ANSME_BACTN
ID ANSME_BACTN Reviewed; 414 AA.
AC Q02550;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 11-APR-2003, sequence version 2.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Serine-type anaerobic sulfatase-maturating enzyme {ECO:0000305};
DE Short=Ser-type anaerobic sulfatase-maturating enzyme {ECO:0000305};
DE EC=1.1.98.7 {ECO:0000269|PubMed:18408004};
DE AltName: Full=Anaerobic sulfatase-maturating enzyme {ECO:0000303|PubMed:18408004};
DE Short=AnSME {ECO:0000303|PubMed:18408004};
DE AltName: Full=Chondroitin sulfate/heparin utilization regulation protein;
GN Name=chuR; OrderedLocusNames=BT_0238;
OS Bacteroides thetaiotaomicron (strain ATCC 29148 / DSM 2079 / JCM 5827 /
OS CCUG 10774 / NCTC 10582 / VPI-5482 / E50).
OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC Bacteroides.
OX NCBI_TaxID=226186;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION IN CHONDROITIN SULFATE
RP UTILIZATION.
RC STRAIN=46-1, and CS3;
RX PubMed=1429442; DOI=10.1128/jb.174.22.7185-7193.1992;
RA Cheng Q., Hwa V., Salyers A.A.;
RT "A locus that contributes to colonization of the intestinal tract by
RT Bacteroides thetaiotaomicron contains a single regulatory gene (chuR) that
RT links two polysaccharide utilization pathways.";
RL J. Bacteriol. 174:7185-7193(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29148 / DSM 2079 / JCM 5827 / CCUG 10774 / NCTC 10582 /
RC VPI-5482 / E50;
RX PubMed=12663928; DOI=10.1126/science.1080029;
RA Xu J., Bjursell M.K., Himrod J., Deng S., Carmichael L.K., Chiang H.C.,
RA Hooper L.V., Gordon J.I.;
RT "A genomic view of the human-Bacteroides thetaiotaomicron symbiosis.";
RL Science 299:2074-2076(2003).
RN [3]
RP FUNCTION AS A SULFATASE-MATURATING ENZYME, CATALYTIC ACTIVITY, SUBSTRATE
RP SPECIFICITY, COFACTOR, AND REACTION MECHANISM.
RC STRAIN=ATCC 29148 / DSM 2079 / JCM 5827 / CCUG 10774 / NCTC 10582 /
RC VPI-5482 / E50;
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 [4]
RP COFACTOR, AND MUTAGENESIS OF CYS-24; CYS-28; CYS-31; CYS-276; CYS-282;
RP CYS-339; CYS-342 AND CYS-348.
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).
CC -!- FUNCTION: Involved in 'Ser-type' sulfatase maturation under anaerobic
CC conditions. Links the heparin and the chondroitin sulfate utilization
CC pathways which contribute to the colonization of the intestinal tract.
CC May catalyze the activation of chondro-6-sulfatase, i.e. the post-
CC translational modification of a specific serine residue into 3-
CC oxoalanine (also known as C(alpha)-formylglycine (FGly)), by a free
CC radical chemical mechanism initiated via the reductive cleavage of S-
CC adenosyl-L-methionine (SAM). Is also able to oxidize a cysteine residue
CC in a synthetic substrate to FGly in vitro, but not in a recombinant
CC Cys-type sulfatase in vivo. But since B.thetaiotaomicron possesses only
CC Ser-type sulfatases, the oxidation of serine residues to FGly is the
CC sole physiological activity. {ECO:0000269|PubMed:1429442,
CC ECO:0000269|PubMed:18408004}.
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:0000269|PubMed:18408004};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU01266,
CC ECO:0000269|PubMed:20218986, ECO:0000305|PubMed:18408004};
CC Note=Binds 3 [4Fe-4S] clusters (PubMed:20218986). 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:0000269|PubMed:20218986};
CC -!- PATHWAY: Protein modification; sulfatase oxidation.
CC -!- SIMILARITY: Belongs to the radical SAM superfamily. Anaerobic
CC sulfatase-maturating enzyme family. {ECO:0000305}.
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DR EMBL; L00678; AAA22908.1; -; Genomic_DNA.
DR EMBL; AE015928; AAO75345.1; -; Genomic_DNA.
DR PIR; A47014; A47014.
DR RefSeq; NP_809151.1; NC_004663.1.
DR RefSeq; WP_008766211.1; NC_004663.1.
DR AlphaFoldDB; Q02550; -.
DR SMR; Q02550; -.
DR STRING; 226186.BT_0238; -.
DR PaxDb; Q02550; -.
DR PRIDE; Q02550; -.
DR EnsemblBacteria; AAO75345; AAO75345; BT_0238.
DR GeneID; 60926202; -.
DR KEGG; bth:BT_0238; -.
DR PATRIC; fig|226186.12.peg.239; -.
DR eggNOG; COG0641; Bacteria.
DR HOGENOM; CLU_009273_10_0_10; -.
DR InParanoid; Q02550; -.
DR OMA; YPCYRFV; -.
DR BRENDA; 1.1.98.7; 709.
DR UniPathway; UPA00910; -.
DR Proteomes; UP000001414; 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; 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 Pfam; PF13186; SPASM; 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 1: Evidence at protein level;
KW 4Fe-4S; Iron; Iron-sulfur; Metal-binding; Oxidoreductase;
KW Reference proteome; S-adenosyl-L-methionine.
FT CHAIN 1..414
FT /note="Serine-type anaerobic sulfatase-maturating enzyme"
FT /id="PRO_0000134462"
FT DOMAIN 5..250
FT /note="Radical SAM core"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01266"
FT ACT_SITE 298
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q0TTH1"
FT BINDING 24
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 ECO:0000305|PubMed:20218986"
FT BINDING 28
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 ECO:0000305|PubMed:20218986"
FT BINDING 30
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q0TTH1"
FT BINDING 31
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 ECO:0000305|PubMed:20218986"
FT BINDING 76
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q0TTH1"
FT BINDING 131
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q0TTH1"
FT BINDING 143
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
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:0000305|PubMed:20218986"
FT BINDING 282
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000305|PubMed:20218986"
FT BINDING 297
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q0TTH1"
FT BINDING 339
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000305|PubMed:20218986"
FT BINDING 342
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000305|PubMed:20218986"
FT BINDING 348
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000305|PubMed:20218986"
FT BINDING 352
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q0TTH1"
FT BINDING 371
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q0TTH1"
FT MUTAGEN 24
FT /note="C->A: Still contains 4Fe-4S but lacks activity; when
FT associated with A-28 and A-31."
FT /evidence="ECO:0000269|PubMed:20218986"
FT MUTAGEN 28
FT /note="C->A: Still contains 4Fe-4S but lacks activity; when
FT associated with A-24 and A-31."
FT /evidence="ECO:0000269|PubMed:20218986"
FT MUTAGEN 31
FT /note="C->A: Still contains 4Fe-4S but lacks activity; when
FT associated with A-24 and A-28."
FT /evidence="ECO:0000269|PubMed:20218986"
FT MUTAGEN 276
FT /note="C->A: Still contains 4Fe-4S but lacks activity; when
FT associated with A-282."
FT /evidence="ECO:0000269|PubMed:20218986"
FT MUTAGEN 282
FT /note="C->A: Still contains 4Fe-4S but lacks activity; when
FT associated with A-276."
FT /evidence="ECO:0000269|PubMed:20218986"
FT MUTAGEN 339
FT /note="C->A: Still contains 4Fe-4S but lacks activity; when
FT associated with A-342 and A-348."
FT /evidence="ECO:0000269|PubMed:20218986"
FT MUTAGEN 342
FT /note="C->A: Still contains 4Fe-4S but lacks activity; when
FT associated with A-339 and A-348."
FT /evidence="ECO:0000269|PubMed:20218986"
FT MUTAGEN 348
FT /note="C->A: Still contains 4Fe-4S but lacks activity; when
FT associated with A-339 and A-342."
FT /evidence="ECO:0000269|PubMed:20218986"
FT CONFLICT 400..414
FT /note="NIMKALKDGSLKIEY -> TS (in Ref. 1; AAA22908)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 414 AA; 47949 MW; F0FCC6B6DCDF34B5 CRC64;
MKATTYAPFA KPLYVMVKPV GAVCNLACEY CYYLEKANLY KENPKHVMSD ELLEKFIDEY
INSQTMPQVL FTWHGGETLM RPLSFYKKAM ELQKKYARGR TIDNCIQTNG TLLTDEWCEF
FRENNWLVGV SIDGPQEFHD EYRKNKMGKP SFVKVMQGIN LLKKHGVEWN AMAVVNDFNA
EYPLDFYNFF KEIDCHYIQF APIVERIVSH QDGRHLASLA EGKEGALADF SVSPEQWGNF
LCTIFDEWVK EDVGKFFIQI FDSTLANWMG EQPGVCTMAK HCGHAGVMEF NGDVYSCDHF
VFPEYKLGNI YSQTLVEMMH SERQHNFGTM KYQSLPTQCK ECDFLFACNG ECPKNRFSRT
ADGEPGLNYL CKGYYQYFQH VAPYMDFMKK ELMNQQAPAN IMKALKDGSL KIEY
