ANSME_CLOPE
ID ANSME_CLOPE Reviewed; 370 AA.
AC Q8XMQ3;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Cysteine-type anaerobic sulfatase-maturating enzyme {ECO:0000250|UniProtKB:Q0TTH1};
DE Short=Cys-type anaerobic sulfatase-maturating enzyme {ECO:0000250|UniProtKB:Q0TTH1};
DE EC=1.8.98.7 {ECO:0000250|UniProtKB:Q0TTH1};
DE AltName: Full=Anaerobic sulfatase-maturating enzyme {ECO:0000250|UniProtKB:Q0TTH1};
DE Short=AnSME {ECO:0000250|UniProtKB:Q0TTH1};
GN OrderedLocusNames=CPE0635;
OS Clostridium perfringens (strain 13 / Type A).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=195102;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=13 / Type A;
RX PubMed=11792842; DOI=10.1073/pnas.022493799;
RA Shimizu T., Ohtani K., Hirakawa H., Ohshima K., Yamashita A., Shiba T.,
RA Ogasawara N., Hattori M., Kuhara S., Hayashi H.;
RT "Complete genome sequence of Clostridium perfringens, an anaerobic flesh-
RT eater.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:996-1001(2002).
CC -!- FUNCTION: Involved in 'Cys-type' sulfatase maturation under anaerobic
CC conditions. Catalyzes the post-translational modification of cysteine
CC into 3-oxoalanine (also known as C(alpha)-formylglycine (FGly)), by a
CC free radical chemical mechanism initiated via the reductive cleavage of
CC S-adenosyl-L-methionine (SAM). {ECO:0000250|UniProtKB:Q0TTH1}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + L-cysteinyl-[sulfatase] + S-adenosyl-L-methionine = 3-
CC oxo-L-alanyl-[sulfatase] + 5'-deoxyadenosine + 2 H(+) + hydrogen
CC sulfide + L-methionine; Xref=Rhea:RHEA:61592, Rhea:RHEA-COMP:12900,
CC Rhea:RHEA-COMP:12901, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17319, ChEBI:CHEBI:29919, ChEBI:CHEBI:29950,
CC ChEBI:CHEBI:57844, ChEBI:CHEBI:59789, ChEBI:CHEBI:85621; EC=1.8.98.7;
CC Evidence={ECO:0000250|UniProtKB:Q0TTH1};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000250|UniProtKB:Q0TTH1};
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 -!- PATHWAY: Protein modification; sulfatase oxidation.
CC {ECO:0000250|UniProtKB:Q0TTH1}.
CC -!- SIMILARITY: Belongs to the radical SAM superfamily. Anaerobic
CC sulfatase-maturating enzyme family. {ECO:0000305}.
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DR EMBL; BA000016; BAB80341.1; -; Genomic_DNA.
DR RefSeq; WP_003476924.1; NC_003366.1.
DR AlphaFoldDB; Q8XMQ3; -.
DR SMR; Q8XMQ3; -.
DR STRING; 195102.gene:10489896; -.
DR EnsemblBacteria; BAB80341; BAB80341; BAB80341.
DR KEGG; cpe:CPE0635; -.
DR HOGENOM; CLU_009273_10_0_9; -.
DR OMA; QRRFHVM; -.
DR BRENDA; 1.1.98.7; 1503.
DR BRENDA; 1.8.98.7; 1503.
DR UniPathway; UPA00910; -.
DR Proteomes; UP000000818; Chromosome.
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; IPR034485; Anaerobic_Cys-type_sulfatase-m.
DR InterPro; IPR007197; rSAM.
DR InterPro; IPR023867; Sulphatase_maturase_rSAM.
DR PANTHER; PTHR43273; PTHR43273; 1.
DR Pfam; PF04055; Radical_SAM; 1.
DR Pfam; PF13186; SPASM; 1.
DR SFLD; SFLDF00289; anaerobic_Cys-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; Iron; Iron-sulfur; Metal-binding; Oxidoreductase;
KW Reference proteome; S-adenosyl-L-methionine.
FT CHAIN 1..370
FT /note="Cysteine-type anaerobic sulfatase-maturating enzyme"
FT /id="PRO_0000333036"
FT DOMAIN 1..227
FT /note="Radical SAM core"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01266"
FT ACT_SITE 277
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q0TTH1"
FT BINDING 15
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:0000250|UniProtKB:Q0TTH1"
FT BINDING 19
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:0000250|UniProtKB:Q0TTH1"
FT BINDING 21
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q0TTH1"
FT BINDING 22
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:0000250|UniProtKB:Q0TTH1"
FT BINDING 66
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q0TTH1"
FT BINDING 122
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q0TTH1"
FT BINDING 134
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q0TTH1"
FT BINDING 195
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q0TTH1"
FT BINDING 255
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q0TTH1"
FT BINDING 261
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 317
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q0TTH1"
FT BINDING 320
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q0TTH1"
FT BINDING 326
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q0TTH1"
FT BINDING 330
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q0TTH1"
FT BINDING 348
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q0TTH1"
SQ SEQUENCE 370 AA; 43371 MW; 9BD3B56E97136E7E CRC64;
MPPLSLLIKP ASSGCNLKCT YCFYHSLSDN RNVKSYGIMR DEVLESMVKR VLNEADGHCS
FAFQGGEPIL AGLEFFERLM ELQRKHNYKN LKIYNSLQTN GTLIDESWAK FLSENKFLVG
LSMDGPKEIH NLNRKDCCGL DTFSKVERAA ELFKKYKVEF NILCVVTSNT ARHVNKIYRY
FKEKDFKFLQ FINCLDPLYE EKGKYNYSLK PQDYTKFLKN LFDLWYEDFL NGNRVSIRYF
DGLLETILLG KSSSCGMNGT CTCQFVVESD GSVYPCDFYV LDKWRLGNIQ DMTMKELFET
NKNHEFIKSS FKVHEECKKC KWFKLCKGGC RRCRDSKEDS DLELNYYCQS YKEFFEYAFP
RLINVANNIK
