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Conserved domains on  [gi|495404195|ref|WP_008128894|]
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MBL fold metallo-hydrolase [Phyllobacterium sp. YR531]

Protein Classification

MBL fold metallo-hydrolase( domain architecture ID 14427476)

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 cd16278
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 22-218 1.44e-83

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: 249.33  E-value: 1.44e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495404195  22 HVQRITVNNPSPFTFYGTNSYLVGR-DTLALIDPGPLDDSHKATLLQAIAGRPVSHIFVSHTHRDHSPLATVLKDELGAL 100
Cdd:cd16278    1 GVRRVLAPNPSPMTLDGTNTYLLGApDGVVVIDPGPDDPAHLDALLAALGGGRVSAILVTHTHRDHSPGAARLAERTGAP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495404195 101 LVAEGPHRAArplhtgevnlldaSADTDFVPDIIAADNTVINGDGWALRTIHTPGHTANHAVFALENTGILFSADHIMAW 180
Cdd:cd16278   81 VRAFGPHRAG-------------GQDTDFAPDRPLADGEVIEGGGLRLTVLHTPGHTSDHLCFALEDEGALFTGDHVMGW 147

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 495404195 181 STSIVAPPDGSMSDYMASLDVMLELDSRVYFPGHGGAV 218
Cdd:cd16278  148 STTVIAPPDGDLGDYLASLERLLALDDRLLLPGHGPPI 185
BLACT_WH pfam17778
Beta-lactamase associated winged helix domain; This winged helix domain is found at the ...
 249-290 2.08e-09

Beta-lactamase associated winged helix domain; This winged helix domain is found at the C-terminus of some beta lactamase enzymes.


:

Pssm-ID: 407650  Cd Length: 46  Bit Score: 52.23  E-value: 2.08e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 495404195  249 TIATMVAAIYRDTDPRLHGAAALSVLAHLEDMVARGLVQTDG 290
Cdd:pfam17778   1 TAMELVKVIYKDVPESLHPAAERGVLAHLEKLEAEGKVVREG 42
 
Name Accession Description Interval E-value
metallo-hydrolase-like_MBL-fold cd16278
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 22-218 1.44e-83

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: 249.33  E-value: 1.44e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495404195  22 HVQRITVNNPSPFTFYGTNSYLVGR-DTLALIDPGPLDDSHKATLLQAIAGRPVSHIFVSHTHRDHSPLATVLKDELGAL 100
Cdd:cd16278    1 GVRRVLAPNPSPMTLDGTNTYLLGApDGVVVIDPGPDDPAHLDALLAALGGGRVSAILVTHTHRDHSPGAARLAERTGAP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495404195 101 LVAEGPHRAArplhtgevnlldaSADTDFVPDIIAADNTVINGDGWALRTIHTPGHTANHAVFALENTGILFSADHIMAW 180
Cdd:cd16278   81 VRAFGPHRAG-------------GQDTDFAPDRPLADGEVIEGGGLRLTVLHTPGHTSDHLCFALEDEGALFTGDHVMGW 147

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 495404195 181 STSIVAPPDGSMSDYMASLDVMLELDSRVYFPGHGGAV 218
Cdd:cd16278  148 STTVIAPPDGDLGDYLASLERLLALDDRLLLPGHGPPI 185
GloB COG0491
Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General ...
 28-238 1.34e-37

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: 132.51  E-value: 1.34e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495404195  28 VNNPSPFTFYGTNSYLV-GRDTLALIDPGpLDDSHKATLLQAIA--GRPVSHIFVSHTHRDHSPLATVLKDELGALLVAe 104
Cdd:COG0491    4 LPGGTPGAGLGVNSYLIvGGDGAVLIDTG-LGPADAEALLAALAalGLDIKAVLLTHLHPDHVGGLAALAEAFGAPVYA- 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495404195 105 gpHRAARPLHTGEVNLlDASADTDFVPDIIAADNTVINGDGWALRTIHTPGHTANHAVFALENTGILFSADHIMAWSTSI 184
Cdd:COG0491   82 --HAAEAEALEAPAAG-ALFGREPVPPDRTLEDGDTLELGGPGLEVIHTPGHTPGHVSFYVPDEKVLFTGDALFSGGVGR 158

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 495404195 185 VAPPDGSMSDYMASLDVMLELDSRVYFPGHGGAVTKpKAFVRGLRGHRKMRERA 238
Cdd:COG0491  159 PDLPDGDLAQWLASLERLLALPPDLVIPGHGPPTTA-EAIDYLEELLAALGERA 211
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 40-214 6.13e-26

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: 101.09  E-value: 6.13e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495404195    40 NSYLV-GRDTLALIDPGPLDDSHKATLLQAIAGRPVSHIFVSHTHRDHSPLATVLKDELGALLVAegPHRAARPLHTGEV 118
Cdd:smart00849   1 NSYLVrDDGGAILIDTGPGEAEDLLAELKKLGPKKIDAIILTHGHPDHIGGLPELLEAPGAPVYA--PEGTAELLKDLLA 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495404195   119 NLLDASA-DTDFVPDIIAADNTVINGDGWALRTIHTPGHTANHAVFALENTGILFSADHIMA--WSTSIVAPPDGSMSDY 195
Cdd:smart00849  79 LLGELGAeAEPAPPDRTLKDGDELDLGGGELEVIHTPGHTPGSIVLYLPEGKILFTGDLLFAggDGRTLVDGGDAAASDA 158

                          170
                   ....*....|....*....
gi 495404195   196 MASLDVMLELDSRVYFPGH 214
Cdd:smart00849 159 LESLLKLLKLLPKLVVPGH 177
Lactamase_B pfam00753
Metallo-beta-lactamase superfamily;
35-214 2.95e-14

Metallo-beta-lactamase superfamily;


Pssm-ID: 425851 [Multi-domain]  Cd Length: 196  Bit Score: 70.09  E-value: 2.95e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495404195   35 TFYGTNSYLV-GRDTLALIDPGPLDDSHKATLLQAIA--GRPVSHIFVSHTHRDHSPLATVLKDELGALLVAEgPHRAAR 111
Cdd:pfam00753   2 GPGQVNSYLIeGGGGAVLIDTGGSAEAALLLLLAALGlgPKDIDAVILTHGHFDHIGGLGELAEATDVPVIVV-AEEARE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495404195  112 PLHTGEVNLLDASADTDFVPDIIAADNTVINGD-----GWALRTIHTPGHTANHAVFALENTGILFSADHIMAWSTSIVA 186
Cdd:pfam00753  81 LLDEELGLAASRLGLPGPPVVPLPPDVVLEEGDgilggGLGLLVTHGPGHGPGHVVVYYGGGKVLFTGDLLFAGEIGRLD 160

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 495404195  187 PP--------DGSMSDYMASLDVMLELDSRVYFPGH 214
Cdd:pfam00753 161 LPlggllvlhPSSAESSLESLLKLAKLKAAVIVPGH 196
BLACT_WH pfam17778
Beta-lactamase associated winged helix domain; This winged helix domain is found at the ...
 249-290 2.08e-09

Beta-lactamase associated winged helix domain; This winged helix domain is found at the C-terminus of some beta lactamase enzymes.


Pssm-ID: 407650  Cd Length: 46  Bit Score: 52.23  E-value: 2.08e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 495404195  249 TIATMVAAIYRDTDPRLHGAAALSVLAHLEDMVARGLVQTDG 290
Cdd:pfam17778   1 TAMELVKVIYKDVPESLHPAAERGVLAHLEKLEAEGKVVREG 42
PLN02398 PLN02398
hydroxyacylglutathione hydrolase
 55-210 3.50e-06

hydroxyacylglutathione hydrolase


Pssm-ID: 215223 [Multi-domain]  Cd Length: 329  Bit Score: 47.92  E-value: 3.50e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495404195  55 GPLDDSHKATLLQAIA--GRPVSHIFVSHTHRDHSPLATVLKDELGALLVAEGphraarplhtgevnlldasADTDFVPD 132
Cdd:PLN02398 101 GVVDPSEAVPVIDALSrkNRNLTYILNTHHHYDHTGGNLELKARYGAKVIGSA-------------------VDKDRIPG 161

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495404195 133 IiaaDNTVINGDGW-----ALRTIHTPGHTANHAVFALENTGILFSADHIMAWSTSIVAppDGSMSDYMASLDVMLEL-- 205
Cdd:PLN02398 162 I---DIVLKDGDKWmfaghEVLVMETPGHTRGHISFYFPGSGAIFTGDTLFSLSCGKLF--EGTPEQMLSSLQKIISLpd 236


                 ....*
gi 495404195 206 DSRVY 210
Cdd:PLN02398 237 DTNIY 241
 
Name Accession Description Interval E-value
metallo-hydrolase-like_MBL-fold cd16278
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 22-218 1.44e-83

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: 249.33  E-value: 1.44e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495404195  22 HVQRITVNNPSPFTFYGTNSYLVGR-DTLALIDPGPLDDSHKATLLQAIAGRPVSHIFVSHTHRDHSPLATVLKDELGAL 100
Cdd:cd16278    1 GVRRVLAPNPSPMTLDGTNTYLLGApDGVVVIDPGPDDPAHLDALLAALGGGRVSAILVTHTHRDHSPGAARLAERTGAP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495404195 101 LVAEGPHRAArplhtgevnlldaSADTDFVPDIIAADNTVINGDGWALRTIHTPGHTANHAVFALENTGILFSADHIMAW 180
Cdd:cd16278   81 VRAFGPHRAG-------------GQDTDFAPDRPLADGEVIEGGGLRLTVLHTPGHTSDHLCFALEDEGALFTGDHVMGW 147

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 495404195 181 STSIVAPPDGSMSDYMASLDVMLELDSRVYFPGHGGAV 218
Cdd:cd16278  148 STTVIAPPDGDLGDYLASLERLLALDDRLLLPGHGPPI 185
GloB COG0491
Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General ...
 28-238 1.34e-37

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: 132.51  E-value: 1.34e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495404195  28 VNNPSPFTFYGTNSYLV-GRDTLALIDPGpLDDSHKATLLQAIA--GRPVSHIFVSHTHRDHSPLATVLKDELGALLVAe 104
Cdd:COG0491    4 LPGGTPGAGLGVNSYLIvGGDGAVLIDTG-LGPADAEALLAALAalGLDIKAVLLTHLHPDHVGGLAALAEAFGAPVYA- 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495404195 105 gpHRAARPLHTGEVNLlDASADTDFVPDIIAADNTVINGDGWALRTIHTPGHTANHAVFALENTGILFSADHIMAWSTSI 184
Cdd:COG0491   82 --HAAEAEALEAPAAG-ALFGREPVPPDRTLEDGDTLELGGPGLEVIHTPGHTPGHVSFYVPDEKVLFTGDALFSGGVGR 158

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 495404195 185 VAPPDGSMSDYMASLDVMLELDSRVYFPGHGGAVTKpKAFVRGLRGHRKMRERA 238
Cdd:COG0491  159 PDLPDGDLAQWLASLERLLALPPDLVIPGHGPPTTA-EAIDYLEELLAALGERA 211
LACTB2-like_MBL-fold cd07722
uncharacterized subgroup which includes human lactamase beta 2 and related proteins; MBL-fold ...
 23-215 2.19e-33

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: 120.72  E-value: 2.19e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495404195  23 VQRITVNNPSPFTFYGTNSYLVGR-DTLALIDPGPLDDSHKATLLQAIAG---RPVSHIFVSHTHRDHSP-LATVLKdel 97
Cdd:cd07722    2 VIRILGQNPGPFTLQGTNTYLVGTgKRRILIDTGEGRPSYIPLLKSVLDSegnATISDILLTHWHHDHVGgLPDVLD--- 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495404195  98 gaLLVAEGP--HRAARPLHTGEVNlldaSADTDFVPdiiAADNTVINGDGWALRTIHTPGHTANHAVFALENTGILFSAD 175
Cdd:cd07722   79 --LLRGPSPrvYKFPRPEEDEDPD----EDGGDIHD---LQDGQVFKVEGATLRVIHTPGHTTDHVCFLLEEENALFTGD 149

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 495404195 176 HIMAWSTSIVappdGSMSDYMASLDVMLELDSRVYFPGHG 215
Cdd:cd07722  150 CVLGHGTAVF----EDLAAYMASLKKLLSLGPGRIYPGHG 185
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 40-214 6.13e-26

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: 101.09  E-value: 6.13e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495404195    40 NSYLV-GRDTLALIDPGPLDDSHKATLLQAIAGRPVSHIFVSHTHRDHSPLATVLKDELGALLVAegPHRAARPLHTGEV 118
Cdd:smart00849   1 NSYLVrDDGGAILIDTGPGEAEDLLAELKKLGPKKIDAIILTHGHPDHIGGLPELLEAPGAPVYA--PEGTAELLKDLLA 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495404195   119 NLLDASA-DTDFVPDIIAADNTVINGDGWALRTIHTPGHTANHAVFALENTGILFSADHIMA--WSTSIVAPPDGSMSDY 195
Cdd:smart00849  79 LLGELGAeAEPAPPDRTLKDGDELDLGGGELEVIHTPGHTPGSIVLYLPEGKILFTGDLLFAggDGRTLVDGGDAAASDA 158

                          170
                   ....*....|....*....
gi 495404195   196 MASLDVMLELDSRVYFPGH 214
Cdd:smart00849 159 LESLLKLLKLLPKLVVPGH 177
metallo-hydrolase-like_MBL-fold cd06262
mainly hydrolytic enzymes and related proteins which carry out various biological functions; ...
 33-214 2.05e-23

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: 94.66  E-value: 2.05e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495404195  33 PFTFYGTNSYLVGRDT--LALIDPGpldDSHKATLLQAIA--GRPVSHIFVSHTHRDHSPLATVLKDELGALLVAegpHR 108
Cdd:cd06262    4 PVGPLQTNCYLVSDEEgeAILIDPG---AGALEKILEAIEelGLKIKAILLTHGHFDHIGGLAELKEAPGAPVYI---HE 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495404195 109 AARP-LHTGEVNLL--DASADTDFVPDIIAADNTVINGDGWALRTIHTPGHTANHAVFALENTGILFSADHIMAWSTSIV 185
Cdd:cd06262   78 ADAElLEDPELNLAffGGGPLPPPEPDILLEDGDTIELGGLELEVIHTPGHTPGSVCFYIEEEGVLFTGDTLFAGSIGRT 157

                        170       180       190
                 ....*....|....*....|....*....|..
gi 495404195 186 APPDGSMSDYMASLDVMLEL---DSRVYfPGH 214
Cdd:cd06262  158 DLPGGDPEQLIESIKKLLLLlpdDTVVY-PGH 188
TTHA1429-like_MBL-fold cd07725
uncharacterized Thermus thermophilus TTHA1429 and related proteins; MBL-fold metallo hydrolase ...
 31-223 3.51e-22

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: 91.21  E-value: 3.51e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495404195  31 PSPFTFYGTNSYLV-GRDTLALIDPGPLDDSHKATLLQAIAGRPVS-----HIFVSHTHRDHSPLATVLKDELGALLvae 104
Cdd:cd07725    7 PLPGPLGHVNVYLLrDGDETTLIDTGLATEEDAEALWEGLKELGLKpsdidRVLLTHHHPDHIGLAGKLQEKSGATV--- 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495404195 105 gphraarplhtgevnlldASADTDFVpdiiaADNTVINGDGWALRTIHTPGHTANHAVFALENTGILFSADHIMAWSTS- 183
Cdd:cd07725   84 ------------------YILDVTPV-----KDGDKIDLGGLRLKVIETPGHTPGHIVLYDEDRRELFVGDAVLPKITPn 140

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 495404195 184 -IVAPP--DGSMSDYMASLDVMLELDSRVYFPGHGGAVTKPKA 223
Cdd:cd07725  141 vSLWAVrvEDPLGAYLESLDKLEKLDVDLAYPGHGGPIKDPKA 183
TTHA1623-like_MBL-fold cd16322
uncharacterized Thermus thermophilus TTHA1623 and related proteins; MBL-fold metallo hydrolase ...
 37-219 1.69e-16

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: 76.23  E-value: 1.69e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495404195  37 YGTNSYLVGR---DTLALIDPGplDDSHKATLLQAIAGRPVSHIFVSHTHRDHSPLATVLKDELGALLVAegpHRAARPL 113
Cdd:cd16322    9 LQENTYLVADeggGEAVLVDPG--DESEKLLARFGTTGLTLLYILLTHAHFDHVGGVADLRRHPGAPVYL---HPDDLPL 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495404195 114 H---TGEVNLLDASADTDFVPDIIAADNTVINGDGWALRTIHTPGHTANHAVFALENTGILFSADHIMAWSTSIVAPPDG 190
Cdd:cd16322   84 YeaaDLGAKAFGLGIEPLPPPDRLLEDGQTLTLGGLEFKVLHTPGHSPGHVCFYVEEEGLLFSGDLLFQGSIGRTDLPGG 163

                        170       180       190
                 ....*....|....*....|....*....|.
gi 495404195 191 SMSDYMASLDVMLEL--DSRVyFPGHGGAVT 219
Cdd:cd16322  164 DPKAMAASLRRLLTLpdETRV-FPGHGPPTT 193
yflN-like_MBL-fold cd07721
uncharacterized subgroup which includes Bacillus subtilis yflN; MBL-fold metallo hydrolase ...
 40-215 2.48e-16

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: 75.72  E-value: 2.48e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495404195  40 NSYLVGRDT-LALIDPGPLddSHKATLLQAIA-----GRPVSHIFVSHTHRDHSPLATVLKDELGALLVA--------EG 105
Cdd:cd07721   12 NAYLIEDDDgLTLIDTGLP--GSAKRILKALRelglsPKDIRRILLTHGHIDHIGSLAALKEAPGAPVYAhereapylEG 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495404195 106 PHRAARPLHTGEVNLLDASADTDFVP-DIIAADNTVINGDGwALRTIHTPGHTANHAVFALENTGILFSADHIMAWSTSI 184
Cdd:cd07721   90 EKPYPPPVRLGLLGLLSPLLPVKPVPvDRTLEDGDTLDLAG-GLRVIHTPGHTPGHISLYLEEDGVLIAGDALVTVGGEL 168

                        170       180       190
                 ....*....|....*....|....*....|....
gi 495404195 185 VAPPDG---SMSDYMASLDVMLELDSRVYFPGHG 215
Cdd:cd07721  169 VPPPPPftwDMEEALESLRKLAELDPEVLAPGHG 202
metallo-hydrolase-like_MBL-fold cd16282
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 44-223 4.66e-16

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: 75.29  E-value: 4.66e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495404195  44 VGRDTLALIDPGPlddSHKAT--LLQAIA---GRPVSHIFVSHTHRDHSPLATVLKDELG---------ALLVAEGPHRA 109
Cdd:cd16282   21 VGDDGVVVIDTGA---SPRLAraLLAAIRkvtDKPVRYVVNTHYHGDHTLGNAAFADAGApiiahentrEELAARGEAYL 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495404195 110 ARPLHTGEvnllDASADTDFV-PDIIAADNTVINGDGWALRTIHT-PGHTANHAVFALENTGILFSADhiMAWSTSIVAP 187
Cdd:cd16282   98 ELMRRLGG----DAMAGTELVlPDRTFDDGLTLDLGGRTVELIHLgPAHTPGDLVVWLPEEGVLFAGD--LVFNGRIPFL 171

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 495404195 188 PDGSMSDYMASLDVMLELDSRVYFPGHGGAVTKPKA 223
Cdd:cd16282  172 PDGSLAGWIAALDRLLALDATVVVPGHGPVGDKADL 207
Lactamase_B pfam00753
Metallo-beta-lactamase superfamily;
35-214 2.95e-14

Metallo-beta-lactamase superfamily;


Pssm-ID: 425851 [Multi-domain]  Cd Length: 196  Bit Score: 70.09  E-value: 2.95e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495404195   35 TFYGTNSYLV-GRDTLALIDPGPLDDSHKATLLQAIA--GRPVSHIFVSHTHRDHSPLATVLKDELGALLVAEgPHRAAR 111
Cdd:pfam00753   2 GPGQVNSYLIeGGGGAVLIDTGGSAEAALLLLLAALGlgPKDIDAVILTHGHFDHIGGLGELAEATDVPVIVV-AEEARE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495404195  112 PLHTGEVNLLDASADTDFVPDIIAADNTVINGD-----GWALRTIHTPGHTANHAVFALENTGILFSADHIMAWSTSIVA 186
Cdd:pfam00753  81 LLDEELGLAASRLGLPGPPVVPLPPDVVLEEGDgilggGLGLLVTHGPGHGPGHVVVYYGGGKVLFTGDLLFAGEIGRLD 160

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 495404195  187 PP--------DGSMSDYMASLDVMLELDSRVYFPGH 214
Cdd:pfam00753 161 LPlggllvlhPSSAESSLESLLKLAKLKAAVIVPGH 196
YcbL-like_MBL-fold cd07737
Salmonella enterica serovar typhimurium YcbL and related proteins; MBL-fold metallo hydrolase ...
 50-214 2.37e-13

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: 67.19  E-value: 2.37e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495404195  50 ALIDPGplDDSHKatLLQAIAGRP--VSHIFVSHTHRDHSPLATVLKDELGALLVaeGPHRAARPL-----HTGEVNLLD 122
Cdd:cd07737   25 AVIDPG--GDADK--ILQAIEDLGltLKKILLTHGHLDHVGGAAELAEHYGVPII--GPHKEDKFLlenlpEQSQMFGFP 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495404195 123 ASADtdFVPDIIAADNTVINGDGWALRTIHTPGHTANHAVFALENTGILFSADHIMAWSTSIVAPPDGSMSDYMASL-DV 201
Cdd:cd07737   99 PAEA--FTPDRWLEEGDTVTVGNLTLEVLHCPGHTPGHVVFFNRESKLAIVGDVLFKGSIGRTDFPGGNHAQLIASIkEK 176

                        170
                 ....*....|....
gi 495404195 202 MLELDSRVYF-PGH 214
Cdd:cd07737  177 LLPLGDDVTFiPGH 190
MBLAC2-like_MBL-fold cd07712
uncharacterized human metallo-beta-lactamase domain-containing protein 2 and related proteins; ...
 34-214 2.72e-13

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: 66.88  E-value: 2.72e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495404195  34 FTFYGTNSYLV-GRDTLALIDPGpLDDSHKATLLQAIAGRPVSHIFvSHTHRDHS------PLATVLKDELGALlvaegp 106
Cdd:cd07712    4 EEDDRVNIYLLrGRDRALLIDTG-LGIGDLKEYVRTLTDLPLLVVA-THGHFDHIgglhefEEVYVHPADAEIL------ 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495404195 107 hraarPLHTGEVNLLDASADTDFVPDI---IAADNTVINGDGWALRTIHTPGHTANHAVFALENTGILFSAD-----HIM 178
Cdd:cd07712   76 -----AAPDNFETLTWDAATYSVPPAGptlPLRDGDVIDLGDRQLEVIHTPGHTPGSIALLDRANRLLFSGDvvydgPLI 150

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 495404195 179 AWstsivaPPDGSMSDYMASLDVMLELDS--RVYFPGH 214
Cdd:cd07712  151 MD------LPHSDLDDYLASLEKLSKLPDefDKVLPGH 182
YmaE-like_MBL-fold cd07727
uncharacterized subgroup which includes Bacillus subtilis YmaE and related proteins; MBL-fold ...
 31-218 1.88e-12

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: 64.52  E-value: 1.88e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495404195  31 PSPFTFyGTNSYLVGR-DTLALID-PGPLDDSHKAtlLQAIAGrpVSHIFVshTHRDHSPLATVLKDELGAllvaegphr 108
Cdd:cd07727    8 HSEKSF-GAASYLILRpEGNILVDsPRYSPPLAKR--IEALGG--IRYIFL--THRDDVADHAKWAERFGA--------- 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495404195 109 aARPLHTGEVNlldASADTDFVPDIIAADNTVINGDgwaLRTIHTPGHTANHAVFALENTGILFSADHImAWST---SIV 185
Cdd:cd07727   72 -KRIIHEDDVN---AVTRPDEVIVLWGGDPWELDPD---LTLIPVPGHTRGSVVLLYKEKGVLFTGDHL-AWSRrrgWLS 143

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 495404195 186 APPD---GSMSDYMASLDVMLELDSRVYFPGHGGAV 218
Cdd:cd07727  144 AFRYvcwYSWPEQAESVERLADLDFEWVLPGHGRRV 179
metallo-hydrolase-like_MBL-fold cd16276
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 42-218 2.91e-12

uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo hydrolase domain; Members of the MBL-fold metallohydrolase superfamily are mainly hydrolytic enzymes which carry out a variety of biological functions. The class B metal beta-lactamases (MBLs) for which this fold was named perform only a small fraction of the activities included in this superfamily.Activities carried out by superfamily members include class B beta-lactamases, hydroxyacylglutathione hydrolases, AHL (acyl homoserine lactone) lactonases, persulfide dioxygenases, flavodiiron proteins, cleavage and polyadenylation specificity factors such as the Int9 and Int11 subunits of Integrator, Sdsa1-like and AtsA-like arylsulfatases, 5'-exonucleases human SNM1A and yeast Pso2p, ribonuclease J and ribonuclease Z, cyclic nucleotide phosphodiesterases, insecticide hydrolases, and proteins required for natural transformation competence. Classical members of the superfamily are di-, or less commonly mono-, zinc-ion-dependent hydrolases, however the diversity of biological roles is reflected in variations in the active site metallo-chemistry.


Pssm-ID: 293834 [Multi-domain]  Cd Length: 188  Bit Score: 64.14  E-value: 2.91e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495404195  42 YLVGRDTLALIDPGPlddSHKATLLQAIAG---RPVSHIFVSHTHRDHSPLATVLKDElGALLVAegpHRAARplhtgev 118
Cdd:cd16276   14 FLVTDKGVIVVDAPP---SLGENLLAAIRKvtdKPVTHVVYSHNHADHIGGASIFKDE-GATIIA---HEATA------- 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495404195 119 NLLDASADTDF-VPDIIAADNTVINGDGwalRTI----HTPGHTANHAVFALENTGILFSADHIMA-WSTSIVAPPDGSM 192
Cdd:cd16276   80 ELLKRNPDPKRpVPTVTFDDEYTLEVGG---QTLelsyFGPNHGPGNIVIYLPKQKVLMAVDLINPgWVPFFNFAGSEDI 156

                        170       180
                 ....*....|....*....|....*.
gi 495404195 193 SDYMASLDVMLELDSRVYFPGHGGAV 218
Cdd:cd16276  157 PGYIEALDELLEYDFDTFVGGHGNRL 182
ST1585-like_MBL-fold cd07726
uncharacterized subgroup which includes Sulfolobus tokodaii ST1585 protein; MBL-fold metallo ...
 41-214 3.61e-10

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: 58.66  E-value: 3.61e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495404195  41 SYLV-GRDTLALIDPGP---LDDSHKATLLQAIAGRPVSHIFVSHTHRDHSPLA-TVLKDELGALLVAegPHRAARPLht 115
Cdd:cd07726   18 SYLLdGEGRPALIDTGPsssVPRLLAALEALGIAPEDVDYIILTHIHLDHAGGAgLLAEALPNAKVYV--HPRGARHL-- 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495404195 116 geVN---LLDAS-------ADTDF-----VPD---IIAADNTVINGDGWALRTIHTPGHTANHAVFALENTGILFSAD-- 175
Cdd:cd07726   94 --IDpskLWASAravygdeADRLGgeilpVPEervIVLEDGETLDLGGRTLEVIDTPGHAPHHLSFLDEESDGLFTGDaa 171

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 495404195 176 --------HIMAWSTSivaPPDGSMSDYMASLDVMLELDSRVYFPGH 214
Cdd:cd07726  172 gvrypeldVVGPPSTP---PPDFDPEAWLESLDRLLSLKPERIYLTH 215
BLACT_WH pfam17778
Beta-lactamase associated winged helix domain; This winged helix domain is found at the ...
 249-290 2.08e-09

Beta-lactamase associated winged helix domain; This winged helix domain is found at the C-terminus of some beta lactamase enzymes.


Pssm-ID: 407650  Cd Length: 46  Bit Score: 52.23  E-value: 2.08e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 495404195  249 TIATMVAAIYRDTDPRLHGAAALSVLAHLEDMVARGLVQTDG 290
Cdd:pfam17778   1 TAMELVKVIYKDVPESLHPAAERGVLAHLEKLEAEGKVVREG 42
hydroxyacylglutathione_hydrolase_MBL-fold cd07723
hydroxyacylglutathione hydrolase, MBL-fold metallo-hydrolase domain; hydroxyacylglutathione ...
 41-214 9.31e-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: 53.62  E-value: 9.31e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495404195  41 SYLVGRD---TLALIDPGpldDShkATLLQAIA--GRPVSHIFVSHTHRDHSPLATVLKDELGALLVAeGPHRAARPLHt 115
Cdd:cd07723   11 IYLIVDEatgEAAVVDPG---EA--EPVLAALEknGLTLTAILTTHHHWDHTGGNAELKALFPDAPVY-GPAEDRIPGL- 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495404195 116 gevnlldasadtdfvpDIIAADNTVINGDGWALRTIHTPGHTANHAVFALENTGILFSADHIMawstsiVA----PPDGS 191
Cdd:cd07723   84 ----------------DHPVKDGDEIKLGGLEVKVLHTPGHTLGHICYYVPDEPALFTGDTLF------SGgcgrFFEGT 141

                        170       180
                 ....*....|....*....|....*
gi 495404195 192 MSDYMASLDVMLELDS--RVYfPGH 214
Cdd:cd07723  142 AEQMYASLQKLLALPDdtLVY-CGH 165
metallo-hydrolase-like_MBL-fold cd07743
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 35-214 1.30e-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) 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: 50.99  E-value: 1.30e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495404195  35 TFY---GTNS--YLVGRDTLALIDPGpLDDSHKATLLQAI--AGRPVSHIFVSHTHRDHSPLATVLKDELGALLVAEGPH 107
Cdd:cd07743    1 TYYipgPTNIgvYVFGDKEALLIDSG-LDEDAGRKIRKILeeLGWKLKAIINTHSHADHIGGNAYLQKKTGCKVYAPKIE 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495404195 108 RAA------RPLHTGEVNLLDA------SADTDFVPDIIAADNTVINGDGwaLRTIHTPGHTANHAVFALENtGILFSAD 175
Cdd:cd07743   80 KAFienpllEPSYLGGAYPPKElrnkflMAKPSKVDDIIEEGELELGGVG--LEIIPLPGHSFGQIGILTPD-GVLFAGD 156

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 495404195 176 HIMawSTSIVA----PPdgsMSD---YMASLDVMLELDSRVYFPGH 214
Cdd:cd07743  157 ALF--GEEVLEkygiPF---LYDveeQLETLEKLEELDADYYVPGH 197
POD-like_MBL-fold cd07724
ETHE1 (PDO type I), persulfide dioxygenase A (PDOA, PDO type II) and related proteins; ...
 38-175 5.50e-07

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: 48.94  E-value: 5.50e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495404195  38 GTNSYLVG---RDTLALIDPGpLDDSHKatLLQAIAGRPVS--HIFVSHTHRDHSPLATVLKDELGAllvaegphraarP 112
Cdd:cd07724   11 GTLSYLVGdpeTGEAAVIDPV-RDSVDR--YLDLAAELGLKitYVLETHVHADHVSGARELAERTGA------------P 75

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 495404195 113 LHTGEvnlldasADTDFVPDIIAADNTVINGDGWALRTIHTPGHTANHAVFALENTGILFSAD 175
Cdd:cd07724   76 IVIGE-------GAPASFFDRLLKDGDVLELGNLTLEVLHTPGHTPESVSYLVGDPDAVFTGD 131
flavodiiron_proteins_MBL-fold cd07709
catalytic domain of flavodiiron proteins (FDPs) and related proteins; MBL-fold ...
 17-175 2.92e-06

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: 47.48  E-value: 2.92e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495404195  17 VNIAPHVQRITVNNPSPFTF-------YGT--NSYLVGRDTLALIDPGplDDSHKATLLQAIA----GRPVSHIFVSHTH 83
Cdd:cd07709    1 VEIADDIYWVGVNDWDLRLFegeyptpRGTsyNSYLIKDEKTALIDTV--KEPFFDEFLENLEevidPRKIDYIVVNHQE 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495404195  84 RDHSP-LATVLKDELGALLVAegpHRAArplhtgeVNLLDASADTDFVPDIIAADNTVINGDGWALRTIHTPG-HTANHA 161
Cdd:cd07709   79 PDHSGsLPELLELAPNAKIVC---SKKA-------ARFLKHFYPGIDERFVVVKDGDTLDLGKHTLKFIPAPMlHWPDTM 148

                        170
                 ....*....|....
gi 495404195 162 VFALENTGILFSAD 175
Cdd:cd07709  149 VTYDPEDKILFSGD 162
PLN02398 PLN02398
hydroxyacylglutathione hydrolase
 55-210 3.50e-06

hydroxyacylglutathione hydrolase


Pssm-ID: 215223 [Multi-domain]  Cd Length: 329  Bit Score: 47.92  E-value: 3.50e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495404195  55 GPLDDSHKATLLQAIA--GRPVSHIFVSHTHRDHSPLATVLKDELGALLVAEGphraarplhtgevnlldasADTDFVPD 132
Cdd:PLN02398 101 GVVDPSEAVPVIDALSrkNRNLTYILNTHHHYDHTGGNLELKARYGAKVIGSA-------------------VDKDRIPG 161

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495404195 133 IiaaDNTVINGDGW-----ALRTIHTPGHTANHAVFALENTGILFSADHIMAWSTSIVAppDGSMSDYMASLDVMLEL-- 205
Cdd:PLN02398 162 I---DIVLKDGDKWmfaghEVLVMETPGHTRGHISFYFPGSGAIFTGDTLFSLSCGKLF--EGTPEQMLSSLQKIISLpd 236


                 ....*
gi 495404195 206 DSRVY 210
Cdd:PLN02398 237 DTNIY 241
AHL_lactonase_MBL-fold cd07729
quorum-quenching N-acyl-homoserine lactonase, MBL-fold metallo-hydrolase domain; Acyl ...
 74-214 7.89e-06

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: 46.05  E-value: 7.89e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495404195  74 VSHIFVSHTHRDHS------PLATVL--KDELGALL--------VAEGPHRAARPLHTGEVNLLDAsaDTDFVPDIiaad 137
Cdd:cd07729   89 IDYVILSHLHFDHAggldlfPNATIIvqRAELEYATgpdplaagYYEDVLALDDDLPGGRVRLVDG--DYDLFPGV---- 162

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495404195 138 ntvingdgwalRTIHTPGHTANH--AVFALENTGILFSADHIMA---WSTSIVAPPDGSMSDYMASLDVMLELDSR---V 209
Cdd:cd07729  163 -----------TLIPTPGHTPGHqsVLVRLPEGTVLLAGDAAYTyenLEEGRPPGINYDPEAALASLERLKALAERegaR 231


                 ....*
gi 495404195 210 YFPGH 214
Cdd:cd07729  232 VIPGH 236
metallo-hydrolase-like_MBL-fold cd16280
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 47-157 1.64e-05

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: 45.27  E-value: 1.64e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495404195  47 DTLALIDPGpLDDSHKATLLQAIA-----GRPVSHIFVSHTHRDHSPLATVLKDELGALLVAEgpHRAARPLHTGEVNLL 121
Cdd:cd16280   31 DGLILIDAL-NNNEAADLIVDGLEklgldPADIKYILITHGHGDHYGGAAYLKDLYGAKVVMS--EADWDMMEEPPEEGD 107

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 495404195 122 DASADTDFVPDIIAADNTVINGDGWALRTIHTPGHT 157
Cdd:cd16280  108 NPRWGPPPERDIVIKDGDTLTLGDTTITVYLTPGHT 143
NorV COG0426
Flavorubredoxin [Energy production and conversion];
16-87 3.03e-05

Flavorubredoxin [Energy production and conversion];


Pssm-ID: 440195 [Multi-domain]  Cd Length: 390  Bit Score: 45.21  E-value: 3.03e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495404195  16 AVNIAPHVQRITVNNPSPFTF-------YGT--NSYLVGRDTLALIDPGplDDSHKATLLQAIA----GRPVSHIFVSHT 82
Cdd:COG0426    2 AVEIAHGVYWVGVLDWDRRLFegeyptpRGTtyNSYLIVDEKTALIDTV--GESFFEEFLENLSkvidPKKIDYIIVNHQ 79


                 ....*
gi 495404195  83 HRDHS 87
Cdd:COG0426   80 EPDHS 84
BaeB-like_MBL-fold cd16275
Bacillus amyloliquefaciens BaeB and related proteins; MBL-fold metallo hydrolase domain; ...
 74-214 4.42e-05

Bacillus amyloliquefaciens BaeB and related proteins; MBL-fold metallo hydrolase domain; Bacillus amyloliquefaciens BaeB may play a role in the synthesis of the antibiotic polyketide bacillaene. 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: 293833 [Multi-domain]  Cd Length: 174  Bit Score: 43.29  E-value: 4.42e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495404195  74 VSHIFVSHTHRDHSPLatvlkdelgallVAEGPHRAARPLHtgeVNLLDASADTDFVPDIIAA-DNTVINGDGWALRTIH 152
Cdd:cd16275   48 LTGILLTHSHFDHVNL------------VEPLLAKYDAPVY---MSKEEIDYYGFRCPNLIPLeDGDTIKIGDTEITCLL 112

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 495404195 153 TPGHTANHAVFALENtgILFSADHIMAWSTSIVAPPDGSMSDYMASLDVMLELDS---RVYfPGH 214
Cdd:cd16275  113 TPGHTPGSMCYLLGD--SLFTGDTLFIEGCGRCDLPGGDPEEMYESLQRLKKLPPpntRVY-PGH 174
MBLAC1-like_MBL-fold cd07711
uncharacterized human metallo-beta-lactamase domain-containing protein 1 and related proteins; ...
 29-168 4.58e-04

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: 40.26  E-value: 4.58e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495404195  29 NNPSPFTFYGTNSYLVGRDTLALIDPGPLDDshKATLLQAIAGR---P--VSHIFVSHTHRDHS------PLATVLKDEL 97
Cdd:cd07711   13 DSDGGFRASSTVTLIKDGGKNILVDTGTPWD--RDLLLKALAEHglsPedIDYVVLTHGHPDHIgnlnlfPNATVIVGWD 90

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 495404195  98 gallvaegphraarpLHTGEVNLLDASADTDFVPDiiaaDNTVIngdgwalrtIHTPGHTANHAVFALENT 168
Cdd:cd07711   91 ---------------ICGDSYDDHSLEEGDGYEID----ENVEV---------IPTPGHTPEDVSVLVETE 133
SMB-1-like_MBL-B3 cd16313
SMB-1, THIN-B and related metallo-beta-lactamases, subclass B3; MBL-fold metallo-hydrolase ...
 33-157 6.73e-04

SMB-1, THIN-B and related metallo-beta-lactamases, subclass B3; 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 SMB-1- and THIN-B-like MBLs belongs to the B3 subclass. Subclass B3 enzymes are most active with two zinc ions bound in the active site, and have a broad-spectrum substrate profile. These B3 enzymes have a modified Zn2/DCH site (Asp-His-His).


Pssm-ID: 293871 [Multi-domain]  Cd Length: 254  Bit Score: 40.62  E-value: 6.73e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495404195  33 PFTFYGtNSYLVGRDTLA-----------LIDPGPLDDSHK-ATLLQAIAGRP--VSHIFVSHTHRDHSPLATVLKDELG 98
Cdd:cd16313    7 PFQIYG-NTYYVGTGGISavlitspqghiLIDGGFPKSPEQiAASIRQLGFKLedVKYILSSHDHWDHAGGIAALQKLTG 85

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 495404195  99 ALLVAeGPhRAARPLHTGEVNLLDAS--ADTDFVPdiIAADNTVINGD-----GWALRTIHTPGHT 157
Cdd:cd16313   86 AQVLA-SP-ATVAVLRSGSMGKDDPQfgGLTPMPP--VASVRAVRDGEvvklgPLAVTAHATPGHT 147
PhnP COG1235
Phosphoribosyl 1,2-cyclic phosphate phosphodiesterase [Inorganic ion transport and metabolism]; ...
 39-86 3.29e-03

Phosphoribosyl 1,2-cyclic phosphate phosphodiesterase [Inorganic ion transport and metabolism];


Pssm-ID: 440848 [Multi-domain]  Cd Length: 259  Bit Score: 38.34  E-value: 3.29e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 495404195  39 TNSYLVGRD-TLALIDPGPldDSHKATLLQAIAGRPVSHIFVSHTHRDH 86
Cdd:COG1235   35 RSSILVEADgTRLLIDAGP--DLREQLLRLGLDPSKIDAILLTHEHADH 81
MBL-B3-like cd07708
metallo-beta-lactamases, subclass B3; MBL-fold metallo-hydrolase domain; MBLs (class B of the ...
 33-157 3.65e-03

metallo-beta-lactamases, subclass B3; 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 B3 enzymes are most active with two zinc ions bound in the active site, and have a broad-spectrum substrate profile. B3 MBLs include Fluoribacter gormanii FEZ-1, Elizabethkingia meningoseptica (Chryseobacterium meningosepticum) GOB-1, Stenotrophomonas Maltophilia L1, and Bradyrhizobium diazoefficiens BJP-1, Serratia marcescens SMB-1, and Pseudomonas Aeruginosa AIM-1. These B3 enzymes have a modified Zn2/DCH site (Asp-His-His).


Pssm-ID: 293794 [Multi-domain]  Cd Length: 248  Bit Score: 38.30  E-value: 3.65e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495404195  33 PFTFYGtNSYLVGRDTLA-----------LIDPG-PLDDSHKATLLQAIAGRP--VSHIFVSHTHRDHSPLATVLKDELG 98
Cdd:cd07708    7 PFQIAG-NTYYVGTDDLAaylivtpqgniLIDGDmEQNAPMIKANIKKLGFKFsdTKLILISHAHFDHAGGSAEIKKQTG 85

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 495404195  99 ALLVAeGPHRAARPLHTGEVNLLDA-SADTDFVP---DIIAADNTVINGDGWALRTIHTPGHT 157
Cdd:cd07708   86 AKVMA-GAEDVSLLLSGGSSDFHYAnDSSTYFPQstvDRAVHDGERVTLGGTVLTAHATPGHT 147
arylsulfatase_Sdsa1-like_MBL-fold cd07710
Pseudomonas aeruginosa arylsulfatase SdsA1, Pseudomonas sp. DSM6611 arylsulfatase Pisa1, and ...
 44-218 5.78e-03

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: 37.48  E-value: 5.78e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495404195  44 VGRDTLALIDPGPLDDSHKA--TLLQAIAG-RPVSHIFVSHTHRDHSPLATVLKDE-------------LGALLVAE--- 104
Cdd:cd07710   24 EGDTGLIIIDTLESAEAAKAalELFRKHTGdKPVKAIIYTHSHPDHFGGAGGFVEEedsgkvpiiapegFMEEAVSEnvl 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495404195 105 -GP---HRAAR----PLHTGEVNLLDA-------SADTDFVP--DIIAADNTVINGDGWALRTIHTPGHTANHAVFALEN 167
Cdd:cd07710  104 aGNamsRRAAYqfgaLLPKGEKGQVGAglgpglsTGTVGFIPptITITETGETLTIDGVELEFQHAPGEAPDEMMVWLPD 183

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 495404195 168 TGILFSADHIMAWSTSIvAPPDGSM----SDYMASLDVMLELDSRVYFPGHGGAV 218
Cdd:cd07710  184 YKVLFCADNVYHTFPNL-YTLRGAKyrdaLAWAKSLDEAISLKAEVLFPSHTWPV 237
Mbl1b-like_MBL-B3 cd16310
Caulobacter crescentus Mbl1b and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 38-157 6.28e-03

Caulobacter crescentus Mbl1b and related metallo-beta-lactamases, subclass B3; 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 Mbl1b-like MBLs belongs to the B3 subclass. Subclass B3 enzymes are most active with two zinc ions bound in the active site, and have a broad-spectrum substrate profile. These B3 enzymes have a modified Zn2/DCH site (Asp-His-His).


Pssm-ID: 293868  Cd Length: 252  Bit Score: 37.43  E-value: 6.28e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495404195  38 GTNSYLVGRDTLA-LIDPGPldDSHKATLLQAIAG-----RPVSHIFVSHTHRDHSPLATVLKDELGALLVAEGPHRAAR 111
Cdd:cd16310   21 GIGSYLITSNHGAiLLDGGL--EENAALIEQNIKAlgfklSDIKIIINTHAHYDHAGGLAQLKADTGAKLWASRGDRPAL 98

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 495404195 112 PL--HTGEvNLLDASADTDFVPDIIAADNTVINGDGWALRTIHTPGHT 157
Cdd:cd16310   99 EAgkHIGD-NITQPAPFPAVKVDRILGDGEKIKLGDITLTATLTPGHT 145
MBL-B1 cd16285
metallo-beta-lactamases, subclass B1; MBL-fold metallo-hydrolase domain; MBLs (class B of the ...
 19-85 7.01e-03

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: 36.88  E-value: 7.01e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 495404195  19 IAPHVQRITVNNPSPFTFYGTNS-YLVGRDTLALIDPgPLDDSHKATLLQAIA---GRPVSHIFVSHTHRD 85
Cdd:cd16285    6 LADNVWVHTSLAEFNGGAVPSNGlIVIDGKGLVLIDT-PWTEAQTATLLDWIEkklGKPVTAAISTHSHDD 75
 
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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