ID A0A2K8SR27_9NOSO Unreviewed; 562 AA. AC A0A2K8SR27; DT 25-APR-2018, integrated into UniProtKB/TrEMBL. DT 25-APR-2018, sequence version 1. DT 02-OCT-2024, entry version 24. DE RecName: Full=NAD(P)H-quinone oxidoreductase chain 4 {ECO:0000256|HAMAP-Rule:MF_00491}; DE EC=7.1.1.- {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; Cyanobacteriota; Cyanophyceae; 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 and RT 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 believed CC to be plastoquinone. Couples the redox reaction to proton translocation CC (for every two electrons transferred, four hydrogen ions are CC translocated across the cytoplasmic membrane), and thus conserves the CC redox energy in a proton gradient. {ECO:0000256|ARBA:ARBA00025624, CC ECO:0000256|HAMAP-Rule:MF_00491}. 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_00491}; 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_00491}; CC -!- SUBCELLULAR LOCATION: Cellular thylakoid membrane {ECO:0000256|HAMAP- CC Rule:MF_00491}; Multi-pass membrane protein {ECO:0000256|HAMAP- CC Rule:MF_00491}. Membrane {ECO:0000256|ARBA:ARBA00004141, CC ECO:0000256|RuleBase:RU000320}; Multi-pass membrane protein CC {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU000320}. 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 AlphaFoldDB; A0A2K8SR27; -. DR KEGG; nfl:COO91_03875; -. DR OrthoDB; 416973at2; -. DR Proteomes; UP000232003; Chromosome. DR GO; GO:0031676; C:plasma membrane-derived 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 NCBIfam; TIGR01972; NDH_I_M; 1. DR PANTHER; PTHR43507:SF1; NAD(P)H-QUINONE OXIDOREDUCTASE CHAIN 4, CHLOROPLASTIC; 1. DR PANTHER; PTHR43507; NADH-UBIQUINONE OXIDOREDUCTASE CHAIN 4; 1. DR Pfam; PF00361; Proton_antipo_M; 1. DR PRINTS; PR01437; NUOXDRDTASE4. PE 3: Inferred from homology; KW Membrane {ECO:0000256|HAMAP-Rule:MF_00491}; KW NAD {ECO:0000256|HAMAP-Rule:MF_00491}; KW NADP {ECO:0000256|ARBA:ARBA00022857, ECO:0000256|HAMAP-Rule:MF_00491}; KW Plastoquinone {ECO:0000256|ARBA:ARBA00022957, ECO:0000256|HAMAP- KW Rule:MF_00491}; KW Quinone {ECO:0000256|ARBA:ARBA00022719, ECO:0000256|HAMAP-Rule:MF_00491}; KW Reference proteome {ECO:0000313|Proteomes:UP000232003}; KW Thylakoid {ECO:0000256|HAMAP-Rule:MF_00491}; KW Translocase {ECO:0000256|HAMAP-Rule:MF_00491}; KW Transmembrane {ECO:0000256|HAMAP-Rule:MF_00491, KW ECO:0000256|RuleBase:RU000320}; KW Transmembrane helix {ECO:0000256|HAMAP-Rule:MF_00491}. FT TRANSMEM 6..27 FT /note="Helical" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00491" FT TRANSMEM 34..54 FT /note="Helical" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00491" FT TRANSMEM 80..103 FT /note="Helical" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00491" FT TRANSMEM 115..133 FT /note="Helical" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00491" FT TRANSMEM 139..157 FT /note="Helical" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00491" FT TRANSMEM 169..193 FT /note="Helical" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00491" FT TRANSMEM 213..235 FT /note="Helical" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00491" FT TRANSMEM 247..264 FT /note="Helical" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00491" FT TRANSMEM 276..295 FT /note="Helical" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00491" FT TRANSMEM 307..325 FT /note="Helical" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00491" FT TRANSMEM 337..355 FT /note="Helical" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00491" FT TRANSMEM 376..393 FT /note="Helical" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00491" FT TRANSMEM 413..436 FT /note="Helical" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00491" FT TRANSMEM 490..507 FT /note="Helical" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00491" FT DOMAIN 133..421 FT /note="NADH:quinone oxidoreductase/Mrp antiporter membrane FT subunit" FT /evidence="ECO:0000259|Pfam: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 //