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Conserved domains on  [gi|406855413|ref|NP_001258363|]
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hydroxyacylglutathione hydrolase-like protein isoform b [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
 1-201 5.60e-79

hydroxyacylglutathione hydrolase


The actual alignment was detected with superfamily member PLN02469:

Pssm-ID: 178088 [Multi-domain]  Cd Length: 258  Bit Score: 237.35  E-value: 5.60e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406855413   1 MKVKVIPVLEDNYMYLIIEEHTREAVAIDVAVAERLLEIAGREGVSLTMVLSTHHHWDHTRGNAELAHILPGLAVLG-AD 79
Cdd:PLN02469   1 MKIIPVPCLEDNYAYLIIDESTKDAAVVDPVDPEKVLQAAHEHGAKIKLVLTTHHHWDHAGGNEKIKKLVPGIKVYGgSL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406855413  80 ERICALTRRLEHGEGLQFGA-IHVRCLLTPGHTSGHMSYFLWEDDCPDsPALFSGDALSVAGCGWHLEDTAQQMYQSLAK 158
Cdd:PLN02469  81 DNVKGCTHPVENGDKLSLGKdVNILALHTPCHTKGHISYYVTGKEGED-PAVFTGDTLFIAGCGKFFEGTAEQMYQSLCV 159

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 406855413 159 TLGTLPPETKVFCGHEHTLSNLEFAQKVEPCNEHVQAKLSWAQ 201
Cdd:PLN02469 160 TLGSLPKPTQVYCGHEYTVKNLKFALTVEPDNEKLKQKLEWAE 202
 
Name Accession Description Interval E-value
PLN02469 PLN02469
hydroxyacylglutathione hydrolase
 1-201 5.60e-79

hydroxyacylglutathione hydrolase


Pssm-ID: 178088 [Multi-domain]  Cd Length: 258  Bit Score: 237.35  E-value: 5.60e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406855413   1 MKVKVIPVLEDNYMYLIIEEHTREAVAIDVAVAERLLEIAGREGVSLTMVLSTHHHWDHTRGNAELAHILPGLAVLG-AD 79
Cdd:PLN02469   1 MKIIPVPCLEDNYAYLIIDESTKDAAVVDPVDPEKVLQAAHEHGAKIKLVLTTHHHWDHAGGNEKIKKLVPGIKVYGgSL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406855413  80 ERICALTRRLEHGEGLQFGA-IHVRCLLTPGHTSGHMSYFLWEDDCPDsPALFSGDALSVAGCGWHLEDTAQQMYQSLAK 158
Cdd:PLN02469  81 DNVKGCTHPVENGDKLSLGKdVNILALHTPCHTKGHISYYVTGKEGED-PAVFTGDTLFIAGCGKFFEGTAEQMYQSLCV 159

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 406855413 159 TLGTLPPETKVFCGHEHTLSNLEFAQKVEPCNEHVQAKLSWAQ 201
Cdd:PLN02469 160 TLGSLPKPTQVYCGHEYTVKNLKFALTVEPDNEKLKQKLEWAE 202
hydroxyacylglutathione_hydrolase_MBL-fold cd07723
hydroxyacylglutathione hydrolase, MBL-fold metallo-hydrolase domain; hydroxyacylglutathione ...
 4-173 1.88e-74

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: 222.34  E-value: 1.88e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406855413   4 KVIPVLEDNYMYLIIEEHTREAVAIDVAVAERLLEIAGREGVSLTMVLSTHHHWDHTRGNAELAHILPGLAVLG-ADERI 82
Cdd:cd07723    1 VPIPALSDNYIYLIVDEATGEAAVVDPGEAEPVLAALEKNGLTLTAILTTHHHWDHTGGNAELKALFPDAPVYGpAEDRI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406855413  83 CALTRRLEHGEGLQFGAIHVRCLLTPGHTSGHMSYFLweddcPDSPALFSGDALSVAGCGWHLEDTAQQMYQSLAKtLGT 162
Cdd:cd07723   81 PGLDHPVKDGDEIKLGGLEVKVLHTPGHTLGHICYYV-----PDEPALFTGDTLFSGGCGRFFEGTAEQMYASLQK-LLA 154

                        170
                 ....*....|.
gi 406855413 163 LPPETKVFCGH 173
Cdd:cd07723  155 LPDDTLVYCGH 165
GSH_gloB TIGR03413
hydroxyacylglutathione hydrolase; Members of this protein family are hydroxyacylglutathione ...
 6-201 3.97e-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: 3.97e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406855413    6 IPVLEDNYMYLIIEEHTReAVAIDVAVAERLLEIAGREGVSLTMVLSTHHHWDHTRGNAELAHILPgLAVLG-ADERICA 84
Cdd:TIGR03413   4 IPALSDNYIWLLHDPDGQ-AAVVDPGEAEPVLDALEARGLTLTAILLTHHHHDHVGGVAELLEAFP-APVYGpAEERIPG 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406855413   85 LTRRLEHGEGLQFGAIHVRCLLTPGHTSGHMSYFLweddcPDSPALFSGDALSVAGCGWHLEDTAQQMYQSLAKtLGTLP 164
Cdd:TIGR03413  82 ITHPVKDGDTVTLGGLEFEVLAVPGHTLGHIAYYL-----PDSPALFCGDTLFSAGCGRLFEGTPEQMYDSLQR-LAALP 155

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 406855413  165 PETKVFCGHEHTLSNLEFAQKVEPCNEHVQAKLSWAQ 201
Cdd:TIGR03413 156 DDTLVYCAHEYTLSNLRFALTVEPDNPALQERLKEVE 192
GloB COG0491
Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General ...
 11-178 3.07e-31

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: 114.02  E-value: 3.07e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406855413  11 DNYMYLIieEHTREAVAID----VAVAERLLEIAGREGVSLTMVLSTHHHWDHTRGNAELA---------------HILP 71
Cdd:COG0491   14 GVNSYLI--VGGDGAVLIDtglgPADAEALLAALAALGLDIKAVLLTHLHPDHVGGLAALAeafgapvyahaaeaeALEA 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406855413  72 GLAVLGADERICALTRRLEHGEGLQFGAIHVRCLLTPGHTSGHMSYFLweddcPDSPALFSGDALSVAGCGW--HLEDTA 149
Cdd:COG0491   92 PAAGALFGREPVPPDRTLEDGDTLELGGPGLEVIHTPGHTPGHVSFYV-----PDEKVLFTGDALFSGGVGRpdLPDGDL 166

                        170       180
                 ....*....|....*....|....*....
gi 406855413 150 QQMYQSLAKtLGTLPPETkVFCGHEHTLS 178
Cdd:COG0491  167 AQWLASLER-LLALPPDL-VIPGHGPPTT 193
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 13-173 3.34e-22

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: 89.15  E-value: 3.34e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406855413    13 YMYLIieEHTREAVAID--VAVAERLLEIAGREGVS-LTMVLSTHHHWDHTRGNAELAHI------------------LP 71
Cdd:smart00849   1 NSYLV--RDDGGAILIDtgPGEAEDLLAELKKLGPKkIDAIILTHGHPDHIGGLPELLEApgapvyapegtaellkdlLA 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406855413    72 GLAVLGADERICALTRRLEHGEGLQFGAIHVRCLLTPGHTSGHMSYFLweddcPDSPALFSGDALSVAGCG-WHLEDTAQ 150
Cdd:smart00849  79 LLGELGAEAEPAPPDRTLKDGDELDLGGGELEVIHTPGHTPGSIVLYL-----PEGKILFTGDLLFAGGDGrTLVDGGDA 153

                          170       180
                   ....*....|....*....|....
gi 406855413   151 QMYQSLAKTLGTL-PPETKVFCGH 173
Cdd:smart00849 154 AASDALESLLKLLkLLPKLVVPGH 177
HAGH_C pfam16123
Hydroxyacylglutathione hydrolase C-terminus; This domain is found at the C-terminus of ...
 174-201 1.73e-08

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: 50.13  E-value: 1.73e-08
                          10        20
                  ....*....|....*....|....*...
gi 406855413  174 EHTLSNLEFAQKVEPCNEHVQAKLSWAQ 201
Cdd:pfam16123   1 EYTLSNLKFALSVEPDNEALQKRLAWVE 28
 
Name Accession Description Interval E-value
PLN02469 PLN02469
hydroxyacylglutathione hydrolase
 1-201 5.60e-79

hydroxyacylglutathione hydrolase


Pssm-ID: 178088 [Multi-domain]  Cd Length: 258  Bit Score: 237.35  E-value: 5.60e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406855413   1 MKVKVIPVLEDNYMYLIIEEHTREAVAIDVAVAERLLEIAGREGVSLTMVLSTHHHWDHTRGNAELAHILPGLAVLG-AD 79
Cdd:PLN02469   1 MKIIPVPCLEDNYAYLIIDESTKDAAVVDPVDPEKVLQAAHEHGAKIKLVLTTHHHWDHAGGNEKIKKLVPGIKVYGgSL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406855413  80 ERICALTRRLEHGEGLQFGA-IHVRCLLTPGHTSGHMSYFLWEDDCPDsPALFSGDALSVAGCGWHLEDTAQQMYQSLAK 158
Cdd:PLN02469  81 DNVKGCTHPVENGDKLSLGKdVNILALHTPCHTKGHISYYVTGKEGED-PAVFTGDTLFIAGCGKFFEGTAEQMYQSLCV 159

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 406855413 159 TLGTLPPETKVFCGHEHTLSNLEFAQKVEPCNEHVQAKLSWAQ 201
Cdd:PLN02469 160 TLGSLPKPTQVYCGHEYTVKNLKFALTVEPDNEKLKQKLEWAE 202
hydroxyacylglutathione_hydrolase_MBL-fold cd07723
hydroxyacylglutathione hydrolase, MBL-fold metallo-hydrolase domain; hydroxyacylglutathione ...
 4-173 1.88e-74

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: 222.34  E-value: 1.88e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406855413   4 KVIPVLEDNYMYLIIEEHTREAVAIDVAVAERLLEIAGREGVSLTMVLSTHHHWDHTRGNAELAHILPGLAVLG-ADERI 82
Cdd:cd07723    1 VPIPALSDNYIYLIVDEATGEAAVVDPGEAEPVLAALEKNGLTLTAILTTHHHWDHTGGNAELKALFPDAPVYGpAEDRI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406855413  83 CALTRRLEHGEGLQFGAIHVRCLLTPGHTSGHMSYFLweddcPDSPALFSGDALSVAGCGWHLEDTAQQMYQSLAKtLGT 162
Cdd:cd07723   81 PGLDHPVKDGDEIKLGGLEVKVLHTPGHTLGHICYYV-----PDEPALFTGDTLFSGGCGRFFEGTAEQMYASLQK-LLA 154

                        170
                 ....*....|.
gi 406855413 163 LPPETKVFCGH 173
Cdd:cd07723  155 LPDDTLVYCGH 165
GSH_gloB TIGR03413
hydroxyacylglutathione hydrolase; Members of this protein family are hydroxyacylglutathione ...
 6-201 3.97e-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: 3.97e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406855413    6 IPVLEDNYMYLIIEEHTReAVAIDVAVAERLLEIAGREGVSLTMVLSTHHHWDHTRGNAELAHILPgLAVLG-ADERICA 84
Cdd:TIGR03413   4 IPALSDNYIWLLHDPDGQ-AAVVDPGEAEPVLDALEARGLTLTAILLTHHHHDHVGGVAELLEAFP-APVYGpAEERIPG 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406855413   85 LTRRLEHGEGLQFGAIHVRCLLTPGHTSGHMSYFLweddcPDSPALFSGDALSVAGCGWHLEDTAQQMYQSLAKtLGTLP 164
Cdd:TIGR03413  82 ITHPVKDGDTVTLGGLEFEVLAVPGHTLGHIAYYL-----PDSPALFCGDTLFSAGCGRLFEGTPEQMYDSLQR-LAALP 155

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 406855413  165 PETKVFCGHEHTLSNLEFAQKVEPCNEHVQAKLSWAQ 201
Cdd:TIGR03413 156 DDTLVYCAHEYTLSNLRFALTVEPDNPALQERLKEVE 192
PLN02398 PLN02398
hydroxyacylglutathione hydrolase
 1-195 9.08e-48

hydroxyacylglutathione hydrolase


Pssm-ID: 215223 [Multi-domain]  Cd Length: 329  Bit Score: 160.01  E-value: 9.08e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406855413   1 MKVKVIPVLEDNYMYLIIEEHTREAVAIDVAVAERLLEIAGREGVSLTMVLSTHHHWDHTRGNAELAHILpGLAVLGAD- 79
Cdd:PLN02398  76 LQIELVPCLKDNYAYLLHDEDTGTVGVVDPSEAVPVIDALSRKNRNLTYILNTHHHYDHTGGNLELKARY-GAKVIGSAv 154

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406855413  80 --ERICALTRRLEHGEGLQFGAIHVRCLLTPGHTSGHMSYFLweddcPDSPALFSGDALSVAGCGWHLEDTAQQMYQSLA 157
Cdd:PLN02398 155 dkDRIPGIDIVLKDGDKWMFAGHEVLVMETPGHTRGHISFYF-----PGSGAIFTGDTLFSLSCGKLFEGTPEQMLSSLQ 229

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 406855413 158 KTLgTLPPETKVFCGHEHTLSNLEFAQKVEPCNEHVQA 195
Cdd:PLN02398 230 KII-SLPDDTNIYCGHEYTLSNSKFALSIEPNNEVLQS 266
BaeB-like_MBL-fold cd16275
Bacillus amyloliquefaciens BaeB and related proteins; MBL-fold metallo hydrolase domain; ...
 11-173 4.69e-37

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: 127.65  E-value: 4.69e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406855413  11 DNYMYLIIEEHTREAVAIDVA-VAERLLEIAGREGVSLTMVLSTHHHWDHTRGNAELAHILPGLAVLGADERI-----CA 84
Cdd:cd16275   11 INYSYIIIDKATREAAVVDPAwDIEKILAKLNELGLTLTGILLTHSHFDHVNLVEPLLAKYDAPVYMSKEEIDyygfrCP 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406855413  85 LTRRLEHGEGLQFGAIHVRCLLTPGHTSGHMSYFLweDDCpdspaLFSGDALSVAGCGwhLEDT----AQQMYQSLAKTL 160
Cdd:cd16275   91 NLIPLEDGDTIKIGDTEITCLLTPGHTPGSMCYLL--GDS-----LFTGDTLFIEGCG--RCDLpggdPEEMYESLQRLK 161

                        170
                 ....*....|...
gi 406855413 161 GTLPPETKVFCGH 173
Cdd:cd16275  162 KLPPPNTRVYPGH 174
PRK10241 PRK10241
hydroxyacylglutathione hydrolase; Provisional
 1-188 1.25e-35

hydroxyacylglutathione hydrolase; Provisional


Pssm-ID: 182327 [Multi-domain]  Cd Length: 251  Bit Score: 126.09  E-value: 1.25e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406855413   1 MKVKVIPVLEDNYMYLIIEEHTReAVAIDVAVAERLLEIAGREGVSLTMVLSTHHHWDHTRGNAELAHILPGLAVLGADE 80
Cdd:PRK10241   1 MNLNSIPAFDDNYIWVLNDEAGR-CLIVDPGEAEPVLNAIAENNWQPEAIFLTHHHHDHVGGVKELVEKFPQIVVYGPQE 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406855413  81 -RICALTRRLEHGEGLQFGAIHVRCLLTPGHTSGHMSYFlweddcpDSPALFSGDALSVAGCGWHLEDTAQQMYQSLAKt 159
Cdd:PRK10241  80 tQDKGTTQVVKDGETAFVLGHEFSVFATPGHTLGHICYF-------SKPYLFCGDTLFSGGCGRLFEGTASQMYQSLKK- 151

                        170       180
                 ....*....|....*....|....*....
gi 406855413 160 LGTLPPETKVFCGHEHTLSNLEFAQKVEP 188
Cdd:PRK10241 152 INALPDDTLICCAHEYTLSNMKFALSILP 180
POD-like_MBL-fold cd07724
ETHE1 (PDO type I), persulfide dioxygenase A (PDOA, PDO type II) and related proteins; ...
 15-173 1.12e-34

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: 121.35  E-value: 1.12e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406855413  15 YLIIEEHTREAVAID--VAVAERLLEIAGREGVSLTMVLSTHHHWDHTRGNAELAHILPGLAVLGADERICALTRRLEHG 92
Cdd:cd07724   15 YLVGDPETGEAAVIDpvRDSVDRYLDLAAELGLKITYVLETHVHADHVSGARELAERTGAPIVIGEGAPASFFDRLLKDG 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406855413  93 EGLQFGAIHVRCLLTPGHTSGHMSYfLWEDdcPDspALFSGDALSVAGCG-----WHLEDTAQQMYQSLAKTLGTLPPET 167
Cdd:cd07724   95 DVLELGNLTLEVLHTPGHTPESVSY-LVGD--PD--AVFTGDTLFVGDVGrpdlpGEAEGLARQLYDSLQRKLLLLPDET 169


                 ....*.
gi 406855413 168 KVFCGH 173
Cdd:cd07724  170 LVYPGH 175
GloB COG0491
Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General ...
 11-178 3.07e-31

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: 114.02  E-value: 3.07e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406855413  11 DNYMYLIieEHTREAVAID----VAVAERLLEIAGREGVSLTMVLSTHHHWDHTRGNAELA---------------HILP 71
Cdd:COG0491   14 GVNSYLI--VGGDGAVLIDtglgPADAEALLAALAALGLDIKAVLLTHLHPDHVGGLAALAeafgapvyahaaeaeALEA 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406855413  72 GLAVLGADERICALTRRLEHGEGLQFGAIHVRCLLTPGHTSGHMSYFLweddcPDSPALFSGDALSVAGCGW--HLEDTA 149
Cdd:COG0491   92 PAAGALFGREPVPPDRTLEDGDTLELGGPGLEVIHTPGHTPGHVSFYV-----PDEKVLFTGDALFSGGVGRpdLPDGDL 166

                        170       180
                 ....*....|....*....|....*....
gi 406855413 150 QQMYQSLAKtLGTLPPETkVFCGHEHTLS 178
Cdd:COG0491  167 AQWLASLER-LLALPPDL-VIPGHGPPTT 193
metallo-hydrolase-like_MBL-fold cd06262
mainly hydrolytic enzymes and related proteins which carry out various biological functions; ...
 15-173 9.36e-30

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: 109.30  E-value: 9.36e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406855413  15 YLIIEEhTREAVAIDVA--VAERLLEIAGREGVSLTMVLSTHHHWDHTRGNAEL---------AH----------ILPGL 73
Cdd:cd06262   13 YLVSDE-EGEAILIDPGagALEKILEAIEELGLKIKAILLTHGHFDHIGGLAELkeapgapvyIHeadaelledpELNLA 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406855413  74 AVLGADERICALTRRLEHGEGLQFGAIHVRCLLTPGHTSGHMSYFlweddCPDSPALFSGDALSVAGCG-WHLEDT-AQQ 151
Cdd:cd06262   92 FFGGGPLPPPEPDILLEDGDTIELGGLELEVIHTPGHTPGSVCFY-----IEEEGVLFTGDTLFAGSIGrTDLPGGdPEQ 166

                        170       180
                 ....*....|....*....|..
gi 406855413 152 MYQSLAKTLGTLPPETKVFCGH 173
Cdd:cd06262  167 LIESIKKLLLLLPDDTVVYPGH 188
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 13-173 3.34e-22

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: 89.15  E-value: 3.34e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406855413    13 YMYLIieEHTREAVAID--VAVAERLLEIAGREGVS-LTMVLSTHHHWDHTRGNAELAHI------------------LP 71
Cdd:smart00849   1 NSYLV--RDDGGAILIDtgPGEAEDLLAELKKLGPKkIDAIILTHGHPDHIGGLPELLEApgapvyapegtaellkdlLA 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406855413    72 GLAVLGADERICALTRRLEHGEGLQFGAIHVRCLLTPGHTSGHMSYFLweddcPDSPALFSGDALSVAGCG-WHLEDTAQ 150
Cdd:smart00849  79 LLGELGAEAEPAPPDRTLKDGDELDLGGGELEVIHTPGHTPGSIVLYL-----PEGKILFTGDLLFAGGDGrTLVDGGDA 153

                          170       180
                   ....*....|....*....|....
gi 406855413   151 QMYQSLAKTLGTL-PPETKVFCGH 173
Cdd:smart00849 154 AASDALESLLKLLkLLPKLVVPGH 177
TTHA1623-like_MBL-fold cd16322
uncharacterized Thermus thermophilus TTHA1623 and related proteins; MBL-fold metallo hydrolase ...
 5-173 6.82e-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: 88.95  E-value: 6.82e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406855413   5 VIPVLEDNyMYLIIEEHTREAVAIDVAV-AERLLEIAGREGVSLTMVLSTHHHWDHTRGNAELAHILPGLAVLGAD---- 79
Cdd:cd16322    5 TLGPLQEN-TYLVADEGGGEAVLVDPGDeSEKLLARFGTTGLTLLYILLTHAHFDHVGGVADLRRHPGAPVYLHPDdlpl 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406855413  80 ---------------ERICALTRRLEHGEGLQFGAIHVRCLLTPGHTSGHMSYFlweddCPDSPALFSGDAL---SVAGC 141
Cdd:cd16322   84 yeaadlgakafglgiEPLPPPDRLLEDGQTLTLGGLEFKVLHTPGHSPGHVCFY-----VEEEGLLFSGDLLfqgSIGRT 158

                        170       180       190
                 ....*....|....*....|....*....|..
gi 406855413 142 GWHLEDtAQQMYQSLAKTLgTLPPETKVFCGH 173
Cdd:cd16322  159 DLPGGD-PKAMAASLRRLL-TLPDETRVFPGH 188
YcbL-like_MBL-fold cd07737
Salmonella enterica serovar typhimurium YcbL and related proteins; MBL-fold metallo hydrolase ...
 3-173 2.17e-18

Salmonella enterica serovar typhimurium YcbL and related proteins; MBL-fold metallo hydrolase domain; This subgroup includes Salmonella enterica serovar typhimurium YcbL which has type II hydroxyacylglutathione hydrolase (EC 3.1.2.6, also known as glyoxalase II) activity, and has a single metal ion binding site, and Thermus thermophilus TTHA1623 which does not have GLX2 activity and has two metal ion binding sites with a glyoxalase II-type metal coordination. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions.


Pssm-ID: 293823 [Multi-domain]  Cd Length: 190  Bit Score: 79.52  E-value: 2.17e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406855413   3 VKVIPV--LEDNyMYLIIEEHTREAVAIDV-AVAERLLEIAGREGVSLTMVLSTHHHWDHTRGNAELA----------HI 69
Cdd:cd07737    1 YQIIPVtpFQQN-CSLIWCEETKEAAVIDPgGDADKILQAIEDLGLTLKKILLTHGHLDHVGGAAELAehygvpiigpHK 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406855413  70 --------LPGLAVL--GADERICALTRRLEHGEGLQFGAIHVRCLLTPGHTSGHMSYFlweddCPDSPALFSGDAL--- 136
Cdd:cd07737   80 edkfllenLPEQSQMfgFPPAEAFTPDRWLEEGDTVTVGNLTLEVLHCPGHTPGHVVFF-----NRESKLAIVGDVLfkg 154

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 406855413 137 SVAGCGWHLEDTaQQMYQSLAKTLGTLPPETKVFCGH 173
Cdd:cd07737  155 SIGRTDFPGGNH-AQLIASIKEKLLPLGDDVTFIPGH 190
PLN02962 PLN02962
hydroxyacylglutathione hydrolase
 13-181 5.06e-18

hydroxyacylglutathione hydrolase


Pssm-ID: 178547 [Multi-domain]  Cd Length: 251  Bit Score: 79.84  E-value: 5.06e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406855413  13 YMYLI--IEEHTREAVAIDVA--VAERLLEIAGREGVSLTMVLSTHHHWDHTRGNAELAHILPGLAVLGADERICALTRR 88
Cdd:PLN02962  24 YTYLLadVSHPDKPALLIDPVdkTVDRDLSLVKELGLKLIYAMNTHVHADHVTGTGLLKTKLPGVKSIISKASGSKADLF 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406855413  89 LEHGEGLQFGAIHVRCLLTPGHTSGHMSYFLWE-DDCPDSPALFSGDALSVAGCGW--HLEDTAQQMYQSLAKTLGTLPP 165
Cdd:PLN02962 104 VEPGDKIYFGDLYLEVRATPGHTAGCVTYVTGEgPDQPQPRMAFTGDALLIRGCGRtdFQGGSSDQLYKSVHSQIFTLPK 183

                        170
                 ....*....|....*....
gi 406855413 166 ETKVFCGHE---HTLSNLE 181
Cdd:PLN02962 184 DTLIYPAHDykgFTVSTVG 202
metallo-hydrolase-like_MBL-fold cd16278
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 34-134 4.73e-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: 72.91  E-value: 4.73e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406855413  34 ERLLEIAGREGVSLTMVlsTHHHWDHTRGNAELAHiLPGLAVLGADERI-------CALTRRLEHGEGLQFGAIHVRCLL 106
Cdd:cd16278   43 DALLAALGGGRVSAILV--THTHRDHSPGAARLAE-RTGAPVRAFGPHRaggqdtdFAPDRPLADGEVIEGGGLRLTVLH 119

                         90       100
                 ....*....|....*....|....*...
gi 406855413 107 TPGHTSGHMSYFLweddcPDSPALFSGD 134
Cdd:cd16278  120 TPGHTSDHLCFAL-----EDEGALFTGD 142
yflN-like_MBL-fold cd07721
uncharacterized subgroup which includes Bacillus subtilis yflN; MBL-fold metallo hydrolase ...
 2-173 4.55e-14

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: 68.02  E-value: 4.55e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406855413   2 KVKVIPVLEDNYMYLIIEEhtREAVAIDVAV---AERLLEIAGREGVS---LTMVLSTHHHWDHTrGNAELAHILPGLAV 75
Cdd:cd07721    1 GVYQLPLLPPVNAYLIEDD--DGLTLIDTGLpgsAKRILKALRELGLSpkdIRRILLTHGHIDHI-GSLAALKEAPGAPV 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406855413  76 L-GADE----------------------------RICALTRRLEHGEGLQF-GAIHVrcLLTPGHTSGHMSYFLWEDDcp 125
Cdd:cd07721   78 YaHEREapylegekpypppvrlgllgllspllpvKPVPVDRTLEDGDTLDLaGGLRV--IHTPGHTPGHISLYLEEDG-- 153

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 406855413 126 dspALFSGDAL-----SVAGCGWHLEDTAQQMYQSLAKtLGTLPPETkVFCGH 173
Cdd:cd07721  154 ---VLIAGDALvtvggELVPPPPPFTWDMEEALESLRK-LAELDPEV-LAPGH 201
TTHA1429-like_MBL-fold cd07725
uncharacterized Thermus thermophilus TTHA1429 and related proteins; MBL-fold metallo hydrolase ...
 29-173 2.51e-11

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: 60.39  E-value: 2.51e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406855413  29 DVAVAERLLEIAGREGVSLTMVLSTHHHWDHTRGNAELAHilpglaVLGADErICALTRRLEHGEGLQFGAIHVRCLLTP 108
Cdd:cd07725   38 DAEALWEGLKELGLKPSDIDRVLLTHHHPDHIGLAGKLQE------KSGATV-YILDVTPVKDGDKIDLGGLRLKVIETP 110

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 406855413 109 GHTSGHMSYFlweddCPDSPALFSGDAL---SVAGCGWH---LEDTAQQMYQSLAKtLGTLPPEtKVFCGH 173
Cdd:cd07725  111 GHTPGHIVLY-----DEDRRELFVGDAVlpkITPNVSLWavrVEDPLGAYLESLDK-LEKLDVD-LAYPGH 174
MBLAC2-like_MBL-fold cd07712
uncharacterized human metallo-beta-lactamase domain-containing protein 2 and related proteins; ...
 7-173 3.91e-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: 3.91e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406855413   7 PVLEDNY---MYLIieEHTREAVAIDVAVAER-LLEIAgregVSLT----MVLSTHHHWDHTRGN----------AELAH 68
Cdd:cd07712    1 LFIEEDDrvnIYLL--RGRDRALLIDTGLGIGdLKEYV----RTLTdlplLVVATHGHFDHIGGLhefeevyvhpADAEI 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406855413  69 I-----LPGLAVLGADERICA--LTRRLEHGEGLQFGAIHVRCLLTPGHTSGHMSyfLWEddcPDSPALFSGDALSVAGC 141
Cdd:cd07712   75 LaapdnFETLTWDAATYSVPPagPTLPLRDGDVIDLGDRQLEVIHTPGHTPGSIA--LLD---RANRLLFSGDVVYDGPL 149

                        170       180       190
                 ....*....|....*....|....*....|....
gi 406855413 142 GWHLEDT-AQQMYQSLAKtLGTLPPE-TKVFCGH 173
Cdd:cd07712  150 IMDLPHSdLDDYLASLEK-LSKLPDEfDKVLPGH 182
LACTB2-like_MBL-fold cd07722
uncharacterized subgroup which includes human lactamase beta 2 and related proteins; MBL-fold ...
 39-173 5.10e-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: 5.10e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406855413  39 IAGREGVSLTMVLSTHHHWDHTRGnaeLAHIL-----------------PGLAVLGADERICaltrRLEHGEGLQFGAIH 101
Cdd:cd07722   49 LDSEGNATISDILLTHWHHDHVGG---LPDVLdllrgpsprvykfprpeEDEDPDEDGGDIH----DLQDGQVFKVEGAT 121

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 406855413 102 VRCLLTPGHTSGHMSYFLWEDDcpdspALFSGDalSVAGCGWH-LEDTAQQMyQSLAKTLGTLPpeTKVFCGH 173
Cdd:cd07722  122 LRVIHTPGHTTDHVCFLLEEEN-----ALFTGD--CVLGHGTAvFEDLAAYM-ASLKKLLSLGP--GRIYPGH 184
ST1585-like_MBL-fold cd07726
uncharacterized subgroup which includes Sulfolobus tokodaii ST1585 protein; MBL-fold metallo ...
 15-167 6.43e-09

uncharacterized subgroup which includes Sulfolobus tokodaii ST1585 protein; MBL-fold metallo hydrolase domain; This subgroup includes the uncharacterized Sulfolobus tokodaii ST1585 protein. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions. The class B metal beta-lactamases (MBLs) from which this fold was named are only a small fraction of the activities which are included in this superfamily. Activities carried out by superfamily members include class B beta-lactamases, hydroxyacylglutathione hydrolases, AHL (acyl homoserine lactone) lactonases, persulfide dioxygenases, flavodiiron proteins, cleavage and polyadenylation specificity factors such as the Int9 and Int11 subunits of Integrator, Sdsa1-like and AtsA-like arylsulfatases, 5'-exonucleases human SNM1A and yeast Pso2p, ribonuclease J and ribonuclease Z, cyclic nucleotide phosphodiesterases, insecticide hydrolases, and proteins required for natural transformation competence. Classical members of the superfamily are di-, or less commonly mono-, zinc-ion-dependent hydrolases, however the diversity of biological roles is reflected in variations in the active site metallo-chemistry.


Pssm-ID: 293812 [Multi-domain]  Cd Length: 215  Bit Score: 54.04  E-value: 6.43e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406855413  15 YLIIEEhtREAVAIDVAVA------ERLLEIAGREGVSLTMVLSTHHHWDHTRGNAELAHILPG---------------- 72
Cdd:cd07726   19 YLLDGE--GRPALIDTGPSssvprlLAALEALGIAPEDVDYIILTHIHLDHAGGAGLLAEALPNakvyvhprgarhlidp 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406855413  73 -------LAVLGAD-------------ERICAltrrLEHGEGLQFGAIHVRCLLTPGHTSGHMSYFLweddcPDSPALFS 132
Cdd:cd07726   97 sklwasaRAVYGDEadrlggeilpvpeERVIV----LEDGETLDLGGRTLEVIDTPGHAPHHLSFLD-----EESDGLFT 167

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 406855413 133 GDALSVAGCGWHLEDTA---------QQMYQSLAKtLGTLPPET 167
Cdd:cd07726  168 GDAAGVRYPELDVVGPPstpppdfdpEAWLESLDR-LLSLKPER 210
HAGH_C pfam16123
Hydroxyacylglutathione hydrolase C-terminus; This domain is found at the C-terminus of ...
 174-201 1.73e-08

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: 50.13  E-value: 1.73e-08
                          10        20
                  ....*....|....*....|....*...
gi 406855413  174 EHTLSNLEFAQKVEPCNEHVQAKLSWAQ 201
Cdd:pfam16123   1 EYTLSNLKFALSVEPDNEALQKRLAWVE 28
Lactamase_B pfam00753
Metallo-beta-lactamase superfamily;
15-173 1.43e-07

Metallo-beta-lactamase superfamily;


Pssm-ID: 425851 [Multi-domain]  Cd Length: 196  Bit Score: 50.06  E-value: 1.43e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406855413   15 YLIieEHTREAVAIDV-----AVAERLLEIAGREGVSLTMVLSTHHHWDHTRGNAELAHILP--------GLAVLGADER 81
Cdd:pfam00753   9 YLI--EGGGGAVLIDTggsaeAALLLLLAALGLGPKDIDAVILTHGHFDHIGGLGELAEATDvpvivvaeEARELLDEEL 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406855413   82 ICALTRRLEHG------------EGLQFGAIHVRCLL---TPGHTSGHMSYFLweddcPDSPALFSGDALSVAGCGWH-- 144
Cdd:pfam00753  87 GLAASRLGLPGppvvplppdvvlEEGDGILGGGLGLLvthGPGHGPGHVVVYY-----GGGKVLFTGDLLFAGEIGRLdl 161

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 406855413  145 -------LEDTAQQMYQSLAKTLGTLPPEtKVFCGH 173
Cdd:pfam00753 162 plggllvLHPSSAESSLESLLKLAKLKAA-VIVPGH 196
AHL_lactonase_MBL-fold cd07729
quorum-quenching N-acyl-homoserine lactonase, MBL-fold metallo-hydrolase domain; Acyl ...
 18-174 1.05e-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: 47.98  E-value: 1.05e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406855413  18 IEEHTREAVAIDVAVAERLLEIagreGVS---LTMVLSTHHHWDHTrGNAEL---AHIL-----------PGLAVLGADE 80
Cdd:cd07729   61 LELAFPPGVTEEQTLEEQLARL----GLDpedIDYVILSHLHFDHA-GGLDLfpnATIIvqraeleyatgPDPLAAGYYE 135

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406855413  81 RICALTRRLEhgeGLQFGAIH--------VRCLLTPGHTSGHMSYFLwedDCPDSPALFSGDA---------LSVAGCGW 143
Cdd:cd07729  136 DVLALDDDLP---GGRVRLVDgdydlfpgVTLIPTPGHTPGHQSVLV---RLPEGTVLLAGDAaytyenleeGRPPGINY 209

                        170       180       190
                 ....*....|....*....|....*....|...
gi 406855413 144 HLEDTAQQMY--QSLAKTLGtlppeTKVFCGHE 174
Cdd:cd07729  210 DPEAALASLErlKALAEREG-----ARVIPGHD 237
metallo-hydrolase-like_MBL-fold cd16282
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 22-173 3.42e-06

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


Pssm-ID: 293840 [Multi-domain]  Cd Length: 209  Bit Score: 46.02  E-value: 3.42e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406855413  22 TREAVA-ID----VAVAERLLE-IAGREGVSLTMVLSTHHHWDHTRGNAEL--------AH-------------ILPGLA 74
Cdd:cd16282   22 GDDGVVvIDtgasPRLARALLAaIRKVTDKPVRYVVNTHYHGDHTLGNAAFadagapiiAHentreelaargeaYLELMR 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406855413  75 VLGADE----RICALTRRLEHGEGLQFGAIHVRCL-LTPGHTSGHMSYFLweddcPDSPALFSGDALSVAGCGWHLEDTA 149
Cdd:cd16282  102 RLGGDAmagtELVLPDRTFDDGLTLDLGGRTVELIhLGPAHTPGDLVVWL-----PEEGVLFAGDLVFNGRIPFLPDGSL 176

                        170       180
                 ....*....|....*....|....
gi 406855413 150 QQMYQSLAKtLGTLPPETkVFCGH 173
Cdd:cd16282  177 AGWIAALDR-LLALDATV-VVPGH 198
SMB-1-like_MBL-B3 cd16313
SMB-1, THIN-B and related metallo-beta-lactamases, subclass B3; MBL-fold metallo-hydrolase ...
 50-117 5.37e-06

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: 46.01  E-value: 5.37e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406855413  50 VLSTHHHWDHTRGNAELAHiLPGLAVLGADERICAL-----------------------TRRLEHGEGLQFGAIHVRCLL 106
Cdd:cd16313   64 ILSSHDHWDHAGGIAALQK-LTGAQVLASPATVAVLrsgsmgkddpqfggltpmppvasVRAVRDGEVVKLGPLAVTAHA 142

                         90
                 ....*....|.
gi 406855413 107 TPGHTSGHMSY 117
Cdd:cd16313  143 TPGHTTGGTSW 153
MBLAC1-like_MBL-fold cd07711
uncharacterized human metallo-beta-lactamase domain-containing protein 1 and related proteins; ...
 34-116 7.86e-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: 44.88  E-value: 7.86e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406855413  34 ERLLEIAGREGVSL---TMVLSTHHHWDHTrGNAEL---AHILPGLAVLGaderICALTRRLEHGEGLQFGAiHVRCLLT 107
Cdd:cd07711   45 DLLLKALAEHGLSPediDYVVLTHGHPDHI-GNLNLfpnATVIVGWDICG----DSYDDHSLEEGDGYEIDE-NVEVIPT 118


                 ....*....
gi 406855413 108 PGHTSGHMS 116
Cdd:cd07711  119 PGHTPEDVS 127
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 ...
 50-163 1.49e-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: 44.65  E-value: 1.49e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406855413  50 VLSTHHHWDHTRGNAELAHI--------LPGLAVL------------GADERICALT--RRLEHGEGLQFGAIHVRCLLT 107
Cdd:cd16290   64 ILNSHAHFDHAGGIAALQRDsgatvaasPAGAAALrsggvdpddpqaGAADPFPPVAkvRVVADGEVVKLGPLAVTAHAT 143

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 406855413 108 PGHTSGHMSYfLWE----DDCPDspaLFSGDALS-VAGCGWHLEDTAQQ-MYQSLAKTLGTL 163
Cdd:cd16290  144 PGHTPGGTSW-TWRscegGRCLD---IVYADSLTaVSADGFRFSDDAHPaRVAAFRRSIATV 201
metallo-hydrolase-like_MBL-fold cd16277
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 48-136 3.62e-04

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: 40.20  E-value: 3.62e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406855413  48 TMVLSTHHHWDH----TR-----------------GNAELAH------------------ILP----GLAVL-GADERIc 83
Cdd:cd16277   65 DYVLCTHLHVDHvgwnTRlvdgrwvptfpnarylfSRAEYDHwsspdaggppnrgvfedsVLPvieaGLADLvDDDHEI- 143

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 406855413  84 altrrlehGEGLQFgaihvrcLLTPGHTSGHMSYFLwedDCPDSPALFSGDAL 136
Cdd:cd16277  144 --------LDGIRL-------EPTPGHTPGHVSVEL---ESGGERALFTGDVM 178
GOB1-like_MBL-B3 cd16308
Elizabethkingia meningoseptica GOB-1 and related metallo-beta-lactamases, subclass B3; ...
 47-119 6.00e-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: 6.00e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 406855413  47 LTMVLSTHHHWDHTRGNAELAHiLPGlAVLGADERICAL-----------------------TRRLEHGEGLQFGAIHVR 103
Cdd:cd16308   61 IKILLTTQAHYDHVGAMAAIKQ-QTG-AKMMVDEKDAKVladggksdyemggygstfapvkaDKLLHDGDTIKLGGTKLT 138

                         90
                 ....*....|....*.
gi 406855413 104 CLLTPGHTSGHMSYFL 119
Cdd:cd16308  139 LLHHPGHTKGSCSFLF 154
 
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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