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Database: UniProt
Entry: A0A2K2FMW8_9FIRM
LinkDB: A0A2K2FMW8_9FIRM
Original site: A0A2K2FMW8_9FIRM 
ID   A0A2K2FMW8_9FIRM        Unreviewed;       598 AA.
AC   A0A2K2FMW8;
DT   28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT   28-MAR-2018, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   SubName: Full=NADH-quinone oxidoreductase subunit F {ECO:0000313|EMBL:PNU01445.1};
GN   ORFNames=CDQ84_00065 {ECO:0000313|EMBL:PNU01445.1};
OS   Pseudoclostridium thermosuccinogenes.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae;
OC   Pseudoclostridium.
OX   NCBI_TaxID=84032 {ECO:0000313|EMBL:PNU01445.1, ECO:0000313|Proteomes:UP000236151};
RN   [1] {ECO:0000313|EMBL:PNU01445.1, ECO:0000313|Proteomes:UP000236151}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 5806 {ECO:0000313|EMBL:PNU01445.1,
RC   ECO:0000313|Proteomes:UP000236151};
RA   Koendjbiharie J.G., van Kranenburg R.;
RT   "Investigating the central metabolism of Clostridium thermosuccinogenes.";
RL   Submitted (JUN-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:PNU01445.1}.
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DR   EMBL; NIOJ01000001; PNU01445.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2K2FMW8; -.
DR   KEGG; cthd:CDO33_16055; -.
DR   OrthoDB; 9761899at2; -.
DR   Proteomes; UP000236151; 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.
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   Reference proteome {ECO:0000313|Proteomes:UP000236151};
KW   Translocase {ECO:0000256|ARBA:ARBA00022967}.
FT   DOMAIN          540..569
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51379"
FT   DOMAIN          570..598
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51379"
SQ   SEQUENCE   598 AA;  65169 MW;  3A5C3A3926F74F06 CRC64;
     MQIYRAHVLV CGGTGCTSSN SEKIIKEFET RLKETNLENE VKVIRTGCFG LCAQGPIVIV
     YPEGSMYTQV KVEDVQEIVE EHLLKGRLVK RLLIGDIDVE DVTKSLENVD FFKRQKRIAL
     RNCGVINPEN IDEYIAYDGY KALEKVLTEM TPAEVIDIVK RSGIRGRGGA GFPTGLKWEF
     ASKSQNEQKY VCCNADEGDP GAFMDRSVLE GDPHSVIEAM AIAGYAIGAN QGYIYVRAEY
     PIAVKRLNIA IAQAKEYGLL GKNILGTGFD FDLELRLGAG AFVCGEETAL MTSIEGKRGE
     PRPRPPFPAV KGLWQKPTIL NNVETYANIP QIILKGPEWF SSIGTEKSKG TKVFAVGGKI
     NHTGLVEVEM GTTLREVIYD IGGGIPNGKK FKAAQMGGPS GGCIPAEHLD TPIDYDSLIQ
     LGAMMGSGGL IVMDEDSCMV DIAKFFLEFT VDESCGKCPP CRIGTKRMLE ILERITSGKG
     EEGDIEKLEL LAKNIKAAAL CGLGQTAPNP VLSTLRYFRD EYIAHVKDKK CPAGVCKALM
     SYTVFEDKCR SCGICAKQCP VGAISGQKGV PYKINKDKCI KCGVCEQKCP FKAIAKAN
//
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