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Information on EC 1.8.98.7 - cysteine-type anaerobic sulfatase-maturating enzyme
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1.8.98.7 cysteine-type anaerobic sulfatase-maturating enzymeIUBMB Comments
A radical S-adenosylmethionine (AdoMet) enzyme that contains three [4Fe-4S] clusters. The enzyme, found in some bacteria, activates a type I sulfatase enzyme (EC 3.1.6.1) by converting a conserved L-cysteine residue in the active site to a unique 3-oxo-L-alanine residue that is essential for the sulfatase activity. Some enzymes can also act on L-serine, see EC 1.1.98.7, serine-type anaerobic sulfatase-maturating enzyme and EC 1.8.3.7, formylglycine-generating enzyme.
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Word Map
- 1.8.98.7
-
sulfatases
- adomet
-
auxiliary
- arylsulfatases
- s-adenosylmethionine
- molybdenum
-
spasm
-
vertical
- perfringens
-
formylglycine
- butirosin
-
saccharolytic
-
cysteinyl
-
seryl
-
facial
-
5\'-deoxyadenosyl
-
oxygen-dependent
- calpha-formylglycine
-
mandibular
-
ser-type
-
palatal
The enzyme appears in viruses and cellular organisms
Reaction Schemes
+
+
=
+
+
+
+
a [sulfatase]-L-cysteine
+
=
a [sulfatase]-3-oxo-L-alanine
+
+
+
Synonyms
ansme, ansmecpe, anaerobic sulfatase-maturating enzyme, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
anaerobic sulfatase-maturating enzyme
AtsB
Cys-type anaerobic sulfatase-maturating enzyme
-
-
-
-
nSMEcpe
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
S-adenosyl-L-methionine + a [sulfatase]-L-cysteine + H2O = a [sulfatase]-3-oxo-L-alanine + 5'-deoxyadenosine + L-methionine + hydrogen sulfide
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-
-
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SYSTEMATIC NAME
IUBMB Comments
[sulfatase]-L-cysteine:S-adenosyl-L-methionine oxidoreductase (3-oxo-L-alanine-forming)
A radical S-adenosylmethionine (AdoMet) enzyme that contains three [4Fe-4S] clusters. The enzyme, found in some bacteria, activates a type I sulfatase enzyme (EC 3.1.6.1) by converting a conserved L-cysteine residue in the active site to a unique 3-oxo-L-alanine residue that is essential for the sulfatase activity. Some enzymes can also act on L-serine, see EC 1.1.98.7, serine-type anaerobic sulfatase-maturating enzyme and EC 1.8.3.7, formylglycine-generating enzyme.
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
Ac-AVPSCIPSRASILTGM-NH2 + S-adenosyl-L-methionine + dithionite
Ac-AVPS-3-oxo-L-Ala-IPSRASILTGM-NH2 + L-methionine + 5'-deoxyadenosine + sulfur dioxide + hydrogen sulfide
Ac-FENAYTAVPSCIASRASILTGMS-NH2 + S-adenosyl-L-methionine + reduced acceptor
Ac-FENAYTAVPS-3-oxo-L-Ala-IASRASILTGMS-NH2 + L-methionine + 5'-deoxyadenosine + acceptor + hydrogen sulfide
-
-
-
?
Ac-FENAYTAVPSCIASRASILTMSQ-NH2 + S-adenosyl-L-methionine + dithionite
Ac-FENAYTAVPS-3-oxo-L-Ala-IASRASILTMSQ-NH2 + L-methionine + 5'-deoxyadenosine + sulfur dioxide + hydrogen sulfide
-
-
-
?
Ac-YTAVPSCIPSRASILTGM + S-adenosyl-L-methionine + dithionite
Ac-YTAVPS-3-oxo-L-Ala-IPSRASILTGM + L-methionine + 5'-deoxyadenosine + sulfur dioxide + hydrogen sulfide
Ac-YYTSPMCAPARSMLLTGN + S-adenosyl-L-methionine
Ac-YYTSPM-3-oxo-L-Ala-APARSMLLTGN + L-methionine + 5'-deoxyadenosine + sulfur dioxide + hydrogen sulfide
Ac-YYTSPMSAPARSMLLTGN + S-adenosyl-L-methionine
Ac-YYTSPM3-oxo-L-Ala-APARSMLLTGN + L-methionine + 5'-deoxyadenosine
Ac-YYTSPMSeCAPARSMLLTGN + S-adenosyl-L-methionine
Ac-YYTSPM-3-oxo-L-Ala-APARSMLLTGN + L-methionine + 5'-deoxyadenosine + sulfur dioxide + hydrogen selenide
Ac-YYTSPMTAPARSMLLTGN + S-adenosyl-L-methionine
Ac-YYTSPM-(2S)-2-amino-3-oxobutanoyl-APARSMLLTGN + L-methionine + 5'-deoxyadenosine + sulfur dioxide + H2O
a flavodoxin/flavodoxin reductase/NADPH system may substitute for dithionite
-
-
?
Tyr-Tyr-Thr-Ser-Pro-Met-Cys-Ala-Pro-Ala-Arg-Ser-Met-Leu-Leu-Thr-Gly-Asn + S-adenosyl-L-methionine
Tyr-Tyr-Thr-Ser-Pro-Met-3-oxo-L-Ala-Ala-Pro-Ala-Arg-Ser-Met-Leu-Leu-Thr-Gly-Asn + L-methionine + 5'-deoxyadenosine + sulfur dioxide + hydrogen sulfide
Ac-AVPSCIPSRASILTGM-NH2 + S-adenosyl-L-methionine + dithionite
Ac-AVPS-3-oxo-L-Ala-IPSRASILTGM-NH2 + L-methionine + 5'-deoxyadenosine + sulfur dioxide + hydrogen sulfide
a flavodoxin/flavodoxin reductase/NADPH system may substitute for dithionite
-
-
?
Ac-AVPSCIPSRASILTGM-NH2 + S-adenosyl-L-methionine + dithionite
Ac-AVPS-3-oxo-L-Ala-IPSRASILTGM-NH2 + L-methionine + 5'-deoxyadenosine + sulfur dioxide + hydrogen sulfide
a flavodoxin/flavodoxin reductase/NADPH system may substitute for dithionite
-
-
?
Ac-YTAVPSCIPSRASILTGM + S-adenosyl-L-methionine + dithionite
Ac-YTAVPS-3-oxo-L-Ala-IPSRASILTGM + L-methionine + 5'-deoxyadenosine + sulfur dioxide + hydrogen sulfide
a flavodoxin/flavodoxin reductase/NADPH system may substitute for dithionite
-
-
?
Ac-YTAVPSCIPSRASILTGM + S-adenosyl-L-methionine + dithionite
Ac-YTAVPS-3-oxo-L-Ala-IPSRASILTGM + L-methionine + 5'-deoxyadenosine + sulfur dioxide + hydrogen sulfide
a flavodoxin/flavodoxin reductase/NADPH system may substitute for dithionite
-
-
?
Ac-YYTSPMCAPARSMLLTGN + S-adenosyl-L-methionine
Ac-YYTSPM-3-oxo-L-Ala-APARSMLLTGN + L-methionine + 5'-deoxyadenosine + sulfur dioxide + hydrogen sulfide
a flavodoxin/flavodoxin reductase/NADPH system may substitute for dithionite
-
-
?
Ac-YYTSPMCAPARSMLLTGN + S-adenosyl-L-methionine
Ac-YYTSPM-3-oxo-L-Ala-APARSMLLTGN + L-methionine + 5'-deoxyadenosine + sulfur dioxide + hydrogen sulfide
a flavodoxin/flavodoxin reductase/NADPH system may substitute for dithionite
-
-
?
Ac-YYTSPMSAPARSMLLTGN + S-adenosyl-L-methionine
Ac-YYTSPM3-oxo-L-Ala-APARSMLLTGN + L-methionine + 5'-deoxyadenosine
a flavodoxin/flavodoxin reductase/NADPH system may substitute for dithionite
-
-
?
Ac-YYTSPMSAPARSMLLTGN + S-adenosyl-L-methionine
Ac-YYTSPM3-oxo-L-Ala-APARSMLLTGN + L-methionine + 5'-deoxyadenosine
a flavodoxin/flavodoxin reductase/NADPH system may substitute for dithionite
-
-
?
Ac-YYTSPMSeCAPARSMLLTGN + S-adenosyl-L-methionine
Ac-YYTSPM-3-oxo-L-Ala-APARSMLLTGN + L-methionine + 5'-deoxyadenosine + sulfur dioxide + hydrogen selenide
a flavodoxin/flavodoxin reductase/NADPH system may substitute for dithionite
-
-
?
Ac-YYTSPMSeCAPARSMLLTGN + S-adenosyl-L-methionine
Ac-YYTSPM-3-oxo-L-Ala-APARSMLLTGN + L-methionine + 5'-deoxyadenosine + sulfur dioxide + hydrogen selenide
a flavodoxin/flavodoxin reductase/NADPH system may substitute for dithionite
-
-
?
Tyr-Tyr-Thr-Ser-Pro-Met-Cys-Ala-Pro-Ala-Arg-Ser-Met-Leu-Leu-Thr-Gly-Asn + S-adenosyl-L-methionine
Tyr-Tyr-Thr-Ser-Pro-Met-3-oxo-L-Ala-Ala-Pro-Ala-Arg-Ser-Met-Leu-Leu-Thr-Gly-Asn + L-methionine + 5'-deoxyadenosine + sulfur dioxide + hydrogen sulfide
a flavodoxin/flavodoxin reductase/NADPH system may substitute for dithionite with higly reduced activity
-
-
?
Tyr-Tyr-Thr-Ser-Pro-Met-Cys-Ala-Pro-Ala-Arg-Ser-Met-Leu-Leu-Thr-Gly-Asn + S-adenosyl-L-methionine
Tyr-Tyr-Thr-Ser-Pro-Met-3-oxo-L-Ala-Ala-Pro-Ala-Arg-Ser-Met-Leu-Leu-Thr-Gly-Asn + L-methionine + 5'-deoxyadenosine + sulfur dioxide + hydrogen sulfide
a flavodoxin/flavodoxin reductase/NADPH system may substitute for dithionite with higly reduced activity
-
-
?
additional information
?
-
the enzme also perfoms the reaction of the Ser-type anaerobic sulfatase-maturating enzyme, converting a serine residue of sulfatase into a 3-oxo-L-alanine residue. The post-translational modification of sulfatases, i.e. the creation of a 3-oxo-L-alanine (i.e. Calpha-formylglycine) residue from a cysteine or serine is vital for the proper function of sulfatases
-
-
?
additional information
?
-
the enzme also perfoms the reaction of the Ser-type anaerobic sulfatase-maturating enzyme, converting a serine residue of sulfatase into a 3-oxo-L-alanine residue. The post-translational modification of sulfatases, i.e. the creation of a 3-oxo-L-alanine (i.e. Calpha-formylglycine) residue from a cysteine or serine is vital for the proper function of sulfatases. No reaction with Ac-YYTSPM(allo)TAPARSMLLTGN
-
-
?
additional information
?
-
-
the enzme also perfoms the reaction of the Ser-type anaerobic sulfatase-maturating enzyme, converting a serine residue of sulfatase into a 3-oxo-L-alanine residue. The post-translational modification of sulfatases, i.e. the creation of a 3-oxo-L-alanine (i.e. Calpha-formylglycine) residue from a cysteine or serine is vital for the proper function of sulfatases. No reaction with Ac-YYTSPM(allo)TAPARSMLLTGN
-
-
?
additional information
?
-
the enzyme converts a cysteine residue of arylsulfatase into a 3-oxo-L-alanine residue. The post-translational modification of sulfatases, i.e. the creation of a 3-oxo-L-alanine (i.e. Calpha-formylglycine) residue from a cysteine or serine is vital for the proper function of sulfatases
-
-
?
additional information
?
-
the enzyme converts a cysteine residue of arylsulfatase into a 3-oxo-L-alanine residue. The post-translational modification of sulfatases, i.e. the creation of a 3-oxo-L-alanine (i.e. Calpha-formylglycine) residue from a cysteine or serine is vital for the proper function of sulfatases
-
-
?
additional information
?
-
the enzme also perfoms the reaction of the Ser-type anaerobic sulfatase-maturating enzyme, converting a serine residue of sulfatase into a 3-oxo-L-alanine residue. The post-translational modification of sulfatases, i.e. the creation of a 3-oxo-L-alanine (i.e. Calpha-formylglycine) residue from a cysteine or serine is vital for the proper function of sulfatases. No reaction with Ac-YYTSPM(allo)TAPARSMLLTGN
-
-
?
additional information
?
-
the enzme also perfoms the reaction of the Ser-type anaerobic sulfatase-maturating enzyme, converting a serine residue of sulfatase into a 3-oxo-L-alanine residue. The post-translational modification of sulfatases, i.e. the creation of a 3-oxo-L-alanine (i.e. Calpha-formylglycine) residue from a cysteine or serine is vital for the proper function of sulfatases
-
-
?
additional information
?
-
the enzme also perfoms the reaction of the Ser-type anaerobic sulfatase-maturating enzyme, converting a serine residue of sulfatase into a 3-oxo-L-alanine residue. The post-translational modification of sulfatases, i.e. the creation of a 3-oxo-L-alanine (i.e. Calpha-formylglycine) residue from a cysteine or serine is vital for the proper function of sulfatases. No reaction with Tyr-Tyr-Thr-Ser-Pro-Met-Ala-Ala-Pro-Ala-Arg-Ser-Met-Leu-Leu-Thr-Gly-Asn-COOH. No reaction with Tyr-Tyr-Thr-Ser-Pro-Met-Ala-Ala-Pro-Ala-Arg-Ser-Met-Leu-Leu-Thr-Gly-Asn-COOH
-
-
?
additional information
?
-
the enzme also perfoms the reaction of the Ser-type anaerobic sulfatase-maturating enzyme, converting a serine residue of sulfatase into a 3-oxo-L-alanine residue. The post-translational modification of sulfatases, i.e. the creation of a 3-oxo-L-alanine (i.e. Calpha-formylglycine) residue from a cysteine or serine is vital for the proper function of sulfatases. No reaction with Tyr-Tyr-Thr-Ser-Pro-Met-Ala-Ala-Pro-Ala-Arg-Ser-Met-Leu-Leu-Thr-Gly-Asn-COOH. No reaction with Tyr-Tyr-Thr-Ser-Pro-Met-Ala-Ala-Pro-Ala-Arg-Ser-Met-Leu-Leu-Thr-Gly-Asn-COOH
-
-
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
[4Fe-4S]2+ cluster
[4Fe-4S]2+ cluster
three [4Fe-4S]2+ clusters per enzyme molecule
[4Fe-4S]2+ cluster
three [4Fe-4S]2+ clusters per enzyme moelcule
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
metabolism
metabolism
involved in the maturation of sulfatases
metabolism
involved in the pathway of sulfatase oxidation
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). ANSME_CLOP1
Clostridium perfringens (strain ATCC 13124 / DSM 756 / JCM 1290 / NCIMB 6125 / NCTC 8237 / Type A)
370
0
43332
Swiss-Prot
-
ANSME_CLOPE
Clostridium perfringens (strain 13 / Type A)
370
0
43371
Swiss-Prot
-
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
monomer
monomer
1* 45740, deduced form the molecular weight of the enzyme/substrate complex
monomer
-
1* 45740, deduced form the molecular weight of the enzyme/substrate complex
-
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
C15A/C19A/C22A
C15A/C19A/C22A
less stable than wild-type enzyme, loss of one of the three [4Fe-4S]2+ clusters
C15A/C19A/C22A
-
less stable than wild-type enzyme, loss of one of the three [4Fe-4S]2+ clusters
-
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-80°C, 0.1 M Tris-HCl buffer, pH 7, 150 mM KCl and 5 mM DTT, anaerobic conditions
-80C, 50 mM potassium HEPES, pH 7.5, 500 mM KCl, 10 mM DTT, and 30% glycerol
-80C, 50 mM potassium HEPES, pH 7.5, 500 mM KCl, 10 mM DTT, and 30% glycerol
-80C, 50 mM potassium HEPES, pH 7.5, 500 mM KCl, 10 mM DTT, and 30% glycerol
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
immobilized metal affinity chromatography under an atmosphere of nitrogen
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21(DE3)
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Grove, T.L.; Lee, K.H.; St Clair, J.; Krebs, C.; Booker, S.J.
In vitro characterization of AtsB, a radical SAM formylglycine-generating enzyme that contains three [4Fe-4S] clusters
Biochemistry
47
7523-7538
2008
Klebsiella pneumoniae (Q9X758), Klebsiella pneumoniae ATCC 700721D (Q9X758)
brenda
Grove, T.L.; Ahlum, J.H.;Quin, R.M.; Lanz, N.D.; Radle, M.I.; Krebs, C.; Booker, S.J.
Further Characterization of Cys-Type and Ser-Type Anaerobic Sulfatase Maturating Enzymes Suggests a Commonality in Mechanism of Catalysis
Biochemistry
52
2874-2887
2013
Clostridium perfringens (Q8XMQ3), Clostridium perfringens, Clostridium perfringens type A (Q8XMQ3)
brenda
Benjdia, A.; Subramanian, S-; Leprince, J.; Vaudry, H.; Johnson, M.K.; Berteau, O.
Anaerobic sulfatase-maturating enzyme--a mechanistic link with glycyl radical-activating enzymes
FEBS J.
277
1906-1920
2010
Clostridium perfringens (Q8XMQ3), Clostridium perfringens type A (Q8XMQ3)
brenda
Benjdia, A.; Leprince, J.; Guillot, A.; Vaudry, H.; Rabot, S.; Berteau, O.
Anaerobic sulfatase-maturating enzymes: radical SAM enzymes able to catalyze in vitro sulfatase post-translational modification
J. Am. Chem. Soc.
129
3462-3463
2007
Clostridium perfringens (Q0TTH1)
brenda
Benjdia, A.; Subramanian, S.; Leprince, J.; Vaudry, H.; Johnson, M.K.; Berteau, O.
Anaerobic sulfatase-maturating enzymes, first dual substrate radical S-adenosylmethionine enzymes
J. Biol. Chem.
283
17815-26
2008
Clostridium perfringens (Q0TTH1)
brenda
Goldman, P.J.; Grove, T.L.; Sites, L.A.; McLaughlin, M.I.; Booker, S.J.; Drennan, C.L.
X-ray structure of an AdoMet radical activase reveals an anaerobic solution for formylglycine posttranslational modification
Proc. Natl. Acad. Sci. USA
110
8519-8524
2013
Clostridium perfringens (Q0TTH1)
brenda
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Release 2023.1 (January 2023)
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