metallo-beta-lactamase superfamily protein [Mycobacterium tuberculosis]
Protein Classification
alkyl/aryl-sulfatase( domain architecture ID 11449593)
alkyl/aryl-sulfatase is a sulfohydrolase that allows the use of primary or secondary sulfates such as SDS as a sole sulfur source
List of domain hits
| Name | Accession | Description | Interval | E-value | |||||||||
| BDS1 | COG2015 | Alkyl sulfatase BDS1 and related hydrolases, metallo-beta-lactamase superfamily [Secondary ... |
1-622 | 0e+00 | |||||||||
Alkyl sulfatase BDS1 and related hydrolases, metallo-beta-lactamase superfamily [Secondary metabolites biosynthesis, transport and catabolism]; : Pssm-ID: 441618 [Multi-domain] Cd Length: 629 Bit Score: 1089.11 E-value: 0e+00
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| Name | Accession | Description | Interval | E-value | |||||||||
| BDS1 | COG2015 | Alkyl sulfatase BDS1 and related hydrolases, metallo-beta-lactamase superfamily [Secondary ... |
1-622 | 0e+00 | |||||||||
Alkyl sulfatase BDS1 and related hydrolases, metallo-beta-lactamase superfamily [Secondary metabolites biosynthesis, transport and catabolism]; Pssm-ID: 441618 [Multi-domain] Cd Length: 629 Bit Score: 1089.11 E-value: 0e+00
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| arylsulfatase_Sdsa1-like_MBL-fold | cd07710 | Pseudomonas aeruginosa arylsulfatase SdsA1, Pseudomonas sp. DSM6611 arylsulfatase Pisa1, and ... |
83-328 | 2.21e-130 | |||||||||
Pseudomonas aeruginosa arylsulfatase SdsA1, Pseudomonas sp. DSM6611 arylsulfatase Pisa1, and related proteins; MBL-fold metallo-hydrolase domain; Arylsulfatase (also known as aryl-sulfate sulfohydrolase, EC 3.1.6.1). Pseudomonas aeruginosa SdsA1 is a secreted SDS hydrolase that allows the bacterium to use primary sulfates such as the detergent SDS common in commercial personal hygiene products as a sole carbon or sulfur source. Pseudomonas inverting secondary alkylsulfatase 1 (Pisa1) is specific for secondary alkyl sulfates. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions. Pssm-ID: 293796 [Multi-domain] Cd Length: 239 Bit Score: 382.23 E-value: 2.21e-130
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| Alkyl_sulf_dimr | pfam14863 | Alkyl sulfatase dimerization; This domain is found in alkyl sulfatases such as the Pseudomonas ... |
359-494 | 1.87e-80 | |||||||||
Alkyl sulfatase dimerization; This domain is found in alkyl sulfatases such as the Pseudomonas aeruginosa SDS hydrolase, where it acts as a dimerization domain Pssm-ID: 464351 Cd Length: 136 Bit Score: 250.09 E-value: 1.87e-80
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| Lactamase_B | smart00849 | Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ... |
101-322 | 2.22e-10 | |||||||||
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins contain this domain. These proteins include thiolesterases, members of the glyoxalase II family, that catalyse the hydrolysis of S-D-lactoyl-glutathione to form glutathione and D-lactic acid and a competence protein that is essential for natural transformation in Neisseria gonorrhoeae and could be a transporter involved in DNA uptake. Except for the competence protein these proteins bind two zinc ions per molecule as cofactor. Pssm-ID: 214854 [Multi-domain] Cd Length: 177 Bit Score: 59.87 E-value: 2.22e-10
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| Name | Accession | Description | Interval | E-value | |||||||||
| BDS1 | COG2015 | Alkyl sulfatase BDS1 and related hydrolases, metallo-beta-lactamase superfamily [Secondary ... |
1-622 | 0e+00 | |||||||||
Alkyl sulfatase BDS1 and related hydrolases, metallo-beta-lactamase superfamily [Secondary metabolites biosynthesis, transport and catabolism]; Pssm-ID: 441618 [Multi-domain] Cd Length: 629 Bit Score: 1089.11 E-value: 0e+00
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| arylsulfatase_Sdsa1-like_MBL-fold | cd07710 | Pseudomonas aeruginosa arylsulfatase SdsA1, Pseudomonas sp. DSM6611 arylsulfatase Pisa1, and ... |
83-328 | 2.21e-130 | |||||||||
Pseudomonas aeruginosa arylsulfatase SdsA1, Pseudomonas sp. DSM6611 arylsulfatase Pisa1, and related proteins; MBL-fold metallo-hydrolase domain; Arylsulfatase (also known as aryl-sulfate sulfohydrolase, EC 3.1.6.1). Pseudomonas aeruginosa SdsA1 is a secreted SDS hydrolase that allows the bacterium to use primary sulfates such as the detergent SDS common in commercial personal hygiene products as a sole carbon or sulfur source. Pseudomonas inverting secondary alkylsulfatase 1 (Pisa1) is specific for secondary alkyl sulfates. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions. Pssm-ID: 293796 [Multi-domain] Cd Length: 239 Bit Score: 382.23 E-value: 2.21e-130
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| Alkyl_sulf_dimr | pfam14863 | Alkyl sulfatase dimerization; This domain is found in alkyl sulfatases such as the Pseudomonas ... |
359-494 | 1.87e-80 | |||||||||
Alkyl sulfatase dimerization; This domain is found in alkyl sulfatases such as the Pseudomonas aeruginosa SDS hydrolase, where it acts as a dimerization domain Pssm-ID: 464351 Cd Length: 136 Bit Score: 250.09 E-value: 1.87e-80
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| Alkyl_sulf_C | pfam14864 | Alkyl sulfatase C-terminal; This domain is found at the C-terminus of alkyl sulfatases. ... |
507-624 | 2.80e-41 | |||||||||
Alkyl sulfatase C-terminal; This domain is found at the C-terminus of alkyl sulfatases. Together with the N-terminal catalytic domain, this domain forms a hydrophobic chute and may recruit hydrophobic substrates. Pssm-ID: 405542 [Multi-domain] Cd Length: 124 Bit Score: 145.80 E-value: 2.80e-41
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| Lactamase_B | pfam00753 | Metallo-beta-lactamase superfamily; |
95-322 | 4.11e-13 | |||||||||
Metallo-beta-lactamase superfamily; Pssm-ID: 425851 [Multi-domain] Cd Length: 196 Bit Score: 68.55 E-value: 4.11e-13
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| metallo-hydrolase-like_MBL-fold | cd16282 | uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ... |
90-252 | 2.50e-12 | |||||||||
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo hydrolase domain; Members of the MBL-fold metallohydrolase superfamily are mainly hydrolytic enzymes which carry out a variety of biological functions. The class B metal beta-lactamases (MBLs) for which this fold was named perform only a small fraction of the activities included in this superfamily.Activities carried out by superfamily members include class B beta-lactamases, hydroxyacylglutathione hydrolases, AHL (acyl homoserine lactone) lactonases, persulfide dioxygenases, flavodiiron proteins, cleavage and polyadenylation specificity factors such as the Int9 and Int11 subunits of Integrator, Sdsa1-like and AtsA-like arylsulfatases, 5'-exonucleases human SNM1A and yeast Pso2p, ribonuclease J and ribonuclease Z, cyclic nucleotide phosphodiesterases, insecticide hydrolases, and proteins required for natural transformation competence. Classical members of the superfamily are di-, or less commonly mono-, zinc-ion-dependent hydrolases, however the diversity of biological roles is reflected in variations in the active site metallo-chemistry. Pssm-ID: 293840 [Multi-domain] Cd Length: 209 Bit Score: 66.44 E-value: 2.50e-12
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| Lactamase_B | smart00849 | Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ... |
101-322 | 2.22e-10 | |||||||||
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins contain this domain. These proteins include thiolesterases, members of the glyoxalase II family, that catalyse the hydrolysis of S-D-lactoyl-glutathione to form glutathione and D-lactic acid and a competence protein that is essential for natural transformation in Neisseria gonorrhoeae and could be a transporter involved in DNA uptake. Except for the competence protein these proteins bind two zinc ions per molecule as cofactor. Pssm-ID: 214854 [Multi-domain] Cd Length: 177 Bit Score: 59.87 E-value: 2.22e-10
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| GloB | COG0491 | Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General ... |
91-156 | 1.75e-07 | |||||||||
Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General function prediction only]; Pssm-ID: 440257 [Multi-domain] Cd Length: 215 Bit Score: 52.39 E-value: 1.75e-07
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| metallo-hydrolase-like_MBL-fold | cd16276 | uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ... |
83-155 | 7.78e-07 | |||||||||
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo hydrolase domain; Members of the MBL-fold metallohydrolase superfamily are mainly hydrolytic enzymes which carry out a variety of biological functions. The class B metal beta-lactamases (MBLs) for which this fold was named perform only a small fraction of the activities included in this superfamily.Activities carried out by superfamily members include class B beta-lactamases, hydroxyacylglutathione hydrolases, AHL (acyl homoserine lactone) lactonases, persulfide dioxygenases, flavodiiron proteins, cleavage and polyadenylation specificity factors such as the Int9 and Int11 subunits of Integrator, Sdsa1-like and AtsA-like arylsulfatases, 5'-exonucleases human SNM1A and yeast Pso2p, ribonuclease J and ribonuclease Z, cyclic nucleotide phosphodiesterases, insecticide hydrolases, and proteins required for natural transformation competence. Classical members of the superfamily are di-, or less commonly mono-, zinc-ion-dependent hydrolases, however the diversity of biological roles is reflected in variations in the active site metallo-chemistry. Pssm-ID: 293834 [Multi-domain] Cd Length: 188 Bit Score: 49.89 E-value: 7.78e-07
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| yflN-like_MBL-fold | cd07721 | uncharacterized subgroup which includes Bacillus subtilis yflN; MBL-fold metallo hydrolase ... |
90-156 | 4.39e-06 | |||||||||
uncharacterized subgroup which includes Bacillus subtilis yflN; MBL-fold metallo hydrolase domain; This subgroup includes the uncharacterized Bacillus subtilis yflN protein. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions. The class B metal beta-lactamases (MBLs) from which this fold was named are only a small fraction of the activities which are included in this superfamily. Activities carried out by superfamily members include class B beta-lactamases, hydroxyacylglutathione hydrolases, AHL (acyl homoserine lactone) lactonases, persulfide dioxygenases, flavodiiron proteins, cleavage and polyadenylation specificity factors such as the Int9 and Int11 subunits of Integrator, Sdsa1-like and AtsA-like arylsulfatases, 5'-exonucleases human SNM1A and yeast Pso2p, ribonuclease J and ribonuclease Z, cyclic nucleotide phosphodiesterases, insecticide hydrolases, and proteins required for natural transformation competence. Classical members of the superfamily are di-, or less commonly mono-, zinc-ion-dependent hydrolases, however the diversity of biological roles is reflected in variations in the active site metallo-chemistry. Pssm-ID: 293807 [Multi-domain] Cd Length: 202 Bit Score: 47.99 E-value: 4.39e-06
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| metallo-hydrolase-like_MBL-fold | cd06262 | mainly hydrolytic enzymes and related proteins which carry out various biological functions; ... |
100-156 | 3.06e-04 | |||||||||
mainly hydrolytic enzymes and related proteins which carry out various biological functions; MBL-fold metallohydrolase domain; Members of the MBL-fold metallohydrolase superfamily are mainly hydrolytic enzymes which carry out a variety of biological functions. The class B metal beta-lactamases (MBLs) for which this fold was named perform only a small fraction of the activities included in this superfamily. Activities carried out by superfamily members include class B beta-lactamases which can catalyze the hydrolysis of a wide range of beta-lactam antibiotics, hydroxyacylglutathione hydrolases (also called glyoxalase II) which hydrolyze S-d-lactoylglutathione to d-lactate in the second step of the glycoxlase system, AHL lactonases which catalyze the hydrolysis and opening of the homoserine lactone rings of acyl homoserine lactones (AHLs), persulfide dioxygenase which catalyze the oxidation of glutathione persulfide to glutathione and persulfite in the mitochondria, flavodiiron proteins which catalyze the reduction of oxygen and/or nitric oxide to water or nitrous oxide respectively, cleavage and polyadenylation specificity factors such as the Int9 and Int11 subunits of Integrator, Sdsa1-like and AtsA-like arylsulfatases, 5'-exonucleases human SNM1A and yeast Pso2p, ribonuclease J which has both 5'-3' exoribonucleolytic and endonucleolytic activity and ribonuclease Z which catalyzes the endonucleolytic removal of the 3' extension of the majority of tRNA precursors, cyclic nucleotide phosphodiesterases which decompose cyclic adenosine and guanosine 3', 5'-monophosphate (cAMP and cGMP) respectively, insecticide hydrolases, and proteins required for natural transformation competence. The diversity of biological roles is reflected in variations in the active site metallo-chemistry, for example classical members of the superfamily are di-, or less commonly mono-, zinc-ion-dependent hydrolases, human persulfide dioxygenase ETHE1 is a mono-iron binding member of the superfamily; Arabidopsis thaliana hydroxyacylglutathione hydrolases incorporates iron, manganese, and zinc in its dinuclear metal binding site, and flavodiiron proteins contains a diiron site. Pssm-ID: 293792 [Multi-domain] Cd Length: 188 Bit Score: 42.27 E-value: 3.06e-04
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| metallo-hydrolase-like_MBL-fold | cd07743 | uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ... |
104-155 | 1.50e-03 | |||||||||
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo hydrolase domain; Members of the MBL-fold metallohydrolase superfamily are mainly hydrolytic enzymes which carry out a variety of biological functions. The class B metal beta-lactamases (MBLs) from which this fold was named are only a small fraction of the activities which are included in this superfamily. Activities carried out by superfamily members include class B beta-lactamases, hydroxyacylglutathione hydrolases, AHL (acyl homoserine lactone) lactonases, persulfide dioxygenases, flavodiiron proteins, cleavage and polyadenylation specificity factors such as the Int9 and Int11 subunits of Integrator, Sdsa1-like and AtsA-like arylsulfatases, 5'-exonucleases human SNM1A and yeast Pso2p, ribonuclease J and ribonuclease Z, cyclic nucleotide phosphodiesterases, insecticide hydrolases, and proteins required for natural transformation competence. Classical members of the superfamily are di-, or less commonly mono-, zinc-ion-dependent hydrolases, however the diversity of biological roles is reflected in variations in the active site metallo-chemistry. Pssm-ID: 293829 [Multi-domain] Cd Length: 197 Bit Score: 40.21 E-value: 1.50e-03
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| Lactamase_B_2 | pfam12706 | Beta-lactamase superfamily domain; This family is part of the beta-lactamase superfamily and ... |
112-157 | 3.07e-03 | |||||||||
Beta-lactamase superfamily domain; This family is part of the beta-lactamase superfamily and is related to pfam00753. Pssm-ID: 432732 [Multi-domain] Cd Length: 196 Bit Score: 39.22 E-value: 3.07e-03
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| metallo-hydrolase-like_MBL-fold | cd16278 | uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ... |
105-156 | 4.60e-03 | |||||||||
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo hydrolase domain; Members of the MBL-fold metallohydrolase superfamily are mainly hydrolytic enzymes which carry out a variety of biological functions. The class B metal beta-lactamases (MBLs) for which this fold was named perform only a small fraction of the activities included in this superfamily.Activities carried out by superfamily members include class B beta-lactamases, hydroxyacylglutathione hydrolases, AHL (acyl homoserine lactone) lactonases, persulfide dioxygenases, flavodiiron proteins, cleavage and polyadenylation specificity factors such as the Int9 and Int11 subunits of Integrator, Sdsa1-like and AtsA-like arylsulfatases, 5'-exonucleases human SNM1A and yeast Pso2p, ribonuclease J and ribonuclease Z, cyclic nucleotide phosphodiesterases, insecticide hydrolases, and proteins required for natural transformation competence. Classical members of the superfamily are di-, or less commonly mono-, zinc-ion-dependent hydrolases, however the diversity of biological roles is reflected in variations in the active site metallo-chemistry. Pssm-ID: 293836 [Multi-domain] Cd Length: 185 Bit Score: 38.63 E-value: 4.60e-03
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| hydroxyacylglutathione_hydrolase_MBL-fold | cd07723 | hydroxyacylglutathione hydrolase, MBL-fold metallo-hydrolase domain; hydroxyacylglutathione ... |
112-183 | 7.80e-03 | |||||||||
hydroxyacylglutathione hydrolase, MBL-fold metallo-hydrolase domain; hydroxyacylglutathione hydrolase (EC 3.1.2.6, also known as, glyoxalase II; S-2-hydroxylacylglutathione hydrolase; hydroxyacylglutathione hydrolase; acetoacetylglutathione hydrolase). In the second step of the glycoxlase system this enzyme hydrolyzes S-d-lactoylglutathione to d-lactate and regenerates glutathione in the process. It has broad substrate specificity for glutathione thiol esters, hydrolyzing a number of these species to their corresponding carboxylic acids and reduced glutathione. It appears to hydrolyze 2-hydroxy thiol esters with greatest efficiency. It belongs to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions. Pssm-ID: 293809 [Multi-domain] Cd Length: 165 Bit Score: 37.44 E-value: 7.80e-03
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| Blast search parameters | ||||
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