ID I0A2R6_FERFK Unreviewed; 179 AA.
AC I0A2R6;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2012, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE SubName: Full=Component HyfH of membrane-bound [Ni,Fe]-hydrogenase {ECO:0000313|EMBL:AFH43273.1};
GN OrderedLocusNames=FFONT_1285 {ECO:0000313|EMBL:AFH43273.1};
OS Fervidicoccus fontis (strain DSM 19380 / JCM 18336 / VKM B-2539 / Kam940).
OC Archaea; Thermoproteota; Thermoprotei; Fervidicoccales; Fervidicoccaceae;
OC Fervidicoccus.
OX NCBI_TaxID=1163730 {ECO:0000313|EMBL:AFH43273.1, ECO:0000313|Proteomes:UP000007391};
RN [1] {ECO:0000313|Proteomes:UP000007391}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 19380 / VKM B-2539 / Kam940
RC {ECO:0000313|Proteomes:UP000007391};
RA Lebedinsky A.V., Mardanov A.V., Gumerov V.M., Beletsky A.V., Kublanov I.V.,
RA Perevalova A.A., Bonch-Osmolovskaya E.A., Ravin N.V., Skryabin K.G.;
RT "Fervidicoccus fontis complete genome analysis confirms its distinct
RT phylogenetic position and predicts its environmental function.";
RL Submitted (MAR-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AFH43273.1, ECO:0000313|Proteomes:UP000007391}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 19380 / VKM B-2539 / Kam940
RC {ECO:0000313|Proteomes:UP000007391};
RX PubMed=24366681; DOI=10.1007/s00792-013-0616-7;
RA Lebedinsky A.V., Mardanov A.V., Kublanov I.V., Gumerov V.M., Beletsky A.V.,
RA Perevalova A.A., Bidzhieva S.Kh., Bonch-Osmolovskaya E.A., Skryabin K.G.,
RA Ravin N.V.;
RT "Analysis of the complete genome of Fervidococcus fontis confirms the
RT distinct phylogenetic position of the order Fervidicoccales and suggests
RT its environmental function.";
RL Extremophiles 18:295-309(2014).
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DR EMBL; CP003423; AFH43273.1; -; Genomic_DNA.
DR AlphaFoldDB; I0A2R6; -.
DR STRING; 1163730.FFONT_1285; -.
DR KEGG; ffo:FFONT_1285; -.
DR eggNOG; arCOG01543; Archaea.
DR HOGENOM; CLU_067218_3_1_2; -.
DR InParanoid; I0A2R6; -.
DR OrthoDB; 23833at2157; -.
DR Proteomes; UP000007391; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:InterPro.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0016651; F:oxidoreductase activity, acting on NAD(P)H; IEA:InterPro.
DR Gene3D; 3.30.70.3270; -; 1.
DR InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR InterPro; IPR017900; 4Fe4S_Fe_S_CS.
DR InterPro; IPR010226; NADH_quinone_OxRdtase_chainI.
DR PANTHER; PTHR10849:SF36; FORMATE HYDROGENLYASE SUBUNIT 6-RELATED; 1.
DR PANTHER; PTHR10849; NADH DEHYDROGENASE UBIQUINONE IRON-SULFUR PROTEIN 8, MITOCHONDRIAL; 1.
DR Pfam; PF12838; Fer4_7; 1.
DR SUPFAM; SSF54862; 4Fe-4S ferredoxins; 1.
DR PROSITE; PS00198; 4FE4S_FER_1; 2.
DR PROSITE; PS51379; 4FE4S_FER_2; 2.
PE 4: Predicted;
KW 4Fe-4S {ECO:0000256|ARBA:ARBA00022485};
KW Iron {ECO:0000256|ARBA:ARBA00022485};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00022485};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022485};
KW Reference proteome {ECO:0000313|Proteomes:UP000007391}.
FT DOMAIN 33..62
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 66..95
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
SQ SEQUENCE 179 AA; 19947 MW; F47D349E76492BA3 CRC64;
MSNLKTITKG IKYGIATVKY PFVPEKVEED YRGKPVLNFD LCIGCGSCSL ACPPDAITFT
RKENHAEWKI FYGRCIFCGR CEEVCPVGAI IQNEEFELAS KKKDDLEVVA NLKVAKCASC
GKSMNVTERE VKYVIDVLRS SLPQSKAEVI SELASLCSEC KRKRFIEKII KTYGKGGGR
//
