ID A0A0E3Y8I1_9ENTR Unreviewed; 918 AA.
AC A0A0E3Y8I1;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 27-MAR-2024, entry version 37.
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:AKC60050.1};
GN ORFNames=BTURN675_482 {ECO:0000313|EMBL:AKC60050.1};
OS Blochmannia endosymbiont of Polyrhachis (Hedomyrma) turneri.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; ant endosymbionts; Blochmannia.
OX NCBI_TaxID=1505596 {ECO:0000313|EMBL:AKC60050.1, ECO:0000313|Proteomes:UP000033094};
RN [1] {ECO:0000313|EMBL:AKC60050.1, ECO:0000313|Proteomes:UP000033094}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=675 {ECO:0000313|EMBL:AKC60050.1,
RC ECO:0000313|Proteomes:UP000033094};
RX PubMed=25861561;
RA Williams L.E., Wernegreen J.J.;
RT "Genome evolution in an ancient bacteria-ant symbiosis: parallel gene loss
RT among Blochmannia spanning the origin of the ant tribe Camponotini.";
RL PeerJ 3:E881-E881(2015).
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}.
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DR EMBL; CP010048; AKC60050.1; -; Genomic_DNA.
DR RefSeq; WP_046288945.1; NZ_CP010048.1.
DR AlphaFoldDB; A0A0E3Y8I1; -.
DR STRING; 1505596.BTURN675_482; -.
DR KEGG; bed:BTURN675_482; -.
DR PATRIC; fig|1505596.4.peg.493; -.
DR HOGENOM; CLU_000422_11_4_6; -.
DR OrthoDB; 9810782at2; -.
DR Proteomes; UP000033094; Chromosome.
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: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 CDD; cd02788; MopB_CT_NDH-1_NuoG2-N7; 1.
DR CDD; cd02771; MopB_NDH-1_NuoG2-N7; 1.
DR Gene3D; 3.10.20.740; -; 1.
DR Gene3D; 3.30.200.210; -; 1.
DR Gene3D; 3.40.50.740; -; 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:SF13; NADH-UBIQUINONE OXIDOREDUCTASE 75 KDA SUBUNIT, MITOCHONDRIAL; 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 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; PS00643; COMPLEX1_75K_3; 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:ARBA00022485};
KW NAD {ECO:0000256|ARBA:ARBA00023027};
KW Quinone {ECO:0000256|ARBA:ARBA00022719};
KW Reference proteome {ECO:0000313|Proteomes:UP000033094};
KW Translocase {ECO:0000256|ARBA:ARBA00022967}.
FT DOMAIN 1..82
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51085"
FT DOMAIN 82..121
FT /note="4Fe-4S His(Cys)3-ligated-type"
FT /evidence="ECO:0000259|PROSITE:PS51839"
FT DOMAIN 220..276
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
SQ SEQUENCE 918 AA; 103889 MW; 9585A5970ABDC2B2 CRC64;
MVSIYIDNKK YCVGESYNLL EVCLSLGLNI PYFCWHPALG SVGSCRQCAV KQYSSDSKSG
RIVMACMTPV VDGLVISIND IEVKEFRETI LELLMINHPH DCPVCSEGGH CHLQDMTVMV
GHYVRRYRFM KRTHVNQYLG PFIAHEMNRC ISCYRCVRYY KDYADGFDFD VYGVHDNLYF
GRFQEGKLES EFSGNLVEIC PTGVFTDKTS SQYYSRKWDM QFSPSICVHC SVGCNIILGE
RYGKICRVDN RYNGSINGYF LCDRGRFGYD YVNNMESRFK KPLHRKDKKN WIELNEEQAI
AAGVKILRIS NKVIGIGSPR ASVESNFALM DLVGADNFYF GINRFEHRVL LLIFNILQNS
GIYIASIKDI EAADAIFLLG EDVTQTSARI ALAIRQSVKG GMLNVAKDKN IPIWHMNAVR
SLASNTNFLF ITNVDKTKLD DVAFWTYYAS LNDQARFGFA VASVLDNTAP TVNDFDNNLI
NKVHMVAQAL LKAKRPVIIS GSNVGNESII SAAANIAKSL KNCGKHVSIN LVVSEVNSIG
LAMMNGGGSL DDALDVSKDN KIDSVIVLES DLCRHLSFKR VESFLRRINH LIVLDHQRLS
FHKHANLVFS VTSVPESDGT LINQEGRAQR FFRVYNPNYY DSSLLIFESW RWLYKLRAVF
CSQNQMRYLN FDDVVDRVVL NLPELSKIRL AAPHASFRIF GQKLSRAPSR YSGRTSYGTD
INVHEPRVCQ DEDSMFSFSM EGNNIPNFGR QHIAFVWSPG WNSPQAWNKF HSGVGNFMDS
GVRIFDHSVK NERRGIDWFV NVPIVSSSLS SNSINISNNM WYVVPYWHIF GSEELSQRSL
SIQKCITNPY VVLSQSDGIQ FGLYDKNILV ITCGDHKLSL PLVFSNKLTS GYIGLPIGLP
GISHFYLGMY ITNIEGKF
//
