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Database: UniProt
Entry: P56914
LinkDB: P56914
Original site: P56914 
ID   NUOG2_RHIME             Reviewed;         853 AA.
AC   P56914;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   02-NOV-2001, sequence version 2.
DT   19-FEB-2014, entry version 104.
DE   RecName: Full=NADH-quinone oxidoreductase subunit G 2;
DE            EC=1.6.99.5;
DE   AltName: Full=NADH dehydrogenase I subunit G 2;
DE   AltName: Full=NDH-1 subunit G 2;
GN   Name=nuoG2; OrderedLocusNames=RA0828; ORFNames=SMa1523;
OS   Rhizobium meliloti (strain 1021) (Ensifer meliloti) (Sinorhizobium
OS   meliloti).
OG   Plasmid pSymA (megaplasmid 1).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX   NCBI_TaxID=266834;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=41;
RA   Putnoky P., Jady B., Chellapilla K.P., Barta F., Kiss E.;
RT   "Rhizobium meliloti carries two sets of nuo genes.";
RL   Submitted (JUL-1999) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1021;
RX   PubMed=11481432; DOI=10.1073/pnas.161294798;
RA   Barnett M.J., Fisher R.F., Jones T., Komp C., Abola A.P.,
RA   Barloy-Hubler F., Bowser L., Capela D., Galibert F., Gouzy J.,
RA   Gurjal M., Hong A., Huizar L., Hyman R.W., Kahn D., Kahn M.L.,
RA   Kalman S., Keating D.H., Palm C., Peck M.C., Surzycki R., Wells D.H.,
RA   Yeh K.-C., Davis R.W., Federspiel N.A., Long S.R.;
RT   "Nucleotide sequence and predicted functions of the entire
RT   Sinorhizobium meliloti pSymA megaplasmid.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:9883-9888(2001).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1021;
RX   PubMed=11474104; DOI=10.1126/science.1060966;
RA   Galibert F., Finan T.M., Long S.R., Puehler A., Abola P., Ampe F.,
RA   Barloy-Hubler F., Barnett M.J., Becker A., Boistard P., Bothe G.,
RA   Boutry M., Bowser L., Buhrmester J., Cadieu E., Capela D., Chain P.,
RA   Cowie A., Davis R.W., Dreano S., Federspiel N.A., Fisher R.F.,
RA   Gloux S., Godrie T., Goffeau A., Golding B., Gouzy J., Gurjal M.,
RA   Hernandez-Lucas I., Hong A., Huizar L., Hyman R.W., Jones T., Kahn D.,
RA   Kahn M.L., Kalman S., Keating D.H., Kiss E., Komp C., Lelaure V.,
RA   Masuy D., Palm C., Peck M.C., Pohl T.M., Portetelle D., Purnelle B.,
RA   Ramsperger U., Surzycki R., Thebault P., Vandenbol M.,
RA   Vorhoelter F.J., Weidner S., Wells D.H., Wong K., Yeh K.-C., Batut J.;
RT   "The composite genome of the legume symbiont Sinorhizobium meliloti.";
RL   Science 293:668-672(2001).
CC   -!- FUNCTION: NDH-1 shuttles electrons from NADH, via FMN and iron-
CC       sulfur (Fe-S) centers, to quinones in the respiratory chain. The
CC       immediate electron acceptor for the enzyme in this species is
CC       believed to be ubiquinone. Couples the redox reaction to proton
CC       translocation (for every two electrons transferred, four hydrogen
CC       ions are translocated across the cytoplasmic membrane), and thus
CC       conserves the redox energy in 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   -!- SIMILARITY: Belongs to the complex I 75 kDa subunit family.
CC   -!- SIMILARITY: Contains 1 2Fe-2S ferredoxin-type domain.
CC   -!- SIMILARITY: Contains 2 4Fe-4S ferredoxin-type domains.
CC   -!- SIMILARITY: Contains 1 4Fe-4S Mo/W bis-MGD-type domain.
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DR   EMBL; AJ245399; CAB51635.1; -; Genomic_DNA.
DR   EMBL; AE006469; AAK65486.1; -; Genomic_DNA.
DR   PIR; D95365; D95365.
DR   RefSeq; NP_436074.1; NC_003037.1.
DR   ProteinModelPortal; P56914; -.
DR   STRING; 266834.SMa1523; -.
DR   EnsemblBacteria; AAK65486; AAK65486; SMa1523.
DR   GeneID; 1235864; -.
DR   KEGG; sme:SMa1523; -.
DR   PATRIC; 23628160; VBISinMel96828_0859.
DR   eggNOG; COG3383; -.
DR   HOGENOM; HOG000031440; -.
DR   KO; K00336; -.
DR   OMA; PENYRAL; -.
DR   OrthoDB; EOG6CVV7G; -.
DR   ProtClustDB; CLSK807690; -.
DR   BioCyc; SMEL266834:GJF6-5837-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:0030151; F:molybdenum ion binding; IEA:InterPro.
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; IPR017896; 4Fe4S_Fe-S-bd.
DR   InterPro; IPR017900; 4Fe4S_Fe_S_CS.
DR   InterPro; IPR009010; Asp_de-COase-like_dom.
DR   InterPro; IPR012675; Beta-grasp_dom.
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   Pfam; PF13237; Fer4_10; 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   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; PS00198; 4FE4S_FER_1; 2.
DR   PROSITE; PS51379; 4FE4S_FER_2; 2.
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; Plasmid; Quinone; Repeat; Ubiquinone.
FT   CHAIN         1    853       NADH-quinone oxidoreductase subunit G 2.
FT                                /FTId=PRO_0000118560.
FT   DOMAIN        1     78       2Fe-2S ferredoxin-type.
FT   DOMAIN      139    170       4Fe-4S ferredoxin-type 1.
FT   DOMAIN      179    209       4Fe-4S ferredoxin-type 2.
FT   DOMAIN      217    273       4Fe-4S Mo/W bis-MGD-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        62     62       Iron-sulfur 1 (2Fe-2S) (By similarity).
FT   METAL        94     94       Iron-sulfur 2 (4Fe-4S); via pros nitrogen
FT                                (By similarity).
FT   METAL        98     98       Iron-sulfur 2 (4Fe-4S) (By similarity).
FT   METAL       101    101       Iron-sulfur 2 (4Fe-4S) (By similarity).
FT   METAL       107    107       Iron-sulfur 2 (4Fe-4S) (By similarity).
FT   METAL       148    148       Iron-sulfur 3 (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       198    198       Iron-sulfur 3 (4Fe-4S) (By similarity).
FT   METAL       224    224       Iron-sulfur 4 (4Fe-4S) (Potential).
FT   METAL       227    227       Iron-sulfur 4 (4Fe-4S) (Potential).
FT   METAL       231    231       Iron-sulfur 4 (4Fe-4S) (Potential).
FT   METAL       259    259       Iron-sulfur 4 (4Fe-4S) (Potential).
FT   CONFLICT    211    211       K -> R (in Ref. 1; CAB51635).
FT   CONFLICT    285    285       T -> A (in Ref. 1; CAB51635).
FT   CONFLICT    452    452       F -> L (in Ref. 1; CAB51635).
FT   CONFLICT    459    459       T -> I (in Ref. 1; CAB51635).
FT   CONFLICT    544    544       S -> G (in Ref. 1; CAB51635).
FT   CONFLICT    554    554       R -> K (in Ref. 1; CAB51635).
FT   CONFLICT    679    679       R -> Q (in Ref. 1; CAB51635).
FT   CONFLICT    734    734       A -> G (in Ref. 1; CAB51635).
FT   CONFLICT    756    756       H -> R (in Ref. 1; CAB51635).
SQ   SEQUENCE   853 AA;  93346 MW;  CDF867CE3BD11A0B CRC64;
     MIKVTIDEQS LEVEAGSTVL AAAERLGIEI PTFCYWKRLP PLASCRMCLV EIEGLRRLQP
     ACATVAADGM VVRTNTPLIE ETRSSMLDML LANHPLDCPI CDKGGECELQ DMVMAYGPGE
     SRFRDPKRVF HSKDIRLSPV IIMNVNRCIQ CQRCVRMCEE VVGAVALGTV EKGMDTAVTG
     FEGSLASCDQ CGNCVEVCPV GALMSFPYRY KARPWDLAET DTICPHCGTG CQLTVGARKG
     EFMRVRSDWE HGVNRETLCV RGRFGLDFIE SRDRIKRPMI RRDGTLTPVS WEEAGDFLRQ
     RLGVAEGKAA GGLISPRLPN EVLYQFQKLM RTVLRTNNVD CSSRWSAPLD ILVPIVASFY
     SRDPLEQVIG KDCVLIIGGN VTEENPVTEY LLRDAARRRH TRLLMLSARP SRLDADARAV
     LRAHPGGEGQ SLAAVVAALV AVTDEGLPDD IFAKTSGTTA SSGANDALDR LVSTLKEGRS
     VTLLVSVDLL RSPLARKTLE QLGNLLQLLR LLGKEPSLQF LFDRANQMGA WDMGVLPGVL
     PGLSPIADEA TRTRFERSWG AEIPREPGAD VDAMLELCEK GGMGVLYVVG SDPLISYPDR
     EFVERALGAA NLLIVQDAFL TDTAGLADVV LPAAGYGEES GTFTNNEGRT QALRKFREPA
     FDARSNLAIF GFIAALRERP LQPSTETVIF EEMTRLVPAY EGLTWEGLGA DGAFTTSAPK
     PWTSGFFAPL SAPAVTDVLQ LITGNCLFHN GYVSEHSETL NSVADDPFIE MSAQDAAGLS
     LSDGDQVLVR SARGELTAKL KVNRRFPHGL VFVPENYRAL RLNSLMRRGE YPCPVEIREC
     AKRAASALDE ERV
//
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