ID A0A4R1L6L4_9BACT Unreviewed; 780 AA.
AC A0A4R1L6L4;
DT 31-JUL-2019, integrated into UniProtKB/TrEMBL.
DT 31-JUL-2019, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE SubName: Full=NADH-quinone oxidoreductase chain G {ECO:0000313|EMBL:TCK73784.1};
GN ORFNames=C7378_1398 {ECO:0000313|EMBL:TCK73784.1};
OS Acidipila rosea.
OC Bacteria; Acidobacteriota; Terriglobia; Terriglobales; Acidobacteriaceae;
OC Acidipila.
OX NCBI_TaxID=768535 {ECO:0000313|EMBL:TCK73784.1, ECO:0000313|Proteomes:UP000295210};
RN [1] {ECO:0000313|EMBL:TCK73784.1, ECO:0000313|Proteomes:UP000295210}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 103428 {ECO:0000313|EMBL:TCK73784.1,
RC ECO:0000313|Proteomes:UP000295210};
RA Goeker M.;
RT "Genomic Encyclopedia of Type Strains, Phase IV (KMG-IV): sequencing the
RT most valuable type-strain genomes for metagenomic binning, comparative
RT biology and taxonomic classification.";
RL Submitted (MAR-2019) to the EMBL/GenBank/DDBJ databases.
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 -!- COFACTOR:
CC Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135;
CC Evidence={ECO:0000256|ARBA:ARBA00034078};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000256|ARBA:ARBA00001966};
CC -!- SIMILARITY: Belongs to the complex I 75 kDa subunit family.
CC {ECO:0000256|ARBA:ARBA00005404, ECO:0000256|RuleBase:RU004523}.
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:TCK73784.1}.
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DR EMBL; SMGK01000002; TCK73784.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A4R1L6L4; -.
DR OrthoDB; 9805142at2; -.
DR Proteomes; UP000295210; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:InterPro.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008137; F:NADH dehydrogenase (ubiquinone) activity; IEA:InterPro.
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; IPR017896; 4Fe4S_Fe-S-bd.
DR InterPro; IPR017900; 4Fe4S_Fe_S_CS.
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; PF00037; Fer4; 1.
DR Pfam; PF04879; Molybdop_Fe4S4; 1.
DR Pfam; PF00384; Molybdopterin; 2.
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; SSF53706; Formate dehydrogenase/DMSO reductase, domains 1-3; 1.
DR PROSITE; PS51085; 2FE2S_FER_2; 1.
DR PROSITE; PS00198; 4FE4S_FER_1; 1.
DR PROSITE; PS51379; 4FE4S_FER_2; 2.
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.
PE 3: Inferred from homology;
KW 4Fe-4S {ECO:0000256|ARBA:ARBA00022485};
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000295210}.
FT DOMAIN 2..80
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51085"
FT DOMAIN 80..119
FT /note="4Fe-4S His(Cys)3-ligated-type"
FT /evidence="ECO:0000259|PROSITE:PS51839"
FT DOMAIN 139..168
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 178..208
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 217..277
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
SQ SEQUENCE 780 AA; 85302 MW; CE00C9A30653192A CRC64;
MADVTFTVDG KKLTAPAGTL LIDACRKAGI EIPAFCYYPG LSLQAACRMC VVRLEKVPKL
QTACTTPVAE GMVVTTESDE IKQSRKAILE LLLGNHPLDC PVCDAGGECE LQDMTFKYGA
AESKYVEIKQ HREEQQWSPV VFFDRPRCIL CYRCVRVCGE GMDVWALGVQ NRGVSSVISP
NGEDHLDCEE CGMCIDICPV GALTSGTYRY KTRPWEMNHV ATVCTHCGDG CKTTLGVRSV
DDGSEIIRGD NRDKSGMNGD FLCIKGRYAF DFTTREDRIT KPLVRQPNGQ LAEVSWEQAL
EHAGMKLREI RDTRGGSAIG VIGSTRTTNE EAYLLQKFAR TVLNTNNIDH HRTADYASFA
AALQGKAGRT ASLRDFLTAP AILLLGNDAT EQHPALAWNI RSNVRQNRAR LYVANHADIK
LHRQAKSFLQ IPQDGYAALV QYLAGNEAGF DGTEISAAFR EALRKEESLV IAFGSEFRGR
DIQSLVDFGL GLPNVKFAAL GDYANSRGAA DMGLMPDLLP GYVPLAAAKH FGEEYPSLPS
APGLDMLQMF DAAEAGNLGA LYVVGSNPVE RYGIDPTALK NTFLIVQDMF MTETAAVADV
IFPAANLYEK SGTVTNTYGD LQLAKKAADK AGVRTDFELI VRLADKMGAD PKKLVPFGRG
VRADMGQTRG AQSGEADRHA VWLAANNLEP KLSPFDPFAV FDEIQRLVPS YNVSRFELLG
GQDKQTRSDL VQIELDPARR DLVLPANDTL FTSGTLGRYS RMLHSVMESR TTKPAETAAD
//
