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Conserved domains on  [gi|323635439|ref|NP_001191148|]
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hydroxyacylglutathione hydrolase-like protein [Canis lupus familiaris]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PLN02469 super family cl31885
hydroxyacylglutathione hydrolase
 1-257 4.44e-92

hydroxyacylglutathione hydrolase


The actual alignment was detected with superfamily member PLN02469:

Pssm-ID: 178088 [Multi-domain]  Cd Length: 258  Bit Score: 273.18  E-value: 4.44e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323635439   1 MKVKVIPVLEDNYMYLVIEERTREAVAVDVAVPKRLLEIVGREGVSLTTVLTTHHHWDHARGNAELARLRPGLAVLG-AD 79
Cdd:PLN02469   1 MKIIPVPCLEDNYAYLIIDESTKDAAVVDPVDPEKVLQAAHEHGAKIKLVLTTHHHWDHAGGNEKIKKLVPGIKVYGgSL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323635439  80 ERICALTRRLVHGEELRFGA-IHARCLLTPGHTSGHMSYFLWEEECPDPpAVFSGDALSVAGCGLRLESTALQMYESLTQ 158
Cdd:PLN02469  81 DNVKGCTHPVENGDKLSLGKdVNILALHTPCHTKGHISYYVTGKEGEDP-AVFTGDTLFIAGCGKFFEGTAEQMYQSLCV 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323635439 159 ILGTLPPETKVFCGHEHTLGNLEFAQKVEPGNDHVRAKLSWAKKRDEDDMPTVPSTLSEELLYNPFLRVAEEPVRKFTGK 238
Cdd:PLN02469 160 TLGSLPKPTQVYCGHEYTVKNLKFALTVEPDNEKLKQKLEWAEKQRQAGLPTVPSTIEEELETNPFMRVDLPEIQEKVGC 239

                        250
                 ....*....|....*....
gi 323635439 239 AAPAEVLEALCKERASFQR 257
Cdd:PLN02469 240 ESPVEALREVRKMKDNWKG 258
 
Name Accession Description Interval E-value
PLN02469 PLN02469
hydroxyacylglutathione hydrolase
 1-257 4.44e-92

hydroxyacylglutathione hydrolase


Pssm-ID: 178088 [Multi-domain]  Cd Length: 258  Bit Score: 273.18  E-value: 4.44e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323635439   1 MKVKVIPVLEDNYMYLVIEERTREAVAVDVAVPKRLLEIVGREGVSLTTVLTTHHHWDHARGNAELARLRPGLAVLG-AD 79
Cdd:PLN02469   1 MKIIPVPCLEDNYAYLIIDESTKDAAVVDPVDPEKVLQAAHEHGAKIKLVLTTHHHWDHAGGNEKIKKLVPGIKVYGgSL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323635439  80 ERICALTRRLVHGEELRFGA-IHARCLLTPGHTSGHMSYFLWEEECPDPpAVFSGDALSVAGCGLRLESTALQMYESLTQ 158
Cdd:PLN02469  81 DNVKGCTHPVENGDKLSLGKdVNILALHTPCHTKGHISYYVTGKEGEDP-AVFTGDTLFIAGCGKFFEGTAEQMYQSLCV 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323635439 159 ILGTLPPETKVFCGHEHTLGNLEFAQKVEPGNDHVRAKLSWAKKRDEDDMPTVPSTLSEELLYNPFLRVAEEPVRKFTGK 238
Cdd:PLN02469 160 TLGSLPKPTQVYCGHEYTVKNLKFALTVEPDNEKLKQKLEWAEKQRQAGLPTVPSTIEEELETNPFMRVDLPEIQEKVGC 239

                        250
                 ....*....|....*....
gi 323635439 239 AAPAEVLEALCKERASFQR 257
Cdd:PLN02469 240 ESPVEALREVRKMKDNWKG 258
GSH_gloB TIGR03413
hydroxyacylglutathione hydrolase; Members of this protein family are hydroxyacylglutathione ...
 6-248 7.14e-85

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: 254.38  E-value: 7.14e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323635439    6 IPVLEDNYMYLVIEERTReAVAVDVAVPKRLLEIVGREGVSLTTVLTTHHHWDHARGNAELARlRPGLAVLG-ADERICA 84
Cdd:TIGR03413   4 IPALSDNYIWLLHDPDGQ-AAVVDPGEAEPVLDALEARGLTLTAILLTHHHHDHVGGVAELLE-AFPAPVYGpAEERIPG 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323635439   85 LTRRLVHGEELRFGAIHARCLLTPGHTSGHMSYFLweeecPDPPAVFSGDALSVAGCGlRL-ESTALQMYESLtQILGTL 163
Cdd:TIGR03413  82 ITHPVKDGDTVTLGGLEFEVLAVPGHTLGHIAYYL-----PDSPALFCGDTLFSAGCG-RLfEGTPEQMYDSL-QRLAAL 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323635439  164 PPETKVFCGHEHTLGNLEFAQKVEPGNDHVRAKLSWAKKRDEDDMPTVPSTLSEELLYNPFLRVAEEPVRKFTGK--AAP 241
Cdd:TIGR03413 155 PDDTLVYCAHEYTLSNLRFALTVEPDNPALQERLKEVEALRAQGQPTLPSTLGLERATNPFLRADDPAVRAALGSqgADP 234


                  ....*..
gi 323635439  242 AEVLEAL 248
Cdd:TIGR03413 235 VEVFAAL 241
hydroxyacylglutathione_hydrolase_MBL-fold cd07723
hydroxyacylglutathione hydrolase, MBL-fold metallo-hydrolase domain; hydroxyacylglutathione ...
 4-173 1.84e-78

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: 235.05  E-value: 1.84e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323635439   4 KVIPVLEDNYMYLVIEERTREAVAVDVAVPKRLLEIVGREGVSLTTVLTTHHHWDHARGNAELARLRPGLAVLG-ADERI 82
Cdd:cd07723    1 VPIPALSDNYIYLIVDEATGEAAVVDPGEAEPVLAALEKNGLTLTAILTTHHHWDHTGGNAELKALFPDAPVYGpAEDRI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323635439  83 CALTRRLVHGEELRFGAIHARCLLTPGHTSGHMSYFLweeecPDPPAVFSGDALSVAGCGlRL-ESTALQMYESLTQILG 161
Cdd:cd07723   81 PGLDHPVKDGDEIKLGGLEVKVLHTPGHTLGHICYYV-----PDEPALFTGDTLFSGGCG-RFfEGTAEQMYASLQKLLA 154

                        170
                 ....*....|..
gi 323635439 162 tLPPETKVFCGH 173
Cdd:cd07723  155 -LPDDTLVYCGH 165
HAGH_C pfam16123
Hydroxyacylglutathione hydrolase C-terminus; This domain is found at the C-terminus of ...
 174-255 1.87e-31

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: 111.76  E-value: 1.87e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323635439  174 EHTLGNLEFAQKVEPGNDHVRAKLSWAKKRDEDDMPTVPSTLSEELLYNPFLRVAEEPVRKFTGKAAPAEVLEALCKERA 253
Cdd:pfam16123   1 EYTLSNLKFALSVEPDNEALQKRLAWVEALRAAGEPTVPSTLGDEKATNPFLRVDDPAVQKATGETDPVEVFAALRELKD 80


                  ..
gi 323635439  254 SF 255
Cdd:pfam16123  81 NF 82
GloB COG0491
Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General ...
 11-177 1.05e-29

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: 111.71  E-value: 1.05e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323635439  11 DNYMYLVieERTREAVAVD----VAVPKRLLEIVGREGVSLTTVLTTHHHWDHARGNAELAR---------------LRP 71
Cdd:COG0491   14 GVNSYLI--VGGDGAVLIDtglgPADAEALLAALAALGLDIKAVLLTHLHPDHVGGLAALAEafgapvyahaaeaeaLEA 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323635439  72 GLAVLGADERICALTRRLVHGEELRFGAIHARCLLTPGHTSGHMSYFLweeecPDPPAVFSGDALSVAGCGL--RLESTA 149
Cdd:COG0491   92 PAAGALFGREPVPPDRTLEDGDTLELGGPGLEVIHTPGHTPGHVSFYV-----PDEKVLFTGDALFSGGVGRpdLPDGDL 166

                        170       180
                 ....*....|....*....|....*...
gi 323635439 150 LQMYESLTQILgTLPPETkVFCGHEHTL 177
Cdd:COG0491  167 AQWLASLERLL-ALPPDL-VIPGHGPPT 192
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 13-173 1.34e-20

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: 86.45  E-value: 1.34e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323635439    13 YMYLVieERTREAVAVD--VAVPKRLLEIVGREGVS-LTTVLTTHHHWDHARGNAELARlRPGLAVLG------------ 77
Cdd:smart00849   1 NSYLV--RDDGGAILIDtgPGEAEDLLAELKKLGPKkIDAIILTHGHPDHIGGLPELLE-APGAPVYApegtaellkdll 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323635439    78 -------ADERICALTRRLVHGEELRFGAIHARCLLTPGHTSGHMSYFLweeecPDPPAVFSGDALSVAGCG-LRLESTA 149
Cdd:smart00849  78 allgelgAEAEPAPPDRTLKDGDELDLGGGELEVIHTPGHTPGSIVLYL-----PEGKILFTGDLLFAGGDGrTLVDGGD 152

                          170       180
                   ....*....|....*....|....*
gi 323635439   150 LQMYESLTQILGTL-PPETKVFCGH 173
Cdd:smart00849 153 AAASDALESLLKLLkLLPKLVVPGH 177
 
Name Accession Description Interval E-value
PLN02469 PLN02469
hydroxyacylglutathione hydrolase
 1-257 4.44e-92

hydroxyacylglutathione hydrolase


Pssm-ID: 178088 [Multi-domain]  Cd Length: 258  Bit Score: 273.18  E-value: 4.44e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323635439   1 MKVKVIPVLEDNYMYLVIEERTREAVAVDVAVPKRLLEIVGREGVSLTTVLTTHHHWDHARGNAELARLRPGLAVLG-AD 79
Cdd:PLN02469   1 MKIIPVPCLEDNYAYLIIDESTKDAAVVDPVDPEKVLQAAHEHGAKIKLVLTTHHHWDHAGGNEKIKKLVPGIKVYGgSL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323635439  80 ERICALTRRLVHGEELRFGA-IHARCLLTPGHTSGHMSYFLWEEECPDPpAVFSGDALSVAGCGLRLESTALQMYESLTQ 158
Cdd:PLN02469  81 DNVKGCTHPVENGDKLSLGKdVNILALHTPCHTKGHISYYVTGKEGEDP-AVFTGDTLFIAGCGKFFEGTAEQMYQSLCV 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323635439 159 ILGTLPPETKVFCGHEHTLGNLEFAQKVEPGNDHVRAKLSWAKKRDEDDMPTVPSTLSEELLYNPFLRVAEEPVRKFTGK 238
Cdd:PLN02469 160 TLGSLPKPTQVYCGHEYTVKNLKFALTVEPDNEKLKQKLEWAEKQRQAGLPTVPSTIEEELETNPFMRVDLPEIQEKVGC 239

                        250
                 ....*....|....*....
gi 323635439 239 AAPAEVLEALCKERASFQR 257
Cdd:PLN02469 240 ESPVEALREVRKMKDNWKG 258
GSH_gloB TIGR03413
hydroxyacylglutathione hydrolase; Members of this protein family are hydroxyacylglutathione ...
 6-248 7.14e-85

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: 254.38  E-value: 7.14e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323635439    6 IPVLEDNYMYLVIEERTReAVAVDVAVPKRLLEIVGREGVSLTTVLTTHHHWDHARGNAELARlRPGLAVLG-ADERICA 84
Cdd:TIGR03413   4 IPALSDNYIWLLHDPDGQ-AAVVDPGEAEPVLDALEARGLTLTAILLTHHHHDHVGGVAELLE-AFPAPVYGpAEERIPG 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323635439   85 LTRRLVHGEELRFGAIHARCLLTPGHTSGHMSYFLweeecPDPPAVFSGDALSVAGCGlRL-ESTALQMYESLtQILGTL 163
Cdd:TIGR03413  82 ITHPVKDGDTVTLGGLEFEVLAVPGHTLGHIAYYL-----PDSPALFCGDTLFSAGCG-RLfEGTPEQMYDSL-QRLAAL 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323635439  164 PPETKVFCGHEHTLGNLEFAQKVEPGNDHVRAKLSWAKKRDEDDMPTVPSTLSEELLYNPFLRVAEEPVRKFTGK--AAP 241
Cdd:TIGR03413 155 PDDTLVYCAHEYTLSNLRFALTVEPDNPALQERLKEVEALRAQGQPTLPSTLGLERATNPFLRADDPAVRAALGSqgADP 234


                  ....*..
gi 323635439  242 AEVLEAL 248
Cdd:TIGR03413 235 VEVFAAL 241
hydroxyacylglutathione_hydrolase_MBL-fold cd07723
hydroxyacylglutathione hydrolase, MBL-fold metallo-hydrolase domain; hydroxyacylglutathione ...
 4-173 1.84e-78

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: 235.05  E-value: 1.84e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323635439   4 KVIPVLEDNYMYLVIEERTREAVAVDVAVPKRLLEIVGREGVSLTTVLTTHHHWDHARGNAELARLRPGLAVLG-ADERI 82
Cdd:cd07723    1 VPIPALSDNYIYLIVDEATGEAAVVDPGEAEPVLAALEKNGLTLTAILTTHHHWDHTGGNAELKALFPDAPVYGpAEDRI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323635439  83 CALTRRLVHGEELRFGAIHARCLLTPGHTSGHMSYFLweeecPDPPAVFSGDALSVAGCGlRL-ESTALQMYESLTQILG 161
Cdd:cd07723   81 PGLDHPVKDGDEIKLGGLEVKVLHTPGHTLGHICYYV-----PDEPALFTGDTLFSGGCG-RFfEGTAEQMYASLQKLLA 154

                        170
                 ....*....|..
gi 323635439 162 tLPPETKVFCGH 173
Cdd:cd07723  155 -LPDDTLVYCGH 165
PLN02398 PLN02398
hydroxyacylglutathione hydrolase
 1-255 1.90e-53

hydroxyacylglutathione hydrolase


Pssm-ID: 215223 [Multi-domain]  Cd Length: 329  Bit Score: 176.57  E-value: 1.90e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323635439   1 MKVKVIPVLEDNYMYLVIEERTREAVAVDVAVPKRLLEIVGREGVSLTTVLTTHHHWDHARGNAELaRLRPGLAVLGAD- 79
Cdd:PLN02398  76 LQIELVPCLKDNYAYLLHDEDTGTVGVVDPSEAVPVIDALSRKNRNLTYILNTHHHYDHTGGNLEL-KARYGAKVIGSAv 154

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323635439  80 --ERICALTRRLVHGEELRFGAIHARCLLTPGHTSGHMSYFLweeecPDPPAVFSGDALSVAGCGLRLESTALQMYESLT 157
Cdd:PLN02398 155 dkDRIPGIDIVLKDGDKWMFAGHEVLVMETPGHTRGHISFYF-----PGSGAIFTGDTLFSLSCGKLFEGTPEQMLSSLQ 229

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323635439 158 QILgTLPPETKVFCGHEHTLGNLEFAQKVEPGNDHVRAKLSWAKKRDEDDMPTVPSTLSEELLYNPFLRVAEEPVRK--- 234
Cdd:PLN02398 230 KII-SLPDDTNIYCGHEYTLSNSKFALSIEPNNEVLQSYAAHVAHLRSKGLPTIPTTVKMEKACNPFLRTSSTDIRKsls 308

                        250       260
                 ....*....|....*....|.
gi 323635439 235 FTGKAAPAEVLEALCKERASF 255
Cdd:PLN02398 309 IPDTADEAEALGIIRRAKDNF 329
BaeB-like_MBL-fold cd16275
Bacillus amyloliquefaciens BaeB and related proteins; MBL-fold metallo hydrolase domain; ...
 11-173 8.21e-36

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: 126.11  E-value: 8.21e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323635439  11 DNYMYLVIEERTREAVAVDvavP----KRLLEIVGREGVSLTTVLTTHHHWDHARGNAELARlRPGLAV-LGADE----R 81
Cdd:cd16275   11 INYSYIIIDKATREAAVVD---PawdiEKILAKLNELGLTLTGILLTHSHFDHVNLVEPLLA-KYDAPVyMSKEEidyyG 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323635439  82 ICAltRRLV---HGEELRFGAIHARCLLTPGHTSGHMSYFLweEECpdppaVFSGDALSVAGCGL--RLESTALQMYESL 156
Cdd:cd16275   87 FRC--PNLIpleDGDTIKIGDTEITCLLTPGHTPGSMCYLL--GDS-----LFTGDTLFIEGCGRcdLPGGDPEEMYESL 157

                        170
                 ....*....|....*..
gi 323635439 157 TQILGTLPPETKVFCGH 173
Cdd:cd16275  158 QRLKKLPPPNTRVYPGH 174
PRK10241 PRK10241
hydroxyacylglutathione hydrolase; Provisional
 1-227 6.21e-35

hydroxyacylglutathione hydrolase; Provisional


Pssm-ID: 182327 [Multi-domain]  Cd Length: 251  Bit Score: 126.48  E-value: 6.21e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323635439   1 MKVKVIPVLEDNYMYLVIEERTReAVAVDVAVPKRLLEIVGREGVSLTTVLTTHHHWDHARGNAELARLRPGLAVLGADE 80
Cdd:PRK10241   1 MNLNSIPAFDDNYIWVLNDEAGR-CLIVDPGEAEPVLNAIAENNWQPEAIFLTHHHHDHVGGVKELVEKFPQIVVYGPQE 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323635439  81 RICALTRRLVH-GEELRFGAIHARCLLTPGHTSGHMSYFlweeecpDPPAVFSGDALSVAGCGLRLESTALQMYESLTQI 159
Cdd:PRK10241  80 TQDKGTTQVVKdGETAFVLGHEFSVFATPGHTLGHICYF-------SKPYLFCGDTLFSGGCGRLFEGTASQMYQSLKKI 152

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 323635439 160 lGTLPPETKVFCGHEHTLGNLEFAQKVEPgndHVRAKLSWAKKRDE---DDMPTVPSTLSEELLYNPFLRV 227
Cdd:PRK10241 153 -NALPDDTLICCAHEYTLSNMKFALSILP---HDLSINDYYRKVKElraKNQITLPVILKNERQINLFLRT 219
POD-like_MBL-fold cd07724
ETHE1 (PDO type I), persulfide dioxygenase A (PDOA, PDO type II) and related proteins; ...
 15-173 1.19e-33

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: 120.58  E-value: 1.19e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323635439  15 YLVIEERTREAVAVD--VAVPKRLLEIVGREGVSLTTVLTTHHHWDHARGNAELARlRPGLA-VLGADERICALTRRLVH 91
Cdd:cd07724   15 YLVGDPETGEAAVIDpvRDSVDRYLDLAAELGLKITYVLETHVHADHVSGARELAE-RTGAPiVIGEGAPASFFDRLLKD 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323635439  92 GEELRFGAIHARCLLTPGHTSGHMSYfLWEeecpDPPAVFSGDALSVAGCGlR------LESTALQMYESLTQILGTLPP 165
Cdd:cd07724   94 GDVLELGNLTLEVLHTPGHTPESVSY-LVG----DPDAVFTGDTLFVGDVG-RpdlpgeAEGLARQLYDSLQRKLLLLPD 167


                 ....*...
gi 323635439 166 ETKVFCGH 173
Cdd:cd07724  168 ETLVYPGH 175
HAGH_C pfam16123
Hydroxyacylglutathione hydrolase C-terminus; This domain is found at the C-terminus of ...
 174-255 1.87e-31

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: 111.76  E-value: 1.87e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323635439  174 EHTLGNLEFAQKVEPGNDHVRAKLSWAKKRDEDDMPTVPSTLSEELLYNPFLRVAEEPVRKFTGKAAPAEVLEALCKERA 253
Cdd:pfam16123   1 EYTLSNLKFALSVEPDNEALQKRLAWVEALRAAGEPTVPSTLGDEKATNPFLRVDDPAVQKATGETDPVEVFAALRELKD 80


                  ..
gi 323635439  254 SF 255
Cdd:pfam16123  81 NF 82
GloB COG0491
Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General ...
 11-177 1.05e-29

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: 111.71  E-value: 1.05e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323635439  11 DNYMYLVieERTREAVAVD----VAVPKRLLEIVGREGVSLTTVLTTHHHWDHARGNAELAR---------------LRP 71
Cdd:COG0491   14 GVNSYLI--VGGDGAVLIDtglgPADAEALLAALAALGLDIKAVLLTHLHPDHVGGLAALAEafgapvyahaaeaeaLEA 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323635439  72 GLAVLGADERICALTRRLVHGEELRFGAIHARCLLTPGHTSGHMSYFLweeecPDPPAVFSGDALSVAGCGL--RLESTA 149
Cdd:COG0491   92 PAAGALFGREPVPPDRTLEDGDTLELGGPGLEVIHTPGHTPGHVSFYV-----PDEKVLFTGDALFSGGVGRpdLPDGDL 166

                        170       180
                 ....*....|....*....|....*...
gi 323635439 150 LQMYESLTQILgTLPPETkVFCGHEHTL 177
Cdd:COG0491  167 AQWLASLERLL-ALPPDL-VIPGHGPPT 192
metallo-hydrolase-like_MBL-fold cd06262
mainly hydrolytic enzymes and related proteins which carry out various biological functions; ...
 15-173 1.55e-28

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: 107.76  E-value: 1.55e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323635439  15 YLVIEErTREAVAVDVA--VPKRLLEIVGREGVSLTTVLTTHHHWDHARGNAELARL-------------------RPGL 73
Cdd:cd06262   13 YLVSDE-EGEAILIDPGagALEKILEAIEELGLKIKAILLTHGHFDHIGGLAELKEApgapvyiheadaelledpeLNLA 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323635439  74 AVLGADERICALTRRLVHGEELRFGAIHARCLLTPGHTSGHMSYFlweeeCPDPPAVFSGDALSVAGCGLR--LESTALQ 151
Cdd:cd06262   92 FFGGGPLPPPEPDILLEDGDTIELGGLELEVIHTPGHTPGSVCFY-----IEEEGVLFTGDTLFAGSIGRTdlPGGDPEQ 166

                        170       180
                 ....*....|....*....|..
gi 323635439 152 MYESLTQILGTLPPETKVFCGH 173
Cdd:cd06262  167 LIESIKKLLLLLPDDTVVYPGH 188
TTHA1623-like_MBL-fold cd16322
uncharacterized Thermus thermophilus TTHA1623 and related proteins; MBL-fold metallo hydrolase ...
 5-225 3.46e-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: 91.26  E-value: 3.46e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323635439   5 VIPVLEDNyMYLVIEERTREAVAVDVAVPK-RLLEIVGREGVSLTTVLTTHHHWDHARGNAELARlRPGLAV-------- 75
Cdd:cd16322    5 TLGPLQEN-TYLVADEGGGEAVLVDPGDESeKLLARFGTTGLTLLYILLTHAHFDHVGGVADLRR-HPGAPVylhpddlp 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323635439  76 -------------LGADERIcALTRRLVHGEELRFGAIHARCLLTPGHTSGHMSYFlweeeCPDPPAVFSGDAL---SVA 139
Cdd:cd16322   83 lyeaadlgakafgLGIEPLP-PPDRLLEDGQTLTLGGLEFKVLHTPGHSPGHVCFY-----VEEEGLLFSGDLLfqgSIG 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323635439 140 GCGLRLESTAlQMYESLTQILgTLPPETKVFCGHehtlgnlefaqkvepgndhvraklswakkrdeddMPtvPSTLSEEL 219
Cdd:cd16322  157 RTDLPGGDPK-AMAASLRRLL-TLPDETRVFPGH----------------------------------GP--PTTLGEER 198


                 ....*.
gi 323635439 220 LYNPFL 225
Cdd:cd16322  199 RTNPFL 204
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 13-173 1.34e-20

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: 86.45  E-value: 1.34e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323635439    13 YMYLVieERTREAVAVD--VAVPKRLLEIVGREGVS-LTTVLTTHHHWDHARGNAELARlRPGLAVLG------------ 77
Cdd:smart00849   1 NSYLV--RDDGGAILIDtgPGEAEDLLAELKKLGPKkIDAIILTHGHPDHIGGLPELLE-APGAPVYApegtaellkdll 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323635439    78 -------ADERICALTRRLVHGEELRFGAIHARCLLTPGHTSGHMSYFLweeecPDPPAVFSGDALSVAGCG-LRLESTA 149
Cdd:smart00849  78 allgelgAEAEPAPPDRTLKDGDELDLGGGELEVIHTPGHTPGSIVLYL-----PEGKILFTGDLLFAGGDGrTLVDGGD 152

                          170       180
                   ....*....|....*....|....*
gi 323635439   150 LQMYESLTQILGTL-PPETKVFCGH 173
Cdd:smart00849 153 AAASDALESLLKLLkLLPKLVVPGH 177
YcbL-like_MBL-fold cd07737
Salmonella enterica serovar typhimurium YcbL and related proteins; MBL-fold metallo hydrolase ...
 3-173 4.62e-17

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: 77.21  E-value: 4.62e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323635439   3 VKVIPV--LEDNyMYLVIEERTREAVAVDV-AVPKRLLEIVGREGVSLTTVLTTHHHWDHARGNAELARLRpGLAVLG-- 77
Cdd:cd07737    1 YQIIPVtpFQQN-CSLIWCEETKEAAVIDPgGDADKILQAIEDLGLTLKKILLTHGHLDHVGGAAELAEHY-GVPIIGph 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323635439  78 -ADE------------------RICALTRRLVHGEELRFGAIHARCLLTPGHTSGHMSYFLWEEECpdppaVFSGDAL-- 136
Cdd:cd07737   79 kEDKfllenlpeqsqmfgfppaEAFTPDRWLEEGDTVTVGNLTLEVLHCPGHTPGHVVFFNRESKL-----AIVGDVLfk 153

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 323635439 137 -SVAGCGLRLESTAlQMYESLTQILGTLPPETKVFCGH 173
Cdd:cd07737  154 gSIGRTDFPGGNHA-QLIASIKEKLLPLGDDVTFIPGH 190
PLN02962 PLN02962
hydroxyacylglutathione hydrolase
 13-230 1.02e-16

hydroxyacylglutathione hydrolase


Pssm-ID: 178547 [Multi-domain]  Cd Length: 251  Bit Score: 77.53  E-value: 1.02e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323635439  13 YMYLV--IEERTREAVAVDvAVPK---RLLEIVGREGVSLTTVLTTHHHWDHARGNAELARLRPGLAVLGADERICALTR 87
Cdd:PLN02962  24 YTYLLadVSHPDKPALLID-PVDKtvdRDLSLVKELGLKLIYAMNTHVHADHVTGTGLLKTKLPGVKSIISKASGSKADL 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323635439  88 RLVHGEELRFGAIHARCLLTPGHTSGHMSYFLWE-EECPDPPAVFSGDALSVAGCGlRLE---STALQMYESL-TQILgT 162
Cdd:PLN02962 103 FVEPGDKIYFGDLYLEVRATPGHTAGCVTYVTGEgPDQPQPRMAFTGDALLIRGCG-RTDfqgGSSDQLYKSVhSQIF-T 180

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 323635439 163 LPPETKVFCGHEHTlGNlefaqkvepgndhvraklswakkrdeddmpTVpSTLSEELLYNPFLRVAEE 230
Cdd:PLN02962 181 LPKDTLIYPAHDYK-GF------------------------------TV-STVGEEMLYNPRLTKDEE 216
metallo-hydrolase-like_MBL-fold cd16278
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 35-134 5.81e-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: 74.06  E-value: 5.81e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323635439  35 RLLEIVGREGVSLttVLTTHHHWDHARGNAELARlRPGLAVLGADERI-------CALTRRLVHGEELRFGAIHARCLLT 107
Cdd:cd16278   44 ALLAALGGGRVSA--ILVTHTHRDHSPGAARLAE-RTGAPVRAFGPHRaggqdtdFAPDRPLADGEVIEGGGLRLTVLHT 120

                         90       100
                 ....*....|....*....|....*..
gi 323635439 108 PGHTSGHMSyFLWEEEcpdpPAVFSGD 134
Cdd:cd16278  121 PGHTSDHLC-FALEDE----GALFTGD 142
yflN-like_MBL-fold cd07721
uncharacterized subgroup which includes Bacillus subtilis yflN; MBL-fold metallo hydrolase ...
 2-173 2.48e-15

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: 72.64  E-value: 2.48e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323635439   2 KVKVIPVLEDNYMYLVIEERtrEAVAVDVAVP---KRLLEIVGREGVS---LTTVLTTHHHWDHArGNAELARLRPGLAV 75
Cdd:cd07721    1 GVYQLPLLPPVNAYLIEDDD--GLTLIDTGLPgsaKRILKALRELGLSpkdIRRILLTHGHIDHI-GSLAALKEAPGAPV 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323635439  76 L-GADE----------------------------RICALTRRLVHGEELRFG----AIHarcllTPGHTSGHMSYFLwee 122
Cdd:cd07721   78 YaHEREapylegekpypppvrlgllgllspllpvKPVPVDRTLEDGDTLDLAgglrVIH-----TPGHTPGHISLYL--- 149

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 323635439 123 ecPDPPAVFSGDALSVAGCGLRLESTAL-----QMYESLtQILGTLPPETkVFCGH 173
Cdd:cd07721  150 --EEDGVLIAGDALVTVGGELVPPPPPFtwdmeEALESL-RKLAELDPEV-LAPGH 201
TTHA1429-like_MBL-fold cd07725
uncharacterized Thermus thermophilus TTHA1429 and related proteins; MBL-fold metallo hydrolase ...
 34-136 6.74e-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: 60.00  E-value: 6.74e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323635439  34 KRLLEIVGREGVSLTTVLTTHHHWDHARGNAELArlrpglAVLGADErICALTRRLVHGEELRFGAIHARCLLTPGHTSG 113
Cdd:cd07725   43 WEGLKELGLKPSDIDRVLLTHHHPDHIGLAGKLQ------EKSGATV-YILDVTPVKDGDKIDLGGLRLKVIETPGHTPG 115

                         90       100
                 ....*....|....*....|...
gi 323635439 114 HMSYFLWEEEcpdppAVFSGDAL 136
Cdd:cd07725  116 HIVLYDEDRR-----ELFVGDAV 133
LACTB2-like_MBL-fold cd07722
uncharacterized subgroup which includes human lactamase beta 2 and related proteins; MBL-fold ...
 15-173 8.07e-10

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: 57.16  E-value: 8.07e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323635439  15 YLVIEERTReaVAVD-----VAVPKRLLEIVGREGV-SLTTVLTTHHHWDHARGNAEL--------------ARLRPGLA 74
Cdd:cd07722   21 YLVGTGKRR--ILIDtgegrPSYIPLLKSVLDSEGNaTISDILLTHWHHDHVGGLPDVldllrgpsprvykfPRPEEDED 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323635439  75 VLGADERICALTrrlvHGEELRFGAIHARCLLTPGHTSGHMSyFLWEEEcpdpPAVFSGDalSVAGCGlrlesTA----L 150
Cdd:cd07722   99 PDEDGGDIHDLQ----DGQVFKVEGATLRVIHTPGHTTDHVC-FLLEEE----NALFTGD--CVLGHG-----TAvfedL 162

                        170       180
                 ....*....|....*....|....
gi 323635439 151 QMY-ESLTQILGTLPpeTKVFCGH 173
Cdd:cd07722  163 AAYmASLKKLLSLGP--GRIYPGH 184
MBLAC2-like_MBL-fold cd07712
uncharacterized human metallo-beta-lactamase domain-containing protein 2 and related proteins; ...
 7-173 1.52e-09

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: 56.10  E-value: 1.52e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323635439   7 PVLEDNY---MYLVieERTREAVAVDVAVPKR-LLEIVgregVSLT----TVLTTHHHWDHARGN----------AELAR 68
Cdd:cd07712    1 LFIEEDDrvnIYLL--RGRDRALLIDTGLGIGdLKEYV----RTLTdlplLVVATHGHFDHIGGLhefeevyvhpADAEI 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323635439  69 LR-----PGLAVLGADERICA--LTRRLVHGEELRFGAIHARCLLTPGHTSGHMSyfLWEEECPDppaVFSGDALSVAGC 141
Cdd:cd07712   75 LAapdnfETLTWDAATYSVPPagPTLPLRDGDVIDLGDRQLEVIHTPGHTPGSIA--LLDRANRL---LFSGDVVYDGPL 149

                        170       180       190
                 ....*....|....*....|....*....|...
gi 323635439 142 GLRLESTALQMY-ESLTQILGTLPPETKVFCGH 173
Cdd:cd07712  150 IMDLPHSDLDDYlASLEKLSKLPDEFDKVLPGH 182
Lactamase_B pfam00753
Metallo-beta-lactamase superfamily;
34-173 3.17e-09

Metallo-beta-lactamase superfamily;


Pssm-ID: 425851 [Multi-domain]  Cd Length: 196  Bit Score: 55.45  E-value: 3.17e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323635439   34 KRLLEIVGREGVSLTTVLTTHHHWDHARGNAELARlRPGLAVLGADERICALTRRLVHGEELRFGAIHARC--------- 104
Cdd:pfam00753  31 LLLLAALGLGPKDIDAVILTHGHFDHIGGLGELAE-ATDVPVIVVAEEARELLDEELGLAASRLGLPGPPVvplppdvvl 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323635439  105 ---------------LLTPGHTSGHMSYflweeECPDPPAVFSGDALSVAGCGL----------RLESTALQMYESLTQI 159
Cdd:pfam00753 110 eegdgilggglgllvTHGPGHGPGHVVV-----YYGGGKVLFTGDLLFAGEIGRldlplggllvLHPSSAESSLESLLKL 184

                         170
                  ....*....|....
gi 323635439  160 LGtlPPETKVFCGH 173
Cdd:pfam00753 185 AK--LKAAVIVPGH 196
ST1585-like_MBL-fold cd07726
uncharacterized subgroup which includes Sulfolobus tokodaii ST1585 protein; MBL-fold metallo ...
 15-146 1.12e-08

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


Pssm-ID: 293812 [Multi-domain]  Cd Length: 215  Bit Score: 54.04  E-value: 1.12e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323635439  15 YLVIEERtrEAVAVD----VAVPkRLLEIVGREGVS---LTTVLTTHHHWDHARGNAELARLRPG--------------- 72
Cdd:cd07726   19 YLLDGEG--RPALIDtgpsSSVP-RLLAALEALGIApedVDYIILTHIHLDHAGGAGLLAEALPNakvyvhprgarhlid 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323635439  73 --------LAVLGAD-------------ERICALTrrlvHGEELRFGAIHARCLLTPGHTSGHMSYFLweeecPDPPAVF 131
Cdd:cd07726   96 psklwasaRAVYGDEadrlggeilpvpeERVIVLE----DGETLDLGGRTLEVIDTPGHAPHHLSFLD-----EESDGLF 166

                        170
                 ....*....|....*
gi 323635439 132 SGDALSVAGCGLRLE 146
Cdd:cd07726  167 TGDAAGVRYPELDVV 181
AHL_lactonase_MBL-fold cd07729
quorum-quenching N-acyl-homoserine lactonase, MBL-fold metallo-hydrolase domain; Acyl ...
 46-135 1.20e-07

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: 51.45  E-value: 1.20e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323635439  46 SLTTVLTTHHHWDHArGNAEL---ARL------------------RPGLAVLGADERICALTRRLVHGE-ELrFGAIhaR 103
Cdd:cd07729   88 DIDYVILSHLHFDHA-GGLDLfpnATIivqraeleyatgpdplaaGYYEDVLALDDDLPGGRVRLVDGDyDL-FPGV--T 163

                         90       100       110
                 ....*....|....*....|....*....|..
gi 323635439 104 CLLTPGHTSGHMSYFLweeECPDPPAVFSGDA 135
Cdd:cd07729  164 LIPTPGHTPGHQSVLV---RLPEGTVLLAGDA 192
SMB-1-like_MBL-B3 cd16313
SMB-1, THIN-B and related metallo-beta-lactamases, subclass B3; MBL-fold metallo-hydrolase ...
 50-117 2.46e-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: 47.55  E-value: 2.46e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323635439  50 VLTTHHHWDHARGNAELARLrPGLAVLGADERICAL-----------------------TRRLVHGEELRFGAIHARCLL 106
Cdd:cd16313   64 ILSSHDHWDHAGGIAALQKL-TGAQVLASPATVAVLrsgsmgkddpqfggltpmppvasVRAVRDGEVVKLGPLAVTAHA 142

                         90
                 ....*....|.
gi 323635439 107 TPGHTSGHMSY 117
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 ...
 26-117 3.33e-06

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: 47.34  E-value: 3.33e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323635439  26 VAVDVAVPK---RLLEIVGREGVSLTTV---LTTHHHWDHARGNAELARLR--------PGLAVL------------GAD 79
Cdd:cd16290   34 ILIDGALPQsapQIEANIRALGFRLEDVkliLNSHAHFDHAGGIAALQRDSgatvaaspAGAAALrsggvdpddpqaGAA 113

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 323635439  80 ERICALT--RRLVHGEELRFGAIHARCLLTPGHTSGHMSY 117
Cdd:cd16290  114 DPFPPVAkvRVVADGEVVKLGPLAVTAHATPGHTPGGTSW 153
metallo-hydrolase-like_MBL-fold cd16282
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 48-173 4.01e-05

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


Pssm-ID: 293840 [Multi-domain]  Cd Length: 209  Bit Score: 43.71  E-value: 4.01e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323635439  48 TTVLTTHHHWDHARGNA-------------------------ELARLRPGLAVLGADERICALTRRLVHGEELRFGAIHA 102
Cdd:cd16282   54 RYVVNTHYHGDHTLGNAafadagapiiahentreelaargeaYLELMRRLGGDAMAGTELVLPDRTFDDGLTLDLGGRTV 133

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 323635439 103 RCL-LTPGHTSGHMSYFLweeecPDPPAVFSGDALSVAGCGLRLESTALQMYESLTQILGTLPpeTKVFCGH 173
Cdd:cd16282  134 ELIhLGPAHTPGDLVVWL-----PEEGVLFAGDLVFNGRIPFLPDGSLAGWIAALDRLLALDA--TVVVPGH 198
Mbl1b-like_MBL-B3 cd16310
Caulobacter crescentus Mbl1b and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 50-140 4.62e-05

Caulobacter crescentus Mbl1b and related metallo-beta-lactamases, subclass B3; MBL-fold metallo-hydrolase domain; MBLs (class B of the Ambler beta-lactamase classification) are a diverse group of metallo-enzymes that are capable of catalyzing the hydrolysis of a wide range of beta-lactam antibiotics. MBLs have been divided into three subclasses B1, B2 and B3, based on sequence/structural relationships and substrates, with the B1 and B2 MBLs being most closely related to each other. This subgroup of Mbl1b-like MBLs belongs to the B3 subclass. Subclass B3 enzymes are most active with two zinc ions bound in the active site, and have a broad-spectrum substrate profile. These B3 enzymes have a modified Zn2/DCH site (Asp-His-His).


Pssm-ID: 293868  Cd Length: 252  Bit Score: 43.98  E-value: 4.62e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323635439  50 VLTTHHHWDHARGnaeLARLR--PGLAVLGADERICALT---------------------RRLVHGEELRFGAIHARCLL 106
Cdd:cd16310   64 IINTHAHYDHAGG---LAQLKadTGAKLWASRGDRPALEagkhigdnitqpapfpavkvdRILGDGEKIKLGDITLTATL 140

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 323635439 107 TPGHTSGHMSyflWEEECPDP----PAVFSGdALSVAG 140
Cdd:cd16310  141 TPGHTKGCTT---WSTTVKENgrplRVVFPC-SLSVAG 174
MBL-B3-like cd07708
metallo-beta-lactamases, subclass B3; MBL-fold metallo-hydrolase domain; MBLs (class B of the ...
 50-140 7.64e-04

metallo-beta-lactamases, subclass B3; MBL-fold metallo-hydrolase domain; MBLs (class B of the Ambler beta-lactamase classification) are a diverse group of metallo-enzymes that are capable of catalyzing the hydrolysis of a wide range of beta-lactam antibiotics. MBLs have been divided into three subclasses B1, B2 and B3, based on sequence/structural relationships and substrates, with the B1 and B2 MBLs being most closely related to each other. Subclass B3 enzymes are most active with two zinc ions bound in the active site, and have a broad-spectrum substrate profile. B3 MBLs include Fluoribacter gormanii FEZ-1, Elizabethkingia meningoseptica (Chryseobacterium meningosepticum) GOB-1, Stenotrophomonas Maltophilia L1, and Bradyrhizobium diazoefficiens BJP-1, Serratia marcescens SMB-1, and Pseudomonas Aeruginosa AIM-1. These B3 enzymes have a modified Zn2/DCH site (Asp-His-His).


Pssm-ID: 293794 [Multi-domain]  Cd Length: 248  Bit Score: 40.22  E-value: 7.64e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323635439  50 VLTTHHHWDHARGNAELARlRPGLAVLGADERICALTR----------------------RLVH-GEELRFGAIHARCLL 106
Cdd:cd07708   64 ILISHAHFDHAGGSAEIKK-QTGAKVMAGAEDVSLLLSggssdfhyandsstyfpqstvdRAVHdGERVTLGGTVLTAHA 142

                         90       100       110
                 ....*....|....*....|....*....|....
gi 323635439 107 TPGHTSGHMSYFLWEEECPDPPAVFSGDALSVAG 140
Cdd:cd07708  143 TPGHTPGCTTWTMTLKDHGKQYQVVFADSLTVNP 176
metallo-hydrolase-like_MBL-fold cd16277
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 48-136 9.08e-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: 39.81  E-value: 9.08e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323635439  48 TTVLTTHHHWDH------------------AR---GNAELARLRP----------------------GLAVL-GADERIc 83
Cdd:cd16277   65 DYVLCTHLHVDHvgwntrlvdgrwvptfpnARylfSRAEYDHWSSpdaggppnrgvfedsvlpvieaGLADLvDDDHEI- 143

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 323635439  84 altrrlvhGEELRFgaiharcLLTPGHTSGHMSYFLweeECPDPPAVFSGDAL 136
Cdd:cd16277  144 --------LDGIRL-------EPTPGHTPGHVSVEL---ESGGERALFTGDVM 178
GOB1-like_MBL-B3 cd16308
Elizabethkingia meningoseptica GOB-1 and related metallo-beta-lactamases, subclass B3; ...
 26-119 1.06e-03

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: 1.06e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323635439  26 VAVDVAVPKRLLEIVGREGVSLTTVLTTHHHWDHARGNAELARLRPglAVLGADERICALTR------------------ 87
Cdd:cd16308   40 LAESVPLIKKNIQALGFKFKDIKILLTTQAHYDHVGAMAAIKQQTG--AKMMVDEKDAKVLAdggksdyemggygstfap 117

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 323635439  88 ----RLVH-GEELRFGAIHARCLLTPGHTSGHMSYFL 119
Cdd:cd16308  118 vkadKLLHdGDTIKLGGTKLTLLHHPGHTKGSCSFLF 154
metallo-hydrolase-like_MBL-fold cd07743
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 32-76 8.19e-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) from which this fold was named are only a small fraction of the activities which are included in this superfamily. Activities carried out by superfamily members include class B beta-lactamases, hydroxyacylglutathione hydrolases, AHL (acyl homoserine lactone) lactonases, persulfide dioxygenases, flavodiiron proteins, cleavage and polyadenylation specificity factors such as the Int9 and Int11 subunits of Integrator, Sdsa1-like and AtsA-like arylsulfatases, 5'-exonucleases human SNM1A and yeast Pso2p, ribonuclease J and ribonuclease Z, cyclic nucleotide phosphodiesterases, insecticide hydrolases, and proteins required for natural transformation competence. Classical members of the superfamily are di-, or less commonly mono-, zinc-ion-dependent hydrolases, however the diversity of biological roles is reflected in variations in the active site metallo-chemistry.


Pssm-ID: 293829 [Multi-domain]  Cd Length: 197  Bit Score: 36.74  E-value: 8.19e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 323635439  32 VPKRLLEIVGREGVSLTTVLTTHHHWDHARGNAELARlRPGLAVL 76
Cdd:cd07743   31 AGRKIRKILEELGWKLKAIINTHSHADHIGGNAYLQK-KTGCKVY 74
 
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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