NUOG_BUCAI
ID NUOG_BUCAI Reviewed; 906 AA.
AC P57257;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2000, sequence version 1.
DT 03-AUG-2022, entry version 120.
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=BU159;
OS Buchnera aphidicola subsp. Acyrthosiphon pisum (strain APS) (Acyrthosiphon
OS pisum symbiotic bacterium).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Buchnera.
OX NCBI_TaxID=107806;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=APS;
RX PubMed=10993077; DOI=10.1038/35024074;
RA Shigenobu S., Watanabe H., Hattori M., Sakaki Y., Ishikawa H.;
RT "Genome sequence of the endocellular bacterial symbiont of aphids Buchnera
RT sp. APS.";
RL Nature 407:81-86(2000).
CC -!- FUNCTION: NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur
CC (Fe-S) centers, to quinones in the respiratory chain. Couples the redox
CC reaction to proton translocation (for every two electrons transferred,
CC four hydrogen ions are translocated across the cytoplasmic membrane),
CC and thus conserves the redox energy in a proton gradient (By
CC 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 (By similarity).
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the complex I 75 kDa subunit family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BA000003; BAB12877.1; -; Genomic_DNA.
DR RefSeq; NP_239991.1; NC_002528.1.
DR RefSeq; WP_010895977.1; NC_002528.1.
DR AlphaFoldDB; P57257; -.
DR SMR; P57257; -.
DR STRING; 107806.10038842; -.
DR PRIDE; P57257; -.
DR EnsemblBacteria; BAB12877; BAB12877; BAB12877.
DR KEGG; buc:BU159; -.
DR PATRIC; fig|107806.10.peg.169; -.
DR eggNOG; COG1034; Bacteria.
DR HOGENOM; CLU_000422_11_4_6; -.
DR OMA; NVYFGRV; -.
DR Proteomes; UP000001806; Chromosome.
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; 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; 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.
FT CHAIN 1..906
FT /note="NADH-quinone oxidoreductase subunit G"
FT /id="PRO_0000118542"
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: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 906 AA; 103761 MW; A1CBA1210C087A54 CRC64;
MAKIYVDSKI YNVNESDNLL QACLSVGINI PYFCWHPLLG SLGACRQCAV TQYDNFQDRK
GRLIMSCMTP VTDGAIISIK STESEVFRSA IVELLLTNHP HDCPVCEEGG HCHLQDMTVM
VKHSMRNYRF KKRTHKNQYL GPFIKHEMNR CIACYRCVRY YNEYADGVDF GVYGSNNNVY
FGRIEDGVLE SEHSGNLIEL CPTGVFTDKT HSKKYNRKWD MQYAPGICHN CSVGCNISIG
ERYGEIRRIE NRYHENINHY LICDLGRFGY SHTNLNTRPK KPTYVNKYND LNVLNFNEAI
KIGVDFFKRY KRVIGVGSAR SSIENNFALQ ELVGKENFSN GMSNKEKECI KSILEFLKNN
YIYIPSLKEI ESYDVILVLG EDLTQTSSRV ALAVRQAVKK KVQDIKNLYG IPKWNTSSNI
HISEKFKNSL YIMHTHESKL DDISEWSYFA SIDKQVNLAS SIAYEIDKSS PKVSNLDSEL
KEKVLLISDR LISSKKTLII SGSHSFSDSI IKASINIAKA IKFRAPDHHV GVTLLTSSVN
SLGAELLGGM SIESALDDLK KEKADAVIFM EYDLYRSVSE YDCEYFFKNK DNIITLDHQY
TQTFKKSMLS LPSTNFTESS GTVINFEGRA QRFFQVYDPN FYDKSNCLCD SWKWLHTIKS
KINNTEICWF NLDDVINSYA EKYSIFKQIK TNELNSNLRI HGQKISRSPI RSSGRTSLRS
NIDVHEPCQP KDINTMFAFS MEGYNQPNSS VSNIPFAWFP GWNSPQAWNK FQVEVGRNLI
SGDSGIHIFK KYEKKTDVYS NIVLKNSIKE KYWNIIPYYH LFGNEELTQY SSIIQENTPL
EYALIGLSDA IKMGLKKDSI VEFNCLKKDY CLPVQVSKYL TEKQIGLPIG RKGFPLALVG
EKIEFL
