GenomeNet

Database: UniProt
Entry: P57257
LinkDB: P57257
Original site: P57257 
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-OCT-2014, entry version 89.
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). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY: NADH + quinone = NAD(+) + quinol.
CC   -!- COFACTOR: Binds 1 2Fe-2S cluster per subunit. {ECO:0000250}.
CC   -!- COFACTOR: Binds 3 4Fe-4S clusters per subunit. {ECO:0000250}.
CC   -!- SUBUNIT: Composed of 13 different subunits. Subunits NuoCD, E, F,
CC       and G constitute the peripheral sector of the complex (By
CC       similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the complex I 75 kDa subunit family.
CC       {ECO:0000305}.
CC   -!- SIMILARITY: Contains 1 2Fe-2S ferredoxin-type domain.
CC       {ECO:0000255|PROSITE-ProRule:PRU00465}.
CC   -!- SIMILARITY: Contains 1 4Fe-4S Mo/W bis-MGD-type domain.
CC       {ECO:0000255|PROSITE-ProRule:PRU01004}.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
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; GYGYVNR; -.
DR   OrthoDB; EOG6CVV7G; -.
DR   BioCyc; BAPH107806:GBZJ-159-MONOMER; -.
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_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; 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; 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                                {ECO:0000255|PROSITE-ProRule:PRU00465}.
FT   DOMAIN      221    277       4Fe-4S Mo/W bis-MGD-type.
FT                                {ECO:0000255|PROSITE-ProRule:PRU01004}.
FT   METAL        34     34       Iron-sulfur 1 (2Fe-2S). {ECO:0000250}.
FT   METAL        45     45       Iron-sulfur 1 (2Fe-2S). {ECO:0000250}.
FT   METAL        48     48       Iron-sulfur 1 (2Fe-2S). {ECO:0000250}.
FT   METAL        67     67       Iron-sulfur 1 (2Fe-2S). {ECO:0000250}.
FT   METAL        99     99       Iron-sulfur 2 (4Fe-4S); via pros
FT                                nitrogen. {ECO:0000250}.
FT   METAL       103    103       Iron-sulfur 2 (4Fe-4S). {ECO:0000250}.
FT   METAL       106    106       Iron-sulfur 2 (4Fe-4S). {ECO:0000250}.
FT   METAL       112    112       Iron-sulfur 2 (4Fe-4S). {ECO:0000250}.
FT   METAL       151    151       Iron-sulfur 3 (4Fe-4S). {ECO:0000250}.
FT   METAL       154    154       Iron-sulfur 3 (4Fe-4S). {ECO:0000250}.
FT   METAL       157    157       Iron-sulfur 3 (4Fe-4S). {ECO:0000250}.
FT   METAL       201    201       Iron-sulfur 3 (4Fe-4S). {ECO:0000250}.
FT   METAL       228    228       Iron-sulfur 4 (4Fe-4S). {ECO:0000255}.
FT   METAL       231    231       Iron-sulfur 4 (4Fe-4S). {ECO:0000255}.
FT   METAL       235    235       Iron-sulfur 4 (4Fe-4S). {ECO:0000255}.
FT   METAL       263    263       Iron-sulfur 4 (4Fe-4S). {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
//
DBGET integrated database retrieval system