ID A0A1C2J765_ACITH Unreviewed; 419 AA.
AC A0A1C2J765;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=NADH-quinone oxidoreductase subunit F {ECO:0000313|EMBL:OCX69111.1};
GN ORFNames=A6M23_16055 {ECO:0000313|EMBL:OCX69111.1}, A6P07_14595
GN {ECO:0000313|EMBL:OCX70362.1};
OS Acidithiobacillus thiooxidans (Thiobacillus thiooxidans).
OC Bacteria; Pseudomonadota; Acidithiobacillia; Acidithiobacillales;
OC Acidithiobacillaceae; Acidithiobacillus.
OX NCBI_TaxID=930 {ECO:0000313|EMBL:OCX69111.1, ECO:0000313|Proteomes:UP000095008};
RN [1] {ECO:0000313|Proteomes:UP000094893, ECO:0000313|Proteomes:UP000095008}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=A02 {ECO:0000313|EMBL:OCX70362.1,
RC ECO:0000313|Proteomes:UP000094893}, and DXS-W
RC {ECO:0000313|EMBL:OCX69111.1, ECO:0000313|Proteomes:UP000095008};
RA Zhang X., Feng X., Tao J., Ma L., Xiao Y., Liang Y., Liu X., Yin H.;
RT "Comparative genomics of the extreme acidophile Acidithiobacillus
RT thiooxidans reveals intraspecific divergence and niche adaptation.";
RL Int. J. Mol. Sci. 0:0-0(2016).
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:OCX69111.1}.
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DR EMBL; LWRY01000233; OCX69111.1; -; Genomic_DNA.
DR EMBL; LWSA01000200; OCX70362.1; -; Genomic_DNA.
DR RefSeq; WP_024894634.1; NZ_LZYI01000149.1.
DR AlphaFoldDB; A0A1C2J765; -.
DR STRING; 930.GCA_002079865_02642; -.
DR GeneID; 60694564; -.
DR eggNOG; COG1894; Bacteria.
DR OrthoDB; 9805533at2; -.
DR Proteomes; UP000094893; Unassembled WGS sequence.
DR Proteomes; UP000095008; 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 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; 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; 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 321..366
FT /note="NADH-ubiquinone oxidoreductase 51kDa subunit iron-
FT sulphur binding"
FT /evidence="ECO:0000259|SMART:SM00928"
SQ SEQUENCE 419 AA; 45173 MW; A94BB5465BD816C7 CRC64;
MEAILSRHFA DPDPADLRAY RDAGGYVGLA RAVQMDPADI IAELEKSGLR GCGGAGFPTG
LKWRLRGVDA PEPRYLVCNL DETEPGSIKD RALLFGAPHH ILEGMFIAAH ALGVRYAVIF
VRGEYAAGAR VLEKALHQAR EAGLMRLPDG DLRLDIHVSL GRYICGEDSA ILNAIEGKRA
NPRKKPPHIS QQGLWQQPTT VNNAETIAHL PGIFAHGADW FRSLGVNGGV GSKLYSVCGP
AKRLGVFELP MGTTAQEILF EHAGGLQPGR TLRAVLPGGS STPFLMPEHF DTPMHFDAVA
KVGSRLGTGG FILMDDRQCP VDFLVATTRF FARESCGFCT PCREGLPYVR WLLERIEAGE
GSAEDIATLH QLGGQIAPNS FCALAPGALM PVLSGLHAFA DDFEAHVRLG HCPYRGPQS
//
