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 01-MAY-2013, entry version 83.
DE RecName: Full=NADH-quinone oxidoreductase subunit G;
DE EC=1.6.99.5;
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)
OS (Acyrthosiphon pisum symbiotic bacterium).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC Enterobacteriaceae; 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
RT Buchnera sp. APS.";
RL Nature 407:81-86(2000).
CC -!- FUNCTION: NDH-1 shuttles electrons from NADH, via FMN and iron-
CC sulfur (Fe-S) centers, to quinones in the respiratory chain.
CC Couples the redox reaction to proton translocation (for every two
CC electrons transferred, four hydrogen ions are translocated across
CC the cytoplasmic membrane), and thus conserves the redox energy in
CC a proton gradient (By similarity).
CC -!- CATALYTIC ACTIVITY: NADH + quinone = NAD(+) + quinol.
CC -!- COFACTOR: Binds 1 2Fe-2S cluster per subunit (By similarity).
CC -!- COFACTOR: Binds 3 4Fe-4S clusters per subunit (By similarity).
CC -!- SUBUNIT: Composed of 13 different subunits. Subunits NuoCD, E, F,
CC and G constitute the peripheral sector of the complex (By
CC similarity).
CC -!- SIMILARITY: Belongs to the complex I 75 kDa subunit family.
CC -!- SIMILARITY: Contains 1 2Fe-2S ferredoxin-type domain.
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DR EMBL; BA000003; BAB12877.1; -; Genomic_DNA.
DR RefSeq; NP_239991.1; NC_002528.1.
DR ProteinModelPortal; P57257; -.
DR EnsemblBacteria; BAB12877; BAB12877; BAB12877.
DR GeneID; 1109603; -.
DR KEGG; buc:BU159; -.
DR PATRIC; 21243834; VBIBucAph127364_0169.
DR eggNOG; COG1034; -.
DR HOGENOM; HOG000276177; -.
DR KO; K00336; -.
DR OMA; SVNHYFL; -.
DR ProtClustDB; PRK08166; -.
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:0009055; F:electron carrier activity; IEA:InterPro.
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 Gene3D; 3.10.20.30; -; 1.
DR InterPro; IPR001041; 2Fe-2S_ferredoxin-type.
DR InterPro; IPR012675; Beta-grasp_dom.
DR InterPro; IPR006656; Mopterin_OxRdtase.
DR InterPro; IPR006963; Mopterin_OxRdtase_Fe4S4_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; Ferredoxin; 1.
DR TIGRFAMs; TIGR01973; NuoG; 1.
DR PROSITE; PS00197; 2FE2S_FER_1; FALSE_NEG.
DR PROSITE; PS51085; 2FE2S_FER_2; 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; Complete proteome; Iron; Iron-sulfur; Metal-binding;
KW NAD; Oxidoreductase; Quinone; Reference proteome.
FT CHAIN 1 906 NADH-quinone oxidoreductase subunit G.
FT /FTId=PRO_0000118542.
FT DOMAIN 2 83 2Fe-2S ferredoxin-type.
FT METAL 34 34 Iron-sulfur 1 (2Fe-2S) (By similarity).
FT METAL 45 45 Iron-sulfur 1 (2Fe-2S) (By similarity).
FT METAL 48 48 Iron-sulfur 1 (2Fe-2S) (By similarity).
FT METAL 67 67 Iron-sulfur 1 (2Fe-2S) (By similarity).
FT METAL 99 99 Iron-sulfur 2 (4Fe-4S); via pros nitrogen
FT (By similarity).
FT METAL 103 103 Iron-sulfur 2 (4Fe-4S) (By similarity).
FT METAL 106 106 Iron-sulfur 2 (4Fe-4S) (By similarity).
FT METAL 112 112 Iron-sulfur 2 (4Fe-4S) (By similarity).
FT METAL 151 151 Iron-sulfur 3 (4Fe-4S) (By similarity).
FT METAL 154 154 Iron-sulfur 3 (4Fe-4S) (By similarity).
FT METAL 157 157 Iron-sulfur 3 (4Fe-4S) (By similarity).
FT METAL 201 201 Iron-sulfur 3 (4Fe-4S) (By similarity).
FT METAL 228 228 Iron-sulfur 4 (4Fe-4S) (Potential).
FT METAL 231 231 Iron-sulfur 4 (4Fe-4S) (Potential).
FT METAL 235 235 Iron-sulfur 4 (4Fe-4S) (Potential).
FT METAL 263 263 Iron-sulfur 4 (4Fe-4S) (Potential).
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
//
