EC 1.1.98.7: serine-type anaerobic sulfatase-maturating enzyme
This is an abbreviated version!
For detailed information about serine-type anaerobic sulfatase-maturating enzyme, go to the full flat file.
Reaction
Synonyms
anaerobic sulfatase-maturating enzyme, anSME, AtsB, cpe0635, nSMEcpe, Ser-type anaerobic sulfatase-maturating enzyme
ECTree
1.1.98.7 serine-type anaerobic sulfatase-maturating enzymeAdvanced search results
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Substrates Products on EC 1.1.98.7 - serine-type anaerobic sulfatase-maturating enzyme
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SUBSTRATE 
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY 
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
Ac-AVPSSIPSRASILTGM-NH2 + S-adenosyl-L-methionine + dithionite
Ac-AVPS-3-oxo-L-Ala-IPSRASILTGM-NH2 + L-methionine + 5'-deoxyadenosine + sulfur dioxide + H2O
Ac-FENAYTAVPSSIASRASILTGMS-NH2 + S-adenosyl-L-methionine
Ac-FENAYTAVPS-3-oxo-L-Ala-IASRASILTGMS-NH2 + L-methionine + 5'-deoxyadenosine
Ac-YYTSPMSAPARSMLLTGN + S-adenosyl-L-methionine
Ac-YYTSPM-3-oxo-L-Ala-APARSMLLTGN + L-methionine + 5'-deoxyadenosine
Ac-YYTSPMTAPARSMLLTGN + S-adenosyl-L-methionine
Ac-YYTSPM-(2S)-2-amino-3-oxobutanoyl-APARSMLLTGN + L-methionine + 5'-deoxyadenosine + sulfur dioxide + H2O
acetyl-Tyr-Tyr-Thr-Ser-Pro-Met-Ser-Ala-Pro-Ala-Arg-Ser-Met-Leu-Leu-Thr-Gly-Asn + S-adenosyl-L-methionine
acetyl-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
S-adenosyl-L-methionine + a [Klebsiella pneumoniae sulfatase]-L-serine
[Klebsiella pneumoniae sulfatase]-3-oxo-L-alanine + 5'-deoxyadenosine + L-methionine
Substrates: the atsB gene product plays a posttranslational role that is essential for the sulfatase to gain its catalytic activity
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S-adenosyl-L-methionine + a [sulfatase]-L-serine
a [sulfatase]-3-oxo-L-alanine + 5'-deoxyadenosine + L-methionine
S-adenosyl-L-methionine + a [sulfatase]-L-serine
[sulfatase]-3-oxo-L-alanine + 5'-deoxyadenosine + L-methionine
Substrates: AtsB from Klebsiella pneumoniae can act on sulfatases of other species. The cytosolic cysteine-type sulfatase of Pseudomonas aeruginosa can be converted into a substrate of Klebsiella pneumoniae AtsB if the cysteine is substituted by serine and a signal peptide is added
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S-adenosyl-L-methionine + [Klebsiella pneumoniae sulfatase]-L-serine
[Klebsiella pneumoniae sulfatase]-3-oxo-L-alanine + 5'-deoxyadenosine + L-methionine
Substrates: peptide analysis of the Klebsiella pneumoniae sulfatase protein expressed in the presence of AtsB reveales that half of the polypeptides carry the formylglycine at position 72, while the remaining polypeptides carry the encoded serine. The inactive sulfatase expressed in the absence of AtsB carries exclusively serine 72, demonstrating that the atsB gene is required for formylglycine modification
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S-adenosyl-L-methionine + [periplasmic sulfatase AtsA]-L-serine
[periplasmic sulfatase AtsA]-3-oxo-L-alanine + 5'-deoxyadenosine + L-methionine
Tyr-Tyr-Thr-Ser-Pro-Met-Ser-Ala-Pro-Ala-Arg-Ser-Met-Leu-Leu-Thr-Gly-Asn + S-adenosyl-L-methionine + dithionite
Tyr-Tyr-Thr-Ser-Pro-Met-Ser-Ala-Pro-Ala-Arg-3-oxo-L-Ala-Met-Leu-Leu-Thr-Gly-Asn + L-methionine + 5'-deoxyadenosine + sulfur dioxide + H2O
[arylsulfatase]-L-serine + S-adenosyl-L-methionine + reduced acceptor
[arylsulfatase]-3-oxo-L-alanine + L-methionine + 5'-deoxyadenosine + acceptor + H2O
Substrates: -
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Ac-AVPSSIPSRASILTGM-NH2 + S-adenosyl-L-methionine + dithionite
Ac-AVPS-3-oxo-L-Ala-IPSRASILTGM-NH2 + L-methionine + 5'-deoxyadenosine + sulfur dioxide + H2O
Substrates: a flavodoxin/flavodoxin reductase/NADPH system may substitute for dithionite
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?
Ac-AVPSSIPSRASILTGM-NH2 + S-adenosyl-L-methionine + dithionite
Ac-AVPS-3-oxo-L-Ala-IPSRASILTGM-NH2 + L-methionine + 5'-deoxyadenosine + sulfur dioxide + H2O
Substrates: a flavodoxin/flavodoxin reductase/NADPH system may substitute for dithionite
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Ac-FENAYTAVPSSIASRASILTGMS-NH2 + S-adenosyl-L-methionine
Ac-FENAYTAVPS-3-oxo-L-Ala-IASRASILTGMS-NH2 + L-methionine + 5'-deoxyadenosine
Substrates: -
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?
Ac-FENAYTAVPSSIASRASILTGMS-NH2 + S-adenosyl-L-methionine
Ac-FENAYTAVPS-3-oxo-L-Ala-IASRASILTGMS-NH2 + L-methionine + 5'-deoxyadenosine
Substrates: -
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?
Ac-YYTSPMSAPARSMLLTGN + S-adenosyl-L-methionine
Ac-YYTSPM-3-oxo-L-Ala-APARSMLLTGN + L-methionine + 5'-deoxyadenosine
Substrates: a flavodoxin/flavodoxin reductase/NADPH system may substitute for dithionite
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Ac-YYTSPMSAPARSMLLTGN + S-adenosyl-L-methionine
Ac-YYTSPM-3-oxo-L-Ala-APARSMLLTGN + L-methionine + 5'-deoxyadenosine
Substrates: a flavodoxin/flavodoxin reductase/NADPH system may substitute for dithionite
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Ac-YYTSPMTAPARSMLLTGN + S-adenosyl-L-methionine
Ac-YYTSPM-(2S)-2-amino-3-oxobutanoyl-APARSMLLTGN + L-methionine + 5'-deoxyadenosine + sulfur dioxide + H2O
Substrates: a flavodoxin/flavodoxin reductase/NADPH system may substitute for dithionite
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Ac-YYTSPMTAPARSMLLTGN + S-adenosyl-L-methionine
Ac-YYTSPM-(2S)-2-amino-3-oxobutanoyl-APARSMLLTGN + L-methionine + 5'-deoxyadenosine + sulfur dioxide + H2O
Substrates: a flavodoxin/flavodoxin reductase/NADPH system may substitute for dithionite
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acetyl-Tyr-Tyr-Thr-Ser-Pro-Met-Ser-Ala-Pro-Ala-Arg-Ser-Met-Leu-Leu-Thr-Gly-Asn + S-adenosyl-L-methionine
acetyl-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
Substrates: a flavodoxin/flavodoxin reductase/NADPH system may substitute for dithionite with higly reduced activity
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acetyl-Tyr-Tyr-Thr-Ser-Pro-Met-Ser-Ala-Pro-Ala-Arg-Ser-Met-Leu-Leu-Thr-Gly-Asn + S-adenosyl-L-methionine
acetyl-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
Substrates: a flavodoxin/flavodoxin reductase/NADPH system may substitute for dithionite with higly reduced activity
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S-adenosyl-L-methionine + a [sulfatase]-L-serine
a [sulfatase]-3-oxo-L-alanine + 5'-deoxyadenosine + L-methionine
Substrates: -
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S-adenosyl-L-methionine + a [sulfatase]-L-serine
a [sulfatase]-3-oxo-L-alanine + 5'-deoxyadenosine + L-methionine
-
Substrates: -
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S-adenosyl-L-methionine + a [sulfatase]-L-serine
a [sulfatase]-3-oxo-L-alanine + 5'-deoxyadenosine + L-methionine
-
Substrates: the enzyme converts nonclassical aldehyde tags of the SX(A/P)XR-type. The enzyme is able to modify the artificial serine-containing motif STAGR
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S-adenosyl-L-methionine + [periplasmic sulfatase AtsA]-L-serine
[periplasmic sulfatase AtsA]-3-oxo-L-alanine + 5'-deoxyadenosine + L-methionine
Substrates: the enzyme is strictly required for modification of Ser72 in the periplasmic sulfatase AtsA of Klebsiella pneumoniae. AtsB-mediated formation of 3-oxo-L-alanine is dependent on the signal peptide of AtsA
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S-adenosyl-L-methionine + [periplasmic sulfatase AtsA]-L-serine
[periplasmic sulfatase AtsA]-3-oxo-L-alanine + 5'-deoxyadenosine + L-methionine
Substrates: AtsB-mediated formation of 3-oxo-L-alanine is dependent on the signal peptide of AtsA. AtsB physically interacts with AtsA in a Ser72-dependent manner
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Tyr-Tyr-Thr-Ser-Pro-Met-Ser-Ala-Pro-Ala-Arg-Ser-Met-Leu-Leu-Thr-Gly-Asn + S-adenosyl-L-methionine + dithionite
Tyr-Tyr-Thr-Ser-Pro-Met-Ser-Ala-Pro-Ala-Arg-3-oxo-L-Ala-Met-Leu-Leu-Thr-Gly-Asn + L-methionine + 5'-deoxyadenosine + sulfur dioxide + H2O
Substrates: a flavodoxin/flavodoxin reductase/NADPH system may substitute for dithionite with higly reduced activity
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Tyr-Tyr-Thr-Ser-Pro-Met-Ser-Ala-Pro-Ala-Arg-Ser-Met-Leu-Leu-Thr-Gly-Asn + S-adenosyl-L-methionine + dithionite
Tyr-Tyr-Thr-Ser-Pro-Met-Ser-Ala-Pro-Ala-Arg-3-oxo-L-Ala-Met-Leu-Leu-Thr-Gly-Asn + L-methionine + 5'-deoxyadenosine + sulfur dioxide + H2O
Substrates: a flavodoxin/flavodoxin reductase/NADPH system may substitute for dithionite with higly reduced activity
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additional information
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Substrates: the enzyme converts a serine 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
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additional information
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Substrates: the enzyme converts a serine 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
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additional information
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Substrates: the enzme also perfoms the reaction of the Cys-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
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additional information
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Substrates: the enzme also perfoms the reaction of the Cys-type anaerobic sulfatase-maturating enzyme, converting a cysteine 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
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additional information
?
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Substrates: the enzme also perfoms the reaction of the Cys-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
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additional information
?
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Substrates: the enzme also perfoms the reaction of the Cys-type anaerobic sulfatase-maturating enzyme, converting a cysteine 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
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additional information
?
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Substrates: the enzme also perfoms the reaction of the Cys-type anaerobic sulfatase-maturating enzyme, converting a cysteine 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
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additional information
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Substrates: the enzyme converts a serine 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
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additional information
?
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Substrates: the enzme also perfoms the reaction of the Cys-type anaerobic sulfatase-maturating enzyme, converting a cysteine 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
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