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Conserved domains on  [gi|51857303|dbj|BAD41461|]
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putative cyclase/dehydrase [Symbiobacterium thermophilum IAM 14863]

Protein Classification

MBL fold metallo-hydrolase( domain architecture ID 10888684)

MBL fold metallo-hydrolase is most likely a hydrolytic enzyme that may have substrate towards phosphotriesters, esters, and/or lactones

CATH:  3.60.15.10
EC:  3.-.-.-
Gene Ontology:  GO:0016787|GO:0046872
PubMed:  17597585|12177301|11471246|11513844
SCOP:  3001057

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
metallo-hydrolase-like_MBL-fold cd16282
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 50-240 6.54e-47

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: 156.96  E-value: 6.54e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51857303  50 PGSSDFPVTAAQVTGQRHRVVVDTLIRPADMAPFAGA---------TLVIYTHFDWDHCWGTAAFP--GVPVIGHQLTRE 118
Cdd:cd16282   8 PDGGGFISNIGFIVGDDGVVVIDTGASPRLARALLAAirkvtdkpvRYVVNTHYHGDHTLGNAAFAdaGAPIIAHENTRE 87

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51857303 119 RLLApEPGEFLERMRAEKPAHFEGSQIIPPDVTFRDRLDIDAGGLTLELHHL-PGHTADSVVVHVPELGLLLAGDAVETP 197
Cdd:cd16282  88 ELAA-RGEAYLELMRRLGGDAMAGTELVLPDRTFDDGLTLDLGGRTVELIHLgPAHTPGDLVVWLPEEGVLFAGDLVFNG 166

                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 51857303 198 LPTLSESGHIRAWAGALRKWSQAGLKHVVPGHGRPGGPELLAA 240
Cdd:cd16282 167 RIPFLPDGSLAGWIAALDRLLALDATVVVPGHGPVGDKADLRA 209
 
Name Accession Description Interval E-value
metallo-hydrolase-like_MBL-fold cd16282
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 50-240 6.54e-47

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: 156.96  E-value: 6.54e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51857303  50 PGSSDFPVTAAQVTGQRHRVVVDTLIRPADMAPFAGA---------TLVIYTHFDWDHCWGTAAFP--GVPVIGHQLTRE 118
Cdd:cd16282   8 PDGGGFISNIGFIVGDDGVVVIDTGASPRLARALLAAirkvtdkpvRYVVNTHYHGDHTLGNAAFAdaGAPIIAHENTRE 87

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51857303 119 RLLApEPGEFLERMRAEKPAHFEGSQIIPPDVTFRDRLDIDAGGLTLELHHL-PGHTADSVVVHVPELGLLLAGDAVETP 197
Cdd:cd16282  88 ELAA-RGEAYLELMRRLGGDAMAGTELVLPDRTFDDGLTLDLGGRTVELIHLgPAHTPGDLVVWLPEEGVLFAGDLVFNG 166

                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 51857303 198 LPTLSESGHIRAWAGALRKWSQAGLKHVVPGHGRPGGPELLAA 240
Cdd:cd16282 167 RIPFLPDGSLAGWIAALDRLLALDATVVVPGHGPVGDKADLRA 209
GloB COG0491
Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General ...
 62-256 5.02e-30

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: 113.25  E-value: 5.02e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51857303  62 VTGQRHRVVVDTLIRPADMAPFAGA--------TLVIYTHFDWDHCWGTAAFP---GVPVIGHQLTRERLLAPEPGEFLe 130
Cdd:COG0491  20 IVGGDGAVLIDTGLGPADAEALLAAlaalgldiKAVLLTHLHPDHVGGLAALAeafGAPVYAHAAEAEALEAPAAGALF- 98

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51857303 131 rmraekpahfeGSQIIPPDVTFRDRLDIDAGGLTLELHHLPGHTADSVVVHVPELGLLLAGDAV---ETPLPTLSEsGHI 207
Cdd:COG0491  99 -----------GREPVPPDRTLEDGDTLELGGPGLEVIHTPGHTPGHVSFYVPDEKVLFTGDALfsgGVGRPDLPD-GDL 166

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 51857303 208 RAWAGALRKWSQAGLKHVVPGHGRPGGPELLAANAAYIEGVLEAAEAGL 256
Cdd:COG0491 167 AQWLASLERLLALPPDLVIPGHGPPTTAEAIDYLEELLAALGERANPFL 215
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 62-229 2.84e-20

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: 86.07  E-value: 2.84e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51857303     62 VTGQRHRVVVDTLIRPADMAPFAGA-------TLVIYTHFDWDHCWGTAAF---PGVPVIGHQLTRErllapepgeFLER 131
Cdd:smart00849   5 VRDDGGAILIDTGPGEAEDLLAELKklgpkkiDAIILTHGHPDHIGGLPELleaPGAPVYAPEGTAE---------LLKD 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51857303    132 MRAEKPAHFEGSQIIPPDVTFRDRLDIDAGGLTLELHHLPGHTADSVVVHVPELGLLLAGDAV--ETPLPTLSESGH--I 207
Cdd:smart00849  76 LLALLGELGAEAEPAPPDRTLKDGDELDLGGGELEVIHTPGHTPGSIVLYLPEGKILFTGDLLfaGGDGRTLVDGGDaaA 155

                          170       180
                   ....*....|....*....|..
gi 51857303    208 RAWAGALRKWSQAGLKHVVPGH 229
Cdd:smart00849 156 SDALESLLKLLKLLPKLVVPGH 177
Lactamase_B pfam00753
Metallo-beta-lactamase superfamily;
62-229 1.15e-15

Metallo-beta-lactamase superfamily;


Pssm-ID: 425851 [Multi-domain]  Cd Length: 196  Bit Score: 73.94  E-value: 1.15e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51857303    62 VTGQRHRVVVDTLIRPADMAPFAGATL---------VIYTHFDWDHCWGTAAFP---GVPVIGHQLTRERLLapepGEFL 129
Cdd:pfam00753  11 IEGGGGAVLIDTGGSAEAALLLLLAALglgpkdidaVILTHGHFDHIGGLGELAeatDVPVIVVAEEARELL----DEEL 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51857303   130 ERMRAEKPAHFEGSQIIPPDVTFRDRLDIDAGGLTLELHHLPGHTADSVVVHVPELGLLLAGDAVETP----------LP 199
Cdd:pfam00753  87 GLAASRLGLPGPPVVPLPPDVVLEEGDGILGGGLGLLVTHGPGHGPGHVVVYYGGGKVLFTGDLLFAGeigrldlplgGL 166

                         170       180       190
                  ....*....|....*....|....*....|
gi 51857303   200 TLSESGHIRAWAGALRKWSQAGLKHVVPGH 229
Cdd:pfam00753 167 LVLHPSSAESSLESLLKLAKLKAAVIVPGH 196
 
Name Accession Description Interval E-value
metallo-hydrolase-like_MBL-fold cd16282
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 50-240 6.54e-47

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: 156.96  E-value: 6.54e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51857303  50 PGSSDFPVTAAQVTGQRHRVVVDTLIRPADMAPFAGA---------TLVIYTHFDWDHCWGTAAFP--GVPVIGHQLTRE 118
Cdd:cd16282   8 PDGGGFISNIGFIVGDDGVVVIDTGASPRLARALLAAirkvtdkpvRYVVNTHYHGDHTLGNAAFAdaGAPIIAHENTRE 87

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51857303 119 RLLApEPGEFLERMRAEKPAHFEGSQIIPPDVTFRDRLDIDAGGLTLELHHL-PGHTADSVVVHVPELGLLLAGDAVETP 197
Cdd:cd16282  88 ELAA-RGEAYLELMRRLGGDAMAGTELVLPDRTFDDGLTLDLGGRTVELIHLgPAHTPGDLVVWLPEEGVLFAGDLVFNG 166

                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 51857303 198 LPTLSESGHIRAWAGALRKWSQAGLKHVVPGHGRPGGPELLAA 240
Cdd:cd16282 167 RIPFLPDGSLAGWIAALDRLLALDATVVVPGHGPVGDKADLRA 209
GloB COG0491
Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General ...
 62-256 5.02e-30

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: 113.25  E-value: 5.02e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51857303  62 VTGQRHRVVVDTLIRPADMAPFAGA--------TLVIYTHFDWDHCWGTAAFP---GVPVIGHQLTRERLLAPEPGEFLe 130
Cdd:COG0491  20 IVGGDGAVLIDTGLGPADAEALLAAlaalgldiKAVLLTHLHPDHVGGLAALAeafGAPVYAHAAEAEALEAPAAGALF- 98

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51857303 131 rmraekpahfeGSQIIPPDVTFRDRLDIDAGGLTLELHHLPGHTADSVVVHVPELGLLLAGDAV---ETPLPTLSEsGHI 207
Cdd:COG0491  99 -----------GREPVPPDRTLEDGDTLELGGPGLEVIHTPGHTPGHVSFYVPDEKVLFTGDALfsgGVGRPDLPD-GDL 166

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 51857303 208 RAWAGALRKWSQAGLKHVVPGHGRPGGPELLAANAAYIEGVLEAAEAGL 256
Cdd:COG0491 167 AQWLASLERLLALPPDLVIPGHGPPTTAEAIDYLEELLAALGERANPFL 215
metallo-hydrolase-like_MBL-fold cd06262
mainly hydrolytic enzymes and related proteins which carry out various biological functions; ...
 87-229 5.88e-21

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: 88.11  E-value: 5.88e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51857303  87 TLVIYTHFDWDHCWGTAAF---PGVPVIGHQLTRERLLAPEPGEFLERMRAEKPAhfegsqiiPPDVTFRDRLDIDAGGL 163
Cdd:cd06262  47 KAILLTHGHFDHIGGLAELkeaPGAPVYIHEADAELLEDPELNLAFFGGGPLPPP--------EPDILLEDGDTIELGGL 118

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 51857303 164 TLELHHLPGHTADSVVVHVPELGLLLAGDAV------ETPLPTLSesgHIRAWAGALRKWSQAGLK-HVVPGH 229
Cdd:cd06262 119 ELEVIHTPGHTPGSVCFYIEEEGVLFTGDTLfagsigRTDLPGGD---PEQLIESIKKLLLLLPDDtVVYPGH 188
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 62-229 2.84e-20

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: 86.07  E-value: 2.84e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51857303     62 VTGQRHRVVVDTLIRPADMAPFAGA-------TLVIYTHFDWDHCWGTAAF---PGVPVIGHQLTRErllapepgeFLER 131
Cdd:smart00849   5 VRDDGGAILIDTGPGEAEDLLAELKklgpkkiDAIILTHGHPDHIGGLPELleaPGAPVYAPEGTAE---------LLKD 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51857303    132 MRAEKPAHFEGSQIIPPDVTFRDRLDIDAGGLTLELHHLPGHTADSVVVHVPELGLLLAGDAV--ETPLPTLSESGH--I 207
Cdd:smart00849  76 LLALLGELGAEAEPAPPDRTLKDGDELDLGGGELEVIHTPGHTPGSIVLYLPEGKILFTGDLLfaGGDGRTLVDGGDaaA 155

                          170       180
                   ....*....|....*....|..
gi 51857303    208 RAWAGALRKWSQAGLKHVVPGH 229
Cdd:smart00849 156 SDALESLLKLLKLLPKLVVPGH 177
metallo-hydrolase-like_MBL-fold cd16276
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 87-236 5.94e-19

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: 82.63  E-value: 5.94e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51857303  87 TLVIYTHFDWDHCWGTAAFP--GVPVIGHQLTRERL-LAPEPgeflermraekpahfegsQIIPPDVTFRDRLDIDAGGL 163
Cdd:cd16276  47 THVVYSHNHADHIGGASIFKdeGATIIAHEATAELLkRNPDP------------------KRPVPTVTFDDEYTLEVGGQ 108

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 51857303 164 TLELH-HLPGHTADSVVVHVPELGLLLAGDAV---ETPLPTLSESGHIRAWAGALRKWSQAGLKHVVPGHG-RPGGPE 236
Cdd:cd16276 109 TLELSyFGPNHGPGNIVIYLPKQKVLMAVDLInpgWVPFFNFAGSEDIPGYIEALDELLEYDFDTFVGGHGnRLGTRE 186
Lactamase_B pfam00753
Metallo-beta-lactamase superfamily;
62-229 1.15e-15

Metallo-beta-lactamase superfamily;


Pssm-ID: 425851 [Multi-domain]  Cd Length: 196  Bit Score: 73.94  E-value: 1.15e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51857303    62 VTGQRHRVVVDTLIRPADMAPFAGATL---------VIYTHFDWDHCWGTAAFP---GVPVIGHQLTRERLLapepGEFL 129
Cdd:pfam00753  11 IEGGGGAVLIDTGGSAEAALLLLLAALglgpkdidaVILTHGHFDHIGGLGELAeatDVPVIVVAEEARELL----DEEL 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51857303   130 ERMRAEKPAHFEGSQIIPPDVTFRDRLDIDAGGLTLELHHLPGHTADSVVVHVPELGLLLAGDAVETP----------LP 199
Cdd:pfam00753  87 GLAASRLGLPGPPVVPLPPDVVLEEGDGILGGGLGLLVTHGPGHGPGHVVVYYGGGKVLFTGDLLFAGeigrldlplgGL 166

                         170       180       190
                  ....*....|....*....|....*....|
gi 51857303   200 TLSESGHIRAWAGALRKWSQAGLKHVVPGH 229
Cdd:pfam00753 167 LVLHPSSAESSLESLLKLAKLKAAVIVPGH 196
arylsulfatase_Sdsa1-like_MBL-fold cd07710
Pseudomonas aeruginosa arylsulfatase SdsA1, Pseudomonas sp. DSM6611 arylsulfatase Pisa1, and ...
 69-232 2.56e-14

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: 70.99  E-value: 2.56e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51857303  69 VVVDTLIRPADMA-------------PFAGatlVIYTHFDWDHCWGTAAF------PGVPVIGHQ-----LTRERLLA-- 122
Cdd:cd07710  30 IIIDTLESAEAAKaalelfrkhtgdkPVKA---IIYTHSHPDHFGGAGGFveeedsGKVPIIAPEgfmeeAVSENVLAgn 106

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51857303 123 --------------PEPGEFLERMRAEKPAHFEGSQIIPPDVTF-RDRLDIDAGGLTLELHHLPGHTADSVVVHVPELGL 187
Cdd:cd07710 107 amsrraayqfgallPKGEKGQVGAGLGPGLSTGTVGFIPPTITItETGETLTIDGVELEFQHAPGEAPDEMMVWLPDYKV 186

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 51857303 188 LLAGD-AVETpLPTL-----SESGHIRAWAGALRKWSQAGLKHVVPGHGRP 232
Cdd:cd07710 187 LFCADnVYHT-FPNLytlrgAKYRDALAWAKSLDEAISLKAEVLFPSHTWP 236
metallo-hydrolase-like_MBL-fold cd07739
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 50-229 1.11e-13

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: 293825 [Multi-domain]  Cd Length: 201  Bit Score: 68.30  E-value: 1.11e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51857303  50 PGSSDFPVTAAQVTGQRHRVVVDTLIRPADMAPFA------GATLV-IY-THFDWDHCWGT----AAFPGVPVIGHQLTR 117
Cdd:cd07739   9 PEISSFPVTSTLIYGETEAVLVDAQFTRADAERLAdwikasGKTLTtIYiTHGHPDHYFGLevllEAFPDAKVVATPAVV 88

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51857303 118 ERL---LAPEPGEFLERMRAEKPAHfegsqIIPPDVTFRDRLDIDagGLTLELHHLP-GHTADSVVVHVPELGLLLAGDA 193
Cdd:cd07739  89 AHIkaqLEPKLAFWGPLLGGNAPAR-----LVVPEPLDGDTLTLE--GHPLEIVGVGgGDTDDTTYLWIPSLKTVVAGDV 161

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 51857303 194 V---------ETPLPTLsesghIRAWAGALRKWSQAGLKHVVPGH 229
Cdd:cd07739 162 VyngvhvwlaDATTPEL-----RAAWLAALDKIEALNPETVVPGH 201
CcrA-like_MBL-B1 cd16302
Bacteroides fragilis CcrA and related metallo-beta-lactamases, subclass B1; MBL-fold ...
 62-238 1.25e-13

Bacteroides fragilis CcrA and related metallo-beta-lactamases, subclass B1; MBL-fold metallo-hydrolase domain; MBLs (class B of the Ambler beta-lactamase classification) are a diverse group of metallo-enzymes that are capable of catalyzing the hydrolysis of a wide range of beta-lactam antibiotics. MBLs have been divided into three subclasses B1, B2 and B3, based on sequence/structural relationships and substrates, with the B1 and B2 MBLs being most closely related to each other. This subgroup of MBLs belongs to the B1 subclass. B1 enzymes are most active with two zinc ions bound in the active site, and have a broad-spectrum substrate profile.


Pssm-ID: 293860  Cd Length: 212  Bit Score: 68.43  E-value: 1.25e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51857303  62 VTGQRHRVVVDT---------LIRPADMAPFAGATLVIYTHFDWDHCWGTAAFP--GVPVIGHQLTRErlLAPEPGefle 130
Cdd:cd16302  32 VINGGEAVVFDTptndsqseeLIDWIENSLKAKVKAVVPTHFHDDCLGGLKAFHrrGIPSYANQKTIA--LAKEKG---- 105

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51857303 131 rmraekpahfegsqIIPPDVTFRDRLDIDAGGLTLELHHL-PGHTADSVVVHVPELGLLLAG---DAVETPLPTLSESgH 206
Cdd:cd16302 106 --------------LPVPQHGFSDSLTLKLGGKKIVCRYFgEGHTKDNIVVYFPSEKVLFGGcmvKSLGAGKGNLEDA-N 170

                       170       180       190
                ....*....|....*....|....*....|....
gi 51857303 207 IRAWAGALRKWSQA--GLKHVVPGHGRPGGPELL 238
Cdd:cd16302 171 VEAWPKTVEKVKAKypDVKIVIPGHGKIGGSELL 204
yflN-like_MBL-fold cd07721
uncharacterized subgroup which includes Bacillus subtilis yflN; MBL-fold metallo hydrolase ...
 87-230 5.14e-13

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: 66.48  E-value: 5.14e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51857303  87 TLVIYTHFDWDHCwGTAAF----PGVPVIGHQL------TRERLLAPEPGEFLERMRAEKPAHfegsqIIPPDVTFRDRL 156
Cdd:cd07721  51 RRILLTHGHIDHI-GSLAAlkeaPGAPVYAHEReapyleGEKPYPPPVRLGLLGLLSPLLPVK-----PVPVDRTLEDGD 124

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51857303 157 DIDAGGlTLELHHLPGHTADSVVVHVPELGLLLAGDAVET-------PLPTLSESgHIRAWAgALRKWSQAGLKHVVPGH 229
Cdd:cd07721 125 TLDLAG-GLRVIHTPGHTPGHISLYLEEDGVLIAGDALVTvggelvpPPPPFTWD-MEEALE-SLRKLAELDPEVLAPGH 201


                .
gi 51857303 230 G 230
Cdd:cd07721 202 G 202
AHL_lactonase_MBL-fold cd07729
quorum-quenching N-acyl-homoserine lactonase, MBL-fold metallo-hydrolase domain; Acyl ...
 41-229 2.49e-12

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: 65.31  E-value: 2.49e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51857303  41 SVTLVTRPLPGSSDFPVTAAQVTGQRHRVVVDTLIRPADMAPFAGA----------------------------TLVIYT 92
Cdd:cd07729  16 SLFYYGRGPGEPIDLPVYAYLIEHPEGTILVDTGFHPDAADDPGGLelafppgvteeqtleeqlarlgldpediDYVILS 95

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51857303  93 HFDWDHCWGTAAFPGVPVIGHQltRErllapepgefLERMRAEKPAHFEGSQIIPPDVTFRDRLDID--------AGGLT 164
Cdd:cd07729  96 HLHFDHAGGLDLFPNATIIVQR--AE----------LEYATGPDPLAAGYYEDVLALDDDLPGGRVRlvdgdydlFPGVT 163

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 51857303 165 leLHHLPGHTA--DSVVVHVPELGLLLAGDAV-------ETPLPTLSESgHIRAWAG--ALRKWSQAGLKHVVPGH 229
Cdd:cd07729 164 --LIPTPGHTPghQSVLVRLPEGTVLLAGDAAytyenleEGRPPGINYD-PEAALASleRLKALAEREGARVIPGH 236
MBLAC2-like_MBL-fold cd07712
uncharacterized human metallo-beta-lactamase domain-containing protein 2 and related proteins; ...
 88-229 2.76e-11

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: 61.49  E-value: 2.76e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51857303  88 LVIYTHFDWDHCWGTAAFPGVPVigHQLTRERLLAPEPGEFLermrAEKPAHFEgsqiIPPDVTFRDRLD---IDAGGLT 164
Cdd:cd07712  45 LVVATHGHFDHIGGLHEFEEVYV--HPADAEILAAPDNFETL----TWDAATYS----VPPAGPTLPLRDgdvIDLGDRQ 114

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 51857303 165 LELHHLPGHTADSVVVHVPELGLLLAGDAVET-PLPTLSESGHIRAWAGALRKWS--QAGLKHVVPGH 229
Cdd:cd07712 115 LEVIHTPGHTPGSIALLDRANRLLFSGDVVYDgPLIMDLPHSDLDDYLASLEKLSklPDEFDKVLPGH 182
MBL-B1-B2-like cd07707
metallo-beta-lactamases; subclasses B1 and B2 and related proteins; MBL-fold metallo-hydrolase ...
 87-238 5.27e-11

metallo-beta-lactamases; subclasses B1 and B2 and related proteins; MBL-fold metallo-hydrolase domain; MBLs (class B of the Ambler beta-lactamase classification) are a diverse group of metallo-enzymes that are capable of catalyzing the hydrolysis of a wide range of beta-lactam antibiotics. MBLs have been divided into three subclasses B1, B2 and B3, based on sequence/structural relationships and substrates, with the B1 and B2 MBLs being most closely related to each other. Subclass B1 enzymes are most active with two zinc ions bound in the active site, and have a broad-spectrum substrate profile. B1 MBls include chromosomally-encoded MBLs such as Bacillus cereus BcII, Bacteroides fragilis CcrA, and Elizabethkingia meningoseptica (Chryseobacterium meningosepticum) BlaB and acquired MBLs including IMP-1, VIM-1, VIM-2, GIM-1, NDM-1 and FIM-1. B2 MBLs have a narrow substrate profile that includes carbapenems, and they are active with one zinc ion bound in the Asp-Cys-His site, binding of a second zinc ion in the modified 3H site (Asn-His-His) inhibits catalysis. B2 MBLs include Aeromonas hydrophyla CphA, Aeromonas veronii ImiS, and Serratia fonticola Sfh-I.


Pssm-ID: 293793 [Multi-domain]  Cd Length: 219  Bit Score: 61.41  E-value: 5.27e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51857303  87 TLVIYTHFDWDHCWGTAAFP--GVPVIGHQLTReRLLAPEPGEFLERMRAEKPaHFEGSQIIPPDVTFRdrLDIDAGGLT 164
Cdd:cd07707  60 TEVINTHFHTDRAGGNAYLKerGAKTVSTALTR-DLAKSEWAEIVAFTRKGLP-EYPDLGYELPDGVLD--GDFNLQFGK 135

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 51857303 165 LELHHL-PGHTADSVVVHVPELGLLLAGDAV-ETPLPTLSESgHIRAWAGALRKWSQ--AGLKHVVPGHGRPGGPELL 238
Cdd:cd07707 136 VEAFYPgPAHTPDNIVVYFPQENVLYGGCIIkETDLGNVADA-DVKEWPTSIERLKKryRNIKAVIPGHGEVGGPELL 212
TTHA1429-like_MBL-fold cd07725
uncharacterized Thermus thermophilus TTHA1429 and related proteins; MBL-fold metallo hydrolase ...
 145-232 2.32e-10

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: 58.85  E-value: 2.32e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51857303 145 IIPPDVTFRDRLDIDAGGLTLELHHLPGHTADSVVVHVPELGLLLAGDAV---ETPLPTL---SESGHIRAWAGALRKWS 218
Cdd:cd07725  84 YILDVTPVKDGDKIDLGGLRLKVIETPGHTPGHIVLYDEDRRELFVGDAVlpkITPNVSLwavRVEDPLGAYLESLDKLE 163

                        90
                ....*....|....
gi 51857303 219 QAGLKHVVPGHGRP 232
Cdd:cd07725 164 KLDVDLAYPGHGGP 177
BcII-like_MBL-B1 cd16304
Bacillus cereus Beta-lactamase 2 and related metallo-beta-lactamases, subclass B1; MBL-fold ...
 87-238 3.89e-10

Bacillus cereus Beta-lactamase 2 and related metallo-beta-lactamases, subclass B1; MBL-fold metallo-hydrolase domain; Bacillus cereus Beta-lactamase 2, also called BcII. MBLs (class B of the Ambler beta-lactamase classification) have been divided into three subclasses B1, B2 and B3, based on sequence/structural relationships and substrates, with the B1 and B2 MBLs being most closely related to each other. BcII is a chromosome-encoded B1 MBL. B1 enzymes are most active with two zinc ions bound in the active site, and have a broad-spectrum substrate profile.


Pssm-ID: 293862 [Multi-domain]  Cd Length: 212  Bit Score: 58.45  E-value: 3.89e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51857303  87 TLVIYTHFDWDHCWGTAAFP--GVPVIGHQLTRErlLAPEPGeflermraeKPAhfegsqiipPDVTFRDRLDIDAGGLT 164
Cdd:cd16304  65 TLAIVTHAHDDRIGGIKALQkrGIPVYSTKLTAQ--LAKKQG---------YPS---------PDGILKDDTTLKFGNTK 124

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51857303 165 LELHHL-PGHTADSVVVHVPELGLLLAGDAVETP----LPTLSESgHIRAWAGALRKWSQ--AGLKHVVPGHGRPGGPEL 237
Cdd:cd16304 125 IETFYPgEGHTADNIVVWLPQSKILFGGCLVKSLeakdLGNTADA-NLKEWPTSIRNVLKryPNAEIVVPGHGEWGDKQL 203


                .
gi 51857303 238 L 238
Cdd:cd16304 204 L 204
MBL-B1 cd16285
metallo-beta-lactamases, subclass B1; MBL-fold metallo-hydrolase domain; MBLs (class B of the ...
 69-238 7.13e-10

metallo-beta-lactamases, subclass B1; MBL-fold metallo-hydrolase domain; MBLs (class B of the Ambler beta-lactamase classification) are a diverse group of metallo-enzymes that are capable of catalyzing the hydrolysis of a wide range of beta-lactam antibiotics. MBLs have been divided into three subclasses B1, B2 and B3, based on sequence/structural relationships and substrates, with the B1 and B2 MBLs being most closely related to each other. Subclass B1 enzymes are most active with two zinc ions bound in the active site, and have a broad-spectrum substrate profile. Includes chromosomally-encoded MBLs such as Bacillus cereus BcII, Bacteroides fragilis CcrA, and Elizabethkingia meningoseptica (Chryseobacterium meningosepticum) BlaB and acquired MBLs including IMP-1, VIM-1, VIM-2, GIM-1, NDM-1 and FIM-1.


Pssm-ID: 293843 [Multi-domain]  Cd Length: 210  Bit Score: 57.68  E-value: 7.13e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51857303  69 VVVDTLIRPADMAPF---------AGATLVIYTHFDWDHCWGTAAF--PGVPVIGHQLTRErLLAPEPGEFlermraekp 137
Cdd:cd16285  38 VLIDTPWTEAQTATLldwiekklgKPVTAAISTHSHDDRTGGIKALnaRGIPTYATALTNE-LAKKEGKPV--------- 107

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51857303 138 ahfegsqiipPDVTFRDRLDIDAGglTLELHHL-PGHTADSVVVHVPELGLLLAGDAVE----TPLPTLSESgHIRAWAG 212
Cdd:cd16285 108 ----------PTHSLKGALTLGFG--PLEVFYPgPGHTPDNIVVWLPKSKILFGGCLVKsasaTSLGNVGDA-DVEAWPK 174

                       170       180       190
                ....*....|....*....|....*....|
gi 51857303 213 A----LRKWSQAglKHVVPGHGRPGGPELL 238
Cdd:cd16285 175 SienlKAKYPEA--RMVVPGHGAPGGTELL 202
SPM-1-like_MBL-B1-B2-like cd16286
Pseudomonas areoginosa SPM-1 and related metallo-beta-lactamases, subclasses B1 and B2 like; ...
 90-238 8.24e-10

Pseudomonas areoginosa SPM-1 and related metallo-beta-lactamases, subclasses B1 and B2 like; MBL-fold metallo-hydrolase domain; SPM-1 was first identified in a Pseudomonas aeruginosa strain from a paediatric leukaemia patient and is a major clinical problem. MBLs (class B of the Ambler beta-lactamase classification) have been divided into three subclasses B1, B2 and B3, based on sequence/structural relationships and substrates, with the B1 and B2 MBLs are most closely related to each other. SPM-1 appears to be a hybrid B1/B2 MBL.


Pssm-ID: 293844 [Multi-domain]  Cd Length: 236  Bit Score: 57.93  E-value: 8.24e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51857303  90 IYTHFDWDHCWGTAAFP--GVPVIGHQLTRERLLapEPGEFLERMRAEK------PAHFEGSQIIPPDVTF--RDRLDID 159
Cdd:cd16286  70 INTHFHLDGTGGNEALKkrGIPTWGSDLTKQLLL--ERGKADRIKAAEFlknedlKRRIESSPPVPPDNVFdlKEGKVFS 147

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51857303 160 AGGLTLELHHL-PGHTADSVVVHVPELGLLLAGDAVETPLPTLSES-GHIRAWAGALRKWSQAGLKHVVPGHGRPGGPEL 237
Cdd:cd16286 148 FGNELVEVSFPgPAHAPDNVVVYFPERKILFGGCMIKPGKELGNLGdANMKAWPDSVRRLKKFDAKIVIPGHGERGDPGM 227


                .
gi 51857303 238 L 238
Cdd:cd16286 228 V 228
TTHA1623-like_MBL-fold cd16322
uncharacterized Thermus thermophilus TTHA1623 and related proteins; MBL-fold metallo hydrolase ...
 69-192 1.04e-09

uncharacterized Thermus thermophilus TTHA1623 and related proteins; MBL-fold metallo hydrolase domain; Includes the MBL-fold metallo hydrolase domain of uncharacterized Thermus thermophilus TTHA1623 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. This family includes homologs present in a wide range of bacteria and archaea and some eukaryota. Members of the MBL-fold metallo-hydrolase superfamily exhibit a variety of active site metallo-chemistry, TTHA1623 exhibiting a uniquely shaped putative substrate-binding pocket with a glyoxalase II-type metal-coordination mode.


Pssm-ID: 293877 [Multi-domain]  Cd Length: 204  Bit Score: 57.36  E-value: 1.04e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51857303  69 VVVDTLIRPADMAPFAGATL-----VIYTHFDWDHCWGTAAF---PGVPVIGHQLTRERLLAPEPGEFLERMRAEKPahf 140
Cdd:cd16322  25 VLVDPGDESEKLLARFGTTGltllyILLTHAHFDHVGGVADLrrhPGAPVYLHPDDLPLYEAADLGAKAFGLGIEPL--- 101

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|..
gi 51857303 141 egsqiIPPDVTFRDRLDIDAGGLTLELHHLPGHTADSVVVHVPELGLLLAGD 192
Cdd:cd16322 102 -----PPPDRLLEDGQTLTLGGLEFKVLHTPGHSPGHVCFYVEEEGLLFSGD 148
metallo-hydrolase-like_MBL-fold cd16278
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 87-232 3.22e-09

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: 55.58  E-value: 3.22e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51857303  87 TLVIYTHFDWDHCWGTAAF---PGVPVIGhqltrerllapepgeFLERMRAEKPAHFegsqiiPPDVTFRDRLDIDAGGL 163
Cdd:cd16278  55 SAILVTHTHRDHSPGAARLaerTGAPVRA---------------FGPHRAGGQDTDF------APDRPLADGEVIEGGGL 113

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 51857303 164 TLELHHLPGHTADSVVVHVPELGLLLAGDAVetplptLSES--------GHIRAWAGALRKWSQAGLKHVVPGHGRP 232
Cdd:cd16278 114 RLTVLHTPGHTSDHLCFALEDEGALFTGDHV------MGWSttviappdGDLGDYLASLERLLALDDRLLLPGHGPP 184
hydroxyacylglutathione_hydrolase_MBL-fold cd07723
hydroxyacylglutathione hydrolase, MBL-fold metallo-hydrolase domain; hydroxyacylglutathione ...
 66-192 7.11e-09

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: 54.00  E-value: 7.11e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51857303  66 RHRVVVDtlirPADMAPFA------GATL--VIYTHFDWDHCWGTAA----FPGVPVIGHQLTRerllapepgeflermr 133
Cdd:cd07723  20 GEAAVVD----PGEAEPVLaaleknGLTLtaILTTHHHWDHTGGNAElkalFPDAPVYGPAEDR---------------- 79

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 51857303 134 aekpahfegsqIIPPDVTFRDRLDIDAGGLTLELHHLPGHTADSVVVHVPELGLLLAGD 192
Cdd:cd07723  80 -----------IPGLDHPVKDGDEIKLGGLEVKVLHTPGHTLGHICYYVPDEPALFTGD 127
metallo-hydrolase-like_MBL-fold cd07730
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 89-210 2.94e-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. Some members of this subgroup are annotated as GumP protein.


Pssm-ID: 293816 [Multi-domain]  Cd Length: 250  Bit Score: 50.73  E-value: 2.94e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51857303  89 VIYTHFDWDHCWGTAAFPGVPVIGHqltrerllapepGEFLERMRAEKPAHFEGSQIIPPDVTFRDRLDIDAGGL----- 163
Cdd:cd07730  87 VILSHLHWDHIGGLSDFPNARLIVG------------PGAKEALRPPGYPSGFLPELLPSDFEGRLVRWEEDDFLwvplg 154

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 51857303 164 ------------TLELHHLPGHTADSVVVHVPELG---LLLAGDAVETPLPTLSESGHIRAW 210
Cdd:cd07730 155 pfpraldlfgdgSLYLVDLPGHAPGHLGLLARTTSgtwVFLAGDACHHRIGLLRPSPLLPLP 216
LACTB2-like_MBL-fold cd07722
uncharacterized subgroup which includes human lactamase beta 2 and related proteins; MBL-fold ...
 89-230 4.26e-07

uncharacterized subgroup which includes human lactamase beta 2 and related proteins; MBL-fold metallo hydrolase domain; Includes functionally uncharacterized human lactamase beta 2. 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: 293808 [Multi-domain]  Cd Length: 188  Bit Score: 49.45  E-value: 4.26e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51857303  89 VIYTHFDWDHcWGtaafpGVPVIghqltRERLLAPEPgeflermRAEK-PAHFEGSQIIPPDVTFRDRLD---IDAGGLT 164
Cdd:cd07722  60 ILLTHWHHDH-VG-----GLPDV-----LDLLRGPSP-------RVYKfPRPEEDEDPDEDGGDIHDLQDgqvFKVEGAT 121

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51857303 165 LELHHLPGHTADSVVVHVPELGLLLAGDAVetplptLSES----GHIRAWAGALRKWSQAGLKHVVPGHG 230
Cdd:cd07722 122 LRVIHTPGHTTDHVCFLLEEENALFTGDCV------LGHGtavfEDLAAYMASLKKLLSLGPGRIYPGHG 185
VIM_type_MBL-B1 cd16303
VIM-type metallo-beta-lactamases, subclass B1; MBL-fold metallo-hydrolase domain; VIM (Verona ...
 171-238 4.37e-06

VIM-type metallo-beta-lactamases, subclass B1; MBL-fold metallo-hydrolase domain; VIM (Verona integron-encoded metallo-beta-lactamase)-type MBLs are integron-associated and are widely distributed acquired MBLs. MBLs (class B of the Ambler beta-lactamase classification) have been divided into three subclasses B1, B2 and B3, based on sequence/structural relationships and substrates, with the B1 and B2 MBLs being most closely related to each other. This subgroup of VIM-type MBLs belongs to the B1 subclass. B1 enzymes are most active with two zinc ions bound in the active site, and have a broad-spectrum substrate profile.


Pssm-ID: 293861 [Multi-domain]  Cd Length: 218  Bit Score: 46.78  E-value: 4.37e-06
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 51857303 171 PGHTADSVVVHVPELGLLLAGDAV----ETPLPTLSEsGHIRAWAGALRKWSQ--AGLKHVVPGHGRPGGPELL 238
Cdd:cd16303 136 AAHSTDNLVVYVPSARVLYGGCAVrelsSTSAGNVAD-ADLAEWPTSIERIQKhyPEAEFVIPGHGLPGGLDLL 208
NDM_FIM-like_MBL-B1 cd16300
NDM-1, FIM-1 and related metallo-beta-lactamases, subclass B1; MBL-fold metallo-hydrolase ...
 87-243 7.25e-06

NDM-1, FIM-1 and related metallo-beta-lactamases, subclass B1; MBL-fold metallo-hydrolase domain; Includes the ISCR-mediated MBLs NDM-1 (NDM (New Delhi metallo-beta-lactamase) and FIM-1 (Florence imipenemase). MBLs (class B of the Ambler beta-lactamase classification) are a diverse group of metallo-enzymes that are capable of catalyzing the hydrolysis of a wide range of beta-lactam antibiotics. MBLs have been divided into three subclasses B1, B2 and B3, based on sequence/structural relationships and substrates, with the B1 and B2 MBLs being most closely related to each other. This subgroup of MBLs belongs to the B1 subclass. B1 enzymes are most active with two zinc ions bound in the active site, and have a broad-spectrum substrate profile.


Pssm-ID: 293858  Cd Length: 214  Bit Score: 45.97  E-value: 7.25e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51857303  87 TLVIYTHFDWDHCWGTAAF--PGVPVIGHQLTRErlLAPEPGefLErmraekPAhfegsqiippdvtfRDRLDIDAGGLT 164
Cdd:cd16300  66 RLAVVTHAHQDKMGGMDALhaAGIATYANALSNQ--LAPQEG--LV------PA--------------QHSLTFAAEPST 121

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51857303 165 LELHHL------PGHTADSVVVHVPELGLLLAG----DAVETPLPTLSESgHIRAWAGALRKWSQA--GLKHVVPGHGRP 232
Cdd:cd16300 122 APNFPLkvfypgPGHTRDNIVVGIDGTGIAFGGclirPSKATSLGNLADA-DTEHWAASARAFGAAfpDASMIVPSHGAP 200

                       170
                ....*....|.
gi 51857303 233 GGPELLAANAA 243
Cdd:cd16300 201 DGRAAITHTAR 211
metallo-hydrolase-like_MBL-fold cd07742
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 89-193 8.03e-06

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: 293828 [Multi-domain]  Cd Length: 249  Bit Score: 46.46  E-value: 8.03e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51857303  89 VIYTHFDWDHCWGTAAFPGVPVigHQLTRERLLAPEPGEFLERMRAEkPAHFEGsqiiPPDVT-----------FRDRLD 157
Cdd:cd07742  84 IVLTHLDLDHAGGLADFPHATV--HVHAAELDAATSPRTRYERRRYR-PQQLAH----GPWWVtyaaggerwfgFEAVRP 156

                        90       100       110
                ....*....|....*....|....*....|....*...
gi 51857303 158 IDAGGLTLELHHLPGHTAD--SVVVHVPELGLLLAGDA 193
Cdd:cd07742 157 LDGLPPEILLVPLPGHTRGhcGVAVRTGDRWLLHAGDA 194
IMP_DIM-like_MBL-B1 cd16301
IMP-1, DIM-1, GIM-1, SIM-1, TMB-1 and related metallo-beta-lactamases, subclass B1; MBL-fold ...
 171-238 9.16e-06

IMP-1, DIM-1, GIM-1, SIM-1, TMB-1 and related metallo-beta-lactamases, subclass B1; MBL-fold metallo-hydrolase domain; Includes the acquired MBLs IMP-1(a beta-lactamase that is active on imipenem), DIM-1 (Dutch imipenemase), GIM-1 (German imipenemase), KHM-1 (Kyorin Health Science MBL 1), SIM-1 (Seoul imipenemase), and TMB-1 (Tripoli metallo-beta-lactamase). IMP-1, DIM-1, GIM-1, SIM-1, and TMB-1 are Class 1 integron-mediated MBLs, KMH-1 is plasmid-mediated. MBLs (class B of the Ambler beta-lactamase classification) are a diverse group of metallo-enzymes that are capable of catalyzing the hydrolysis of a wide range of beta-lactam antibiotics. MBLs have been divided into three subclasses B1, B2 and B3, based on sequence/structural relationships and substrates, with the B1 and B2 MBLs being most closely related to each other. This subgroup of acquired MBLs belongs to the B1 subclass. B1 enzymes are most active with two zinc ions bound in the active site, and have a broad-spectrum substrate profile.


Pssm-ID: 293859 [Multi-domain]  Cd Length: 215  Bit Score: 45.74  E-value: 9.16e-06
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 51857303 171 PGHTADSVVVHVPELGLLLAGDAVEtPLPTLS----ESGHIRAWAGA----LRKWSQAglKHVVPGHGRPGGPELL 238
Cdd:cd16301 133 AGHTKDNLVVWLPKEKILFGGCLVK-SLESKGlgntGDASISQWPASaqkvLSKYPNA--KLVVPGHGKVGDVSLL 205
YmaE-like_MBL-fold cd07727
uncharacterized subgroup which includes Bacillus subtilis YmaE and related proteins; MBL-fold ...
 130-232 1.33e-05

uncharacterized subgroup which includes Bacillus subtilis YmaE and related proteins; MBL-fold metallo hydrolase domain; Includes the uncharacterized Bacillus subtilis YmaE and Nostoc all1228 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. 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: 293813 [Multi-domain]  Cd Length: 181  Bit Score: 44.88  E-value: 1.33e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51857303 130 ERMRAEKPAHFEGSqiippdvtfrDRLDIDAGgltLELHHLPGHTADSVVVHVPELGLLLAGD--AVETPLPTLSESGH- 206
Cdd:cd07727  82 AVTRPDEVIVLWGG----------DPWELDPD---LTLIPVPGHTRGSVVLLYKEKGVLFTGDhlAWSRRRGWLSAFRYv 148

                        90       100       110
                ....*....|....*....|....*....|
gi 51857303 207 ----IRAWAGALRKWSQAGLKHVVPGHGRP 232
Cdd:cd07727 149 cwysWPEQAESVERLADLDFEWVLPGHGRR 178
metallo-hydrolase-like_MBL-fold cd07743
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 89-194 3.43e-04

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: 40.98  E-value: 3.43e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51857303  89 VIYTHFDWDHCWGTAAF---PGVPVIGHQL----TRERLL-------APEPGEFLERMRAEKPAHFEgsQIIPPDvtfrd 154
Cdd:cd07743  49 IINTHSHADHIGGNAYLqkkTGCKVYAPKIekafIENPLLepsylggAYPPKELRNKFLMAKPSKVD--DIIEEG----- 121

                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 51857303 155 rlDIDAGGLTLELHHLPGHTADSVVVHVPElGLLLAGDAV 194
Cdd:cd07743 122 --ELELGGVGLEIIPLPGHSFGQIGILTPD-GVLFAGDAL 158
POD-like_MBL-fold cd07724
ETHE1 (PDO type I), persulfide dioxygenase A (PDOA, PDO type II) and related proteins; ...
 148-194 5.30e-04

ETHE1 (PDO type I), persulfide dioxygenase A (PDOA, PDO type II) and related proteins; MBL-fold metallo-hydrolase domain; Persulfide dioxygenase (PDO, also known as sulfur dioxygenase, SDO, EC 1.13.11.18) is a non-heme iron-dependent oxygenase which catalyzes the oxidation of glutathione persulfide to glutathione and persulfite in the mitochondria. Mutations in ethe1 (the human PDO gene) are responsible for a rare autosomal recessive metabolic disorder called ethylmalonic encephalopathy. Arabidopsis thaliana ETHE1 is essential for embryo and endosperm development. Bacterial ETHE1-type PDOs are also called Type 1 PDOs. Type II PDOs (also called PDOAs), are mainly proteobacterial. 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: 293810 [Multi-domain]  Cd Length: 177  Bit Score: 40.08  E-value: 5.30e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*..
gi 51857303 148 PDVTFRDRLDIDAGGLTLELHHLPGHTADSVVVHVPELGLLLAGDAV 194
Cdd:cd07724  87 FDRLLKDGDVLELGNLTLEVLHTPGHTPESVSYLVGDPDAVFTGDTL 133
YcbL-like_MBL-fold cd07737
Salmonella enterica serovar typhimurium YcbL and related proteins; MBL-fold metallo hydrolase ...
 89-192 5.66e-04

Salmonella enterica serovar typhimurium YcbL and related proteins; MBL-fold metallo hydrolase domain; This subgroup includes Salmonella enterica serovar typhimurium YcbL which has type II hydroxyacylglutathione hydrolase (EC 3.1.2.6, also known as glyoxalase II) activity, and has a single metal ion binding site, and Thermus thermophilus TTHA1623 which does not have GLX2 activity and has two metal ion binding sites with a glyoxalase II-type metal coordination. 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: 293823 [Multi-domain]  Cd Length: 190  Bit Score: 40.23  E-value: 5.66e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51857303  89 VIYTHFDWDHCWGTAAFP---GVPVIGHQLTRERLLA--PEPGEFLermraekpaHFEGSQIIPPDVTFRDRLDIDAGGL 163
Cdd:cd07737  50 ILLTHGHLDHVGGAAELAehyGVPIIGPHKEDKFLLEnlPEQSQMF---------GFPPAEAFTPDRWLEEGDTVTVGNL 120

                        90       100
                ....*....|....*....|....*....
gi 51857303 164 TLELHHLPGHTADSVVVHVPELGLLLAGD 192
Cdd:cd07737 121 TLEVLHCPGHTPGHVVFFNRESKLAIVGD 149
IND_BlaB-like_MBL-B1 cd16299
IND1, IND2, BlaB-1 and related metallo-beta-lactamases, subclass B1; MBL-fold ...
 89-229 7.51e-03

IND1, IND2, BlaB-1 and related metallo-beta-lactamases, subclass B1; MBL-fold metallo-hydrolase domain; Includes the chromosome-encoded metallo-beta-lactamases Chryseobacterium indologenes IND-1, IND-2, and IND-7, Elizabethkingia meningoseptica (Chryseobacterium meningosepticum) BlaB, Chryseobacterium gleum CGB-1, and Empedobacter brevis EBR-1. MBLs (class B of the Ambler beta-lactamase classification) are a diverse group of metallo-enzymes that are capable of catalyzing the hydrolysis of a wide range of beta-lactam antibiotics. MBLs have been divided into three subclasses B1, B2 and B3, based on sequence/structural relationships and substrates, with the B1 and B2 MBLs being most closely related to each other. This subgroup of MBLs belongs to the B1 subclass. B1 enzymes are most active with two zinc ions bound in the active site, and have a broad-spectrum substrate profile.


Pssm-ID: 293857  Cd Length: 212  Bit Score: 37.04  E-value: 7.51e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51857303  89 VIYTHFDWDHCWGTAAFP--GVPVIGHQLTRERLLAPEPGEFLERMRAEKPAHFEGSQIIppdvtfrdrldIDAGGltle 166
Cdd:cd16299  67 VIATHSHEDRAGGLGYFNkiGIPTYATAMTNSILKKENKPQATYLIETDKTYKIGGEKFV-----------VYFFG---- 131

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 51857303 167 lhhlPGHTADSVVVHVPELGLLLAG----DAVETPLPTLSEsGHIRAWAGALRKWSQ--AGLKHVVPGH 229
Cdd:cd16299 132 ----EGHTADNVVVWFPKEKVLDGGclikSAEATDLGYIGE-ANVKEWPKTIHKLKQkfKKAKVVIPGH 195
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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