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Conserved domains on  [gi|406855417|ref|NP_001258365|]
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hydroxyacylglutathione hydrolase-like protein isoform d [Mus musculus]

Protein Classification

hydroxyacylglutathione hydrolase( domain architecture ID 1004484)

hydroxyacylglutathione hydrolase catalyzes the hydrolysis of S-D-lactoyl-glutathione to form glutathione and D-lactic acid

CATH:  3.60.15.10
EC:  3.1.2.6
Gene Ontology:  GO:0004416|GO:0019243|GO:0046872
SCOP:  4002292

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PLN02469 super family cl31885
hydroxyacylglutathione hydrolase
 1-197 4.21e-75

hydroxyacylglutathione hydrolase


The actual alignment was detected with superfamily member PLN02469:

Pssm-ID: 178088 [Multi-domain]  Cd Length: 258  Bit Score: 228.11  E-value: 4.21e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406855417   1 MVLSTHHHWDHTRGNAELAHILPGLAVLG-ADERICALTRRLEHGEGLQFGA-IHVRCLLTPGHTSGHMSYFLWEDDCPD 78
Cdd:PLN02469  49 LVLTTHHHWDHAGGNEKIKKLVPGIKVYGgSLDNVKGCTHPVENGDKLSLGKdVNILALHTPCHTKGHISYYVTGKEGED 128

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406855417  79 sPALFSGDALSVAGCGWHLEDTAQQMYQSLAKTLGTLPPETKVFCGHEHTLSNLEFAQKVEPCNEHVQAKLSWAQERDDE 158
Cdd:PLN02469 129 -PAVFTGDTLFIAGCGKFFEGTAEQMYQSLCVTLGSLPKPTQVYCGHEYTVKNLKFALTVEPDNEKLKQKLEWAEKQRQA 207

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 406855417 159 DIPTVPSTLGEELMYNPFLRVTEDAVRAFTGQVAPAQVL 197
Cdd:PLN02469 208 GLPTVPSTIEEELETNPFMRVDLPEIQEKVGCESPVEAL 246
 
Name Accession Description Interval E-value
PLN02469 PLN02469
hydroxyacylglutathione hydrolase
 1-197 4.21e-75

hydroxyacylglutathione hydrolase


Pssm-ID: 178088 [Multi-domain]  Cd Length: 258  Bit Score: 228.11  E-value: 4.21e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406855417   1 MVLSTHHHWDHTRGNAELAHILPGLAVLG-ADERICALTRRLEHGEGLQFGA-IHVRCLLTPGHTSGHMSYFLWEDDCPD 78
Cdd:PLN02469  49 LVLTTHHHWDHAGGNEKIKKLVPGIKVYGgSLDNVKGCTHPVENGDKLSLGKdVNILALHTPCHTKGHISYYVTGKEGED 128

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406855417  79 sPALFSGDALSVAGCGWHLEDTAQQMYQSLAKTLGTLPPETKVFCGHEHTLSNLEFAQKVEPCNEHVQAKLSWAQERDDE 158
Cdd:PLN02469 129 -PAVFTGDTLFIAGCGKFFEGTAEQMYQSLCVTLGSLPKPTQVYCGHEYTVKNLKFALTVEPDNEKLKQKLEWAEKQRQA 207

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 406855417 159 DIPTVPSTLGEELMYNPFLRVTEDAVRAFTGQVAPAQVL 197
Cdd:PLN02469 208 GLPTVPSTIEEELETNPFMRVDLPEIQEKVGCESPVEAL 246
GSH_gloB TIGR03413
hydroxyacylglutathione hydrolase; Members of this protein family are hydroxyacylglutathione ...
 1-207 5.07e-72

hydroxyacylglutathione hydrolase; Members of this protein family are hydroxyacylglutathione hydrolase, a detoxification enzyme known as glyoxalase II. It follows lactoylglutathione lyase, or glyoxalase I, and acts to remove the toxic metabolite methylglyoxal and related compounds. This protein belongs to the broader metallo-beta-lactamase family (pfam00753). [Cellular processes, Detoxification]


Pssm-ID: 274569 [Multi-domain]  Cd Length: 248  Bit Score: 219.71  E-value: 5.07e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406855417    1 MVLSTHHHWDHTRGNAELAHILPgLAVLG-ADERICALTRRLEHGEGLQFGAIHVRCLLTPGHTSGHMSYFLweddcPDS 79
Cdd:TIGR03413  46 AILLTHHHHDHVGGVAELLEAFP-APVYGpAEERIPGITHPVKDGDTVTLGGLEFEVLAVPGHTLGHIAYYL-----PDS 119

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406855417   80 PALFSGDALSVAGCGWHLEDTAQQMYQSLAKtLGTLPPETKVFCGHEHTLSNLEFAQKVEPCNEHVQAKLSWAQERDDED 159
Cdd:TIGR03413 120 PALFCGDTLFSAGCGRLFEGTPEQMYDSLQR-LAALPDDTLVYCAHEYTLSNLRFALTVEPDNPALQERLKEVEALRAQG 198

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 406855417  160 IPTVPSTLGEELMYNPFLRVTEDAVRAFTGQVA--PAQVLEALCRERARF 207
Cdd:TIGR03413 199 QPTLPSTLGLERATNPFLRADDPAVRAALGSQGadPVEVFAALRAWKDNF 248
hydroxyacylglutathione_hydrolase_MBL-fold cd07723
hydroxyacylglutathione hydrolase, MBL-fold metallo-hydrolase domain; hydroxyacylglutathione ...
 1-125 1.52e-52

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: 167.25  E-value: 1.52e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406855417   1 MVLSTHHHWDHTRGNAELAHILPGLAVLG-ADERICALTRRLEHGEGLQFGAIHVRCLLTPGHTSGHMSYFLweddcPDS 79
Cdd:cd07723   46 AILTTHHHWDHTGGNAELKALFPDAPVYGpAEDRIPGLDHPVKDGDEIKLGGLEVKVLHTPGHTLGHICYYV-----PDE 120

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 406855417  80 PALFSGDALSVAGCGWHLEDTAQQMYQSLAKtLGTLPPETKVFCGH 125
Cdd:cd07723  121 PALFTGDTLFSGGCGRFFEGTAEQMYASLQK-LLALPDDTLVYCGH 165
HAGH_C pfam16123
Hydroxyacylglutathione hydrolase C-terminus; This domain is found at the C-terminus of ...
 126-207 7.68e-35

Hydroxyacylglutathione hydrolase C-terminus; This domain is found at the C-terminus of hydroxyacylglutathione hydrolase enzymes. Substrate binding occurs at the interface between this domain and the catalytic domain (pfam00753).


Pssm-ID: 465030 [Multi-domain]  Cd Length: 82  Bit Score: 119.08  E-value: 7.68e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406855417  126 EHTLSNLEFAQKVEPCNEHVQAKLSWAQERDDEDIPTVPSTLGEELMYNPFLRVTEDAVRAFTGQVAPAQVLEALCRERA 205
Cdd:pfam16123   1 EYTLSNLKFALSVEPDNEALQKRLAWVEALRAAGEPTVPSTLGDEKATNPFLRVDDPAVQKATGETDPVEVFAALRELKD 80


                  ..
gi 406855417  206 RF 207
Cdd:pfam16123  81 NF 82
GloB COG0491
Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General ...
 2-130 4.78e-24

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: 95.53  E-value: 4.78e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406855417   2 VLSTHHHWDHTRGNAELA---------------HILPGLAVLGADERICALTRRLEHGEGLQFGAIHVRCLLTPGHTSGH 66
Cdd:COG0491   55 VLLTHLHPDHVGGLAALAeafgapvyahaaeaeALEAPAAGALFGREPVPPDRTLEDGDTLELGGPGLEVIHTPGHTPGH 134

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 406855417  67 MSYFLweddcPDSPALFSGDALSVAGCGW--HLEDTAQQMYQSLAKtLGTLPPETkVFCGHEHTLS 130
Cdd:COG0491  135 VSFYV-----PDEKVLFTGDALFSGGVGRpdLPDGDLAQWLASLER-LLALPPDL-VIPGHGPPTT 193
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 2-125 2.85e-19

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: 81.83  E-value: 2.85e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406855417     2 VLSTHHHWDHTRGNAELAHI------------------LPGLAVLGADERICALTRRLEHGEGLQFGAIHVRCLLTPGHT 63
Cdd:smart00849  39 IILTHGHPDHIGGLPELLEApgapvyapegtaellkdlLALLGELGAEAEPAPPDRTLKDGDELDLGGGELEVIHTPGHT 118

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 406855417    64 SGHMSYFLweddcPDSPALFSGDALSVAGCG-WHLEDTAQQMYQSLAKTLGTL-PPETKVFCGH 125
Cdd:smart00849 119 PGSIVLYL-----PEGKILFTGDLLFAGGDGrTLVDGGDAAASDALESLLKLLkLLPKLVVPGH 177
 
Name Accession Description Interval E-value
PLN02469 PLN02469
hydroxyacylglutathione hydrolase
 1-197 4.21e-75

hydroxyacylglutathione hydrolase


Pssm-ID: 178088 [Multi-domain]  Cd Length: 258  Bit Score: 228.11  E-value: 4.21e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406855417   1 MVLSTHHHWDHTRGNAELAHILPGLAVLG-ADERICALTRRLEHGEGLQFGA-IHVRCLLTPGHTSGHMSYFLWEDDCPD 78
Cdd:PLN02469  49 LVLTTHHHWDHAGGNEKIKKLVPGIKVYGgSLDNVKGCTHPVENGDKLSLGKdVNILALHTPCHTKGHISYYVTGKEGED 128

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406855417  79 sPALFSGDALSVAGCGWHLEDTAQQMYQSLAKTLGTLPPETKVFCGHEHTLSNLEFAQKVEPCNEHVQAKLSWAQERDDE 158
Cdd:PLN02469 129 -PAVFTGDTLFIAGCGKFFEGTAEQMYQSLCVTLGSLPKPTQVYCGHEYTVKNLKFALTVEPDNEKLKQKLEWAEKQRQA 207

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 406855417 159 DIPTVPSTLGEELMYNPFLRVTEDAVRAFTGQVAPAQVL 197
Cdd:PLN02469 208 GLPTVPSTIEEELETNPFMRVDLPEIQEKVGCESPVEAL 246
GSH_gloB TIGR03413
hydroxyacylglutathione hydrolase; Members of this protein family are hydroxyacylglutathione ...
 1-207 5.07e-72

hydroxyacylglutathione hydrolase; Members of this protein family are hydroxyacylglutathione hydrolase, a detoxification enzyme known as glyoxalase II. It follows lactoylglutathione lyase, or glyoxalase I, and acts to remove the toxic metabolite methylglyoxal and related compounds. This protein belongs to the broader metallo-beta-lactamase family (pfam00753). [Cellular processes, Detoxification]


Pssm-ID: 274569 [Multi-domain]  Cd Length: 248  Bit Score: 219.71  E-value: 5.07e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406855417    1 MVLSTHHHWDHTRGNAELAHILPgLAVLG-ADERICALTRRLEHGEGLQFGAIHVRCLLTPGHTSGHMSYFLweddcPDS 79
Cdd:TIGR03413  46 AILLTHHHHDHVGGVAELLEAFP-APVYGpAEERIPGITHPVKDGDTVTLGGLEFEVLAVPGHTLGHIAYYL-----PDS 119

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406855417   80 PALFSGDALSVAGCGWHLEDTAQQMYQSLAKtLGTLPPETKVFCGHEHTLSNLEFAQKVEPCNEHVQAKLSWAQERDDED 159
Cdd:TIGR03413 120 PALFCGDTLFSAGCGRLFEGTPEQMYDSLQR-LAALPDDTLVYCAHEYTLSNLRFALTVEPDNPALQERLKEVEALRAQG 198

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 406855417  160 IPTVPSTLGEELMYNPFLRVTEDAVRAFTGQVA--PAQVLEALCRERARF 207
Cdd:TIGR03413 199 QPTLPSTLGLERATNPFLRADDPAVRAALGSQGadPVEVFAALRAWKDNF 248
hydroxyacylglutathione_hydrolase_MBL-fold cd07723
hydroxyacylglutathione hydrolase, MBL-fold metallo-hydrolase domain; hydroxyacylglutathione ...
 1-125 1.52e-52

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: 167.25  E-value: 1.52e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406855417   1 MVLSTHHHWDHTRGNAELAHILPGLAVLG-ADERICALTRRLEHGEGLQFGAIHVRCLLTPGHTSGHMSYFLweddcPDS 79
Cdd:cd07723   46 AILTTHHHWDHTGGNAELKALFPDAPVYGpAEDRIPGLDHPVKDGDEIKLGGLEVKVLHTPGHTLGHICYYV-----PDE 120

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 406855417  80 PALFSGDALSVAGCGWHLEDTAQQMYQSLAKtLGTLPPETKVFCGH 125
Cdd:cd07723  121 PALFTGDTLFSGGCGRFFEGTAEQMYASLQK-LLALPDDTLVYCGH 165
PLN02398 PLN02398
hydroxyacylglutathione hydrolase
 2-207 5.15e-49

hydroxyacylglutathione hydrolase


Pssm-ID: 215223 [Multi-domain]  Cd Length: 329  Bit Score: 163.48  E-value: 5.15e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406855417   2 VLSTHHHWDHTRGNAELAHILpGLAVLGAD---ERICALTRRLEHGEGLQFGAIHVRCLLTPGHTSGHMSYFLweddcPD 78
Cdd:PLN02398 125 ILNTHHHYDHTGGNLELKARY-GAKVIGSAvdkDRIPGIDIVLKDGDKWMFAGHEVLVMETPGHTRGHISFYF-----PG 198

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406855417  79 SPALFSGDALSVAGCGWHLEDTAQQMYQSLAKTLgTLPPETKVFCGHEHTLSNLEFAQKVEPCNEHVQAKLSWAQERDDE 158
Cdd:PLN02398 199 SGAIFTGDTLFSLSCGKLFEGTPEQMLSSLQKII-SLPDDTNIYCGHEYTLSNSKFALSIEPNNEVLQSYAAHVAHLRSK 277

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 406855417 159 DIPTVPSTLGEELMYNPFLRVTEDAVR---AFTGQVAPAQVLEALCRERARF 207
Cdd:PLN02398 278 GLPTIPTTVKMEKACNPFLRTSSTDIRkslSIPDTADEAEALGIIRRAKDNF 329
HAGH_C pfam16123
Hydroxyacylglutathione hydrolase C-terminus; This domain is found at the C-terminus of ...
 126-207 7.68e-35

Hydroxyacylglutathione hydrolase C-terminus; This domain is found at the C-terminus of hydroxyacylglutathione hydrolase enzymes. Substrate binding occurs at the interface between this domain and the catalytic domain (pfam00753).


Pssm-ID: 465030 [Multi-domain]  Cd Length: 82  Bit Score: 119.08  E-value: 7.68e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406855417  126 EHTLSNLEFAQKVEPCNEHVQAKLSWAQERDDEDIPTVPSTLGEELMYNPFLRVTEDAVRAFTGQVAPAQVLEALCRERA 205
Cdd:pfam16123   1 EYTLSNLKFALSVEPDNEALQKRLAWVEALRAAGEPTVPSTLGDEKATNPFLRVDDPAVQKATGETDPVEVFAALRELKD 80


                  ..
gi 406855417  206 RF 207
Cdd:pfam16123  81 NF 82
PRK10241 PRK10241
hydroxyacylglutathione hydrolase; Provisional
 2-183 3.41e-33

hydroxyacylglutathione hydrolase; Provisional


Pssm-ID: 182327 [Multi-domain]  Cd Length: 251  Bit Score: 120.31  E-value: 3.41e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406855417   2 VLSTHHHWDHTRGNAELAHILPGLAVLGADE-RICALTRRLEHGEGLQFGAIHVRCLLTPGHTSGHMSYFlweddcpDSP 80
Cdd:PRK10241  49 IFLTHHHHDHVGGVKELVEKFPQIVVYGPQEtQDKGTTQVVKDGETAFVLGHEFSVFATPGHTLGHICYF-------SKP 121

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406855417  81 ALFSGDALSVAGCGWHLEDTAQQMYQSLAKtLGTLPPETKVFCGHEHTLSNLEFAQKVEPCNEHVQAKLSWAQERDDEDI 160
Cdd:PRK10241 122 YLFCGDTLFSGGCGRLFEGTASQMYQSLKK-INALPDDTLICCAHEYTLSNMKFALSILPHDLSINDYYRKVKELRAKNQ 200

                        170       180
                 ....*....|....*....|...
gi 406855417 161 PTVPSTLGEELMYNPFLRvTEDA 183
Cdd:PRK10241 201 ITLPVILKNERQINLFLR-TEDI 222
BaeB-like_MBL-fold cd16275
Bacillus amyloliquefaciens BaeB and related proteins; MBL-fold metallo hydrolase domain; ...
 1-125 4.07e-24

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: 94.53  E-value: 4.07e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406855417   1 MVLSTHHHWDHTRGNAELAHILPGLAVLGADERI-----CALTRRLEHGEGLQFGAIHVRCLLTPGHTSGHMSYFLweDD 75
Cdd:cd16275   50 GILLTHSHFDHVNLVEPLLAKYDAPVYMSKEEIDyygfrCPNLIPLEDGDTIKIGDTEITCLLTPGHTPGSMCYLL--GD 127

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 406855417  76 CpdspaLFSGDALSVAGCGwhLEDT----AQQMYQSLAKTLGTLPPETKVFCGH 125
Cdd:cd16275  128 S-----LFTGDTLFIEGCG--RCDLpggdPEEMYESLQRLKKLPPPNTRVYPGH 174
metallo-hydrolase-like_MBL-fold cd06262
mainly hydrolytic enzymes and related proteins which carry out various biological functions; ...
 1-125 4.46e-24

mainly hydrolytic enzymes and related proteins which carry out various biological functions; MBL-fold metallohydrolase domain; Members of the MBL-fold metallohydrolase superfamily are mainly hydrolytic enzymes which carry out a variety of biological functions. The class B metal beta-lactamases (MBLs) for which this fold was named perform only a small fraction of the activities included in this superfamily. Activities carried out by superfamily members include class B beta-lactamases which can catalyze the hydrolysis of a wide range of beta-lactam antibiotics, hydroxyacylglutathione hydrolases (also called glyoxalase II) which hydrolyze S-d-lactoylglutathione to d-lactate in the second step of the glycoxlase system, AHL lactonases which catalyze the hydrolysis and opening of the homoserine lactone rings of acyl homoserine lactones (AHLs), persulfide dioxygenase which catalyze the oxidation of glutathione persulfide to glutathione and persulfite in the mitochondria, flavodiiron proteins which catalyze the reduction of oxygen and/or nitric oxide to water or nitrous oxide respectively, cleavage and polyadenylation specificity factors such as the Int9 and Int11 subunits of Integrator, Sdsa1-like and AtsA-like arylsulfatases, 5'-exonucleases human SNM1A and yeast Pso2p, ribonuclease J which has both 5'-3' exoribonucleolytic and endonucleolytic activity and ribonuclease Z which catalyzes the endonucleolytic removal of the 3' extension of the majority of tRNA precursors, cyclic nucleotide phosphodiesterases which decompose cyclic adenosine and guanosine 3', 5'-monophosphate (cAMP and cGMP) respectively, insecticide hydrolases, and proteins required for natural transformation competence. The diversity of biological roles is reflected in variations in the active site metallo-chemistry, for example classical members of the superfamily are di-, or less commonly mono-, zinc-ion-dependent hydrolases, human persulfide dioxygenase ETHE1 is a mono-iron binding member of the superfamily; Arabidopsis thaliana hydroxyacylglutathione hydrolases incorporates iron, manganese, and zinc in its dinuclear metal binding site, and flavodiiron proteins contains a diiron site.


Pssm-ID: 293792 [Multi-domain]  Cd Length: 188  Bit Score: 94.66  E-value: 4.46e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406855417   1 MVLSTHHHWDHTRGNAEL---------AH----------ILPGLAVLGADERICALTRRLEHGEGLQFGAIHVRCLLTPG 61
Cdd:cd06262   48 AILLTHGHFDHIGGLAELkeapgapvyIHeadaelledpELNLAFFGGGPLPPPEPDILLEDGDTIELGGLELEVIHTPG 127

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 406855417  62 HTSGHMSYFlweddCPDSPALFSGDALSVAGCG-WHLEDT-AQQMYQSLAKTLGTLPPETKVFCGH 125
Cdd:cd06262  128 HTPGSVCFY-----IEEEGVLFTGDTLFAGSIGrTDLPGGdPEQLIESIKKLLLLLPDDTVVYPGH 188
GloB COG0491
Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General ...
 2-130 4.78e-24

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: 95.53  E-value: 4.78e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406855417   2 VLSTHHHWDHTRGNAELA---------------HILPGLAVLGADERICALTRRLEHGEGLQFGAIHVRCLLTPGHTSGH 66
Cdd:COG0491   55 VLLTHLHPDHVGGLAALAeafgapvyahaaeaeALEAPAAGALFGREPVPPDRTLEDGDTLELGGPGLEVIHTPGHTPGH 134

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 406855417  67 MSYFLweddcPDSPALFSGDALSVAGCGW--HLEDTAQQMYQSLAKtLGTLPPETkVFCGHEHTLS 130
Cdd:COG0491  135 VSFYV-----PDEKVLFTGDALFSGGVGRpdLPDGDLAQWLASLER-LLALPPDL-VIPGHGPPTT 193
POD-like_MBL-fold cd07724
ETHE1 (PDO type I), persulfide dioxygenase A (PDOA, PDO type II) and related proteins; ...
 2-125 1.38e-23

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: 93.23  E-value: 1.38e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406855417   2 VLSTHHHWDHTRGNAELAHILPGLAVLGADERICALTRRLEHGEGLQFGAIHVRCLLTPGHTSGHMSYfLWEDdcPDspA 81
Cdd:cd07724   52 VLETHVHADHVSGARELAERTGAPIVIGEGAPASFFDRLLKDGDVLELGNLTLEVLHTPGHTPESVSY-LVGD--PD--A 126

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 406855417  82 LFSGDALSVAGCG-----WHLEDTAQQMYQSLAKTLGTLPPETKVFCGH 125
Cdd:cd07724  127 VFTGDTLFVGDVGrpdlpGEAEGLARQLYDSLQRKLLLLPDETLVYPGH 175
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 2-125 2.85e-19

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: 81.83  E-value: 2.85e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406855417     2 VLSTHHHWDHTRGNAELAHI------------------LPGLAVLGADERICALTRRLEHGEGLQFGAIHVRCLLTPGHT 63
Cdd:smart00849  39 IILTHGHPDHIGGLPELLEApgapvyapegtaellkdlLALLGELGAEAEPAPPDRTLKDGDELDLGGGELEVIHTPGHT 118

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 406855417    64 SGHMSYFLweddcPDSPALFSGDALSVAGCG-WHLEDTAQQMYQSLAKTLGTL-PPETKVFCGH 125
Cdd:smart00849 119 PGSIVLYL-----PEGKILFTGDLLFAGGDGrTLVDGGDAAASDALESLLKLLkLLPKLVVPGH 177
PLN02962 PLN02962
hydroxyacylglutathione hydrolase
 2-182 5.16e-16

hydroxyacylglutathione hydrolase


Pssm-ID: 178547 [Multi-domain]  Cd Length: 251  Bit Score: 74.45  E-value: 5.16e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406855417   2 VLSTHHHWDHTRGNAELAHILPGLAVLGADERICALTRRLEHGEGLQFGAIHVRCLLTPGHTSGHMSYFLWE-DDCPDSP 80
Cdd:PLN02962  65 AMNTHVHADHVTGTGLLKTKLPGVKSIISKASGSKADLFVEPGDKIYFGDLYLEVRATPGHTAGCVTYVTGEgPDQPQPR 144

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406855417  81 ALFSGDALSVAGCGW--HLEDTAQQMYQSLAKTLGTLPPETKVFCGHE---HTLsnlefaqkvepcnehvqaklswaqer 155
Cdd:PLN02962 145 MAFTGDALLIRGCGRtdFQGGSSDQLYKSVHSQIFTLPKDTLIYPAHDykgFTV-------------------------- 198

                        170       180
                 ....*....|....*....|....*..
gi 406855417 156 ddediptvpSTLGEELMYNPflRVTED 182
Cdd:PLN02962 199 ---------STVGEEMLYNP--RLTKD 214
TTHA1623-like_MBL-fold cd16322
uncharacterized Thermus thermophilus TTHA1623 and related proteins; MBL-fold metallo hydrolase ...
 2-177 3.08e-15

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: 71.61  E-value: 3.08e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406855417   2 VLSTHHHWDHTRGNAELAHILPGLAVLGAD-------------------ERICALTRRLEHGEGLQFGAIHVRCLLTPGH 62
Cdd:cd16322   50 ILLTHAHFDHVGGVADLRRHPGAPVYLHPDdlplyeaadlgakafglgiEPLPPPDRLLEDGQTLTLGGLEFKVLHTPGH 129

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406855417  63 TSGHMSYFlweddCPDSPALFSGDAL---SVAGCGWHLEDtAQQMYQSLAKTLgTLPPETKVFCGHehtlsnlefaqkve 139
Cdd:cd16322  130 SPGHVCFY-----VEEEGLLFSGDLLfqgSIGRTDLPGGD-PKAMAASLRRLL-TLPDETRVFPGH-------------- 188

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 406855417 140 pcnehvqaklswaqerddedipTVPSTLGEELMYNPFL 177
Cdd:cd16322  189 ----------------------GPPTTLGEERRTNPFL 204
metallo-hydrolase-like_MBL-fold cd16278
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 2-86 3.84e-14

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: 68.29  E-value: 3.84e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406855417   2 VLSTHHHWDHTRGNAELAHiLPGLAVLGADERI-------CALTRRLEHGEGLQFGAIHVRCLLTPGHTSGHMSYFLwed 74
Cdd:cd16278   57 ILVTHTHRDHSPGAARLAE-RTGAPVRAFGPHRaggqdtdFAPDRPLADGEVIEGGGLRLTVLHTPGHTSDHLCFAL--- 132

                         90
                 ....*....|..
gi 406855417  75 dcPDSPALFSGD 86
Cdd:cd16278  133 --EDEGALFTGD 142
YcbL-like_MBL-fold cd07737
Salmonella enterica serovar typhimurium YcbL and related proteins; MBL-fold metallo hydrolase ...
 2-125 5.25e-11

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: 59.87  E-value: 5.25e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406855417   2 VLSTHHHWDHTRGNAELA----------HI--------LPGLAVL--GADERICALTRRLEHGEGLQFGAIHVRCLLTPG 61
Cdd:cd07737   50 ILLTHGHLDHVGGAAELAehygvpiigpHKedkfllenLPEQSQMfgFPPAEAFTPDRWLEEGDTVTVGNLTLEVLHCPG 129

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 406855417  62 HTSGHMSYFlweddCPDSPALFSGDAL---SVAGCGWHLEDTaQQMYQSLAKTLGTLPPETKVFCGH 125
Cdd:cd07737  130 HTPGHVVFF-----NRESKLAIVGDVLfkgSIGRTDFPGGNH-AQLIASIKEKLLPLGDDVTFIPGH 190
yflN-like_MBL-fold cd07721
uncharacterized subgroup which includes Bacillus subtilis yflN; MBL-fold metallo hydrolase ...
 5-125 8.97e-11

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: 59.16  E-value: 8.97e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406855417   5 THHHWDHTrGNAELAHILPGLAVL-GADE----------------------------RICALTRRLEHGEGLQF-GAIHV 54
Cdd:cd07721   56 THGHIDHI-GSLAALKEAPGAPVYaHEREapylegekpypppvrlgllgllspllpvKPVPVDRTLEDGDTLDLaGGLRV 134

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 406855417  55 rcLLTPGHTSGHMSYFLWEDDcpdspALFSGDAL-----SVAGCGWHLEDTAQQMYQSLAKtLGTLPPETkVFCGH 125
Cdd:cd07721  135 --IHTPGHTPGHISLYLEEDG-----VLIAGDALvtvggELVPPPPPFTWDMEEALESLRK-LAELDPEV-LAPGH 201
MBLAC2-like_MBL-fold cd07712
uncharacterized human metallo-beta-lactamase domain-containing protein 2 and related proteins; ...
 1-125 4.73e-10

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: 56.87  E-value: 4.73e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406855417   1 MVLSTHHHWDHTRGN----------AELAHI-----LPGLAVLGADERICA--LTRRLEHGEGLQFGAIHVRCLLTPGHT 63
Cdd:cd07712   45 LVVATHGHFDHIGGLhefeevyvhpADAEILaapdnFETLTWDAATYSVPPagPTLPLRDGDVIDLGDRQLEVIHTPGHT 124

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 406855417  64 SGHMSyfLWEddcPDSPALFSGDALSVAGCGWHLEDT-AQQMYQSLAKtLGTLPPE-TKVFCGH 125
Cdd:cd07712  125 PGSIA--LLD---RANRLLFSGDVVYDGPLIMDLPHSdLDDYLASLEK-LSKLPDEfDKVLPGH 182
TTHA1429-like_MBL-fold cd07725
uncharacterized Thermus thermophilus TTHA1429 and related proteins; MBL-fold metallo hydrolase ...
 2-125 1.77e-09

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: 55.38  E-value: 1.77e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406855417   2 VLSTHHHWDHTRGNAELAHilpglaVLGADErICALTRRLEHGEGLQFGAIHVRCLLTPGHTSGHMSYFlweddCPDSPA 81
Cdd:cd07725   59 VLLTHHHPDHIGLAGKLQE------KSGATV-YILDVTPVKDGDKIDLGGLRLKVIETPGHTPGHIVLY-----DEDRRE 126

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 406855417  82 LFSGDAL---SVAGCGWH---LEDTAQQMYQSLAKtLGTLPPEtKVFCGH 125
Cdd:cd07725  127 LFVGDAVlpkITPNVSLWavrVEDPLGAYLESLDK-LEKLDVD-LAYPGH 174
LACTB2-like_MBL-fold cd07722
uncharacterized subgroup which includes human lactamase beta 2 and related proteins; MBL-fold ...
 2-125 4.91e-09

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: 54.08  E-value: 4.91e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406855417   2 VLSTHHHWDHTRGnaeLAHIL-----------------PGLAVLGADERICaltrRLEHGEGLQFGAIHVRCLLTPGHTS 64
Cdd:cd07722   60 ILLTHWHHDHVGG---LPDVLdllrgpsprvykfprpeEDEDPDEDGGDIH----DLQDGQVFKVEGATLRVIHTPGHTT 132

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 406855417  65 GHMSYFLWEDDcpdspALFSGDalSVAGCGWH-LEDTAQQMyQSLAKTLGTLPpeTKVFCGH 125
Cdd:cd07722  133 DHVCFLLEEEN-----ALFTGD--CVLGHGTAvFEDLAAYM-ASLKKLLSLGP--GRIYPGH 184
ST1585-like_MBL-fold cd07726
uncharacterized subgroup which includes Sulfolobus tokodaii ST1585 protein; MBL-fold metallo ...
 2-119 1.91e-07

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: 49.80  E-value: 1.91e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406855417   2 VLSTHHHWDHTRGNAELAHILPG-----------------------LAVLGAD-------------ERICAltrrLEHGE 45
Cdd:cd07726   58 IILTHIHLDHAGGAGLLAEALPNakvyvhprgarhlidpsklwasaRAVYGDEadrlggeilpvpeERVIV----LEDGE 133

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406855417  46 GLQFGAIHVRCLLTPGHTSGHMSYFLweddcPDSPALFSGDALSVAGCGWHLEDTA---------QQMYQSLAKtLGTLP 116
Cdd:cd07726  134 TLDLGGRTLEVIDTPGHAPHHLSFLD-----EESDGLFTGDAAGVRYPELDVVGPPstpppdfdpEAWLESLDR-LLSLK 207


                 ...
gi 406855417 117 PET 119
Cdd:cd07726  208 PER 210
Lactamase_B pfam00753
Metallo-beta-lactamase superfamily;
2-125 1.84e-06

Metallo-beta-lactamase superfamily;


Pssm-ID: 425851 [Multi-domain]  Cd Length: 196  Bit Score: 46.98  E-value: 1.84e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406855417    2 VLSTHHHWDHTRGNAELAHILP--------GLAVLGADERICALTRRLEHG------------EGLQFGAIHVRCLL--- 58
Cdd:pfam00753  47 VILTHGHFDHIGGLGELAEATDvpvivvaeEARELLDEELGLAASRLGLPGppvvplppdvvlEEGDGILGGGLGLLvth 126

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 406855417   59 TPGHTSGHMSYFLweddcPDSPALFSGDALSVAGCGWH---------LEDTAQQMYQSLAKTLGTLPPEtKVFCGH 125
Cdd:pfam00753 127 GPGHGPGHVVVYY-----GGGKVLFTGDLLFAGEIGRLdlplggllvLHPSSAESSLESLLKLAKLKAA-VIVPGH 196
AHL_lactonase_MBL-fold cd07729
quorum-quenching N-acyl-homoserine lactonase, MBL-fold metallo-hydrolase domain; Acyl ...
 2-126 3.59e-06

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


Pssm-ID: 293815 [Multi-domain]  Cd Length: 238  Bit Score: 46.44  E-value: 3.59e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406855417   2 VLSTHHHWDHTrGNAEL---AHIL-----------PGLAVLGADERICALTRRLEhgeGLQFGAIH--------VRCLLT 59
Cdd:cd07729   92 VILSHLHFDHA-GGLDLfpnATIIvqraeleyatgPDPLAAGYYEDVLALDDDLP---GGRVRLVDgdydlfpgVTLIPT 167

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 406855417  60 PGHTSGHMSYFLwedDCPDSPALFSGDA---------LSVAGCGWHLEDTAQQMY--QSLAKTLGtlppeTKVFCGHE 126
Cdd:cd07729  168 PGHTPGHQSVLV---RLPEGTVLLAGDAaytyenleeGRPPGINYDPEAALASLErlKALAEREG-----ARVIPGHD 237
MBLAC1-like_MBL-fold cd07711
uncharacterized human metallo-beta-lactamase domain-containing protein 1 and related proteins; ...
 2-68 1.10e-05

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: 44.50  E-value: 1.10e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406855417   2 VLSTHHHWDHTrGNAEL---AHILPGLAVLGaderICALTRRLEHGEGLQFGAiHVRCLLTPGHTSGHMS 68
Cdd:cd07711   64 VVLTHGHPDHI-GNLNLfpnATVIVGWDICG----DSYDDHSLEEGDGYEIDE-NVEVIPTPGHTPEDVS 127
SMB-1-like_MBL-B3 cd16313
SMB-1, THIN-B and related metallo-beta-lactamases, subclass B3; MBL-fold metallo-hydrolase ...
 2-69 1.14e-05

SMB-1, THIN-B and related metallo-beta-lactamases, subclass B3; MBL-fold metallo-hydrolase domain; MBLs (class B of the Ambler beta-lactamase classification) are a diverse group of metallo-enzymes that are capable of catalyzing the hydrolysis of a wide range of beta-lactam antibiotics. MBLs have been divided into three subclasses B1, B2 and B3, based on sequence/structural relationships and substrates, with the B1 and B2 MBLs being most closely related to each other. This subgroup of SMB-1- and THIN-B-like MBLs belongs to the B3 subclass. Subclass B3 enzymes are most active with two zinc ions bound in the active site, and have a broad-spectrum substrate profile. These B3 enzymes have a modified Zn2/DCH site (Asp-His-His).


Pssm-ID: 293871 [Multi-domain]  Cd Length: 254  Bit Score: 45.24  E-value: 1.14e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406855417   2 VLSTHHHWDHTRGNAELAHiLPGLAVLGADERICAL-----------------------TRRLEHGEGLQFGAIHVRCLL 58
Cdd:cd16313   64 ILSSHDHWDHAGGIAALQK-LTGAQVLASPATVAVLrsgsmgkddpqfggltpmppvasVRAVRDGEVVKLGPLAVTAHA 142

                         90
                 ....*....|.
gi 406855417  59 TPGHTSGHMSY 69
Cdd:cd16313  143 TPGHTTGGTSW 153
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 ...
 2-115 5.29e-05

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: 43.11  E-value: 5.29e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406855417   2 VLSTHHHWDHTRGNAELAHI--------LPGLAVL------------GADERICALT--RRLEHGEGLQFGAIHVRCLLT 59
Cdd:cd16290   64 ILNSHAHFDHAGGIAALQRDsgatvaasPAGAAALrsggvdpddpqaGAADPFPPVAkvRVVADGEVVKLGPLAVTAHAT 143

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 406855417  60 PGHTSGHMSYfLWE----DDCPDspaLFSGDALS-VAGCGWHLEDTAQQ-MYQSLAKTLGTL 115
Cdd:cd16290  144 PGHTPGGTSW-TWRscegGRCLD---IVYADSLTaVSADGFRFSDDAHPaRVAAFRRSIATV 201
GOB1-like_MBL-B3 cd16308
Elizabethkingia meningoseptica GOB-1 and related metallo-beta-lactamases, subclass B3; ...
 1-71 7.35e-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: 39.76  E-value: 7.35e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406855417   1 MVLSTHHHWDHTRGNAELAHiLPGlAVLGADERICAL-----------------------TRRLEHGEGLQFGAIHVRCL 57
Cdd:cd16308   63 ILLTTQAHYDHVGAMAAIKQ-QTG-AKMMVDEKDAKVladggksdyemggygstfapvkaDKLLHDGDTIKLGGTKLTLL 140

                         90
                 ....*....|....
gi 406855417  58 LTPGHTSGHMSYFL 71
Cdd:cd16308  141 HHPGHTKGSCSFLF 154
metallo-hydrolase-like_MBL-fold cd16277
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 1-88 1.00e-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: 39.04  E-value: 1.00e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406855417   1 MVLSTHHHWDH----TR-----------------GNAELAH------------------ILP----GLAVL-GADERIca 36
Cdd:cd16277   66 YVLCTHLHVDHvgwnTRlvdgrwvptfpnarylfSRAEYDHwsspdaggppnrgvfedsVLPvieaGLADLvDDDHEI-- 143

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 406855417  37 ltrrlehGEGLQFgaihvrcLLTPGHTSGHMSYFLwedDCPDSPALFSGDAL 88
Cdd:cd16277  144 -------LDGIRL-------EPTPGHTPGHVSVEL---ESGGERALFTGDVM 178
 
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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