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Conserved domains on  [gi|1394533491|ref|NP_001350841|]
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hydroxyacylglutathione hydrolase, mitochondrial isoform 4 precursor [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
 49-275 3.38e-119

hydroxyacylglutathione hydrolase


The actual alignment was detected with superfamily member PLN02469:

Pssm-ID: 178088 [Multi-domain]  Cd Length: 258  Bit Score: 342.90  E-value: 3.38e-119
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533491  49 MKVEVLPALTDNYMYLVIDDETKEAAIVDPVQPQKVVDAARKHGVKLTTVLTTHHHWDHAGGNEKLVKLESGLKVYGGD- 127
Cdd:PLN02469    1 MKIIPVPCLEDNYAYLIIDESTKDAAVVDPVDPEKVLQAAHEHGAKIKLVLTTHHHWDHAGGNEKIKKLVPGIKVYGGSl 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533491 128 DRIGALTHKITHLSTLQVGS-LNVKCLATPCHTSGHICYFV-SKPGgsEPPAVFTGDTLFVAGCGKFYEGTADEMCKALL 205
Cdd:PLN02469   81 DNVKGCTHPVENGDKLSLGKdVNILALHTPCHTKGHISYYVtGKEG--EDPAVFTGDTLFIAGCGKFFEGTAEQMYQSLC 158

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533491 206 EVLGRLPPDTRVYCGHEYTINNLKFARHVEPGNAAIREKLAWAKEKYSIGEPTVPSTLAEEFTYNPFMRV 275
Cdd:PLN02469  159 VTLGSLPKPTQVYCGHEYTVKNLKFALTVEPDNEKLKQKLEWAEKQRQAGLPTVPSTIEEELETNPFMRV 228
 
Name Accession Description Interval E-value
PLN02469 PLN02469
hydroxyacylglutathione hydrolase
 49-275 3.38e-119

hydroxyacylglutathione hydrolase


Pssm-ID: 178088 [Multi-domain]  Cd Length: 258  Bit Score: 342.90  E-value: 3.38e-119
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533491  49 MKVEVLPALTDNYMYLVIDDETKEAAIVDPVQPQKVVDAARKHGVKLTTVLTTHHHWDHAGGNEKLVKLESGLKVYGGD- 127
Cdd:PLN02469    1 MKIIPVPCLEDNYAYLIIDESTKDAAVVDPVDPEKVLQAAHEHGAKIKLVLTTHHHWDHAGGNEKIKKLVPGIKVYGGSl 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533491 128 DRIGALTHKITHLSTLQVGS-LNVKCLATPCHTSGHICYFV-SKPGgsEPPAVFTGDTLFVAGCGKFYEGTADEMCKALL 205
Cdd:PLN02469   81 DNVKGCTHPVENGDKLSLGKdVNILALHTPCHTKGHISYYVtGKEG--EDPAVFTGDTLFIAGCGKFFEGTAEQMYQSLC 158

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533491 206 EVLGRLPPDTRVYCGHEYTINNLKFARHVEPGNAAIREKLAWAKEKYSIGEPTVPSTLAEEFTYNPFMRV 275
Cdd:PLN02469  159 VTLGSLPKPTQVYCGHEYTVKNLKFALTVEPDNEKLKQKLEWAEKQRQAGLPTVPSTIEEELETNPFMRV 228
hydroxyacylglutathione_hydrolase_MBL-fold cd07723
hydroxyacylglutathione hydrolase, MBL-fold metallo-hydrolase domain; hydroxyacylglutathione ...
 52-221 9.15e-93

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: 272.03  E-value: 9.15e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533491  52 EVLPALTDNYMYLVIDDETKEAAIVDPVQPQKVVDAARKHGVKLTTVLTTHHHWDHAGGNEKLVKLESGLKVYGG-DDRI 130
Cdd:cd07723     1 VPIPALSDNYIYLIVDEATGEAAVVDPGEAEPVLAALEKNGLTLTAILTTHHHWDHTGGNAELKALFPDAPVYGPaEDRI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533491 131 GALTHKITHLSTLQVGSLNVKCLATPCHTSGHICYFVskpggSEPPAVFTGDTLFVAGCGKFYEGTADEMCKALLEVLGr 210
Cdd:cd07723    81 PGLDHPVKDGDEIKLGGLEVKVLHTPGHTLGHICYYV-----PDEPALFTGDTLFSGGCGRFFEGTAEQMYASLQKLLA- 154

                         170
                  ....*....|.
gi 1394533491 211 LPPDTRVYCGH 221
Cdd:cd07723   155 LPDDTLVYCGH 165
GSH_gloB TIGR03413
hydroxyacylglutathione hydrolase; Members of this protein family are hydroxyacylglutathione ...
 54-274 3.25e-92

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: 274.03  E-value: 3.25e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533491  54 LPALTDNYMYLVIDDEtKEAAIVDPVQPQKVVDAARKHGVKLTTVLTTHHHWDHAGGNEKLVKlESGLKVYGG-DDRIGA 132
Cdd:TIGR03413   4 IPALSDNYIWLLHDPD-GQAAVVDPGEAEPVLDALEARGLTLTAILLTHHHHDHVGGVAELLE-AFPAPVYGPaEERIPG 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533491 133 LTHKITHLSTLQVGSLNVKCLATPCHTSGHICYFvskpgGSEPPAVFTGDTLFVAGCGKFYEGTADEMCKALLEvLGRLP 212
Cdd:TIGR03413  82 ITHPVKDGDTVTLGGLEFEVLAVPGHTLGHIAYY-----LPDSPALFCGDTLFSAGCGRLFEGTPEQMYDSLQR-LAALP 155

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1394533491 213 PDTRVYCGHEYTINNLKFARHVEPGNAAIREKLAWAKEKYSIGEPTVPSTLAEEFTYNPFMR 274
Cdd:TIGR03413 156 DDTLVYCAHEYTLSNLRFALTVEPDNPALQERLKEVEALRAQGQPTLPSTLGLERATNPFLR 217
GloB COG0491
Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General ...
 51-244 2.00e-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: 122.11  E-value: 2.00e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533491  51 VEVLPALTDNYMYLVIDDEtkEAAIVDP----VQPQKVVDAARKHGVKLTTVLTTHHHWDHAGGNEKLVKlESGLKVYGG 126
Cdd:COG0491     6 GGTPGAGLGVNSYLIVGGD--GAVLIDTglgpADAEALLAALAALGLDIKAVLLTHLHPDHVGGLAALAE-AFGAPVYAH 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533491 127 DDRIGALTHK----------------ITHLSTLQVGSLNVKCLATPCHTSGHICYFVSKPGgseppAVFTGDTLFVAGCG 190
Cdd:COG0491    83 AAEAEALEAPaagalfgrepvppdrtLEDGDTLELGGPGLEVIHTPGHTPGHVSFYVPDEK-----VLFTGDALFSGGVG 157

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1394533491 191 K--FYEGTADEMCKAlLEVLGRLPPDtRVYCGHEYTINNLKFARHVEpGNAAIREK 244
Cdd:COG0491   158 RpdLPDGDLAQWLAS-LERLLALPPD-LVIPGHGPPTTAEAIDYLEE-LLAALGER 210
HAGH_C pfam16123
Hydroxyacylglutathione hydrolase C-terminus; This domain is found at the C-terminus of ...
 222-275 1.83e-27

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: 102.13  E-value: 1.83e-27
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1394533491 222 EYTINNLKFARHVEPGNAAIREKLAWAKEKYSIGEPTVPSTLAEEFTYNPFMRV 275
Cdd:pfam16123   1 EYTLSNLKFALSVEPDNEALQKRLAWVEALRAAGEPTVPSTLGDEKATNPFLRV 54
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 61-221 5.31e-27

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: 103.79  E-value: 5.31e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533491   61 YMYLVIDDetKEAAIVDPV--QPQKVVDAARKHGV-KLTTVLTTHHHWDHAGGNEKLVKlESGLKVYG------------ 125
Cdd:smart00849   1 NSYLVRDD--GGAILIDTGpgEAEDLLAELKKLGPkKIDAIILTHGHPDHIGGLPELLE-APGAPVYApegtaellkdll 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533491  126 -------GDDRIGALTHKITHLSTLQVGSLNVKCLATPCHTSGHICYFVskpggSEPPAVFTGDTLFVAGCG-KFYEGTA 197
Cdd:smart00849  78 allgelgAEAEPAPPDRTLKDGDELDLGGGELEVIHTPGHTPGSIVLYL-----PEGKILFTGDLLFAGGDGrTLVDGGD 152

                          170       180
                   ....*....|....*....|....*
gi 1394533491  198 DEMCKALLEVLGRL-PPDTRVYCGH 221
Cdd:smart00849 153 AAASDALESLLKLLkLLPKLVVPGH 177
 
Name Accession Description Interval E-value
PLN02469 PLN02469
hydroxyacylglutathione hydrolase
 49-275 3.38e-119

hydroxyacylglutathione hydrolase


Pssm-ID: 178088 [Multi-domain]  Cd Length: 258  Bit Score: 342.90  E-value: 3.38e-119
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533491  49 MKVEVLPALTDNYMYLVIDDETKEAAIVDPVQPQKVVDAARKHGVKLTTVLTTHHHWDHAGGNEKLVKLESGLKVYGGD- 127
Cdd:PLN02469    1 MKIIPVPCLEDNYAYLIIDESTKDAAVVDPVDPEKVLQAAHEHGAKIKLVLTTHHHWDHAGGNEKIKKLVPGIKVYGGSl 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533491 128 DRIGALTHKITHLSTLQVGS-LNVKCLATPCHTSGHICYFV-SKPGgsEPPAVFTGDTLFVAGCGKFYEGTADEMCKALL 205
Cdd:PLN02469   81 DNVKGCTHPVENGDKLSLGKdVNILALHTPCHTKGHISYYVtGKEG--EDPAVFTGDTLFIAGCGKFFEGTAEQMYQSLC 158

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533491 206 EVLGRLPPDTRVYCGHEYTINNLKFARHVEPGNAAIREKLAWAKEKYSIGEPTVPSTLAEEFTYNPFMRV 275
Cdd:PLN02469  159 VTLGSLPKPTQVYCGHEYTVKNLKFALTVEPDNEKLKQKLEWAEKQRQAGLPTVPSTIEEELETNPFMRV 228
hydroxyacylglutathione_hydrolase_MBL-fold cd07723
hydroxyacylglutathione hydrolase, MBL-fold metallo-hydrolase domain; hydroxyacylglutathione ...
 52-221 9.15e-93

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: 272.03  E-value: 9.15e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533491  52 EVLPALTDNYMYLVIDDETKEAAIVDPVQPQKVVDAARKHGVKLTTVLTTHHHWDHAGGNEKLVKLESGLKVYGG-DDRI 130
Cdd:cd07723     1 VPIPALSDNYIYLIVDEATGEAAVVDPGEAEPVLAALEKNGLTLTAILTTHHHWDHTGGNAELKALFPDAPVYGPaEDRI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533491 131 GALTHKITHLSTLQVGSLNVKCLATPCHTSGHICYFVskpggSEPPAVFTGDTLFVAGCGKFYEGTADEMCKALLEVLGr 210
Cdd:cd07723    81 PGLDHPVKDGDEIKLGGLEVKVLHTPGHTLGHICYYV-----PDEPALFTGDTLFSGGCGRFFEGTAEQMYASLQKLLA- 154

                         170
                  ....*....|.
gi 1394533491 211 LPPDTRVYCGH 221
Cdd:cd07723   155 LPDDTLVYCGH 165
GSH_gloB TIGR03413
hydroxyacylglutathione hydrolase; Members of this protein family are hydroxyacylglutathione ...
 54-274 3.25e-92

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: 274.03  E-value: 3.25e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533491  54 LPALTDNYMYLVIDDEtKEAAIVDPVQPQKVVDAARKHGVKLTTVLTTHHHWDHAGGNEKLVKlESGLKVYGG-DDRIGA 132
Cdd:TIGR03413   4 IPALSDNYIWLLHDPD-GQAAVVDPGEAEPVLDALEARGLTLTAILLTHHHHDHVGGVAELLE-AFPAPVYGPaEERIPG 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533491 133 LTHKITHLSTLQVGSLNVKCLATPCHTSGHICYFvskpgGSEPPAVFTGDTLFVAGCGKFYEGTADEMCKALLEvLGRLP 212
Cdd:TIGR03413  82 ITHPVKDGDTVTLGGLEFEVLAVPGHTLGHIAYY-----LPDSPALFCGDTLFSAGCGRLFEGTPEQMYDSLQR-LAALP 155

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1394533491 213 PDTRVYCGHEYTINNLKFARHVEPGNAAIREKLAWAKEKYSIGEPTVPSTLAEEFTYNPFMR 274
Cdd:TIGR03413 156 DDTLVYCAHEYTLSNLRFALTVEPDNPALQERLKEVEALRAQGQPTLPSTLGLERATNPFLR 217
PLN02398 PLN02398
hydroxyacylglutathione hydrolase
 23-274 6.47e-64

hydroxyacylglutathione hydrolase


Pssm-ID: 215223 [Multi-domain]  Cd Length: 329  Bit Score: 204.31  E-value: 6.47e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533491  23 RGLGPAL-LGVFChtdlrkNLTVDEGTMKVEVLPALTDNYMYLVIDDETKEAAIVDPVQPQKVVDAARKHGVKLTTVLTT 101
Cdd:PLN02398   55 RGAGRTLkVAQFC------SVSNVSSSLQIELVPCLKDNYAYLLHDEDTGTVGVVDPSEAVPVIDALSRKNRNLTYILNT 128

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533491 102 HHHWDHAGGNEKLvKLESGLKVYGGD---DRIGALTHKITHLSTLQVGSLNVKCLATPCHTSGHICYFVskPGGSeppAV 178
Cdd:PLN02398  129 HHHYDHTGGNLEL-KARYGAKVIGSAvdkDRIPGIDIVLKDGDKWMFAGHEVLVMETPGHTRGHISFYF--PGSG---AI 202

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533491 179 FTGDTLFVAGCGKFYEGTADEMCKALLEVLGrLPPDTRVYCGHEYTINNLKFARHVEPGNAAIREKLAWAKEKYSIGEPT 258
Cdd:PLN02398  203 FTGDTLFSLSCGKLFEGTPEQMLSSLQKIIS-LPDDTNIYCGHEYTLSNSKFALSIEPNNEVLQSYAAHVAHLRSKGLPT 281

                         250
                  ....*....|....*.
gi 1394533491 259 VPSTLAEEFTYNPFMR 274
Cdd:PLN02398  282 IPTTVKMEKACNPFLR 297
PRK10241 PRK10241
hydroxyacylglutathione hydrolase; Provisional
 49-275 1.67e-46

hydroxyacylglutathione hydrolase; Provisional


Pssm-ID: 182327 [Multi-domain]  Cd Length: 251  Bit Score: 157.29  E-value: 1.67e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533491  49 MKVEVLPALTDNYMYLVIDDETKeAAIVDPVQPQKVVDAARKHGVKLTTVLTTHHHWDHAGGNEKLVKLESGLKVYG-GD 127
Cdd:PRK10241    1 MNLNSIPAFDDNYIWVLNDEAGR-CLIVDPGEAEPVLNAIAENNWQPEAIFLTHHHHDHVGGVKELVEKFPQIVVYGpQE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533491 128 DRIGALTHKITHLSTLQVGSLNVKCLATPCHTSGHICYFVSkpggsepPAVFTGDTLFVAGCGKFYEGTADEMCKALLEV 207
Cdd:PRK10241   80 TQDKGTTQVVKDGETAFVLGHEFSVFATPGHTLGHICYFSK-------PYLFCGDTLFSGGCGRLFEGTASQMYQSLKKI 152

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1394533491 208 lGRLPPDTRVYCGHEYTINNLKFARHVEPGNAAIREKLAWAKEKYSIGEPTVPSTLAEEFTYNPFMRV 275
Cdd:PRK10241  153 -NALPDDTLICCAHEYTLSNMKFALSILPHDLSINDYYRKVKELRAKNQITLPVILKNERQINLFLRT 219
BaeB-like_MBL-fold cd16275
Bacillus amyloliquefaciens BaeB and related proteins; MBL-fold metallo hydrolase domain; ...
 59-221 4.09e-41

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: 140.75  E-value: 4.09e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533491  59 DNYMYLVIDDETKEAAIVDPV-QPQKVVDAARKHGVKLTTVLTTHHHWDHAGGNEKLVKlESGLKVY-------GGDDRI 130
Cdd:cd16275    11 INYSYIIIDKATREAAVVDPAwDIEKILAKLNELGLTLTGILLTHSHFDHVNLVEPLLA-KYDAPVYmskeeidYYGFRC 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533491 131 GALtHKITHLSTLQVGSLNVKCLATPCHTSGHICYFVskpGGSeppaVFTGDTLFVAGCG--KFYEGTADEMCKAlLEVL 208
Cdd:cd16275    90 PNL-IPLEDGDTIKIGDTEITCLLTPGHTPGSMCYLL---GDS----LFTGDTLFIEGCGrcDLPGGDPEEMYES-LQRL 160

                         170
                  ....*....|....
gi 1394533491 209 GRL-PPDTRVYCGH 221
Cdd:cd16275   161 KKLpPPNTRVYPGH 174
POD-like_MBL-fold cd07724
ETHE1 (PDO type I), persulfide dioxygenase A (PDOA, PDO type II) and related proteins; ...
 63-223 4.52e-36

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: 127.52  E-value: 4.52e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533491  63 YLVIDDETKEAAIVDPV--QPQKVVDAARKHGVKLTTVLTTHHHWDHAGGNEKLvKLESGLKVYGGDDRIGALTHkiTHL 140
Cdd:cd07724    15 YLVGDPETGEAAVIDPVrdSVDRYLDLAAELGLKITYVLETHVHADHVSGAREL-AERTGAPIVIGEGAPASFFD--RLL 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533491 141 S---TLQVGSLNVKCLATPCHTSGHICYFVSKPGgseppAVFTGDTLFVAGCG-----KFYEGTADEMCKALLEVLGRLP 212
Cdd:cd07724    92 KdgdVLELGNLTLEVLHTPGHTPESVSYLVGDPD-----AVFTGDTLFVGDVGrpdlpGEAEGLARQLYDSLQRKLLLLP 166

                         170
                  ....*....|.
gi 1394533491 213 PDTRVYCGHEY 223
Cdd:cd07724   167 DETLVYPGHDY 177
metallo-hydrolase-like_MBL-fold cd06262
mainly hydrolytic enzymes and related proteins which carry out various biological functions; ...
 65-221 4.13e-34

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: 122.78  E-value: 4.13e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533491  65 VIDDETKEAAIVDPVQP--QKVVDAARKHGVKLTTVLTTHHHWDHAGGNEKLVKlESGLKVY------------------ 124
Cdd:cd06262    14 LVSDEEGEAILIDPGAGalEKILEAIEELGLKIKAILLTHGHFDHIGGLAELKE-APGAPVYiheadaelledpelnlaf 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533491 125 --GGDDRIGALTHKITHLSTLQVGSLNVKCLATPCHTSGHICYFVSKPGgseppAVFTGDTLFVAGCGK--FYEGTADEM 200
Cdd:cd06262    93 fgGGPLPPPEPDILLEDGDTIELGGLELEVIHTPGHTPGSVCFYIEEEG-----VLFTGDTLFAGSIGRtdLPGGDPEQL 167

                         170       180
                  ....*....|....*....|.
gi 1394533491 201 CKALLEVLGRLPPDTRVYCGH 221
Cdd:cd06262   168 IESIKKLLLLLPDDTVVYPGH 188
GloB COG0491
Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General ...
 51-244 2.00e-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: 122.11  E-value: 2.00e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533491  51 VEVLPALTDNYMYLVIDDEtkEAAIVDP----VQPQKVVDAARKHGVKLTTVLTTHHHWDHAGGNEKLVKlESGLKVYGG 126
Cdd:COG0491     6 GGTPGAGLGVNSYLIVGGD--GAVLIDTglgpADAEALLAALAALGLDIKAVLLTHLHPDHVGGLAALAE-AFGAPVYAH 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533491 127 DDRIGALTHK----------------ITHLSTLQVGSLNVKCLATPCHTSGHICYFVSKPGgseppAVFTGDTLFVAGCG 190
Cdd:COG0491    83 AAEAEALEAPaagalfgrepvppdrtLEDGDTLELGGPGLEVIHTPGHTPGHVSFYVPDEK-----VLFTGDALFSGGVG 157

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1394533491 191 K--FYEGTADEMCKAlLEVLGRLPPDtRVYCGHEYTINNLKFARHVEpGNAAIREK 244
Cdd:COG0491   158 RpdLPDGDLAQWLAS-LERLLALPPD-LVIPGHGPPTTAEAIDYLEE-LLAALGER 210
HAGH_C pfam16123
Hydroxyacylglutathione hydrolase C-terminus; This domain is found at the C-terminus of ...
 222-275 1.83e-27

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: 102.13  E-value: 1.83e-27
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1394533491 222 EYTINNLKFARHVEPGNAAIREKLAWAKEKYSIGEPTVPSTLAEEFTYNPFMRV 275
Cdd:pfam16123   1 EYTLSNLKFALSVEPDNEALQKRLAWVEALRAAGEPTVPSTLGDEKATNPFLRV 54
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 61-221 5.31e-27

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: 103.79  E-value: 5.31e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533491   61 YMYLVIDDetKEAAIVDPV--QPQKVVDAARKHGV-KLTTVLTTHHHWDHAGGNEKLVKlESGLKVYG------------ 125
Cdd:smart00849   1 NSYLVRDD--GGAILIDTGpgEAEDLLAELKKLGPkKIDAIILTHGHPDHIGGLPELLE-APGAPVYApegtaellkdll 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533491  126 -------GDDRIGALTHKITHLSTLQVGSLNVKCLATPCHTSGHICYFVskpggSEPPAVFTGDTLFVAGCG-KFYEGTA 197
Cdd:smart00849  78 allgelgAEAEPAPPDRTLKDGDELDLGGGELEVIHTPGHTPGSIVLYL-----PEGKILFTGDLLFAGGDGrTLVDGGD 152

                          170       180
                   ....*....|....*....|....*
gi 1394533491  198 DEMCKALLEVLGRL-PPDTRVYCGH 221
Cdd:smart00849 153 AAASDALESLLKLLkLLPKLVVPGH 177
TTHA1623-like_MBL-fold cd16322
uncharacterized Thermus thermophilus TTHA1623 and related proteins; MBL-fold metallo hydrolase ...
 52-221 6.06e-23

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: 93.95  E-value: 6.06e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533491  52 EVLPALTDNyMYLVIDDETKEAAIVDP-VQPQKVVDAARKHGVKLTTVLTTHHHWDHAGGNEKLVKL--------ESGLK 122
Cdd:cd16322     4 FTLGPLQEN-TYLVADEGGGEAVLVDPgDESEKLLARFGTTGLTLLYILLTHAHFDHVGGVADLRRHpgapvylhPDDLP 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533491 123 VYGGDDRIGAL-----------THKITHLSTLQVGSLNVKCLATPCHTSGHICYFVSKPGgseppAVFTGDTLFVAGCGK 191
Cdd:cd16322    83 LYEAADLGAKAfglgieplpppDRLLEDGQTLTLGGLEFKVLHTPGHSPGHVCFYVEEEG-----LLFSGDLLFQGSIGR 157

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1394533491 192 F-YEGTADEMCKALLEVLGRLPPDTRVYCGH 221
Cdd:cd16322   158 TdLPGGDPKAMAASLRRLLTLPDETRVFPGH 188
YcbL-like_MBL-fold cd07737
Salmonella enterica serovar typhimurium YcbL and related proteins; MBL-fold metallo hydrolase ...
 63-221 1.94e-22

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: 92.23  E-value: 1.94e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533491  63 YLVIDDETKEAAIVDP-VQPQKVVDAARKHGVKLTTVLTTHHHWDHAGGNEKLVKlESGLKVYGG--DDR--IGAL---- 133
Cdd:cd07737    14 SLIWCEETKEAAVIDPgGDADKILQAIEDLGLTLKKILLTHGHLDHVGGAAELAE-HYGVPIIGPhkEDKflLENLpeqs 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533491 134 -------------THKITHLSTLQVGSLNVKCLATPCHTSGHICYFvskpggsEPPA--VFTGDTLFVAGCGK--FYEGT 196
Cdd:cd07737    93 qmfgfppaeaftpDRWLEEGDTVTVGNLTLEVLHCPGHTPGHVVFF-------NRESklAIVGDVLFKGSIGRtdFPGGN 165

                         170       180
                  ....*....|....*....|....*
gi 1394533491 197 ADEMCKALLEVLGRLPPDTRVYCGH 221
Cdd:cd07737   166 HAQLIASIKEKLLPLGDDVTFIPGH 190
PLN02962 PLN02962
hydroxyacylglutathione hydrolase
 61-223 7.85e-17

hydroxyacylglutathione hydrolase


Pssm-ID: 178547 [Multi-domain]  Cd Length: 251  Bit Score: 78.30  E-value: 7.85e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533491  61 YMYLVID--DETKEAAIVDPVQpqKVVDA----ARKHGVKLTTVLTTHHHWDHAGGNEKLVKLESGLKVYGGDDRIGALT 134
Cdd:PLN02962   24 YTYLLADvsHPDKPALLIDPVD--KTVDRdlslVKELGLKLIYAMNTHVHADHVTGTGLLKTKLPGVKSIISKASGSKAD 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533491 135 HKITHLSTLQVGSLNVKCLATPCHTSGHICYFVSK-PGGSEPPAVFTGDTLFVAGCGK--FYEGTADEMCKALLEVLGRL 211
Cdd:PLN02962  102 LFVEPGDKIYFGDLYLEVRATPGHTAGCVTYVTGEgPDQPQPRMAFTGDALLIRGCGRtdFQGGSSDQLYKSVHSQIFTL 181

                         170
                  ....*....|..
gi 1394533491 212 PPDTRVYCGHEY 223
Cdd:PLN02962  182 PKDTLIYPAHDY 193
yflN-like_MBL-fold cd07721
uncharacterized subgroup which includes Bacillus subtilis yflN; MBL-fold metallo hydrolase ...
 50-221 6.36e-14

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


Pssm-ID: 293807 [Multi-domain]  Cd Length: 202  Bit Score: 69.17  E-value: 6.36e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533491  50 KVEVLPALTDNYMYLVIDDEtkEAAIVD---PVQPQKVVDAARKHGVK---LTTVLTTHHHWDHAGGNEKLVKlESGLKV 123
Cdd:cd07721     1 GVYQLPLLPPVNAYLIEDDD--GLTLIDtglPGSAKRILKALRELGLSpkdIRRILLTHGHIDHIGSLAALKE-APGAPV 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533491 124 YGGDDRIGALTHKITHLSTLQVGSL----------------------------NVKCLATPCHTSGHICYFVSKPGgsep 175
Cdd:cd07721    78 YAHEREAPYLEGEKPYPPPVRLGLLgllspllpvkpvpvdrtledgdtldlagGLRVIHTPGHTPGHISLYLEEDG---- 153

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1394533491 176 pAVFTGDTLFVAG---CGKFYEGTAD-EMCKALLEVLGRLPPDTrVYCGH 221
Cdd:cd07721   154 -VLIAGDALVTVGgelVPPPPPFTWDmEEALESLRKLAELDPEV-LAPGH 201
metallo-hydrolase-like_MBL-fold cd16278
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 63-183 2.23e-12

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: 64.43  E-value: 2.23e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533491  63 YLVIDDEtkEAAIVDPvQP------QKVVDAARkhGVKLTTVLTTHHHWDHAGGNEKLVKLeSGLKVYGGDDRIGAL--- 133
Cdd:cd16278    21 YLLGAPD--GVVVIDP-GPddpahlDALLAALG--GGRVSAILVTHTHRDHSPGAARLAER-TGAPVRAFGPHRAGGqdt 94

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1394533491 134 ----THKITHLSTLQVGSLNVKCLATPCHTSGHICYFVSKPGgseppAVFTGDT 183
Cdd:cd16278    95 dfapDRPLADGEVIEGGGLRLTVLHTPGHTSDHLCFALEDEG-----ALFTGDH 143
LACTB2-like_MBL-fold cd07722
uncharacterized subgroup which includes human lactamase beta 2 and related proteins; MBL-fold ...
 95-221 1.20e-11

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: 1.20e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533491  95 LTTVLTTHHHWDHAGGNEKLVKL--ESGLKVY-----GGDDRIGALTHKITHLS---TLQVGSLNVKCLATPCHTSGHIC 164
Cdd:cd07722    57 ISDILLTHWHHDHVGGLPDVLDLlrGPSPRVYkfprpEEDEDPDEDGGDIHDLQdgqVFKVEGATLRVIHTPGHTTDHVC 136

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1394533491 165 YFVskpggSEPPAVFTGDTlfVAGcgkfyEGTA------DEMckALLEVLGRLPPdTRVYCGH 221
Cdd:cd07722   137 FLL-----EEENALFTGDC--VLG-----HGTAvfedlaAYM--ASLKKLLSLGP-GRIYPGH 184
TTHA1429-like_MBL-fold cd07725
uncharacterized Thermus thermophilus TTHA1429 and related proteins; MBL-fold metallo hydrolase ...
 96-229 1.92e-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: 61.93  E-value: 1.92e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533491  96 TTVLTTHHHWDHAGGNEKLVKlESGLKVYGGDDRIgalthkITHLSTLQVGSLNVKCLATPCHTSGHICYFVSKPGGsep 175
Cdd:cd07725    57 DRVLLTHHHPDHIGLAGKLQE-KSGATVYILDVTP------VKDGDKIDLGGLRLKVIETPGHTPGHIVLYDEDRRE--- 126

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1394533491 176 paVFTGDTL--FVAGCGKFYEGTADEMCKALLEVLGRLP--PDTRVYCGHEYTINNLK 229
Cdd:cd07725   127 --LFVGDAVlpKITPNVSLWAVRVEDPLGAYLESLDKLEklDVDLAYPGHGGPIKDPK 182
ST1585-like_MBL-fold cd07726
uncharacterized subgroup which includes Sulfolobus tokodaii ST1585 protein; MBL-fold metallo ...
 63-221 2.03e-11

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: 62.12  E-value: 2.03e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533491  63 YLVIDDetKEAAIVDP---VQPQKVVDAARKHGV---KLTTVLTTHHHWDHAGG---------NEKLV------------ 115
Cdd:cd07726    19 YLLDGE--GRPALIDTgpsSSVPRLLAALEALGIapeDVDYIILTHIHLDHAGGagllaealpNAKVYvhprgarhlidp 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533491 116 -KL-ESGLKVYGGD-------------DRIGALTHKithlSTLQVGSLNVKCLATPCHTSGHICYFVSKPGGseppaVFT 180
Cdd:cd07726    97 sKLwASARAVYGDEadrlggeilpvpeERVIVLEDG----ETLDLGGRTLEVIDTPGHAPHHLSFLDEESDG-----LFT 167

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1394533491 181 GDTLFVAGCGKFYEGTAD--------EMCKALLEVLGRLPPDtRVYCGH 221
Cdd:cd07726   168 GDAAGVRYPELDVVGPPStpppdfdpEAWLESLDRLLSLKPE-RIYLTH 215
Lactamase_B pfam00753
Metallo-beta-lactamase superfamily;
63-221 4.10e-10

Metallo-beta-lactamase superfamily;


Pssm-ID: 425851 [Multi-domain]  Cd Length: 196  Bit Score: 58.15  E-value: 4.10e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533491  63 YLVIDDEtkEAAIVDP-----VQPQKVVDAARKHGVKLTTVLTTHHHWDHAGGNEKLVKlESGLKVYGGDDRIGALTHKI 137
Cdd:pfam00753   9 YLIEGGG--GAVLIDTggsaeAALLLLLAALGLGPKDIDAVILTHGHFDHIGGLGELAE-ATDVPVIVVAEEARELLDEE 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533491 138 THLSTLQVGSLNVKC----------------------LATPCHTSGHICYFVSKPGGSeppAVFTGDTLFVAGCGKFYEG 195
Cdd:pfam00753  86 LGLAASRLGLPGPPVvplppdvvleegdgilggglglLVTHGPGHGPGHVVVYYGGGK---VLFTGDLLFAGEIGRLDLP 162

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1394533491 196 TAD---------EMCKALLEVLGRLPPDtRVYCGH 221
Cdd:pfam00753 163 LGGllvlhpssaESSLESLLKLAKLKAA-VIVPGH 196
MBLAC1-like_MBL-fold cd07711
uncharacterized human metallo-beta-lactamase domain-containing protein 1 and related proteins; ...
 64-163 1.11e-07

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: 51.05  E-value: 1.11e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533491  64 LVIDDETKeaAIVDPVQP---QKVVDAARKHGVKL---TTVLTTHHHWDHAGGNEklvkLESGLKVYggDDRIGALTHKI 137
Cdd:cd07711    26 LIKDGGKN--ILVDTGTPwdrDLLLKALAEHGLSPediDYVVLTHGHPDHIGNLN----LFPNATVI--VGWDICGDSYD 97

                          90       100       110
                  ....*....|....*....|....*....|
gi 1394533491 138 THlSTLQVG----SLNVKCLATPCHTSGHI 163
Cdd:cd07711    98 DH-SLEEGDgyeiDENVEVIPTPGHTPEDV 126
AHL_lactonase_MBL-fold cd07729
quorum-quenching N-acyl-homoserine lactonase, MBL-fold metallo-hydrolase domain; Acyl ...
 65-182 1.31e-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: 1.31e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533491  65 VIDDETKEAAIVDPVQP--QKVVDAARKHGVK---LTTVLTTHHHWDHAGGNEKLVK---------LESGLKVYGGDDRI 130
Cdd:cd07729    54 AADDPGGLELAFPPGVTeeQTLEEQLARLGLDpedIDYVILSHLHFDHAGGLDLFPNatiivqraeLEYATGPDPLAAGY 133

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1394533491 131 GALTHKITHLST-LQVGSLN--------VKCLATPCHTSGHICYFVSKPGGsepPAVFTGD 182
Cdd:cd07729   134 YEDVLALDDDLPgGRVRLVDgdydlfpgVTLIPTPGHTPGHQSVLVRLPEG---TVLLAGD 191
SMB-1-like_MBL-B3 cd16313
SMB-1, THIN-B and related metallo-beta-lactamases, subclass B3; MBL-fold metallo-hydrolase ...
 81-240 1.01e-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: 49.09  E-value: 1.01e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533491  81 PQKVVDAARKHGVKLTTV---LTTHHHWDHAGGNEKLVKLeSGLKVYGG---------------DDRIGALTH--KITHL 140
Cdd:cd16313    44 PEQIAASIRQLGFKLEDVkyiLSSHDHWDHAGGIAALQKL-TGAQVLASpatvavlrsgsmgkdDPQFGGLTPmpPVASV 122

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533491 141 ST------LQVGSLNVKCLATPCHTSGHICY-FVSKPGGSEPPAVFtGDTLFVAGCGKfYEGTADEMCKALLE----VLG 209
Cdd:cd16313   123 RAvrdgevVKLGPLAVTAHATPGHTTGGTSWtWQSCEQGRCANMVF-ADSLTAVSADG-YRFSAHPAVLADVEqsiaAVE 200

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1394533491 210 RLPPDTRVYCGHEYTINNLKFARHVEPGNAA 240
Cdd:cd16313   201 KLACDILVSAHPEFSDMWTRVKRGAAEGNAA 231
metallo-hydrolase-like_MBL-fold cd07743
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 65-124 2.88e-06

uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo hydrolase domain; Members of the MBL-fold metallohydrolase superfamily are mainly hydrolytic enzymes which carry out a variety of biological functions. The class B metal beta-lactamases (MBLs) 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: 47.14  E-value: 2.88e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1394533491  65 VIDDETKEAAIVDPVQPQKVVDAARK----HGVKLTTVLTTHHHWDHAGGNEKLVKlESGLKVY 124
Cdd:cd07743    12 VYVFGDKEALLIDSGLDEDAGRKIRKileeLGWKLKAIINTHSHADHIGGNAYLQK-KTGCKVY 74
metallo-hydrolase-like_MBL-fold cd16282
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 64-221 4.41e-06

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


Pssm-ID: 293840 [Multi-domain]  Cd Length: 209  Bit Score: 46.79  E-value: 4.41e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533491  64 LVIDDEtkEAAIVD----PVQPQKVVDAARKH-GVKLTTVLTTHHHWDHAGGN-------------------------EK 113
Cdd:cd16282    19 FIVGDD--GVVVIDtgasPRLARALLAAIRKVtDKPVRYVVNTHYHGDHTLGNaafadagapiiahentreelaargeAY 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533491 114 LVKLESGLKVYGGDDRIGALTHKITHLSTLQVGSLNVKCLAT-PCHTSGHICYFVSKPGgseppAVFTGDTLFVAGCGKF 192
Cdd:cd16282    97 LELMRRLGGDAMAGTELVLPDRTFDDGLTLDLGGRTVELIHLgPAHTPGDLVVWLPEEG-----VLFAGDLVFNGRIPFL 171

                         170       180
                  ....*....|....*....|....*....
gi 1394533491 193 YEGTADEMCKAlLEVLGRLPPdTRVYCGH 221
Cdd:cd16282   172 PDGSLAGWIAA-LDRLLALDA-TVVVPGH 198
Mbl1b-like_MBL-B3 cd16310
Caulobacter crescentus Mbl1b and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 57-161 1.78e-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: 42.05  E-value: 1.78e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533491  57 LTDNYMYLVIDDETKEAAivdpvqpqKVVDA-ARKHGVKLTTV---LTTHHHWDHAGGNEKLvKLESGLKVYGGDDRIGA 132
Cdd:cd16310    27 ITSNHGAILLDGGLEENA--------ALIEQnIKALGFKLSDIkiiINTHAHYDHAGGLAQL-KADTGAKLWASRGDRPA 97

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1394533491 133 LTH-----------------KITHL----STLQVGSLNVKCLATPCHTSG 161
Cdd:cd16310    98 LEAgkhigdnitqpapfpavKVDRIlgdgEKIKLGDITLTATLTPGHTKG 147
IND_BlaB-like_MBL-B1 cd16299
IND1, IND2, BlaB-1 and related metallo-beta-lactamases, subclass B1; MBL-fold ...
 60-110 3.02e-04

IND1, IND2, BlaB-1 and related metallo-beta-lactamases, subclass B1; MBL-fold metallo-hydrolase domain; Includes the chromosome-encoded metallo-beta-lactamases Chryseobacterium indologenes IND-1, IND-2, and IND-7, Elizabethkingia meningoseptica (Chryseobacterium meningosepticum) BlaB, Chryseobacterium gleum CGB-1, and Empedobacter brevis EBR-1. 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 MBLs belongs to the B1 subclass. B1 enzymes are most active with two zinc ions bound in the active site, and have a broad-spectrum substrate profile.


Pssm-ID: 293857  Cd Length: 212  Bit Score: 41.28  E-value: 3.02e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1394533491  60 NYMYLViddeTKEAAIV-----DPVQPQKVVDAAR-KHGVKLTTVLTTHHHWDHAGG 110
Cdd:cd16299    27 NAMYLV----TKKGVILfdtpwDKDQYQPLLDSIRkKHNLPVIAVIATHSHEDRAGG 79
COG1237 COG1237
Metal-dependent hydrolase, beta-lactamase superfamily II [General function prediction only];
88-128 7.69e-04

Metal-dependent hydrolase, beta-lactamase superfamily II [General function prediction only];


Pssm-ID: 440850  Cd Length: 273  Bit Score: 40.25  E-value: 7.69e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1394533491  88 ARKHGVKLTT----VLTtHHHWDHAGGNEKLVKLESGLKVYGGDD 128
Cdd:COG1237    48 AEKLGIDLSDidavVLS-HGHYDHTGGLPALLELNPKAPVYAHPD 91
ElaC COG1234
Ribonuclease BN, tRNA processing enzyme [Translation, ribosomal structure and biogenesis];
84-198 7.94e-04

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


Pssm-ID: 440847 [Multi-domain]  Cd Length: 250  Bit Score: 40.18  E-value: 7.94e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533491  84 VVDAARKHGV---KLTTVLTTHHHWDHAGG------NEKLVKLESGLKVYG---GDDRIGALT-------------HKIT 138
Cdd:COG1234    39 TQRQLLRAGLdprDIDAIFITHLHGDHIAGlpgllsTRSLAGREKPLTIYGppgTKEFLEALLkasgtdldfplefHEIE 118

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533491 139 HLSTLQVGSLNVKCLATpCHTSGHICYFVSKPGGSeppAVFTGDTLFVAGCGKFYEGtAD 198
Cdd:COG1234   119 PGEVFEIGGFTVTAFPL-DHPVPAYGYRFEEPGRS---LVYSGDTRPCEALVELAKG-AD 173
metallo-hydrolase-like_MBL-fold cd07739
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 71-107 1.02e-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: 293825 [Multi-domain]  Cd Length: 201  Bit Score: 39.41  E-value: 1.02e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1394533491  71 KEAAIVDPV----QPQKVVDAARKHGVKLTTVLTTHHHWDH 107
Cdd:cd07739    25 TEAVLVDAQftraDAERLADWIKASGKTLTTIYITHGHPDH 65
BJP-1-like_MBL-B3 cd16309
Bradyrhizobium diazoefficiens BJP-1 and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 78-179 6.87e-03

Bradyrhizobium diazoefficiens BJP-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 BJP-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: 293867 [Multi-domain]  Cd Length: 252  Bit Score: 37.46  E-value: 6.87e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533491  78 PVQPQKVVDAARKHGVKLTTV---LTTHHHWDHAGGNEKLVK---------------LESGLkVYGGD-----------D 128
Cdd:cd16309    41 PQSTPLIKDNIKKLGFDVKDVkylLNTHAHFDHAGGLAELKKatgaqlvasaadkplLESGY-VGSGDtknlqfppvrvD 119

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1394533491 129 RIGALTHKIThlstlqVGSLNVKCLATPCHTSGHICY-FVSKPGGSEPPAVF 179
Cdd:cd16309   120 RVIGDGDKVT------LGGTTLTAHLTPGHSPGCTSWtTTVKDTAGPPREVL 165
SPM-1-like_MBL-B1-B2-like cd16286
Pseudomonas areoginosa SPM-1 and related metallo-beta-lactamases, subclasses B1 and B2 like; ...
 37-127 7.08e-03

Pseudomonas areoginosa SPM-1 and related metallo-beta-lactamases, subclasses B1 and B2 like; MBL-fold metallo-hydrolase domain; SPM-1 was first identified in a Pseudomonas aeruginosa strain from a paediatric leukaemia patient and is a major clinical problem. MBLs (class B of the Ambler beta-lactamase classification) have been divided into three subclasses B1, B2 and B3, based on sequence/structural relationships and substrates, with the B1 and B2 MBLs are most closely related to each other. SPM-1 appears to be a hybrid B1/B2 MBL.


Pssm-ID: 293844 [Multi-domain]  Cd Length: 236  Bit Score: 37.13  E-value: 7.08e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1394533491  37 DLRKNLTVDEGTMKVEVLpalTDNYMY----LVIDDETKEAAIVDP----VQPQKVVD-AARKHGVKLTTVLTTHHHWDH 107
Cdd:cd16286     2 DLPYNLTAREIDPDVFVI---THRDPWssnvLVVKMLDGTVVIVDSpytnLATQTVLDwIAKTMGPRKVVAINTHFHLDG 78

                          90       100
                  ....*....|....*....|
gi 1394533491 108 AGGNEKLVKLesGLKVYGGD 127
Cdd:cd16286    79 TGGNEALKKR--GIPTWGSD 96
 
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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