ID A0A2A6RI58_9CHLR Unreviewed; 929 AA.
AC A0A2A6RI58;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
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:PDW02702.1};
GN ORFNames=CJ255_12655 {ECO:0000313|EMBL:PDW02702.1};
OS Candidatus Viridilinea mediisalina.
OC Bacteria; Chloroflexota; Chloroflexia; Chloroflexales; Chloroflexineae;
OC Oscillochloridaceae; Viridilinea.
OX NCBI_TaxID=2024553 {ECO:0000313|EMBL:PDW02702.1, ECO:0000313|Proteomes:UP000220527};
RN [1] {ECO:0000313|Proteomes:UP000220527}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Kir15-3F {ECO:0000313|Proteomes:UP000220527};
RA Grouzdev D.S., Gaisin V.A., Rysina M.S., Gorlenko V.M.;
RL Submitted (AUG-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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PDW02702.1}.
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DR EMBL; NQWI01000055; PDW02702.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2A6RI58; -.
DR OrthoDB; 9803192at2; -.
DR Proteomes; UP000220527; 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:0043546; F:molybdopterin cofactor binding; IEA:InterPro.
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; cd02775; MopB_CT; 1.
DR Gene3D; 2.40.40.20; -; 1.
DR Gene3D; 3.10.20.740; -; 1.
DR Gene3D; 3.30.70.20; -; 1.
DR Gene3D; 3.40.50.740; -; 1.
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; IPR006657; MoPterin_dinucl-bd_dom.
DR InterPro; IPR006656; Mopterin_OxRdtase.
DR InterPro; IPR006963; Mopterin_OxRdtase_4Fe-4S_dom.
DR InterPro; IPR006655; Mopterin_OxRdtase_prok_CS.
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:SF15; FORMATE DEHYDROGENASE H; 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; PF01568; Molydop_binding; 1.
DR Pfam; PF10588; NADH-G_4Fe-4S_3; 1.
DR PIRSF; PIRSF036643; FDH_alpha; 2.
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.
DR PROSITE; PS00490; MOLYBDOPTERIN_PROK_2; 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 Reference proteome {ECO:0000313|Proteomes:UP000220527};
KW Translocase {ECO:0000256|RuleBase:RU003525}.
FT DOMAIN 2..102
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51085"
FT DOMAIN 102..141
FT /note="4Fe-4S His(Cys)3-ligated-type"
FT /evidence="ECO:0000259|PROSITE:PS51839"
FT DOMAIN 241..297
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
FT REGION 663..682
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 717..742
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 929 AA; 100160 MW; 07CAAAD4A1D527D8 CRC64;
MPDVTITVDG RSFSVPAGTN VVDAARMGGI AIPVFCYHPR MPAVGMCRMC LVQVGMPKLD
PATRQPLMDA QGQPVIALMP KLQTGCTTPV SEGMVINTKT EEVQFAQKGV LEFLLTSHPL
DCPVCDKGGE CPLQNLTMEW GPGQSRFDYN DKVHFEKPVP LGDLILLDRE RCILCSRCVR
FQDELADDSV LGFDHRGRNW MIVSKSDPPF ASKFSGNTTD ICPVGALTTA DFRFKARVWE
LSSKPGICTL CPVGCNLNFD MRHDRLMRVM PRENGAVNDI WLCDKGRFGH RFIEHESRLH
APLIRHGDHF VEASWEEALT LVAEKLAAVQ SARGGSAIAG LAAPRLSNED LYLFQRLFRE
QLGSNNLDHH LGSPDDGDHD DLGGLLAVGK GTNLMELGAG TTVLVFGADP EEEAPLYLLR
LRALVQRGAQ LFVANQRATK LERSATQALR YSVGGELALA RALVRELLER GAAERIKLKH
SGLDALRKQV LAQTPEQLAA AAGIAHEQIV ALATALLEAE HGLIMYGAEA RSAGLALIET
LGALAVLSGN VGKPNSGMIA LLPGGNSRGA LDLGVRPDAR PGYVLMPQRG LPAQQLWSAA
RDGHVRALWI AGLDPAACLP DAREALTAAE FVVVQELFMS ETARMADVVL PAASVAERDG
TYTNAERRVQ RSRAARAPHG QSRPDWQIFQ DVAQMLADMM VLPHPRVEAE GAKPAKAAKG
AKTAKGQNEQ VVTRPPEPPR WDYLTPDEVA AEIAERVPSY GGVTYEALAA TGNPGVWGRQ
ANEAVFYDGT SYENTEGIGI ALPSLISTGR FTLSLSPRPA PVVKDERPLL LLAQPLAYGG
DPLLRGSLLE RQLAQPAIVI SQSDAEKLNI QNGDRVRIVS AVGELSAAAR VHADLPPGLV
MVPAGLPGLC LSRIQTGPRT RVSLVKVVV
//
