF_00491}; KW Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_00491}; KW Plastoquinone {ECO:0000256|HAMAP-Rule:MF_00491}; KW Quinone {ECO:0000256|HAMAP-Rule:MF_00491}; KW Reference proteome {ECO:0000313|Proteomes:UP000232003}; KW Thylakoid {ECO:0000256|HAMAP-Rule:MF_00491}; KW Transmembrane {ECO:0000256|HAMAP-Rule:MF_00491}; KW Transmembrane helix {ECO:0000256|HAMAP-Rule:MF_00491}. FT TRANSMEM 6 27 Helical. {ECO:0000256|HAMAP-Rule: FT MF_00491}. FT TRANSMEM 34 54 Helical. {ECO:0000256|HAMAP-Rule: FT MF_00491}. FT TRANSMEM 80 103 Helical. {ECO:0000256|HAMAP-Rule: FT MF_00491}. FT TRANSMEM 115 133 Helical. {ECO:0000256|HAMAP-Rule: FT MF_00491}. FT TRANSMEM 139 157 Helical. {ECO:0000256|HAMAP-Rule: FT MF_00491}. FT TRANSMEM 169 193 Helical. {ECO:0000256|HAMAP-Rule: FT MF_00491}. FT TRANSMEM 213 235 Helical. {ECO:0000256|HAMAP-Rule: FT MF_00491}. FT TRANSMEM 247 264 Helical. {ECO:0000256|HAMAP-Rule: FT MF_00491}. FT TRANSMEM 276 295 Helical. {ECO:0000256|HAMAP-Rule: FT MF_00491}. FT TRANSMEM 307 325 Helical. {ECO:0000256|HAMAP-Rule: FT MF_00491}. FT TRANSMEM 337 355 Helical. {ECO:0000256|HAMAP-Rule: FT MF_00491}. FT TRANSMEM 376 393 Helical. {ECO:0000256|HAMAP-Rule: FT MF_00491}. FT TRANSMEM 413 436 Helical. {ECO:0000256|HAMAP-Rule: FT MF_00491}. FT TRANSMEM 490 507 Helical. {ECO:0000256|HAMAP-Rule: FT MF_00491}. FT DOMAIN 133 423 Proton_antipo_M. {ECO:0000259|Pfam: FT PF00361}. SQ SEQUENCE 562 AA; 61297 MW; 270995527D2C42D0 CRC64; MIADQFPWLT AIVLLPLIAS LLIPVLPDKD GKRVRWYALG IGIADFALMC YAFWKHYDAS SASFQLVESY AWMPQLGLNW AVSVDGLSVP LVLLAGFVTT LSMFSAWQVD HRPRLFYFLM LVLYSAQVGV FVAKDLLLFF IMWEVELIPV YLLVCIWGGQ RRRYAATKFL LYTAAASIFI LVAALAMGLY GSGDMTFDIT ALAKKEYPLG LQLLLYAGLL IAFGVKLAVF PMHTWLPDAH GEASSPVSMI LAGVLLKMGG YGLIRLNLEL LPDAHIYFAP VLAILGVVNI IYGALNSFAQ TNMKRRLAYS SISHMGFVLL GIASFTDLGI NGAMLQMISH GLIASVLFFL AGVTYDRTHT MVMKDMGGIG QAMPKVFALF TISAMASLAL PGMSGFAGEL SVFVGVASSD VYSSTFCTVT VFLAAVGVIL TPIYLLSMLR EVFYGKDAAL LCDINNAGSQ NQEDEGTVCF GTDCLVPEEA VYDDARPREV FIAACFLLMI IGIGFYPKMA MQMYDVKTVA VNANLRQSYA IVSQTNPQIY AKGFLVPQIS EVEAAPVLGT LK //