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Database: UniProt
Entry: A0A417HBH4_9FIRM
LinkDB: A0A417HBH4_9FIRM
Original site: A0A417HBH4_9FIRM 
ID   A0A417HBH4_9FIRM        Unreviewed;       624 AA.
AC   A0A417HBH4;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   27-MAR-2024, entry version 16.
DE   SubName: Full=NADH-quinone oxidoreductase subunit NuoF {ECO:0000313|EMBL:RHT69163.1};
GN   ORFNames=DW741_13130 {ECO:0000313|EMBL:RHT69163.1};
OS   Ruminococcaceae bacterium AM28-23LB.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae.
OX   NCBI_TaxID=2292269 {ECO:0000313|EMBL:RHT69163.1, ECO:0000313|Proteomes:UP000284026};
RN   [1] {ECO:0000313|EMBL:RHT69163.1, ECO:0000313|Proteomes:UP000284026}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AM28-23LB {ECO:0000313|EMBL:RHT69163.1,
RC   ECO:0000313|Proteomes:UP000284026};
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:RHT69163.1}.
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DR   EMBL; QUJM01000043; RHT69163.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A417HBH4; -.
DR   OrthoDB; 9761899at2; -.
DR   Proteomes; UP000284026; 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; 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; PS00198; 4FE4S_FER_1; 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:UP000284026};
KW   Translocase {ECO:0000256|ARBA:ARBA00022967}.
FT   DOMAIN          567..596
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51379"
FT   DOMAIN          597..624
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51379"
SQ   SEQUENCE   624 AA;  68044 MW;  5FA9CE0B61767C3F CRC64;
     MLKTREELSV LRQTLEGRFA SQVKKILVCA GTGCVAGGSL DIYARLVELL QEKGIHCQVD
     LAHEPHGDDV GVKRSGCHGF CEMGPLVRIE PQGWLYIKVK KDDCQEIIEK TILGGEPIER
     LCYKMNGEIY KTQEEIPFYK KQTRTVLEHC GHIDATSIQE YIAIGGYKAF EKALFDMDGQ
     EIVEEIQKSN LRGRGGGGFP AGRKWAQVRA QEATPKYIVC NGDEGDPGAF MDRSVMEGDP
     HRLLEGMMIA GVACGASQGY IYVRAEYPMA VSRLDGAIRQ ARELGLLGEN ILGSGFDFDI
     HISRGAGAFV CGEGSALTAS IEGRRGMPRV KPPRTVERGL FDKPTVLNNV ETLANVPHII
     TRGADWYRSI GPENSPGTKA FALTGNIQNT GLIEVPMGTT LREIIFDIGG GMRNGAEFKA
     VQIGGPSGGC LTKEHLDLPL DFDSLKKVGA MIGSGGLVVM DDKTCMVEVA RFFMNFTQNE
     SCGKCVPCRE GTKRMLEILE RIVAGQGKDG DIDLLLELAE TISATALCGL GKTAAQPVVS
     TIRYFRDEYE AHVKEKRCPT HNCQKLKRYY IDPQECKGCS KCARMCPVGA ISGEIRSPFT
     IDPDKCIKCG ACFGGCSFHA VKEG
//
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