ID F6AC95_PSEF1 Unreviewed; 909 AA.
AC F6AC95;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 27-JUL-2011, sequence version 1.
DT 27-MAR-2024, entry version 66.
DE RecName: Full=NADH-quinone oxidoreductase {ECO:0000256|RuleBase:RU003525};
DE EC=7.1.1.- {ECO:0000256|RuleBase:RU003525};
GN OrderedLocusNames=Psefu_2310 {ECO:0000313|EMBL:AEF22277.1};
OS Pseudomonas fulva (strain 12-X).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=743720 {ECO:0000313|EMBL:AEF22277.1, ECO:0000313|Proteomes:UP000000686};
RN [1] {ECO:0000313|EMBL:AEF22277.1, ECO:0000313|Proteomes:UP000000686}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=12-X {ECO:0000313|Proteomes:UP000000686};
RG US DOE Joint Genome Institute;
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Mikhailova N., Pagani I., Davenport K., Han C., Tapia R.,
RA Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., Lcollab F.I.,
RA Woyke T.;
RT "Complete sequence of Pseudomonas fulva 12-X.";
RL Submitted (APR-2011) 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}.
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; CP002727; AEF22277.1; -; Genomic_DNA.
DR RefSeq; WP_013791406.1; NC_015556.1.
DR AlphaFoldDB; F6AC95; -.
DR STRING; 743720.Psefu_2310; -.
DR KEGG; pfv:Psefu_2310; -.
DR eggNOG; COG1034; Bacteria.
DR HOGENOM; CLU_000422_11_4_6; -.
DR OrthoDB; 9810782at2; -.
DR Proteomes; UP000000686; Chromosome.
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 CDD; cd02788; MopB_CT_NDH-1_NuoG2-N7; 1.
DR CDD; cd02771; MopB_NDH-1_NuoG2-N7; 1.
DR Gene3D; 2.40.40.20; -; 1.
DR Gene3D; 3.10.20.740; -; 1.
DR Gene3D; 3.40.50.740; -; 1.
DR Gene3D; 2.20.25.90; ADC-like domains; 1.
DR InterPro; IPR036010; 2Fe-2S_ferredoxin-like_sf.
DR InterPro; IPR001041; 2Fe-2S_ferredoxin-type.
DR InterPro; IPR009010; Asp_de-COase-like_dom_sf.
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; PF04879; Molybdop_Fe4S4; 1.
DR Pfam; PF00384; Molybdopterin; 1.
DR Pfam; PF10588; NADH-G_4Fe-4S_3; 1.
DR SMART; SM00926; Molybdop_Fe4S4; 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; SSF50692; ADC-like; 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|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU003525};
KW NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|RuleBase:RU003525};
KW Oxidoreductase {ECO:0000313|EMBL:AEF22277.1};
KW Quinone {ECO:0000256|RuleBase:RU003525};
KW Reference proteome {ECO:0000313|Proteomes:UP000000686};
KW Translocase {ECO:0000256|ARBA:ARBA00022967, ECO:0000256|RuleBase:RU003525}.
FT DOMAIN 1..83
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51085"
FT DOMAIN 83..122
FT /note="4Fe-4S His(Cys)3-ligated-type"
FT /evidence="ECO:0000259|PROSITE:PS51839"
FT DOMAIN 221..277
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
SQ SEQUENCE 909 AA; 98342 MW; 73093BEB2DDBABC2 CRC64;
MATIHVDGKD LEVDGADNLL QACLSLGLDI PYFCWHPALG SVGACRQCAV KQYTDENDKR
GRLVMSCMTP ATDNSWISID DEEAVAFRKS VVEWLMTNHP HDCPVCEEGG HCHLQDMTVM
TGHNARRYRF SKRTHQNQEL GPFIAHEMNR CIACYRCVRY YKDYAGGTDL GVYGAHDNVY
FGRVEDGTLE SEFSGNLVEV CPTGVFTDKT HSERYNRKWD MQFAPSICHG CSSGCNTSPG
ERYGEVRRIE NRFNGSVNQY FLCDRGRFGY GYVNREDRPR QPVMMLSKMK MGLDAALDQA
AALLKGRKVI GIGSPRASLE GNFALRELVG AGNFYSGIAA AEQANIRLIR DVLQNGPLPV
PTLRDIESHD AVFVLGEDLT QTAARVALAL RQSVKGKATE IAAGAKIQDW HMAAVQNVAQ
HALNPLFIAS VTATRLDDVA EQCVHAAPDD LARIGFAVAH AIDPSAPAVE GLEAEAGELV
QRIAEALLNA KRPLIVSGAS LGNRALIEAA ANIASALKNR EKNGSISLVV PEANSMGMAL
LMGEQFSGNS LDDALEALTS GQADALVVLE NDLYHRADAA RVDAALAAAK VVIVADHQST
ATTAKAHLLL PAASFAEGDG TLVSQEGRAQ RFFQVYDPSY YDANILVREG WRWLHALHST
LHNRVVDWTQ LDQVTAACAE SSAQLAGIRD AAPSASFRIK GLKLAREPHR YSGRTAMRAN
ISVHEPRQPQ DKDSAFAFSM EGYSGSKEDR QQIPFAWSPG WNSPQAWNKF QDEVGGHLRA
GDPGVRLIEA KGASLGWFSA PTAFNPAQGT WQAVPLHHLF GSEEMSSRAT PIAERTPEAY
VALAKDEADR LGVNDGALLQ LSVNGQSLRL PLRVSEELGI GLVGLPVGLA GIPAAIAGAA
VSNIGEAAQ
//
