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Conserved domains on  [gi|1232081121|gb|OYU29728|]
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MBL fold metallo-hydrolase [Comamonadaceae bacterium PBBC2]

Protein Classification

MBL fold metallo-hydrolase( domain architecture ID 10869981)

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
POD-like_MBL-fold cd07724
ETHE1 (PDO type I), persulfide dioxygenase A (PDOA, PDO type II) and related proteins; ...
 2-183 1.00e-67

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: 206.48  E-value: 1.00e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232081121   2 FFKQLPTHE-ASLSYFFGCAGYGlavavdvvaadE-----------DWFIEQARLNQVRITHVIDTHIHADHYTGGRELA 69
Cdd:cd07724     1 IFRQFFDPGlGTLSYLVGDPETG-----------EaavidpvrdsvDRYLDLAAELGLKITYVLETHVHADHVSGARELA 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232081121  70 RRTGAPYCLHEDArnSVKFGYQPLTDGQVLALGNVQVQVMHTPGHTLDSICLLVSDarrgpePWFVITGDTLFVGAVGRP 149
Cdd:cd07724    70 ERTGAPIVIGEGA--PASFFDRLLKDGDVLELGNLTLEVLHTPGHTPESVSYLVGD------PDAVFTGDTLFVGDVGRP 141

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1232081121 150 DLAGRELEMAGLLHQSLHDKLLRLPAGLEIYPGH 183
Cdd:cd07724   142 DLPGEAEGLARQLYDSLQRKLLLLPDETLVYPGH 175
 
Name Accession Description Interval E-value
POD-like_MBL-fold cd07724
ETHE1 (PDO type I), persulfide dioxygenase A (PDOA, PDO type II) and related proteins; ...
 2-183 1.00e-67

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: 206.48  E-value: 1.00e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232081121   2 FFKQLPTHE-ASLSYFFGCAGYGlavavdvvaadE-----------DWFIEQARLNQVRITHVIDTHIHADHYTGGRELA 69
Cdd:cd07724     1 IFRQFFDPGlGTLSYLVGDPETG-----------EaavidpvrdsvDRYLDLAAELGLKITYVLETHVHADHVSGARELA 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232081121  70 RRTGAPYCLHEDArnSVKFGYQPLTDGQVLALGNVQVQVMHTPGHTLDSICLLVSDarrgpePWFVITGDTLFVGAVGRP 149
Cdd:cd07724    70 ERTGAPIVIGEGA--PASFFDRLLKDGDVLELGNLTLEVLHTPGHTPESVSYLVGD------PDAVFTGDTLFVGDVGRP 141

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1232081121 150 DLAGRELEMAGLLHQSLHDKLLRLPAGLEIYPGH 183
Cdd:cd07724   142 DLPGEAEGLARQLYDSLQRKLLLLPDETLVYPGH 175
GloB COG0491
Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General ...
 36-183 2.36e-33

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: 119.80  E-value: 2.36e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232081121  36 DWFIEQARLNQVRITHVIDTHIHADHYTGGRELARRTGAPYCLHEDAR-------NSVKFGYQP------LTDGQVLALG 102
Cdd:COG0491    39 EALLAALAALGLDIKAVLLTHLHPDHVGGLAALAEAFGAPVYAHAAEAealeapaAGALFGREPvppdrtLEDGDTLELG 118

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232081121 103 NVQVQVMHTPGHTLDSICLLVsdarrgPEPWFVITGDTLFVGAVGRPDLAGRELEMaglLHQSLhDKLLRLPAGLeIYPG 182
Cdd:COG0491   119 GPGLEVIHTPGHTPGHVSFYV------PDEKVLFTGDALFSGGVGRPDLPDGDLAQ---WLASL-ERLLALPPDL-VIPG 187


                  .
gi 1232081121 183 H 183
Cdd:COG0491   188 H 188
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 35-183 9.20e-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: 99.16  E-value: 9.20e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232081121   35 EDWFIEQARLNQVRITHVIDTHIHADHYTGGRELARRTGAPYCLHEDARNSVKFG----------------YQPLTDGQV 98
Cdd:smart00849  22 EDLLAELKKLGPKKIDAIILTHGHPDHIGGLPELLEAPGAPVYAPEGTAELLKDLlallgelgaeaepappDRTLKDGDE 101

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232081121   99 LALGNVQVQVMHTPGHTLDSICLLVSDARrgpepwFVITGDTLFVGAVGRPDLAGRELEMAGLLHqSLHDKLLRLPAglE 178
Cdd:smart00849 102 LDLGGGELEVIHTPGHTPGSIVLYLPEGK------ILFTGDLLFAGGDGRTLVDGGDAAASDALE-SLLKLLKLLPK--L 172


                   ....*
gi 1232081121  179 IYPGH 183
Cdd:smart00849 173 VVPGH 177
PLN02962 PLN02962
hydroxyacylglutathione hydrolase
 47-241 4.55e-23

hydroxyacylglutathione hydrolase


Pssm-ID: 178547 [Multi-domain]  Cd Length: 251  Bit Score: 93.71  E-value: 4.55e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232081121  47 VRITHVIDTHIHADHYTGGRELarRTGAPYCLHEDARNSVKFGYQPLTDGQVLALGNVQVQVMHTPGHTLDSICLLVSDA 126
Cdd:PLN02962   60 LKLIYAMNTHVHADHVTGTGLL--KTKLPGVKSIISKASGSKADLFVEPGDKIYFGDLYLEVRATPGHTAGCVTYVTGEG 137

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232081121 127 RRGPEPWFVITGDTLFVGAVGRPDLAGRElemAGLLHQSLHDKLLRLPAGLEIYPGHQagsacgagISGKPSSTIGFEQR 206
Cdd:PLN02962  138 PDQPQPRMAFTGDALLIRGCGRTDFQGGS---SDQLYKSVHSQIFTLPKDTLIYPAHD--------YKGFTVSTVGEEML 206

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1232081121 207 WNPFLSMDQETFVREVT-ANLPeRPAHMDHIVAANI 241
Cdd:PLN02962  207 YNPRLTKDEETFKTIMEnLNLP-YPKMIDVAVPANM 241
Lactamase_B pfam00753
Metallo-beta-lactamase superfamily;
37-183 2.78e-13

Metallo-beta-lactamase superfamily;


Pssm-ID: 425851 [Multi-domain]  Cd Length: 196  Bit Score: 66.24  E-value: 2.78e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232081121  37 WFIEQARLNQVRITHVIDTHIHADHYTGGRELARRTGAP-YCLHEDARNSVKFGYQP--------------------LTD 95
Cdd:pfam00753  32 LLLAALGLGPKDIDAVILTHGHFDHIGGLGELAEATDVPvIVVAEEARELLDEELGLaasrlglpgppvvplppdvvLEE 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232081121  96 GQVLALGNVQVQVMHTPGHTLDSICLLVSDARrgpepwFVITGDTLFVGAVGRPDLAGRELE-MAGLLHQSLHDKLLRL- 173
Cdd:pfam00753 112 GDGILGGGLGLLVTHGPGHGPGHVVVYYGGGK------VLFTGDLLFAGEIGRLDLPLGGLLvLHPSSAESSLESLLKLa 185

                         170
                  ....*....|.
gi 1232081121 174 -PAGLEIYPGH 183
Cdd:pfam00753 186 kLKAAVIVPGH 196
 
Name Accession Description Interval E-value
POD-like_MBL-fold cd07724
ETHE1 (PDO type I), persulfide dioxygenase A (PDOA, PDO type II) and related proteins; ...
 2-183 1.00e-67

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: 206.48  E-value: 1.00e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232081121   2 FFKQLPTHE-ASLSYFFGCAGYGlavavdvvaadE-----------DWFIEQARLNQVRITHVIDTHIHADHYTGGRELA 69
Cdd:cd07724     1 IFRQFFDPGlGTLSYLVGDPETG-----------EaavidpvrdsvDRYLDLAAELGLKITYVLETHVHADHVSGARELA 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232081121  70 RRTGAPYCLHEDArnSVKFGYQPLTDGQVLALGNVQVQVMHTPGHTLDSICLLVSDarrgpePWFVITGDTLFVGAVGRP 149
Cdd:cd07724    70 ERTGAPIVIGEGA--PASFFDRLLKDGDVLELGNLTLEVLHTPGHTPESVSYLVGD------PDAVFTGDTLFVGDVGRP 141

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1232081121 150 DLAGRELEMAGLLHQSLHDKLLRLPAGLEIYPGH 183
Cdd:cd07724   142 DLPGEAEGLARQLYDSLQRKLLLLPDETLVYPGH 175
metallo-hydrolase-like_MBL-fold cd06262
mainly hydrolytic enzymes and related proteins which carry out various biological functions; ...
 35-183 2.11e-33

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: 119.31  E-value: 2.11e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232081121  35 EDWFIEQARLNQVRITHVIDTHIHADHYTGGRELARRTGAPYCLHED--------ARNSVKFGYQP---------LTDGQ 97
Cdd:cd06262    32 LEKILEAIEELGLKIKAILLTHGHFDHIGGLAELKEAPGAPVYIHEAdaelledpELNLAFFGGGPlpppepdilLEDGD 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232081121  98 VLALGNVQVQVMHTPGHTLDSICLLVsdarrgPEPWFVITGDTLFVGAVGRPDLAGRELEmagLLHQSLHDKLLRLPAGL 177
Cdd:cd06262   112 TIELGGLELEVIHTPGHTPGSVCFYI------EEEGVLFTGDTLFAGSIGRTDLPGGDPE---QLIESIKKLLLLLPDDT 182


                  ....*.
gi 1232081121 178 EIYPGH 183
Cdd:cd06262   183 VVYPGH 188
GloB COG0491
Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General ...
 36-183 2.36e-33

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: 119.80  E-value: 2.36e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232081121  36 DWFIEQARLNQVRITHVIDTHIHADHYTGGRELARRTGAPYCLHEDAR-------NSVKFGYQP------LTDGQVLALG 102
Cdd:COG0491    39 EALLAALAALGLDIKAVLLTHLHPDHVGGLAALAEAFGAPVYAHAAEAealeapaAGALFGREPvppdrtLEDGDTLELG 118

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232081121 103 NVQVQVMHTPGHTLDSICLLVsdarrgPEPWFVITGDTLFVGAVGRPDLAGRELEMaglLHQSLhDKLLRLPAGLeIYPG 182
Cdd:COG0491   119 GPGLEVIHTPGHTPGHVSFYV------PDEKVLFTGDALFSGGVGRPDLPDGDLAQ---WLASL-ERLLALPPDL-VIPG 187


                  .
gi 1232081121 183 H 183
Cdd:COG0491   188 H 188
hydroxyacylglutathione_hydrolase_MBL-fold cd07723
hydroxyacylglutathione hydrolase, MBL-fold metallo-hydrolase domain; hydroxyacylglutathione ...
 39-183 4.26e-30

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: 109.86  E-value: 4.26e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232081121  39 IEQARLNQVRITHVIDTHIHADHyTGG-RELARRTG-APYCLHEDARnsVKFGYQPLTDGQVLALGNVQVQVMHTPGHTL 116
Cdd:cd07723    34 LAALEKNGLTLTAILTTHHHWDH-TGGnAELKALFPdAPVYGPAEDR--IPGLDHPVKDGDEIKLGGLEVKVLHTPGHTL 110

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1232081121 117 DSICLLVSDARrgpepwFVITGDTLFVGAVGRPDLaGRELEMagllHQSLhDKLLRLPAGLEIYPGH 183
Cdd:cd07723   111 GHICYYVPDEP------ALFTGDTLFSGGCGRFFE-GTAEQM----YASL-QKLLALPDDTLVYCGH 165
TTHA1623-like_MBL-fold cd16322
uncharacterized Thermus thermophilus TTHA1623 and related proteins; MBL-fold metallo hydrolase ...
 44-211 9.10e-28

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: 105.12  E-value: 9.10e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232081121  44 LNQVRITHVIDTHIHADHYTGGRELARRTGAPYCLHEDARN--------------SVKFGYQP---LTDGQVLALGNVQV 106
Cdd:cd16322    42 TTGLTLLYILLTHAHFDHVGGVADLRRHPGAPVYLHPDDLPlyeaadlgakafglGIEPLPPPdrlLEDGQTLTLGGLEF 121

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232081121 107 QVMHTPGHTLDSICLLVsdarrgPEPWFVITGDTLFVGAVGRPDLAGRelemAGLLHQSLHDKLLRLPAGLEIYPGHQag 186
Cdd:cd16322   122 KVLHTPGHSPGHVCFYV------EEEGLLFSGDLLFQGSIGRTDLPGG----DPKAMAASLRRLLTLPDETRVFPGHG-- 189

                         170       180
                  ....*....|....*....|....*
gi 1232081121 187 sacgagisgkPSSTIGFEQRWNPFL 211
Cdd:cd16322   190 ----------PPTTLGEERRTNPFL 204
BaeB-like_MBL-fold cd16275
Bacillus amyloliquefaciens BaeB and related proteins; MBL-fold metallo hydrolase domain; ...
 38-183 8.45e-26

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: 99.15  E-value: 8.45e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232081121  38 FIEQARLNQVRITHVIDTHIHADHYTGGRELARRTGAP-YCLHEDARNSvkfGYQ-----PLTDGQVLALGNVQVQVMHT 111
Cdd:cd16275    37 ILAKLNELGLTLTGILLTHSHFDHVNLVEPLLAKYDAPvYMSKEEIDYY---GFRcpnliPLEDGDTIKIGDTEITCLLT 113

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1232081121 112 PGHTLDSICLLVSDArrgpepwfVITGDTLFVGAVGRPDLAGRElemAGLLHQSLHdKLLRLPAG-LEIYPGH 183
Cdd:cd16275   114 PGHTPGSMCYLLGDS--------LFTGDTLFIEGCGRCDLPGGD---PEEMYESLQ-RLKKLPPPnTRVYPGH 174
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 35-183 9.20e-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: 99.16  E-value: 9.20e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232081121   35 EDWFIEQARLNQVRITHVIDTHIHADHYTGGRELARRTGAPYCLHEDARNSVKFG----------------YQPLTDGQV 98
Cdd:smart00849  22 EDLLAELKKLGPKKIDAIILTHGHPDHIGGLPELLEAPGAPVYAPEGTAELLKDLlallgelgaeaepappDRTLKDGDE 101

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232081121   99 LALGNVQVQVMHTPGHTLDSICLLVSDARrgpepwFVITGDTLFVGAVGRPDLAGRELEMAGLLHqSLHDKLLRLPAglE 178
Cdd:smart00849 102 LDLGGGELEVIHTPGHTPGSIVLYLPEGK------ILFTGDLLFAGGDGRTLVDGGDAAASDALE-SLLKLLKLLPK--L 172


                   ....*
gi 1232081121  179 IYPGH 183
Cdd:smart00849 173 VVPGH 177
PLN02962 PLN02962
hydroxyacylglutathione hydrolase
 47-241 4.55e-23

hydroxyacylglutathione hydrolase


Pssm-ID: 178547 [Multi-domain]  Cd Length: 251  Bit Score: 93.71  E-value: 4.55e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232081121  47 VRITHVIDTHIHADHYTGGRELarRTGAPYCLHEDARNSVKFGYQPLTDGQVLALGNVQVQVMHTPGHTLDSICLLVSDA 126
Cdd:PLN02962   60 LKLIYAMNTHVHADHVTGTGLL--KTKLPGVKSIISKASGSKADLFVEPGDKIYFGDLYLEVRATPGHTAGCVTYVTGEG 137

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232081121 127 RRGPEPWFVITGDTLFVGAVGRPDLAGRElemAGLLHQSLHDKLLRLPAGLEIYPGHQagsacgagISGKPSSTIGFEQR 206
Cdd:PLN02962  138 PDQPQPRMAFTGDALLIRGCGRTDFQGGS---SDQLYKSVHSQIFTLPKDTLIYPAHD--------YKGFTVSTVGEEML 206

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1232081121 207 WNPFLSMDQETFVREVT-ANLPeRPAHMDHIVAANI 241
Cdd:PLN02962  207 YNPRLTKDEETFKTIMEnLNLP-YPKMIDVAVPANM 241
metallo-hydrolase-like_MBL-fold cd16278
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 48-183 5.15e-21

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: 86.78  E-value: 5.15e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232081121  48 RITHVIDTHIHADHYTGGRELARRTGAP-YCLHEDARNSVKFGYQP---LTDGQVLALGNVQVQVMHTPGHTLDSICLLV 123
Cdd:cd16278    53 RVSAILVTHTHRDHSPGAARLAERTGAPvRAFGPHRAGGQDTDFAPdrpLADGEVIEGGGLRLTVLHTPGHTSDHLCFAL 132

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1232081121 124 SDARRgpepwfVITGDTLFVGA---VGRPDlaGReleMAGLLhQSLhDKLLRLPAGLeIYPGH 183
Cdd:cd16278   133 EDEGA------LFTGDHVMGWSttvIAPPD--GD---LGDYL-ASL-ERLLALDDRL-LLPGH 181
YcbL-like_MBL-fold cd07737
Salmonella enterica serovar typhimurium YcbL and related proteins; MBL-fold metallo hydrolase ...
 39-183 8.96e-18

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: 78.36  E-value: 8.96e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232081121  39 IEQARLNQVRITHVIDTHIHADHYTGGRELARRTGAP---------YCLHEDARNSVKFGYQP---------LTDGQVLA 100
Cdd:cd07737    37 LQAIEDLGLTLKKILLTHGHLDHVGGAAELAEHYGVPiigphkedkFLLENLPEQSQMFGFPPaeaftpdrwLEEGDTVT 116

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232081121 101 LGNVQVQVMHTPGHTLDSICLLVSDARrgpepwFVITGDTLFVGAVGRPDLAGRELEmagLLHQSLHDKLLRLPAGLEIY 180
Cdd:cd07737   117 VGNLTLEVLHCPGHTPGHVVFFNRESK------LAIVGDVLFKGSIGRTDFPGGNHA---QLIASIKEKLLPLGDDVTFI 187


                  ...
gi 1232081121 181 PGH 183
Cdd:cd07737   188 PGH 190
LACTB2-like_MBL-fold cd07722
uncharacterized subgroup which includes human lactamase beta 2 and related proteins; MBL-fold ...
 42-183 2.18e-16

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: 74.49  E-value: 2.18e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232081121  42 ARLNQVRITHVIDTHIHADHyTGG----RELARRTGA-----PYCLHEDARNSVKFGYQPLTDGQVLALGNVQVQVMHTP 112
Cdd:cd07722    50 DSEGNATISDILLTHWHHDH-VGGlpdvLDLLRGPSPrvykfPRPEEDEDPDEDGGDIHDLQDGQVFKVEGATLRVIHTP 128

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1232081121 113 GHTLDSICLLVsdarrgPEPWFVITGDT-LFVGAVGRPDLAgrelemagLLHQSLHdKLLRLPAGLeIYPGH 183
Cdd:cd07722   129 GHTTDHVCFLL------EEENALFTGDCvLGHGTAVFEDLA--------AYMASLK-KLLSLGPGR-IYPGH 184
PLN02469 PLN02469
hydroxyacylglutathione hydrolase
 39-227 1.71e-14

hydroxyacylglutathione hydrolase


Pssm-ID: 178088 [Multi-domain]  Cd Length: 258  Bit Score: 70.56  E-value: 1.71e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232081121  39 IEQARLNQVRITHVIDTHIHADHyTGGRELARRTGAPYCLHEDARNSVKFGYQPLTDGQVLALGN-VQVQVMHTPGHTLD 117
Cdd:PLN02469   37 LQAAHEHGAKIKLVLTTHHHWDH-AGGNEKIKKLVPGIKVYGGSLDNVKGCTHPVENGDKLSLGKdVNILALHTPCHTKG 115

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232081121 118 SICLLVsDARRGPEPwFVITGDTLFVGAVGRpDLAGRELEMagllHQSLHDKLLRLPAGLEIYPGHQAGS---------- 187
Cdd:PLN02469  116 HISYYV-TGKEGEDP-AVFTGDTLFIAGCGK-FFEGTAEQM----YQSLCVTLGSLPKPTQVYCGHEYTVknlkfaltve 188

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1232081121 188 ------------ACGAGISGKPS--STIGFEQRWNPFLSMDQETFVREVTANLP 227
Cdd:PLN02469  189 pdneklkqklewAEKQRQAGLPTvpSTIEEELETNPFMRVDLPEIQEKVGCESP 242
TTHA1429-like_MBL-fold cd07725
uncharacterized Thermus thermophilus TTHA1429 and related proteins; MBL-fold metallo hydrolase ...
 39-183 2.39e-14

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: 68.86  E-value: 2.39e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232081121  39 IEQARLNQVRITHVIDTHIHADHYTGGRELARRTGAP-YCLhedarnsvkfGYQPLTDGQVLALGNVQVQVMHTPGHTLD 117
Cdd:cd07725    46 LKELGLKPSDIDRVLLTHHHPDHIGLAGKLQEKSGATvYIL----------DVTPVKDGDKIDLGGLRLKVIETPGHTPG 115

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1232081121 118 SICLLVSDARRgpepwfVITGDTL--------FVGAVGRPDLAGRELEmagllhqSLhDKLLRLPAgLEIYPGH 183
Cdd:cd07725   116 HIVLYDEDRRE------LFVGDAVlpkitpnvSLWAVRVEDPLGAYLE-------SL-DKLEKLDV-DLAYPGH 174
yflN-like_MBL-fold cd07721
uncharacterized subgroup which includes Bacillus subtilis yflN; MBL-fold metallo hydrolase ...
 39-183 2.24e-13

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


Pssm-ID: 293807 [Multi-domain]  Cd Length: 202  Bit Score: 66.48  E-value: 2.24e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232081121  39 IEQARLNQVRITHVIDTHIHADHYTGGRELARRTGAP-YCLHEDAR-------------------------NSVKFGYQP 92
Cdd:cd07721    40 LRELGLSPKDIRRILLTHGHIDHIGSLAALKEAPGAPvYAHEREAPylegekpypppvrlgllgllspllpVKPVPVDRT 119

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232081121  93 LTDGQVLALGnVQVQVMHTPGHTLDSICLLVSDARrgpepwFVITGDTLFV---GAVGRPDLAGRELEMAgllHQSLHdK 169
Cdd:cd07721   120 LEDGDTLDLA-GGLRVIHTPGHTPGHISLYLEEDG------VLIAGDALVTvggELVPPPPPFTWDMEEA---LESLR-K 188

                         170
                  ....*....|....
gi 1232081121 170 LLRLPAGLeIYPGH 183
Cdd:cd07721   189 LAELDPEV-LAPGH 201
Lactamase_B pfam00753
Metallo-beta-lactamase superfamily;
37-183 2.78e-13

Metallo-beta-lactamase superfamily;


Pssm-ID: 425851 [Multi-domain]  Cd Length: 196  Bit Score: 66.24  E-value: 2.78e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232081121  37 WFIEQARLNQVRITHVIDTHIHADHYTGGRELARRTGAP-YCLHEDARNSVKFGYQP--------------------LTD 95
Cdd:pfam00753  32 LLLAALGLGPKDIDAVILTHGHFDHIGGLGELAEATDVPvIVVAEEARELLDEELGLaasrlglpgppvvplppdvvLEE 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232081121  96 GQVLALGNVQVQVMHTPGHTLDSICLLVSDARrgpepwFVITGDTLFVGAVGRPDLAGRELE-MAGLLHQSLHDKLLRL- 173
Cdd:pfam00753 112 GDGILGGGLGLLVTHGPGHGPGHVVVYYGGGK------VLFTGDLLFAGEIGRLDLPLGGLLvLHPSSAESSLESLLKLa 185

                         170
                  ....*....|.
gi 1232081121 174 -PAGLEIYPGH 183
Cdd:pfam00753 186 kLKAAVIVPGH 196
MBLAC2-like_MBL-fold cd07712
uncharacterized human metallo-beta-lactamase domain-containing protein 2 and related proteins; ...
 52-183 5.92e-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: 62.26  E-value: 5.92e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232081121  52 VIDTHIHADHYTGGRELARRTGAPY------------CLHEDARNSVKFGY---QPLTDGQVLALGNVQVQVMHTPGHTL 116
Cdd:cd07712    46 VVATHGHFDHIGGLHEFEEVYVHPAdaeilaapdnfeTLTWDAATYSVPPAgptLPLRDGDVIDLGDRQLEVIHTPGHTP 125

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1232081121 117 DSICLLvsDARRGpepwFVITGDTLFVGAVgRPDLAGRELEMaglLHQSLhDKLLRLPAGLE-IYPGH 183
Cdd:cd07712   126 GSIALL--DRANR----LLFSGDVVYDGPL-IMDLPHSDLDD---YLASL-EKLSKLPDEFDkVLPGH 182
PLN02398 PLN02398
hydroxyacylglutathione hydrolase
 49-184 5.60e-10

hydroxyacylglutathione hydrolase


Pssm-ID: 215223 [Multi-domain]  Cd Length: 329  Bit Score: 58.32  E-value: 5.60e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232081121  49 ITHVIDTHIHADHYTGGRELARRTGAPYCLHEDARNSVKFGYQPLTDGQVLALGNVQVQVMHTPGHTLDSICLLVSDARR 128
Cdd:PLN02398  122 LTYILNTHHHYDHTGGNLELKARYGAKVIGSAVDKDRIPGIDIVLKDGDKWMFAGHEVLVMETPGHTRGHISFYFPGSGA 201

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1232081121 129 gpepwfVITGDTLFVGAVGRPdLAGRELEMagllHQSLHdKLLRLPAGLEIYPGHQ 184
Cdd:PLN02398  202 ------IFTGDTLFSLSCGKL-FEGTPEQM----LSSLQ-KIISLPDDTNIYCGHE 245
metallo-hydrolase-like_MBL-fold cd16280
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 39-122 1.36e-09

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


Pssm-ID: 293838 [Multi-domain]  Cd Length: 251  Bit Score: 56.82  E-value: 1.36e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232081121  39 IEQARLNQVRITHVIDTHIHADHYTGGRELARRTGAP--------YCLHEDARNSVKFGYQP-------LTDGQVLALGN 103
Cdd:cd16280    52 LEKLGLDPADIKYILITHGHGDHYGGAAYLKDLYGAKvvmseadwDMMEEPPEEGDNPRWGPpperdivIKDGDTLTLGD 131

                          90
                  ....*....|....*....
gi 1232081121 104 VQVQVMHTPGHTLDSICLL 122
Cdd:cd16280   132 TTITVYLTPGHTPGTLSLI 150
YmaE-like_MBL-fold cd07727
uncharacterized subgroup which includes Bacillus subtilis YmaE and related proteins; MBL-fold ...
 49-148 8.19e-08

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: 50.66  E-value: 8.19e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232081121  49 ITHVIDTHIhaDHYTGGRELARRTGAPYCLHEDARNSVK--FGYQPLTDGQVLALGNvQVQVMHTPGHTLDSICLLVSDA 126
Cdd:cd07727    48 IRYIFLTHR--DDVADHAKWAERFGAKRIIHEDDVNAVTrpDEVIVLWGGDPWELDP-DLTLIPVPGHTRGSVVLLYKEK 124

                          90       100
                  ....*....|....*....|..
gi 1232081121 127 RrgpepwFVITGDTLFVGAVGR 148
Cdd:cd07727   125 G------VLFTGDHLAWSRRRG 140
metallo-hydrolase-like_MBL-fold cd16282
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 42-183 7.83e-07

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


Pssm-ID: 293840 [Multi-domain]  Cd Length: 209  Bit Score: 48.33  E-value: 7.83e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232081121  42 ARLNQVRITHVIDTHIHADHyTGGRELARRTGAPYCLHEDARNSVKFGY------------------------QPLTDGQ 97
Cdd:cd16282    46 RKVTDKPVRYVVNTHYHGDH-TLGNAAFADAGAPIIAHENTREELAARGeaylelmrrlggdamagtelvlpdRTFDDGL 124

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232081121  98 VLALGNVQVQVMHT-PGHTLDSICLLVSDARrgpepwFVITGDTLFVGAVGrPDLAGRELEMAGLLhqslhDKLLRLPAg 176
Cdd:cd16282   125 TLDLGGRTVELIHLgPAHTPGDLVVWLPEEG------VLFAGDLVFNGRIP-FLPDGSLAGWIAAL-----DRLLALDA- 191


                  ....*...
gi 1232081121 177 lEIY-PGH 183
Cdd:cd16282   192 -TVVvPGH 198
ST1585-like_MBL-fold cd07726
uncharacterized subgroup which includes Sulfolobus tokodaii ST1585 protein; MBL-fold metallo ...
 39-183 1.28e-06

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: 47.87  E-value: 1.28e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232081121  39 IEQARLNQVRITHVIDTHIHADHYTGGRELARRT----------GAPYC-----LHEDARNSV-----KFGYQP------ 92
Cdd:cd07726    45 LEALGIAPEDVDYIILTHIHLDHAGGAGLLAEALpnakvyvhprGARHLidpskLWASARAVYgdeadRLGGEIlpvpee 124

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232081121  93 ----LTDGQVLALGNVQVQVMHTPGHTLDSICLLVSDARrgpepwFVITGDTlfVGAVGRPDLAGR---------ELEMA 159
Cdd:cd07726   125 rvivLEDGETLDLGGRTLEVIDTPGHAPHHLSFLDEESD------GLFTGDA--AGVRYPELDVVGppstpppdfDPEAW 196

                         170       180
                  ....*....|....*....|....
gi 1232081121 160 gllHQSLhDKLLRLPAGLeIYPGH 183
Cdd:cd07726   197 ---LESL-DRLLSLKPER-IYLTH 215
MBLAC1-like_MBL-fold cd07711
uncharacterized human metallo-beta-lactamase domain-containing protein 1 and related proteins; ...
 49-139 1.32e-06

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: 47.20  E-value: 1.32e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232081121  49 ITHVIDTHIHADHYTGgreLARRTGAPYCLHEDARNSVKFGYQPLTDGQVLALGNVQVqvMHTPGHTLDSICLLVSDARR 128
Cdd:cd07711    61 IDYVVLTHGHPDHIGN---LNLFPNATVIVGWDICGDSYDDHSLEEGDGYEIDENVEV--IPTPGHTPEDVSVLVETEKK 135

                          90
                  ....*....|.
gi 1232081121 129 GPepwFVITGD 139
Cdd:cd07711   136 GT---VAVAGD 143
GOB1-like_MBL-B3 cd16308
Elizabethkingia meningoseptica GOB-1 and related metallo-beta-lactamases, subclass B3; ...
 55-152 1.02e-05

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: 45.54  E-value: 1.02e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232081121  55 THIHADHYTGGRELARRTGAPYCLHE-------DARNS----VKFGY--------QPLTDGQVLALGNVQVQVMHTPGHT 115
Cdd:cd16308    67 TQAHYDHVGAMAAIKQQTGAKMMVDEkdakvlaDGGKSdyemGGYGStfapvkadKLLHDGDTIKLGGTKLTLLHHPGHT 146

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1232081121 116 LDSiCLLVSDARRGPEPWFV-------ITGDTLFVGAVGRPDLA 152
Cdd:cd16308   147 KGS-CSFLFDVKDEKRTYRVlianmptILPDTKLSGMPGYPGIA 189
metallo-hydrolase-like_MBL-fold cd07743
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 48-142 1.17e-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) 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: 44.83  E-value: 1.17e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232081121  48 RITHVIDTHIHADHYTGGRELARRTGA------------------PYCLH-----EDARNSVKFGyQP------LTDGQv 98
Cdd:cd07743    45 KLKAIINTHSHADHIGGNAYLQKKTGCkvyapkiekafienpllePSYLGgayppKELRNKFLMA-KPskvddiIEEGE- 122

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1232081121  99 LALGNVQVQVMHTPGHTLDSICLLVSDarrgpEPWFVitGDTLF 142
Cdd:cd07743   123 LELGGVGLEIIPLPGHSFGQIGILTPD-----GVLFA--GDALF 159
ComEC COG2333
DNA uptake channel protein ComEC C-terminal domain, metallo-beta-lactamase superfamily ...
 48-139 1.22e-05

DNA uptake channel protein ComEC C-terminal domain, metallo-beta-lactamase superfamily [Intracellular trafficking, secretion, and vesicular transport];


Pssm-ID: 441904 [Multi-domain]  Cd Length: 253  Bit Score: 45.23  E-value: 1.22e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232081121  48 RITHVIDTHIHADHYTGGRELARR-------------TGAPYCLHEDARNSVKFGYQPLTDGQVLALGNVQVQVMHTPGH 114
Cdd:COG2333    52 RLDLLVLTHPDADHIGGLAAVLEAfpvgrvlvsgppdTSETYERLLEALKEKGIPVRPCRAGDTWQLGGVRFEVLWPPED 131

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1232081121 115 TL-------DSICLLVSDARRGpepwFVITGD 139
Cdd:COG2333   132 LLegsdennNSLVLRLTYGGFS----FLLTGD 159
AHL_lactonase_MBL-fold cd07729
quorum-quenching N-acyl-homoserine lactonase, MBL-fold metallo-hydrolase domain; Acyl ...
 49-139 1.72e-05

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: 44.51  E-value: 1.72e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232081121  49 ITHVIDTHIHADHyTGG-------------RELARRTGAPYClHEDARNSVKFGYQPLTDGQVLAL-GNVQ----VQVMH 110
Cdd:cd07729    89 IDYVILSHLHFDH-AGGldlfpnatiivqrAELEYATGPDPL-AAGYYEDVLALDDDLPGGRVRLVdGDYDlfpgVTLIP 166

                          90       100
                  ....*....|....*....|....*....
gi 1232081121 111 TPGHTLDSICLLVsdarRGPEPWFVITGD 139
Cdd:cd07729   167 TPGHTPGHQSVLV----RLPEGTVLLAGD 191
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 ...
 43-119 1.22e-04

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: 42.34  E-value: 1.22e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232081121  43 RLNQVRIthVIDTHIHADHYTGGRELARRTGAPYC--------------LHEDARNSVKFGYQP------LTDGQVLALG 102
Cdd:cd16290    57 RLEDVKL--ILNSHAHFDHAGGIAALQRDSGATVAaspagaaalrsggvDPDDPQAGAADPFPPvakvrvVADGEVVKLG 134

                          90
                  ....*....|....*..
gi 1232081121 103 NVQVQVMHTPGHTLDSI 119
Cdd:cd16290   135 PLAVTAHATPGHTPGGT 151
MBL-B3-like cd07708
metallo-beta-lactamases, subclass B3; MBL-fold metallo-hydrolase domain; MBLs (class B of the ...
 52-153 2.21e-04

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: 41.38  E-value: 2.21e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232081121  52 VIDTHIHADHYTGGRELARRTGAPYCLHEDARNSVKFGYQP--------------------LTDGQVLALGNVQVQVMHT 111
Cdd:cd07708    64 ILISHAHFDHAGGSAEIKKQTGAKVMAGAEDVSLLLSGGSSdfhyandsstyfpqstvdraVHDGERVTLGGTVLTAHAT 143

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1232081121 112 PGHTLDSICLLVSDARRGpEPWFVITGDTLfvGAVGRPDLAG 153
Cdd:cd07708   144 PGHTPGCTTWTMTLKDHG-KQYQVVFADSL--TVNPGYRLVD 182
BJP-1_FEZ-1-like_MBL-B3 cd16288
BJP-1, FEZ-1, GOB-1, Mbl1b and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 43-115 3.42e-04

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: 40.77  E-value: 3.42e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232081121  43 RLNQVRIthVIDTHIHADHYTGGRELARRTGAP-YCLHEDAR------------NSVKFGYQP------LTDGQVLALGN 103
Cdd:cd16288    57 KPSDIKI--LLNSHAHLDHAGGLAALKKLTGAKlMASAEDAAllasggksdfhyGDDSLAFPPvkvdrvLKDGDRVTLGG 134

                          90
                  ....*....|..
gi 1232081121 104 VQVQVMHTPGHT 115
Cdd:cd16288   135 TTLTAHLTPGHT 146
EVM-1-like_MBL-B3 cd16315
Erythrobacter vulgaris EVM-1 and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 43-115 3.76e-04

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: 40.80  E-value: 3.76e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232081121  43 RLNQVRIthVIDTHIHADHYTGGRELARRTGAPYCLHEDARNSVKFGyQP---------------------LTDGQVLAL 101
Cdd:cd16315    57 DPKDVRW--LLSSHEHFDHVGGLAALQRATGARVAASAAAAPVLESG-KPapddpqaglhepfppvrvdriVEDGDTVAL 133

                          90
                  ....*....|....
gi 1232081121 102 GNVQVQVMHTPGHT 115
Cdd:cd16315   134 GSLRLTAHATPGHT 147
PRK10241 PRK10241
hydroxyacylglutathione hydrolase; Provisional
 55-148 4.93e-04

hydroxyacylglutathione hydrolase; Provisional


Pssm-ID: 182327 [Multi-domain]  Cd Length: 251  Bit Score: 40.19  E-value: 4.93e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232081121  55 THIHADHYTGGRELARRTgaPY-CLHEDARNSVKFGYQPLTDGQVLALGNVQVQVMHTPGHTLDSICLLvsdarrgPEPw 133
Cdd:PRK10241   52 THHHHDHVGGVKELVEKF--PQiVVYGPQETQDKGTTQVVKDGETAFVLGHEFSVFATPGHTLGHICYF-------SKP- 121

                          90
                  ....*....|....*
gi 1232081121 134 FVITGDTLFVGAVGR 148
Cdd:PRK10241  122 YLFCGDTLFSGGCGR 136
BcII-like_MBL-B1 cd16304
Bacillus cereus Beta-lactamase 2 and related metallo-beta-lactamases, subclass B1; MBL-fold ...
 41-119 5.13e-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: 39.96  E-value: 5.13e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232081121  41 QARLNQvRITHVIDTHIHADHYTGGRELARRtGAP-YCLHEDARNSVKFGY-QP---LTDGQVLALGNVQVQVMHT-PGH 114
Cdd:cd16304    57 KKKLKK-PVTLAIVTHAHDDRIGGIKALQKR-GIPvYSTKLTAQLAKKQGYpSPdgiLKDDTTLKFGNTKIETFYPgEGH 134


                  ....*
gi 1232081121 115 TLDSI 119
Cdd:cd16304   135 TADNI 139
ComA-like_MBL-fold cd07731
Competence protein ComA, ComEC and related proteins; MBL-fold metallo hydrolase domain; This ...
 48-139 6.80e-04

Competence protein ComA, ComEC and related proteins; MBL-fold metallo hydrolase domain; This subgroup includes proteins required for natural transformation competence including Neisseria gonorrhoeae ComA, Pseudomonas stutzeri ComA, Bacillus subtilis ComEC (also known as ComE operon protein 3) and Haemophilus influenza ORF2 encoded by the rec-2 gene, as well as Escherichia coli YcaI which does not mediate spontaneous plasmid transformation on nutrient-containing agar plates. It also includes the phosphorylcholine esterase (Pce) domain of choline-binding protein e from streptococcus pneumonia. 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: 293817 [Multi-domain]  Cd Length: 179  Bit Score: 39.42  E-value: 6.80e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232081121  48 RITHVIDTHIHADHYTGGRELARR-------------TGAPYCLHEDARNSVKFGYQPLTDGQVLALGNVQVQVMHTPGH 114
Cdd:cd07731    48 KLDYLILTHPDADHIGGLDAVLKNfpvkevympgvthTTKTYEDLLDAIKEKGIPVTPCKAGDRWQLGGVSFEVLSPPKD 127

                          90       100       110
                  ....*....|....*....|....*....|
gi 1232081121 115 TLD-----SICLLVSDARRGpepwFVITGD 139
Cdd:cd07731   128 DYDdlnnnSCVLRLTYGGTS----FLLTGD 153
ElaC COG1234
Ribonuclease BN, tRNA processing enzyme [Translation, ribosomal structure and biogenesis];
39-142 1.08e-03

Ribonuclease BN, tRNA processing enzyme [Translation, ribosomal structure and biogenesis];


Pssm-ID: 440847 [Multi-domain]  Cd Length: 250  Bit Score: 39.41  E-value: 1.08e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232081121  39 IEQARLNQVRITHVIDTHIHADHYTG------GRELARRTG-----APYCLHEDARNSVKFG---------YQPLTDGQV 98
Cdd:COG1234    43 LLRAGLDPRDIDAIFITHLHGDHIAGlpgllsTRSLAGREKpltiyGPPGTKEFLEALLKASgtdldfpleFHEIEPGEV 122

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1232081121  99 LALGNVQVQVMHTPgHTLDSICLLVSDARRgpepWFVITGDTLF 142
Cdd:COG1234   123 FEIGGFTVTAFPLD-HPVPAYGYRFEEPGR----SLVYSGDTRP 161
Mbl1b-like_MBL-B3 cd16310
Caulobacter crescentus Mbl1b and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 44-115 1.21e-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: 38.97  E-value: 1.21e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232081121  44 LNQVRIthVIDTHIHADHYTGGRELARRTGAPYCLHEDARNSVKFG-------YQP-----------LTDGQVLALGNVQ 105
Cdd:cd16310    58 LSDIKI--IINTHAHYDHAGGLAQLKADTGAKLWASRGDRPALEAGkhigdniTQPapfpavkvdriLGDGEKIKLGDIT 135

                          90
                  ....*....|
gi 1232081121 106 VQVMHTPGHT 115
Cdd:cd16310   136 LTATLTPGHT 145
metallo-hydrolase-like_MBL-fold cd16277
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 49-141 1.86e-03

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


Pssm-ID: 293835 [Multi-domain]  Cd Length: 222  Bit Score: 38.27  E-value: 1.86e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232081121  49 ITHVIDTHIHADH------YTGGREL-----AR----RTGAPYCLHEDARNSVKFGY-----QPL---------TDGQVL 99
Cdd:cd16277    64 VDYVLCTHLHVDHvgwntrLVDGRWVptfpnARylfsRAEYDHWSSPDAGGPPNRGVfedsvLPVieagladlvDDDHEI 143

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1232081121 100 ALGnvqVQVMHTPGHTLDSICLLVSDARRGpepwFVITGDTL 141
Cdd:cd16277   144 LDG---IRLEPTPGHTPGHVSVELESGGER----ALFTGDVM 178
L1_POM-1-like_MBL-B3 cd16289
Stenotrophomonas maltophilia L1, Pseudomonas otitidis POM-1 and related ...
 52-129 1.93e-03

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: 38.64  E-value: 1.93e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232081121  52 VIDTHIHADHYTGGRELARRTGA--------PYCLHEDARNSVKFG----YQP------LTDGQVLALGNVQVQVMHTPG 113
Cdd:cd16289    64 ILHSHAHADHAGPLAALKRATGArvaanaesAVLLARGGSDDIHFGdgitFPPvqadriVMDGEVVTLGGVTFTAHFTPG 143

                          90
                  ....*....|....*.
gi 1232081121 114 HTLDSICLLVSDARRG 129
Cdd:cd16289   144 HTPGSTSWTWTDTRDG 159
PhnP COG1235
Phosphoribosyl 1,2-cyclic phosphate phosphodiesterase [Inorganic ion transport and metabolism]; ...
 39-140 3.11e-03

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


Pssm-ID: 440848 [Multi-domain]  Cd Length: 259  Bit Score: 37.95  E-value: 3.11e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232081121  39 IEQARLNQVRITHVIDTHIHADHYTGGRELARRTGAP----YCLHEDARN-SVKFGY-----------QPLTDGQVLALG 102
Cdd:COG1235    59 LLRLGLDPSKIDAILLTHEHADHIAGLDDLRPRYGPNpipvYATPGTLEAlERRFPYlfapypgklefHEIEPGEPFEIG 138

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1232081121 103 NVQVQVMHTPGHTLDSICLLVSDARRGpepwFVITGDT 140
Cdd:COG1235   139 GLTVTPFPVPHDAGDPVGYRIEDGGKK----LAYATDT 172
metallo-hydrolase-like_MBL-fold cd16276
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 49-174 4.35e-03

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


Pssm-ID: 293834 [Multi-domain]  Cd Length: 188  Bit Score: 37.18  E-value: 4.35e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232081121  49 ITHVIDTHIHADHyTGGRELARRTGAPYCLHEDARNSVKFGYQP--------LTDGQVLALGNVQVQVM-HTPGHTLDSI 119
Cdd:cd16276    46 VTHVVYSHNHADH-IGGASIFKDEGATIIAHEATAELLKRNPDPkrpvptvtFDDEYTLEVGGQTLELSyFGPNHGPGNI 124

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1232081121 120 CLLVsdarrgPEPWFVITGDTLFVGAVGRPDLAGRElEMAGLLHQslHDKLLRLP 174
Cdd:cd16276   125 VIYL------PKQKVLMAVDLINPGWVPFFNFAGSE-DIPGYIEA--LDELLEYD 170
 
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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