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Database: UniProt
Entry: A0A1M5MP58_9FIRM
LinkDB: A0A1M5MP58_9FIRM
Original site: A0A1M5MP58_9FIRM 
ID   A0A1M5MP58_9FIRM        Unreviewed;       604 AA.
AC   A0A1M5MP58;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   SubName: Full=NADH-quinone oxidoreductase subunit F {ECO:0000313|EMBL:SHG78977.1};
GN   ORFNames=SAMN02745221_00982 {ECO:0000313|EMBL:SHG78977.1};
OS   Thermosyntropha lipolytica DSM 11003.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Syntrophomonadaceae;
OC   Thermosyntropha.
OX   NCBI_TaxID=1123382 {ECO:0000313|EMBL:SHG78977.1, ECO:0000313|Proteomes:UP000242329};
RN   [1] {ECO:0000313|Proteomes:UP000242329}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 11003 {ECO:0000313|Proteomes:UP000242329};
RA   Varghese N., Submissions S.;
RL   Submitted (NOV-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; FQWY01000012; SHG78977.1; -; Genomic_DNA.
DR   RefSeq; WP_073090867.1; NZ_FQWY01000012.1.
DR   AlphaFoldDB; A0A1M5MP58; -.
DR   STRING; 1123382.SAMN02745221_00982; -.
DR   OrthoDB; 9761899at2; -.
DR   Proteomes; UP000242329; 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; PF13237; Fer4_10; 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:UP000242329};
KW   Translocase {ECO:0000256|ARBA:ARBA00022967}.
FT   DOMAIN          547..576
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51379"
FT   DOMAIN          577..604
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51379"
SQ   SEQUENCE   604 AA;  66536 MW;  69E13528101E7B00 CRC64;
     MKENNVKEKG CTKIMVCCGT GCTANGARQV LARLEEKLRG NKNFEVVPVL KATGCNGWCE
     KGPLVKIMPE DITYCQVKAE DVDEIIEKTL LRGEKIKRLL YRDPQTKEFL VSLHQTDFYR
     KQKKIALRNI GEIDPASIDD YIERDGYKAL EKALKYMTPD EVLEEVIKSG LRGRGGGGFP
     TGRKWQACKK VPRFPKYIIC NGDEGDPGAF MDRSIMEGDP HTIIEGMLIC AYVLQAEKGF
     IYVRDEYDLA VKHLTQAILD ARRCGFLGKN ILGSSLSFDI ELVRGGGAFV CGEETALIKS
     IEGFPGEPRD KYIFPTESGL WGQPTVINNV ETWANIPVII LEGGEKFASL GTEGSKGTKV
     FSLVGKVVNT GLVEVPMGIT LREIIYEIGG GIPNGRQFKA VQTGGPSGGC IPAQLLDLEI
     DFDTLTREGS MMGSGGIIVM DDTTCMVEVA RYYTNFLAVE SCGKCTPCRE GLRALLAILT
     RIVKGEGKME DLELLQEISE VMQEASLCAL GRTAPNPVLS TLKYFQDEYV AHIIDRRCPA
     GVCPELTVFE IDAELCTGCT LCQKNCPVDA ITGEAKKAHI IQQDKCIRCG ECYRSCRFRA
     VKVK
//
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