ANSME_CLOP1
ID ANSME_CLOP1 Reviewed; 370 AA.
AC Q0TTH1;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 19-SEP-2006, sequence version 1.
DT 03-AUG-2022, entry version 91.
DE RecName: Full=Cysteine-type anaerobic sulfatase-maturating enzyme {ECO:0000305};
DE Short=Cys-type anaerobic sulfatase-maturating enzyme;
DE EC=1.8.98.7 {ECO:0000269|PubMed:17335281, ECO:0000269|PubMed:18408004, ECO:0000269|PubMed:19489556, ECO:0000269|PubMed:20218986, ECO:0000269|PubMed:23477283};
DE AltName: Full=Anaerobic sulfatase-maturating enzyme {ECO:0000303|PubMed:16766528};
DE Short=AnSME {ECO:0000303|PubMed:16766528};
DE AltName: Full=anSMEcpe {ECO:0000303|PubMed:23477283};
GN OrderedLocusNames=CPF_0616;
OS Clostridium perfringens (strain ATCC 13124 / DSM 756 / JCM 1290 / NCIMB
OS 6125 / NCTC 8237 / Type A).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=195103;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 13124 / DSM 756 / JCM 1290 / NCIMB 6125 / NCTC 8237 / S 107 /
RC Type A;
RX PubMed=16825665; DOI=10.1101/gr.5238106;
RA Myers G.S.A., Rasko D.A., Cheung J.K., Ravel J., Seshadri R., DeBoy R.T.,
RA Ren Q., Varga J., Awad M.M., Brinkac L.M., Daugherty S.C., Haft D.H.,
RA Dodson R.J., Madupu R., Nelson W.C., Rosovitz M.J., Sullivan S.A.,
RA Khouri H., Dimitrov G.I., Watkins K.L., Mulligan S., Benton J., Radune D.,
RA Fisher D.J., Atkins H.S., Hiscox T., Jost B.H., Billington S.J.,
RA Songer J.G., McClane B.A., Titball R.W., Rood J.I., Melville S.B.,
RA Paulsen I.T.;
RT "Skewed genomic variability in strains of the toxigenic bacterial pathogen,
RT Clostridium perfringens.";
RL Genome Res. 16:1031-1040(2006).
RN [2]
RP FUNCTION IN SULFATASE MATURATION.
RX PubMed=16766528; DOI=10.1074/jbc.m602504200;
RA Berteau O., Guillot A., Benjdia A., Rabot S.;
RT "A new type of bacterial sulfatase reveals a novel maturation pathway in
RT prokaryotes.";
RL J. Biol. Chem. 281:22464-22470(2006).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, AND REACTION MECHANISM.
RX PubMed=17335281; DOI=10.1021/ja067175e;
RA Benjdia A., Leprince J., Guillot A., Vaudry H., Rabot S., Berteau O.;
RT "Anaerobic sulfatase-maturating enzymes: radical SAM enzymes able to
RT catalyze in vitro sulfatase post-translational modification.";
RL J. Am. Chem. Soc. 129:3462-3463(2007).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, COFACTOR,
RP SPECTROSCOPIC STUDIES, AND REACTION MECHANISM.
RX PubMed=18408004; DOI=10.1074/jbc.m710074200;
RA Benjdia A., Subramanian S., Leprince J., Vaudry H., Johnson M.K.,
RA Berteau O.;
RT "Anaerobic sulfatase-maturating enzymes - first dual substrate radical S-
RT adenosylmethionine enzymes.";
RL J. Biol. Chem. 283:17815-17826(2008).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, AND REACTION MECHANISM.
RX PubMed=19489556; DOI=10.1021/ja901571p;
RA Benjdia A., Leprince J., Sandstroem C., Vaudry H., Berteau O.;
RT "Mechanistic investigations of anaerobic sulfatase-maturating enzyme:
RT direct Cbeta H-atom abstraction catalyzed by a radical AdoMet enzyme.";
RL J. Am. Chem. Soc. 131:8348-8349(2009).
RN [6]
RP CATALYTIC ACTIVITY.
RX PubMed=20218986; DOI=10.1111/j.1742-4658.2010.07613.x;
RA Benjdia A., Subramanian S., Leprince J., Vaudry H., Johnson M.K.,
RA Berteau O.;
RT "Anaerobic sulfatase-maturating enzyme--a mechanistic link with glycyl
RT radical-activating enzymes?";
RL FEBS J. 277:1906-1920(2010).
RN [7]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, SUBUNIT, AND MUTAGENESIS OF CYS-15;
RP CYS-19; CYS-22 AND CYS-276.
RC STRAIN=ATCC 13124 / DSM 756 / JCM 1290 / NCIMB 6125 / NCTC 8237 / S 107 /
RC Type A;
RX PubMed=23477283; DOI=10.1021/bi400136u;
RA Grove T.L., Ahlum J.H., Qin R.M., Lanz N.D., Radle M.I., Krebs C.,
RA Booker S.J.;
RT "Further characterization of Cys-type and Ser-type anaerobic sulfatase
RT maturating enzymes suggests a commonality in the mechanism of catalysis.";
RL Biochemistry 52:2874-2887(2013).
RN [8] {ECO:0007744|PDB:4K36, ECO:0007744|PDB:4K37, ECO:0007744|PDB:4K38, ECO:0007744|PDB:4K39}
RP X-RAY CRYSTALLOGRAPHY (1.62 ANGSTROMS) IN COMPLEXES WITH IRON-SULFUR
RP (4FE-4S); S-ADENOSYL-L-METHIONINE AND PEPTIDYL-SUBSTRATES, COFACTOR,
RP REACTION MECHANISM, ACTIVE SITE, AND MUTAGENESIS OF TYR-24 AND ASP-277.
RX PubMed=23650368; DOI=10.1073/pnas.1302417110;
RA Goldman P.J., Grove T.L., Sites L.A., McLaughlin M.I., Booker S.J.,
RA Drennan C.L.;
RT "X-ray structure of an AdoMet radical activase reveals an anaerobic
RT solution for formylglycine posttranslational modification.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:8519-8524(2013).
CC -!- FUNCTION: Involved in 'Cys-type' sulfatase maturation under anaerobic
CC conditions. Catalyzes the post-translational modification of cysteine
CC ('Cys-51' in the arylsulfatase CPF_0221) into 3-oxoalanine (also known
CC as C(alpha)-formylglycine (FGly)), by a free radical chemical mechanism
CC initiated via the reductive cleavage of S-adenosyl-L-methionine (SAM)
CC (PubMed:18408004, PubMed:16766528, PubMed:17335281, PubMed:19489556,
CC PubMed:23477283). Is also able to oxidize a serine residue in a
CC synthetic substrate to FGly in vitro, and in a serine variant of a Cys-
CC type sulfatase in vivo, but this activity is not physiological
CC (PubMed:18408004, PubMed:23477283). Converts threonyl peptides to the
CC corresponding ketone product, and also allo-threonyl peptides, but with
CC a significantly reduced efficiency (PubMed:23477283).
CC {ECO:0000269|PubMed:16766528, ECO:0000269|PubMed:17335281,
CC ECO:0000269|PubMed:18408004, ECO:0000269|PubMed:19489556,
CC ECO:0000269|PubMed:23477283}.
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:0000269|PubMed:17335281, ECO:0000269|PubMed:18408004,
CC ECO:0000269|PubMed:19489556, ECO:0000269|PubMed:20218986,
CC ECO:0000269|PubMed:23477283};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000269|PubMed:17335281, ECO:0000269|PubMed:18408004,
CC ECO:0000269|PubMed:23477283, ECO:0000269|PubMed:23650368};
CC Note=Binds 3 [4Fe-4S] clusters (PubMed:23477283, PubMed:23650368). The
CC first cluster is coordinated with 3 cysteines and an exchangeable S-
CC adenosyl-L-methionine (PubMed:23650368). The two auxiliary clusters may
CC create a conduit for electrons to travel from the buried substrate to
CC the protein surface (PubMed:23650368). {ECO:0000269|PubMed:23477283,
CC ECO:0000269|PubMed:23650368};
CC -!- PATHWAY: Protein modification; sulfatase oxidation. {ECO:0000305}.
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:23477283}.
CC -!- MISCELLANEOUS: Recognizes the CXAXR sulfatase signature, in contrast to
CC the oxygen-dependent formylglycine-generating enzyme system (FGE) that
CC recognizes the CXPXR motif.
CC -!- SIMILARITY: Belongs to the radical SAM superfamily. Anaerobic
CC sulfatase-maturating enzyme family. {ECO:0000305}.
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DR EMBL; CP000246; ABG83662.1; -; Genomic_DNA.
DR RefSeq; WP_011590280.1; NC_008261.1.
DR PDB; 4K36; X-ray; 1.62 A; A/B=1-370.
DR PDB; 4K37; X-ray; 1.62 A; A/B=1-370.
DR PDB; 4K38; X-ray; 1.83 A; A/B=1-370.
DR PDB; 4K39; X-ray; 1.78 A; A/B=1-370.
DR PDBsum; 4K36; -.
DR PDBsum; 4K37; -.
DR PDBsum; 4K38; -.
DR PDBsum; 4K39; -.
DR AlphaFoldDB; Q0TTH1; -.
DR SMR; Q0TTH1; -.
DR STRING; 195103.CPF_0616; -.
DR EnsemblBacteria; ABG83662; ABG83662; CPF_0616.
DR GeneID; 29572256; -.
DR KEGG; cpf:CPF_0616; -.
DR eggNOG; COG0641; Bacteria.
DR HOGENOM; CLU_009273_10_0_9; -.
DR OMA; QRRFHVM; -.
DR OrthoDB; 1172757at2; -.
DR BRENDA; 1.8.98.7; 1503.
DR UniPathway; UPA00910; -.
DR Proteomes; UP000001823; 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; SFLDS00029; Radical_SAM; 1.
DR SFLD; SFLDG01384; thioether_bond_formation_requi; 1.
DR TIGRFAMs; TIGR04085; rSAM_more_4Fe4S; 1.
DR PROSITE; PS51918; RADICAL_SAM; 1.
PE 1: Evidence at protein level;
KW 3D-structure; 4Fe-4S; Iron; Iron-sulfur; Metal-binding; Oxidoreductase;
KW S-adenosyl-L-methionine.
FT CHAIN 1..370
FT /note="Cysteine-type anaerobic sulfatase-maturating enzyme"
FT /id="PRO_0000333035"
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:0000305|PubMed:23650368"
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:0000269|PubMed:23650368,
FT ECO:0007744|PDB:4K36, ECO:0007744|PDB:4K37,
FT ECO:0007744|PDB:4K38, ECO:0007744|PDB:4K39"
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:0000269|PubMed:23650368,
FT ECO:0007744|PDB:4K36, ECO:0007744|PDB:4K37,
FT ECO:0007744|PDB:4K38, ECO:0007744|PDB:4K39"
FT BINDING 21
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000269|PubMed:23650368,
FT ECO:0007744|PDB:4K36, ECO:0007744|PDB:4K37,
FT ECO:0007744|PDB:4K38, ECO:0007744|PDB:4K39"
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:0000269|PubMed:23650368,
FT ECO:0007744|PDB:4K36, ECO:0007744|PDB:4K37,
FT ECO:0007744|PDB:4K38, ECO:0007744|PDB:4K39"
FT BINDING 66
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000269|PubMed:23650368,
FT ECO:0007744|PDB:4K36, ECO:0007744|PDB:4K37,
FT ECO:0007744|PDB:4K38, ECO:0007744|PDB:4K39"
FT BINDING 122
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000269|PubMed:23650368,
FT ECO:0007744|PDB:4K36, ECO:0007744|PDB:4K37,
FT ECO:0007744|PDB:4K38, ECO:0007744|PDB:4K39"
FT BINDING 134
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000269|PubMed:23650368,
FT ECO:0007744|PDB:4K36, ECO:0007744|PDB:4K37,
FT ECO:0007744|PDB:4K38, ECO:0007744|PDB:4K39"
FT BINDING 195
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000269|PubMed:23650368,
FT ECO:0007744|PDB:4K36, ECO:0007744|PDB:4K37,
FT ECO:0007744|PDB:4K38, ECO:0007744|PDB:4K39"
FT BINDING 255
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:23650368,
FT ECO:0007744|PDB:4K36, ECO:0007744|PDB:4K37,
FT ECO:0007744|PDB:4K38, ECO:0007744|PDB:4K39"
FT BINDING 261
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:23650368,
FT ECO:0007744|PDB:4K36, ECO:0007744|PDB:4K37,
FT ECO:0007744|PDB:4K38, ECO:0007744|PDB:4K39"
FT BINDING 276
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:23650368,
FT ECO:0007744|PDB:4K36, ECO:0007744|PDB:4K37,
FT ECO:0007744|PDB:4K38, ECO:0007744|PDB:4K39"
FT BINDING 317
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000269|PubMed:23650368,
FT ECO:0007744|PDB:4K36, ECO:0007744|PDB:4K37,
FT ECO:0007744|PDB:4K38, ECO:0007744|PDB:4K39"
FT BINDING 320
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000269|PubMed:23650368,
FT ECO:0007744|PDB:4K36, ECO:0007744|PDB:4K37,
FT ECO:0007744|PDB:4K38, ECO:0007744|PDB:4K39"
FT BINDING 326
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000269|PubMed:23650368,
FT ECO:0007744|PDB:4K36, ECO:0007744|PDB:4K37,
FT ECO:0007744|PDB:4K38, ECO:0007744|PDB:4K39"
FT BINDING 330
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:23650368,
FT ECO:0007744|PDB:4K36, ECO:0007744|PDB:4K37,
FT ECO:0007744|PDB:4K38, ECO:0007744|PDB:4K39"
FT BINDING 348
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000269|PubMed:23650368,
FT ECO:0007744|PDB:4K36, ECO:0007744|PDB:4K37,
FT ECO:0007744|PDB:4K38, ECO:0007744|PDB:4K39"
FT MUTAGEN 15
FT /note="C->A: Decrease in 4Fe-4S content; when associated
FT with A-19 and A-22."
FT /evidence="ECO:0000269|PubMed:23477283"
FT MUTAGEN 19
FT /note="C->A: Decrease in 4Fe-4S content; when associated
FT with A-15 and A-22."
FT /evidence="ECO:0000269|PubMed:23477283"
FT MUTAGEN 22
FT /note="C->A: Decrease in 4Fe-4S content; when associated
FT with A-15 and A-19."
FT /evidence="ECO:0000269|PubMed:23477283"
FT MUTAGEN 24
FT /note="Y->F: Retains 11.7% of FGly production activity."
FT /evidence="ECO:0000269|PubMed:23650368"
FT MUTAGEN 276
FT /note="C->A: Exhibits reduced solubility and drastically
FT reduced activity."
FT /evidence="ECO:0000269|PubMed:23477283"
FT MUTAGEN 277
FT /note="D->N: Retains 0.8% of FGly production activity."
FT /evidence="ECO:0000269|PubMed:23650368"
FT STRAND 4..8
FT /evidence="ECO:0007829|PDB:4K36"
FT TURN 10..13
FT /evidence="ECO:0007829|PDB:4K36"
FT STRAND 23..26
FT /evidence="ECO:0007829|PDB:4K37"
FT HELIX 41..54
FT /evidence="ECO:0007829|PDB:4K36"
FT STRAND 57..63
FT /evidence="ECO:0007829|PDB:4K36"
FT HELIX 68..71
FT /evidence="ECO:0007829|PDB:4K36"
FT HELIX 73..86
FT /evidence="ECO:0007829|PDB:4K36"
FT STRAND 92..99
FT /evidence="ECO:0007829|PDB:4K36"
FT HELIX 106..114
FT /evidence="ECO:0007829|PDB:4K36"
FT STRAND 118..122
FT /evidence="ECO:0007829|PDB:4K36"
FT HELIX 127..133
FT /evidence="ECO:0007829|PDB:4K36"
FT HELIX 143..156
FT /evidence="ECO:0007829|PDB:4K36"
FT STRAND 159..166
FT /evidence="ECO:0007829|PDB:4K36"
FT HELIX 168..172
FT /evidence="ECO:0007829|PDB:4K36"
FT HELIX 174..183
FT /evidence="ECO:0007829|PDB:4K36"
FT STRAND 188..193
FT /evidence="ECO:0007829|PDB:4K36"
FT HELIX 211..230
FT /evidence="ECO:0007829|PDB:4K36"
FT HELIX 238..249
FT /evidence="ECO:0007829|PDB:4K36"
FT STRAND 257..260
FT /evidence="ECO:0007829|PDB:4K36"
FT STRAND 271..275
FT /evidence="ECO:0007829|PDB:4K36"
FT HELIX 277..279
FT /evidence="ECO:0007829|PDB:4K36"
FT HELIX 282..284
FT /evidence="ECO:0007829|PDB:4K36"
FT TURN 289..291
FT /evidence="ECO:0007829|PDB:4K36"
FT HELIX 294..298
FT /evidence="ECO:0007829|PDB:4K36"
FT HELIX 301..309
FT /evidence="ECO:0007829|PDB:4K36"
FT HELIX 315..319
FT /evidence="ECO:0007829|PDB:4K36"
FT HELIX 323..326
FT /evidence="ECO:0007829|PDB:4K36"
FT HELIX 331..333
FT /evidence="ECO:0007829|PDB:4K36"
FT HELIX 348..368
FT /evidence="ECO:0007829|PDB:4K36"
SQ SEQUENCE 370 AA; 43332 MW; F5A9A7F046B4CC22 CRC64;
MPPLSLLIKP ASSGCNLKCT YCFYHSLSDN RNVKSYGIMR DEVLESMVKR VLNEANGHCS
FAFQGGEPTL AGLEFFEKLM ELQRKHNYKN LKIYNSLQTN GTLIDESWAK FLSENKFLVG
LSMDGPKEIH NLNRKDCCGL DTFSKVERAA ELFKKYKVEF NILCVVTSNT ARHVNKVYKY
FKEKDFKFLQ FINCLDPLYE EKGKYNYSLK PKDYTKFLKN LFDFWYEDFL NGNRVSIRYF
DGLLETILLG KSSSCGMNGT CTCQFVVESD GSVYPCDFYV LDKWRLGNIQ DMTMKELFET
NKNHEFIKLS FKVHEECKKC KWFRLCKGGC RRCRDSKEDS ALELNYYCQS YKEFFEYAFP
RLINVANNIK
