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Conserved domains on  [gi|588480498|ref|NP_001277068|]
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hydroxyacylglutathione hydrolase-like protein isoform 2 [Homo sapiens]

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
 1-244 6.32e-90

hydroxyacylglutathione hydrolase


The actual alignment was detected with superfamily member PLN02469:

Pssm-ID: 178088 [Multi-domain]  Cd Length: 258  Bit Score: 267.40  E-value: 6.32e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 588480498   1 MKVKVIPVLEDNYMYLVIEELTREAVAVDVAVPKRLLEIVGREGVSLTAVLTTHHHWDHARGNPELARLRPGLAVLG-AD 79
Cdd:PLN02469   1 MKIIPVPCLEDNYAYLIIDESTKDAAVVDPVDPEKVLQAAHEHGAKIKLVLTTHHHWDHAGGNEKIKKLVPGIKVYGgSL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 588480498  80 ERIFSLTRRLAHGEELRFGA-IHVRCLLTPGHTAGHMSYFLWEDDCPDPpALFSGDALSVAGCGSCLEGSAQQMYQSLAE 158
Cdd:PLN02469  81 DNVKGCTHPVENGDKLSLGKdVNILALHTPCHTKGHISYYVTGKEGEDP-AVFTGDTLFIAGCGKFFEGTAEQMYQSLCV 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 588480498 159 -LGTLPPETKVFCGHEHTLSNLEFAQKVEPCNDHVRAKLSWAKKRDEDDVPTVPSTLGEERLYNPFLRVAEEPVRKFTGK 237
Cdd:PLN02469 160 tLGSLPKPTQVYCGHEYTVKNLKFALTVEPDNEKLKQKLEWAEKQRQAGLPTVPSTIEEELETNPFMRVDLPEIQEKVGC 239


                 ....*..
gi 588480498 238 AVPADVL 244
Cdd:PLN02469 240 ESPVEAL 246
 
Name Accession Description Interval E-value
PLN02469 PLN02469
hydroxyacylglutathione hydrolase
 1-244 6.32e-90

hydroxyacylglutathione hydrolase


Pssm-ID: 178088 [Multi-domain]  Cd Length: 258  Bit Score: 267.40  E-value: 6.32e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 588480498   1 MKVKVIPVLEDNYMYLVIEELTREAVAVDVAVPKRLLEIVGREGVSLTAVLTTHHHWDHARGNPELARLRPGLAVLG-AD 79
Cdd:PLN02469   1 MKIIPVPCLEDNYAYLIIDESTKDAAVVDPVDPEKVLQAAHEHGAKIKLVLTTHHHWDHAGGNEKIKKLVPGIKVYGgSL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 588480498  80 ERIFSLTRRLAHGEELRFGA-IHVRCLLTPGHTAGHMSYFLWEDDCPDPpALFSGDALSVAGCGSCLEGSAQQMYQSLAE 158
Cdd:PLN02469  81 DNVKGCTHPVENGDKLSLGKdVNILALHTPCHTKGHISYYVTGKEGEDP-AVFTGDTLFIAGCGKFFEGTAEQMYQSLCV 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 588480498 159 -LGTLPPETKVFCGHEHTLSNLEFAQKVEPCNDHVRAKLSWAKKRDEDDVPTVPSTLGEERLYNPFLRVAEEPVRKFTGK 237
Cdd:PLN02469 160 tLGSLPKPTQVYCGHEYTVKNLKFALTVEPDNEKLKQKLEWAEKQRQAGLPTVPSTIEEELETNPFMRVDLPEIQEKVGC 239


                 ....*..
gi 588480498 238 AVPADVL 244
Cdd:PLN02469 240 ESPVEAL 246
GSH_gloB TIGR03413
hydroxyacylglutathione hydrolase; Members of this protein family are hydroxyacylglutathione ...
 6-254 3.16e-87

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: 260.16  E-value: 3.16e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 588480498    6 IPVLEDNYMYLVIEELTReAVAVDVAVPKRLLEIVGREGVSLTAVLTTHHHWDHARGNPELARlRPGLAVLG-ADERIFS 84
Cdd:TIGR03413   4 IPALSDNYIWLLHDPDGQ-AAVVDPGEAEPVLDALEARGLTLTAILLTHHHHDHVGGVAELLE-AFPAPVYGpAEERIPG 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 588480498   85 LTRRLAHGEELRFGAIHVRCLLTPGHTAGHMSYFLweddcPDPPALFSGDALSVAGCGSCLEGSAQQMYQSLAELGTLPP 164
Cdd:TIGR03413  82 ITHPVKDGDTVTLGGLEFEVLAVPGHTLGHIAYYL-----PDSPALFCGDTLFSAGCGRLFEGTPEQMYDSLQRLAALPD 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 588480498  165 ETKVFCGHEHTLSNLEFAQKVEPCNDHVRAKLSWAKKRDEDDVPTVPSTLGEERLYNPFLRVAEEPVRKFTGK--AVPAD 242
Cdd:TIGR03413 157 DTLVYCAHEYTLSNLRFALTVEPDNPALQERLKEVEALRAQGQPTLPSTLGLERATNPFLRADDPAVRAALGSqgADPVE 236

                         250
                  ....*....|..
gi 588480498  243 VLEALCKERARF 254
Cdd:TIGR03413 237 VFAALRAWKDNF 248
hydroxyacylglutathione_hydrolase_MBL-fold cd07723
hydroxyacylglutathione hydrolase, MBL-fold metallo-hydrolase domain; hydroxyacylglutathione ...
 4-172 1.54e-82

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: 245.45  E-value: 1.54e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 588480498   4 KVIPVLEDNYMYLVIEELTREAVAVDVAVPKRLLEIVGREGVSLTAVLTTHHHWDHARGNPELARLRPGLAVLG-ADERI 82
Cdd:cd07723    1 VPIPALSDNYIYLIVDEATGEAAVVDPGEAEPVLAALEKNGLTLTAILTTHHHWDHTGGNAELKALFPDAPVYGpAEDRI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 588480498  83 FSLTRRLAHGEELRFGAIHVRCLLTPGHTAGHMSYFLweddcPDPPALFSGDALSVAGCGSCLEGSAQQMYQSLAELGTL 162
Cdd:cd07723   81 PGLDHPVKDGDEIKLGGLEVKVLHTPGHTLGHICYYV-----PDEPALFTGDTLFSGGCGRFFEGTAEQMYASLQKLLAL 155

                        170
                 ....*....|
gi 588480498 163 PPETKVFCGH 172
Cdd:cd07723  156 PDDTLVYCGH 165
GloB COG0491
Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General ...
 11-177 2.25e-33

Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General function prediction only];


Pssm-ID: 440257 [Multi-domain]  Cd Length: 215  Bit Score: 121.34  E-value: 2.25e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 588480498  11 DNYMYLVIEelTREAVAVD----VAVPKRLLEIVGREGVSLTAVLTTHHHWDHARGNPELAR---------------LRP 71
Cdd:COG0491   14 GVNSYLIVG--GDGAVLIDtglgPADAEALLAALAALGLDIKAVLLTHLHPDHVGGLAALAEafgapvyahaaeaeaLEA 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 588480498  72 GLAVLGADERIFSLTRRLAHGEELRFGAIHVRCLLTPGHTAGHMSYFLweddcPDPPALFSGDALSVAGCGS--CLEGSA 149
Cdd:COG0491   92 PAAGALFGREPVPPDRTLEDGDTLELGGPGLEVIHTPGHTPGHVSFYV-----PDEKVLFTGDALFSGGVGRpdLPDGDL 166

                        170       180
                 ....*....|....*....|....*...
gi 588480498 150 QQMYQSLAELGTLPPETkVFCGHEHTLS 177
Cdd:COG0491  167 AQWLASLERLLALPPDL-VIPGHGPPTT 193
HAGH_C pfam16123
Hydroxyacylglutathione hydrolase C-terminus; This domain is found at the C-terminus of ...
 173-254 5.06e-33

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: 116.00  E-value: 5.06e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 588480498  173 EHTLSNLEFAQKVEPCNDHVRAKLSWAKKRDEDDVPTVPSTLGEERLYNPFLRVAEEPVRKFTGKAVPADVLEALCKERA 252
Cdd:pfam16123   1 EYTLSNLKFALSVEPDNEALQKRLAWVEALRAAGEPTVPSTLGDEKATNPFLRVDDPAVQKATGETDPVEVFAALRELKD 80


                  ..
gi 588480498  253 RF 254
Cdd:pfam16123  81 NF 82
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 13-172 1.90e-23

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


Pssm-ID: 214854 [Multi-domain]  Cd Length: 177  Bit Score: 94.16  E-value: 1.90e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 588480498    13 YMYLVIEEltREAVAVD--VAVPKRLLEIVGREGVS-LTAVLTTHHHWDHARGNPELARlRPGLAVLG------------ 77
Cdd:smart00849   1 NSYLVRDD--GGAILIDtgPGEAEDLLAELKKLGPKkIDAIILTHGHPDHIGGLPELLE-APGAPVYApegtaellkdll 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 588480498    78 -------ADERIFSLTRRLAHGEELRFGAIHVRCLLTPGHTAGHMSYFLweddcPDPPALFSGDALSVAGCG-SCLEGSA 149
Cdd:smart00849  78 allgelgAEAEPAPPDRTLKDGDELDLGGGELEVIHTPGHTPGSIVLYL-----PEGKILFTGDLLFAGGDGrTLVDGGD 152

                          170       180
                   ....*....|....*....|....*
gi 588480498   150 QQMYQSLAELGTL--PPETKVFCGH 172
Cdd:smart00849 153 AAASDALESLLKLlkLLPKLVVPGH 177
 
Name Accession Description Interval E-value
PLN02469 PLN02469
hydroxyacylglutathione hydrolase
 1-244 6.32e-90

hydroxyacylglutathione hydrolase


Pssm-ID: 178088 [Multi-domain]  Cd Length: 258  Bit Score: 267.40  E-value: 6.32e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 588480498   1 MKVKVIPVLEDNYMYLVIEELTREAVAVDVAVPKRLLEIVGREGVSLTAVLTTHHHWDHARGNPELARLRPGLAVLG-AD 79
Cdd:PLN02469   1 MKIIPVPCLEDNYAYLIIDESTKDAAVVDPVDPEKVLQAAHEHGAKIKLVLTTHHHWDHAGGNEKIKKLVPGIKVYGgSL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 588480498  80 ERIFSLTRRLAHGEELRFGA-IHVRCLLTPGHTAGHMSYFLWEDDCPDPpALFSGDALSVAGCGSCLEGSAQQMYQSLAE 158
Cdd:PLN02469  81 DNVKGCTHPVENGDKLSLGKdVNILALHTPCHTKGHISYYVTGKEGEDP-AVFTGDTLFIAGCGKFFEGTAEQMYQSLCV 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 588480498 159 -LGTLPPETKVFCGHEHTLSNLEFAQKVEPCNDHVRAKLSWAKKRDEDDVPTVPSTLGEERLYNPFLRVAEEPVRKFTGK 237
Cdd:PLN02469 160 tLGSLPKPTQVYCGHEYTVKNLKFALTVEPDNEKLKQKLEWAEKQRQAGLPTVPSTIEEELETNPFMRVDLPEIQEKVGC 239


                 ....*..
gi 588480498 238 AVPADVL 244
Cdd:PLN02469 240 ESPVEAL 246
GSH_gloB TIGR03413
hydroxyacylglutathione hydrolase; Members of this protein family are hydroxyacylglutathione ...
 6-254 3.16e-87

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: 260.16  E-value: 3.16e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 588480498    6 IPVLEDNYMYLVIEELTReAVAVDVAVPKRLLEIVGREGVSLTAVLTTHHHWDHARGNPELARlRPGLAVLG-ADERIFS 84
Cdd:TIGR03413   4 IPALSDNYIWLLHDPDGQ-AAVVDPGEAEPVLDALEARGLTLTAILLTHHHHDHVGGVAELLE-AFPAPVYGpAEERIPG 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 588480498   85 LTRRLAHGEELRFGAIHVRCLLTPGHTAGHMSYFLweddcPDPPALFSGDALSVAGCGSCLEGSAQQMYQSLAELGTLPP 164
Cdd:TIGR03413  82 ITHPVKDGDTVTLGGLEFEVLAVPGHTLGHIAYYL-----PDSPALFCGDTLFSAGCGRLFEGTPEQMYDSLQRLAALPD 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 588480498  165 ETKVFCGHEHTLSNLEFAQKVEPCNDHVRAKLSWAKKRDEDDVPTVPSTLGEERLYNPFLRVAEEPVRKFTGK--AVPAD 242
Cdd:TIGR03413 157 DTLVYCAHEYTLSNLRFALTVEPDNPALQERLKEVEALRAQGQPTLPSTLGLERATNPFLRADDPAVRAALGSqgADPVE 236

                         250
                  ....*....|..
gi 588480498  243 VLEALCKERARF 254
Cdd:TIGR03413 237 VFAALRAWKDNF 248
hydroxyacylglutathione_hydrolase_MBL-fold cd07723
hydroxyacylglutathione hydrolase, MBL-fold metallo-hydrolase domain; hydroxyacylglutathione ...
 4-172 1.54e-82

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: 245.45  E-value: 1.54e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 588480498   4 KVIPVLEDNYMYLVIEELTREAVAVDVAVPKRLLEIVGREGVSLTAVLTTHHHWDHARGNPELARLRPGLAVLG-ADERI 82
Cdd:cd07723    1 VPIPALSDNYIYLIVDEATGEAAVVDPGEAEPVLAALEKNGLTLTAILTTHHHWDHTGGNAELKALFPDAPVYGpAEDRI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 588480498  83 FSLTRRLAHGEELRFGAIHVRCLLTPGHTAGHMSYFLweddcPDPPALFSGDALSVAGCGSCLEGSAQQMYQSLAELGTL 162
Cdd:cd07723   81 PGLDHPVKDGDEIKLGGLEVKVLHTPGHTLGHICYYV-----PDEPALFTGDTLFSGGCGRFFEGTAEQMYASLQKLLAL 155

                        170
                 ....*....|
gi 588480498 163 PPETKVFCGH 172
Cdd:cd07723  156 PDDTLVYCGH 165
PLN02398 PLN02398
hydroxyacylglutathione hydrolase
 1-247 2.36e-55

hydroxyacylglutathione hydrolase


Pssm-ID: 215223 [Multi-domain]  Cd Length: 329  Bit Score: 181.58  E-value: 2.36e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 588480498   1 MKVKVIPVLEDNYMYLVIEELTREAVAVDVAVPKRLLEIVGREGVSLTAVLTTHHHWDHARGNPELaRLRPGLAVLGAD- 79
Cdd:PLN02398  76 LQIELVPCLKDNYAYLLHDEDTGTVGVVDPSEAVPVIDALSRKNRNLTYILNTHHHYDHTGGNLEL-KARYGAKVIGSAv 154

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 588480498  80 --ERIFSLTRRLAHGEELRFGAIHVRCLLTPGHTAGHMSYFLweddcPDPPALFSGDALSVAGCGSCLEGSAQQMYQSLA 157
Cdd:PLN02398 155 dkDRIPGIDIVLKDGDKWMFAGHEVLVMETPGHTRGHISFYF-----PGSGAIFTGDTLFSLSCGKLFEGTPEQMLSSLQ 229

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 588480498 158 ELGTLPPETKVFCGHEHTLSNLEFAQKVEPCNDHVRAKLSWAKKRDEDDVPTVPSTLGEERLYNPFLRVAEEPVRKFTGK 237
Cdd:PLN02398 230 KIISLPDDTNIYCGHEYTLSNSKFALSIEPNNEVLQSYAAHVAHLRSKGLPTIPTTVKMEKACNPFLRTSSTDIRKSLSI 309

                        250
                 ....*....|
gi 588480498 238 AVPADVLEAL 247
Cdd:PLN02398 310 PDTADEAEAL 319
BaeB-like_MBL-fold cd16275
Bacillus amyloliquefaciens BaeB and related proteins; MBL-fold metallo hydrolase domain; ...
 11-172 3.91e-43

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: 144.99  E-value: 3.91e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 588480498  11 DNYMYLVIEELTREAVAVDvavP----KRLLEIVGREGVSLTAVLTTHHHWDHARGNPELARlRPGLAV-LGADERIFS- 84
Cdd:cd16275   11 INYSYIIIDKATREAAVVD---PawdiEKILAKLNELGLTLTGILLTHSHFDHVNLVEPLLA-KYDAPVyMSKEEIDYYg 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 588480498  85 -LTRRLA---HGEELRFGAIHVRCLLTPGHTAGHMSYFLweDDCpdppaLFSGDALSVAGCGSC--LEGSAQQMYQSLAE 158
Cdd:cd16275   87 fRCPNLIpleDGDTIKIGDTEITCLLTPGHTPGSMCYLL--GDS-----LFTGDTLFIEGCGRCdlPGGDPEEMYESLQR 159

                        170
                 ....*....|....*
gi 588480498 159 LGTLPPE-TKVFCGH 172
Cdd:cd16275  160 LKKLPPPnTRVYPGH 174
PRK10241 PRK10241
hydroxyacylglutathione hydrolase; Provisional
 1-226 2.48e-40

hydroxyacylglutathione hydrolase; Provisional


Pssm-ID: 182327 [Multi-domain]  Cd Length: 251  Bit Score: 140.34  E-value: 2.48e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 588480498   1 MKVKVIPVLEDNYMYLVIEELTReAVAVDVAVPKRLLEIVGREGVSLTAVLTTHHHWDHARGNPELARLRPGLAVLGADE 80
Cdd:PRK10241   1 MNLNSIPAFDDNYIWVLNDEAGR-CLIVDPGEAEPVLNAIAENNWQPEAIFLTHHHHDHVGGVKELVEKFPQIVVYGPQE 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 588480498  81 -RIFSLTRRLAHGEELRFGAIHVRCLLTPGHTAGHMSYFlweddcpDPPALFSGDALSVAGCGSCLEGSAQQMYQSLAEL 159
Cdd:PRK10241  80 tQDKGTTQVVKDGETAFVLGHEFSVFATPGHTLGHICYF-------SKPYLFCGDTLFSGGCGRLFEGTASQMYQSLKKI 152

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 588480498 160 GTLPPETKVFCGHEHTLSNLEFAQKVEP----CNDHVR-AKLSWAKKRDeddvpTVPSTLGEERLYNPFLRV 226
Cdd:PRK10241 153 NALPDDTLICCAHEYTLSNMKFALSILPhdlsINDYYRkVKELRAKNQI-----TLPVILKNERQINLFLRT 219
POD-like_MBL-fold cd07724
ETHE1 (PDO type I), persulfide dioxygenase A (PDOA, PDO type II) and related proteins; ...
 15-172 2.73e-35

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: 124.82  E-value: 2.73e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 588480498  15 YLVIEELTREAVAVD--VAVPKRLLEIVGREGVSLTAVLTTHHHWDHARGNPELARlRPGLA-VLGADERIFSLTRRLAH 91
Cdd:cd07724   15 YLVGDPETGEAAVIDpvRDSVDRYLDLAAELGLKITYVLETHVHADHVSGARELAE-RTGAPiVIGEGAPASFFDRLLKD 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 588480498  92 GEELRFGAIHVRCLLTPGHTAGHMSYfLWEddcpDPPALFSGDALSVAGCGSC-----LEGSAQQMYQSLAE-LGTLPPE 165
Cdd:cd07724   94 GDVLELGNLTLEVLHTPGHTPESVSY-LVG----DPDAVFTGDTLFVGDVGRPdlpgeAEGLARQLYDSLQRkLLLLPDE 168


                 ....*..
gi 588480498 166 TKVFCGH 172
Cdd:cd07724  169 TLVYPGH 175
GloB COG0491
Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General ...
 11-177 2.25e-33

Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General function prediction only];


Pssm-ID: 440257 [Multi-domain]  Cd Length: 215  Bit Score: 121.34  E-value: 2.25e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 588480498  11 DNYMYLVIEelTREAVAVD----VAVPKRLLEIVGREGVSLTAVLTTHHHWDHARGNPELAR---------------LRP 71
Cdd:COG0491   14 GVNSYLIVG--GDGAVLIDtglgPADAEALLAALAALGLDIKAVLLTHLHPDHVGGLAALAEafgapvyahaaeaeaLEA 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 588480498  72 GLAVLGADERIFSLTRRLAHGEELRFGAIHVRCLLTPGHTAGHMSYFLweddcPDPPALFSGDALSVAGCGS--CLEGSA 149
Cdd:COG0491   92 PAAGALFGREPVPPDRTLEDGDTLELGGPGLEVIHTPGHTPGHVSFYV-----PDEKVLFTGDALFSGGVGRpdLPDGDL 166

                        170       180
                 ....*....|....*....|....*...
gi 588480498 150 QQMYQSLAELGTLPPETkVFCGHEHTLS 177
Cdd:COG0491  167 AQWLASLERLLALPPDL-VIPGHGPPTT 193
HAGH_C pfam16123
Hydroxyacylglutathione hydrolase C-terminus; This domain is found at the C-terminus of ...
 173-254 5.06e-33

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: 116.00  E-value: 5.06e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 588480498  173 EHTLSNLEFAQKVEPCNDHVRAKLSWAKKRDEDDVPTVPSTLGEERLYNPFLRVAEEPVRKFTGKAVPADVLEALCKERA 252
Cdd:pfam16123   1 EYTLSNLKFALSVEPDNEALQKRLAWVEALRAAGEPTVPSTLGDEKATNPFLRVDDPAVQKATGETDPVEVFAALRELKD 80


                  ..
gi 588480498  253 RF 254
Cdd:pfam16123  81 NF 82
metallo-hydrolase-like_MBL-fold cd06262
mainly hydrolytic enzymes and related proteins which carry out various biological functions; ...
 15-172 2.06e-31

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: 115.08  E-value: 2.06e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 588480498  15 YLVIEElTREAVAVDVA--VPKRLLEIVGREGVSLTAVLTTHHHWDHARGNPELARL-------------------RPGL 73
Cdd:cd06262   13 YLVSDE-EGEAILIDPGagALEKILEAIEELGLKIKAILLTHGHFDHIGGLAELKEApgapvyiheadaelledpeLNLA 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 588480498  74 AVLGADERIFSLTRRLAHGEELRFGAIHVRCLLTPGHTAGHMSYFlweddCPDPPALFSGDALSVAGCGSC--LEGSAQQ 151
Cdd:cd06262   92 FFGGGPLPPPEPDILLEDGDTIELGGLELEVIHTPGHTPGSVCFY-----IEEEGVLFTGDTLFAGSIGRTdlPGGDPEQ 166

                        170       180
                 ....*....|....*....|..
gi 588480498 152 MYQSLAE-LGTLPPETKVFCGH 172
Cdd:cd06262  167 LIESIKKlLLLLPDDTVVYPGH 188
TTHA1623-like_MBL-fold cd16322
uncharacterized Thermus thermophilus TTHA1623 and related proteins; MBL-fold metallo hydrolase ...
 5-224 2.16e-27

uncharacterized Thermus thermophilus TTHA1623 and related proteins; MBL-fold metallo hydrolase domain; Includes the MBL-fold metallo hydrolase domain of uncharacterized Thermus thermophilus TTHA1623 and related proteins. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions. This family includes homologs present in a wide range of bacteria and archaea and some eukaryota. Members of the MBL-fold metallo-hydrolase superfamily exhibit a variety of active site metallo-chemistry, TTHA1623 exhibiting a uniquely shaped putative substrate-binding pocket with a glyoxalase II-type metal-coordination mode.


Pssm-ID: 293877 [Multi-domain]  Cd Length: 204  Bit Score: 105.12  E-value: 2.16e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 588480498   5 VIPVLEDNyMYLVIEELTREAVAVDVAVPK-RLLEIVGREGVSLTAVLTTHHHWDHARGNPELARLRPGLAVLGADE--- 80
Cdd:cd16322    5 TLGPLQEN-TYLVADEGGGEAVLVDPGDESeKLLARFGTTGLTLLYILLTHAHFDHVGGVADLRRHPGAPVYLHPDDlpl 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 588480498  81 --------RIFSL--------TRRLAHGEELRFGAIHVRCLLTPGHTAGHMSYFlweddCPDPPALFSGDALSVAGCGSC 144
Cdd:cd16322   84 yeaadlgaKAFGLgieplpppDRLLEDGQTLTLGGLEFKVLHTPGHSPGHVCFY-----VEEEGLLFSGDLLFQGSIGRT 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 588480498 145 -LEGSA-QQMYQSLAELGTLPPETKVFCGHehtlsnlefaqkvepcndhvraklswakkrdeddvpTVPSTLGEERLYNP 222
Cdd:cd16322  159 dLPGGDpKAMAASLRRLLTLPDETRVFPGH------------------------------------GPPTTLGEERRTNP 202


                 ..
gi 588480498 223 FL 224
Cdd:cd16322  203 FL 204
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 13-172 1.90e-23

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


Pssm-ID: 214854 [Multi-domain]  Cd Length: 177  Bit Score: 94.16  E-value: 1.90e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 588480498    13 YMYLVIEEltREAVAVD--VAVPKRLLEIVGREGVS-LTAVLTTHHHWDHARGNPELARlRPGLAVLG------------ 77
Cdd:smart00849   1 NSYLVRDD--GGAILIDtgPGEAEDLLAELKKLGPKkIDAIILTHGHPDHIGGLPELLE-APGAPVYApegtaellkdll 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 588480498    78 -------ADERIFSLTRRLAHGEELRFGAIHVRCLLTPGHTAGHMSYFLweddcPDPPALFSGDALSVAGCG-SCLEGSA 149
Cdd:smart00849  78 allgelgAEAEPAPPDRTLKDGDELDLGGGELEVIHTPGHTPGSIVLYL-----PEGKILFTGDLLFAGGDGrTLVDGGD 152

                          170       180
                   ....*....|....*....|....*
gi 588480498   150 QQMYQSLAELGTL--PPETKVFCGH 172
Cdd:smart00849 153 AAASDALESLLKLlkLLPKLVVPGH 177
PLN02962 PLN02962
hydroxyacylglutathione hydrolase
 13-244 1.52e-19

hydroxyacylglutathione hydrolase


Pssm-ID: 178547 [Multi-domain]  Cd Length: 251  Bit Score: 85.23  E-value: 1.52e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 588480498  13 YMYLV--IEELTREAVAVDvAVPK---RLLEIVGREGVSLTAVLTTHHHWDHARGNPELARLRPGLAVL-----GADERI 82
Cdd:PLN02962  24 YTYLLadVSHPDKPALLID-PVDKtvdRDLSLVKELGLKLIYAMNTHVHADHVTGTGLLKTKLPGVKSIiskasGSKADL 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 588480498  83 FsltrrLAHGEELRFGAIHVRCLLTPGHTAGHMSYFLWE-DDCPDPPALFSGDALSVAGCGSC--LEGSAQQMYQSL-AE 158
Cdd:PLN02962 103 F-----VEPGDKIYFGDLYLEVRATPGHTAGCVTYVTGEgPDQPQPRMAFTGDALLIRGCGRTdfQGGSSDQLYKSVhSQ 177

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 588480498 159 LGTLPPETKVFCGHE---HTLsnlefaqkvepcndhvraklswakkrdeddvptvpSTLGEERLYNPFLRVAEE------ 229
Cdd:PLN02962 178 IFTLPKDTLIYPAHDykgFTV-----------------------------------STVGEEMLYNPRLTKDEEtfktim 222

                        250       260
                 ....*....|....*....|
gi 588480498 230 -----PVRKFTGKAVPADVL 244
Cdd:PLN02962 223 enlnlPYPKMIDVAVPANMV 242
YcbL-like_MBL-fold cd07737
Salmonella enterica serovar typhimurium YcbL and related proteins; MBL-fold metallo hydrolase ...
 3-172 3.65e-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: 80.29  E-value: 3.65e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 588480498   3 VKVIPV--LEDNyMYLVIEELTREAVAVDV-AVPKRLLEIVGREGVSLTAVLTTHHHWDHARGNPELARL---------- 69
Cdd:cd07737    1 YQIIPVtpFQQN-CSLIWCEETKEAAVIDPgGDADKILQAIEDLGLTLKKILLTHGHLDHVGGAAELAEHygvpiigphk 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 588480498  70 --RPGLAVLGADERIFSL--------TRRLAHGEELRFGAIHVRCLLTPGHTAGHMSYFlweddCPDPPALFSGDALSVA 139
Cdd:cd07737   80 edKFLLENLPEQSQMFGFppaeaftpDRWLEEGDTVTVGNLTLEVLHCPGHTPGHVVFF-----NRESKLAIVGDVLFKG 154

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 588480498 140 GCGSC--LEGSAQQMYQSLAE-LGTLPPETKVFCGH 172
Cdd:cd07737  155 SIGRTdfPGGNHAQLIASIKEkLLPLGDDVTFIPGH 190
metallo-hydrolase-like_MBL-fold cd16278
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 35-172 6.33e-18

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: 79.46  E-value: 6.33e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 588480498  35 RLLEIVGREGVSltAVLTTHHHWDHARGNPELARlRPGLAVLGADERI-------FSLTRRLAHGEELRFGAIHVRCLLT 107
Cdd:cd16278   44 ALLAALGGGRVS--AILVTHTHRDHSPGAARLAE-RTGAPVRAFGPHRaggqdtdFAPDRPLADGEVIEGGGLRLTVLHT 120

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 588480498 108 PGHTAGHMSyFLWEDDcpdpPALFSGDAlsVAGCGSCL----EGSAQQMYQSLAELGTLPPETkVFCGH 172
Cdd:cd16278  121 PGHTSDHLC-FALEDE----GALFTGDH--VMGWSTTViappDGDLGDYLASLERLLALDDRL-LLPGH 181
yflN-like_MBL-fold cd07721
uncharacterized subgroup which includes Bacillus subtilis yflN; MBL-fold metallo hydrolase ...
 2-172 1.68e-17

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: 78.80  E-value: 1.68e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 588480498   2 KVKVIPVLEDNYMYLVIEEltREAVAVDVAVP---KRLLEIVGREGVS---LTAVLTTHHHWDHARGNPELARlRPGLAV 75
Cdd:cd07721    1 GVYQLPLLPPVNAYLIEDD--DGLTLIDTGLPgsaKRILKALRELGLSpkdIRRILLTHGHIDHIGSLAALKE-APGAPV 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 588480498  76 L-GADE----------------------------RIFSLTRRLAHGEELRF-GAIHVrcLLTPGHTAGHMSYFLWEDDcp 125
Cdd:cd07721   78 YaHEREapylegekpypppvrlgllgllspllpvKPVPVDRTLEDGDTLDLaGGLRV--IHTPGHTPGHISLYLEEDG-- 153

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 588480498 126 dppALFSGDALSVAGcgscleGSA-----------QQMYQSLAELGTLPPETkVFCGH 172
Cdd:cd07721  154 ---VLIAGDALVTVG------GELvpppppftwdmEEALESLRKLAELDPEV-LAPGH 201
TTHA1429-like_MBL-fold cd07725
uncharacterized Thermus thermophilus TTHA1429 and related proteins; MBL-fold metallo hydrolase ...
 34-172 3.71e-12

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: 63.47  E-value: 3.71e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 588480498  34 KRLLEIVGREGVSLTAVLTTHHHWDHARGNPELArlrpglAVLGADERIfSLTRRLAHGEELRFGAIHVRCLLTPGHTAG 113
Cdd:cd07725   43 WEGLKELGLKPSDIDRVLLTHHHPDHIGLAGKLQ------EKSGATVYI-LDVTPVKDGDKIDLGGLRLKVIETPGHTPG 115

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 588480498 114 HMSYFLWEDDcpdppALFSGDAL------SVAGCGSCLEGSAQQMYQSLAELGTLPPEtKVFCGH 172
Cdd:cd07725  116 HIVLYDEDRR-----ELFVGDAVlpkitpNVSLWAVRVEDPLGAYLESLDKLEKLDVD-LAYPGH 174
LACTB2-like_MBL-fold cd07722
uncharacterized subgroup which includes human lactamase beta 2 and related proteins; MBL-fold ...
 34-172 9.81e-12

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: 62.55  E-value: 9.81e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 588480498  34 KRLLEivGREGVSLTAVLTTHHHWDHARGNPELARLRPGLAV-------LGADERIFSLTRR---LAHGEELRFGAIHVR 103
Cdd:cd07722   46 KSVLD--SEGNATISDILLTHWHHDHVGGLPDVLDLLRGPSPrvykfprPEEDEDPDEDGGDihdLQDGQVFKVEGATLR 123

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 588480498 104 CLLTPGHTAGHMSYFLWEDDcpdppALFSGDalSVAGCGSC-LEGSAQQMyQSLAELGTLPPeTKVFCGH 172
Cdd:cd07722  124 VIHTPGHTTDHVCFLLEEEN-----ALFTGD--CVLGHGTAvFEDLAAYM-ASLKKLLSLGP-GRIYPGH 184
ST1585-like_MBL-fold cd07726
uncharacterized subgroup which includes Sulfolobus tokodaii ST1585 protein; MBL-fold metallo ...
 15-166 6.41e-10

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: 57.89  E-value: 6.41e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 588480498  15 YLVIEEltREAVAVD----VAVPkRLLEIVGREGVS---LTAVLTTHHHWDHARGNPELARLRPG--------------- 72
Cdd:cd07726   19 YLLDGE--GRPALIDtgpsSSVP-RLLAALEALGIApedVDYIILTHIHLDHAGGAGLLAEALPNakvyvhprgarhlid 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 588480498  73 --------LAVLGAD-------------ERIFSLtrrlAHGEELRFGAIHVRCLLTPGHTAGHMSYFLWEDDcpdppALF 131
Cdd:cd07726   96 psklwasaRAVYGDEadrlggeilpvpeERVIVL----EDGETLDLGGRTLEVIDTPGHAPHHLSFLDEESD-----GLF 166

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 588480498 132 SGDALSVAGCGSCLEGSA---------QQMYQSLAELGTLPPET 166
Cdd:cd07726  167 TGDAAGVRYPELDVVGPPstpppdfdpEAWLESLDRLLSLKPER 210
MBLAC2-like_MBL-fold cd07712
uncharacterized human metallo-beta-lactamase domain-containing protein 2 and related proteins; ...
 7-172 1.27e-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: 56.48  E-value: 1.27e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 588480498   7 PVLEDNY---MYLVieELTREAVAVDVAVPKR-LLEIVgregVSLTA----VLTTHHHWDHARGN------------PEL 66
Cdd:cd07712    1 LFIEEDDrvnIYLL--RGRDRALLIDTGLGIGdLKEYV----RTLTDlpllVVATHGHFDHIGGLhefeevyvhpadAEI 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 588480498  67 ARLRPGLAVLGADERIFSL-----TRRLAHGEELRFGAIHVRCLLTPGHTAGHMSyfLWEddcPDPPALFSGDALSVAGC 141
Cdd:cd07712   75 LAAPDNFETLTWDAATYSVppagpTLPLRDGDVIDLGDRQLEVIHTPGHTPGSIA--LLD---RANRLLFSGDVVYDGPL 149

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 588480498 142 -----GSCLEgsaqQMYQSLAELGTLPPE-TKVFCGH 172
Cdd:cd07712  150 imdlpHSDLD----DYLASLEKLSKLPDEfDKVLPGH 182
Lactamase_B pfam00753
Metallo-beta-lactamase superfamily;
34-172 1.35e-09

Metallo-beta-lactamase superfamily;


Pssm-ID: 425851 [Multi-domain]  Cd Length: 196  Bit Score: 56.61  E-value: 1.35e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 588480498   34 KRLLEIVGREGVSLTAVLTTHHHWDHARGNPELARlRPGLAVLGADERIFSLTRRLAHGEELRFGA-------------- 99
Cdd:pfam00753  31 LLLLAALGLGPKDIDAVILTHGHFDHIGGLGELAE-ATDVPVIVVAEEARELLDEELGLAASRLGLpgppvvplppdvvl 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 588480498  100 -----IHVRCLL-----TPGHTAGHMSYFLweddcPDPPALFSGDALSVAGCGSCLE----------GSAQQMYQSLAEL 159
Cdd:pfam00753 110 eegdgILGGGLGllvthGPGHGPGHVVVYY-----GGGKVLFTGDLLFAGEIGRLDLplggllvlhpSSAESSLESLLKL 184

                         170
                  ....*....|...
gi 588480498  160 GTLPPEtKVFCGH 172
Cdd:pfam00753 185 AKLKAA-VIVPGH 196
metallo-hydrolase-like_MBL-fold cd16282
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 48-172 1.86e-08

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: 53.34  E-value: 1.86e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 588480498  48 TAVLTTHHHWDHARGN-------------------------PELARLRPGLAVLGADERIFSLTRRLAHGEELRFGAIHV 102
Cdd:cd16282   54 RYVVNTHYHGDHTLGNaafadagapiiahentreelaargeAYLELMRRLGGDAMAGTELVLPDRTFDDGLTLDLGGRTV 133

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 588480498 103 RCL-LTPGHTAGHMSYFLweddcPDPPALFSGDALSVAGCGSCLEGSAQQMYQSLAELGTLPPETkVFCGH 172
Cdd:cd16282  134 ELIhLGPAHTPGDLVVWL-----PEEGVLFAGDLVFNGRIPFLPDGSLAGWIAALDRLLALDATV-VVPGH 198
AHL_lactonase_MBL-fold cd07729
quorum-quenching N-acyl-homoserine lactonase, MBL-fold metallo-hydrolase domain; Acyl ...
 46-135 1.03e-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: 48.75  E-value: 1.03e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 588480498  46 SLTAVLTTHHHWDHArGN---------------------PELARLRPGLAVLGADERIFSLTRRLAHGE-ELrFGAIHVr 103
Cdd:cd07729   88 DIDYVILSHLHFDHA-GGldlfpnatiivqraeleyatgPDPLAAGYYEDVLALDDDLPGGRVRLVDGDyDL-FPGVTL- 164

                         90       100       110
                 ....*....|....*....|....*....|..
gi 588480498 104 cLLTPGHTAGHMSYFLwedDCPDPPALFSGDA 135
Cdd:cd07729  165 -IPTPGHTPGHQSVLV---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 3.41e-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: 47.16  E-value: 3.41e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 588480498  50 VLTTHHHWDHARGNPELARLRpGLAVLGADERIFSL-----------------------TRRLAHGEELRFGAIHVRCLL 106
Cdd:cd16313   64 ILSSHDHWDHAGGIAALQKLT-GAQVLASPATVAVLrsgsmgkddpqfggltpmppvasVRAVRDGEVVKLGPLAVTAHA 142

                         90
                 ....*....|.
gi 588480498 107 TPGHTAGHMSY 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 1.57e-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: 45.42  E-value: 1.57e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 588480498  26 VAVDVAVPK---RLLEIVGREGVSLTAV---LTTHHHWDHARGNPELARLR--------PGLAVL-----GADERIFSL- 85
Cdd:cd16290   34 ILIDGALPQsapQIEANIRALGFRLEDVkliLNSHAHFDHAGGIAALQRDSgatvaaspAGAAALrsggvDPDDPQAGAa 113

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 588480498  86 --------TRRLAHGEELRFGAIHVRCLLTPGHTAGHMSY 117
Cdd:cd16290  114 dpfppvakVRVVADGEVVKLGPLAVTAHATPGHTPGGTSW 153
metallo-hydrolase-like_MBL-fold cd07743
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 32-136 2.08e-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) 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: 41.36  E-value: 2.08e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 588480498  32 VPKRLLEIVGREGVSLTAVLTTHHHWDHARGNPELARlRPGLAVL-GADERIF------------------SLTRRLAHG 92
Cdd:cd07743   31 AGRKIRKILEELGWKLKAIINTHSHADHIGGNAYLQK-KTGCKVYaPKIEKAFienpllepsylggayppkELRNKFLMA 109

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 588480498  93 -----------EELRFGAIHVRCLLTPGHTAGHMSyFLWEDDcpdppALFSGDAL 136
Cdd:cd07743  110 kpskvddiieeGELELGGVGLEIIPLPGHSFGQIG-ILTPDG-----VLFAGDAL 158
Mbl1b-like_MBL-B3 cd16310
Caulobacter crescentus Mbl1b and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 50-113 3.66e-04

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: 40.90  E-value: 3.66e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 588480498  50 VLTTHHHWDHARGnpeLARL--------------RPGLAVlGA--DERIFSLT--------RRLAHGEELRFGAIHVRCL 105
Cdd:cd16310   64 IINTHAHYDHAGG---LAQLkadtgaklwasrgdRPALEA-GKhiGDNITQPApfpavkvdRILGDGEKIKLGDITLTAT 139


                 ....*...
gi 588480498 106 LTPGHTAG 113
Cdd:cd16310  140 LTPGHTKG 147
UlaG COG2220
L-ascorbate lactonase UlaG, metallo-beta-lactamase superfamily [Carbohydrate transport and ...
 47-135 6.23e-04

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


Pssm-ID: 441822 [Multi-domain]  Cd Length: 224  Bit Score: 40.29  E-value: 6.23e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 588480498  47 LTAVLTTHHHWDHArGNPELARLRPGLAV----LGADERI----FSLTRRLAHGEELRFGAIHVRCllTPG-HTAGH--- 114
Cdd:COG2220   49 IDAVLVTHDHYDHL-DDATLRALKRTGATvvapLGVAAWLrawgFPRVTELDWGESVELGGLTVTA--VPArHSSGRpdr 125

                         90       100
                 ....*....|....*....|....*.
gi 588480498 115 -----MSYFLwedDCPDPPALFSGDA 135
Cdd:COG2220  126 ngglwVGFVI---ETDGKTIYHAGDT 148
metallo-hydrolase-like_MBL-fold cd16280
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 50-118 6.43e-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: 293838 [Multi-domain]  Cd Length: 251  Bit Score: 40.26  E-value: 6.43e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 588480498  50 VLTTHHHWDHARG--------NP---------ELARLRPGLavlGADERIFSLTRR---LAHGEELRFGAIHVRCLLTPG 109
Cdd:cd16280   65 ILITHGHGDHYGGaaylkdlyGAkvvmseadwDMMEEPPEE---GDNPRWGPPPERdivIKDGDTLTLGDTTITVYLTPG 141


                 ....*....
gi 588480498 110 HTAGHMSYF 118
Cdd:cd16280  142 HTPGTLSLI 150
MBLAC1-like_MBL-fold cd07711
uncharacterized human metallo-beta-lactamase domain-containing protein 1 and related proteins; ...
 34-116 7.64e-04

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: 39.49  E-value: 7.64e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 588480498  34 KRLLEIVGREGVSL---TAVLTTHHHWDHARGNP--ELARLrpglaVLGADERIFSLTR-RLAHGEELRFGAiHVRCLLT 107
Cdd:cd07711   45 DLLLKALAEHGLSPediDYVVLTHGHPDHIGNLNlfPNATV-----IVGWDICGDSYDDhSLEEGDGYEIDE-NVEVIPT 118


                 ....*....
gi 588480498 108 PGHTAGHMS 116
Cdd:cd07711  119 PGHTPEDVS 127
GOB1-like_MBL-B3 cd16308
Elizabethkingia meningoseptica GOB-1 and related metallo-beta-lactamases, subclass B3; ...
 14-119 7.77e-04

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


Pssm-ID: 293866 [Multi-domain]  Cd Length: 254  Bit Score: 40.15  E-value: 7.77e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 588480498  14 MYLVIEE----LTREAVAVDVAVPKRLLEIVGREGVSLTAVLTTHHHWDHARGNPELAR---------------LRPGLA 74
Cdd:cd16308   24 CYLIVTPkgniLINTGLAESVPLIKKNIQALGFKFKDIKILLTTQAHYDHVGAMAAIKQqtgakmmvdekdakvLADGGK 103

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 588480498  75 ---VLGADERIF---SLTRRLAHGEELRFGAIHVRCLLTPGHTAGHMSYFL 119
Cdd:cd16308  104 sdyEMGGYGSTFapvKADKLLHDGDTIKLGGTKLTLLHHPGHTKGSCSFLF 154
metallo-hydrolase-like_MBL-fold cd16277
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 48-136 1.36e-03

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


Pssm-ID: 293835 [Multi-domain]  Cd Length: 222  Bit Score: 39.04  E-value: 1.36e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 588480498  48 TAVLTTHHHWDH------------------AR---GNPELARLRPGLAVLGADERIF--SLTRRLAHGEELRFGAIH--- 101
Cdd:cd16277   65 DYVLCTHLHVDHvgwntrlvdgrwvptfpnARylfSRAEYDHWSSPDAGGPPNRGVFedSVLPVIEAGLADLVDDDHeil 144

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 588480498 102 --VRCLLTPGHTAGHMSYFLwedDCPDPPALFSGDAL 136
Cdd:cd16277  145 dgIRLEPTPGHTPGHVSVEL---ESGGERALFTGDVM 178
BJP-1_FEZ-1-like_MBL-B3 cd16288
BJP-1, FEZ-1, GOB-1, Mbl1b and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 50-117 1.47e-03

BJP-1, FEZ-1, GOB-1, Mbl1b and related metallo-beta-lactamases, subclass B3; MBL-fold metallo-hydrolase domain; This subgroup of B3 subclass MBLs includes Bradyrhizobium diazoefficiens BJP-1, Fluoribacter gormanii FEZ-1, Elizabethkingia meningoseptica (Chryseobacterium meningosepticum) GOB-1, Caulobacter crescentus Mbl1b. MBLs (class B of the Ambler beta-lactamase classification) are a diverse group of metallo-enzymes that are capable of catalyzing the hydrolysis of a wide range of beta-lactam antibiotics. MBLs have been divided into three subclasses B1, B2 and B3, based on sequence/structural relationships and substrates, with the B1 and B2 MBLs being most closely related to each other. Subclass B3 enzymes are most active with two zinc ions bound in the active site, and have a broad-spectrum substrate profile. These B3 enzymes have a modified Zn2/DCH site (Asp-His-His).


Pssm-ID: 293846 [Multi-domain]  Cd Length: 254  Bit Score: 39.23  E-value: 1.47e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 588480498  50 VLTTHHHWDHARGNPELARL-----------RPGLA-------VLGADERIFS---LTRRLAHGEELRFGAIHVRCLLTP 108
Cdd:cd16288   64 LLNSHAHLDHAGGLAALKKLtgaklmasaedAALLAsggksdfHYGDDSLAFPpvkVDRVLKDGDRVTLGGTTLTAHLTP 143


                 ....*....
gi 588480498 109 GHTAGHMSY 117
Cdd:cd16288  144 GHTRGCTTW 152
YycJ-like_MBL-fold cd07733
uncharacterized subgroup which includes Bacillus subtilis YycJ and related proteins; MBL-fold ...
 12-68 2.05e-03

uncharacterized subgroup which includes Bacillus subtilis YycJ and related proteins; MBL-fold metallo hydrolase domain; Includes the uncharacterized Bacillus subtilis YycJ 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: 293819 [Multi-domain]  Cd Length: 151  Bit Score: 38.01  E-value: 2.05e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 588480498  12 NYMYLvieELTREAVAVDVAVPKR----LLEIVGREGVSLTAVLTTHHHWDHARGNPELAR 68
Cdd:cd07733   10 NCTYL---ETEDGKLLIDAGLSGRkitgRLAEIGRDPEDIDAILVTHEHADHIKGLGVLAR 67
PhnP COG1235
Phosphoribosyl 1,2-cyclic phosphate phosphodiesterase [Inorganic ion transport and metabolism]; ...
 34-111 9.38e-03

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


Pssm-ID: 440848 [Multi-domain]  Cd Length: 259  Bit Score: 36.80  E-value: 9.38e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 588480498  34 KRLLEIVGREGVSLTAVLTTHHHWDHARGNPELAR--LRPGLAVLGADERIFSLTRRLAHGEELRFGAIHVRClLTPGHT 111
Cdd:COG1235   56 REQLLRLGLDPSKIDAILLTHEHADHIAGLDDLRPryGPNPIPVYATPGTLEALERRFPYLFAPYPGKLEFHE-IEPGEP 134
 
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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