NUOG_PSEFL
ID NUOG_PSEFL Reviewed; 904 AA.
AC Q9KGW3;
DT 28-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 97.
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;
OS Pseudomonas fluorescens.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=294;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND INDUCTION.
RC STRAIN=WCS365;
RX PubMed=12118882; DOI=10.1094/mpmi.2002.15.7.662;
RA Camacho-Carvajal M.M., Wijfjes A.H.M., Mulders I.H.M., Lugtenberg B.J.J.,
RA Bloemberg G.V.;
RT "Characterization of NADH dehydrogenases of Pseudomonas fluorescens WCS365
RT and their role in competitive root colonization.";
RL Mol. Plant Microbe Interact. 15:662-671(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). Required for plants roots
CC colonization. {ECO:0000250, ECO:0000269|PubMed:12118882}.
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 -!- INDUCTION: By low oxygen growth conditions, especially in rhizosphere.
CC {ECO:0000269|PubMed:12118882}.
CC -!- SIMILARITY: Belongs to the complex I 75 kDa subunit family.
CC {ECO:0000305}.
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DR EMBL; AF281148; AAF97803.1; -; Genomic_DNA.
DR RefSeq; WP_003203377.1; NZ_QQAQ01000007.1.
DR AlphaFoldDB; Q9KGW3; -.
DR SMR; Q9KGW3; -.
DR STRING; 690597.JH730963_gene2517; -.
DR GeneID; 57260309; -.
DR PATRIC; fig|294.126.peg.2748; -.
DR eggNOG; COG1034; Bacteria.
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: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; 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; 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 2: Evidence at transcript level;
KW 2Fe-2S; 4Fe-4S; Iron; Iron-sulfur; Metal-binding; NAD; Quinone;
KW Translocase; Ubiquinone.
FT CHAIN 1..904
FT /note="NADH-quinone oxidoreductase subunit G"
FT /id="PRO_0000118550"
FT DOMAIN 1..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 904 AA; 98158 MW; C25E86C6D4DFA457 CRC64;
MATIHVDGKE LEVDGADNLL QACLSLGLDI PYFCWHPALG SVGACRQCAV KQYTDENDKR
GRIVMSCMTP ATDGSWISID DEEAKVFRAS VVEWLMTNHP HDCPVCEEGG HCHLQDMTVM
TGHNERRYRF TKRTHQNQDL GPFISHEMNR CIACYRCVRF YKDYAGGTDL GVFGAHDNVY
FGRVEDGTLE SEFSGNLTEV CPTGVFTDKT HSERYNRKWD MQFSPSICHG CSSGCNISPG
ERYGELRRIE NRFNGSVNQY FLCDRGRFGY GYVNRKDRPR QPLLANGAKL SLDQALDKAA
ELLRGRNIVG IGSPRASLES NYALRELVGA EHFYSGIEAG ELERIRLVLQ VLKDSPLPVP
NMRDIEDHDA VFVLGEDLTQ TAARMALALR QSVKGKAEDM ADAMRVQPWL DAAVKNIGQH
ALNPLFIASL AETKLDDVAE ECVHAAPDDL ARIGFAVAHA LDASAPAVDG LDSEAAALAQ
RIADALLAAK RPLIIAGTSL GSKALIEAAA NIAKALKLRE KNGSISLIVP EANSLGLAML
GGESVDAALQ AVIDGSADAI VVLENDLYTR TDKAKVDAAL NAAKVLIVAD HQKTATTDRA
HLVLPAASFA EGDGTLVSQE GRAQRFFQVF DPQYLDASIL VHEGWRWLHA LRATLLDQPI
DWTQLDHVTA AVASSSPQLA AIVDAAPSAS FRIKGLKLAR EPLRYSGRTA MRADISVHEP
RTSQDNDTAF SFSMEGYSGS TEPRSQVPFA WSPGWNSPQA WNKFQDEVGG HLRAGDPGTR
LIESQGDHLS WFASVPRAFN PAPGTWQVVP FHHLFGSEEN SSKAAPVQER IPAAYVSLAK
SEADRLGVND GALLSLNVAG QTLRLPLRIN EELGAGLVAL PAGLAGIPPA IFGKTVDGLQ
EAAQ
