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Database: UniProt
Entry: A0A416JSS6_9FIRM
LinkDB: A0A416JSS6_9FIRM
Original site: A0A416JSS6_9FIRM 
ID   A0A416JSS6_9FIRM        Unreviewed;       595 AA.
AC   A0A416JSS6;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   24-JAN-2024, entry version 14.
DE   SubName: Full=NADH-quinone oxidoreductase subunit NuoF {ECO:0000313|EMBL:RHQ16009.1};
GN   ORFNames=DW974_10245 {ECO:0000313|EMBL:RHQ16009.1};
OS   Lachnospiraceae bacterium AM48-27BH.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae.
OX   NCBI_TaxID=2292271 {ECO:0000313|EMBL:RHQ16009.1, ECO:0000313|Proteomes:UP000285913};
RN   [1] {ECO:0000313|EMBL:RHQ16009.1, ECO:0000313|Proteomes:UP000285913}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AM48-27BH {ECO:0000313|EMBL:RHQ16009.1,
RC   ECO:0000313|Proteomes:UP000285913};
RA   Zou Y., Xue W., Luo G.;
RT   "A genome reference for cultivated species of the human gut microbiota.";
RL   Submitted (AUG-2018) 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:RHQ16009.1}.
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DR   EMBL; QUFC01000017; RHQ16009.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A416JSS6; -.
DR   Proteomes; UP000285913; Unassembled WGS sequence.
DR   GO; GO:0110165; C:cellular anatomical entity; IEA:UniProt.
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; 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:SF3; HYDROGENASE SUBUNIT; 1.
DR   PANTHER; PTHR43578; NADH-QUINONE OXIDOREDUCTASE SUBUNIT F; 1.
DR   Pfam; PF01257; 2Fe-2S_thioredx; 1.
DR   Pfam; PF01512; Complex1_51K; 1.
DR   Pfam; PF00037; Fer4; 2.
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; PS51379; 4FE4S_FER_2; 2.
DR   PROSITE; PS00645; COMPLEX1_51K_2; 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   Reference proteome {ECO:0000313|Proteomes:UP000285913};
KW   Translocase {ECO:0000256|ARBA:ARBA00022967}.
FT   DOMAIN          538..567
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51379"
FT   DOMAIN          568..595
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51379"
SQ   SEQUENCE   595 AA;  64627 MW;  1A7E9C8D488A2A01 CRC64;
     MYRSHVLVCG GTGCTSSGSQ QIIETLKAEL EKNGLSNEVS VVQTGCHGLC ALGPIMIVYP
     DAAFYSMVKV EDIPEIVEEH LLKGRVVTRL LYKETVTPNG IRALSDTDFY KKQHRIALRN
     CGVINPEIIE EYIGTGGYQA LGKVLTKMTP DDVIQCLLDS GLRGRGGGGF PTGLKWKLAK
     GNDADQKYVC CNADEGDPGA FMDRSILEGD PHAVLEAMAI AGYAIGASQG YIYVRAEYPI
     AVQRLRIAIE QAREMELLGK DIFGTGFDFD IDLRLGAGAF VCGEETALMT SIEGNRGEPR
     PRPPFPAQKG LFGKPTILNN VETYANIPQI ILNGPEWFAS MGTEKSKGTK VFALGGKIHN
     TGLVEIPMGT TLREVIEEIG GGIPNGKKFK AAQTGGPSGG CIPAEHFDIP IDYDNLISIG
     SMMGSGGLIV MDETDCMVDI AKFFLEFTVE ESCGKCTPCR VGTKRMLEIL TKITKGQATM
     EDLDKLEELC YYIKENSLCG LGQTAPNPVL STLHYFRDEY EAHIKEKRCP AGVCKALLSY
     HIDSSKCKGC TLCARNCPNS AIIGTVRNPH IIDQEKCIKC GACMEKCKFG AIYKK
//
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