ID A0A2S8Y5H8_9PSED Unreviewed; 519 AA.
AC A0A2S8Y5H8;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 24-JAN-2024, entry version 18.
DE RecName: Full=NADH-quinone oxidoreductase subunit F {ECO:0000256|ARBA:ARBA00019901};
DE AltName: Full=NADH dehydrogenase I subunit F {ECO:0000256|ARBA:ARBA00031578};
DE AltName: Full=NDH-1 subunit F {ECO:0000256|ARBA:ARBA00032787};
GN ORFNames=CQZ98_15150 {ECO:0000313|EMBL:PRA52796.1};
OS Pseudomonas sp. MYb115.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=1848717 {ECO:0000313|EMBL:PRA52796.1, ECO:0000313|Proteomes:UP000239970};
RN [1] {ECO:0000313|EMBL:PRA52796.1, ECO:0000313|Proteomes:UP000239970}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MYb115 {ECO:0000313|EMBL:PRA52796.1,
RC ECO:0000313|Proteomes:UP000239970};
RA Zimmermann J., Obeng N., Yang W., Obeng O., Kissoyan K., Pees B.,
RA Dirksen P., Hoppner M., Franke A., Rosenstiel P., Leippe M., Dierking K.,
RA Kaleta C., Schulenburg H.;
RT "Genomic, metabolic, and phenotypic characteristics of bacterial isolates
RT from the natural microbiome of the model nematode Caenorhabditis elegans.";
RL Submitted (SEP-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the complex I 51 kDa subunit family.
CC {ECO:0000256|ARBA:ARBA00007523}.
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:PRA52796.1}.
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DR EMBL; PCQM01000010; PRA52796.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2S8Y5H8; -.
DR Proteomes; UP000239970; 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; cd03063; TRX_Fd_FDH_beta; 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; 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 PANTHER; PTHR43578:SF3; HYDROGENASE SUBUNIT; 1.
DR PANTHER; PTHR43578; 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};
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723}.
FT DOMAIN 425..471
FT /note="NADH-ubiquinone oxidoreductase 51kDa subunit iron-
FT sulphur binding"
FT /evidence="ECO:0000259|SMART:SM00928"
SQ SEQUENCE 519 AA; 54942 MW; DF5A967CAC7FE689 CRC64;
MPTLYLPTDS LARAVGADEV AVALITQARA RNLPLELQRT SSRGLYWLEP LLEVESPQGR
IGFGPLTAAD VPSVLDALQD PSSQHPLALG LVEALPYLKT QQRLLFARAG ITRPLSLDDY
RAHGGFEGLT RAVNLGGEQT ATEVFDSGLR GRGGAAFPAG IKWRTVRAAQ AEQKYIVCNA
DEGDSGTFAD RMLMEGDPFL LIEGMAIAGL CTGATFGYIY VRSEYPDAVA TLRQALNLAR
EAGYLGANVG GSGQAFDLEV RVGAGAYICG EETALLDSLE GKRGYVRAKP PIPALKGLFG
QPTLVHNVLT LASVPLILAK GAPFYRDYGM GRSLGTMPFQ LAGNVRQGGL VERAFGLTLR
ELVEDYGGGT ASGRPLKAAQ VGGPLGAWVP PSQFDTPLDY EAFAAIGAML GHGGVVVADD
SLDMAQMARF AMQFCAEESC GKCTPCRIGS TRGVEVIDRL LAAPEQSARD QQVVILKDLC
DTLQYGSLCA LGGMVSFPVA SALKHFPADF GVHASEAEQ
//