ANSME_KLEAE
ID ANSME_KLEAE Reviewed; 405 AA.
AC P20714;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1991, sequence version 1.
DT 03-AUG-2022, entry version 85.
DE RecName: Full=Serine-type anaerobic sulfatase-maturating enzyme {ECO:0000250|UniProtKB:Q9X758};
DE Short=Ser-type anaerobic sulfatase-maturating enzyme {ECO:0000250|UniProtKB:Q9X758};
DE EC=1.1.98.7 {ECO:0000250|UniProtKB:Q9X758};
DE AltName: Full=Anaerobic sulfatase-maturating enzyme {ECO:0000250|UniProtKB:Q9X758};
DE Short=AnSME {ECO:0000250|UniProtKB:Q9X758};
DE AltName: Full=Arylsulfatase-activating protein {ECO:0000250|UniProtKB:Q9X758};
DE AltName: Full=Formylglycine-generating enzyme {ECO:0000250|UniProtKB:Q9X758};
GN Name=atsB {ECO:0000303|PubMed:2180918};
OS Klebsiella aerogenes (Enterobacter aerogenes).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella.
OX NCBI_TaxID=548;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2180918; DOI=10.1128/jb.172.4.2131-2140.1990;
RA Murooka Y., Ishibashi K., Yasumoto M., Sasaki M., Sugino H., Azakami H.,
RA Yamashita M.;
RT "A sulfur- and tyramine-regulated Klebsiella aerogenes operon containing
RT the arylsulfatase (atsA) gene and the atsB gene.";
RL J. Bacteriol. 172:2131-2140(1990).
CC -!- FUNCTION: Involved in 'Ser-type' sulfatase maturation under anaerobic
CC conditions. Catalyzes the post-translational modification of serine
CC ('Ser-72' in the arylsulfatase AtsA) into 3-oxoalanine (also known as
CC C(alpha)-formylglycine (FGly)), by a free radical chemical mechanism
CC initiated via the reductive cleavage of S-adenosyl-L-methionine (SAM).
CC {ECO:0000250|UniProtKB:Q9X758}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-seryl-[sulfatase] + S-adenosyl-L-methionine = 3-oxo-L-
CC alanyl-[sulfatase] + 5'-deoxyadenosine + H(+) + L-methionine;
CC Xref=Rhea:RHEA:17609, Rhea:RHEA-COMP:12901, Rhea:RHEA-COMP:15882,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17319, ChEBI:CHEBI:29999,
CC ChEBI:CHEBI:57844, ChEBI:CHEBI:59789, ChEBI:CHEBI:85621; EC=1.1.98.7;
CC Evidence={ECO:0000250|UniProtKB:Q9X758};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000250|UniProtKB:Q9X758,
CC ECO:0000255|PROSITE-ProRule:PRU01266};
CC Note=Binds 3 [4Fe-4S] clusters (By similarity). The first cluster is
CC coordinated with 3 cysteines and an exchangeable S-adenosyl-L-
CC methionine (By similarity). {ECO:0000250|UniProtKB:Q0TTH1,
CC ECO:0000250|UniProtKB:Q9X758};
CC -!- PATHWAY: Protein modification; sulfatase oxidation.
CC {ECO:0000250|UniProtKB:Q9X758}.
CC -!- SUBUNIT: Monomer (By similarity). Interacts with AtsA prior to its
CC export to the periplasm (By similarity).
CC {ECO:0000250|UniProtKB:Q9X758}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9X758}.
CC -!- SIMILARITY: Belongs to the radical SAM superfamily. Anaerobic
CC sulfatase-maturating enzyme family. {ECO:0000305}.
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DR EMBL; M31938; AAA25050.1; -; Genomic_DNA.
DR AlphaFoldDB; P20714; -.
DR SMR; P20714; -.
DR STRING; 548.EAG7_02823; -.
DR UniPathway; UPA00910; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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:UniProtKB-KW.
DR Gene3D; 3.20.20.70; -; 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; IPR023867; Sulphatase_maturase_rSAM.
DR PANTHER; PTHR43273; PTHR43273; 1.
DR Pfam; PF04055; Radical_SAM; 1.
DR SFLD; SFLDF00285; anaerobic_Ser-type_sulfatase-m; 1.
DR SFLD; SFLDG01384; thioether_bond_formation_requi; 1.
DR TIGRFAMs; TIGR04085; rSAM_more_4Fe4S; 1.
DR PROSITE; PS51918; RADICAL_SAM; 1.
PE 3: Inferred from homology;
KW 4Fe-4S; Cytoplasm; Iron; Iron-sulfur; Metal-binding; Oxidoreductase;
KW S-adenosyl-L-methionine.
FT CHAIN 1..405
FT /note="Serine-type anaerobic sulfatase-maturating enzyme"
FT /id="PRO_0000134460"
FT DOMAIN 18..249
FT /note="Radical SAM core"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01266"
FT ACT_SITE 292
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q0TTH1"
FT BINDING 35
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /ligand_note="4Fe-4S-S-AdoMet"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01266"
FT BINDING 39
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /ligand_note="4Fe-4S-S-AdoMet"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01266"
FT BINDING 41
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q0TTH1"
FT BINDING 42
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /ligand_note="4Fe-4S-S-AdoMet"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01266"
FT BINDING 84
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q0TTH1"
FT BINDING 140
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q0TTH1"
FT BINDING 152
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q0TTH1"
FT BINDING 270
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q0TTH1"
FT BINDING 276
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q0TTH1"
FT BINDING 291
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q0TTH1"
FT BINDING 331
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q0TTH1"
FT BINDING 334
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q0TTH1"
FT BINDING 340
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q0TTH1"
FT BINDING 344
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q0TTH1"
FT BINDING 357
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q0TTH1"
SQ SEQUENCE 405 AA; 45372 MW; 1A7DBABD298AB2AB CRC64;
MLNIAALRQQ QIPLAAEPRS PVPFHILMKP IGPACNLACR YCYYPQDETP VNKMDDARLE
QFIRRYIAAQ PAGAREINFV WQGGEPLLAG LSFYKKALAL QARYAPDGVT ISNSLQTNGT
LINDAWCRLF REHGFIIGLS LEGNEALQDY HRPDKRGRST WSAALRGIDL LHQHQVDFNL
LVVVHNEMAA HAAAIYDRLV SLGARYLQFQ PLMSEGAALR EGYQLSADNW GRFMVGIWRQ
WRKRCDRGRV FVINIEQAWA QYFTHTSGSC VHSARCGSNL VMEPDGQLYA CDHLINAEHR
LGRLDEQTLA AAVDASVQLP FGQQKSLRRE CQTCSVKMVC QGGCPAHLNA AGNNRLCGGY
YRFFSDILAP LRPFSRDLNG LKAWRAAFVG TAAYCVAPYP DDIPL
