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Database: UniProt
Entry: A0A1W9PCD5_9BACT
LinkDB: A0A1W9PCD5_9BACT
Original site: A0A1W9PCD5_9BACT 
ID   A0A1W9PCD5_9BACT        Unreviewed;       633 AA.
AC   A0A1W9PCD5;
DT   05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2017, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   SubName: Full=NADH-quinone oxidoreductase subunit F {ECO:0000313|EMBL:OQX56064.1};
GN   ORFNames=B5M54_00175 {ECO:0000313|EMBL:OQX56064.1};
OS   Candidatus Aminicenantes bacterium 4484_214.
OC   Bacteria; Candidatus Aminicenantes.
OX   NCBI_TaxID=1968529 {ECO:0000313|EMBL:OQX56064.1, 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:OQX56064.1}.
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DR   EMBL; MZGL01000001; OQX56064.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1W9PCD5; -.
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; -; 2.
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   633 AA;  70068 MW;  B9349AB4263EBF0C CRC64;
     MKITNIEKLK EKVINSRDKT KTWVTVCGGT GCRAYGCMKV VEAFQEEIKK KNLVDTVGVR
     TTGCHGFCER GPLVVIQPEG IFYQRVGVDD VPAIVEETVV NKKIVEKLLY RDPQTKQAII
     HEQDVPFYSK QKRIIFGNNG LIDPTDIRDY IAVDGYQALA KVLFEMTADE VIEEIKKSGL
     RGRGGAGFLT GLKWEICRRE SAPIKYLICN ADEGDPGAYM DRSLLEGNPH SVIEGMIIGA
     YAIGATEGFI YVRMEYPLAV KNITIAIEQA RKFGLLGESI LGSEFSFELH VFKGAGAFVS
     GEETSLMASI EGRRAFPRQK PPFPAQKGLW GYPTNINNVE TWANVPFIIN KGADWYSKIG
     TKSSKGTKIF SLVGKINNTG LVEVPMGISL REIIYEIGGG IKDNKKFKAV QTGGPSGGCI
     PAEMLDLPID FDTLTKAGSM MGSGGMIVMD EDTCMVDVAR YFLQFTQEES CGKCVPCRLG
     TRQLYEILTR ITKGQGKPED LKRLEDLAKT VKTGSLCGLG QTAPNPVLTT LKYFRHEYEA
     HIFRHECPAL SCKDLIIYYI EPEKCVGCLL CLKNCPVGAI SGERKQVHVI DQELCVKCGA
     CLDVCPPKVR AVSKYTGKKK QQILNKEKKA RRR
//
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