ID A0A160T3R6_9CHLR Unreviewed; 862 AA.
AC A0A160T3R6;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 2.
DT 27-MAR-2024, entry version 33.
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:CUS03668.2};
GN ORFNames=CFX0092_A1790 {ECO:0000313|EMBL:CUS03668.2};
OS Candidatus Promineifilum breve.
OC Bacteria; Chloroflexota; Ardenticatenia; Candidatus Promineifilales;
OC Candidatus Promineifilaceae; Candidatus Promineifilum.
OX NCBI_TaxID=1806508 {ECO:0000313|EMBL:CUS03668.2, ECO:0000313|Proteomes:UP000215027};
RN [1] {ECO:0000313|EMBL:CUS03668.2, ECO:0000313|Proteomes:UP000215027}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Cfx-K {ECO:0000313|EMBL:CUS03668.2,
RC ECO:0000313|Proteomes:UP000215027};
RA Oliw E.H.;
RL Submitted (JAN-2016) 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; LN890655; CUS03668.2; -; Genomic_DNA.
DR AlphaFoldDB; A0A160T3R6; -.
DR KEGG; pbf:CFX0092_A1790; -.
DR OrthoDB; 9803192at2; -.
DR Proteomes; UP000215027; Chromosome i.
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; 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; 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: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; 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; 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|RuleBase:RU003525};
KW Oxidoreductase {ECO:0000313|EMBL:CUS03668.2};
KW Quinone {ECO:0000256|RuleBase:RU003525};
KW Reference proteome {ECO:0000313|Proteomes:UP000215027};
KW Translocase {ECO:0000256|RuleBase:RU003525}.
FT DOMAIN 3..103
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51085"
FT DOMAIN 103..142
FT /note="4Fe-4S His(Cys)3-ligated-type"
FT /evidence="ECO:0000259|PROSITE:PS51839"
FT DOMAIN 242..305
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
SQ SEQUENCE 862 AA; 92741 MW; 764D478E2A9A13E3 CRC64;
MSDMVTLTID GAEISVPKGM LVVDAAKKID IDIPVFCYHP KLNPVGMCRM CLVEIGLPVI
DRATGQKVLN PDGSVKLNFG KGLQTGCTVV VSEGMVVRTA TVPVQDARED IIEFLLTSHP
LDCPVCDKGG ECPLQNLTLA YGRDESRMDF RDKMKLAKHV PLGELIVLDR ERCIQCARCT
RFQAEIVDDP VIHFHNRGRR LEIVTFSDPG FDSYWSGNTT DICPVGALTS SDFRFEARPW
ELTPVASICP HCPVGCNTTM STRREAISGG RNVIKRIMPR QNEAVNEIWI CDKGRFVHHF
ADAPERLTRP LVRRDSRLEP VSWDDALDYV AGKLQQHKGA AAGIAGERLS NEDYFQFQRL
FRQGLGSGNL DLAERRLAGG DVVAQVGLSR GSNLRDLKKG DVILVVAADL HEEAPVWWLR
VKQAAERGAT LIVLNARATR LDKFARYARH YAPGGALAAA RELLTLAHVD TGAPEPDSAG
AVAAALVEAE NLVIFYGAEG LTYDESDALA RTLGNLLLLK RGDDDTAASH AGRPNNGLVP
VWSHGNTQGA WDMGIHPAFG PGYTAAANQG RGAAEIYAAA AEGRVEALYV LGADPVGDGL
LRAKPGFLVV QELFLTETAA LADVVLPAQS WAEREGTYTN GERRVQRFYP AIAAMGEARP
DWQILAQIGE RVGLGKPPFA AALVFKEIAA VVAPYKGLDY RTLAHVEAQW PIVGGPDLYF
GGTAYANRQG LGQQWAAAAE TGALPSYELP LDGPAGRSGG GLRVMRIPAL YTPGTLIDHT
DLLNRRMARP ALYLNPADAG LYADGEALTV AVGGESFDVT ATISDMAPAG VALLRGVPGA
HPLGIEPAIV SRRPVAEMAA AD
//
