NUOG_SALTY
ID NUOG_SALTY Reviewed; 908 AA.
AC P0A1Y4; P33900;
DT 01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 109.
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;
GN Name=nuoG; OrderedLocusNames=STM2323;
OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=99287;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=11677609; DOI=10.1038/35101614;
RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA Wilson R.K.;
RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL Nature 413:852-856(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-612.
RX PubMed=8234329; DOI=10.1073/pnas.90.21.9877;
RA Archer C.D., Wang X., Elliott T.;
RT "Mutants defective in the energy-conserving NADH dehydrogenase of
RT Salmonella typhimurium identified by a decrease in energy-dependent
RT proteolysis after carbon starvation.";
RL Proc. Natl. Acad. Sci. U.S.A. 90:9877-9881(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 612-908.
RC STRAIN=F98;
RX PubMed=9371470; DOI=10.1128/jb.179.22.7186-7190.1997;
RA Zhang-Barber L.Z., Turner A.K., Martin G., Fraenkel G., Dougan G.,
RA Barrow P.A.;
RT "Influence of genes encoding proton-translocating enzymes on suppression of
RT Salmonella typhimurium growth and colonization.";
RL J. Bacteriol. 179:7186-7190(1997).
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=AAA16063.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAL21224.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=L42521; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AE006468; AAL21224.1; ALT_INIT; Genomic_DNA.
DR EMBL; L22504; AAA16063.1; ALT_INIT; Unassigned_DNA.
DR EMBL; L42521; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; NP_461265.3; NC_003197.2.
DR AlphaFoldDB; P0A1Y4; -.
DR SMR; P0A1Y4; -.
DR STRING; 99287.STM2323; -.
DR PaxDb; P0A1Y4; -.
DR PRIDE; P0A1Y4; -.
DR EnsemblBacteria; AAL21224; AAL21224; STM2323.
DR GeneID; 1253845; -.
DR KEGG; stm:STM2323; -.
DR PATRIC; fig|99287.12.peg.2460; -.
DR HOGENOM; CLU_000422_11_4_6; -.
DR OMA; NVYFGRV; -.
DR PhylomeDB; P0A1Y4; -.
DR BioCyc; SENT99287:STM2323-MON; -.
DR Proteomes; UP000001014; Chromosome.
DR GO; GO:0045272; C:plasma membrane respiratory chain complex I; IBA:GO_Central.
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; IBA:GO_Central.
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 GO; GO:0045333; P:cellular respiration; IBA:GO_Central.
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 Reference proteome; 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_0000118554"
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:0000250"
FT BINDING 231
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 235
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 263
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT CONFLICT 678
FT /note="A -> V (in Ref. 3)"
FT /evidence="ECO:0000305"
FT CONFLICT 786
FT /note="I -> L (in Ref. 3)"
FT /evidence="ECO:0000305"
FT CONFLICT 847
FT /note="A -> T (in Ref. 3)"
FT /evidence="ECO:0000305"
FT CONFLICT 854
FT /note="A -> T (in Ref. 3)"
FT /evidence="ECO:0000305"
FT CONFLICT 888
FT /note="M -> I (in Ref. 3)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 908 AA; 100028 MW; 6A4BAB18E60C20EC CRC64;
MATIHVDGKE YEVNGADNLL QACLSLGLDI PYFCWHPALG SVGACRQCAV KQYQNAEDTR
GRLVMSCMTP ATDGTFISID DEEAKQFRES VVEWLMTNHP HDCPVCEEGG NCHLQDMTVM
TGHSFRRYRF TKRTHRNQDL GPFISHEMNR CIACYRCVRY YKDYADGTDL GVYGAHDNVY
FGRPEDGTLE SEFSGNLVEI CPTGVFTDKT HSERYNRKWD MQFAPSICQQ CSIGCNISPG
ERYGELRRIE NRYNGTVNHY FLCDRGRFGY GYVNLKDRPR QPVQRRGDDF ITLNAEQAMQ
GAADILRQSK KVIGIGSPRA SIESNFALRE LVGAENFYTG IARGEQERLQ LALKVLREGG
IYTPALREIE SYDAVLVLGE DVTQTGARVA LAVRQAVKGK AREMAAAQKV ADWQIAAILN
IGQRAKHPLF VTNVDDTRLD DIAAWTYRAP VEDQARLGFA IAHALDNTAP AVDGIDSDLQ
NKIDVIVQAL AGAKKPLIIS GTNAGSSEVI QAAANVAKAL KGRGADVGIT MIARSVNSMG
LGMMGGGSLD DALGELETGS ADAVVVLEND LHRHASATRV NAALAKAPLV MVVDHQRTAI
MENAHLVLSA ASFAESDGTV INNEGRAQRF FQVYDPAYYD NKTIMLESWR WLHSLHSTVE
NREVDWTQLD HVIDAVIAAM PQFAGIKDAA PDATFRIRGQ KLAREPHRYS GRTAMRANIS
VHEPRQPQDK DTMFAFSMEG NNQPTAPRSE IPFAWAPGWN SPQAWNKFQD EVGGKLRHGD
PGVRLIEATE GGLDYFTTVP ASFQAQDGQW RIAPYYHLFG SDELSQRSPV FQSRMPQPYI
KLNPADAAKL GVNAGTRVSF SYDGNTVTLP VEISEGLAAG QVGLPMGMPG IAPVLAGARL
EDLREAQQ
