ID A0A1H3CP36_9FIRM Unreviewed; 627 AA.
AC A0A1H3CP36;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=NADH-quinone oxidoreductase subunit F {ECO:0000313|EMBL:SDX55189.1};
GN ORFNames=SAMN02910264_00126 {ECO:0000313|EMBL:SDX55189.1};
OS Ruminococcaceae bacterium YAD3003.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae.
OX NCBI_TaxID=1520816 {ECO:0000313|EMBL:SDX55189.1, ECO:0000313|Proteomes:UP000199204};
RN [1] {ECO:0000313|EMBL:SDX55189.1, ECO:0000313|Proteomes:UP000199204}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YAD3003 {ECO:0000313|EMBL:SDX55189.1,
RC ECO:0000313|Proteomes:UP000199204};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the complex I 51 kDa subunit family.
CC {ECO:0000256|ARBA:ARBA00007523}.
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DR EMBL; FNPA01000001; SDX55189.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H3CP36; -.
DR STRING; 1520816.SAMN02910264_00126; -.
DR OrthoDB; 9761899at2; -.
DR Proteomes; UP000199204; 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; PF12838; Fer4_7; 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.
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:UP000199204};
KW Translocase {ECO:0000256|ARBA:ARBA00022967}.
FT DOMAIN 563..592
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 600..627
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
SQ SEQUENCE 627 AA; 67688 MW; D0454376D4DAB11C CRC64;
MISTVNDLNE RFEALSKSLD DKIKGGDGKR HIVLCGGTGC LSAHSTEIME RFNALIKEKG
IEDKATVNQV GCFGFCSQGP FVKIYPEDTL YKMVKIEDVD EIVEKDLIGG EIVDRLLYVD
PKTNEKVTKQ EDILFYKKQR RVALNGCGVI NPEDINEAIG NGAFQGIKRA LTMTQQEVID
EVLASGLRGR GGGGFPTGRK WQFALNVEAD QKYVVCNGDE GDPGAFMDRS ILEGNPLAVI
EGMMIAGYAF GASEGYFYVR AEYPIAVKRL RIAIEQAKAE GLLGKNILGS DFSFDCQIRL
GAGAFVCGEE TALLNSIEGK RGMPRPRPPF PAIKGLWGKP TCVNNVETLA CVPYILREGA
ANFASVGTEK SKGTKVFALG GKVNNVGLVE VPMGTTLREL IYDIGGGIPD GKQFKAIQTG
GPSGGCLTAE YLDEPIDFDN LVAKGSMMGS GGAIVMDEDN CMVDVAKFYL EFICDESCGK
CTPCRIGTKR MLEILTRITE GKGTMKDLDE LEELSQTIKA NSLCALGQTA SNPVNSTLAH
FRDEYIAHIV DKKCPAHVCK NLMQYTIDAD KCIGCGMCAK GCPASCITRT DYVAEGHKLA
SMAIDADKCV KCGACISTCK FNAISKV
//
