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Database: UniProt
Entry: V9VZG4_9RHOB
LinkDB: V9VZG4_9RHOB
Original site: V9VZG4_9RHOB 
ID   V9VZG4_9RHOB            Unreviewed;       562 AA.
AC   V9VZG4;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   27-MAR-2024, entry version 49.
DE   SubName: Full=NADH-quinone oxidoreductase subunit F {ECO:0000313|EMBL:AHD02267.1};
GN   ORFNames=METH_18085 {ECO:0000313|EMBL:AHD02267.1};
OS   Leisingera methylohalidivorans DSM 14336.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Leisingera.
OX   NCBI_TaxID=999552 {ECO:0000313|EMBL:AHD02267.1, ECO:0000313|Proteomes:UP000018780};
RN   [1] {ECO:0000313|EMBL:AHD02267.1, ECO:0000313|Proteomes:UP000018780}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 14336 {ECO:0000313|EMBL:AHD02267.1,
RC   ECO:0000313|Proteomes:UP000018780};
RG   DOE Joint Genome Institute;
RA   Klenk H.-P., Huntemann M., Han J., Chen A., Kyrpides N., Mavromatis K.,
RA   Markowitz V., Palaniappan K., Ivanova N., Schaumberg A., Pati A.,
RA   Liolios K., Nordberg H.P., Cantor M.N., Hua S.X., Woyke T.;
RL   Submitted (SEP-2013) 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; CP006773; AHD02267.1; -; Genomic_DNA.
DR   RefSeq; WP_024091759.1; NC_023135.1.
DR   AlphaFoldDB; V9VZG4; -.
DR   STRING; 999552.METH_18085; -.
DR   KEGG; lmd:METH_18085; -.
DR   PATRIC; fig|999552.6.peg.3584; -.
DR   HOGENOM; CLU_014881_3_1_5; -.
DR   OrthoDB; 9761899at2; -.
DR   Proteomes; UP000018780; Chromosome.
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; cd03082; TRX_Fd_NuoE_W_FDH_beta; 1.
DR   Gene3D; 3.10.20.600; -; 1.
DR   Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR   Gene3D; 1.10.10.1590; NADH-quinone oxidoreductase subunit E; 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; IPR011538; Nuo51_FMN-bd.
DR   InterPro; IPR037225; Nuo51_FMN-bd_sf.
DR   InterPro; IPR041921; NuoE_N.
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; 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   SUPFAM; SSF52833; Thioredoxin-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};
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   Translocase {ECO:0000256|ARBA:ARBA00022967}.
FT   DOMAIN          486..531
FT                   /note="NADH-ubiquinone oxidoreductase 51kDa subunit iron-
FT                   sulphur binding"
FT                   /evidence="ECO:0000259|SMART:SM00928"
FT   REGION          1..26
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   562 AA;  61226 MW;  DD52B9BBF3BDA260 CRC64;
     MAPLDDSKGV WKSGKGKGRR TPKGRQVDDI ALSEVQELLG DRPRNRDLLI EFLHLIQDKY
     GCLSAAHIRA LAEEMRTGQA EIYEVATFYA HFDVVKEGET PPPALTIRVC DSLSCELAGA
     QQLQKALEDG LDASQVRVLR APCMGRCDTA PVLEIGHNHI DHATPEKVQA AIAANDTHAH
     VPDYETFAAY EAEGGYATLK DLRANGDWEA VQAKVKEAGL RGLGGAGFPS GTKWGFVRAN
     EGPRYLAVNG DEGEPGTFKD RYYLERTPHV FLEGMLMAAW AVEAEKAFIY MRDEYPAVLE
     ILATEIRALE DAGIVEEGYI DLRRGAGAYI CGEESAMIES IEGKRGEPRH RPPFVAQVGV
     FGRPTLVHNV ETLYWVCKIN REGPECLNSV EKNGRKGLRS YSVSGRVKNP GVHMLPAGST
     ITDIIEACGG MIDGHAFKAY QPGGPSSGLL PASMNDIPLD FDTLQPHGTF IGSAAVVVLS
     DQDSARDAAL NMLRFFEDES CGQCTPCRVG CEKAVKLMSE KKWDQGLLEE LSTAMVDTSI
     CGLGQAAPNP IRLTIKHFPE EV
//
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