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Conserved domains on  [gi|1437577626|emb|STX68081|]
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hydroxyacylglutathione hydrolase [Legionella pneumophila]

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; ...
 2-173 1.17e-83

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: 246.54  E-value: 1.17e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437577626   2 IFHQLFDQDSCTYTYLIGSTFSKHAIIIDPVRSQVSHYINLINKLELNLVASIDTHLHADHITGSGQLTILTDCHSMIGM 81
Cdd:cd07724     1 IFRQFFDPGLGTLSYLVGDPETGEAAVIDPVRDSVDRYLDLAAELGLKITYVLETHVHADHVSGARELAERTGAPIVIGE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437577626  82 ESKAKFVHIKFHDNEILNFGNIKIKAMHTPGHTPDSYCFVMED--RIFTGDTLLINATGRTDFQN---GSASAQYDSLFN 156
Cdd:cd07724    81 GAPASFFDRLLKDGDVLELGNLTLEVLHTPGHTPESVSYLVGDpdAVFTGDTLFVGDVGRPDLPGeaeGLARQLYDSLQR 160

                         170
                  ....*....|....*..
gi 1437577626 157 KLLKLPGFMRIYPGHDY 173
Cdd:cd07724   161 KLLLLPDETLVYPGHDY 177
 
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; ...
 2-173 1.17e-83

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: 246.54  E-value: 1.17e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437577626   2 IFHQLFDQDSCTYTYLIGSTFSKHAIIIDPVRSQVSHYINLINKLELNLVASIDTHLHADHITGSGQLTILTDCHSMIGM 81
Cdd:cd07724     1 IFRQFFDPGLGTLSYLVGDPETGEAAVIDPVRDSVDRYLDLAAELGLKITYVLETHVHADHVSGARELAERTGAPIVIGE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437577626  82 ESKAKFVHIKFHDNEILNFGNIKIKAMHTPGHTPDSYCFVMED--RIFTGDTLLINATGRTDFQN---GSASAQYDSLFN 156
Cdd:cd07724    81 GAPASFFDRLLKDGDVLELGNLTLEVLHTPGHTPESVSYLVGDpdAVFTGDTLFVGDVGRPDLPGeaeGLARQLYDSLQR 160

                         170
                  ....*....|....*..
gi 1437577626 157 KLLKLPGFMRIYPGHDY 173
Cdd:cd07724   161 KLLLLPDETLVYPGHDY 177
PLN02962 PLN02962
hydroxyacylglutathione hydrolase
 1-233 1.68e-59

hydroxyacylglutathione hydrolase


Pssm-ID: 178547 [Multi-domain]  Cd Length: 251  Bit Score: 188.08  E-value: 1.68e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437577626   1 MIFHQLFDQDSCTYTYLIGSTF--SKHAIIIDPVRSQVSHYINLINKLELNLVASIDTHLHADHITGSGQL-TILTDCHS 77
Cdd:PLN02962   11 LLFRQLFEKESSTYTYLLADVShpDKPALLIDPVDKTVDRDLSLVKELGLKLIYAMNTHVHADHVTGTGLLkTKLPGVKS 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437577626  78 MIGMESKAKFVHIKFHDNEIlNFGNIKIKAMHTPGHTPDSYCFVMED-------RI-FTGDTLLINATGRTDFQNGSASA 149
Cdd:PLN02962   91 IISKASGSKADLFVEPGDKI-YFGDLYLEVRATPGHTAGCVTYVTGEgpdqpqpRMaFTGDALLIRGCGRTDFQGGSSDQ 169

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437577626 150 QYDSLFNKLLKLPGFMRIYPGHDYNQKQYSTIDDEKKNNPRLqVKSRQEYVEMMGNLSLSFPKNMHFAVPANLNNGLteQ 229
Cdd:PLN02962  170 LYKSVHSQIFTLPKDTLIYPAHDYKGFTVSTVGEEMLYNPRL-TKDEETFKTIMENLNLPYPKMIDVAVPANMVCGL--Q 246


                  ....
gi 1437577626 230 EVNA 233
Cdd:PLN02962  247 DPPA 250
GloB COG0491
Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General ...
 1-173 1.14e-35

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: 125.57  E-value: 1.14e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437577626   1 MIFHQLFDQDSCTYTYLIGSTfsKHAIIIDPVRS--QVSHYINLINKLELNLVASIDTHLHADHITGSGQLTILTDCHSM 78
Cdd:COG0491     3 VLPGGTPGAGLGVNSYLIVGG--DGAVLIDTGLGpaDAEALLAALAALGLDIKAVLLTHLHPDHVGGLAALAEAFGAPVY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437577626  79 IG------MESKAKFVHIK---------FHDNEILNFGNIKIKAMHTPGHTPDSYCFVMEDR--IFTGDTLLINATGRTD 141
Cdd:COG0491    81 AHaaeaeaLEAPAAGALFGrepvppdrtLEDGDTLELGGPGLEVIHTPGHTPGHVSFYVPDEkvLFTGDALFSGGVGRPD 160

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1437577626 142 FQNGSASAQYDSLfNKLLKLPgFMRIYPGHDY 173
Cdd:COG0491   161 LPDGDLAQWLASL-ERLLALP-PDLVIPGHGP 190
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 14-171 2.93e-23

Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins contain this domain. These proteins include thiolesterases, members of the glyoxalase II family, that catalyse the hydrolysis of S-D-lactoyl-glutathione to form glutathione and D-lactic acid and a competence protein that is essential for natural transformation in Neisseria gonorrhoeae and could be a transporter involved in DNA uptake. Except for the competence protein these proteins bind two zinc ions per molecule as cofactor.


Pssm-ID: 214854 [Multi-domain]  Cd Length: 177  Bit Score: 92.23  E-value: 2.93e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437577626   14 YTYLIGSTfsKHAIIIDPVRSQVSHYINLINKLEL-NLVASIDTHLHADHITGSGQLTILTDC----------------- 75
Cdd:smart00849   1 NSYLVRDD--GGAILIDTGPGEAEDLLAELKKLGPkKIDAIILTHGHPDHIGGLPELLEAPGApvyapegtaellkdlla 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437577626   76 -HSMIGMESKAKFVHIKFHDNEILNFGNIKIKAMHTPGHTPDSYCFVMEDR--IFTGDTLLINATGRTDFQNGSASAqyD 152
Cdd:smart00849  79 lLGELGAEAEPAPPDRTLKDGDELDLGGGELEVIHTPGHTPGSIVLYLPEGkiLFTGDLLFAGGDGRTLVDGGDAAA--S 156

                          170       180
                   ....*....|....*....|.
gi 1437577626  153 SLFNKLLKLPGFM--RIYPGH 171
Cdd:smart00849 157 DALESLLKLLKLLpkLVVPGH 177
Lactamase_B pfam00753
Metallo-beta-lactamase superfamily;
13-171 1.08e-13

Metallo-beta-lactamase superfamily;


Pssm-ID: 425851 [Multi-domain]  Cd Length: 196  Bit Score: 67.39  E-value: 1.08e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437577626  13 TYTYLIGSTfsKHAIIIDPVRSQVSHYINLINKLELNLvASID----THLHADHITGSGQLTILTDCHSMIGME------ 82
Cdd:pfam00753   6 VNSYLIEGG--GGAVLIDTGGSAEAALLLLLAALGLGP-KDIDavilTHGHFDHIGGLGELAEATDVPVIVVAEearell 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437577626  83 ------------SKAKFVHIKFHDNEILN-----FGNIKIKAMHTPGHTPDSYCFVMEDR--IFTGDTLLINATGRTDFQ 143
Cdd:pfam00753  83 deelglaasrlgLPGPPVVPLPPDVVLEEgdgilGGGLGLLVTHGPGHGPGHVVVYYGGGkvLFTGDLLFAGEIGRLDLP 162

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1437577626 144 NGSASAQYDSLFNKLLKL------PGFMRIYPGH 171
Cdd:pfam00753 163 LGGLLVLHPSSAESSLESllklakLKAAVIVPGH 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; ...
 2-173 1.17e-83

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: 246.54  E-value: 1.17e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437577626   2 IFHQLFDQDSCTYTYLIGSTFSKHAIIIDPVRSQVSHYINLINKLELNLVASIDTHLHADHITGSGQLTILTDCHSMIGM 81
Cdd:cd07724     1 IFRQFFDPGLGTLSYLVGDPETGEAAVIDPVRDSVDRYLDLAAELGLKITYVLETHVHADHVSGARELAERTGAPIVIGE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437577626  82 ESKAKFVHIKFHDNEILNFGNIKIKAMHTPGHTPDSYCFVMED--RIFTGDTLLINATGRTDFQN---GSASAQYDSLFN 156
Cdd:cd07724    81 GAPASFFDRLLKDGDVLELGNLTLEVLHTPGHTPESVSYLVGDpdAVFTGDTLFVGDVGRPDLPGeaeGLARQLYDSLQR 160

                         170
                  ....*....|....*..
gi 1437577626 157 KLLKLPGFMRIYPGHDY 173
Cdd:cd07724   161 KLLLLPDETLVYPGHDY 177
PLN02962 PLN02962
hydroxyacylglutathione hydrolase
 1-233 1.68e-59

hydroxyacylglutathione hydrolase


Pssm-ID: 178547 [Multi-domain]  Cd Length: 251  Bit Score: 188.08  E-value: 1.68e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437577626   1 MIFHQLFDQDSCTYTYLIGSTF--SKHAIIIDPVRSQVSHYINLINKLELNLVASIDTHLHADHITGSGQL-TILTDCHS 77
Cdd:PLN02962   11 LLFRQLFEKESSTYTYLLADVShpDKPALLIDPVDKTVDRDLSLVKELGLKLIYAMNTHVHADHVTGTGLLkTKLPGVKS 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437577626  78 MIGMESKAKFVHIKFHDNEIlNFGNIKIKAMHTPGHTPDSYCFVMED-------RI-FTGDTLLINATGRTDFQNGSASA 149
Cdd:PLN02962   91 IISKASGSKADLFVEPGDKI-YFGDLYLEVRATPGHTAGCVTYVTGEgpdqpqpRMaFTGDALLIRGCGRTDFQGGSSDQ 169

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437577626 150 QYDSLFNKLLKLPGFMRIYPGHDYNQKQYSTIDDEKKNNPRLqVKSRQEYVEMMGNLSLSFPKNMHFAVPANLNNGLteQ 229
Cdd:PLN02962  170 LYKSVHSQIFTLPKDTLIYPAHDYKGFTVSTVGEEMLYNPRL-TKDEETFKTIMENLNLPYPKMIDVAVPANMVCGL--Q 246


                  ....
gi 1437577626 230 EVNA 233
Cdd:PLN02962  247 DPPA 250
BaeB-like_MBL-fold cd16275
Bacillus amyloliquefaciens BaeB and related proteins; MBL-fold metallo hydrolase domain; ...
 14-171 1.28e-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: 131.89  E-value: 1.28e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437577626  14 YTYLIGSTFSKHAIIIDPVRsQVSHYINLINKLELNLVASIDTHLHADHITGSGQLTILTDC--HsMIGMEskAKFVHIK 91
Cdd:cd16275    13 YSYIIIDKATREAAVVDPAW-DIEKILAKLNELGLTLTGILLTHSHFDHVNLVEPLLAKYDApvY-MSKEE--IDYYGFR 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437577626  92 ------FHDNEILNFGNIKIKAMHTPGHTPDSYCFVMEDRIFTGDTLLINATGRTDFQNGSASAQYDSLfNKLLKL-PGF 164
Cdd:cd16275    89 cpnlipLEDGDTIKIGDTEITCLLTPGHTPGSMCYLLGDSLFTGDTLFIEGCGRCDLPGGDPEEMYESL-QRLKKLpPPN 167


                  ....*..
gi 1437577626 165 MRIYPGH 171
Cdd:cd16275   168 TRVYPGH 174
metallo-hydrolase-like_MBL-fold cd06262
mainly hydrolytic enzymes and related proteins which carry out various biological functions; ...
 13-171 2.03e-36

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: 126.63  E-value: 2.03e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437577626  13 TYTYLIGSTfSKHAIIIDPVRSQVSHYINLINKLELNLVASIDTHLHADHITGSGQLTILTDC----------------- 75
Cdd:cd06262    10 TNCYLVSDE-EGEAILIDPGAGALEKILEAIEELGLKIKAILLTHGHFDHIGGLAELKEAPGApvyiheadaelledpel 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437577626  76 --HSMIGMESKAKFVHIKFHDNEILNFGNIKIKAMHTPGHTPDSYCFVMEDR--IFTGDTLLINATGRTDFQNGSASAQY 151
Cdd:cd06262    89 nlAFFGGGPLPPPEPDILLEDGDTIELGGLELEVIHTPGHTPGSVCFYIEEEgvLFTGDTLFAGSIGRTDLPGGDPEQLI 168

                         170       180
                  ....*....|....*....|
gi 1437577626 152 DSLFNKLLKLPGFMRIYPGH 171
Cdd:cd06262   169 ESIKKLLLLLPDDTVVYPGH 188
GloB COG0491
Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General ...
 1-173 1.14e-35

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: 125.57  E-value: 1.14e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437577626   1 MIFHQLFDQDSCTYTYLIGSTfsKHAIIIDPVRS--QVSHYINLINKLELNLVASIDTHLHADHITGSGQLTILTDCHSM 78
Cdd:COG0491     3 VLPGGTPGAGLGVNSYLIVGG--DGAVLIDTGLGpaDAEALLAALAALGLDIKAVLLTHLHPDHVGGLAALAEAFGAPVY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437577626  79 IG------MESKAKFVHIK---------FHDNEILNFGNIKIKAMHTPGHTPDSYCFVMEDR--IFTGDTLLINATGRTD 141
Cdd:COG0491    81 AHaaeaeaLEAPAAGALFGrepvppdrtLEDGDTLELGGPGLEVIHTPGHTPGHVSFYVPDEkvLFTGDALFSGGVGRPD 160

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1437577626 142 FQNGSASAQYDSLfNKLLKLPgFMRIYPGHDY 173
Cdd:COG0491   161 LPDGDLAQWLASL-ERLLALP-PDLVIPGHGP 190
hydroxyacylglutathione_hydrolase_MBL-fold cd07723
hydroxyacylglutathione hydrolase, MBL-fold metallo-hydrolase domain; hydroxyacylglutathione ...
 14-171 1.93e-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: 123.34  E-value: 1.93e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437577626  14 YTYLIGSTFSKHAIIIDPVRSQVshYINLINKLELNLVASIDTHLHADHITGSGQLTILT-DCHSMIGMESKAKFVHIKF 92
Cdd:cd07723    10 YIYLIVDEATGEAAVVDPGEAEP--VLAALEKNGLTLTAILTTHHHWDHTGGNAELKALFpDAPVYGPAEDRIPGLDHPV 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437577626  93 HDNEILNFGNIKIKAMHTPGHTPDSYCFVMEDR--IFTGDTLLINATGRtdFQNGSASAQYDSLfNKLLKLPGFMRIYPG 170
Cdd:cd07723    88 KDGDEIKLGGLEVKVLHTPGHTLGHICYYVPDEpaLFTGDTLFSGGCGR--FFEGTAEQMYASL-QKLLALPDDTLVYCG 164


                  .
gi 1437577626 171 H 171
Cdd:cd07723   165 H 165
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 14-171 2.93e-23

Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins contain this domain. These proteins include thiolesterases, members of the glyoxalase II family, that catalyse the hydrolysis of S-D-lactoyl-glutathione to form glutathione and D-lactic acid and a competence protein that is essential for natural transformation in Neisseria gonorrhoeae and could be a transporter involved in DNA uptake. Except for the competence protein these proteins bind two zinc ions per molecule as cofactor.


Pssm-ID: 214854 [Multi-domain]  Cd Length: 177  Bit Score: 92.23  E-value: 2.93e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437577626   14 YTYLIGSTfsKHAIIIDPVRSQVSHYINLINKLEL-NLVASIDTHLHADHITGSGQLTILTDC----------------- 75
Cdd:smart00849   1 NSYLVRDD--GGAILIDTGPGEAEDLLAELKKLGPkKIDAIILTHGHPDHIGGLPELLEAPGApvyapegtaellkdlla 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437577626   76 -HSMIGMESKAKFVHIKFHDNEILNFGNIKIKAMHTPGHTPDSYCFVMEDR--IFTGDTLLINATGRTDFQNGSASAqyD 152
Cdd:smart00849  79 lLGELGAEAEPAPPDRTLKDGDELDLGGGELEVIHTPGHTPGSIVLYLPEGkiLFTGDLLFAGGDGRTLVDGGDAAA--S 156

                          170       180
                   ....*....|....*....|.
gi 1437577626  153 SLFNKLLKLPGFM--RIYPGH 171
Cdd:smart00849 157 DALESLLKLLKLLpkLVVPGH 177
TTHA1623-like_MBL-fold cd16322
uncharacterized Thermus thermophilus TTHA1623 and related proteins; MBL-fold metallo hydrolase ...
 15-191 1.64e-22

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: 90.87  E-value: 1.64e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437577626  15 TYLIGSTFSKHAIIIDPvRSQVSHYINLINKLELNLVASIDTHLHADHITGSGQLTILTD----CHSM-------IGMES 83
Cdd:cd16322    13 TYLVADEGGGEAVLVDP-GDESEKLLARFGTTGLTLLYILLTHAHFDHVGGVADLRRHPGapvyLHPDdlplyeaADLGA 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437577626  84 KAKFVHIKF--------HDNEILNFGNIKIKAMHTPGHTPDSYCFVMEDR--IFTGDTLLINATGRTDFQnGSASAQYDS 153
Cdd:cd16322    92 KAFGLGIEPlpppdrllEDGQTLTLGGLEFKVLHTPGHSPGHVCFYVEEEglLFSGDLLFQGSIGRTDLP-GGDPKAMAA 170

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1437577626 154 LFNKLLKLPGFMRIYPGHdynqKQYSTIDDEKKNNPRL 191
Cdd:cd16322   171 SLRRLLTLPDETRVFPGH----GPPTTLGEERRTNPFL 204
YcbL-like_MBL-fold cd07737
Salmonella enterica serovar typhimurium YcbL and related proteins; MBL-fold metallo hydrolase ...
 3-171 7.71e-20

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: 83.76  E-value: 7.71e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437577626   3 FHQlfdqdSCTytyLIGSTFSKHAIIIDPvRSQVSHYINLINKLELNLVASIDTHLHADHITGSGQL------------- 69
Cdd:cd07737     9 FQQ-----NCS---LIWCEETKEAAVIDP-GGDADKILQAIEDLGLTLKKILLTHGHLDHVGGAAELaehygvpiigphk 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437577626  70 -------TILTDCHSMIGMESKAKFVHIKFHDNEILNFGNIKIKAMHTPGHTPDSYCFV-MEDRI-FTGDTLLINATGRT 140
Cdd:cd07737    80 edkflleNLPEQSQMFGFPPAEAFTPDRWLEEGDTVTVGNLTLEVLHCPGHTPGHVVFFnRESKLaIVGDVLFKGSIGRT 159

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1437577626 141 DFQNGSASAQYDSLFNKLLKLPGFMRIYPGH 171
Cdd:cd07737   160 DFPGGNHAQLIASIKEKLLPLGDDVTFIPGH 190
LACTB2-like_MBL-fold cd07722
uncharacterized subgroup which includes human lactamase beta 2 and related proteins; MBL-fold ...
 13-171 9.06e-19

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: 80.66  E-value: 9.06e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437577626  13 TYTYLIGSTFSKhaIIID---PVRSqvshYINLINK-LELNLVASID----THLHADHITG---------SGQLTI---L 72
Cdd:cd07722    18 TNTYLVGTGKRR--ILIDtgeGRPS----YIPLLKSvLDSEGNATISdillTHWHHDHVGGlpdvldllrGPSPRVykfP 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437577626  73 TDCHSMIGMESKAKFVHIkfHDNEILNFGNIKIKAMHTPGHTPDSYCFVM--EDRIFTGDTLLinATGRTDFQNGSAsaq 150
Cdd:cd07722    92 RPEEDEDPDEDGGDIHDL--QDGQVFKVEGATLRVIHTPGHTTDHVCFLLeeENALFTGDCVL--GHGTAVFEDLAA--- 164

                         170       180
                  ....*....|....*....|..
gi 1437577626 151 Y-DSLfNKLLKLpGFMRIYPGH 171
Cdd:cd07722   165 YmASL-KKLLSL-GPGRIYPGH 184
PLN02469 PLN02469
hydroxyacylglutathione hydrolase
 14-200 1.24e-17

hydroxyacylglutathione hydrolase


Pssm-ID: 178088 [Multi-domain]  Cd Length: 258  Bit Score: 79.03  E-value: 1.24e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437577626  14 YTYLIGSTFSKHAIIIDPVrsQVSHYINLINKLELNLVASIDTHLHADHITGSGQLT-ILTDCHSMIGMESKAKFVHIKF 92
Cdd:PLN02469   13 YAYLIIDESTKDAAVVDPV--DPEKVLQAAHEHGAKIKLVLTTHHHWDHAGGNEKIKkLVPGIKVYGGSLDNVKGCTHPV 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437577626  93 HDNEILNFGN-IKIKAMHTPGHTPDSYCFVMEDR------IFTGDTLLINATGRtdFQNGSASAQYDSLFNKLLKLPGFM 165
Cdd:PLN02469   91 ENGDKLSLGKdVNILALHTPCHTKGHISYYVTGKegedpaVFTGDTLFIAGCGK--FFEGTAEQMYQSLCVTLGSLPKPT 168

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1437577626 166 RIYPGHDYNQKQY--------------------------------STIDDEKKNNP--RLQVKSRQEYV 200
Cdd:PLN02469  169 QVYCGHEYTVKNLkfaltvepdneklkqklewaekqrqaglptvpSTIEEELETNPfmRVDLPEIQEKV 237
metallo-hydrolase-like_MBL-fold cd16278
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 13-171 2.98e-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: 293836 [Multi-domain]  Cd Length: 185  Bit Score: 73.68  E-value: 2.98e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437577626  13 TYTYLIGStfSKHAIIIDPVRSQVSHYINLIN-----KLELNLVasidTHLHADHITGSGQLTILTDC------HSMIGM 81
Cdd:cd16278    18 TNTYLLGA--PDGVVVIDPGPDDPAHLDALLAalgggRVSAILV----THTHRDHSPGAARLAERTGApvrafgPHRAGG 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437577626  82 ESKAKFVHIKFHDNEILNFGNIKIKAMHTPGHTPDSYCFVM--EDRIFTGDTLLinatGR-------TDfqnGSASAQYD 152
Cdd:cd16278    92 QDTDFAPDRPLADGEVIEGGGLRLTVLHTPGHTSDHLCFALedEGALFTGDHVM----GWsttviapPD---GDLGDYLA 164

                         170
                  ....*....|....*....
gi 1437577626 153 SLfNKLLKLPGfMRIYPGH 171
Cdd:cd16278   165 SL-ERLLALDD-RLLLPGH 181
Lactamase_B pfam00753
Metallo-beta-lactamase superfamily;
13-171 1.08e-13

Metallo-beta-lactamase superfamily;


Pssm-ID: 425851 [Multi-domain]  Cd Length: 196  Bit Score: 67.39  E-value: 1.08e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437577626  13 TYTYLIGSTfsKHAIIIDPVRSQVSHYINLINKLELNLvASID----THLHADHITGSGQLTILTDCHSMIGME------ 82
Cdd:pfam00753   6 VNSYLIEGG--GGAVLIDTGGSAEAALLLLLAALGLGP-KDIDavilTHGHFDHIGGLGELAEATDVPVIVVAEearell 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437577626  83 ------------SKAKFVHIKFHDNEILN-----FGNIKIKAMHTPGHTPDSYCFVMEDR--IFTGDTLLINATGRTDFQ 143
Cdd:pfam00753  83 deelglaasrlgLPGPPVVPLPPDVVLEEgdgilGGGLGLLVTHGPGHGPGHVVVYYGGGkvLFTGDLLFAGEIGRLDLP 162

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1437577626 144 NGSASAQYDSLFNKLLKL------PGFMRIYPGH 171
Cdd:pfam00753 163 LGGLLVLHPSSAESSLESllklakLKAAVIVPGH 196
TTHA1429-like_MBL-fold cd07725
uncharacterized Thermus thermophilus TTHA1429 and related proteins; MBL-fold metallo hydrolase ...
 56-171 3.51e-13

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: 65.40  E-value: 3.51e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437577626  56 THLHADHITGSGQLtiltdCHSMIGMESKAKFVHIKfhDNEILNFGNIKIKAMHTPGHTPDSYCFVMEDR--IFTGDTLL 133
Cdd:cd07725    62 THHHPDHIGLAGKL-----QEKSGATVYILDVTPVK--DGDKIDLGGLRLKVIETPGHTPGHIVLYDEDRreLFVGDAVL 134

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1437577626 134 I----NATGRTDFQNGSASAQYDSLfNKLLKLpGFMRIYPGH 171
Cdd:cd07725   135 PkitpNVSLWAVRVEDPLGAYLESL-DKLEKL-DVDLAYPGH 174
MBLAC2-like_MBL-fold cd07712
uncharacterized human metallo-beta-lactamase domain-containing protein 2 and related proteins; ...
 39-171 8.35e-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: 61.88  E-value: 8.35e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437577626  39 YINLINKLELNLVAsidTHLHADHITGSGQ-------------------LTILTDCHSMIGMESKAKFVHIKfhDNEILN 99
Cdd:cd07712    35 YVRTLTDLPLLVVA---THGHFDHIGGLHEfeevyvhpadaeilaapdnFETLTWDAATYSVPPAGPTLPLR--DGDVID 109

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1437577626 100 FGNIKIKAMHTPGHTPDSYCFVMEDR--IFTGDTllINATGRTDFQNGSASAQYDSLFNKLLKLPG-FMRIYPGH 171
Cdd:cd07712   110 LGDRQLEVIHTPGHTPGSIALLDRANrlLFSGDV--VYDGPLIMDLPHSDLDDYLASLEKLSKLPDeFDKVLPGH 182
PLN02398 PLN02398
hydroxyacylglutathione hydrolase
 14-173 5.42e-10

hydroxyacylglutathione hydrolase


Pssm-ID: 215223 [Multi-domain]  Cd Length: 329  Bit Score: 58.32  E-value: 5.42e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437577626  14 YTYLIGSTFSKHAIIIDPvrSQVSHYINLINKLELNLVASIDTHLHADHITGSGQLTILTDChSMIGME---SKAKFVHI 90
Cdd:PLN02398   88 YAYLLHDEDTGTVGVVDP--SEAVPVIDALSRKNRNLTYILNTHHHYDHTGGNLELKARYGA-KVIGSAvdkDRIPGIDI 164

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437577626  91 KFHDNEILNFGNIKIKAMHTPGHTPD--SYCFVMEDRIFTGDTLLINATGRtdFQNGSASAQYDSLfNKLLKLPGFMRIY 168
Cdd:PLN02398  165 VLKDGDKWMFAGHEVLVMETPGHTRGhiSFYFPGSGAIFTGDTLFSLSCGK--LFEGTPEQMLSSL-QKIISLPDDTNIY 241


                  ....*
gi 1437577626 169 PGHDY 173
Cdd:PLN02398  242 CGHEY 246
yflN-like_MBL-fold cd07721
uncharacterized subgroup which includes Bacillus subtilis yflN; MBL-fold metallo hydrolase ...
 56-171 1.21e-08

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


Pssm-ID: 293807 [Multi-domain]  Cd Length: 202  Bit Score: 53.38  E-value: 1.21e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437577626  56 THLHADHITGSGQLTILTD----CHS-----MIGMES-------------------KAKFVHIKFHDNEILNFGnIKIKA 107
Cdd:cd07721    56 THGHIDHIGSLAALKEAPGapvyAHEreapyLEGEKPypppvrlgllgllspllpvKPVPVDRTLEDGDTLDLA-GGLRV 134

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1437577626 108 MHTPGHTPDSYCFVMEDR--IFTGDtLLINATGRT---------DFQNGSASAQydslfnKLLKLPgFMRIYPGH 171
Cdd:cd07721   135 IHTPGHTPGHISLYLEEDgvLIAGD-ALVTVGGELvpppppftwDMEEALESLR------KLAELD-PEVLAPGH 201
ST1585-like_MBL-fold cd07726
uncharacterized subgroup which includes Sulfolobus tokodaii ST1585 protein; MBL-fold metallo ...
 13-171 3.33e-08

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: 52.11  E-value: 3.33e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437577626  13 TYTYLIGStfSKHAIIIDP-VRSQVSHYINLINKLELNLvASID----THLHADHITGSGQL-------TILtdCHS--- 77
Cdd:cd07726    16 IASYLLDG--EGRPALIDTgPSSSVPRLLAALEALGIAP-EDVDyiilTHIHLDHAGGAGLLaealpnaKVY--VHPrga 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437577626  78 --MI-------------GMESKAKFVHIK---------FHDNEILNFGNIKIKAMHTPGHTPDSYCFVME--DRIFTGDT 131
Cdd:cd07726    91 rhLIdpsklwasaravyGDEADRLGGEILpvpeervivLEDGETLDLGGRTLEVIDTPGHAPHHLSFLDEesDGLFTGDA 170

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1437577626 132 LLINatGRTDFQNGSASA---QYD------SLfNKLLKLPgFMRIYPGH 171
Cdd:cd07726   171 AGVR--YPELDVVGPPSTpppDFDpeawleSL-DRLLSLK-PERIYLTH 215
metallo-hydrolase-like_MBL-fold cd07743
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 23-132 1.18e-07

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


Pssm-ID: 293829 [Multi-domain]  Cd Length: 197  Bit Score: 50.22  E-value: 1.18e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437577626  23 SKHAIIIDP--VRSQVSHYINLINKLELNLVASIDTHLHADHITGSGQLTILTDCH------------------SMIGME 82
Cdd:cd07743    17 DKEALLIDSglDEDAGRKIRKILEELGWKLKAIINTHSHADHIGGNAYLQKKTGCKvyapkiekafienpllepSYLGGA 96

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1437577626  83 SKAKFVHIKFH-----------DNEILNFGNIKIKAMHTPGHTPDSYCFVMEDRI-FTGDTL 132
Cdd:cd07743    97 YPPKELRNKFLmakpskvddiiEEGELELGGVGLEIIPLPGHSFGQIGILTPDGVlFAGDAL 158
MBLAC1-like_MBL-fold cd07711
uncharacterized human metallo-beta-lactamase domain-containing protein 1 and related proteins; ...
 11-172 1.27e-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: 1.27e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437577626  11 SCTYTYLIGStfsKHAIIIDPvrSQVSHYINLINKL-ELNLVAS-ID----THLHADHItgsGQLTILTD---CHSMIGM 81
Cdd:cd07711    21 SSTVTLIKDG---GKNILVDT--GTPWDRDLLLKALaEHGLSPEdIDyvvlTHGHPDHI---GNLNLFPNatvIVGWDIC 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437577626  82 ESKAKFVHIKFHDNEILnFGNIKIkaMHTPGHTPDSYCFVMEDR-----IFTGDTLL--INATGRTDFQNGSA--SAQYD 152
Cdd:cd07711    93 GDSYDDHSLEEGDGYEI-DENVEV--IPTPGHTPEDVSVLVETEkkgtvAVAGDLFEreEDLEDPILWDPLSEdpELQEE 169

                         170       180
                  ....*....|....*....|
gi 1437577626 153 SLfNKLLKLPGFmrIYPGHD 172
Cdd:cd07711   170 SR-KRILALADW--IIPGHG 186
PRK10241 PRK10241
hydroxyacylglutathione hydrolase; Provisional
 27-173 1.50e-05

hydroxyacylglutathione hydrolase; Provisional


Pssm-ID: 182327 [Multi-domain]  Cd Length: 251  Bit Score: 44.82  E-value: 1.50e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437577626  27 IIIDPvrSQVSHYINLINKLELNLVASIDTHLHADHITGSGQLTILTDCHSMIG-MESKAKFVHIKFHDNEILNFGNIKI 105
Cdd:PRK10241   25 LIVDP--GEAEPVLNAIAENNWQPEAIFLTHHHHDHVGGVKELVEKFPQIVVYGpQETQDKGTTQVVKDGETAFVLGHEF 102

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1437577626 106 KAMHTPGHTPDSYCFVMEDRIFTGDTLLINATGRTdFQnGSASAQYDSlFNKLLKLPGFMRIYPGHDY 173
Cdd:PRK10241  103 SVFATPGHTLGHICYFSKPYLFCGDTLFSGGCGRL-FE-GTASQMYQS-LKKINALPDDTLICCAHEY 167
YmaE-like_MBL-fold cd07727
uncharacterized subgroup which includes Bacillus subtilis YmaE and related proteins; MBL-fold ...
 105-171 2.11e-04

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: 40.64  E-value: 2.11e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1437577626 105 IKAMHTPGHTPDSYCFVMEDR--IFTGDTLLINATGRT-----DFQNGSASAQYDSLfNKLLKLPgFMRIYPGH 171
Cdd:cd07727   104 LTLIPVPGHTRGSVVLLYKEKgvLFTGDHLAWSRRRGWlsafrYVCWYSWPEQAESV-ERLADLD-FEWVLPGH 175
GOB1-like_MBL-B3 cd16308
Elizabethkingia meningoseptica GOB-1 and related metallo-beta-lactamases, subclass B3; ...
 56-123 2.67e-04

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: 40.92  E-value: 2.67e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437577626  56 THLHADHITGSGQLTILTDCHSMIGmESKAK------------------FVHIK----FHDNEILNFGNIKIKAMHTPGH 113
Cdd:cd16308    67 TQAHYDHVGAMAAIKQQTGAKMMVD-EKDAKvladggksdyemggygstFAPVKadklLHDGDTIKLGGTKLTLLHHPGH 145

                          90
                  ....*....|
gi 1437577626 114 TPDSYCFVME 123
Cdd:cd16308   146 TKGSCSFLFD 155
ElaC COG1234
Ribonuclease BN, tRNA processing enzyme [Translation, ribosomal structure and biogenesis];
56-131 3.00e-04

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


Pssm-ID: 440847 [Multi-domain]  Cd Length: 250  Bit Score: 40.95  E-value: 3.00e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437577626  56 THLHADHITG-------------SGQLTI---------LTDCHSMIGMESKAKFVHIKFHDNEILNFGNIKIKAMHTPgH 113
Cdd:COG1234    59 THLHGDHIAGlpgllstrslagrEKPLTIygppgtkefLEALLKASGTDLDFPLEFHEIEPGEVFEIGGFTVTAFPLD-H 137

                          90       100
                  ....*....|....*....|..
gi 1437577626 114 TPDSYCFVMEDR----IFTGDT 131
Cdd:COG1234   138 PVPAYGYRFEEPgrslVYSGDT 159
BJP-1_FEZ-1-like_MBL-B3 cd16288
BJP-1, FEZ-1, GOB-1, Mbl1b and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 54-123 6.12e-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: 40.00  E-value: 6.12e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437577626  54 IDTHLHADHITGSGQLTILTDCHSMIG------MESKAKF---------------VHIKFHDNEILNFGNIKIKAMHTPG 112
Cdd:cd16288    65 LNSHAHLDHAGGLAALKKLTGAKLMASaedaalLASGGKSdfhygddslafppvkVDRVLKDGDRVTLGGTTLTAHLTPG 144

                          90
                  ....*....|.
gi 1437577626 113 HTPDSYCFVME 123
Cdd:cd16288   145 HTRGCTTWTMT 155
UlaG COG2220
L-ascorbate lactonase UlaG, metallo-beta-lactamase superfamily [Carbohydrate transport and ...
 9-134 6.16e-04

L-ascorbate lactonase UlaG, metallo-beta-lactamase superfamily [Carbohydrate transport and metabolism];


Pssm-ID: 441822 [Multi-domain]  Cd Length: 224  Bit Score: 39.90  E-value: 6.16e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437577626   9 QDSCTYTYLIGSTF----SKHAIIIDPVRSQVSHYINLiNKLELNLVASID----THLHADHITGSGQLTILTDCHSMIG 80
Cdd:COG2220     1 PGGMKITWLGHATFlietGGKRILIDPVFSGRASPVNP-LPLDPEDLPKIDavlvTHDHYDHLDDATLRALKRTGATVVA 79

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1437577626  81 MESKAKFVH-------IKFHDNEILNFGNIKIK---AMHTPGHTPDSYC----FVMED---RIF-TGDTLLI 134
Cdd:COG2220    80 PLGVAAWLRawgfprvTELDWGESVELGGLTVTavpARHSSGRPDRNGGlwvgFVIETdgkTIYhAGDTGYF 151
AHL_lactonase_MBL-fold cd07729
quorum-quenching N-acyl-homoserine lactonase, MBL-fold metallo-hydrolase domain; Acyl ...
 56-172 6.55e-04

quorum-quenching N-acyl-homoserine lactonase, MBL-fold metallo-hydrolase domain; Acyl Homoserine Lactones (also known as AHLs) are signal molecules which coordinate gene expression in quorum sensing, in many Gram-negative bacteria. Quorum-quenching N-acyl-homoserine lactonase (also known as AHL lactonase, N-acyl-L-homoserine lactone hydrolase, EC 3.1.1.81) catalyzes the hydrolysis and opening of the homoserine lactone rings of AHLs, a reaction that can block quorum sensing. These enzymes belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions.


Pssm-ID: 293815 [Multi-domain]  Cd Length: 238  Bit Score: 39.89  E-value: 6.55e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437577626  56 THLHADHItgsGQL------TIL--------------TDCHSMIGMESKAKFVH---IKFHDNEILNFGNIKIkaMHTPG 112
Cdd:cd07729    95 SHLHFDHA---GGLdlfpnaTIIvqraeleyatgpdpLAAGYYEDVLALDDDLPggrVRLVDGDYDLFPGVTL--IPTPG 169

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1437577626 113 HTPDSYCFV--MEDR--IFTGDT--LLIN-ATGRTDFQNGSASAQYDSL--FNKLLKLPGfMRIYPGHD 172
Cdd:cd07729   170 HTPGHQSVLvrLPEGtvLLAGDAayTYENlEEGRPPGINYDPEAALASLerLKALAEREG-ARVIPGHD 237
metallo-hydrolase-like_MBL-fold cd16277
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 52-132 1.97e-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: 1.97e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437577626  52 ASID----THLHADHItgsGQLTILTD---------------------CHSMIGMES--------------KAKFVHIKF 92
Cdd:cd16277    62 EDVDyvlcTHLHVDHV---GWNTRLVDgrwvptfpnarylfsraeydhWSSPDAGGPpnrgvfedsvlpviEAGLADLVD 138

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1437577626  93 HDNEILNfgniKIKAMHTPGHTPDSYCFVMEDR----IFTGDTL 132
Cdd:cd16277   139 DDHEILD----GIRLEPTPGHTPGHVSVELESGgeraLFTGDVM 178
metallo-hydrolase-like_MBL-fold cd16280
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 56-124 6.55e-03

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


Pssm-ID: 293838 [Multi-domain]  Cd Length: 251  Bit Score: 36.79  E-value: 6.55e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437577626  56 THLHADHITG-------SGQLTILT--DCHSMIGMESKAKF--------VHIKFHDNEILNFGNIKIKAMHTPGHTPD-- 116
Cdd:cd16280    68 THGHGDHYGGaaylkdlYGAKVVMSeaDWDMMEEPPEEGDNprwgpppeRDIVIKDGDTLTLGDTTITVYLTPGHTPGtl 147


                  ....*...
gi 1437577626 117 SYCFVMED 124
Cdd:cd16280   148 SLIFPVKD 155
 
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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