ID A0A5R9PH34_9GAMM Unreviewed; 744 AA.
AC A0A5R9PH34;
DT 26-FEB-2020, integrated into UniProtKB/TrEMBL.
DT 26-FEB-2020, sequence version 1.
DT 27-MAR-2024, entry version 14.
DE RecName: Full=NADH-quinone oxidoreductase subunit G {ECO:0000256|ARBA:ARBA00019902};
DE AltName: Full=NADH dehydrogenase I subunit G {ECO:0000256|ARBA:ARBA00031577};
DE AltName: Full=NDH-1 subunit G {ECO:0000256|ARBA:ARBA00032783};
GN Name=nuoG {ECO:0000313|EMBL:TLX22313.1};
GN ORFNames=E5S66_07325 {ECO:0000313|EMBL:TLX22313.1};
OS Thermomonas fusca.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Thermomonas.
OX NCBI_TaxID=215690 {ECO:0000313|EMBL:TLX22313.1, ECO:0000313|Proteomes:UP000308508};
RN [1] {ECO:0000313|EMBL:TLX22313.1, ECO:0000313|Proteomes:UP000308508}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SHC 3-19 {ECO:0000313|EMBL:TLX22313.1,
RC ECO:0000313|Proteomes:UP000308508};
RA Grouzdev D.S., Nazina T.N.;
RL Submitted (APR-2019) 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. 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. {ECO:0000256|ARBA:ARBA00002378}.
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 -!- SUBUNIT: Composed of 13 different subunits. Subunits NuoCD, E, F, and G
CC constitute the peripheral sector of the complex.
CC {ECO:0000256|ARBA:ARBA00026021}.
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:TLX22313.1}.
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DR EMBL; SROY01000002; TLX22313.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A5R9PH34; -.
DR STRING; 1123377.GCA_000423885_00271; -.
DR Proteomes; UP000308508; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProt.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IEA:UniProt.
DR GO; GO:0016020; C:membrane; IEA:InterPro.
DR GO; GO:1990204; C:oxidoreductase complex; IEA:UniProt.
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:0042773; P:ATP synthesis coupled electron transport; IEA:InterPro.
DR CDD; cd00207; fer2; 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; -; 2.
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; 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:SF13; NADH-UBIQUINONE OXIDOREDUCTASE 75 KDA SUBUNIT, MITOCHONDRIAL; 1.
DR PANTHER; PTHR43105; RESPIRATORY NITRATE REDUCTASE; 1.
DR Pfam; PF13510; Fer2_4; 1.
DR Pfam; PF00384; Molybdopterin; 1.
DR Pfam; PF01568; Molydop_binding; 1.
DR Pfam; PF10588; NADH-G_4Fe-4S_3; 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; 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:ARBA00022485};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00022485};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW NAD {ECO:0000256|ARBA:ARBA00023027};
KW Oxidoreductase {ECO:0000313|EMBL:TLX22313.1};
KW Translocase {ECO:0000256|ARBA:ARBA00022967}.
FT DOMAIN 13..95
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51085"
FT DOMAIN 95..134
FT /note="4Fe-4S His(Cys)3-ligated-type"
FT /evidence="ECO:0000259|PROSITE:PS51839"
SQ SEQUENCE 744 AA; 78021 MW; 7D625EEB4AAF0A5F CRC64;
MSAQPVNPNL PPDHVTVFID GVEMAAPKGS MIIQAADKAG VPIPRFCYHE KLPIAANCRM
CLVDTEVGGR AAPKPSPACA TPVMDGMKVF TRNEKALKAQ RNVMEFLLIN HPLDCPVCDQ
GGECELQDLS LGYGRSVNRF VERKRAVADE DLGPLVASEM TRCIHCTRCI RVTAEIAGTY
ELGGMYRGEN LQIGTYDGKP LTTELSGNVI DVCPVGALTN KVFRFKARPW ELTARPSLGY
HDALGSNLFH HVRRGDLLRS VPRDNEAVNE CWLSDRDRYA HEGLAAADRA SVPLIRDGEG
FREASWEEAL AMASQILRDN AGDALGVLAH PATSNEEGAL LARMASGLGS GNLDHRIGQL
DLSDGAAAEA FGMPVAEIES ADAIIIVGSN VRHEVPLLHQ RIRKAFKKGA KIHVVNPVDF
DFTFSIASKA IVPPSQLAAA LAGVDVGDAG NIAVIVGGVA ENGPHAAAIR KAAADFAAAR
NARLCRIPQG ANALGLSRLG VLPTARDAQS MLREPRKAYV IYGIEPGLDF ADQQLALKAL
GGAQVVAFSQ FACQSTRAVA DVILPIGALP EIDATLTNLD GIQQQAVAAG KLPGLAHSGW
RVLRALGGDL ALPGFEFTDL AGLRAGLAPK AVQVAKGAPA SMAGNGLEVA ASAAIYRVDA
VIRRCDALQA HPLTTGPRAA LNPADAAALG LAEGVMAKCA TAAGTATLQV ALDPRVAPGS
VWVESGYGAT APLLAAAKLE VARA
//
