ID L0DBH9_SINAD Unreviewed; 590 AA.
AC L0DBH9;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 56.
DE SubName: Full=NADH:ubiquinone oxidoreductase chain G-like protein {ECO:0000313|EMBL:AGA26602.1};
GN OrderedLocusNames=Sinac_2284 {ECO:0000313|EMBL:AGA26602.1};
OS Singulisphaera acidiphila (strain ATCC BAA-1392 / DSM 18658 / VKM B-2454 /
OS MOB10).
OC Bacteria; Planctomycetota; Planctomycetia; Isosphaerales; Isosphaeraceae;
OC Singulisphaera.
OX NCBI_TaxID=886293 {ECO:0000313|EMBL:AGA26602.1, ECO:0000313|Proteomes:UP000010798};
RN [1] {ECO:0000313|EMBL:AGA26602.1, ECO:0000313|Proteomes:UP000010798}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1392 / DSM 18658 / VKM B-2454 / MOB10
RC {ECO:0000313|Proteomes:UP000010798};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Peters L., Ovchinnikova G., Chertkov O.,
RA Kyrpides N., Mavromatis K., Ivanova N., Brettin T., Detter J.C., Han C.,
RA Larimer F., Land M., Hauser L., Markowitz V., Cheng J.-F., Hugenholtz P.,
RA Woyke T., Wu D., Tindall B., Pomrenke H., Brambilla E., Klenk H.-P.,
RA Eisen J.A.;
RT "Complete sequence of chromosome of Singulisphaera acidiphila DSM 18658.";
RL Submitted (FEB-2012) 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};
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DR EMBL; CP003364; AGA26602.1; -; Genomic_DNA.
DR RefSeq; WP_015245758.1; NZ_JH621489.1.
DR AlphaFoldDB; L0DBH9; -.
DR STRING; 886293.Sinac_2284; -.
DR KEGG; saci:Sinac_2284; -.
DR eggNOG; COG1034; Bacteria.
DR HOGENOM; CLU_000422_11_7_0; -.
DR OrthoDB; 9803192at2; -.
DR Proteomes; UP000010798; 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: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; cd00368; Molybdopterin-Binding; 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 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; 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; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000010798};
KW Ubiquinone {ECO:0000313|EMBL:AGA26602.1}.
FT DOMAIN 90..129
FT /note="4Fe-4S His(Cys)3-ligated-type"
FT /evidence="ECO:0000259|PROSITE:PS51839"
FT DOMAIN 227..283
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
FT REGION 570..590
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 590 AA; 64466 MW; 65EC50362BD8823B CRC64;
MATIFINGQE HEIPEGEKLN AIQMASRVGV DIPYYCWHPA LSVVANCRMC EIEVGNKDPK
TGEIKMIPKL VPACQTPAKD ATVLVTDSPK VKEHQRMIME YLLINHPLDC PVCDQAGECG
LQDYSYEHGQ ANHRFVEERT VNPRKDVSDL IQLNQDRCIM CTRCVRFTRE ITQTGELQVM
NRGNHAEINT FPDHPLENPL AGNVVDICPV GALLDKDFLH KQRVWFLSKH DSVCTRCSTG
CNVSAEENRG QLWRYKPRFN PNVNDYWMCD EGRYGYKDAN DPALLNAMYV RTQGDLKPAS
IDQALKDAGQ GLARISEAGG LVAGILSPFM TVEEAYLLAT YLKGLNPANV LALGPVPRSG
VDQTFQPDLQ KGRTGDTSFV VPRPFTIHAE KCPNRRGVEA ILEHFQGQVI DFASISGRAG
HGEFRGLFVV SDAIEAAFTE EDVKKLRPKV EFLVVQDTLV TELAQAADVV LAGATFAEKA
GCYVNADGRL QYAEASLPPR DGSLPDLDLL AILIGRSTGP VQSREILAEL AGVVPGFSIA
EGGQVAPFGA ILGSAEPVGA GVAFRDAWMQ PRGAKTDHSS EPSPRGGKDA
//