ID A0A068R445_9GAMM Unreviewed; 910 AA.
AC A0A068R445;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 53.
DE RecName: Full=NADH-quinone oxidoreductase {ECO:0000256|RuleBase:RU003525};
DE EC=7.1.1.- {ECO:0000256|RuleBase:RU003525};
GN Name=nuoG {ECO:0000313|EMBL:CDG20890.1};
GN ORFNames=XPG1_1235 {ECO:0000313|EMBL:CDG20890.1};
OS Xenorhabdus poinarii G6.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Morganellaceae; Xenorhabdus.
OX NCBI_TaxID=1354304 {ECO:0000313|EMBL:CDG20890.1, ECO:0000313|Proteomes:UP000032735};
RN [1] {ECO:0000313|EMBL:CDG20890.1, ECO:0000313|Proteomes:UP000032735}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=G6 {ECO:0000313|EMBL:CDG20890.1,
RC ECO:0000313|Proteomes:UP000032735};
RA Genoscope - CEA;
RL Submitted (JUL-2013) 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; FO704551; CDG20890.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A068R445; -.
DR STRING; 1354304.XPG1_1235; -.
DR KEGG; xpo:XPG1_1235; -.
DR HOGENOM; CLU_000422_11_4_6; -.
DR Proteomes; UP000032735; 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; 3.30.200.210; -; 1.
DR Gene3D; 3.40.50.740; -; 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:CDG20890.1};
KW Quinone {ECO:0000256|ARBA:ARBA00022719, ECO:0000256|RuleBase:RU003525};
KW Translocase {ECO:0000256|ARBA:ARBA00022967, ECO:0000256|RuleBase:RU003525}.
FT DOMAIN 3..86
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51085"
FT DOMAIN 86..125
FT /note="4Fe-4S His(Cys)3-ligated-type"
FT /evidence="ECO:0000259|PROSITE:PS51839"
FT DOMAIN 224..280
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
SQ SEQUENCE 910 AA; 101506 MW; 48CF2950C0C65EDC CRC64;
MLTMATIHVD GKEYDVNGAD NLLQACLSLG LDIPYFCWHP ALGSVGACRQ CAVKQYQNAE
DTRGRLVMSC MTPAADGTYI SIDDEEAKQF RASVVEWLMT NHPHDCPVCE EGGNCHLQDM
TVMTGHSFRK YRFTKRTHQN QALGPFIAHE MNRCIACYRC VRYYKDYADG TDFGVYGAHD
NVYFGRPESG TLESEFAGNL VEICPTGVFT DKTHSERYNR KWDMQFAPSI CQQCSIGCNT
SPGERYGELR RIENRYNGTI NHYFMCDRGR FGYGYVNRDD RPRKPQQLRG DQWISLNAEQ
VMQGGADILR QAKNTIGIGS PRASIESNFA LRELVGAQNF YSGISAEEQH RLDMMLEILQ
QGGVYTPALR EIEDYDAVLI LGEDLTQTAA RMALSVRQAV KGKAREMAAA QKVADWQIAA
IMNIGQRAKY PLFLTSVDET RLDDIAAWSY HAPVDDQARL GFAIAHTLNS IAPAVDDLPD
ELKSKAEIIA QALRDAKKPL IISGSNPGSD TLIQAAANIA WALKDKGAHV GLSYVAAYAN
SLGLAMMEAQ PLDAALQRIA KGNSDTVIVV ENDLYRHAPA DKIDRALDNL KNLIVVDHQR
TAIMDKANLI LSASSFAESD GTLVNQEGRA QRYFQVYEPA FYDKSIVMLE SWRWMHSLYT
TYTQCQTDWT QLDHVINACV KAMPQFKDIV NAAPDATFRI RGQKLARSPH RYSGRTAMLA
DVSVHEQRQP QDIDTAFAFS MEGNNSPYAP RQQIPFAWAP GWNSPQAWNK FQAEVGGKLR
FGDPGVRLIE TVDGGLNYFD AIPAPFTAQQ GQWRVAPYFH LFGSDELSQR SEVIQERMPE
PYVMINHHDA EHLNVKEGAM MTFDCEGQQL RLTVRLSGNL AQGQIGLPLG MPGIPPVLAG
KSVNNLREVA
//
