ANSME_CLONN
ID ANSME_CLONN Reviewed; 374 AA.
AC A0Q2E1;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2007, sequence version 1.
DT 03-AUG-2022, entry version 82.
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=NT01CX_0295;
OS Clostridium novyi (strain NT).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=386415;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NT;
RX PubMed=17115055; DOI=10.1038/nbt1256;
RA Bettegowda C., Huang X., Lin J., Cheong I., Kohli M., Szabo S.A., Zhang X.,
RA Diaz L.A. Jr., Velculescu V.E., Parmigiani G., Kinzler K.W., Vogelstein B.,
RA Zhou S.;
RT "The genome and transcriptomes of the anti-tumor agent Clostridium novyi-
RT NT.";
RL Nat. Biotechnol. 24:1573-1580(2006).
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; CP000382; ABK62380.1; -; Genomic_DNA.
DR RefSeq; WP_011722778.1; NC_008593.1.
DR AlphaFoldDB; A0Q2E1; -.
DR SMR; A0Q2E1; -.
DR STRING; 386415.NT01CX_0295; -.
DR EnsemblBacteria; ABK62380; ABK62380; NT01CX_0295.
DR KEGG; cno:NT01CX_0295; -.
DR eggNOG; COG0641; Bacteria.
DR HOGENOM; CLU_009273_10_0_9; -.
DR OMA; QRRFHVM; -.
DR OrthoDB; 1172757at2; -.
DR UniPathway; UPA00910; -.
DR Proteomes; UP000008220; 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..374
FT /note="Cysteine-type anaerobic sulfatase-maturating enzyme"
FT /id="PRO_0000333037"
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 374 AA; 44086 MW; 762E55064053C84B CRC64;
MKSLSMLIKP ASSNCNLRCT YCFYYDICNN REIKSFGMMK LNLLETIVKR AFNEAEQNCT
FAFQGGEPTL VGIDFYREFI NFVKKYNTRN INVFYSIQTN GTTINEDWAK FFKENNFLVG
ISLDGTKEIH DKYRLDANKK GSFNKIMTNI KILNRYKVEY NILTVVNKNT SRHIDKIYKF
FKKQDFRFLQ FIPCLDPIND PRESHPYSLN PKDYETFLNK LFDLWFKDFL DGRFVSIRYF
DDLLSILLGN NPKSCCMNGF CSCEFVIESD GSVYPCDFYV LDEYKIGYIE EKTFSELFNS
NVTKNFIDSS LNHDVKCKNC NWYPLCRSGC RRNKEPNFPN GTNDNIFCES FKSFFEKNIS
KLTYVAKTLA YRQH
