NUOG_ECOL6
ID NUOG_ECOL6 Reviewed; 908 AA.
AC Q8FFJ9;
DT 28-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=NADH-quinone oxidoreductase subunit G;
DE EC=7.1.1.-;
DE AltName: Full=NADH dehydrogenase I subunit G;
DE AltName: Full=NDH-1 subunit G;
DE AltName: Full=NUO7;
GN Name=nuoG; OrderedLocusNames=c2824;
OS Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=199310;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CFT073 / ATCC 700928 / UPEC;
RX PubMed=12471157; DOI=10.1073/pnas.252529799;
RA Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P., Rasko D.,
RA Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., Mayhew G.F.,
RA Rose D.J., Zhou S., Schwartz D.C., Perna N.T., Mobley H.L.T.,
RA Donnenberg M.S., Blattner F.R.;
RT "Extensive mosaic structure revealed by the complete genome sequence of
RT uropathogenic Escherichia coli.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002).
CC -!- FUNCTION: NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur
CC (Fe-S) centers, to quinones in the respiratory chain. The immediate
CC electron acceptor for the enzyme in this species is believed to be
CC ubiquinone. Couples the redox reaction to proton translocation (for
CC every two electrons transferred, four hydrogen ions are translocated
CC across the cytoplasmic membrane), and thus conserves the redox energy
CC in a proton gradient (By similarity). {ECO:0000250}.
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 -!- COFACTOR:
CC Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135; Evidence={ECO:0000250};
CC Note=Binds 1 [2Fe-2S] cluster per subunit. {ECO:0000250};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Evidence={ECO:0000250};
CC Note=Binds 3 [4Fe-4S] clusters per subunit. {ECO:0000250};
CC -!- SUBUNIT: Composed of 13 different subunits. Subunits NuoCD, E, F, and G
CC constitute the peripheral sector of the complex.
CC -!- SIMILARITY: Belongs to the complex I 75 kDa subunit family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAN81278.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AE014075; AAN81278.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_024182245.1; NC_004431.1.
DR AlphaFoldDB; Q8FFJ9; -.
DR SMR; Q8FFJ9; -.
DR STRING; 199310.c2824; -.
DR PRIDE; Q8FFJ9; -.
DR DNASU; 1038363; -.
DR EnsemblBacteria; AAN81278; AAN81278; c2824.
DR KEGG; ecc:c2824; -.
DR eggNOG; COG1034; Bacteria.
DR HOGENOM; CLU_000422_11_4_6; -.
DR OMA; NVYFGRV; -.
DR Proteomes; UP000001410; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:InterPro.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
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:0043546; F:molybdopterin cofactor binding; IEA:InterPro.
DR GO; GO:0008137; F:NADH dehydrogenase (ubiquinone) activity; IEA:InterPro.
DR GO; GO:0048038; F:quinone binding; IEA:UniProtKB-KW.
DR GO; GO:0042773; P:ATP synthesis coupled electron transport; IEA:InterPro.
DR CDD; cd00207; fer2; 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; IPR000283; NADH_UbQ_OxRdtase_75kDa_su_CS.
DR InterPro; IPR010228; NADH_UbQ_OxRdtase_Gsu.
DR InterPro; IPR019574; NADH_UbQ_OxRdtase_Gsu_4Fe4S-bd.
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 SMART; SM00926; Molybdop_Fe4S4; 1.
DR SMART; SM00929; NADH-G_4Fe-4S_3; 1.
DR SUPFAM; SSF50692; SSF50692; 1.
DR SUPFAM; SSF54292; SSF54292; 1.
DR TIGRFAMs; TIGR01973; NuoG; 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; 4Fe-4S; Iron; Iron-sulfur; Metal-binding; NAD; Quinone;
KW Translocase; Ubiquinone.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..908
FT /note="NADH-quinone oxidoreductase subunit G"
FT /id="PRO_0000118548"
FT DOMAIN 2..83
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT DOMAIN 83..122
FT /note="4Fe-4S His(Cys)3-ligated-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01184"
FT DOMAIN 221..277
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01004"
FT BINDING 34
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000250"
FT BINDING 45
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000250"
FT BINDING 48
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000250"
FT BINDING 67
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000250"
FT BINDING 99
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01184"
FT BINDING 103
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01184"
FT BINDING 106
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01184"
FT BINDING 112
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01184"
FT BINDING 151
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 154
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 157
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 201
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 228
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000255"
FT BINDING 231
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000255"
FT BINDING 235
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000255"
FT BINDING 263
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000255"
SQ SEQUENCE 908 AA; 100351 MW; 5A7E1A01344A96B4 CRC64;
MATIHVDGKE YEVNGADNLL EACLSLGLDI PYFCWHPALG SVGACRQCAV KQYQNAEDTR
GRLVMSCMTP ASDGTFISID DEEAKQFRES VVEWLMTNHP HDCPVCEEGG NCHLQDMTVM
TGHSFRRYRF TKRTHRNQDL GPFISHEMNR CIACYRCVRY YKDYADGTDL GVYGAHDNVY
FGRPEDGTLE SEFSGNLVEI CPTGVFTDKT HSERYNRKWD MQFAPSICQQ CSIGCNISPG
ERYGELRRIE NRYNGTVNHY FLCDRGRFGY GYVNLKDRPR QPVQRRGDDF ITLNAEQAMQ
GAADILRQSK KVIGIGSPRA SVESNFALRE LVGEENFYTG IAHGEQERLQ LALKVLREGG
IYTPALREIE SYDAVLVLGE DVTQTGARVA LAVRQAVKGK AREMAAAQKV ADWQIAAILN
IGQRAKHPLF VTNVDDTRLD DIAAWTYRAP VEDQARLGFA IAHALDNSAP AVDGIEPELQ
SKIDVIVQAL AGAKKPLIIS GTNTGSAEVI QAAANVAKAL KGRGADVGIT MIARSVNSMG
LGIMGGGSLE EALTELETGR ADAVVVLEND LHRHASATRV NAALAKAPLV MVVDHQRTAI
MENAHLVLSA ASFAESDGTV INNEGRAQRF FQVYDPAYYD SQTVMLESWR WLHSLHSTLL
SREVDWTQLD HVIDAVVAKI PELAGIKDAA PDATFRIRGQ KLAREPHRYS GRTAMRANIS
VHEPRQPQDI DTMFTFSMEG NNQPTAHRSQ VPFAWAPGWN SPQAWNKFQD EVGGKLRFGD
PGVRLFETSE NSLDYFTSVP ARFQPQDGKW RIAPYYHLFG SDELSQRAPV FQSRMPQPYI
KLNPADAAKL GVNAGTRVSF SYDGNMVTLP VEISEGLTAG QVGLPMGMSG IAPVLAGAHL
EDLKEAQQ
