ID   NUOF_MYCBO              Reviewed;         445 AA.
AC   P65568; A0A1R3Y397; P95176; X2BN76;
DT   11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   02-SEP-2026, entry version 115.
DE   RecName: Full=NADH-quinone oxidoreductase subunit F;
DE            EC=7.1.1.-;
DE   AltName: Full=NADH dehydrogenase I subunit F;
DE   AltName: Full=NDH-1 subunit F;
GN   Name=nuoF; OrderedLocusNames=BQ2027_MB3174;
OS   Mycobacterium bovis (strain ATCC BAA-935 / AF2122/97).
OC   Bacteria; Bacillati; Actinomycetota; Actinomycetes; Mycobacteriales;
OC   Mycobacteriaceae; Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=233413;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-935 / AF2122/97;
RX   PubMed=12788972; DOI=10.1073/pnas.1130426100;
RA   Garnier T., Eiglmeier K., Camus J.-C., Medina N., Mansoor H., Pryor M.,
RA   Duthoy S., Grondin S., Lacroix C., Monsempe C., Simon S., Harris B.,
RA   Atkin R., Doggett J., Mayes R., Keating L., Wheeler P.R., Parkhill J.,
RA   Barrell B.G., Cole S.T., Gordon S.V., Hewinson R.G.;
RT   "The complete genome sequence of Mycobacterium bovis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:7877-7882(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC   STRAIN=ATCC BAA-935 / AF2122/97;
RX   PubMed=28385856; DOI=10.1128/genomea.00157-17;
RA   Malone K.M., Farrell D., Stuber T.P., Schubert O.T., Aebersold R.,
RA   Robbe-Austerman S., Gordon S.V.;
RT   "Updated reference genome sequence and annotation of Mycobacterium bovis
RT   AF2122/97.";
RL   Genome Announc. 5:E00157-E00157(2017).
CC   -!- FUNCTION: NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur
CC       (Fe-S) centers, to quinones in the respiratory chain. The immediate
CC       electron acceptor for the enzyme in this species is believed to be
CC       menaquinone. Couples the redox reaction to proton translocation (for
CC       every two electrons transferred, four hydrogen ions are translocated
CC       across the cytoplasmic membrane), and thus conserves the redox energy
CC       in a proton gradient (By similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a quinone + NADH + 5 H(+)(in) = a quinol + NAD(+) + 4
CC         H(+)(out); Xref=Rhea:RHEA:57888, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:24646, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945,
CC         ChEBI:CHEBI:132124;
CC   -!- COFACTOR:
CC       Name=FMN; Xref=ChEBI:CHEBI:58210; Evidence={ECO:0000305};
CC       Note=Binds 1 FMN. {ECO:0000305};
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Evidence={ECO:0000305};
CC       Note=Binds 1 [4Fe-4S] cluster. {ECO:0000305};
CC   -!- SIMILARITY: Belongs to the complex I 51 kDa subunit family.
CC       {ECO:0000305}.
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DR   EMBL; LT708304; SIU01801.1; -; Genomic_DNA.
DR   RefSeq; WP_003416439.1; NC_002945.4.
DR   AlphaFoldDB; P65568; -.
DR   SMR; P65568; -.
DR   GeneID; 45427137; -.
DR   KEGG; mbo:BQ2027_MB3174; -.
DR   PATRIC; fig|233413.5.peg.3492; -.
DR   Proteomes; UP000001419; Chromosome.
DR   GO; GO:0045271; C:respiratory chain complex I; IEA:UniProtKB-ARBA.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:InterPro.
DR   GO; GO:0010181; F:FMN binding; IEA:InterPro.
DR   GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR   GO; GO:0008137; F:NADH dehydrogenase (ubiquinone) activity; IEA:InterPro.
DR   GO; GO:0045333; P:cellular respiration; IEA:TreeGrafter.
DR   FunFam; 1.20.1440.230:FF:000001; Mitochondrial NADH dehydrogenase flavoprotein 1; 1.
DR   FunFam; 3.40.50.11540:FF:000001; NADH dehydrogenase [ubiquinone] flavoprotein 1, mitochondrial; 1.
DR   FunFam; 3.10.20.600:FF:000003; NADH-quinone oxidoreductase subunit F; 1.
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; IPR050837; ComplexI_51kDa_subunit.
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   NCBIfam; NF010120; PRK13596.1; 1.
DR   PANTHER; PTHR11780:SF10; NADH DEHYDROGENASE [UBIQUINONE] FLAVOPROTEIN 1, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR11780; NADH-UBIQUINONE OXIDOREDUCTASE FLAVOPROTEIN 1 NDUFV1; 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; Flavoprotein; FMN; Iron; Iron-sulfur; Metal-binding; NAD; Quinone;
KW   Reference proteome; Translocase.
FT   CHAIN           1..445
FT                   /note="NADH-quinone oxidoreductase subunit F"
FT                   /id="PRO_0000118575"
FT   BINDING         61..70
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         177..224
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000250"
FT   BINDING         353
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255"
FT   BINDING         356
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255"
FT   BINDING         359
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255"
FT   BINDING         399
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   445 AA;  48102 MW;  C02A660F43842926 CRC64;
     MTTQATPLTP VISRHWDDPE SWTLATYQRH DRYRGYQALQ KALTMPPDDV ISIVKDSGLR
     GRGGAGFATG TKWSFIPQGD TGAAAKPHYL VVNADESEPG TCKDIPLMLA TPHVLIEGVI
     IAAYAIRAHH AFVYVRGEVV PVLRRLHNAV AEAYAAGFLG RNIGGSGFDL ELVVHAGAGA
     YICGEETALL DSLEGRRGQP RLRPPFPAVA GLYGCPTVIN NVETIASVPS IILGGIDWFR
     SMGSEKSPGF TLYSLSGHVT RPGQYEAPLG ITLRELLDYA GGVRAGHRLK FWTPGGSSTP
     LLTDEHLDVP LDYEGVGAAG SMLGTKALEI FDETTCVVRA VRRWTEFYKH ESCGKCTPCR
     EGTFWLDKIY ERLETGRGSH EDIDKLLDIS DSILGKSFCA LGDGAASPVM SSIKHFRDEY
     LAHVEGGGCP FDPRDSMLVA NGVDA
//