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Database: UniProt
Entry: B9M3Y4_GEODF
LinkDB: B9M3Y4_GEODF
Original site: B9M3Y4_GEODF 
ID   B9M3Y4_GEODF            Unreviewed;       630 AA.
AC   B9M3Y4;
DT   24-MAR-2009, integrated into UniProtKB/TrEMBL.
DT   24-MAR-2009, sequence version 1.
DT   27-MAR-2024, entry version 82.
DE   SubName: Full=NADH dehydrogenase I, G subunit {ECO:0000313|EMBL:ACM19627.1};
GN   Name=nuoG-2 {ECO:0000313|EMBL:ACM19627.1};
GN   OrderedLocusNames=Geob_1267 {ECO:0000313|EMBL:ACM19627.1};
OS   Geotalea daltonii (strain DSM 22248 / JCM 15807 / FRC-32) (Geobacter
OS   daltonii).
OC   Bacteria; Thermodesulfobacteriota; Desulfuromonadia; Geobacterales;
OC   Geobacteraceae; Geotalea.
OX   NCBI_TaxID=316067 {ECO:0000313|EMBL:ACM19627.1, ECO:0000313|Proteomes:UP000007721};
RN   [1] {ECO:0000313|EMBL:ACM19627.1, ECO:0000313|Proteomes:UP000007721}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 22248 / JCM 15807 / FRC-32
RC   {ECO:0000313|Proteomes:UP000007721};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Saunders E., Brettin T., Detter J.C.,
RA   Han C., Larimer F., Land M., Hauser L., Kyrpides N., Ovchinnikova G.,
RA   Kostka J., Richardson P.;
RT   "Complete sequence of Geobacter sp. FRC-32.";
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a quinone + 5 H(+)(in) + NADH = a quinol + 4 H(+)(out) +
CC         NAD(+); Xref=Rhea:RHEA:57888, ChEBI:CHEBI:15378, ChEBI:CHEBI:24646,
CC         ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:132124;
CC         Evidence={ECO:0000256|ARBA:ARBA00000100};
CC   -!- COFACTOR:
CC       Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135;
CC         Evidence={ECO:0000256|ARBA:ARBA00034078};
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000256|ARBA:ARBA00001966};
CC   -!- SIMILARITY: Belongs to the complex I 75 kDa subunit family.
CC       {ECO:0000256|ARBA:ARBA00005404, ECO:0000256|RuleBase:RU004523}.
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DR   EMBL; CP001390; ACM19627.1; -; Genomic_DNA.
DR   RefSeq; WP_012646356.1; NC_011979.1.
DR   AlphaFoldDB; B9M3Y4; -.
DR   STRING; 316067.Geob_1267; -.
DR   KEGG; geo:Geob_1267; -.
DR   eggNOG; COG1034; Bacteria.
DR   HOGENOM; CLU_000422_11_4_7; -.
DR   OrthoDB; 9816402at2; -.
DR   Proteomes; UP000007721; Chromosome.
DR   GO; GO:0016020; C:membrane; IEA:InterPro.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0008137; F:NADH dehydrogenase (ubiquinone) activity; IEA:InterPro.
DR   GO; GO:0042773; P:ATP synthesis coupled electron transport; IEA:InterPro.
DR   CDD; cd00207; fer2; 1.
DR   Gene3D; 3.10.20.740; -; 1.
DR   Gene3D; 3.40.50.740; -; 2.
DR   Gene3D; 2.20.25.90; ADC-like domains; 1.
DR   Gene3D; 3.40.228.10; Dimethylsulfoxide Reductase, domain 2; 1.
DR   InterPro; IPR036010; 2Fe-2S_ferredoxin-like_sf.
DR   InterPro; IPR001041; 2Fe-2S_ferredoxin-type.
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   NCBIfam; TIGR01973; NuoG; 1.
DR   PANTHER; PTHR43105:SF13; NADH-UBIQUINONE OXIDOREDUCTASE 75 KDA SUBUNIT, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR43105; RESPIRATORY NITRATE REDUCTASE; 1.
DR   Pfam; PF13510; Fer2_4; 1.
DR   Pfam; PF04879; Molybdop_Fe4S4; 1.
DR   Pfam; PF00384; Molybdopterin; 2.
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; 2Fe-2S ferredoxin-like; 1.
DR   SUPFAM; SSF54862; 4Fe-4S ferredoxins; 1.
DR   SUPFAM; SSF53706; Formate dehydrogenase/DMSO reductase, domains 1-3; 1.
DR   PROSITE; PS51085; 2FE2S_FER_2; 1.
DR   PROSITE; PS51839; 4FE4S_HC3; 1.
DR   PROSITE; PS51669; 4FE4S_MOW_BIS_MGD; 1.
DR   PROSITE; PS00641; COMPLEX1_75K_1; 1.
DR   PROSITE; PS00642; COMPLEX1_75K_2; 1.
PE   3: Inferred from homology;
KW   4Fe-4S {ECO:0000256|ARBA:ARBA00022485};
KW   Iron {ECO:0000256|ARBA:ARBA00023004};
KW   Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022485};
KW   NAD {ECO:0000256|ARBA:ARBA00023027};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007721};
KW   Translocase {ECO:0000256|ARBA:ARBA00022967}.
FT   DOMAIN          2..80
FT                   /note="2Fe-2S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51085"
FT   DOMAIN          80..119
FT                   /note="4Fe-4S His(Cys)3-ligated-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51839"
FT   DOMAIN          217..273
FT                   /note="4Fe-4S Mo/W bis-MGD-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51669"
SQ   SEQUENCE   630 AA;  68088 MW;  811DF7C8603936DF CRC64;
     MPKLTIDNIP VEVPAGTNVL EAARQVGVWI PHFCYHPALG SVGACRLCAM KFLEGPVKGV
     QMSCMIPAQD GMVVSTTDGE AAKMRQMVIE WLMINHPHDC PVCDEGGECL LQDYTIAGGH
     GIRRYRGKKR TFNNQFLGPY IEHEMNRCIE CYRCARFYQD FAGGTDFGVM GSAGRVYFGR
     FREGQLQSPF SGNLVDICPT GVFTDKTARF RARYWDYDMA PSICPHCSLG CNTIPAARYR
     ELLKTMARRN DAVNGWFICD RGRFEKYPVN DPARPRAPGI DGVEASWDQA LDALVQRLGE
     VTALHGQGSI AVVGSPRLSL EGLVMLPLLA ETMGSGNFCF FTDKDESDKA KAAVEKLTLA
     NSASMADVQT ADAVVVMACD LLTEGAMMAL AVRQAWRNGA RVFLLKANVS ALTAGVGIVV
     EAVDSLSAIP FADFKRPVVI CGTAQADTAT IEKAANAGAK ISYMLSGANA FAAARLSLKH
     GARDLQTAVA GGKIKGIIAF EADLAADLVE KLPFVAIADY MPSDLTGKAS VFLPATTTIE
     MDGTFINNEG RAQRFKKVME PGLPIKGLDP ALHPPHVHRL SPPGGEVRPS WQIIAALIEL
     LSGEKIVEPL VGQWEKLRDL DAENGGLSIL
//
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