ID A0A1B6BK34_9FIRM Unreviewed; 429 AA.
AC A0A1B6BK34;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=Arylarge subunitlfatase regulator {ECO:0000313|EMBL:GAU80078.1};
GN ORFNames=F3D3_4744 {ECO:0000313|EMBL:GAU80078.1};
OS Fusibacter sp. 3D3.
OC Bacteria; Bacillota; Clostridia; Eubacteriales;
OC Eubacteriales Family XII. Incertae Sedis; Fusibacter.
OX NCBI_TaxID=1048380 {ECO:0000313|EMBL:GAU80078.1, ECO:0000313|Proteomes:UP000095197};
RN [1] {ECO:0000313|EMBL:GAU80078.1, ECO:0000313|Proteomes:UP000095197}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=3D3 {ECO:0000313|EMBL:GAU80078.1,
RC ECO:0000313|Proteomes:UP000095197};
RA Serrano A.E., Escudero L.V., Encalada O., Tebes C.J., Fernandez S.,
RA Demergasso C.S.;
RT "Draft genome sequence of Fusibacter ascotence 3D3 isolated from the high
RT arsenic level Ascotan salt flat in northern Chile.";
RL Submitted (SEP-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000256|ARBA:ARBA00001966};
CC -!- SIMILARITY: Belongs to the radical SAM superfamily. Anaerobic
CC sulfatase-maturating enzyme family. {ECO:0000256|ARBA:ARBA00023601}.
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:GAU80078.1}.
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; BDHH01000043; GAU80078.1; -; Genomic_DNA.
DR RefSeq; WP_069876842.1; NZ_BDHH01000043.1.
DR AlphaFoldDB; A0A1B6BK34; -.
DR STRING; 1048380.F3D3_4744; -.
DR OrthoDB; 9808591at2; -.
DR UniPathway; UPA00782; -.
DR Proteomes; UP000095197; Unassembled WGS sequence.
DR GO; GO:0051536; F:iron-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:InterPro.
DR GO; GO:0009399; P:nitrogen fixation; IEA:UniProtKB-KW.
DR CDD; cd01335; Radical_SAM; 1.
DR Gene3D; 3.20.20.70; Aldolase class I; 1.
DR InterPro; IPR023885; 4Fe4S-binding_SPASM_dom.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR007197; rSAM.
DR InterPro; IPR023867; Sulphatase_maturase_rSAM.
DR NCBIfam; TIGR04085; rSAM_more_4Fe4S; 1.
DR PANTHER; PTHR43787:SF3; FEMO COFACTOR BIOSYNTHESIS PROTEIN NIFB; 1.
DR PANTHER; PTHR43787; FEMO COFACTOR BIOSYNTHESIS PROTEIN NIFB-RELATED; 1.
DR Pfam; PF13353; Fer4_12; 1.
DR Pfam; PF04055; Radical_SAM; 1.
DR SFLD; SFLDG01383; cyclic_pyranopterin_phosphate; 1.
DR SFLD; SFLDG01384; thioether_bond_formation_requi; 1.
DR SUPFAM; SSF102114; Radical SAM enzymes; 1.
DR PROSITE; PS51918; RADICAL_SAM; 1.
PE 3: Inferred from homology;
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000095197};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691}.
FT DOMAIN 90..324
FT /note="Radical SAM core"
FT /evidence="ECO:0000259|PROSITE:PS51918"
SQ SEQUENCE 429 AA; 49855 MW; BF5CE5235CD058D2 CRC64;
MKESNSIKYV KSNFTILLEN SEEIYYLFNT RTSAICKLDK AAFEFYENYP NNHIDDNFEN
LHSILISEGF LIESNQKEID YIKHNLYKSR YDEKTLSLTI APTMNCNFSC SYCFETNKEF
GKMDSTVITQ LKEFVSKKLH HQTKLEITWF GGEPLLALDT ITELTESFIS ICKEKKCTYN
SNLITNGYLV SQDILPILKN NLIRTIQITL DGSEEYHNQK RFLSDGSGTY KTLIHNIKLL
KDNEFAVTVR LNQEKSNINS ISEVLKDFES YEIDNVPVSF GRIEAYGNSE YHDKCLDVPE
FAEIELNYHQ TRLKQNKTKK VKLPTRLRNY CLADQVYAYV FDSKGFIYKC WNDIGNIDHS
IGNLNTNLIN NQDLFLSYMK FDPTIDKECK NCNVMPLCMG GCPHNRIYTN RTCSNLRYNI
SELVKLVVV
//
