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Database: UniProt
Entry: A0A0D6XAJ7_THEFI
LinkDB: A0A0D6XAJ7_THEFI
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ID   A0A0D6XAJ7_THEFI        Unreviewed;       437 AA.
AC   A0A0D6XAJ7;
DT   27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT   27-MAY-2015, sequence version 1.
DT   27-MAR-2024, entry version 31.
DE   RecName: Full=NADH-quinone oxidoreductase subunit F {ECO:0000256|RuleBase:RU364066};
DE            EC=7.1.1.- {ECO:0000256|RuleBase:RU364066};
GN   ORFNames=THFILI_03600 {ECO:0000313|EMBL:KIX84697.1};
OS   Thermus filiformis.
OC   Bacteria; Deinococcota; Deinococci; Thermales; Thermaceae; Thermus.
OX   NCBI_TaxID=276 {ECO:0000313|EMBL:KIX84697.1, ECO:0000313|Proteomes:UP000030364};
RN   [1] {ECO:0000313|EMBL:KIX84697.1, ECO:0000313|Proteomes:UP000030364}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43280 {ECO:0000313|EMBL:KIX84697.1,
RC   ECO:0000313|Proteomes:UP000030364};
RA   Mandelli F., Ramires B.O., Paixao D.A., Camilo C.M., Polikarpov I.,
RA   Couger M.B., Prade R., Riano-Pachon D.M., Squina F.M.;
RT   "Draft Genome Sequence of the thermophile Thermus filiformis ATCC43280
RT   producer of carotenoid-(di)glucoside-branched fatty acids (di)esters.";
RL   Submitted (FEB-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur
CC       (Fe-S) centers, to quinones in the respiratory chain.
CC       {ECO:0000256|RuleBase:RU364066}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a quinone + 5 H(+)(in) + NADH = a quinol + 4 H(+)(out) +
CC         NAD(+); Xref=Rhea:RHEA:57888, ChEBI:CHEBI:15378, ChEBI:CHEBI:24646,
CC         ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:132124;
CC         Evidence={ECO:0000256|RuleBase:RU364066};
CC   -!- COFACTOR:
CC       Name=FMN; Xref=ChEBI:CHEBI:58210;
CC         Evidence={ECO:0000256|ARBA:ARBA00001917,
CC         ECO:0000256|RuleBase:RU364066};
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000256|ARBA:ARBA00001966,
CC         ECO:0000256|RuleBase:RU364066};
CC   -!- SIMILARITY: Belongs to the complex I 51 kDa subunit family.
CC       {ECO:0000256|ARBA:ARBA00007523, ECO:0000256|RuleBase:RU364066}.
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:KIX84697.1}.
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DR   EMBL; JPSL02000037; KIX84697.1; -; Genomic_DNA.
DR   RefSeq; WP_038067476.1; NZ_JPSL02000037.1.
DR   AlphaFoldDB; A0A0D6XAJ7; -.
DR   STRING; 276.THFILI_03600; -.
DR   OrthoDB; 9761899at2; -.
DR   Proteomes; UP000030364; Unassembled WGS sequence.
DR   GO; GO:0045271; C:respiratory chain complex I; IEA:UniProt.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0010181; F:FMN binding; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0051287; F:NAD binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0008137; F:NADH dehydrogenase (ubiquinone) activity; IEA:InterPro.
DR   GO; GO:0048038; F:quinone binding; IEA:UniProtKB-KW.
DR   Gene3D; 3.10.20.600; -; 1.
DR   Gene3D; 6.10.250.1450; -; 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; IPR001949; NADH-UbQ_OxRdtase_51kDa_CS.
DR   InterPro; IPR011537; NADH-UbQ_OxRdtase_suF.
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   NCBIfam; TIGR01959; nuoF_fam; 1.
DR   PANTHER; PTHR43578; NADH-QUINONE OXIDOREDUCTASE SUBUNIT F; 1.
DR   PANTHER; PTHR43578:SF1; NADH-QUINONE OXIDOREDUCTASE SUBUNIT F; 1.
DR   Pfam; PF01512; Complex1_51K; 1.
DR   Pfam; PF10589; NADH_4Fe-4S; 1.
DR   Pfam; PF10531; SLBB; 1.
DR   SMART; SM00928; NADH_4Fe-4S; 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   PROSITE; PS00644; COMPLEX1_51K_1; 1.
DR   PROSITE; PS00645; COMPLEX1_51K_2; 1.
PE   3: Inferred from homology;
KW   4Fe-4S {ECO:0000256|ARBA:ARBA00022485, ECO:0000256|RuleBase:RU364066};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630,
KW   ECO:0000256|RuleBase:RU364066};
KW   FMN {ECO:0000256|ARBA:ARBA00022643, ECO:0000256|RuleBase:RU364066};
KW   Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|RuleBase:RU364066};
KW   Iron-sulfur {ECO:0000256|ARBA:ARBA00023014, ECO:0000256|RuleBase:RU364066};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|RuleBase:RU364066};
KW   NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|RuleBase:RU364066};
KW   Oxidoreductase {ECO:0000313|EMBL:KIX84697.1};
KW   Quinone {ECO:0000256|RuleBase:RU364066};
KW   Translocase {ECO:0000256|ARBA:ARBA00022967}.
FT   DOMAIN          337..383
FT                   /note="NADH-ubiquinone oxidoreductase 51kDa subunit iron-
FT                   sulphur binding"
FT                   /evidence="ECO:0000259|SMART:SM00928"
SQ   SEQUENCE   437 AA;  48448 MW;  24DA252CFF4AE568 CRC64;
     MTGPIVSGHD PRFERTLYAH VGKEGSWTLD YYLRHGGYET ARRVLKEKTP DEVIEEVKRS
     GLRGRGGAGF PTGLKWSFMP KDGKQHYLIC NADESEPGSF KDRYILEDVP HLLIEGMILA
     GYAIRATVGY IYVRGEYRRA YDRLVAAIRE AQARGYLGDD LFGSGFSFRL YVHRGAGAYI
     CGEETALMNS LEGLRANPRL KPPFPAQAGL WGKPTTINNV ETLASVVPIL ERGADWFAQM
     GTERSKGMKL YQVSGPVKRP GVYELPMGTT FRELIYDWAG GPLEPIQALI PGGSSTPPLP
     FTDEVLDTPM DYESLQAKGS LLGTGGVILI PERVSMVDAM WNVTRFYAHE SCGKCTPCRE
     GVAGFMVNLF AKIGTGQGEE EDVENLENLL DLIEGRSFCP LADAAVWPVR GSLKHFKDQY
     LALAKEKKPV PRVSLWR
//
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