ID A0A239DU38_9ACTN Unreviewed; 837 AA.
AC A0A239DU38;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE RecName: Full=NADH-quinone oxidoreductase {ECO:0000256|RuleBase:RU003525};
DE EC=7.1.1.- {ECO:0000256|RuleBase:RU003525};
GN ORFNames=SAMN06265355_115129 {ECO:0000313|EMBL:SNS35084.1};
OS Actinomadura mexicana.
OC Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC Thermomonosporaceae; Actinomadura.
OX NCBI_TaxID=134959 {ECO:0000313|EMBL:SNS35084.1, ECO:0000313|Proteomes:UP000198420};
RN [1] {ECO:0000313|EMBL:SNS35084.1, ECO:0000313|Proteomes:UP000198420}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44485 {ECO:0000313|EMBL:SNS35084.1,
RC ECO:0000313|Proteomes:UP000198420};
RA Kim H.J., Triplett B.A.;
RL Submitted (JUN-2017) 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 -!- 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; FZNP01000015; SNS35084.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A239DU38; -.
DR OrthoDB; 9810782at2; -.
DR Proteomes; UP000198420; Unassembled WGS sequence.
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 Gene3D; 3.10.20.740; -; 1.
DR Gene3D; 3.30.70.20; -; 1.
DR Gene3D; 3.40.50.740; -; 2.
DR Gene3D; 2.20.25.90; ADC-like domains; 1.
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; 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:SF12; NADH-QUINONE OXIDOREDUCTASE SUBUNIT G; 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}; NAD {ECO:0000256|RuleBase:RU003525};
KW Quinone {ECO:0000256|RuleBase:RU003525};
KW Translocase {ECO:0000256|RuleBase:RU003525}.
FT DOMAIN 25..109
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51085"
FT DOMAIN 111..150
FT /note="4Fe-4S His(Cys)3-ligated-type"
FT /evidence="ECO:0000259|PROSITE:PS51839"
FT DOMAIN 249..305
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
SQ SEQUENCE 837 AA; 87829 MW; 2AEA0286B0D8C087 CRC64;
MSTTVSGSSA AQSAPRARGD VPPVEMVACT IDGFEIEVPK GTLIIRAAEL LGIQIPRFCD
HPLLDPVGAC RQCLVEIPDA GNGRGMPKPQ ASCTTAVMPG MVVKTQLTSP VADKAQHGVM
ELLLINHPLD CPICDKGGEC PLQNQAMSNG RGESRFVEAK RTFPKPIPLS SQVLLDRERC
IQCARCTRFS DQIAGDAFID LFERGAKEQV GAADGKPFQS YFSGNTVQIC PVGALTGAAY
RFRSRPFDLV SQPSVCEHCA SGCALRTDHR RGKITRRLAG DDPQVNEEWN CDKGRWAFTY
GTQPERLAQP LVRGEDGELE PASWPEALTI AARGLAAAHG SAGVLTGGRV TLEDAYAYAK
FARIALGTND VDFRARPLSE EESRFLASSV AGHPIEVTYA DLEKAPVVLL AGFEPEEESP
IVFLRLRKAF RKNRLKVFAA APFTTRGLAK VGGTLLPTPP GSEAEVLGSL IGDDAGIGDD
ARPDVRTLLE TPGAVILVGE RLATSPGALT SATRVAQATG ARLAWVPRRA GERGAIEAGA
LPGLLPIGRP VADPGARAEV ARTWGVADLP AGPGEDTAGI IAAAAAGRRG ALLVGGVDPY
DLPDPEAMLR ALEATPFVVS LEQRPSAVTD RADVVLPVAA VAEKSGTFVD WEGRGRPFDI
VLKSAGRMSD LRVLDALADE MDVHLGLPGP EAARREMAGL GAYRGERPDA PSVAQGLAPH
PEQGEALLAT WRLLLDRGRL QDGEPFLAGT AKPAAARLSP ATAAEIGATV AVTVSAPRGE
VTLPLEITPD LPDRVVWLPT NSAGCALHRD LGAAAGGVVK IAAAVPAAAT ENAGGIE
//