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 01-MAY-2013, entry version 100.
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.
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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; QCGNCVE; -.
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:0016661; F:oxidoreductase activity, acting on other nitrogenous compounds as donors; 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; 2.40.40.20; -; 1.
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_Fe4S4_dom.
DR InterPro; IPR006655; Mopterin_OxRdtase_prok_CS.
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; Asp_decarb_fold; 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; PS00198; 4FE4S_FER_1; 2.
DR PROSITE; PS51379; 4FE4S_FER_2; 2.
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 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
//
