ID C6E8V6_GEOSM Unreviewed; 794 AA.
AC C6E8V6;
DT 01-SEP-2009, integrated into UniProtKB/TrEMBL.
DT 01-SEP-2009, sequence version 1.
DT 01-MAY-2013, entry version 33.
DE SubName: Full=NADH dehydrogenase I, D subunit;
GN OrderedLocusNames=GM21_0160;
OS Geobacter sp. (strain M21).
OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfuromonadales;
OC Geobacteraceae; Geobacter.
OX NCBI_TaxID=443144;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M21;
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E.,
RA Tice H., Bruce D., Goodwin L., Pitluck S., Saunders E., Brettin T.,
RA Detter J.C., Han C., Larimer F., Land M., Hauser L., Kyrpides N.,
RA Ovchinnikova G., Lovley D.;
RT "Complete sequence of Geobacter sp. M21.";
RL Submitted (JUL-2009) to the EMBL/GenBank/DDBJ databases.
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.
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DR EMBL; CP001661; ACT16245.1; -; Genomic_DNA.
DR RefSeq; YP_003020003.1; NC_012918.1.
DR STRING; 443144.GM21_0160; -.
DR EnsemblBacteria; ACT16245; ACT16245; GM21_0160.
DR GeneID; 8135463; -.
DR KEGG; gem:GM21_0160; -.
DR PATRIC; 22014812; VBIGeoSp56140_0162.
DR eggNOG; COG0649; -.
DR HOGENOM; HOG000228264; -.
DR KO; K13380; -.
DR OMA; VWDMFGI; -.
DR ProtClustDB; PRK13292; -.
DR BioCyc; GSP443144:GHKM-164-MONOMER; -.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:InterPro.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0008137; F:NADH dehydrogenase (ubiquinone) activity; IEA:InterPro.
DR GO; GO:0048038; F:quinone binding; IEA:InterPro.
DR Gene3D; 3.40.50.700; -; 1.
DR HAMAP; MF_01356; NDH1_NuoB; 1; -.
DR HAMAP; MF_01357; NDH1_NuoC; 1; -.
DR HAMAP; MF_01358; NDH1_NuoD; 1; -.
DR InterPro; IPR010218; NADH_DH_suC.
DR InterPro; IPR001135; NADH_Q_OxRdtase_suD.
DR InterPro; IPR006137; NADH_UbQ_OxRdtase-like_20kDa.
DR InterPro; IPR001268; NADH_UbQ_OxRdtase_30kDa_su.
DR InterPro; IPR014029; NADH_UbQ_OxRdtase_49kDa_CS.
DR InterPro; IPR020396; NADH_UbQ_OxRdtase_CS.
DR InterPro; IPR006138; NADH_UQ_OxRdtase_20Kd_su.
DR InterPro; IPR022885; NDH1_su_D/H.
DR Pfam; PF00329; Complex1_30kDa; 1.
DR Pfam; PF00346; Complex1_49kDa; 1.
DR Pfam; PF01058; Oxidored_q6; 1.
DR ProDom; PD001581; NADH_UbQ_OxRdtase_30kDa_su; 1.
DR TIGRFAMs; TIGR01957; nuoB_fam; 1.
DR TIGRFAMs; TIGR01962; NuoD; 1.
DR PROSITE; PS00542; COMPLEX1_30K; 1.
DR PROSITE; PS00535; COMPLEX1_49K; 1.
PE 3: Inferred from homology;
KW Cell inner membrane; Cell membrane; Complete proteome; Membrane;
KW Multifunctional enzyme; Ubiquinone.
SQ SEQUENCE 794 AA; 90049 MW; E2EED30CCDAE8BB3 CRC64;
MSQGDDDKIP ENVLFASLDD MINWGRANSL WPMFFGLSCC FVEMMTSFTS RYDVSRFGAE
VLRGTPRESD LMVIAGTVFK KMAPSILRLY DQMAEPKWVI SMGSCANSGG MYDVYSVVQG
VDQILPVDLY IPGCPPRPES FLEGLMLLQQ KIRSEERPTR PVLRMQGGTQ GTVAPILVDG
ATKSRDTRGP GMEGSAIRGS AMQPPHFAAP RSDELWRPKQ TRLPYPDFNL KEELQGAFAG
QVVLDETACD MLTYRAPARL VPEILRHLKE RKESPFRRLE DIACVDESCR RDRDRYKDFT
VNYHLTCFDT PGRVRIKTEL EGSYPETPSV TSVFPVADWY EREAYDMFGI RFAGHPNLRR
ILMPPDWVGH PLRKEHPARA TELPPYTAED ARRQKALPGG DFFDRVDDET LILNLGPQHP
GTHGVIRFVL KLSGEEIVDM DSDIGYHHRA AEKTGERQNW HQYIPYTDRV DYLSGVQNNL
AYLNSVETLC GIEIPDRAIY IRVMLCELFR IANHLVWLGT FASDLGAMTP VFYTFTDREK
IFDIVEFITG GRMHPAWFRI GGVAEDLPEG WQEKVHSFLE WFPARLAEYE KLLTGNPIFV
ARLKGVSAIT LDTALEWGIS GPNLRACDFA WDLRKKIPYG GYDRFEFEVA TAHGGDCYAR
YKVRMEEMRQ SLSIVRQAAA GMPGGRFISP DYRYTLPQKR DTLEDIESLI HHFVNATRGI
SPPKGECYAP IEGSKGEYGY FAVSDGLHTA YRMRIRTATF PHIQSLPVLS RGWLVSDFLA
ILGSLDFVLS DLDR
//