ID G0HIW5_THES4 Unreviewed; 600 AA.
AC G0HIW5;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 66.
DE SubName: Full=NADH:ubiquinone oxidoreductase, NADH-binding subunit F {ECO:0000313|EMBL:AEK72894.1};
GN OrderedLocusNames=GQS_04965 {ECO:0000313|EMBL:AEK72894.1};
OS Thermococcus sp. (strain CGMCC 1.5172 / 4557).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Thermococcus.
OX NCBI_TaxID=1042877 {ECO:0000313|EMBL:AEK72894.1, ECO:0000313|Proteomes:UP000000874};
RN [1] {ECO:0000313|EMBL:AEK72894.1, ECO:0000313|Proteomes:UP000000874}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.5172 / 4557 {ECO:0000313|Proteomes:UP000000874};
RX PubMed=21914870; DOI=10.1128/JB.05851-11;
RA Wang X., Gao Z., Xu X., Ruan L.;
RT "Complete genome sequence of Thermococcus sp. strain 4557, a
RT hyperthermophilic archaeon isolated from a deep-sea hydrothermal vent
RT area.";
RL J. Bacteriol. 193:5544-5545(2011).
CC -!- SIMILARITY: Belongs to the complex I 51 kDa subunit family.
CC {ECO:0000256|ARBA:ARBA00007523}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP002920; AEK72894.1; -; Genomic_DNA.
DR RefSeq; WP_014012577.1; NC_015865.1.
DR AlphaFoldDB; G0HIW5; -.
DR STRING; 1042877.GQS_04965; -.
DR GeneID; 11015663; -.
DR KEGG; the:GQS_04965; -.
DR PATRIC; fig|1042877.9.peg.973; -.
DR eggNOG; arCOG01609; Archaea.
DR eggNOG; arCOG04537; Archaea.
DR HOGENOM; CLU_014881_3_2_2; -.
DR OrthoDB; 297477at2157; -.
DR Proteomes; UP000000874; Chromosome.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProt.
DR CDD; cd02980; TRX_Fd_family; 1.
DR Gene3D; 3.10.20.600; -; 1.
DR Gene3D; 3.30.70.20; -; 1.
DR Gene3D; 6.10.250.1450; -; 1.
DR Gene3D; 3.40.30.10; Glutaredoxin; 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; IPR017896; 4Fe4S_Fe-S-bd.
DR InterPro; IPR017900; 4Fe4S_Fe_S_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 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; PF01512; Complex1_51K; 1.
DR Pfam; PF00037; Fer4; 2.
DR Pfam; PF10589; NADH_4Fe-4S; 1.
DR Pfam; PF10531; SLBB; 1.
DR SMART; SM00928; NADH_4Fe-4S; 1.
DR SUPFAM; SSF54862; 4Fe-4S ferredoxins; 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; PS00198; 4FE4S_FER_1; 1.
DR PROSITE; PS51379; 4FE4S_FER_2; 2.
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};
KW Ubiquinone {ECO:0000313|EMBL:AEK72894.1}.
FT DOMAIN 538..567
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 568..597
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
SQ SEQUENCE 600 AA; 65821 MW; 0E74AF6AE928C8F8 CRC64;
MSEIKAIAVG MNSCGIAAGA RETYEAIKAE LEKRNLDVEL KIVGCVGMCY REPLVDIITD
DEIITYGHVD PKKVPRIIEE HVVNGKPIEE WVVKRDWWEN GERKTWDVDG YFSKQRKIVL
ENSGYIDPEN IEEYIAAGGY EALKKALKMK PEEIIDVITK SGLRGRGGAG FPTGLKWKFA
REAKGDVKYI VCNADEGDPG AFMDRNVLEG DPHRVIEGMI IGAYAIGATK GFIYVRAEYP
LAIRRLKIAL KQARERGFLG ENILGSGFSF DIAIKEGAGA FVCGEETALI ASIEGKRGMP
RPRPPYPAQK GLWGKPTNIN NVETWANVPW IIKHGPEAYA SIGTEKSKGT KVFALSGKIK
HGGNVEVPMG MTLREILYEI GGGTKTGKKI KAVQLGGPSG GCIPEYLFDT PVDYESVNAT
GAIMGSGGMV VMDEDTCMVD VAKFFLDFTV KESCGKCTFC RLGTKRMWEI LDKFTRGEAT
EEDLEKLERL AYQVKAGSLC GLGQTAPNPV LTTIRYFRDE YLAHIQGKCP AKVCKPLIKY
VIIADRCTGC TACAIFCPVK AIEGEKLKPH VIDQSACIKC GTCYEVCRFN AIEIVDAGGE
//
