ID A0A075K6F5_9GAMM Unreviewed; 773 AA.
AC A0A075K6F5;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 54.
DE RecName: Full=NADH-quinone oxidoreductase {ECO:0000256|RuleBase:RU003525};
DE EC=7.1.1.- {ECO:0000256|RuleBase:RU003525};
GN ORFNames=HY57_10960 {ECO:0000313|EMBL:AIF47748.1};
OS Dyella japonica A8.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Rhodanobacteraceae; Dyella.
OX NCBI_TaxID=1217721 {ECO:0000313|EMBL:AIF47748.1, ECO:0000313|Proteomes:UP000027987};
RN [1] {ECO:0000313|EMBL:AIF47748.1, ECO:0000313|Proteomes:UP000027987}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=A8 {ECO:0000313|EMBL:AIF47748.1,
RC ECO:0000313|Proteomes:UP000027987};
RA Hui R.K.H., Chen J.-W., Chan K.-G., Leung F.C.C.;
RT "Complete Genome Sequence of Dyella japonica Strain A8 Isolated from
RT Malaysian Tropical Soil.";
RL Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur
CC (Fe-S) centers, to quinones in the respiratory chain. Couples the redox
CC reaction to proton translocation (for every two electrons transferred,
CC four hydrogen ions are translocated across the cytoplasmic membrane),
CC and thus conserves the redox energy in a proton gradient.
CC {ECO:0000256|RuleBase:RU003525}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a quinone + 5 H(+)(in) + NADH = a quinol + 4 H(+)(out) +
CC NAD(+); Xref=Rhea:RHEA:57888, ChEBI:CHEBI:15378, ChEBI:CHEBI:24646,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:132124;
CC Evidence={ECO:0000256|ARBA:ARBA00000100,
CC ECO:0000256|RuleBase:RU003525};
CC -!- COFACTOR:
CC Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135;
CC Evidence={ECO:0000256|RuleBase:RU003525};
CC Note=Binds 1 [2Fe-2S] cluster per subunit.
CC {ECO:0000256|RuleBase:RU003525};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000256|ARBA:ARBA00001966,
CC ECO:0000256|RuleBase:RU003525};
CC -!- SUBUNIT: Composed of 13 different subunits. Subunits NuoCD, E, F, and G
CC constitute the peripheral sector of the complex.
CC {ECO:0000256|ARBA:ARBA00026021}.
CC -!- SIMILARITY: Belongs to the complex I 75 kDa subunit family.
CC {ECO:0000256|ARBA:ARBA00005404, ECO:0000256|RuleBase:RU003525}.
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DR EMBL; CP008884; AIF47748.1; -; Genomic_DNA.
DR RefSeq; WP_019466199.1; NZ_CP008884.1.
DR AlphaFoldDB; A0A075K6F5; -.
DR STRING; 1217721.HY57_10960; -.
DR KEGG; dja:HY57_10960; -.
DR PATRIC; fig|1217721.7.peg.2265; -.
DR HOGENOM; CLU_000422_11_6_6; -.
DR OrthoDB; 9810782at2; -.
DR Proteomes; UP000027987; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProt.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IEA:UniProt.
DR GO; GO:0016020; C:membrane; IEA:InterPro.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-UniRule.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0008137; F:NADH dehydrogenase (ubiquinone) activity; IEA:UniProtKB-UniRule.
DR GO; GO:0048038; F:quinone binding; IEA:UniProtKB-UniRule.
DR GO; GO:0042773; P:ATP synthesis coupled electron transport; IEA:InterPro.
DR CDD; cd00207; fer2; 1.
DR Gene3D; 3.10.20.740; -; 1.
DR Gene3D; 3.30.70.20; -; 1.
DR Gene3D; 3.40.50.740; -; 2.
DR Gene3D; 3.40.228.10; Dimethylsulfoxide Reductase, domain 2; 1.
DR InterPro; IPR036010; 2Fe-2S_ferredoxin-like_sf.
DR InterPro; IPR001041; 2Fe-2S_ferredoxin-type.
DR InterPro; IPR006656; Mopterin_OxRdtase.
DR InterPro; IPR006963; Mopterin_OxRdtase_4Fe-4S_dom.
DR InterPro; IPR000283; NADH_UbQ_OxRdtase_75kDa_su_CS.
DR InterPro; IPR010228; NADH_UbQ_OxRdtase_Gsu.
DR InterPro; IPR019574; NADH_UbQ_OxRdtase_Gsu_4Fe4S-bd.
DR NCBIfam; TIGR01973; NuoG; 1.
DR PANTHER; PTHR43105:SF13; NADH-UBIQUINONE OXIDOREDUCTASE 75 KDA SUBUNIT, MITOCHONDRIAL; 1.
DR PANTHER; PTHR43105; RESPIRATORY NITRATE REDUCTASE; 1.
DR Pfam; PF13510; Fer2_4; 1.
DR Pfam; PF00384; Molybdopterin; 1.
DR Pfam; PF10588; NADH-G_4Fe-4S_3; 1.
DR SMART; SM00929; NADH-G_4Fe-4S_3; 1.
DR SUPFAM; SSF54292; 2Fe-2S ferredoxin-like; 1.
DR SUPFAM; SSF54862; 4Fe-4S ferredoxins; 1.
DR SUPFAM; SSF53706; Formate dehydrogenase/DMSO reductase, domains 1-3; 1.
DR PROSITE; PS51085; 2FE2S_FER_2; 1.
DR PROSITE; PS51839; 4FE4S_HC3; 1.
DR PROSITE; PS51669; 4FE4S_MOW_BIS_MGD; 1.
DR PROSITE; PS00641; COMPLEX1_75K_1; 1.
DR PROSITE; PS00642; COMPLEX1_75K_2; 1.
DR PROSITE; PS00643; COMPLEX1_75K_3; 1.
PE 3: Inferred from homology;
KW 2Fe-2S {ECO:0000256|RuleBase:RU003525};
KW 4Fe-4S {ECO:0000256|ARBA:ARBA00022485, ECO:0000256|RuleBase:RU003525};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|RuleBase:RU003525};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014, ECO:0000256|RuleBase:RU003525};
KW Metal-binding {ECO:0000256|RuleBase:RU003525};
KW NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|RuleBase:RU003525};
KW Quinone {ECO:0000256|RuleBase:RU003525};
KW Translocase {ECO:0000256|ARBA:ARBA00022967, ECO:0000256|RuleBase:RU003525}.
FT DOMAIN 11..93
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51085"
FT DOMAIN 93..132
FT /note="4Fe-4S His(Cys)3-ligated-type"
FT /evidence="ECO:0000259|PROSITE:PS51839"
FT DOMAIN 230..286
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
SQ SEQUENCE 773 AA; 82030 MW; 6DB4453040055AB3 CRC64;
MSAQPTTPNL DLLNIEIDGK PTQIRKGAMI IEAADAIGVS IPRFCYHRKL PIAANCRMCL
VEVEMGGKPM PKPQPACATP VAEGMKVKTR TDVALKYQKD VMEFLLINHP LDCPICDQGG
ECELQDVALG YGRSVSRYTE RKRTIADENL GPLVATEMTR CIQCTRCVRF TSEIAGTYEL
GGMSRGDNLQ IGTYIGKTIE TELSGNIIDV CPVGALTNKP FQFQARAWEL IAKPSVAYHD
ALGSNLWLHT RRGEVLRTVP RDNESINECW LSDRDRYSHQ GLYAADRVSA PQVKRNGQWV
TTTWEDALGA AAEALKAVPG SDLGVLVHPA TTNEEGDVLV RLARGLGSAH VDHRVRQLDF
ADNAIATAFG KPVAELDKVK AALLVGSDLR HELPLVNHRI HQAVKKGAKV YAVNPASFHF
NYKLAGEAIV APQALVDALL ALAKAAVESG ASAPAALADA INGATSDQGD KDAIADLKSG
SAVVILGEAA VTHPQASWLR AVAQFIAQAT GAAYNELPVG ANAVGLGRVG VLPGNGGLDA
QAMLAQPRKA YVLYGVEPLD VADGAAFLKA LKGAQKVVAF SAYASDELRA VADVILPIGL
LPEIDGTLVN VDGLSQSVAA GAKAPGETRP GWKVLRALGG VLKLAGFEFD DLAGLREGIT
ERAHPSRAEL APRQPTGGLS RLATWPIYRT DAVLRRATAL SKHPLNRAPA VRVNADEAKR
LGLGEGDAVR VADAVLPLVI DMTVPDGAAW IEAAHDDTVT LPPYGAALTL SKA
//
