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Database: UniProt
Entry: A0A1W9P8M3_9BACT
LinkDB: A0A1W9P8M3_9BACT
Original site: A0A1W9P8M3_9BACT 
ID   A0A1W9P8M3_9BACT        Unreviewed;       632 AA.
AC   A0A1W9P8M3;
DT   05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2017, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   SubName: Full=NADH-quinone oxidoreductase subunit F {ECO:0000313|EMBL:OQX54714.1};
GN   ORFNames=B5M54_04840 {ECO:0000313|EMBL:OQX54714.1};
OS   Candidatus Aminicenantes bacterium 4484_214.
OC   Bacteria; Candidatus Aminicenantes.
OX   NCBI_TaxID=1968529 {ECO:0000313|EMBL:OQX54714.1, ECO:0000313|Proteomes:UP000192734};
RN   [1] {ECO:0000313|Proteomes:UP000192734}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Dombrowski N., Seitz K., Teske A., Baker B.;
RT   "Novel pathways for hydrocarbon cycling and metabolic interdependencies in
RT   hydrothermal sediment communities.";
RL   Submitted (MAR-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the complex I 51 kDa subunit family.
CC       {ECO:0000256|ARBA:ARBA00007523}.
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:OQX54714.1}.
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DR   EMBL; MZGL01000019; OQX54714.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1W9P8M3; -.
DR   Proteomes; UP000192734; Unassembled WGS sequence.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0010181; F:FMN binding; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0008137; F:NADH dehydrogenase (ubiquinone) activity; IEA:InterPro.
DR   CDD; cd02980; TRX_Fd_family; 1.
DR   Gene3D; 3.10.20.600; -; 1.
DR   Gene3D; 3.30.70.20; -; 1.
DR   Gene3D; 6.10.250.1450; -; 1.
DR   Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR   Gene3D; 3.40.50.11540; NADH-ubiquinone oxidoreductase 51kDa subunit; 1.
DR   Gene3D; 1.20.1440.230; NADH-ubiquinone oxidoreductase 51kDa subunit, iron-sulphur binding domain; 1.
DR   InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR   InterPro; IPR017900; 4Fe4S_Fe_S_CS.
DR   InterPro; IPR001949; NADH-UbQ_OxRdtase_51kDa_CS.
DR   InterPro; IPR011538; Nuo51_FMN-bd.
DR   InterPro; IPR037225; Nuo51_FMN-bd_sf.
DR   InterPro; IPR019575; Nuop51_4Fe4S-bd.
DR   InterPro; IPR037207; Nuop51_4Fe4S-bd_sf.
DR   InterPro; IPR019554; Soluble_ligand-bd.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   PANTHER; PTHR43578; NADH-QUINONE OXIDOREDUCTASE SUBUNIT F; 1.
DR   PANTHER; PTHR43578:SF3; NADH-QUINONE OXIDOREDUCTASE SUBUNIT F; 1.
DR   Pfam; PF01257; 2Fe-2S_thioredx; 1.
DR   Pfam; PF01512; Complex1_51K; 1.
DR   Pfam; PF14697; Fer4_21; 1.
DR   Pfam; PF10589; NADH_4Fe-4S; 1.
DR   Pfam; PF10531; SLBB; 1.
DR   SMART; SM00928; NADH_4Fe-4S; 1.
DR   SUPFAM; SSF54862; 4Fe-4S ferredoxins; 1.
DR   SUPFAM; SSF142019; Nqo1 FMN-binding domain-like; 1.
DR   SUPFAM; SSF142984; Nqo1 middle domain-like; 1.
DR   SUPFAM; SSF140490; Nqo1C-terminal domain-like; 1.
DR   SUPFAM; SSF52833; Thioredoxin-like; 1.
DR   PROSITE; PS00198; 4FE4S_FER_1; 1.
DR   PROSITE; PS51379; 4FE4S_FER_2; 2.
DR   PROSITE; PS00645; COMPLEX1_51K_2; 1.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   3: Inferred from homology;
KW   4Fe-4S {ECO:0000256|ARBA:ARBA00022485};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW   FMN {ECO:0000256|ARBA:ARBA00022643}; Iron {ECO:0000256|ARBA:ARBA00023004};
KW   Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   NAD {ECO:0000256|ARBA:ARBA00023027};
KW   Translocase {ECO:0000256|ARBA:ARBA00022967}.
FT   DOMAIN          556..585
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51379"
FT   DOMAIN          586..615
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51379"
SQ   SEQUENCE   632 AA;  69840 MW;  E5E1A2990A5BC59B CRC64;
     MKVTNIEKLK EKILKSRDKT KTWVTVCGGT GCQAYGCQKV VKAFQEEIKR LGLGDSVGVR
     TTGCHGFCEK GPLVVIQPEG IFYQRVSVED VPEIINETVV NKKIVERLLY KDPQTGQKII
     HEHDVPFYSK QKRIIFGNNG LIDPTDIRDY IAVDGYQALS KVLFEMTAEE VIEEIKKSGL
     RGRGGAGFLT GLKWEICRRV SSPVKYLICN ADEGDPGAYM DRSLLEGNPH SVIEGMVIGA
     YAIGATEGFI YVRLEYPLAV KNITLAIEQA REFGFLGDSI LGSEFSFDLH VFKGAGAFVS
     GEETSLMASI EGRRAFPRQK PPFPAQKGLW GRPTNINNVE TWANVPLIIK KGADWYSQIG
     TRTSKGTKIF SLVGKINNTG LVEVPMGITL REIIYDIGGG IKDNKKFKAV QTGGPSGGCI
     PAEMLDLPID FDTLTKAGSM MGSGGMIVMD EDTCMVDVAR YFLQFTQEES CGKCVPCRLG
     TRQLYEILTR ITKGEGEEED LKRLEDLAKT IKAGSLCGLG QTAPNPVLTT LKYFRHEYEA
     HIKRKECPAL SCKDLIIYYI EPDKCVGCLL CLKNCPVGAI SGERKKVHVI NQDLCVKCGA
     CYEVCPPKIR AVSKYTGRKK EAILKKEKQS KE
//
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