ID A0A2U3QEZ2_9BACT Unreviewed; 860 AA.
AC A0A2U3QEZ2;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Putative NADH-quinone oxidoreductase, subunit G (NuoG) {ECO:0000313|EMBL:SPP99954.1};
DE EC=1.6.5.11 {ECO:0000313|EMBL:SPP99954.1};
GN ORFNames=NBG4_140014 {ECO:0000313|EMBL:SPP99954.1};
OS Candidatus Sulfobium mesophilum.
OC Bacteria; Nitrospirota; Nitrospiria; Nitrospirales; Nitrospiraceae;
OC Sulfobium.
OX NCBI_TaxID=2016548 {ECO:0000313|EMBL:SPP99954.1, ECO:0000313|Proteomes:UP000245125};
RN [1] {ECO:0000313|Proteomes:UP000245125}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Zecchin S.;
RL Submitted (MAR-2018) 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}.
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DR EMBL; OUUY01000046; SPP99954.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2U3QEZ2; -.
DR OrthoDB; 9803192at2; -.
DR Proteomes; UP000245125; Unassembled WGS sequence.
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: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; 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; 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; IPR027467; MopterinOxRdtase_cofactor_BS.
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; PF12838; Fer4_7; 1.
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 PIRSF; PIRSF036643; FDH_alpha; 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; SSF50692; ADC-like; 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; 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.
DR PROSITE; PS00551; MOLYBDOPTERIN_PROK_1; 1.
PE 3: Inferred from homology;
KW 2Fe-2S {ECO:0000256|ARBA:ARBA00022714};
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 Oxidoreductase {ECO:0000313|EMBL:SPP99954.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000245125};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 1..78
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51085"
FT DOMAIN 78..117
FT /note="4Fe-4S His(Cys)3-ligated-type"
FT /evidence="ECO:0000259|PROSITE:PS51839"
FT DOMAIN 172..206
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 216..272
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
SQ SEQUENCE 860 AA; 94479 MW; 4C34A20770C94A13 CRC64;
MIKVTINGKE INLEKAMTVL EAARSAGIKI PTLCYHEQLE KYGGCRLCLV EVERMPRLQT
ACTLMVTDGM VVRTETEAIA NVRRSVLEFL LINHPLDCPY CDKAGECELQ DLVEKYGPAT
SRFKESKRKV TESLEDPVLV RNMERCIVCT RCVRMCEGVQ GAAAIAVIDR GGHSHIEPFS
GGKFDCEYCG NCVSVCPVGA IMSRLHRHSY RPWQLVSETE TICPYCGVGC TLVVQVRDDV
IKRVVPRIGT AVNNGLLCSR GRFGYEFVGH KDRLTAPLIK KDGVFEEATW EEAIRLIARR
LGEIKDTFGG SSIAGIASPR CTNEDNYVFQ KFMRVTLGSN NIDSTARTGY AGAQAFIENI
FGQGATANLI PGLSNSDAVV VAGGDPTAMN PILGLQIRAC ARKGGNILTI GHIKGLRHYT
PVELRPSLFS EDILLEGILS ALKDKKGLPG SNQILEGKIK DINLSSAEVT RVCGISEKDF
ALFIDKLSGA SNAAVVIGKE VVQSSGGSYR LLLLAAITYL INGRVYLLSE RANEQGLLDM
GCAPDLLPGY RPLGYAEFRK KYEIAWKSPL PEQPGLTIFE MIEAAKSGLL KAMYIMGENP
VFNMPNSKEV EAALKKVDFL IVQDIFLTES ARLADVVLPA LSWSEKNGTY TNMERRIQRL
RKAVTREGME DWRIVLEIAR NMGSKMNYED SENVFFEISR VSPLHRDLGY EEIEKGTAIY
PYKGEPLRSL TEEIRTEKGG SIESAGKLYL RLERPLFHSG TLSRKSQALV NIYAGAVARI
SPGTAGRLSL KDGDIIRISS GIGSLDLPLA VEKAVEDSVL MLTNNFEGRG AFSLMEYSID
PVTKAPVIDG NVVTVEKVGR
//
