ID Q8XCX1_ECO57 Unreviewed; 445 AA.
AC Q8XCX1; A0A0H3JMC5; A0A6M0JN80; Q7AC09;
DT 01-MAR-2002, integrated into UniProtKB/TrEMBL.
DT 01-MAR-2002, sequence version 1.
DT 27-MAR-2024, entry version 153.
DE RecName: Full=NADH-quinone oxidoreductase subunit F {ECO:0000256|ARBA:ARBA00019901, ECO:0000256|RuleBase:RU364066};
DE EC=7.1.1.- {ECO:0000256|RuleBase:RU364066};
GN Name=nuoF {ECO:0000313|EMBL:BAB36591.1};
GN ORFNames=ECs_3168 {ECO:0000313|EMBL:BAB36591.1};
OS Escherichia coli O157:H7.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83334 {ECO:0000313|EMBL:BAB36591.1, ECO:0000313|Proteomes:UP000000558};
RN [1] {ECO:0000313|EMBL:BAB36591.1, ECO:0000313|Proteomes:UP000000558}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC
RC {ECO:0000313|Proteomes:UP000000558};
RX PubMed=11258796; DOI=.1093/dnares/8.1.11;
RA Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA Han C.G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T.,
RA Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S.,
RA Shiba T., Hattori M., Shinagawa H.;
RT "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and
RT genomic comparison with a laboratory strain K-12.";
RL DNA Res. 8:11-22(2001).
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}.
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DR EMBL; BA000007; BAB36591.1; -; Genomic_DNA.
DR RefSeq; NP_311195.1; NC_002695.1.
DR RefSeq; WP_000789502.1; NZ_VOAI01000001.1.
DR AlphaFoldDB; Q8XCX1; -.
DR STRING; 155864.Z3543; -.
DR DNASU; 916876; -.
DR GeneID; 75205670; -.
DR GeneID; 916876; -.
DR KEGG; ecs:ECs_3168; -.
DR PATRIC; fig|386585.9.peg.3306; -.
DR eggNOG; COG1894; Bacteria.
DR HOGENOM; CLU_014881_0_1_6; -.
DR OMA; KWQFIPQ; -.
DR Proteomes; UP000000558; Chromosome.
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 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 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 Quinone {ECO:0000256|RuleBase:RU364066};
KW Reference proteome {ECO:0000313|Proteomes:UP000000558};
KW Translocase {ECO:0000256|ARBA:ARBA00022967}.
FT DOMAIN 336..381
FT /note="NADH-ubiquinone oxidoreductase 51kDa subunit iron-
FT sulphur binding"
FT /evidence="ECO:0000259|SMART:SM00928"
SQ SEQUENCE 445 AA; 49321 MW; 258F7CB6576676D0 CRC64;
MKNIIRTPET HPLTWRLRDD KQPVWLDEYR SKNGYEGARK ALTGLSPDEI VNQVKDAGLK
GRGGAGFSTG LKWSLMPKDE SMNIRYLLCN ADEMEPGTYK DRLLMEQLPH LLVEGMLISA
FALKAYRGYI FLRGEYIEAA VNLRRAIAEA TEAGLLGKNI MGTGFDFELF VHTGAGRYIC
GEETALINSL EGRRANPRSK PPFPATSGVW GKPTCVNNVE TLCNVPAILA NGVEWYQNIS
KSKDAGTKLM GFSGRVKNPG LWELPFGTTA REILEDYAGG MRDGLKFKAW QPGGAGTDFL
TEAHLDLPME FESIGKAGSR LGTALAMAVD HEINMVSLVR NLEEFFARES CGWCTPCRDG
LPWSVKILRA LERGEGQPGD IETLEQLCRF LGPGKTFCAH APGAVEPLQS AIKYFREEFE
AGIKQPFSNT HLINGIQPNL LKERW
//
