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Database: UniProt
Entry: Q74GA2_GEOSL
LinkDB: Q74GA2_GEOSL
Original site: Q74GA2_GEOSL 
ID   Q74GA2_GEOSL            Unreviewed;       826 AA.
AC   Q74GA2;
DT   05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2004, sequence version 1.
DT   27-MAR-2024, entry version 136.
DE   SubName: Full=NADH dehydrogenase I, G subunit {ECO:0000313|EMBL:AAR33677.1};
GN   Name=nuoG-1 {ECO:0000313|EMBL:AAR33677.1};
GN   OrderedLocusNames=GSU0344 {ECO:0000313|EMBL:AAR33677.1};
OS   Geobacter sulfurreducens (strain ATCC 51573 / DSM 12127 / PCA).
OC   Bacteria; Thermodesulfobacteriota; Desulfuromonadia; Geobacterales;
OC   Geobacteraceae; Geobacter.
OX   NCBI_TaxID=243231 {ECO:0000313|EMBL:AAR33677.1, ECO:0000313|Proteomes:UP000000577};
RN   [1] {ECO:0000313|EMBL:AAR33677.1, ECO:0000313|Proteomes:UP000000577}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51573 / DSM 12127 / PCA
RC   {ECO:0000313|Proteomes:UP000000577};
RX   PubMed=14671304; DOI=10.1126/science.1088727;
RA   Methe B.A., Nelson K.E., Eisen J.A., Paulsen I.T., Nelson W.,
RA   Heidelberg J.F., Wu D., Wu M., Ward N., Beanan M.J., Dodson R.J.,
RA   Madupu R., Brinkac L.M., Daugherty S.C., DeBoy R.T., Durkin A.S., Gwinn M.,
RA   Kolonay J.F., Sullivan S.A., Haft D.H., Selengut J., Davidsen T.M.,
RA   Zafar N., White O., Tran B., Romero C., Forberger H.A., Weidman J.,
RA   Khouri H., Feldblyum T.V., Utterback T.R., Van Aken S.E., Lovley D.R.,
RA   Fraser C.M.;
RT   "Genome of Geobacter sulfurreducens: metal reduction in subsurface
RT   environments.";
RL   Science 302:1967-1969(2003).
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};
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DR   EMBL; AE017180; AAR33677.1; -; Genomic_DNA.
DR   RefSeq; NP_951404.1; NC_002939.5.
DR   RefSeq; WP_010941012.1; NC_002939.5.
DR   AlphaFoldDB; Q74GA2; -.
DR   SMR; Q74GA2; -.
DR   STRING; 243231.GSU0344; -.
DR   EnsemblBacteria; AAR33677; AAR33677; GSU0344.
DR   KEGG; gsu:GSU0344; -.
DR   PATRIC; fig|243231.5.peg.341; -.
DR   eggNOG; COG3383; Bacteria.
DR   HOGENOM; CLU_000422_4_0_7; -.
DR   InParanoid; Q74GA2; -.
DR   OrthoDB; 9816402at2; -.
DR   Proteomes; UP000000577; Chromosome.
DR   GO; GO:0045272; C:plasma membrane respiratory chain complex I; IBA:GO_Central.
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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0043546; F:molybdopterin cofactor binding; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR   GO; GO:0045333; P:cellular respiration; IBA:GO_Central.
DR   CDD; cd00207; fer2; 1.
DR   CDD; cd02771; MopB_NDH-1_NuoG2-N7; 1.
DR   Gene3D; 2.40.40.20; -; 1.
DR   Gene3D; 3.10.20.740; -; 1.
DR   Gene3D; 3.30.70.20; -; 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; IPR017896; 4Fe4S_Fe-S-bd.
DR   InterPro; IPR017900; 4Fe4S_Fe_S_CS.
DR   InterPro; IPR009010; Asp_de-COase-like_dom_sf.
DR   InterPro; IPR006657; MoPterin_dinucl-bd_dom.
DR   InterPro; IPR006656; Mopterin_OxRdtase.
DR   InterPro; IPR006963; Mopterin_OxRdtase_4Fe-4S_dom.
DR   InterPro; IPR006655; Mopterin_OxRdtase_prok_CS.
DR   InterPro; IPR027467; MopterinOxRdtase_cofactor_BS.
DR   InterPro; IPR019574; NADH_UbQ_OxRdtase_Gsu_4Fe4S-bd.
DR   PANTHER; PTHR43105:SF15; FORMATE DEHYDROGENASE H; 1.
DR   PANTHER; PTHR43105; RESPIRATORY NITRATE REDUCTASE; 1.
DR   Pfam; PF13510; Fer2_4; 1.
DR   Pfam; PF12838; Fer4_7; 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; SSF54292; 2Fe-2S ferredoxin-like; 1.
DR   SUPFAM; SSF54862; 4Fe-4S ferredoxins; 1.
DR   SUPFAM; SSF50692; ADC-like; 1.
DR   SUPFAM; SSF53706; Formate dehydrogenase/DMSO reductase, domains 1-3; 1.
DR   PROSITE; PS51085; 2FE2S_FER_2; 1.
DR   PROSITE; PS00198; 4FE4S_FER_1; 1.
DR   PROSITE; PS51379; 4FE4S_FER_2; 2.
DR   PROSITE; PS51839; 4FE4S_HC3; 1.
DR   PROSITE; PS51669; 4FE4S_MOW_BIS_MGD; 1.
DR   PROSITE; PS00551; MOLYBDOPTERIN_PROK_1; 1.
DR   PROSITE; PS00490; MOLYBDOPTERIN_PROK_2; 1.
PE   4: Predicted;
KW   2Fe-2S {ECO:0000256|ARBA:ARBA00022714};
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:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000577};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT   DOMAIN          1..79
FT                   /note="2Fe-2S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51085"
FT   DOMAIN          79..118
FT                   /note="4Fe-4S His(Cys)3-ligated-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51839"
FT   DOMAIN          138..166
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51379"
FT   DOMAIN          177..207
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51379"
FT   DOMAIN          216..272
FT                   /note="4Fe-4S Mo/W bis-MGD-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51669"
SQ   SEQUENCE   826 AA;  88098 MW;  CCCDC5F37736AEB5 CRC64;
     MVTLTIDDKQ VTVPKDATIF DAAKQAGIRI PILCHDKKLH PFGGCRMCLV EVEQMKGRQI
     PACTTPVTEG MIVRTMTDEI VKARKMVLEL LLLKHPIDCP VCDAAGDCDL QNLTYEYGVD
     TNRFTDEKFN WKIDYVNPLI ERDMNRCVHC GKCARICDEI VSFGAYSFIN RGIEAKIGTE
     FDGPLNCEFC GSCVSVCPVG ALISRPFKFK ARWWALNKVK TVCSYCGTGC QLTLGVKDNK
     VLTTIYDENQ GFHNGQLCTR GRWGYQFVNS SKRLTTPLIR KGDTLQPASW DEALGMVADR
     LKTSKDAAAT LVTPRLTNEE LYLLKRVVKD AVGSDNLDHS GGYAHEALTA GARESLGFPG
     SPSVIADIQK SELLLVIKTD AYETHPVIGF EVNLAVKRQG VALRILSDKK GKLSRLPGAQ
     TYVHTPGAEL VLVNALAKTI VDEGLHDASS VGAIKGFDAW LKSIESCTPD QAAGQCGIAA
     DTIKAVAREY AAAGKALIML PLGMGYPGHG KALAQALINL ALLTGRVGKE GCGVLIMGEK
     NNSQGAADLG IHPTANGLNA QAILAGCSAG SIKTLYVVGE NPVVSYPNRK QVEAALDAVE
     FLVVQDLFLT ETASKADVVL PACSFAEKDG TFTSLGGAVQ RVNRAITPLG DCRSDFDILN
     MLHAKLTGQA AYTSQKEAFA DLAAATPGYA GLTLEGLGDA GAVRVNNCTA SFVPVATSTV
     TTEAGKFALL TGSALNHSGT LSLYGEGPML VCPEGYLELN KDDAAKLSIT EGDAVTMKSA
     TGELRLKAKV GTRLPQGVAF APYHFAEASI NSLTGATAIT WITISK
//
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