ID A0A0J6YWM6_9BACT Unreviewed; 877 AA.
AC A0A0J6YWM6;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE SubName: Full=NADH-quinone oxidoreductase, subunit G {ECO:0000313|EMBL:KMP11348.1};
GN ORFNames=UR09_03600 {ECO:0000313|EMBL:KMP11348.1};
OS Candidatus Nitromaritima sp. SCGC AAA799-A02.
OC Bacteria; Nitrospinae/Tectomicrobia group; Nitrospinota; Nitrospinia;
OC Nitrospinales; Nitrospinaceae; Candidatus Nitromaritima.
OX NCBI_TaxID=1628278 {ECO:0000313|EMBL:KMP11348.1, ECO:0000313|Proteomes:UP000035948};
RN [1] {ECO:0000313|EMBL:KMP11348.1, ECO:0000313|Proteomes:UP000035948}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SCGC_AAA799_A02 {ECO:0000313|EMBL:KMP11348.1};
RA Ngugi D.K., Blom J., Stepanauskas R., Stingl U.;
RT "Diversification and niche adaptations of Nitrospina-like bacteria in the
RT poly-extreme interfaces of the Atlantis II Deep brine from the Red Sea.";
RL Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases.
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:KMP11348.1}.
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DR EMBL; JZKI01000024; KMP11348.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0J6YWM6; -.
DR PATRIC; fig|1628278.3.peg.532; -.
DR Proteomes; UP000035948; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:InterPro.
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: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; 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; -; 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; 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; 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; 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 PIRSF; PIRSF036643; FDH_alpha; 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; PS00642; COMPLEX1_75K_2; 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:UP000035948}.
FT DOMAIN 7..90
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51085"
FT DOMAIN 88..127
FT /note="4Fe-4S His(Cys)3-ligated-type"
FT /evidence="ECO:0000259|PROSITE:PS51839"
FT DOMAIN 147..177
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 187..217
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 225..283
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
SQ SEQUENCE 877 AA; 96138 MW; CA83E47B789AE30F CRC64;
MSTVVKKTIH FKINGKDVSA PEGTVIIEAA KQNGFEITNL CYNRKLKPFA ACRTCMVDVR
SADGKKELVY SCTHPVAEGT EVTIHTEETD RYNGACLEML LVEHPLDCPI CDKSGVCPLQ
DNTEAMQLHN GRFEIQRRNE PSDKSNPLIE FYLNRCILCG LCVRACDEIQ GVQALDFHKR
GMKSMIGTAN QEPLDCEFCG QCITVCPTGA LMDMSSEVRG LAALFKRNHT TCGYCSWGCT
AQMETKKGRV VRFVADEGQN IGINEGNLCA KGRFGHGIIH NENRIQTPLM NFGGNFKEVS
WEEALKTIAD RVQATINRNG PKTVAGIGGE KLTNEENYLF QKLFRGLFGS NQVTNLANLR
APGINPFLAR CFENGIESKP VTELDKSDVV LIFNSDLPSE YPVGGNSVRK GAVFAGTDVI
IANPRKVVFK SESNIEIRLS YSLGSDAVVV NRICRILIDQ KIVDTAKIKS AVPNYEELAQ
SLAPYTAEAA EKATGLSDET FARAAKRFGR TADRFILVGN DIFDSGQGEE VLNALLNLSI
LVQHGAEGSV SIFPPREHCN SQGINDMGLT PDFLPGYRPV TDSAALSALA GEWGTGPLKF
DGDNPANDLF ANCINGTIKF LHIAGEDPVH SYYKGALVKE ALNTVPFLVV QDVYMTDTAR
MADLVLPTTT YAEKEGTFTN MTRHVQRVTP ATAPQGQSRT DHDIFVELAK ACGKPFSKTT
VSEVQDEISR TVPIYKGTLP GTNSKQWVPE GFAQNPRFQI ADSPREVKPK EGFPYQLVSN
NHMFHIGSYT QYAKALTDVG PDCIAELNPE DARQLNVEDG DRILIESDTH KVEVPVKASP
VTAKGMVYVP KNWVAVPLNM LRNGEEGPVS IKISKAD
//
