FprA family A-type flavoprotein [Clostridioides difficile]
FprA family A-type flavoprotein( domain architecture ID 11417996)
FprA family A-type flavoprotein contains an MBL fold metallo-hydrolase domain having a binuclear iron center, and a flavodoxin-like domain containing one FMN moiety; similar to Desulfovibrio gigas rubredoxin-oxygen oxidoreductase, which catalyzes the four-electron reduction of one oxygen molecule to two water molecules
List of domain hits
Name | Accession | Description | Interval | E-value | ||||||
NorV | COG0426 | Flavorubredoxin [Energy production and conversion]; |
3-396 | 3.04e-171 | ||||||
Flavorubredoxin [Energy production and conversion]; : Pssm-ID: 440195 [Multi-domain] Cd Length: 390 Bit Score: 483.56 E-value: 3.04e-171
|
||||||||||
Name | Accession | Description | Interval | E-value | ||||||
NorV | COG0426 | Flavorubredoxin [Energy production and conversion]; |
3-396 | 3.04e-171 | ||||||
Flavorubredoxin [Energy production and conversion]; Pssm-ID: 440195 [Multi-domain] Cd Length: 390 Bit Score: 483.56 E-value: 3.04e-171
|
||||||||||
flavodiiron_proteins_MBL-fold | cd07709 | catalytic domain of flavodiiron proteins (FDPs) and related proteins; MBL-fold ... |
6-243 | 2.10e-114 | ||||||
catalytic domain of flavodiiron proteins (FDPs) and related proteins; MBL-fold metallo-hydrolase domain; FDPs catalyze the reduction of oxygen and/or nitric oxide to water or nitrous oxide respectively. In addition to this N-terminal catalytic domain they contain a C-terminal flavin mononucleotide-binding flavodoxin-like domain. Although some FDPs are able to reduce NO or O2 with similar catalytic efficiencies others are selective for either NO or O2, such as Escherichia coli flavorubredoxin which is selective toward NO and G. intestinalis FDP which is selective toward O2. These enzymes belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions. Some members of this subgroup are single domain. Pssm-ID: 293795 [Multi-domain] Cd Length: 238 Bit Score: 333.30 E-value: 2.10e-114
|
||||||||||
PRK11921 | PRK11921 | anaerobic nitric oxide reductase flavorubredoxin; |
5-397 | 1.53e-106 | ||||||
anaerobic nitric oxide reductase flavorubredoxin; Pssm-ID: 237023 [Multi-domain] Cd Length: 394 Bit Score: 319.33 E-value: 1.53e-106
|
||||||||||
Lactamase_B | smart00849 | Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ... |
37-189 | 2.59e-23 | ||||||
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: 95.70 E-value: 2.59e-23
|
||||||||||
flav_short | TIGR01753 | flavodoxin, short chain; Flavodoxins are small redox-active proteins with a flavin ... |
255-393 | 7.44e-18 | ||||||
flavodoxin, short chain; Flavodoxins are small redox-active proteins with a flavin mononucleotide (FMN) prosthetic group. They can act in nitrogen fixation by nitrogenase, in sulfite reduction, and light-dependent NADP+ reduction in during photosynthesis, among other roles. This model describes the short chain type. Many of these are involved in sulfite reduction. [Energy metabolism, Electron transport] Pssm-ID: 273789 [Multi-domain] Cd Length: 140 Bit Score: 79.30 E-value: 7.44e-18
|
||||||||||
Lactamase_B | pfam00753 | Metallo-beta-lactamase superfamily; |
37-224 | 8.07e-11 | ||||||
Metallo-beta-lactamase superfamily; Pssm-ID: 425851 [Multi-domain] Cd Length: 196 Bit Score: 60.85 E-value: 8.07e-11
|
||||||||||
Name | Accession | Description | Interval | E-value | ||||||
NorV | COG0426 | Flavorubredoxin [Energy production and conversion]; |
3-396 | 3.04e-171 | ||||||
Flavorubredoxin [Energy production and conversion]; Pssm-ID: 440195 [Multi-domain] Cd Length: 390 Bit Score: 483.56 E-value: 3.04e-171
|
||||||||||
flavodiiron_proteins_MBL-fold | cd07709 | catalytic domain of flavodiiron proteins (FDPs) and related proteins; MBL-fold ... |
6-243 | 2.10e-114 | ||||||
catalytic domain of flavodiiron proteins (FDPs) and related proteins; MBL-fold metallo-hydrolase domain; FDPs catalyze the reduction of oxygen and/or nitric oxide to water or nitrous oxide respectively. In addition to this N-terminal catalytic domain they contain a C-terminal flavin mononucleotide-binding flavodoxin-like domain. Although some FDPs are able to reduce NO or O2 with similar catalytic efficiencies others are selective for either NO or O2, such as Escherichia coli flavorubredoxin which is selective toward NO and G. intestinalis FDP which is selective toward O2. These enzymes belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions. Some members of this subgroup are single domain. Pssm-ID: 293795 [Multi-domain] Cd Length: 238 Bit Score: 333.30 E-value: 2.10e-114
|
||||||||||
PRK11921 | PRK11921 | anaerobic nitric oxide reductase flavorubredoxin; |
5-397 | 1.53e-106 | ||||||
anaerobic nitric oxide reductase flavorubredoxin; Pssm-ID: 237023 [Multi-domain] Cd Length: 394 Bit Score: 319.33 E-value: 1.53e-106
|
||||||||||
PRK05452 | PRK05452 | anaerobic nitric oxide reductase flavorubredoxin; Provisional |
7-394 | 1.02e-83 | ||||||
anaerobic nitric oxide reductase flavorubredoxin; Provisional Pssm-ID: 235475 [Multi-domain] Cd Length: 479 Bit Score: 263.54 E-value: 1.02e-83
|
||||||||||
Lactamase_B | smart00849 | Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ... |
37-189 | 2.59e-23 | ||||||
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: 95.70 E-value: 2.59e-23
|
||||||||||
flav_short | TIGR01753 | flavodoxin, short chain; Flavodoxins are small redox-active proteins with a flavin ... |
255-393 | 7.44e-18 | ||||||
flavodoxin, short chain; Flavodoxins are small redox-active proteins with a flavin mononucleotide (FMN) prosthetic group. They can act in nitrogen fixation by nitrogenase, in sulfite reduction, and light-dependent NADP+ reduction in during photosynthesis, among other roles. This model describes the short chain type. Many of these are involved in sulfite reduction. [Energy metabolism, Electron transport] Pssm-ID: 273789 [Multi-domain] Cd Length: 140 Bit Score: 79.30 E-value: 7.44e-18
|
||||||||||
GloB | COG0491 | Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General ... |
37-248 | 3.41e-13 | ||||||
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: 68.18 E-value: 3.41e-13
|
||||||||||
FldA | COG0716 | Flavodoxin [Energy production and conversion]; Flavodoxin is part of the Pathway/BioSystem: ... |
257-392 | 9.43e-13 | ||||||
Flavodoxin [Energy production and conversion]; Flavodoxin is part of the Pathway/BioSystem: Heme biosynthesis Pssm-ID: 440480 [Multi-domain] Cd Length: 135 Bit Score: 64.92 E-value: 9.43e-13
|
||||||||||
metallo-hydrolase-like_MBL-fold | cd06262 | mainly hydrolytic enzymes and related proteins which carry out various biological functions; ... |
37-163 | 6.18e-11 | ||||||
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: 61.15 E-value: 6.18e-11
|
||||||||||
Lactamase_B | pfam00753 | Metallo-beta-lactamase superfamily; |
37-224 | 8.07e-11 | ||||||
Metallo-beta-lactamase superfamily; Pssm-ID: 425851 [Multi-domain] Cd Length: 196 Bit Score: 60.85 E-value: 8.07e-11
|
||||||||||
Flavodoxin_1 | pfam00258 | Flavodoxin; |
257-389 | 1.21e-09 | ||||||
Flavodoxin; Pssm-ID: 425562 [Multi-domain] Cd Length: 142 Bit Score: 56.22 E-value: 1.21e-09
|
||||||||||
PRK05568 | PRK05568 | flavodoxin; Provisional |
254-394 | 4.71e-09 | ||||||
flavodoxin; Provisional Pssm-ID: 235508 [Multi-domain] Cd Length: 142 Bit Score: 54.43 E-value: 4.71e-09
|
||||||||||
DHPS-like_MBL-fold | cd07713 | Methanocaldococcus jannaschii dihydropteroate synthase, Thermoanaerobacter tengcongensis Tflp, ... |
38-143 | 5.05e-09 | ||||||
Methanocaldococcus jannaschii dihydropteroate synthase, Thermoanaerobacter tengcongensis Tflp, and related proteins; MBL-fold metallo hydrolase domain; This subgroup includes Methanocaldococcus jannaschii 7,8-dihydropterin-6-methyl-4-(beta-D-ribofuranosyl)-aminobenzene-5'-phosphate synthase (EC 2.5.1.15), a folate biosynthetic enzyme also known as dihydropteroate synthase and 7,8 dihydropteroate synthase. Thermoanaerobacter tengcongensis Tflp is a ferredoxin-like member. 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: 293799 Cd Length: 269 Bit Score: 56.86 E-value: 5.05e-09
|
||||||||||
TTHA1429-like_MBL-fold | cd07725 | uncharacterized Thermus thermophilus TTHA1429 and related proteins; MBL-fold metallo hydrolase ... |
37-166 | 6.78e-09 | ||||||
uncharacterized Thermus thermophilus TTHA1429 and related proteins; MBL-fold metallo hydrolase domain; Includes the MBL-fold metallo hydrolase domain of uncharacterized Thermus thermophilus TTHA1429 and related proteins. 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: 293811 [Multi-domain] Cd Length: 184 Bit Score: 55.00 E-value: 6.78e-09
|
||||||||||
yflN-like_MBL-fold | cd07721 | uncharacterized subgroup which includes Bacillus subtilis yflN; MBL-fold metallo hydrolase ... |
31-225 | 1.50e-08 | ||||||
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: 54.53 E-value: 1.50e-08
|
||||||||||
PRK06756 | PRK06756 | flavodoxin; Provisional |
254-396 | 7.68e-08 | ||||||
flavodoxin; Provisional Pssm-ID: 168663 [Multi-domain] Cd Length: 148 Bit Score: 51.42 E-value: 7.68e-08
|
||||||||||
ST1585-like_MBL-fold | cd07726 | uncharacterized subgroup which includes Sulfolobus tokodaii ST1585 protein; MBL-fold metallo ... |
38-168 | 1.95e-07 | ||||||
uncharacterized subgroup which includes Sulfolobus tokodaii ST1585 protein; MBL-fold metallo hydrolase domain; This subgroup includes the uncharacterized Sulfolobus tokodaii ST1585 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: 293812 [Multi-domain] Cd Length: 215 Bit Score: 51.34 E-value: 1.95e-07
|
||||||||||
PRK05569 | PRK05569 | flavodoxin; Provisional |
254-394 | 2.69e-07 | ||||||
flavodoxin; Provisional Pssm-ID: 135442 [Multi-domain] Cd Length: 141 Bit Score: 49.45 E-value: 2.69e-07
|
||||||||||
WrbA | COG0655 | Multimeric flavodoxin WrbA, includes NAD(P)H:quinone oxidoreductase [Energy production and ... |
257-397 | 1.18e-06 | ||||||
Multimeric flavodoxin WrbA, includes NAD(P)H:quinone oxidoreductase [Energy production and conversion]; Pssm-ID: 440420 [Multi-domain] Cd Length: 181 Bit Score: 48.39 E-value: 1.18e-06
|
||||||||||
UlaG | COG2220 | L-ascorbate lactonase UlaG, metallo-beta-lactamase superfamily [Carbohydrate transport and ... |
37-147 | 8.47e-06 | ||||||
L-ascorbate lactonase UlaG, metallo-beta-lactamase superfamily [Carbohydrate transport and metabolism]; Pssm-ID: 441822 [Multi-domain] Cd Length: 224 Bit Score: 46.45 E-value: 8.47e-06
|
||||||||||
metallo-hydrolase-like_MBL-fold | cd07732 | uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ... |
32-162 | 9.66e-05 | ||||||
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo hydrolase domain; Includes functionally uncharacterized Enterococcus faecalis EF2904. 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: 293818 [Multi-domain] Cd Length: 202 Bit Score: 42.98 E-value: 9.66e-05
|
||||||||||
AHL_lactonase_MBL-fold | cd07729 | quorum-quenching N-acyl-homoserine lactonase, MBL-fold metallo-hydrolase domain; Acyl ... |
36-106 | 2.57e-04 | ||||||
quorum-quenching N-acyl-homoserine lactonase, MBL-fold metallo-hydrolase domain; Acyl Homoserine Lactones (also known as AHLs) are signal molecules which coordinate gene expression in quorum sensing, in many Gram-negative bacteria. Quorum-quenching N-acyl-homoserine lactonase (also known as AHL lactonase, N-acyl-L-homoserine lactone hydrolase, EC 3.1.1.81) catalyzes the hydrolysis and opening of the homoserine lactone rings of AHLs, a reaction that can block quorum sensing. These enzymes 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: 293815 [Multi-domain] Cd Length: 238 Bit Score: 42.20 E-value: 2.57e-04
|
||||||||||
hydroxyacylglutathione_hydrolase_MBL-fold | cd07723 | hydroxyacylglutathione hydrolase, MBL-fold metallo-hydrolase domain; hydroxyacylglutathione ... |
38-143 | 2.94e-04 | ||||||
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: 40.91 E-value: 2.94e-04
|
||||||||||
PRK06703 | PRK06703 | flavodoxin; Provisional |
257-393 | 5.89e-04 | ||||||
flavodoxin; Provisional Pssm-ID: 235854 [Multi-domain] Cd Length: 151 Bit Score: 40.13 E-value: 5.89e-04
|
||||||||||
MBLAC2-like_MBL-fold | cd07712 | uncharacterized human metallo-beta-lactamase domain-containing protein 2 and related proteins; ... |
37-224 | 1.25e-03 | ||||||
uncharacterized human metallo-beta-lactamase domain-containing protein 2 and related proteins; MBL-fold metallo hydrolase domain; Includes the MBL-fold metallo hydrolase domain of uncharacterized human MBLAC2 and related proteins. 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: 293798 [Multi-domain] Cd Length: 182 Bit Score: 39.53 E-value: 1.25e-03
|
||||||||||
Lactamase_B_2 | pfam12706 | Beta-lactamase superfamily domain; This family is part of the beta-lactamase superfamily and ... |
46-158 | 1.44e-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: 39.60 E-value: 1.44e-03
|
||||||||||
TTHA0252-CPSF-like_MBL-fold | cd16295 | Thermus thermophilus TTHA0252 and related cleavage and polyadenylation specificity factors; ... |
38-111 | 3.04e-03 | ||||||
Thermus thermophilus TTHA0252 and related cleavage and polyadenylation specificity factors; MBL-fold metallo-hydrolase domain; Includes the archaeal cleavage and polyadenylation specificity factors (CPSFs) such as Methanothermobacter thermautotrophicus MTH1203, and Pyrococcus horikoshii PH1404. In addition to the MBL-fold metallo-hydrolase nuclease and the beta-CASP domains, members of this subgroup contain two contiguous KH domains. 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: 293853 [Multi-domain] Cd Length: 197 Bit Score: 38.59 E-value: 3.04e-03
|
||||||||||
MBLAC1-like_MBL-fold | cd07711 | uncharacterized human metallo-beta-lactamase domain-containing protein 1 and related proteins; ... |
40-89 | 3.13e-03 | ||||||
uncharacterized human metallo-beta-lactamase domain-containing protein 1 and related proteins; MBL-fold metallo hydrolase domain; Includes the MBL-fold metallo hydrolase domain of uncharacterized human MBLAC1 and related proteins. 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: 293797 [Multi-domain] Cd Length: 190 Bit Score: 38.34 E-value: 3.13e-03
|
||||||||||
metallo-hydrolase-like_MBL-fold | cd16280 | uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ... |
38-143 | 6.19e-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: 293838 [Multi-domain] Cd Length: 251 Bit Score: 37.95 E-value: 6.19e-03
|
||||||||||
OPHC2-like_MBL-fold | cd07720 | Pseudomonas pseudoalcaligenes organophosphorus hydrolase C2, and related proteins; MBL-fold ... |
34-89 | 6.58e-03 | ||||||
Pseudomonas pseudoalcaligenes organophosphorus hydrolase C2, and related proteins; MBL-fold metallo hydrolase domain; Pseudomonas pseudoalcaligenes OPHC2 is a thermostable organophosphorus hydrolase which a broad substrate activity spectrum: it hydrolyzes various phosphotriesters, esters, and a lactone. This subgroup also includes Pseudomonas oleovorans PoOPH which exhibits high lactonase and esterase activities, and latent PTE activity. However, double mutations His250Ile/Ile263Trp switch PoOPH into an efficient and thermostable PTE. 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: 293806 [Multi-domain] Cd Length: 251 Bit Score: 37.91 E-value: 6.58e-03
|
||||||||||
Blast search parameters | ||||
|