ID A5ULB0_METS3 Unreviewed; 335 AA.
AC A5ULB0;
DT 10-JUL-2007, integrated into UniProtKB/TrEMBL.
DT 10-JUL-2007, sequence version 1.
DT 27-MAR-2024, entry version 85.
DE SubName: Full=Tungsten formylmethanofuran dehydrogenase, subunit F, FwdF {ECO:0000313|EMBL:ABQ86988.1};
DE EC=1.6.5.3 {ECO:0000313|EMBL:ABQ86988.1};
DE EC=1.6.99.3 {ECO:0000313|EMBL:ABQ86988.1};
GN OrderedLocusNames=Msm_0783 {ECO:0000313|EMBL:ABQ86988.1};
OS Methanobrevibacter smithii (strain ATCC 35061 / DSM 861 / OCM 144 / PS).
OC Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC Methanobacteriales; Methanobacteriaceae; Methanobrevibacter.
OX NCBI_TaxID=420247 {ECO:0000313|EMBL:ABQ86988.1, ECO:0000313|Proteomes:UP000001992};
RN [1] {ECO:0000313|EMBL:ABQ86988.1, ECO:0000313|Proteomes:UP000001992}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35061 / DSM 861 / OCM 144 / PS
RC {ECO:0000313|Proteomes:UP000001992};
RX PubMed=17563350; DOI=10.1073/pnas.0704189104;
RA Samuel B.S., Hansen E.E., Manchester J.K., Coutinho P.M., Henrissat B.,
RA Fulton R., Latreille P., Kim K., Wilson R.K., Gordon J.I.;
RT "Genomic and metabolic adaptations of Methanobrevibacter smithii to the
RT human gut.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:10643-10648(2007).
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; CP000678; ABQ86988.1; -; Genomic_DNA.
DR RefSeq; WP_011954090.1; NZ_CP117965.1.
DR AlphaFoldDB; A5ULB0; -.
DR STRING; 420247.Msm_0783; -.
DR EnsemblBacteria; ABQ86988; ABQ86988; Msm_0783.
DR GeneID; 78817412; -.
DR KEGG; msi:Msm_0783; -.
DR PATRIC; fig|420247.28.peg.780; -.
DR eggNOG; arCOG02180; Archaea.
DR HOGENOM; CLU_050974_0_0_2; -.
DR BioCyc; MSMI420247:GHWZ-797-MONOMER; -.
DR Proteomes; UP000001992; Chromosome.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR CDD; cd10549; MtMvhB_like; 2.
DR Gene3D; 3.30.70.20; -; 6.
DR InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR InterPro; IPR017900; 4Fe4S_Fe_S_CS.
DR InterPro; IPR043256; MvhB-like.
DR PANTHER; PTHR43687:SF5; 4FE-4S FERREDOXIN-TYPE DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR43687; ADENYLYLSULFATE REDUCTASE, BETA SUBUNIT; 1.
DR Pfam; PF00037; Fer4; 2.
DR Pfam; PF12838; Fer4_7; 2.
DR PIRSF; PIRSF005658; FwdF; 1.
DR SUPFAM; SSF54862; 4Fe-4S ferredoxins; 1.
DR PROSITE; PS00198; 4FE4S_FER_1; 4.
DR PROSITE; PS51379; 4FE4S_FER_2; 8.
PE 4: Predicted;
KW Oxidoreductase {ECO:0000313|EMBL:ABQ86988.1}.
FT DOMAIN 12..41
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 52..81
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 96..125
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 135..164
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 174..203
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 218..247
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 253..283
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 284..313
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
SQ SEQUENCE 335 AA; 36527 MW; 90BBAC928263A093 CRC64;
MFNVERSGEE TRKLSHNNDR CVGCGICTDV CPTSSLRLGP IVPIARGLIE MDLVSVTSNT
CVLCGLCSVA CPFDALSLTI NGNDIKETGN YPVWEVESEI NDDDCIYCGR CYSVCPRDTI
LFKRELPSRE DLVIGEISVD EDKCVYCSIC SEMCPAGAIS LTNNPEFSND NLNNTIEVDT
SKCIYCGVCK RACPQDAIKA VCSTCMLQDQ IKAPEINGTA SILKDGCVNC SWCKEVCPVD
TINVTKPFEG TLKLVETDES TCKGDACHAC QDVCPCDAVE IIDNKATINL DYCNLCGACV
NACPQNIREV TRTSMKLNNI NSESWRDILT SNLLS
//
