ID C9RB68_AMMDK Unreviewed; 826 AA.
AC C9RB68;
DT 24-NOV-2009, integrated into UniProtKB/TrEMBL.
DT 24-NOV-2009, sequence version 1.
DT 27-MAR-2024, entry version 73.
DE SubName: Full=NADH:ubiquinone oxidoreductase, subunit G, iron-sulphur binding protein {ECO:0000313|EMBL:ACX51495.1};
GN OrderedLocusNames=Adeg_0334 {ECO:0000313|EMBL:ACX51495.1};
OS Ammonifex degensii (strain DSM 10501 / KC4).
OC Bacteria; Bacillota; Clostridia; Thermoanaerobacterales;
OC Thermoanaerobacteraceae; Ammonifex.
OX NCBI_TaxID=429009 {ECO:0000313|EMBL:ACX51495.1, ECO:0000313|Proteomes:UP000002620};
RN [1] {ECO:0000313|EMBL:ACX51495.1, ECO:0000313|Proteomes:UP000002620}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 10501 / KC4 {ECO:0000313|Proteomes:UP000002620};
RG US DOE Joint Genome Institute;
RA Kerfeld C., Goodner B., Huber H., Stetter K., Lucas S., Copeland A.,
RA Lapidus A., Glavina del Rio T., Dalin E., Tice H., Bruce D., Goodwin L.,
RA Pitluck S., Saunders E., Brettin T., Detter J.C., Han C., Larimer F.,
RA Land M., Hauser L., Kyrpides N., Ovchinnikova G., Richardson P.;
RT "Complete sequence of chromosome of Ammonifex degensii KC4.";
RL Submitted (OCT-2009) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Mo-bis(molybdopterin guanine dinucleotide);
CC Xref=ChEBI:CHEBI:60539; Evidence={ECO:0000256|ARBA:ARBA00001942};
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; CP001785; ACX51495.1; -; Genomic_DNA.
DR AlphaFoldDB; C9RB68; -.
DR STRING; 429009.Adeg_0334; -.
DR KEGG; adg:Adeg_0334; -.
DR eggNOG; COG3383; Bacteria.
DR HOGENOM; CLU_000422_4_0_9; -.
DR OrthoDB; 9803192at2; -.
DR Proteomes; UP000002620; 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:0046872; F:metal ion 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 CDD; cd02775; MopB_CT; 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; IPR006656; Mopterin_OxRdtase.
DR InterPro; IPR006963; Mopterin_OxRdtase_4Fe-4S_dom.
DR InterPro; IPR000283; NADH_UbQ_OxRdtase_75kDa_su_CS.
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; PF13187; Fer4_9; 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; 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; PS00641; COMPLEX1_75K_1; 1.
PE 4: Predicted;
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:UP000002620}.
FT DOMAIN 3..81
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51085"
FT DOMAIN 81..120
FT /note="4Fe-4S His(Cys)3-ligated-type"
FT /evidence="ECO:0000259|PROSITE:PS51839"
FT DOMAIN 139..168
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 181..210
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
SQ SEQUENCE 826 AA; 89953 MW; CDEE2505D4877F52 CRC64;
MAGMVTLTID GRKVTVPEGT TILHAAEALG IEIPHLCYCP GLEGTGACRL CVVEVEKVRG
LVVACMRRVA EGMVVHTNTP RVREARKFVL ELLLSRHPGL CLSCDKSGSC KLQQYAYELG
IKRPFFEVRD PGYEVKEDLF IVRDYNLCIL CGRCIRVCRT QGADILDFMK RGIETRVGTP
LDRSLLESGC DFCGSCVSVC PTGALMEKER LGKGREWELE KVHSRCSYCG AACGLNYHLR
KGEIVKVSSP EPVAYLCARG RFGYGYLQSG ERLTTPLVRR DGELVPADWD EALSLVAENF
QQAIERYGAE GVGGILSPLV SCETAYSFQK FFRSGLRTNN VDCSLRIGAG LELLRHADAV
TGGPEGYAGW KDVLEANVIL LVGDVCQRVP AVWGYLKRAV GRGAKLIYLG FYKDRPARLA
QVWLQALPGE EPLVLARLAW LILQNPTYRT LAERVPNFTS FAEGVERLAR VEVSVPEEDL
ARAAELWSEE ARGVLLLPVD GVSPATGKAA LNLLLLTGRR EKALFPTSAF VNAQGVWRLG
GVAEFFPGLR PAPEAASEFA AFWGRVPNGT PGLNLTAMLR PGSPVKALYL LGEDPLSSYP
GNGSIAAKLE ELDFLVVQDL TLTKTAEKAH VVLPLASLPE TGGTVIATHG EKHHLSSALS
PRTLMPWQVF ALLAAKMNLE LNLSAQELLL NEIKAVTPEF GLVPAERRPG FWELGEVGPG
RGDSQLKLTT LAFYPSFYRQ DWLKLSGLEV LLPYEGNFIA LSPEEGLEEG AVVEVSTPHG
TFTTRVRLDK ALPRGVAAVP AFSSAAAALF PLETPWEPVP ASIARA
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