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Conserved domains on  [gi|15596029|ref|NP_249523|]
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hypothetical protein PA0832 [Pseudomonas aeruginosa PAO1]

Protein Classification

MBL fold metallo-hydrolase( domain architecture ID 581040)

MBL fold metallo-hydrolase is most likely a hydrolytic enzyme

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
metallo-hydrolase-like_MBL-fold super family cl23716
mainly hydrolytic enzymes and related proteins which carry out various biological functions; ...
 10-195 1.32e-67

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.


The actual alignment was detected with superfamily member cd07737:

Pssm-ID: 451500 [Multi-domain]  Cd Length: 190  Bit Score: 205.48  E-value: 1.32e-67
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596029  10 ETFPVGPLQCNCTIIGDPLTRKAIVVDPGGDHELILQRLDRLGLQVVSIIHTHAHLDHFLASGEMKKRTGAS-LHLHKDD 88
Cdd:cd07737   2 QIIPVTPFQQNCSLIWCEETKEAAVIDPGGDADKILQAIEDLGLTLKKILLTHGHLDHVGGAAELAEHYGVPiIGPHKED 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596029  89 QFLWDNLEMQCQLFGVPYTPVPAPDRWLADDEELACGCGV--ALHTPGHTPGSMSFWFPRAKLLIAGDTLFRRGIGRTDL 166
Cdd:cd07737  82 KFLLENLPEQSQMFGFPPAEAFTPDRWLEEGDTVTVGNLTleVLHCPGHTPGHVVFFNRESKLAIVGDVLFKGSIGRTDF 161

                       170       180
                ....*....|....*....|....*....
gi 15596029 167 WGGDSAAIQRSIRQRLYSLDEDATVVAGH 195
Cdd:cd07737 162 PGGNHAQLIASIKEKLLPLGDDVTFIPGH 190
 
Name Accession Description Interval E-value
YcbL-like_MBL-fold cd07737
Salmonella enterica serovar typhimurium YcbL and related proteins; MBL-fold metallo hydrolase ...
 10-195 1.32e-67

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: 205.48  E-value: 1.32e-67
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596029  10 ETFPVGPLQCNCTIIGDPLTRKAIVVDPGGDHELILQRLDRLGLQVVSIIHTHAHLDHFLASGEMKKRTGAS-LHLHKDD 88
Cdd:cd07737   2 QIIPVTPFQQNCSLIWCEETKEAAVIDPGGDADKILQAIEDLGLTLKKILLTHGHLDHVGGAAELAEHYGVPiIGPHKED 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596029  89 QFLWDNLEMQCQLFGVPYTPVPAPDRWLADDEELACGCGV--ALHTPGHTPGSMSFWFPRAKLLIAGDTLFRRGIGRTDL 166
Cdd:cd07737  82 KFLLENLPEQSQMFGFPPAEAFTPDRWLEEGDTVTVGNLTleVLHCPGHTPGHVVFFNRESKLAIVGDVLFKGSIGRTDF 161

                       170       180
                ....*....|....*....|....*....
gi 15596029 167 WGGDSAAIQRSIRQRLYSLDEDATVVAGH 195
Cdd:cd07737 162 PGGNHAQLIASIKEKLLPLGDDVTFIPGH 190
GloB COG0491
Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General ...
 8-200 8.22e-50

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: 161.01  E-value: 8.22e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596029   8 IRETFPVGPLQCNCTIIGDplTRKAIVVDPGGD---HELILQRLDRLGLQVVSIIHTHAHLDHFLASGEMKKRTGASLHL 84
Cdd:COG0491   4 LPGGTPGAGLGVNSYLIVG--GDGAVLIDTGLGpadAEALLAALAALGLDIKAVLLTHLHPDHVGGLAALAEAFGAPVYA 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596029  85 HKDDQFLWDNLEMQcQLFGVPytpVPAPDRWLADDEELACGCG--VALHTPGHTPGSMSFWFPRAKLLIAGDTLFRRGIG 162
Cdd:COG0491  82 HAAEAEALEAPAAG-ALFGRE---PVPPDRTLEDGDTLELGGPglEVIHTPGHTPGHVSFYVPDEKVLFTGDALFSGGVG 157

                       170       180       190
                ....*....|....*....|....*....|....*...
gi 15596029 163 RTDLWGGDSAAIQRSIRqRLYSLDEDaTVVAGHGPDTT 200
Cdd:COG0491 158 RPDLPDGDLAQWLASLE-RLLALPPD-LVIPGHGPPTT 193
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 20-195 3.58e-35

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: 122.66  E-value: 3.58e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596029     20 NCTIIGDPltRKAIVVDPG-GDHELILQRLDRLGL-QVVSIIHTHAHLDHFLASGEMKKRTGASLHLHKDDQFLWDNLEM 97
Cdd:smart00849   1 NSYLVRDD--GGAILIDTGpGEAEDLLAELKKLGPkKIDAIILTHGHPDHIGGLPELLEAPGAPVYAPEGTAELLKDLLA 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596029     98 QCQLFGVPYTPVPaPDRWLADDEELACGCG--VALHTPGHTPGSMSFWFPRAKLLIAGDTLFRRGIGRTDLWGGDSAAIQ 175
Cdd:smart00849  79 LLGELGAEAEPAP-PDRTLKDGDELDLGGGelEVIHTPGHTPGSIVLYLPEGKILFTGDLLFAGGDGRTLVDGGDAAASD 157

                          170       180
                   ....*....|....*....|
gi 15596029    176 RSIRQRLYSLDEDATVVAGH 195
Cdd:smart00849 158 ALESLLKLLKLLPKLVVPGH 177
Lactamase_B pfam00753
Metallo-beta-lactamase superfamily;
14-195 9.24e-31

Metallo-beta-lactamase superfamily;


Pssm-ID: 425851 [Multi-domain]  Cd Length: 196  Bit Score: 111.69  E-value: 9.24e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596029    14 VGPLQCNCTIIGDPltRKAIVVDPGGD----HELILQRLDRLGLQVVSIIHTHAHLDHFLASGEMKKRTGASLHLHKDDQ 89
Cdd:pfam00753   1 LGPGQVNSYLIEGG--GGAVLIDTGGSaeaaLLLLLAALGLGPKDIDAVILTHGHFDHIGGLGELAEATDVPVIVVAEEA 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596029    90 FLWDNLEMQCQLF------GVPYTPVPAPDRWLADDEELACGCGVALHTPGHTPGSMSFWFPRAKLLIAGDTLFRRGIGR 163
Cdd:pfam00753  79 RELLDEELGLAASrlglpgPPVVPLPPDVVLEEGDGILGGGLGLLVTHGPGHGPGHVVVYYGGGKVLFTGDLLFAGEIGR 158

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 15596029   164 TDLWGGDSAAIQRSIRQ------RLYSLDEDATVVAGH 195
Cdd:pfam00753 159 LDLPLGGLLVLHPSSAEssleslLKLAKLKAAVIVPGH 196
PLN02962 PLN02962
hydroxyacylglutathione hydrolase
 24-209 1.16e-14

hydroxyacylglutathione hydrolase


Pssm-ID: 178547 [Multi-domain]  Cd Length: 251  Bit Score: 70.21  E-value: 1.16e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596029   24 IGDPlTRKAIVVDP---GGDHELILqrLDRLGLQVVSIIHTHAHLDHFLASGEMKKR-------------TGASLHLHKD 87
Cdd:PLN02962  31 VSHP-DKPALLIDPvdkTVDRDLSL--VKELGLKLIYAMNTHVHADHVTGTGLLKTKlpgvksiiskasgSKADLFVEPG 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596029   88 DQFLWDNLemqcqlfgvpYTPVPApdrwladdeelacgcgvalhTPGHTPGSMSFWF------PRAKLLIAGDTLFRRGI 161
Cdd:PLN02962 108 DKIYFGDL----------YLEVRA--------------------TPGHTAGCVTYVTgegpdqPQPRMAFTGDALLIRGC 157

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 15596029  162 GRTDLWGGDSAAIQRSIRQRLYSLDEDATVVAGHGPD----TTLGEEMRENP 209
Cdd:PLN02962 158 GRTDFQGGSSDQLYKSVHSQIFTLPKDTLIYPAHDYKgftvSTVGEEMLYNP 209
 
Name Accession Description Interval E-value
YcbL-like_MBL-fold cd07737
Salmonella enterica serovar typhimurium YcbL and related proteins; MBL-fold metallo hydrolase ...
 10-195 1.32e-67

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: 205.48  E-value: 1.32e-67
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596029  10 ETFPVGPLQCNCTIIGDPLTRKAIVVDPGGDHELILQRLDRLGLQVVSIIHTHAHLDHFLASGEMKKRTGAS-LHLHKDD 88
Cdd:cd07737   2 QIIPVTPFQQNCSLIWCEETKEAAVIDPGGDADKILQAIEDLGLTLKKILLTHGHLDHVGGAAELAEHYGVPiIGPHKED 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596029  89 QFLWDNLEMQCQLFGVPYTPVPAPDRWLADDEELACGCGV--ALHTPGHTPGSMSFWFPRAKLLIAGDTLFRRGIGRTDL 166
Cdd:cd07737  82 KFLLENLPEQSQMFGFPPAEAFTPDRWLEEGDTVTVGNLTleVLHCPGHTPGHVVFFNRESKLAIVGDVLFKGSIGRTDF 161

                       170       180
                ....*....|....*....|....*....
gi 15596029 167 WGGDSAAIQRSIRQRLYSLDEDATVVAGH 195
Cdd:cd07737 162 PGGNHAQLIASIKEKLLPLGDDVTFIPGH 190
metallo-hydrolase-like_MBL-fold cd06262
mainly hydrolytic enzymes and related proteins which carry out various biological functions; ...
 10-195 3.54e-67

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: 204.44  E-value: 3.54e-67
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596029  10 ETFPVGPLQCNCTIIGDPlTRKAIVVDPGGD-HELILQRLDRLGLQVVSIIHTHAHLDHFLASGEMKKRTGASLHLHKDD 88
Cdd:cd06262   1 KRLPVGPLQTNCYLVSDE-EGEAILIDPGAGaLEKILEAIEELGLKIKAILLTHGHFDHIGGLAELKEAPGAPVYIHEAD 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596029  89 QFLWDNLEMQCQLFGVPYTPVPAPDRWLADDEELACGCG--VALHTPGHTPGSMSFWFPRAKLLIAGDTLFRRGIGRTDL 166
Cdd:cd06262  80 AELLEDPELNLAFFGGGPLPPPEPDILLEDGDTIELGGLelEVIHTPGHTPGSVCFYIEEEGVLFTGDTLFAGSIGRTDL 159

                       170       180
                ....*....|....*....|....*....
gi 15596029 167 WGGDSAAIQRSIRQRLYSLDEDATVVAGH 195
Cdd:cd06262 160 PGGDPEQLIESIKKLLLLLPDDTVVYPGH 188
TTHA1623-like_MBL-fold cd16322
uncharacterized Thermus thermophilus TTHA1623 and related proteins; MBL-fold metallo hydrolase ...
 10-211 1.64e-63

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: 195.65  E-value: 1.64e-63
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596029  10 ETFPVGPLQCNCTIIGDPLTRKAIVVDPGGDHELILQRLDRLGLQVVSIIHTHAHLDHFLASGEMKKRTGASLHLHKDDQ 89
Cdd:cd16322   2 RPFTLGPLQENTYLVADEGGGEAVLVDPGDESEKLLARFGTTGLTLLYILLTHAHFDHVGGVADLRRHPGAPVYLHPDDL 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596029  90 FLWDNLEMQCQLFGVPYTPVPAPDRWLADDEELACGcGV---ALHTPGHTPGSMSFWFPRAKLLIAGDTLFRRGIGRTDL 166
Cdd:cd16322  82 PLYEAADLGAKAFGLGIEPLPPPDRLLEDGQTLTLG-GLefkVLHTPGHSPGHVCFYVEEEGLLFSGDLLFQGSIGRTDL 160

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 15596029 167 WGGDSAAIQRSIRqRLYSLDEDATVVAGHGPDTTLGEEMRENPFV 211
Cdd:cd16322 161 PGGDPKAMAASLR-RLLTLPDETRVFPGHGPPTTLGEERRTNPFL 204
GloB COG0491
Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General ...
 8-200 8.22e-50

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: 161.01  E-value: 8.22e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596029   8 IRETFPVGPLQCNCTIIGDplTRKAIVVDPGGD---HELILQRLDRLGLQVVSIIHTHAHLDHFLASGEMKKRTGASLHL 84
Cdd:COG0491   4 LPGGTPGAGLGVNSYLIVG--GDGAVLIDTGLGpadAEALLAALAALGLDIKAVLLTHLHPDHVGGLAALAEAFGAPVYA 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596029  85 HKDDQFLWDNLEMQcQLFGVPytpVPAPDRWLADDEELACGCG--VALHTPGHTPGSMSFWFPRAKLLIAGDTLFRRGIG 162
Cdd:COG0491  82 HAAEAEALEAPAAG-ALFGRE---PVPPDRTLEDGDTLELGGPglEVIHTPGHTPGHVSFYVPDEKVLFTGDALFSGGVG 157

                       170       180       190
                ....*....|....*....|....*....|....*...
gi 15596029 163 RTDLWGGDSAAIQRSIRqRLYSLDEDaTVVAGHGPDTT 200
Cdd:COG0491 158 RPDLPDGDLAQWLASLE-RLLALPPD-LVIPGHGPPTT 193
POD-like_MBL-fold cd07724
ETHE1 (PDO type I), persulfide dioxygenase A (PDOA, PDO type II) and related proteins; ...
 23-196 3.34e-41

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: 137.92  E-value: 3.34e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596029  23 IIGDPLTRKAIVVDPGGDH-ELILQRLDRLGLQVVSIIHTHAHLDHFLASGEMKKRTGASLHLHKDDqflwdnlemqcql 101
Cdd:cd07724  16 LVGDPETGEAAVIDPVRDSvDRYLDLAAELGLKITYVLETHVHADHVSGARELAERTGAPIVIGEGA------------- 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596029 102 fgvpytPVPAPDRWLADDEELACGC--GVALHTPGHTPGSMSFWFPRAKLLIAGDTLFRRGIGRTDLWG---GDSAAIQR 176
Cdd:cd07724  83 ------PASFFDRLLKDGDVLELGNltLEVLHTPGHTPESVSYLVGDPDAVFTGDTLFVGDVGRPDLPGeaeGLARQLYD 156

                       170       180
                ....*....|....*....|
gi 15596029 177 SIRQRLYSLDEDATVVAGHG 196
Cdd:cd07724 157 SLQRKLLLLPDETLVYPGHD 176
BaeB-like_MBL-fold cd16275
Bacillus amyloliquefaciens BaeB and related proteins; MBL-fold metallo hydrolase domain; ...
 20-195 3.96e-38

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: 129.96  E-value: 3.96e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596029  20 NCTIIGDPLTRKAIVVDPGGDHELILQRLDRLGLQVVSIIHTHAHLDHFLASGEMKKRTGASLHLHKDDqflwdnlemqc 99
Cdd:cd16275  13 YSYIIIDKATREAAVVDPAWDIEKILAKLNELGLTLTGILLTHSHFDHVNLVEPLLAKYDAPVYMSKEE----------- 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596029 100 qlfgVPYTPVPAPD-RWLADDEELACG-----CgvaLHTPGHTPGSMSFWFPRAklLIAGDTLFRRGIGRTDLWGGDSAA 173
Cdd:cd16275  82 ----IDYYGFRCPNlIPLEDGDTIKIGdteitC---LLTPGHTPGSMCYLLGDS--LFTGDTLFIEGCGRCDLPGGDPEE 152

                       170       180
                ....*....|....*....|...
gi 15596029 174 IQRSIrQRLYSLDEDATVV-AGH 195
Cdd:cd16275 153 MYESL-QRLKKLPPPNTRVyPGH 174
hydroxyacylglutathione_hydrolase_MBL-fold cd07723
hydroxyacylglutathione hydrolase, MBL-fold metallo-hydrolase domain; hydroxyacylglutathione ...
 23-195 2.99e-35

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: 122.18  E-value: 2.99e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596029  23 IIGDPLTRKAIVVDPGgDHELILQRLDRLGLQVVSIIHTHAHLDHFLASGEMKKRTGaslhlhkddqflwdnlemQCQLF 102
Cdd:cd07723  13 LIVDEATGEAAVVDPG-EAEPVLAALEKNGLTLTAILTTHHHWDHTGGNAELKALFP------------------DAPVY 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596029 103 GVPYTPVPAPDRWLADDEELACGCGV--ALHTPGHTPGSMSFWFPRAKLLIAGDTLFRRGIGRtdLWGGDSAAIQRSIrQ 180
Cdd:cd07723  74 GPAEDRIPGLDHPVKDGDEIKLGGLEvkVLHTPGHTLGHICYYVPDEPALFTGDTLFSGGCGR--FFEGTAEQMYASL-Q 150

                       170
                ....*....|....*
gi 15596029 181 RLYSLDEDATVVAGH 195
Cdd:cd07723 151 KLLALPDDTLVYCGH 165
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 20-195 3.58e-35

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: 122.66  E-value: 3.58e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596029     20 NCTIIGDPltRKAIVVDPG-GDHELILQRLDRLGL-QVVSIIHTHAHLDHFLASGEMKKRTGASLHLHKDDQFLWDNLEM 97
Cdd:smart00849   1 NSYLVRDD--GGAILIDTGpGEAEDLLAELKKLGPkKIDAIILTHGHPDHIGGLPELLEAPGAPVYAPEGTAELLKDLLA 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596029     98 QCQLFGVPYTPVPaPDRWLADDEELACGCG--VALHTPGHTPGSMSFWFPRAKLLIAGDTLFRRGIGRTDLWGGDSAAIQ 175
Cdd:smart00849  79 LLGELGAEAEPAP-PDRTLKDGDELDLGGGelEVIHTPGHTPGSIVLYLPEGKILFTGDLLFAGGDGRTLVDGGDAAASD 157

                          170       180
                   ....*....|....*....|
gi 15596029    176 RSIRQRLYSLDEDATVVAGH 195
Cdd:smart00849 158 ALESLLKLLKLLPKLVVPGH 177
Lactamase_B pfam00753
Metallo-beta-lactamase superfamily;
14-195 9.24e-31

Metallo-beta-lactamase superfamily;


Pssm-ID: 425851 [Multi-domain]  Cd Length: 196  Bit Score: 111.69  E-value: 9.24e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596029    14 VGPLQCNCTIIGDPltRKAIVVDPGGD----HELILQRLDRLGLQVVSIIHTHAHLDHFLASGEMKKRTGASLHLHKDDQ 89
Cdd:pfam00753   1 LGPGQVNSYLIEGG--GGAVLIDTGGSaeaaLLLLLAALGLGPKDIDAVILTHGHFDHIGGLGELAEATDVPVIVVAEEA 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596029    90 FLWDNLEMQCQLF------GVPYTPVPAPDRWLADDEELACGCGVALHTPGHTPGSMSFWFPRAKLLIAGDTLFRRGIGR 163
Cdd:pfam00753  79 RELLDEELGLAASrlglpgPPVVPLPPDVVLEEGDGILGGGLGLLVTHGPGHGPGHVVVYYGGGKVLFTGDLLFAGEIGR 158

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 15596029   164 TDLWGGDSAAIQRSIRQ------RLYSLDEDATVVAGH 195
Cdd:pfam00753 159 LDLPLGGLLVLHPSSAEssleslLKLAKLKAAVIVPGH 196
yflN-like_MBL-fold cd07721
uncharacterized subgroup which includes Bacillus subtilis yflN; MBL-fold metallo hydrolase ...
 19-196 1.26e-30

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: 111.54  E-value: 1.26e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596029  19 CNCTIIGDPltRKAIVVDPG--GDHELILQRLDRLGL---QVVSIIHTHAHLDHFLASGEMKKRTGASLHLHKDD----- 88
Cdd:cd07721  11 VNAYLIEDD--DGLTLIDTGlpGSAKRILKALRELGLspkDIRRILLTHGHIDHIGSLAALKEAPGAPVYAHEREapyle 88

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596029  89 ---QFLWDNLEMQCQLFGVPY-TPVPAPDRWLADDEELACGCGV-ALHTPGHTPGSMSFWFPRAKLLIAGDTLFRRGiGR 163
Cdd:cd07721  89 gekPYPPPVRLGLLGLLSPLLpVKPVPVDRTLEDGDTLDLAGGLrVIHTPGHTPGHISLYLEEDGVLIAGDALVTVG-GE 167

                       170       180       190
                ....*....|....*....|....*....|....*..
gi 15596029 164 TDLWGG----DSAAIQRSIRqRLYSLDEDaTVVAGHG 196
Cdd:cd07721 168 LVPPPPpftwDMEEALESLR-KLAELDPE-VLAPGHG 202
metallo-hydrolase-like_MBL-fold cd16278
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 20-197 1.49e-20

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: 84.85  E-value: 1.49e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596029  20 NCTIIGDPLTrkAIVVDPGGDHELILQRLDRL--GLQVVSIIHTHAHLDHFLASGEMKKRTGASLHLHKDDQFLWDNLEm 97
Cdd:cd16278  19 NTYLLGAPDG--VVVIDPGPDDPAHLDALLAAlgGGRVSAILVTHTHRDHSPGAARLAERTGAPVRAFGPHRAGGQDTD- 95

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596029  98 qcqlfgvpytpvPAPDRWLADDEELACGCG--VALHTPGHTPGSMSFWFPRAKLLIAGDTLFRRG---IGRTDlwgGDSA 172
Cdd:cd16278  96 ------------FAPDRPLADGEVIEGGGLrlTVLHTPGHTSDHLCFALEDEGALFTGDHVMGWSttvIAPPD---GDLG 160

                       170       180
                ....*....|....*....|....*
gi 15596029 173 AIQRSIRqRLYSLDeDATVVAGHGP 197
Cdd:cd16278 161 DYLASLE-RLLALD-DRLLLPGHGP 183
metallo-hydrolase-like_MBL-fold cd16282
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 19-197 4.03e-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: 293840 [Multi-domain]  Cd Length: 209  Bit Score: 81.46  E-value: 4.03e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596029  19 CNCT-IIGDpltRKAIVVDPGGDHEL---ILQRLDRL-GLQVVSIIHTHAHLDHFL-------------ASGEMKKRtga 80
Cdd:cd16282  15 SNIGfIVGD---DGVVVIDTGASPRLaraLLAAIRKVtDKPVRYVVNTHYHGDHTLgnaafadagapiiAHENTREE--- 88

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596029  81 slhLHKDDQFLWDNLEMQCQlFGVPYTPVPAPDRWLADDEELACGcGVALH----TPGHTPGSMSFWFPRAKLLIAGDTL 156
Cdd:cd16282  89 ---LAARGEAYLELMRRLGG-DAMAGTELVLPDRTFDDGLTLDLG-GRTVElihlGPAHTPGDLVVWLPEEGVLFAGDLV 163

                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 15596029 157 FRRGIgrTDLWGGDSAAIQRSIrQRLYSLDeDATVVAGHGP 197
Cdd:cd16282 164 FNGRI--PFLPDGSLAGWIAAL-DRLLALD-ATVVVPGHGP 200
metallo-hydrolase-like_MBL-fold cd16280
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 42-213 1.14e-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: 293838 [Multi-domain]  Cd Length: 251  Bit Score: 75.70  E-value: 1.14e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596029  42 ELILQRLDRLGL---QVVSIIHTHAHLDHFLASGEMKKRTGASLHLHKDDqflWDNLEMQCQLFGVP-YTPVPAPDRWLA 117
Cdd:cd16280  46 DLIVDGLEKLGLdpaDIKYILITHGHGDHYGGAAYLKDLYGAKVVMSEAD---WDMMEEPPEEGDNPrWGPPPERDIVIK 122

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596029 118 DDEELACGcGVALH---TPGHTPGSMSFWFPraklLIAGDTLFRRGigrtdLWGG-------DSAAIQRSIRqrlySLDE 187
Cdd:cd16280 123 DGDTLTLG-DTTITvylTPGHTPGTLSLIFP----VKDGGKTHRAG-----LWGGtglntgpNLERREQYIA----SLER 188

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 15596029 188 DATVVAGHGPDTTLG------------EEMRE------NPFVRG 213
Cdd:cd16280 189 FKKIAEEAGVDVFLSnhpfqdgslekrEALRNrkpgepNPFVDG 232
PLN02962 PLN02962
hydroxyacylglutathione hydrolase
 24-209 1.16e-14

hydroxyacylglutathione hydrolase


Pssm-ID: 178547 [Multi-domain]  Cd Length: 251  Bit Score: 70.21  E-value: 1.16e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596029   24 IGDPlTRKAIVVDP---GGDHELILqrLDRLGLQVVSIIHTHAHLDHFLASGEMKKR-------------TGASLHLHKD 87
Cdd:PLN02962  31 VSHP-DKPALLIDPvdkTVDRDLSL--VKELGLKLIYAMNTHVHADHVTGTGLLKTKlpgvksiiskasgSKADLFVEPG 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596029   88 DQFLWDNLemqcqlfgvpYTPVPApdrwladdeelacgcgvalhTPGHTPGSMSFWF------PRAKLLIAGDTLFRRGI 161
Cdd:PLN02962 108 DKIYFGDL----------YLEVRA--------------------TPGHTAGCVTYVTgegpdqPQPRMAFTGDALLIRGC 157

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 15596029  162 GRTDLWGGDSAAIQRSIRQRLYSLDEDATVVAGHGPD----TTLGEEMRENP 209
Cdd:PLN02962 158 GRTDFQGGSSDQLYKSVHSQIFTLPKDTLIYPAHDYKgftvSTVGEEMLYNP 209
AHL_lactonase_MBL-fold cd07729
quorum-quenching N-acyl-homoserine lactonase, MBL-fold metallo-hydrolase domain; Acyl ...
 19-195 9.08e-13

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: 64.93  E-value: 9.08e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596029  19 CNCTIIGDPLTRKAIVVDPGGDHELILQRLDRLGL---QVVSIIHTHAHLDHflaSGEMKKRTGASLHLHKDD------- 88
Cdd:cd07729  50 FHPDAADDPGGLELAFPPGVTEEQTLEEQLARLGLdpeDIDYVILSHLHFDH---AGGLDLFPNATIIVQRAEleyatgp 126

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596029  89 -----QFLWDNLEMQCQLFGVPYTPVPapdrwlaDDEELACGCgVALHTPGHTPGSMSFWF--PRAKLLIAGDTL-FRRG 160
Cdd:cd07729 127 dplaaGYYEDVLALDDDLPGGRVRLVD-------GDYDLFPGV-TLIPTPGHTPGHQSVLVrlPEGTVLLAGDAAyTYEN 198

                       170       180       190
                ....*....|....*....|....*....|....*....
gi 15596029 161 I--GRTDLWGGDSAAIQRSIRqRLYSL--DEDATVVAGH 195
Cdd:cd07729 199 LeeGRPPGINYDPEAALASLE-RLKALaeREGARVIPGH 236
BJP-1_FEZ-1-like_MBL-B3 cd16288
BJP-1, FEZ-1, GOB-1, Mbl1b and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 43-145 4.48e-12

BJP-1, FEZ-1, GOB-1, Mbl1b and related metallo-beta-lactamases, subclass B3; MBL-fold metallo-hydrolase domain; This subgroup of B3 subclass MBLs includes Bradyrhizobium diazoefficiens BJP-1, Fluoribacter gormanii FEZ-1, Elizabethkingia meningoseptica (Chryseobacterium meningosepticum) GOB-1, Caulobacter crescentus Mbl1b. 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. These B3 enzymes have a modified Zn2/DCH site (Asp-His-His).


Pssm-ID: 293846 [Multi-domain]  Cd Length: 254  Bit Score: 63.11  E-value: 4.48e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596029  43 LILQRLDRLGL---QVVSIIHTHAHLDHFLASGEMKKRTGASLHLHKDD----------QFLWDNLEMqcqlfgvPYTPV 109
Cdd:cd16288  46 MIKANIRKLGFkpsDIKILLNSHAHLDHAGGLAALKKLTGAKLMASAEDaallasggksDFHYGDDSL-------AFPPV 118

                        90       100       110
                ....*....|....*....|....*....|....*....
gi 15596029 110 PApDRWLADDEELACGcGV---ALHTPGHTPGSMSFWFP 145
Cdd:cd16288 119 KV-DRVLKDGDRVTLG-GTtltAHLTPGHTRGCTTWTMT 155
TTHA1429-like_MBL-fold cd07725
uncharacterized Thermus thermophilus TTHA1429 and related proteins; MBL-fold metallo hydrolase ...
 11-196 4.71e-12

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: 61.93  E-value: 4.71e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596029  11 TFPVGPLqcNCTIIGDPLTRkaIVVDPG----GDHELILQRLDRLGLQVVSI---IHTHAHLDHFLASGEMKKrtgaslh 83
Cdd:cd07725   9 PGPLGHV--NVYLLRDGDET--TLIDTGlateEDAEALWEGLKELGLKPSDIdrvLLTHHHPDHIGLAGKLQE------- 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596029  84 lhkddqflwdnlEMQCQLFGVPYTPVPAPDRWLADDEELacgcgVALHTPGHTPGSMSFWFPRAKLLIAGDTLFRR---- 159
Cdd:cd07725  78 ------------KSGATVYILDVTPVKDGDKIDLGGLRL-----KVIETPGHTPGHIVLYDEDRRELFVGDAVLPKitpn 140

                       170       180       190
                ....*....|....*....|....*....|....*..
gi 15596029 160 GIGRTDLWGGDSAAIQRSIRqRLYSLDEDaTVVAGHG 196
Cdd:cd07725 141 VSLWAVRVEDPLGAYLESLD-KLEKLDVD-LAYPGHG 175
metallo-hydrolase-like_MBL-fold cd07743
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 30-157 8.05e-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) 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: 61.78  E-value: 8.05e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596029  30 RKAIVVDPGGDHEL---ILQRLDRLGLQVVSIIHTHAHLDHFLASGEMKKRTGASLHLHKDDQFLWDN--LEMQCqLFGv 104
Cdd:cd07743  18 KEALLIDSGLDEDAgrkIRKILEELGWKLKAIINTHSHADHIGGNAYLQKKTGCKVYAPKIEKAFIENplLEPSY-LGG- 95

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15596029 105 pYTPVPAP------------DRWLADDEELACGCGV-ALHTPGHTPGSMSFWFPrAKLLIAGDTLF 157
Cdd:cd07743  96 -AYPPKELrnkflmakpskvDDIIEEGELELGGVGLeIIPLPGHSFGQIGILTP-DGVLFAGDALF 159
MBLAC2-like_MBL-fold cd07712
uncharacterized human metallo-beta-lactamase domain-containing protein 2 and related proteins; ...
 29-156 8.98e-12

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: 61.11  E-value: 8.98e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596029  29 TRKAIVVDPG-GDHEL--ILQRLDRLGLQVVSiihTHAHLDHFLASGEMKKRtgaslHLHKDD------QFLWDNLEMQC 99
Cdd:cd07712  17 RDRALLIDTGlGIGDLkeYVRTLTDLPLLVVA---THGHFDHIGGLHEFEEV-----YVHPADaeilaaPDNFETLTWDA 88

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 15596029 100 QLFGVPYTPvpaPDRWLADDEELACG--CGVALHTPGHTPGSMSFWFPRAKLLIAGDTL 156
Cdd:cd07712  89 ATYSVPPAG---PTLPLRDGDVIDLGdrQLEVIHTPGHTPGSIALLDRANRLLFSGDVV 144
PLN02398 PLN02398
hydroxyacylglutathione hydrolase
 34-195 1.38e-11

hydroxyacylglutathione hydrolase


Pssm-ID: 215223 [Multi-domain]  Cd Length: 329  Bit Score: 62.55  E-value: 1.38e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596029   34 VVDPGgDHELILQRLDRLGLQVVSIIHTHAHLDHFLASGEMKKRTGASL---HLHKD-----DQFLWDNlemqcqlfgvp 105
Cdd:PLN02398 102 VVDPS-EAVPVIDALSRKNRNLTYILNTHHHYDHTGGNLELKARYGAKVigsAVDKDripgiDIVLKDG----------- 169

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596029  106 ytpvpapDRWLADDEELacgcgVALHTPGHTPGSMSFWFPRAKLLIAGDTLFRRGIGRtdLWGGDSAAIQRSIrQRLYSL 185
Cdd:PLN02398 170 -------DKWMFAGHEV-----LVMETPGHTRGHISFYFPGSGAIFTGDTLFSLSCGK--LFEGTPEQMLSSL-QKIISL 234

                        170
                 ....*....|
gi 15596029  186 DEDATVVAGH 195
Cdd:PLN02398 235 PDDTNIYCGH 244
Mbl1b-like_MBL-B3 cd16310
Caulobacter crescentus Mbl1b and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 30-143 3.26e-11

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: 60.93  E-value: 3.26e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596029  30 RKAIVVDPGGDH--ELILQRLDRLGLQ---VVSIIHTHAHLDHFLASGEMKKRTGASLHLHKDD-------QFLWDNLem 97
Cdd:cd16310  31 HGAILLDGGLEEnaALIEQNIKALGFKlsdIKIIINTHAHYDHAGGLAQLKADTGAKLWASRGDrpaleagKHIGDNI-- 108

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
gi 15596029  98 qcqLFGVPYTPVpAPDRWLADDEELACGcGVALH---TPGHTPGSMSfW 143
Cdd:cd16310 109 ---TQPAPFPAV-KVDRILGDGEKIKLG-DITLTatlTPGHTKGCTT-W 151
GOB1-like_MBL-B3 cd16308
Elizabethkingia meningoseptica GOB-1 and related metallo-beta-lactamases, subclass B3; ...
 43-152 6.71e-11

Elizabethkingia meningoseptica GOB-1 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 GOB-1-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: 293866 [Multi-domain]  Cd Length: 254  Bit Score: 59.79  E-value: 6.71e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596029  43 LILQRLDRLGLQVVSI---IHTHAHLDHFLASGEMKKRTGASLHLH-KDDQFLWD--NLEMQCQLFGVPYTPVpAPDRWL 116
Cdd:cd16308  46 LIKKNIQALGFKFKDIkilLTTQAHYDHVGAMAAIKQQTGAKMMVDeKDAKVLADggKSDYEMGGYGSTFAPV-KADKLL 124

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 15596029 117 ADDEELACGCG--VALHTPGHTPGSMSFWFP-----RA-KLLIA 152
Cdd:cd16308 125 HDGDTIKLGGTklTLLHHPGHTKGSCSFLFDvkdekRTyRVLIA 168
MBLAC1-like_MBL-fold cd07711
uncharacterized human metallo-beta-lactamase domain-containing protein 1 and related proteins; ...
 19-197 1.64e-10

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: 57.98  E-value: 1.64e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596029  19 CNCTIIGDPLTRkaIVVDPGG--DHELILQRLDRLGL---QVVSIIHTHAHLDHFLASGEMKKrtgASLHLHKDdqfLWD 93
Cdd:cd07711  22 STVTLIKDGGKN--ILVDTGTpwDRDLLLKALAEHGLspeDIDYVVLTHGHPDHIGNLNLFPN---ATVIVGWD---ICG 93

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596029  94 NLEMQCQLFGVpytpvpapdrwlaDDEELACGCGVaLHTPGHTPGSMSFWFPRAKL---LIAGDTLFRRG-IGRTDLWGG 169
Cdd:cd07711  94 DSYDDHSLEEG-------------DGYEIDENVEV-IPTPGHTPEDVSVLVETEKKgtvAVAGDLFEREEdLEDPILWDP 159

                       170       180       190
                ....*....|....*....|....*....|
gi 15596029 170 DSA--AIQRSIRQRLysLDEDATVVAGHGP 197
Cdd:cd07711 160 LSEdpELQEESRKRI--LALADWIIPGHGP 187
PLN02469 PLN02469
hydroxyacylglutathione hydrolase
 10-212 2.18e-10

hydroxyacylglutathione hydrolase


Pssm-ID: 178088 [Multi-domain]  Cd Length: 258  Bit Score: 58.62  E-value: 2.18e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596029   10 ETFPVGPLQCNCT-IIGDPLTRKAIVVDPGgDHELILQRLDRLGLQVVSIIHTHAHLDHFLASGEMKKrtgaslhlhkdd 88
Cdd:PLN02469   2 KIIPVPCLEDNYAyLIIDESTKDAAVVDPV-DPEKVLQAAHEHGAKIKLVLTTHHHWDHAGGNEKIKK------------ 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596029   89 qflwdnLEMQCQLFGVPYTPVPAPDRWLADDEELACGCGV---ALHTPGHTPGSMSFWFPRAK----LLIAGDTLFRRGI 161
Cdd:PLN02469  69 ------LVPGIKVYGGSLDNVKGCTHPVENGDKLSLGKDVnilALHTPCHTKGHISYYVTGKEgedpAVFTGDTLFIAGC 142

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596029  162 GRtdLWGGDSAAIQRSIRQRLYSLDEDATVVAGH-------------GPD-----------------------TTLGEEM 205
Cdd:PLN02469 143 GK--FFEGTAEQMYQSLCVTLGSLPKPTQVYCGHeytvknlkfaltvEPDneklkqklewaekqrqaglptvpSTIEEEL 220


                 ....*..
gi 15596029  206 RENPFVR 212
Cdd:PLN02469 221 ETNPFMR 227
ST1585-like_MBL-fold cd07726
uncharacterized subgroup which includes Sulfolobus tokodaii ST1585 protein; MBL-fold metallo ...
 31-155 3.08e-09

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: 54.81  E-value: 3.08e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596029  31 KAIVVDPGGDH--ELILQRLDRLGLQVVSIIH---THAHLDHFLASGE-MKKRTGASLHLH-------KDDQFLWDNLEM 97
Cdd:cd07726  26 RPALIDTGPSSsvPRLLAALEALGIAPEDVDYiilTHIHLDHAGGAGLlAEALPNAKVYVHprgarhlIDPSKLWASARA 105

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15596029  98 ----QCQLFGVPYTPVPAPD-RWLADDEELACGCG--VALHTPGHTPGSMSFWFPRAKLLIAGDT 155
Cdd:cd07726 106 vygdEADRLGGEILPVPEERvIVLEDGETLDLGGRtlEVIDTPGHAPHHLSFLDEESDGLFTGDA 170
L1_POM-1-like_MBL-B3 cd16289
Stenotrophomonas maltophilia L1, Pseudomonas otitidis POM-1 and related ...
 32-142 4.16e-09

Stenotrophomonas maltophilia L1, Pseudomonas otitidis POM-1 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 L1- and Pom-1-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: 293847  Cd Length: 239  Bit Score: 54.82  E-value: 4.16e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596029  32 AIVVDPG----GDHelILQRLDRLGL---QVVSIIHTHAHLDHFLASGEMKKRTGASLHLHKDDQFLWDNLEMQCQLFG- 103
Cdd:cd16289  33 AVLLDGGmpqaADM--LLDNMRALGVapgDLKLILHSHAHADHAGPLAALKRATGARVAANAESAVLLARGGSDDIHFGd 110

                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
gi 15596029 104 -VPYTPVPApDRWLADDEELACGcGVAL---HTPGHTPGSMSF 142
Cdd:cd16289 111 gITFPPVQA-DRIVMDGEVVTLG-GVTFtahFTPGHTPGSTSW 151
AIM-1_SMB-1-like_MBL-B3 cd16290
AIM-1, SMB-1, EVM-1, THIN-B and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 42-143 3.18e-07

AIM-1, SMB-1, EVM-1, THIN-B and related metallo-beta-lactamases, subclass B3; MBL-fold metallo-hydrolase domain; This subgroup of B3 subclass MBLs includes Pseudomonas Aeruginosa AIM-1, Serratia marcescens SMB-1, Erythrobacter vulgaris EVM-1, and Janthinobacterium lividum THIN-B. 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 AIM-1-,SMB-1-, EVM-1-, 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: 293848 [Multi-domain]  Cd Length: 256  Bit Score: 49.27  E-value: 3.18e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596029  42 ELILQRLDRLGLQ---VVSIIHTHAHLDHFLASGEMKKRTGASL-------------HLHKDD-QFLWDNlemqcqlfgv 104
Cdd:cd16290  45 PQIEANIRALGFRledVKLILNSHAHFDHAGGIAALQRDSGATVaaspagaaalrsgGVDPDDpQAGAAD---------- 114

                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 15596029 105 PYTPVpAPDRWLADDEELACGcGVAL---HTPGHTPGSMSfW 143
Cdd:cd16290 115 PFPPV-AKVRVVADGEVVKLG-PLAVtahATPGHTPGGTS-W 153
MBL-B3-like cd07708
metallo-beta-lactamases, subclass B3; MBL-fold metallo-hydrolase domain; MBLs (class B of the ...
 58-143 4.52e-07

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: 49.08  E-value: 4.52e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596029  58 IIHTHAHLDHFLASGEMKKRTGASLHL------------HKDDQFLWDNLEmqcqlfgvpYTPVPAPDRWLADDEELACG 125
Cdd:cd07708  64 ILISHAHFDHAGGSAEIKKQTGAKVMAgaedvslllsggSSDFHYANDSST---------YFPQSTVDRAVHDGERVTLG 134

                        90       100
                ....*....|....*....|.
gi 15596029 126 cGVAL--H-TPGHTPGSMSfW 143
Cdd:cd07708 135 -GTVLtaHaTPGHTPGCTT-W 153
EVM-1-like_MBL-B3 cd16315
Erythrobacter vulgaris EVM-1 and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 42-147 8.41e-07

Erythrobacter vulgaris EVM-1 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 EVM-1-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: 293873 [Multi-domain]  Cd Length: 248  Bit Score: 48.11  E-value: 8.41e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596029  42 ELILQRLDRLGLQ---VVSIIHTHAHLDHFLASGEMKKRTGASL-------------HLHKDDQflwdnlemQCQLFGvP 105
Cdd:cd16315  45 PLVLANIRKLGFDpkdVRWLLSSHEHFDHVGGLAALQRATGARVaasaaaapvlesgKPAPDDP--------QAGLHE-P 115

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 15596029 106 YTPVPApDRWLADDEELACGCGV--ALHTPGHTPGSMSfWFPRA 147
Cdd:cd16315 116 FPPVRV-DRIVEDGDTVALGSLRltAHATPGHTPGALS-WTWRS 157
OPHC2-like_MBL-fold cd07720
Pseudomonas pseudoalcaligenes organophosphorus hydrolase C2, and related proteins; MBL-fold ...
 44-157 9.81e-07

Pseudomonas pseudoalcaligenes organophosphorus hydrolase C2, and related proteins; MBL-fold metallo hydrolase domain; Pseudomonas pseudoalcaligenes OPHC2 is a thermostable organophosphorus hydrolase which a broad substrate activity spectrum: it hydrolyzes various phosphotriesters, esters, and a lactone. This subgroup also includes Pseudomonas oleovorans PoOPH which exhibits high lactonase and esterase activities, and latent PTE activity. However, double mutations His250Ile/Ile263Trp switch PoOPH into an efficient and thermostable PTE. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions.


Pssm-ID: 293806 [Multi-domain]  Cd Length: 251  Bit Score: 47.93  E-value: 9.81e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596029  44 ILQRLDRLGL---QVVSIIHTHAHLDHF---LASGEMKKRTGASLHLHK-------DDQFLWDNLEMQCQLFGV------ 104
Cdd:cd07720  78 LLANLAAAGIdpeDIDDVLLTHLHPDHIgglVDAGGKPVFPNAEVHVSEaewdfwlDDANAAKAPEGAKRFFDAardrlr 157

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*
gi 15596029 105 PYtpvpAPDRWLADDEELACGCgVALHTPGHTPGSMSFWF--PRAKLLIAGDTLF 157
Cdd:cd07720 158 PY----AAAGRFEDGDEVLPGI-TAVPAPGHTPGHTGYRIesGGERLLIWGDIVH 207
LACTB2-like_MBL-fold cd07722
uncharacterized subgroup which includes human lactamase beta 2 and related proteins; MBL-fold ...
 20-155 1.17e-06

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: 47.14  E-value: 1.17e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596029  20 NCTIIGDPLTRkaIVVDPG-GDHELI--LQR-LDRLGLQVVS-IIHTHAHLDHFLASGEMKKR-TGASLHLHKddqFLWD 93
Cdd:cd07722  19 NTYLVGTGKRR--ILIDTGeGRPSYIplLKSvLDSEGNATISdILLTHWHHDHVGGLPDVLDLlRGPSPRVYK---FPRP 93

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15596029  94 NLEMQCQLFGVPYTPvpapdrwLADDEELACGcGV---ALHTPGHTPGSMSFWFPRAKLLIAGDT 155
Cdd:cd07722  94 EEDEDPDEDGGDIHD-------LQDGQVFKVE-GAtlrVIHTPGHTTDHVCFLLEEENALFTGDC 150
metallo-hydrolase-like_MBL-fold cd07739
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 12-195 1.51e-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: 293825 [Multi-domain]  Cd Length: 201  Bit Score: 46.73  E-value: 1.51e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596029  12 FPVgplqcNCTII-GDpltRKAIVVDPG---GDHELILQRLDRLGLQVVSIIHTHAHLDHFLASGEMKKR---------- 77
Cdd:cd07739  14 FPV-----TSTLIyGE---TEAVLVDAQftrADAERLADWIKASGKTLTTIYITHGHPDHYFGLEVLLEAfpdakvvatp 85

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596029  78 -TGASLHLHKDDQFLWDNLEMQCQlfgVPYTPVpAPDRWLADDEELAcGCGVALHTPGH--TPGSMSFWFPRAKLLIAGD 154
Cdd:cd07739  86 aVVAHIKAQLEPKLAFWGPLLGGN---APARLV-VPEPLDGDTLTLE-GHPLEIVGVGGgdTDDTTYLWIPSLKTVVAGD 160

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 15596029 155 TLFrrgiGRTDLWGGDSAAIQrSIRQRLYSLDEDA-----TVVAGH 195
Cdd:cd07739 161 VVY----NGVHVWLADATTPE-LRAAWLAALDKIEalnpeTVVPGH 201
BJP-1-like_MBL-B3 cd16309
Bradyrhizobium diazoefficiens BJP-1 and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 33-142 2.55e-06

Bradyrhizobium diazoefficiens BJP-1 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 BJP-1-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: 293867 [Multi-domain]  Cd Length: 252  Bit Score: 46.71  E-value: 2.55e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596029  33 IVVDPG--GDHELILQRLDRLGLQVVSI---IHTHAHLDHFLASGEMKKRTGASLHLHKDDQFLwdnLEMQCQLFG-VPY 106
Cdd:cd16309  34 ILIDGAmpQSTPLIKDNIKKLGFDVKDVkylLNTHAHFDHAGGLAELKKATGAQLVASAADKPL---LESGYVGSGdTKN 110

                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 15596029 107 TPVPA--PDRWLADDEELACGcGVAL--H-TPGHTPGSMSF 142
Cdd:cd16309 111 LQFPPvrVDRVIGDGDKVTLG-GTTLtaHlTPGHSPGCTSW 150
MBL-B1-B2-like cd07707
metallo-beta-lactamases; subclasses B1 and B2 and related proteins; MBL-fold metallo-hydrolase ...
 36-197 2.54e-05

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: 43.69  E-value: 2.54e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596029  36 DPGGDHELILQRLDRLGLQVVSIIHTHAHLDHflASG-EMKKRTGASLH-------LHKDDQFLWDNLEMQCQLFGVPYT 107
Cdd:cd07707  40 TPKTTKELIKEIEKVSQKPVTEVINTHFHTDR--AGGnAYLKERGAKTVstaltrdLAKSEWAEIVAFTRKGLPEYPDLG 117

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596029 108 PVPaPDRWLADDEELACGCGVALHT-PGHTPGSMSFWFPRAKLLIAGDTLFRRGIGrtDLWGGDSAAIQRSIRqRLYSLD 186
Cdd:cd07707 118 YEL-PDGVLDGDFNLQFGKVEAFYPgPAHTPDNIVVYFPQENVLYGGCIIKETDLG--NVADADVKEWPTSIE-RLKKRY 193

                       170
                ....*....|..
gi 15596029 187 EDA-TVVAGHGP 197
Cdd:cd07707 194 RNIkAVIPGHGE 205
metallo-hydrolase-like_MBL-fold cd16276
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 33-197 3.07e-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: 293834 [Multi-domain]  Cd Length: 188  Bit Score: 42.96  E-value: 3.07e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596029  33 IVVD-PGGDHELILQRLDRL-GLQVVSIIHTHAHLDHFLASGEMK---------KRTGASLHLHKDDQflwdnlemqcql 101
Cdd:cd16276  22 IVVDaPPSLGENLLAAIRKVtDKPVTHVVYSHNHADHIGGASIFKdegatiiahEATAELLKRNPDPK------------ 89

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596029 102 fgvpytpVPAPDRWLADDEELACGcGVAL----HTPGHTPGSMSFWFPRAKLLIAGDTLFrrgIGRTDLWG-GDSAAIQR 176
Cdd:cd16276  90 -------RPVPTVTFDDEYTLEVG-GQTLelsyFGPNHGPGNIVIYLPKQKVLMAVDLIN---PGWVPFFNfAGSEDIPG 158

                       170       180
                ....*....|....*....|...
gi 15596029 177 SIRQ--RLYSLDEDaTVVAGHGP 197
Cdd:cd16276 159 YIEAldELLEYDFD-TFVGGHGN 180
YmaE-like_MBL-fold cd07727
uncharacterized subgroup which includes Bacillus subtilis YmaE and related proteins; MBL-fold ...
 64-157 6.41e-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: 42.18  E-value: 6.41e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596029  64 HLDHFLASGEMKKRTGASLHLHKDDQflwdnlemqcqlfgvpyTPVPAPDRW--LADDEELACGCGVAL-HTPGHTPGSM 140
Cdd:cd07727  55 HRDDVADHAKWAERFGAKRIIHEDDV-----------------NAVTRPDEVivLWGGDPWELDPDLTLiPVPGHTRGSV 117

                        90
                ....*....|....*..
gi 15596029 141 SFWFPRAKLLIAGDTLF 157
Cdd:cd07727 118 VLLYKEKGVLFTGDHLA 134
BcII-like_MBL-B1 cd16304
Bacillus cereus Beta-lactamase 2 and related metallo-beta-lactamases, subclass B1; MBL-fold ...
 28-197 2.43e-04

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: 40.73  E-value: 2.43e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596029  28 LTRKAIV-VDPGGD----HELILQRLDRLGLQVVSIIHTHAHLDHFLASGEMKKRtgaslhlhkddqflwdnlemqcqlf 102
Cdd:cd16304  32 ETSKGVVlIDTPWDdeqtEELLDWIKKKLKKPVTLAIVTHAHDDRIGGIKALQKR------------------------- 86

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596029 103 GVP--YTPV----------PAPDRWLADDEELACGcGVALHT----PGHTPGSMSFWFPRAKLLIAG---DTLFRRGIGR 163
Cdd:cd16304  87 GIPvySTKLtaqlakkqgyPSPDGILKDDTTLKFG-NTKIETfypgEGHTADNIVVWLPQSKILFGGclvKSLEAKDLGN 165

                       170       180       190
                ....*....|....*....|....*....|....
gi 15596029 164 TDlwGGDSAAIQRSIRQRLYSLDEDATVVAGHGP 197
Cdd:cd16304 166 TA--DANLKEWPTSIRNVLKRYPNAEIVVPGHGE 197
AIM-1-like_MBL-B3 cd16314
Pseudomonas Aeruginosa AIM-1 and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 33-142 3.21e-04

Pseudomonas Aeruginosa AIM-1 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 AIM-1-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: 293872 [Multi-domain]  Cd Length: 255  Bit Score: 40.65  E-value: 3.21e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596029  33 IVVDPGGDH--ELILQRLDRLGLQ---VVSIIHTHAHLDHFLASGEMKKRTGASL-------------HLHKDD-QFlwd 93
Cdd:cd16314  34 ILIDGGTDKaaPLIEANIRALGFRpedVRYIVSSHEHFDHAGGIARLQRATGAPVvarepaattlergRSDRSDpQF--- 110

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 15596029  94 nlemqcqLFGVPYTPVpAPDRWLADDEELACG--CGVALHTPGHTPGSMSF 142
Cdd:cd16314 111 -------LVVEKFPPV-ASVQRIGDGEVLRVGplALTAHATPGHTPGGTSW 153
FEZ-1-like_MBL-B3 cd16307
Fluoribacter gormanii FEZ-1 and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 43-138 3.95e-04

Fluoribacter gormanii FEZ-1 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 FEZ-1-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: 293865  Cd Length: 255  Bit Score: 40.12  E-value: 3.95e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596029  43 LILQRLDRLGLQVVS---IIHTHAHLDHFLASGEMKKRTGASLHLH-----------KDDQFLWDNLEMQcqlfgvpYTP 108
Cdd:cd16307  46 QIKASIEKLGFKFSDtkiLLISHAHFDHAAGSALIKRETHAKYMVMdgdvdvvesggKSDFFYGNDPSTY-------FPP 118

                        90       100       110
                ....*....|....*....|....*....|...
gi 15596029 109 VPApDRWLADDEELACGcGVAL--H-TPGHTPG 138
Cdd:cd16307 119 AHV-DKVLHDGEQVELG-GTVLtaHlTAGHTKG 149
MBL-B1 cd16285
metallo-beta-lactamases, subclass B1; MBL-fold metallo-hydrolase domain; MBLs (class B of the ...
 49-196 1.45e-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: 38.42  E-value: 1.45e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596029  49 DRLGLQVVSIIHTHAHLDhflasgemkkRTGASLHLHKDDQFLWDNlEMQCQLFGVPYTPVPAPDrwLADDEELACGcGV 128
Cdd:cd16285  58 KKLGKPVTAAISTHSHDD----------RTGGIKALNARGIPTYAT-ALTNELAKKEGKPVPTHS--LKGALTLGFG-PL 123

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15596029 129 ALHTPG--HTPGSMSFWFPRAKLLIAGdtLFRRGIGRTDLW---GGDSAAIQRSIR--QRLYSldEDATVVAGHG 196
Cdd:cd16285 124 EVFYPGpgHTPDNIVVWLPKSKILFGG--CLVKSASATSLGnvgDADVEAWPKSIEnlKAKYP--EARMVVPGHG 194
 
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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