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Database: UniProt
Entry: A0A1G1BD91_9BACT
LinkDB: A0A1G1BD91_9BACT
Original site: A0A1G1BD91_9BACT 
ID   A0A1G1BD91_9BACT        Unreviewed;       562 AA.
AC   A0A1G1BD91;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   SubName: Full=NADH dehydrogenase {ECO:0000313|EMBL:OGV80711.1};
GN   ORFNames=A2X65_05945 {ECO:0000313|EMBL:OGV80711.1};
OS   Stygiobacter sp. GWF2_38_21.
OC   Bacteria; Ignavibacteriota; Ignavibacteria; Ignavibacteriales;
OC   Melioribacteraceae; Stygiobacter.
OX   NCBI_TaxID=1801612 {ECO:0000313|EMBL:OGV80711.1, ECO:0000313|Proteomes:UP000176810};
RN   [1] {ECO:0000313|EMBL:OGV80711.1, ECO:0000313|Proteomes:UP000176810}
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:OGV80711.1}.
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DR   EMBL; MHBR01000017; OGV80711.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G1BD91; -.
DR   Proteomes; UP000176810; Unassembled WGS sequence.
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; 3.30.70.20; -; 1.
DR   Gene3D; 3.40.50.740; -; 2.
DR   Gene3D; 2.20.25.90; ADC-like domains; 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; 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; 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; PS00643; COMPLEX1_75K_3; 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:ARBA00022485}.
FT   DOMAIN          2..78
FT                   /note="2Fe-2S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51085"
FT   DOMAIN          78..117
FT                   /note="4Fe-4S His(Cys)3-ligated-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51839"
FT   DOMAIN          216..272
FT                   /note="4Fe-4S Mo/W bis-MGD-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51669"
SQ   SEQUENCE   562 AA;  62885 MW;  76B3E8A000E78393 CRC64;
     MPTITIDGKQ IEFKQGQTVI EVAREAGVEI PHFCYHPKLS VSGNCRVCLV EIEKMPKLAI
     SCATLAGDGM VVHTNSTKTL EARNAVMEFI LINHPLDCPI CDEAGECKLQ DYAYAHSRGE
     SRFEEIKNRK EKRVQLGPRI KFDGDRCISC SRCIRFSDEI AKSNQLTFVN RGDKVTISTF
     PGESFDNPYS MNTVDICPVG ALTNNDFRFK SRVWEMSFTN SICVGCARGC NTEIGVRNNE
     ILRLTPRQNE EVNSFWMCDN GRLSTFKNVN ADDRIDGTFV RKEGQLQKVS WDEALEVAAK
     SLKEYKSNEI AFVGSAFATC EDNFVLLKLA KQLNVTSVDF ARHSVADDQD DILIREDKTP
     NTTGAELVIA KSNGAKLEGI YRLIKEGKVK TLFVMEDDLG ALSEEWEQAL GMLDLLIVTA
     TNSSKTTALA DIVFPAASYA EKHGTFVNFQ GRVQRIRPAV SLDEMDRALD GMNMSRWDKF
     GTKFDKWNQG RKHDAKPSWK ILAQLSSHLG GKIKYEMAEE VFDEISNSVD AFKGLDYDMI
     GELGVQLKIL NSESRLATTK SL
//
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