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Database: UniProt
Entry: A0A1F3MI01_9BACT
LinkDB: A0A1F3MI01_9BACT
Original site: A0A1F3MI01_9BACT 
ID   A0A1F3MI01_9BACT        Unreviewed;       398 AA.
AC   A0A1F3MI01;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   SubName: Full=Anaerobic sulfatase maturase {ECO:0000313|EMBL:OFY52357.1};
GN   ORFNames=A2X22_10175 {ECO:0000313|EMBL:OFY52357.1};
OS   Bacteroidetes bacterium GWF2_49_14.
OC   Bacteria; Bacteroidota.
OX   NCBI_TaxID=1797354 {ECO:0000313|EMBL:OFY52357.1, ECO:0000313|Proteomes:UP000177245};
RN   [1] {ECO:0000313|EMBL:OFY52357.1, ECO:0000313|Proteomes:UP000177245}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=27774985; DOI=10.1038/ncomms13219;
RA   Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA   Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA   Williams K.H., Hubbard S.S., Banfield J.F.;
RT   "Thousands of microbial genomes shed light on interconnected biogeochemical
RT   processes in an aquifer system.";
RL   Nat. Commun. 7:13219-13219(2016).
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:OFY52357.1}.
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DR   EMBL; MEOR01000073; OFY52357.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1F3MI01; -.
DR   STRING; 1797354.A2X22_10175; -.
DR   Proteomes; UP000177245; Unassembled WGS sequence.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR   CDD; cd01335; Radical_SAM; 1.
DR   CDD; cd21120; SPASM_anSME; 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; IPR034491; Anaerob_Ser_sulfatase-maturase.
DR   InterPro; IPR007197; rSAM.
DR   InterPro; IPR047207; SPASM_anSME.
DR   InterPro; IPR023867; Sulphatase_maturase_rSAM.
DR   NCBIfam; TIGR04085; rSAM_more_4Fe4S; 1.
DR   NCBIfam; TIGR03942; sulfatase_rSAM; 1.
DR   PANTHER; PTHR43273; ANAEROBIC SULFATASE-MATURATING ENZYME HOMOLOG ASLB-RELATED; 1.
DR   PANTHER; PTHR43273:SF3; ANAEROBIC SULFATASE-MATURATING ENZYME HOMOLOG ASLB-RELATED; 1.
DR   Pfam; PF04055; Radical_SAM; 1.
DR   Pfam; PF13186; SPASM; 1.
DR   SFLD; SFLDF00285; anaerobic_Ser-type_sulfatase-m; 1.
DR   SFLD; SFLDS00029; Radical_SAM; 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   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691}.
FT   DOMAIN          1..229
FT                   /note="Radical SAM core"
FT                   /evidence="ECO:0000259|PROSITE:PS51918"
SQ   SEQUENCE   398 AA;  45505 MW;  30E0060B21CA38D6 CRC64;
     MVMAKPIGPV CNLNCSYCYY LEKEHLYQET RNFKMSDEVL ESFIKQFIES QEVPLVTFTW
     QGGEPTLLGL EYFEKVVALQ QKYRGRKKID NAFQTNGTRL SEDWCRFFKK NNFLVGISVD
     GPAPIHDKYR KTKGGKPSFE EMMKGIRLLK RFRVEFNTLS VVNNANVNQP LEVYRFLKRA
     GSGFLQFIPI VERSAGMPTA EGLTLVPPIF GENAELTDWS VRARQYGKFM ISIFDEWVRN
     DVGKVFVQLF DVTLANWVGG SPGLCVFAET CGEAAVMEHN GDIYSCDHFV YPEYFLGNIL
     ETPLASLMGQ HRQIQFGKDK RDTLPRQCLL CDVRFACHGG CPKSRFATTA DGQPGLNWLC
     EGYKMFFEHV KPYMEFMANE LMHEHPPSNI MSSPLVKS
//
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