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Information on EC 1.1.98.7 - serine-type anaerobic sulfatase-maturating enzyme
for references in articles please use BRENDA:EC1.1.98.7
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EC Tree 1 Oxidoreductases
1.1 Acting on the CH-OH group of donors
1.1.98 With other, known, physiological acceptors
1.1.98.7 serine-type anaerobic sulfatase-maturating enzyme
IUBMB Comments
A bacterial radical S-adenosyl-L-methionine (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-serine residue in the active site to a unique 3-oxo-L-alanine residue that is essential for the sulfatase activity. While the enzyme from Klebsiella pneumoniae is specific for L-serine, the enzyme from Clostridium perfringens can also act on L-cysteine, see EC 1.8.98.7, cysteine-type anaerobic sulfatase-maturating enzyme.
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Reaction Schemes
show+
=
+
+
+
a [sulfatase]-L-serine
=
a [sulfatase]-3-oxo-L-alanine
+
+
Synonyms
anaerobic sulfatase-maturating enzyme, anSME, AtsB, cpe0635, nSMEcpe, Ser-type anaerobic sulfatase-maturating enzyme, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
anaerobic sulfatase-maturating enzyme
anSME
AtsB
nSMEcpe
Ser-type anaerobic sulfatase-maturating enzyme
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
S-adenosyl-L-methionine + a [sulfatase]-L-serine = a [sulfatase]-3-oxo-L-alanine + 5'-deoxyadenosine + L-methionine
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SYSTEMATIC NAME
IUBMB Comments
[sulfatase]-L-serine:S-adenosyl-L-methionine oxidoreductase (3-oxo-L-alanine-forming)
A bacterial radical S-adenosyl-L-methionine (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-serine residue in the active site to a unique 3-oxo-L-alanine residue that is essential for the sulfatase activity. While the enzyme from Klebsiella pneumoniae is specific for L-serine, the enzyme from Clostridium perfringens can also act on L-cysteine, see EC 1.8.98.7, cysteine-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
Products: -
Products: -
?
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
Products: -
Products: -
?
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
Products: -
Products: -
?
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: -
Products: -
Products: -
?
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
Products: -
Products: -
?
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
Products: -
Products: -
?
Ac-FENAYTAVPSSIASRASILTGMS-NH2 + S-adenosyl-L-methionine
Ac-FENAYTAVPS-3-oxo-L-Ala-IASRASILTGMS-NH2 + L-methionine + 5'-deoxyadenosine
Substrates: -
Products: -
Products: -
?
Ac-FENAYTAVPSSIASRASILTGMS-NH2 + S-adenosyl-L-methionine
Ac-FENAYTAVPS-3-oxo-L-Ala-IASRASILTGMS-NH2 + L-methionine + 5'-deoxyadenosine
Substrates: -
Products: -
Products: -
?
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
Products: -
Products: -
?
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
Products: -
Products: -
?
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
Products: -
Products: -
?
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
Products: -
Products: -
?
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
Products: -
Products: -
?
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
Products: -
Products: -
?
S-adenosyl-L-methionine + a [sulfatase]-L-serine
a [sulfatase]-3-oxo-L-alanine + 5'-deoxyadenosine + L-methionine
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + a [sulfatase]-L-serine
a [sulfatase]-3-oxo-L-alanine + 5'-deoxyadenosine + L-methionine
-
Substrates: -
Products: -
Products: -
?
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
Products: -
Products: -
?
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
Products: -
Products: -
?
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
Products: -
Products: -
?
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
Products: -
Products: -
?
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
Products: -
Products: -
?
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
Products: -
Products: -
?
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
Products: -
Products: -
?
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
Products: -
Products: -
?
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
Products: -
Products: -
?
additional information
?
-
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
Products: -
Products: -
?
additional information
?
-
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
Products: -
Products: -
?
additional information
?
-
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
Products: -
Products: -
?
additional information
?
-
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
Products: -
Products: -
?
additional information
?
-
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
Products: -
Products: -
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
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
Products: -
Products: -
?
S-adenosyl-L-methionine + a [sulfatase]-L-serine
a [sulfatase]-3-oxo-L-alanine + 5'-deoxyadenosine + L-methionine
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
Products: -
Products: -
?
S-adenosyl-L-methionine + a [sulfatase]-L-serine
a [sulfatase]-3-oxo-L-alanine + 5'-deoxyadenosine + L-methionine
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + a [sulfatase]-L-serine
a [sulfatase]-3-oxo-L-alanine + 5'-deoxyadenosine + L-methionine
-
Substrates: -
Products: -
Products: -
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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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 molecule
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
metabolism
metabolism
involved in the pathway of sulfatase oxidation
metabolism
the enzyme is strictly required for modification of Ser72 in the periplasmic sulfatase AtsA of Klebsiella pneumoniae
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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_KLEAE
405
0
45372
Swiss-Prot
other Location (Reliability: 2)
ANSME_BACTN
Bacteroides thetaiotaomicron (strain ATCC 29148 / DSM 2079 / JCM 5827 / CCUG 10774 / NCTC 10582 / VPI-5482 / E50)
414
0
47949
Swiss-Prot
-
ANSME_CLOPE
Clostridium perfringens (strain 13 / Type A)
370
0
43371
Swiss-Prot
other Location (Reliability: 3)
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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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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
-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)
expressed in inactive form in Escherichia coli transformed with the structural gene atsA
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
molecular biology
-
enzymatic modification of a DARPin model protein carrying the aldehyde tag sequence SAPAR enables the production of a fluorescent conjugate. Thus proving its potential for bioconjugation chemistry. This tag system could be useful in orthogonal combination with the standard cysteine-type tag system targeted by formylglycine-generating enzyme, which is regularly utilized for protein labeling
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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 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
Fang, Q.; Peng, J.; Dierks, T.
Post-translational formylglycine modification of bacterial sulfatases by the radical S-adenosylmethionine protein AtsB
J. Biol. Chem.
279
14570-14578
2004
Klebsiella pneumoniae (Q9X758)
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
Bacteroides thetaiotaomicron (Q02550), Bacteroides thetaiotaomicron DSM 2079 (Q02550)
brenda
Krger, T.; Weiland, S.; Boschanski, M.; Sinha, P.K.; Falck, G.; Meller, K.M.; Dierks, T.; Sewald, N.
Conversion of serine-type aldehyde tags by the radical SAM protein AtsB from Methanosarcina mazei
Chembiochem
20
2074-2078
2019
Methanosarcina mazei
brenda
Szameit, C.; Miech, C.; Balleininger, M.; Schmidt, B.; von Figura, K.; Dierks, T.
The iron sulfur protein AtsB is required for posttranslational formation of formylglycine in the Klebsiella sulfatase
J. Biol. Chem.
274
15375-15381
1999
Klebsiella pneumoniae (Q9X758)
brenda
Marquordt, C.; Fang, Q.; Will, E.; Peng, J.; von Figura, K.; Dierks, T.
Posttranslational modification of serine to formylglycine in bacterial sulfatases. Recognition of the modification motif by the iron-sulfur protein AtsB
J. Biol. Chem.
278
2212-2218
2002
Klebsiella pneumoniae (Q9X758)
brenda
Berteau, O.; Guillot, A.; Benjdia, A.; Rabot, S.
A new type of bacterial sulfatase reveals a novel maturation pathway in prokaryotes
J. Biol. Chem.
281
22464-22470
2006
Clostridium perfringens (Q8XMQ3)
brenda
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