ID A0A1G1FC19_9BACT Unreviewed; 719 AA.
AC A0A1G1FC19;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=NADH dehydrogenase (Quinone) subunit G {ECO:0008006|Google:ProtNLM};
GN ORFNames=A2X56_13860 {ECO:0000313|EMBL:OGW29308.1};
OS Nitrospirae bacterium GWC2_57_13.
OC Bacteria; Nitrospirota.
OX NCBI_TaxID=1801697 {ECO:0000313|EMBL:OGW29308.1, ECO:0000313|Proteomes:UP000177780};
RN [1] {ECO:0000313|EMBL:OGW29308.1, ECO:0000313|Proteomes:UP000177780}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27774985; DOI=10.1038/ncomms13219;
RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA Williams K.H., Hubbard S.S., Banfield J.F.;
RT "Thousands of microbial genomes shed light on interconnected biogeochemical
RT processes in an aquifer system.";
RL Nat. Commun. 7:13219-13219(2016).
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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OGW29308.1}.
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DR EMBL; MHDZ01000025; OGW29308.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G1FC19; -.
DR STRING; 1801697.A2X56_13860; -.
DR Proteomes; UP000177780; Unassembled WGS sequence.
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:0016491; F:oxidoreductase activity; IEA:InterPro.
DR CDD; cd00207; fer2; 1.
DR Gene3D; 3.10.20.740; -; 1.
DR Gene3D; 3.30.70.20; -; 1.
DR Gene3D; 3.40.50.740; -; 1.
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; IPR006656; Mopterin_OxRdtase.
DR InterPro; IPR006963; Mopterin_OxRdtase_4Fe-4S_dom.
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; 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; PS00198; 4FE4S_FER_1; 1.
DR PROSITE; PS51379; 4FE4S_FER_2; 2.
DR PROSITE; PS51839; 4FE4S_HC3; 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}.
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 140..169
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 182..211
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
SQ SEQUENCE 719 AA; 74913 MW; B3A05BC910930910 CRC64;
MSKMVNMEFD GKAVTVPEGM TLVDAAATAG IHIPNLCHIK ELRGVGACRM CMVEIEGMKT
PVTACTMKVK EGMKVATRTD KVEEIRKFVV DLVLSFHPLD CMTCPKAGDC DLQRYAADLG
IRESSFGRKS FNYELNDRSP FITIDNNYCI LCGRCVRVCK EQGTNVLDFM GRGITTKVST
ALDKPLHESE CTFCGSCVDA CPVNALMERD RWQHGREWDL DKRESACTAC GSGCRVVVNK
KDGKIVKVNA KEDNGYICVI GRFGFDSLAA ANRVVSPMVR KGAKLAPATW GDAIKAAAEG
LKKAGANAGF LASGSLMNEE AYALQSLARD VVGSGNIDTP ASSYAGGLLS ALSAVYGDGG
AAIASQADLS TADLVVVIGA DPSQKKQSLQ EVDVMIRRRA QAGAKVIVIS TEKTGLAAHQ
NAILLQLKAG ADPVLLAGLM SAVLAEGVSP ASKGFDGVKK TLISVEEAAA ASGVAAEQIV
TAAKAYAAAK SPIVVIGMGI GESEEASLQA LNLALMKDAG VLPLLPEANA LGVMQMGCTP
DAGSGKAKKG GKGYEEMQSG MKALFVAGNV PDMNSKADFL IVQTSHLSPL AAKADVVLPM
TALYEREGTI VNTYGQQKVL VAANEAEGTA KNGADIAAEL SLVINKTKGF TLKDAESGAK
KVKAAKIAAG SFKPVAAKAV KASARSTSDL LKAINQGMLQ ESGVSKVLVV TGSAAVAKG
//
