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Conserved domains on  [gi|823296123|ref|WP_047051708|]
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MULTISPECIES: MBL fold metallo-hydrolase [Enterobacter cloacae complex]

Protein Classification

MBL fold metallo-hydrolase( domain architecture ID 10870212)

MBL fold metallo-hydrolase similar to Salmonella enterica YcbL: a type II glyoxalase

Gene Ontology:  GO:0016787
PubMed:  17597585

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
YcbL-like_MBL-fold cd07737
Salmonella enterica serovar typhimurium YcbL and related proteins; MBL-fold metallo hydrolase ...
 3-192 2.10e-127

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: 356.86  E-value: 2.10e-127
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296123   3 YRIIPVTAFSQNCSLIWCEQTKLAALVDPGGDAKTIKQEVAASGVTLMQILLTHGHLDHVGAAAELAEHYGVPIIGPEKE 82
Cdd:cd07737    1 YQIIPVTPFQQNCSLIWCEETKEAAVIDPGGDADKILQAIEDLGLTLKKILLTHGHLDHVGGAAELAEHYGVPIIGPHKE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296123  83 DEFWLQGLPAQSRMFGLDDCQPLTPDRWLNEDDRVNVGNVTLQVLHCPGHTPGHIVFFDDVSRLLISGDVIFKGGVGRSD 162
Cdd:cd07737   81 DKFLLENLPEQSQMFGFPPAEAFTPDRWLEEGDTVTVGNLTLEVLHCPGHTPGHVVFFNRESKLAIVGDVLFKGSIGRTD 160

                        170       180       190
                 ....*....|....*....|....*....|
gi 823296123 163 FPRGDHGQLIQSIKQKLLPLGDDVTFIPGH 192
Cdd:cd07737  161 FPGGNHAQLIASIKEKLLPLGDDVTFIPGH 190
 
Name Accession Description Interval E-value
YcbL-like_MBL-fold cd07737
Salmonella enterica serovar typhimurium YcbL and related proteins; MBL-fold metallo hydrolase ...
 3-192 2.10e-127

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: 356.86  E-value: 2.10e-127
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296123   3 YRIIPVTAFSQNCSLIWCEQTKLAALVDPGGDAKTIKQEVAASGVTLMQILLTHGHLDHVGAAAELAEHYGVPIIGPEKE 82
Cdd:cd07737    1 YQIIPVTPFQQNCSLIWCEETKEAAVIDPGGDADKILQAIEDLGLTLKKILLTHGHLDHVGGAAELAEHYGVPIIGPHKE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296123  83 DEFWLQGLPAQSRMFGLDDCQPLTPDRWLNEDDRVNVGNVTLQVLHCPGHTPGHIVFFDDVSRLLISGDVIFKGGVGRSD 162
Cdd:cd07737   81 DKFLLENLPEQSQMFGFPPAEAFTPDRWLEEGDTVTVGNLTLEVLHCPGHTPGHVVFFNRESKLAIVGDVLFKGSIGRTD 160

                        170       180       190
                 ....*....|....*....|....*....|
gi 823296123 163 FPRGDHGQLIQSIKQKLLPLGDDVTFIPGH 192
Cdd:cd07737  161 FPGGNHAQLIASIKEKLLPLGDDVTFIPGH 190
GloB COG0491
Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General ...
 7-208 9.91e-60

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: 186.43  E-value: 9.91e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296123   7 PVTAFSQNCSLIWCeqTKLAALVDPGGD---AKTIKQEVAASGVTLMQILLTHGHLDHVGAAAELAEHYGVPIIGPEKED 83
Cdd:COG0491    9 PGAGLGVNSYLIVG--GDGAVLIDTGLGpadAEALLAALAALGLDIKAVLLTHLHPDHVGGLAALAEAFGAPVYAHAAEA 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296123  84 EFWLQglPAQSRMFGLDdcqPLTPDRWLNEDDRVNVGNVTLQVLHCPGHTPGHIVFFDDVSRLLISGDVIFKGGVGRSDF 163
Cdd:COG0491   87 EALEA--PAAGALFGRE---PVPPDRTLEDGDTLELGGPGLEVIHTPGHTPGHVSFYVPDEKVLFTGDALFSGGVGRPDL 161

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 823296123 164 PRGDHGQLIQSIkQKLLPLGDDVtFIPGHGPMSTLGD-----------ERLHNPFL 208
Cdd:COG0491  162 PDGDLAQWLASL-ERLLALPPDL-VIPGHGPPTTAEAidyleellaalGERANPFL 215
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 14-192 2.35e-41

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: 138.46  E-value: 2.35e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296123    14 NCSLIWCEQTklAALVDPG-GDAKTIKQEVAASGV-TLMQILLTHGHLDHVGAAAELAEHYGVPIIGPEKEDEFWLQGLP 91
Cdd:smart00849   1 NSYLVRDDGG--AILIDTGpGEAEDLLAELKKLGPkKIDAIILTHGHPDHIGGLPELLEAPGAPVYAPEGTAELLKDLLA 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296123    92 AQSRMFGLDDcqPLTPDRWLNEDDRVNVGNVTLQVLHCPGHTPGHIVFFDDVSRLLISGDVIFKGGVGRSDFPRGDHGQL 171
Cdd:smart00849  79 LLGELGAEAE--PAPPDRTLKDGDELDLGGGELEVIHTPGHTPGSIVLYLPEGKILFTGDLLFAGGDGRTLVDGGDAAAS 156

                          170       180
                   ....*....|....*....|.
gi 823296123   172 IQSIKQKLLPLGDDVTFIPGH 192
Cdd:smart00849 157 DALESLLKLLKLLPKLVVPGH 177
GSH_gloB TIGR03413
hydroxyacylglutathione hydrolase; Members of this protein family are hydroxyacylglutathione ...
 5-208 6.28e-38

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: 131.89  E-value: 6.28e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296123    5 IIPVTAFSQNCSLIWCEQTKLAALVDPGgDAKTIKQEVAASGVTLMQILLTHGHLDHVGAAAELAEHYGVPIIGPEKEDe 84
Cdd:TIGR03413   1 IIPIPALSDNYIWLLHDPDGQAAVVDPG-EAEPVLDALEARGLTLTAILLTHHHHDHVGGVAELLEAFPAPVYGPAEER- 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296123   85 fwlqgLPAQsrmfglddcqpltpDRWLNEDDRVNVGNVTLQVLHCPGHTPGHIVFFDDVSRLLISGDVIFKGGVGRSdFp 164
Cdd:TIGR03413  79 -----IPGI--------------THPVKDGDTVTLGGLEFEVLAVPGHTLGHIAYYLPDSPALFCGDTLFSAGCGRL-F- 137

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296123  165 RGDHGQLIQSIkQKLLPLGDDVTFIPGH---------------------------------GPM---STLGDERLHNPFL 208
Cdd:TIGR03413 138 EGTPEQMYDSL-QRLAALPDDTLVYCAHeytlsnlrfaltvepdnpalqerlkevealraqGQPtlpSTLGLERATNPFL 216
Lactamase_B pfam00753
Metallo-beta-lactamase superfamily;
8-192 3.46e-32

Metallo-beta-lactamase superfamily;


Pssm-ID: 425851 [Multi-domain]  Cd Length: 196  Bit Score: 115.54  E-value: 3.46e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296123    8 VTAFSQNCSLIwcEQTKLAALVDPGGDAKTIKQE----VAASGVTLMQILLTHGHLDHVGAAAELAEHYGVPIIGPEKED 83
Cdd:pfam00753   1 LGPGQVNSYLI--EGGGGAVLIDTGGSAEAALLLllaaLGLGPKDIDAVILTHGHFDHIGGLGELAEATDVPVIVVAEEA 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296123   84 EFWLQGLPAQSRMFGLDD---CQPLTPDRWLNEDDRVNVGNVTLQVLHCPGHTPGHIVFFDDVSRLLISGDVIFKGGVGR 160
Cdd:pfam00753  79 RELLDEELGLAASRLGLPgppVVPLPPDVVLEEGDGILGGGLGLLVTHGPGHGPGHVVVYYGGGKVLFTGDLLFAGEIGR 158

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 823296123  161 SDFPRGDHGQLIQSIKQKLLPLGDDV------TFIPGH 192
Cdd:pfam00753 159 LDLPLGGLLVLHPSSAESSLESLLKLaklkaaVIVPGH 196
PLN02398 PLN02398
hydroxyacylglutathione hydrolase
 21-192 5.15e-16

hydroxyacylglutathione hydrolase


Pssm-ID: 215223 [Multi-domain]  Cd Length: 329  Bit Score: 75.26  E-value: 5.15e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296123  21 EQTKLAALVDPGgDAKTIKQEVAASGVTLMQILLTHGHLDHVGAAAELAEHYGVPIIGPEKEdefwlqglpaQSRMFGLD 100
Cdd:PLN02398  95 EDTGTVGVVDPS-EAVPVIDALSRKNRNLTYILNTHHHYDHTGGNLELKARYGAKVIGSAVD----------KDRIPGID 163

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296123 101 DCqpltpdrwLNEDDRVNVGNVTLQVLHCPGHTPGHIVFFDDVSRLLISGDVIFKGGVGRsdFPRGDHGQLIQSIkQKLL 180
Cdd:PLN02398 164 IV--------LKDGDKWMFAGHEVLVMETPGHTRGHISFYFPGSGAIFTGDTLFSLSCGK--LFEGTPEQMLSSL-QKII 232

                        170
                 ....*....|..
gi 823296123 181 PLGDDVTFIPGH 192
Cdd:PLN02398 233 SLPDDTNIYCGH 244
 
Name Accession Description Interval E-value
YcbL-like_MBL-fold cd07737
Salmonella enterica serovar typhimurium YcbL and related proteins; MBL-fold metallo hydrolase ...
 3-192 2.10e-127

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: 356.86  E-value: 2.10e-127
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296123   3 YRIIPVTAFSQNCSLIWCEQTKLAALVDPGGDAKTIKQEVAASGVTLMQILLTHGHLDHVGAAAELAEHYGVPIIGPEKE 82
Cdd:cd07737    1 YQIIPVTPFQQNCSLIWCEETKEAAVIDPGGDADKILQAIEDLGLTLKKILLTHGHLDHVGGAAELAEHYGVPIIGPHKE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296123  83 DEFWLQGLPAQSRMFGLDDCQPLTPDRWLNEDDRVNVGNVTLQVLHCPGHTPGHIVFFDDVSRLLISGDVIFKGGVGRSD 162
Cdd:cd07737   81 DKFLLENLPEQSQMFGFPPAEAFTPDRWLEEGDTVTVGNLTLEVLHCPGHTPGHVVFFNRESKLAIVGDVLFKGSIGRTD 160

                        170       180       190
                 ....*....|....*....|....*....|
gi 823296123 163 FPRGDHGQLIQSIKQKLLPLGDDVTFIPGH 192
Cdd:cd07737  161 FPGGNHAQLIASIKEKLLPLGDDVTFIPGH 190
metallo-hydrolase-like_MBL-fold cd06262
mainly hydrolytic enzymes and related proteins which carry out various biological functions; ...
 4-192 1.21e-68

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: 208.29  E-value: 1.21e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296123   4 RIIPVTAFSQNCSLIWCEQTKlAALVDPGGDAKT-IKQEVAASGVTLMQILLTHGHLDHVGAAAELAEHYGVPIIGPEKe 82
Cdd:cd06262    1 KRLPVGPLQTNCYLVSDEEGE-AILIDPGAGALEkILEAIEELGLKIKAILLTHGHFDHIGGLAELKEAPGAPVYIHEA- 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296123  83 DEFWLQGLPAQSRMFGLDDCQPLTPDRWLNEDDRVNVGNVTLQVLHCPGHTPGHIVFFDDVSRLLISGDVIFKGGVGRSD 162
Cdd:cd06262   79 DAELLEDPELNLAFFGGGPLPPPEPDILLEDGDTIELGGLELEVIHTPGHTPGSVCFYIEEEGVLFTGDTLFAGSIGRTD 158

                        170       180       190
                 ....*....|....*....|....*....|
gi 823296123 163 FPRGDHGQLIQSIKQKLLPLGDDVTFIPGH 192
Cdd:cd06262  159 LPGGDPEQLIESIKKLLLLLPDDTVVYPGH 188
TTHA1623-like_MBL-fold cd16322
uncharacterized Thermus thermophilus TTHA1623 and related proteins; MBL-fold metallo hydrolase ...
 4-208 3.65e-68

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: 207.59  E-value: 3.65e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296123   4 RIIPVTAFSQNCSLIWCEQTKLAALVDPGGDAKTIKQEVAASGVTLMQILLTHGHLDHVGAAAELAEHYGVPIIGPEKED 83
Cdd:cd16322    2 RPFTLGPLQENTYLVADEGGGEAVLVDPGDESEKLLARFGTTGLTLLYILLTHAHFDHVGGVADLRRHPGAPVYLHPDDL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296123  84 EFWlQGLPAQSRMFGLDDCQPLTPDRWLNEDDRVNVGNVTLQVLHCPGHTPGHIVFFDDVSRLLISGDVIFKGGVGRSDF 163
Cdd:cd16322   82 PLY-EAADLGAKAFGLGIEPLPPPDRLLEDGQTLTLGGLEFKVLHTPGHSPGHVCFYVEEEGLLFSGDLLFQGSIGRTDL 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 823296123 164 PRGDHGQLIQSIKqKLLPLGDDVTFIPGHGPMSTLGDERLHNPFL 208
Cdd:cd16322  161 PGGDPKAMAASLR-RLLTLPDETRVFPGHGPPTTLGEERRTNPFL 204
GloB COG0491
Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General ...
 7-208 9.91e-60

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: 186.43  E-value: 9.91e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296123   7 PVTAFSQNCSLIWCeqTKLAALVDPGGD---AKTIKQEVAASGVTLMQILLTHGHLDHVGAAAELAEHYGVPIIGPEKED 83
Cdd:COG0491    9 PGAGLGVNSYLIVG--GDGAVLIDTGLGpadAEALLAALAALGLDIKAVLLTHLHPDHVGGLAALAEAFGAPVYAHAAEA 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296123  84 EFWLQglPAQSRMFGLDdcqPLTPDRWLNEDDRVNVGNVTLQVLHCPGHTPGHIVFFDDVSRLLISGDVIFKGGVGRSDF 163
Cdd:COG0491   87 EALEA--PAAGALFGRE---PVPPDRTLEDGDTLELGGPGLEVIHTPGHTPGHVSFYVPDEKVLFTGDALFSGGVGRPDL 161

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 823296123 164 PRGDHGQLIQSIkQKLLPLGDDVtFIPGHGPMSTLGD-----------ERLHNPFL 208
Cdd:COG0491  162 PDGDLAQWLASL-ERLLALPPDL-VIPGHGPPTTAEAidyleellaalGERANPFL 215
hydroxyacylglutathione_hydrolase_MBL-fold cd07723
hydroxyacylglutathione hydrolase, MBL-fold metallo-hydrolase domain; hydroxyacylglutathione ...
 6-192 6.62e-43

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: 141.83  E-value: 6.62e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296123   6 IPVTAFSQN-CSLIWCEQTKLAALVDPGgDAKTIKQEVAASGVTLMQILLTHGHLDHVGAAAELAEHYG-VPIIGPEKEd 83
Cdd:cd07723    1 VPIPALSDNyIYLIVDEATGEAAVVDPG-EAEPVLAALEKNGLTLTAILTTHHHWDHTGGNAELKALFPdAPVYGPAED- 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296123  84 efwlqglpaqsRMFGLDdcqpltpdRWLNEDDRVNVGNVTLQVLHCPGHTPGHIVFFDDVSRLLISGDVIFKGGVGRsdF 163
Cdd:cd07723   79 -----------RIPGLD--------HPVKDGDEIKLGGLEVKVLHTPGHTLGHICYYVPDEPALFTGDTLFSGGCGR--F 137

                        170       180
                 ....*....|....*....|....*....
gi 823296123 164 PRGDHGQLIQSIkQKLLPLGDDVTFIPGH 192
Cdd:cd07723  138 FEGTAEQMYASL-QKLLALPDDTLVYCGH 165
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 14-192 2.35e-41

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: 138.46  E-value: 2.35e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296123    14 NCSLIWCEQTklAALVDPG-GDAKTIKQEVAASGV-TLMQILLTHGHLDHVGAAAELAEHYGVPIIGPEKEDEFWLQGLP 91
Cdd:smart00849   1 NSYLVRDDGG--AILIDTGpGEAEDLLAELKKLGPkKIDAIILTHGHPDHIGGLPELLEAPGAPVYAPEGTAELLKDLLA 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296123    92 AQSRMFGLDDcqPLTPDRWLNEDDRVNVGNVTLQVLHCPGHTPGHIVFFDDVSRLLISGDVIFKGGVGRSDFPRGDHGQL 171
Cdd:smart00849  79 LLGELGAEAE--PAPPDRTLKDGDELDLGGGELEVIHTPGHTPGSIVLYLPEGKILFTGDLLFAGGDGRTLVDGGDAAAS 156

                          170       180
                   ....*....|....*....|.
gi 823296123   172 IQSIKQKLLPLGDDVTFIPGH 192
Cdd:smart00849 157 DALESLLKLLKLLPKLVVPGH 177
POD-like_MBL-fold cd07724
ETHE1 (PDO type I), persulfide dioxygenase A (PDOA, PDO type II) and related proteins; ...
 17-193 4.62e-41

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: 137.53  E-value: 4.62e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296123  17 LIWCEQTKLAALVDPGGD-AKTIKQEVAASGVTLMQILLTHGHLDHVGAAAELAEHYGVPI-IGPEKEDEFwlqglpaqs 94
Cdd:cd07724   16 LVGDPETGEAAVIDPVRDsVDRYLDLAAELGLKITYVLETHVHADHVSGARELAERTGAPIvIGEGAPASF--------- 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296123  95 rmfglddcqpltPDRWLNEDDRVNVGNVTLQVLHCPGHTPGHIVFFDDVSRLLISGDVIFKGGVGRSDFP---RGDHGQL 171
Cdd:cd07724   87 ------------FDRLLKDGDVLELGNLTLEVLHTPGHTPESVSYLVGDPDAVFTGDTLFVGDVGRPDLPgeaEGLARQL 154

                        170       180
                 ....*....|....*....|..
gi 823296123 172 IQSIKQKLLPLGDDVTFIPGHG 193
Cdd:cd07724  155 YDSLQRKLLLLPDETLVYPGHD 176
GSH_gloB TIGR03413
hydroxyacylglutathione hydrolase; Members of this protein family are hydroxyacylglutathione ...
 5-208 6.28e-38

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: 131.89  E-value: 6.28e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296123    5 IIPVTAFSQNCSLIWCEQTKLAALVDPGgDAKTIKQEVAASGVTLMQILLTHGHLDHVGAAAELAEHYGVPIIGPEKEDe 84
Cdd:TIGR03413   1 IIPIPALSDNYIWLLHDPDGQAAVVDPG-EAEPVLDALEARGLTLTAILLTHHHHDHVGGVAELLEAFPAPVYGPAEER- 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296123   85 fwlqgLPAQsrmfglddcqpltpDRWLNEDDRVNVGNVTLQVLHCPGHTPGHIVFFDDVSRLLISGDVIFKGGVGRSdFp 164
Cdd:TIGR03413  79 -----IPGI--------------THPVKDGDTVTLGGLEFEVLAVPGHTLGHIAYYLPDSPALFCGDTLFSAGCGRL-F- 137

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296123  165 RGDHGQLIQSIkQKLLPLGDDVTFIPGH---------------------------------GPM---STLGDERLHNPFL 208
Cdd:TIGR03413 138 EGTPEQMYDSL-QRLAALPDDTLVYCAHeytlsnlrfaltvepdnpalqerlkevealraqGQPtlpSTLGLERATNPFL 216
BaeB-like_MBL-fold cd16275
Bacillus amyloliquefaciens BaeB and related proteins; MBL-fold metallo hydrolase domain; ...
 23-192 2.42e-35

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: 122.65  E-value: 2.42e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296123  23 TKLAALVDPGGDAKTIKQEVAASGVTLMQILLTHGHLDHVGAAAELAEHYGVPIIGPEKEDEFWlqGLPaqsrmfglddC 102
Cdd:cd16275   22 TREAAVVDPAWDIEKILAKLNELGLTLTGILLTHSHFDHVNLVEPLLAKYDAPVYMSKEEIDYY--GFR----------C 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296123 103 QPLTPdrwLNEDDRVNVGNVTLQVLHCPGHTPGHIVFFddVSRLLISGDVIFKGGVGRSDFPRGDHGQLIQSIKQ--KLL 180
Cdd:cd16275   90 PNLIP---LEDGDTIKIGDTEITCLLTPGHTPGSMCYL--LGDSLFTGDTLFIEGCGRCDLPGGDPEEMYESLQRlkKLP 164

                        170
                 ....*....|..
gi 823296123 181 PlgDDVTFIPGH 192
Cdd:cd16275  165 P--PNTRVYPGH 174
yflN-like_MBL-fold cd07721
uncharacterized subgroup which includes Bacillus subtilis yflN; MBL-fold metallo hydrolase ...
 14-193 6.37e-34

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: 120.02  E-value: 6.37e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296123  14 NCSLIWCEQTKLaaLVDPG--GDAKTIKQEVAASGVTLMQ---ILLTHGHLDHVGAAAELAEHYGVPI-IGPE------- 80
Cdd:cd07721   12 NAYLIEDDDGLT--LIDTGlpGSAKRILKALRELGLSPKDirrILLTHGHIDHIGSLAALKEAPGAPVyAHEReapyleg 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296123  81 KEDEFWLQGLPAQSRMFGLDDCQPLTPDRWLNEDDRVNVGnVTLQVLHCPGHTPGHIVFFDDVSRLLISGDVIFKGGvGR 160
Cdd:cd07721   90 EKPYPPPVRLGLLGLLSPLLPVKPVPVDRTLEDGDTLDLA-GGLRVIHTPGHTPGHISLYLEEDGVLIAGDALVTVG-GE 167

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 823296123 161 SDFPRG----DHGQLIQSIKqKLLPLGDDVtFIPGHG 193
Cdd:cd07721  168 LVPPPPpftwDMEEALESLR-KLAELDPEV-LAPGHG 202
Lactamase_B pfam00753
Metallo-beta-lactamase superfamily;
8-192 3.46e-32

Metallo-beta-lactamase superfamily;


Pssm-ID: 425851 [Multi-domain]  Cd Length: 196  Bit Score: 115.54  E-value: 3.46e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296123    8 VTAFSQNCSLIwcEQTKLAALVDPGGDAKTIKQE----VAASGVTLMQILLTHGHLDHVGAAAELAEHYGVPIIGPEKED 83
Cdd:pfam00753   1 LGPGQVNSYLI--EGGGGAVLIDTGGSAEAALLLllaaLGLGPKDIDAVILTHGHFDHIGGLGELAEATDVPVIVVAEEA 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296123   84 EFWLQGLPAQSRMFGLDD---CQPLTPDRWLNEDDRVNVGNVTLQVLHCPGHTPGHIVFFDDVSRLLISGDVIFKGGVGR 160
Cdd:pfam00753  79 RELLDEELGLAASRLGLPgppVVPLPPDVVLEEGDGILGGGLGLLVTHGPGHGPGHVVVYYGGGKVLFTGDLLFAGEIGR 158

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 823296123  161 SDFPRGDHGQLIQSIKQKLLPLGDDV------TFIPGH 192
Cdd:pfam00753 159 LDLPLGGLLVLHPSSAESSLESLLKLaklkaaVIVPGH 196
metallo-hydrolase-like_MBL-fold cd16278
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 26-194 1.48e-28

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: 105.65  E-value: 1.48e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296123  26 AALVDPGGDAKTIKQEV--AASGVTLMQILLTHGHLDHVGAAAELAEHYGVPIIGPEKEDEFWLQGLPAqsrmfglddcq 103
Cdd:cd16278   29 VVVIDPGPDDPAHLDALlaALGGGRVSAILVTHTHRDHSPGAARLAERTGAPVRAFGPHRAGGQDTDFA----------- 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296123 104 pltPDRWLNEDDRVNVGNVTLQVLHCPGHTPGHIVFFDDVSRLLISGDVIFkggvGRS----DFPRGDHGQLIQSIkQKL 179
Cdd:cd16278   98 ---PDRPLADGEVIEGGGLRLTVLHTPGHTSDHLCFALEDEGALFTGDHVM----GWSttviAPPDGDLGDYLASL-ERL 169

                        170
                 ....*....|....*
gi 823296123 180 LPLGDDVtFIPGHGP 194
Cdd:cd16278  170 LALDDRL-LLPGHGP 183
MBLAC2-like_MBL-fold cd07712
uncharacterized human metallo-beta-lactamase domain-containing protein 2 and related proteins; ...
 26-192 9.15e-23

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: 90.38  E-value: 9.15e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296123  26 AALVDPGGDAKTIKQEVAASGVTLMQILLTHGHLDHVGAAAELAEHYGVPIIGPEKEDEFWLQGLPAQSRMFGLddcQPL 105
Cdd:cd07712   20 ALLIDTGLGIGDLKEYVRTLTDLPLLVVATHGHFDHIGGLHEFEEVYVHPADAEILAAPDNFETLTWDAATYSV---PPA 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296123 106 TPDRWLNEDDRVNVGNVTLQVLHCPGHTPGHIVFFDDVSRLLISGDVIFKGGVgRSDFPRGDHGQLIQSIkQKLLPLGDD 185
Cdd:cd07712   97 GPTLPLRDGDVIDLGDRQLEVIHTPGHTPGSIALLDRANRLLFSGDVVYDGPL-IMDLPHSDLDDYLASL-EKLSKLPDE 174


                 ....*...
gi 823296123 186 VTFI-PGH 192
Cdd:cd07712  175 FDKVlPGH 182
metallo-hydrolase-like_MBL-fold cd16282
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 26-202 2.20e-22

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: 90.32  E-value: 2.20e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296123  26 AALVDPGGD---AKTIKQEVAA-SGVTLMQILLTHGHLDHVGAAAELAEHyGVPIIGPEK-------EDEFWLQGLPAQS 94
Cdd:cd16282   26 VVVIDTGASprlARALLAAIRKvTDKPVRYVVNTHYHGDHTLGNAAFADA-GAPIIAHENtreelaaRGEAYLELMRRLG 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296123  95 RmFGLDDCQPLTPDRWLNEDDRVNVGNVTLQVLH-CPGHTPGHIVFFDDVSRLLISGDVIFKGGVgrsdfPRGDHGQLIQ 173
Cdd:cd16282  105 G-DAMAGTELVLPDRTFDDGLTLDLGGRTVELIHlGPAHTPGDLVVWLPEEGVLFAGDLVFNGRI-----PFLPDGSLAG 178

                        170       180       190
                 ....*....|....*....|....*....|.
gi 823296123 174 SIK--QKLLPLGDDVtFIPGHGPMSTLGDER 202
Cdd:cd16282  179 WIAalDRLLALDATV-VVPGHGPVGDKADLR 208
ST1585-like_MBL-fold cd07726
uncharacterized subgroup which includes Sulfolobus tokodaii ST1585 protein; MBL-fold metallo ...
 26-152 2.06e-18

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: 79.84  E-value: 2.06e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296123  26 AALVDPGGD--AKTIKQEVAASGVTLMQ---ILLTHGHLDHVGAAAELAEHY----------GVP-IIGPEK-------- 81
Cdd:cd07726   27 PALIDTGPSssVPRLLAALEALGIAPEDvdyIILTHIHLDHAGGAGLLAEALpnakvyvhprGARhLIDPSKlwasarav 106

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 823296123  82 ----EDEFWLQGLP-AQSRMFGLDDcqpltpdrwlneDDRVNVGNVTLQVLHCPGHTPGHIVFFDDVSRLLISGDV 152
Cdd:cd07726  107 ygdeADRLGGEILPvPEERVIVLED------------GETLDLGGRTLEVIDTPGHAPHHLSFLDEESDGLFTGDA 170
TTHA1429-like_MBL-fold cd07725
uncharacterized Thermus thermophilus TTHA1429 and related proteins; MBL-fold metallo hydrolase ...
 27-193 4.13e-18

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: 78.49  E-value: 4.13e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296123  27 ALVDPG----GDAKTIKQEVAASGVTLMQI---LLTHGHLDHVGAAAELAEHYGVPIIGPekedefwlqglpaqsrmfgl 99
Cdd:cd07725   27 TLIDTGlateEDAEALWEGLKELGLKPSDIdrvLLTHHHPDHIGLAGKLQEKSGATVYIL-------------------- 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296123 100 ddcqpltPDRWLNEDDRVNVGNVTLQVLHCPGHTPGHIVFFDDVSRLLISGDVI---FKGGVGRSDFPRGDH-GQLIQSI 175
Cdd:cd07725   87 -------DVTPVKDGDKIDLGGLRLKVIETPGHTPGHIVLYDEDRRELFVGDAVlpkITPNVSLWAVRVEDPlGAYLESL 159

                        170
                 ....*....|....*...
gi 823296123 176 kQKLLPLGDDVtFIPGHG 193
Cdd:cd07725  160 -DKLEKLDVDL-AYPGHG 175
metallo-hydrolase-like_MBL-fold cd16280
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 52-143 1.36e-17

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: 78.40  E-value: 1.36e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296123  52 ILLTHGHLDHVGAAAELAEHYGVPIIGPEKEDEfWLQGLPAQSRMFGLDdcQPLTPDRWLNEDDRVNVGNVTLQVLHCPG 131
Cdd:cd16280   65 ILITHGHGDHYGGAAYLKDLYGAKVVMSEADWD-MMEEPPEEGDNPRWG--PPPERDIVIKDGDTLTLGDTTITVYLTPG 141

                         90
                 ....*....|..
gi 823296123 132 HTPGHIVFFDDV 143
Cdd:cd16280  142 HTPGTLSLIFPV 153
LACTB2-like_MBL-fold cd07722
uncharacterized subgroup which includes human lactamase beta 2 and related proteins; MBL-fold ...
 14-194 1.69e-16

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: 74.11  E-value: 1.69e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296123  14 NCSLIWCEQTKLaaLVDPG----GDAKTIKQEVAASGV-TLMQILLTHGHLDHVGAAAELAEHYGVPiigpekEDEFWLQ 88
Cdd:cd07722   19 NTYLVGTGKRRI--LIDTGegrpSYIPLLKSVLDSEGNaTISDILLTHWHHDHVGGLPDVLDLLRGP------SPRVYKF 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296123  89 GLPAQSRMFGLDDcQPLTPdrwLNEDDRVNVGNVTLQVLHCPGHTPGHIVFFDDVSRLLISGDVIFkgGVGRSDFprGDH 168
Cdd:cd07722   91 PRPEEDEDPDEDG-GDIHD---LQDGQVFKVEGATLRVIHTPGHTTDHVCFLLEEENALFTGDCVL--GHGTAVF--EDL 162

                        170       180
                 ....*....|....*....|....*.
gi 823296123 169 GQLIQSIKqKLLPLGDDVTFiPGHGP 194
Cdd:cd07722  163 AAYMASLK-KLLSLGPGRIY-PGHGP 186
PLN02398 PLN02398
hydroxyacylglutathione hydrolase
 21-192 5.15e-16

hydroxyacylglutathione hydrolase


Pssm-ID: 215223 [Multi-domain]  Cd Length: 329  Bit Score: 75.26  E-value: 5.15e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296123  21 EQTKLAALVDPGgDAKTIKQEVAASGVTLMQILLTHGHLDHVGAAAELAEHYGVPIIGPEKEdefwlqglpaQSRMFGLD 100
Cdd:PLN02398  95 EDTGTVGVVDPS-EAVPVIDALSRKNRNLTYILNTHHHYDHTGGNLELKARYGAKVIGSAVD----------KDRIPGID 163

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296123 101 DCqpltpdrwLNEDDRVNVGNVTLQVLHCPGHTPGHIVFFDDVSRLLISGDVIFKGGVGRsdFPRGDHGQLIQSIkQKLL 180
Cdd:PLN02398 164 IV--------LKDGDKWMFAGHEVLVMETPGHTRGHISFYFPGSGAIFTGDTLFSLSCGK--LFEGTPEQMLSSL-QKII 232

                        170
                 ....*....|..
gi 823296123 181 PLGDDVTFIPGH 192
Cdd:PLN02398 233 SLPDDTNIYCGH 244
PRK10241 PRK10241
hydroxyacylglutathione hydrolase; Provisional
 1-210 7.52e-16

hydroxyacylglutathione hydrolase; Provisional


Pssm-ID: 182327 [Multi-domain]  Cd Length: 251  Bit Score: 73.71  E-value: 7.52e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296123   1 MNYRIIPvtAFSQNCSLIWCEQTKLAALVDPGgDAKTIKQEVAASGVTLMQILLTHGHLDHVGAAAELAEHYgvpiigpe 80
Cdd:PRK10241   1 MNLNSIP--AFDDNYIWVLNDEAGRCLIVDPG-EAEPVLNAIAENNWQPEAIFLTHHHHDHVGGVKELVEKF-------- 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296123  81 kedefwlqglpAQSRMFGLDDCQPLTPDRWLNEDDRVNVGNVTLQVLHCPGHTPGHIVFFDdvSRLLISGDVIFKGGVGR 160
Cdd:PRK10241  70 -----------PQIVVYGPQETQDKGTTQVVKDGETAFVLGHEFSVFATPGHTLGHICYFS--KPYLFCGDTLFSGGCGR 136

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 823296123 161 sdFPRGDHGQLIQSIkQKLLPLGDDVTFIPGHgpMSTLGDERL------HNPFLQD 210
Cdd:PRK10241 137 --LFEGTASQMYQSL-KKINALPDDTLICCAH--EYTLSNMKFalsilpHDLSIND 187
PLN02469 PLN02469
hydroxyacylglutathione hydrolase
 4-192 3.59e-14

hydroxyacylglutathione hydrolase


Pssm-ID: 178088 [Multi-domain]  Cd Length: 258  Bit Score: 69.02  E-value: 3.59e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296123   4 RIIPVTAFSQNCS-LIWCEQTKLAALVDPGgDAKTIKQEVAASGVTLMQILLTHGHLDHVGAAAELAEHygVPIIgpeke 82
Cdd:PLN02469   2 KIIPVPCLEDNYAyLIIDESTKDAAVVDPV-DPEKVLQAAHEHGAKIKLVLTTHHHWDHAGGNEKIKKL--VPGI----- 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296123  83 defwlqglpaqsRMFG--LDDCQPLTPDrwLNEDDRVNVGN-VTLQVLHCPGHTPGHIVFF----DDVSRLLISGDVIFK 155
Cdd:PLN02469  74 ------------KVYGgsLDNVKGCTHP--VENGDKLSLGKdVNILALHTPCHTKGHISYYvtgkEGEDPAVFTGDTLFI 139

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 823296123 156 GGVGRsdFPRGDHGQLIQSIKQKLLPLGDDVTFIPGH 192
Cdd:PLN02469 140 AGCGK--FFEGTAEQMYQSLCVTLGSLPKPTQVYCGH 174
metallo-hydrolase-like_MBL-fold cd07743
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 26-154 3.85e-13

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: 65.24  E-value: 3.85e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296123  26 AALVDPGGD---AKTIKQEVAASGVTLMQILLTHGHLDHVGAAAELAEHYGVPIIGPEKEDEF----------------- 85
Cdd:cd07743   20 ALLIDSGLDedaGRKIRKILEELGWKLKAIINTHSHADHIGGNAYLQKKTGCKVYAPKIEKAFienpllepsylggaypp 99

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 823296123  86 ------WLQGLPAQsrmfgLDDcqpltpdrwLNEDDRVNVGNVTLQVLHCPGHTPGHI-VFFDDvsRLLISGDVIF 154
Cdd:cd07743  100 kelrnkFLMAKPSK-----VDD---------IIEEGELELGGVGLEIIPLPGHSFGQIgILTPD--GVLFAGDALF 159
PLN02962 PLN02962
hydroxyacylglutathione hydrolase
 24-211 1.92e-12

hydroxyacylglutathione hydrolase


Pssm-ID: 178547 [Multi-domain]  Cd Length: 251  Bit Score: 64.43  E-value: 1.92e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296123  24 KLAALVDP-----GGDAKTIKQevaaSGVTLMQILLTHGHLDHVGAAAELAEHygVPIIGPekedefwlqglpAQSRMFG 98
Cdd:PLN02962  36 KPALLIDPvdktvDRDLSLVKE----LGLKLIYAMNTHVHADHVTGTGLLKTK--LPGVKS------------IISKASG 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296123  99 LDdcqpltPDRWLNEDDRVNVGNVTLQVLHCPGHTPGHIVFF-----DDVS-RLLISGDVIFKGGVGRSDFPRGDHGQLI 172
Cdd:PLN02962  98 SK------ADLFVEPGDKIYFGDLYLEVRATPGHTAGCVTYVtgegpDQPQpRMAFTGDALLIRGCGRTDFQGGSSDQLY 171

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 823296123 173 QSIKQKLLPLGDDVTFIPGHG----PMSTLGDERLHNPFL-QDE 211
Cdd:PLN02962 172 KSVHSQIFTLPKDTLIYPAHDykgfTVSTVGEEMLYNPRLtKDE 215
GOB1-like_MBL-B3 cd16308
Elizabethkingia meningoseptica GOB-1 and related metallo-beta-lactamases, subclass B3; ...
 38-143 8.21e-12

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: 62.49  E-value: 8.21e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296123  38 IKQEVAASGVTLMQI---LLTHGHLDHVGAAAELAEHYGVPIIGPEKEDEFWLQGLPAQSRMFGLDDC-QPLTPDRWLNE 113
Cdd:cd16308   47 IKKNIQALGFKFKDIkilLTTQAHYDHVGAMAAIKQQTGAKMMVDEKDAKVLADGGKSDYEMGGYGSTfAPVKADKLLHD 126

                         90       100       110
                 ....*....|....*....|....*....|
gi 823296123 114 DDRVNVGNVTLQVLHCPGHTPGHIVFFDDV 143
Cdd:cd16308  127 GDTIKLGGTKLTLLHHPGHTKGSCSFLFDV 156
MBLAC1-like_MBL-fold cd07711
uncharacterized human metallo-beta-lactamase domain-containing protein 1 and related proteins; ...
 7-195 8.47e-12

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: 61.45  E-value: 8.47e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296123   7 PVTAFSqNCSLIWCEQTKLaaLVDPGG--DAKTIKQEVAASGVTLMQI---LLTHGHLDHVGAAA--ELAEHY-GVPIIG 78
Cdd:cd07711   17 GFRASS-TVTLIKDGGKNI--LVDTGTpwDRDLLLKALAEHGLSPEDIdyvVLTHGHPDHIGNLNlfPNATVIvGWDICG 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296123  79 PEKEDEFWLQGLPaqsrmFGLDDCqpltpdrwlneddrvnvgnvtLQVLHCPGHTPGHI-VFFDDVS--RLLISGDVIFK 155
Cdd:cd07711   94 DSYDDHSLEEGDG-----YEIDEN---------------------VEVIPTPGHTPEDVsVLVETEKkgTVAVAGDLFER 147

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 823296123 156 GG--VGRSDFPRGDH--GQLIQSIKqKLLPLGDDVtfIPGHGPM 195
Cdd:cd07711  148 EEdlEDPILWDPLSEdpELQEESRK-RILALADWI--IPGHGPP 188
Mbl1b-like_MBL-B3 cd16310
Caulobacter crescentus Mbl1b and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 26-135 1.08e-09

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: 56.69  E-value: 1.08e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296123  26 AALVDPGGD--AKTIKQEVAASGVTLMQ---ILLTHGHLDHVGAAAELAEHYGVPIIGPEKEDEFWLQGLPAQSRMFGLD 100
Cdd:cd16310   33 AILLDGGLEenAALIEQNIKALGFKLSDikiIINTHAHYDHAGGLAQLKADTGAKLWASRGDRPALEAGKHIGDNITQPA 112

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 823296123 101 DCQPLTPDRWLNEDDRVNVGNVTLQVLHCPGHTPG 135
Cdd:cd16310  113 PFPAVKVDRILGDGEKIKLGDITLTATLTPGHTKG 147
YycJ-like_MBL-fold cd07733
uncharacterized subgroup which includes Bacillus subtilis YycJ and related proteins; MBL-fold ...
 14-81 1.91e-09

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: 54.19  E-value: 1.91e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 823296123  14 NCSLIWCEQTKLaaLVDPGGDAKTIKQEVAASGVTLMQ---ILLTHGHLDHVGAAAELAEHYGVPIIGPEK 81
Cdd:cd07733   10 NCTYLETEDGKL--LIDAGLSGRKITGRLAEIGRDPEDidaILVTHEHADHIKGLGVLARKYNVPIYATAG 78
OPHC2-like_MBL-fold cd07720
Pseudomonas pseudoalcaligenes organophosphorus hydrolase C2, and related proteins; MBL-fold ...
 43-154 3.03e-09

Pseudomonas pseudoalcaligenes organophosphorus hydrolase C2, and related proteins; MBL-fold metallo hydrolase domain; Pseudomonas pseudoalcaligenes OPHC2 is a thermostable organophosphorus hydrolase which a broad substrate activity spectrum: it hydrolyzes various phosphotriesters, esters, and a lactone. This subgroup also includes Pseudomonas oleovorans PoOPH which exhibits high lactonase and esterase activities, and latent PTE activity. However, double mutations His250Ile/Ile263Trp switch PoOPH into an efficient and thermostable PTE. 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: 293806 [Multi-domain]  Cd Length: 251  Bit Score: 55.25  E-value: 3.03e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296123  43 AASGVTLMQI---LLTHGHLDHVG----AAAEL----AEHYgVPiigpEKEDEFWL-----QGLPAQSRMFgLDDCQP-L 105
Cdd:cd07720   83 AAAGIDPEDIddvLLTHLHPDHIGglvdAGGKPvfpnAEVH-VS----EAEWDFWLddanaAKAPEGAKRF-FDAARDrL 156

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 823296123 106 TP--DRWLNEDDRVNVGNVTlqVLHCPGHTPGHIVFF--DDVSRLLISGDVIF 154
Cdd:cd07720  157 RPyaAAGRFEDGDEVLPGIT--AVPAPGHTPGHTGYRieSGGERLLIWGDIVH 207
AHL_lactonase_MBL-fold cd07729
quorum-quenching N-acyl-homoserine lactonase, MBL-fold metallo-hydrolase domain; Acyl ...
 52-192 3.40e-09

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: 54.91  E-value: 3.40e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296123  52 ILLTHGHLDHVGAAAELAehyGVPIIGPEKEDEFWLQGLPAQsRMFGLDDCQPLTPDRWLN----EDDRVNVGNVTLqvL 127
Cdd:cd07729   92 VILSHLHFDHAGGLDLFP---NATIIVQRAELEYATGPDPLA-AGYYEDVLALDDDLPGGRvrlvDGDYDLFPGVTL--I 165

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 823296123 128 HCPGHTPGHIVFFDDVSR--LLISGDVI-----FKGGVGrsDFPRGDHGQLIQSIKQ-KLLPLGDDVTFIPGH 192
Cdd:cd07729  166 PTPGHTPGHQSVLVRLPEgtVLLAGDAAytyenLEEGRP--PGINYDPEAALASLERlKALAEREGARVIPGH 236
MBL-B3-like cd07708
metallo-beta-lactamases, subclass B3; MBL-fold metallo-hydrolase domain; MBLs (class B of the ...
 26-135 3.88e-09

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


Pssm-ID: 293794 [Multi-domain]  Cd Length: 248  Bit Score: 54.86  E-value: 3.88e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296123  26 AALVDPGGDAKT--IKQEVAASGVTLMQ---ILLTHGHLDHVGAAAELAEHYGVPIIGPEKEDEFWLQGLPAQSRMFGLD 100
Cdd:cd07708   33 NILIDGDMEQNApmIKANIKKLGFKFSDtklILISHAHFDHAGGSAEIKKQTGAKVMAGAEDVSLLLSGGSSDFHYANDS 112

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 823296123 101 DCQ--PLTPDRWLNEDDRVNVGNVTLQVLHCPGHTPG 135
Cdd:cd07708  113 STYfpQSTVDRAVHDGERVTLGGTVLTAHATPGHTPG 149
BJP-1_FEZ-1-like_MBL-B3 cd16288
BJP-1, FEZ-1, GOB-1, Mbl1b and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 28-135 1.00e-08

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: 53.86  E-value: 1.00e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296123  28 LVDPGGDAKT--IKQEVAASGVTLMQI---LLTHGHLDHVGAAAELAEHYGVPIIGPEKEDEFWLQGlpaQSRMFGLDDC 102
Cdd:cd16288   35 LIDTGLESSApmIKANIRKLGFKPSDIkilLNSHAHLDHAGGLAALKKLTGAKLMASAEDAALLASG---GKSDFHYGDD 111

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 823296123 103 Q----PLTPDRWLNEDDRVNVGNVTLQVLHCPGHTPG 135
Cdd:cd16288  112 SlafpPVKVDRVLKDGDRVTLGGTTLTAHLTPGHTRG 148
BJP-1-like_MBL-B3 cd16309
Bradyrhizobium diazoefficiens BJP-1 and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 52-135 1.16e-08

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: 53.64  E-value: 1.16e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296123  52 ILLTHGHLDHVGAAAELAEHYGVPIIGPEKEDEFWLQGL----PAQSRMFglddcQPLTPDRWLNEDDRVNVGNVTLQVL 127
Cdd:cd16309   64 LLNTHAHFDHAGGLAELKKATGAQLVASAADKPLLESGYvgsgDTKNLQF-----PPVRVDRVIGDGDKVTLGGTTLTAH 138


                 ....*...
gi 823296123 128 HCPGHTPG 135
Cdd:cd16309  139 LTPGHSPG 146
PhnP COG1235
Phosphoribosyl 1,2-cyclic phosphate phosphodiesterase [Inorganic ion transport and metabolism]; ...
 13-152 1.27e-08

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


Pssm-ID: 440848 [Multi-domain]  Cd Length: 259  Bit Score: 53.36  E-value: 1.27e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296123  13 QNCSLIWCEQTKLaaLVDPGGDAKTIKQEVAASGVTLMQILLTHGHLDHVGAAAELAEHYG---VPIIGPEKEDEFWLQG 89
Cdd:COG1235   35 RSSILVEADGTRL--LIDAGPDLREQLLRLGLDPSKIDAILLTHEHADHIAGLDDLRPRYGpnpIPVYATPGTLEALERR 112

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 823296123  90 LP-AQSRMFGLDDCQPLTPdrwlneDDRVNVGNVTLQ---VLHcPGHTPGHIVFFDDVSRLLISGDV 152
Cdd:COG1235  113 FPyLFAPYPGKLEFHEIEP------GEPFEIGGLTVTpfpVPH-DAGDPVGYRIEDGGKKLAYATDT 172
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 ...
 28-135 1.34e-08

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: 53.51  E-value: 1.34e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296123  28 LVDPG--GDAKTIKQEVAASGVTLMQ---ILLTHGHLDHVGAAAELAEHYGVPII-GPEKEDEFWLQGLPAQSRMFG-LD 100
Cdd:cd16290   35 LIDGAlpQSAPQIEANIRALGFRLEDvklILNSHAHFDHAGGIAALQRDSGATVAaSPAGAAALRSGGVDPDDPQAGaAD 114

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 823296123 101 DCQPLTPDRWLNEDDRVNVGNVTLQVLHCPGHTPG 135
Cdd:cd16290  115 PFPPVAKVRVVADGEVVKLGPLAVTAHATPGHTPG 149
YmaE-like_MBL-fold cd07727
uncharacterized subgroup which includes Bacillus subtilis YmaE and related proteins; MBL-fold ...
 52-154 1.54e-08

uncharacterized subgroup which includes Bacillus subtilis YmaE and related proteins; MBL-fold metallo hydrolase domain; Includes the uncharacterized Bacillus subtilis YmaE and Nostoc all1228 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. 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: 293813 [Multi-domain]  Cd Length: 181  Bit Score: 52.20  E-value: 1.54e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296123  52 ILLTHghLDHVGAAAELAEHYGVPIIGPEKEDEfWLQGlPAQSRMFGLDDCQPLTPDrwlneddrvnvgnvtLQVLHCPG 131
Cdd:cd07727   51 IFLTH--RDDVADHAKWAERFGAKRIIHEDDVN-AVTR-PDEVIVLWGGDPWELDPD---------------LTLIPVPG 111

                         90       100
                 ....*....|....*....|...
gi 823296123 132 HTPGHIVFFDDVSRLLISGDVIF 154
Cdd:cd07727  112 HTRGSVVLLYKEKGVLFTGDHLA 134
NorV COG0426
Flavorubredoxin [Energy production and conversion];
26-152 7.26e-08

Flavorubredoxin [Energy production and conversion];


Pssm-ID: 440195 [Multi-domain]  Cd Length: 390  Bit Score: 51.76  E-value: 7.26e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296123  26 AALVDPGGDAKT------IKQEVAASGVTLmqILLTHGHLDHVGAAAELAEHY-GVPIIGPEKedefWLQGLPAqsrMFG 98
Cdd:COG0426   44 TALIDTVGESFFeeflenLSKVIDPKKIDY--IIVNHQEPDHSGSLPELLELApNAKIVCSKK----AARFLPH---FYG 114

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 823296123  99 LDDcqpltpDRWL--NEDDRVNVGNVTLQVLHCPG-HTPGHIVFFDDVSRLLISGDV 152
Cdd:COG0426  115 IPD------FRFIvvKEGDTLDLGGHTLQFIPAPMlHWPDTMFTYDPEDKILFSGDA 165
EVM-1-like_MBL-B3 cd16315
Erythrobacter vulgaris EVM-1 and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 52-135 1.39e-07

Erythrobacter vulgaris EVM-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 EVM-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: 293873 [Multi-domain]  Cd Length: 248  Bit Score: 50.43  E-value: 1.39e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296123  52 ILLTHGHLDHVGAAAELAEHYGVPIIGPEKEDEFWLQGLPA----QSRMfgLDDCQPLTPDRWLNEDDRVNVGNVTLQVL 127
Cdd:cd16315   64 LLSSHEHFDHVGGLAALQRATGARVAASAAAAPVLESGKPApddpQAGL--HEPFPPVRVDRIVEDGDTVALGSLRLTAH 141


                 ....*...
gi 823296123 128 HCPGHTPG 135
Cdd:cd16315  142 ATPGHTPG 149
metallo-hydrolase-like_MBL-fold cd07739
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 7-154 2.56e-07

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: 49.04  E-value: 2.56e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296123   7 PVTAFSQNCSLIWCEQTklAALVDPG---GDAKTIKQEVAASGVTLMQILLTHGHLDHVGAAAELAEHY-GVPIIGP--- 79
Cdd:cd07739   10 EISSFPVTSTLIYGETE--AVLVDAQftrADAERLADWIKASGKTLTTIYITHGHPDHYFGLEVLLEAFpDAKVVATpav 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296123  80 --------EKEDEFWLQGLPAQSrmfgldDCQPLTPDRWlnEDDRVNVGNVTLQVLHCPGHTPGHIVFFDDVS-RLLISG 150
Cdd:cd07739   88 vahikaqlEPKLAFWGPLLGGNA------PARLVVPEPL--DGDTLTLEGHPLEIVGVGGGDTDDTTYLWIPSlKTVVAG 159


                 ....
gi 823296123 151 DVIF 154
Cdd:cd07739  160 DVVY 163
flavodiiron_proteins_MBL-fold cd07709
catalytic domain of flavodiiron proteins (FDPs) and related proteins; MBL-fold ...
 26-195 3.66e-07

catalytic domain of flavodiiron proteins (FDPs) and related proteins; MBL-fold metallo-hydrolase domain; FDPs catalyze the reduction of oxygen and/or nitric oxide to water or nitrous oxide respectively. In addition to this N-terminal catalytic domain they contain a C-terminal flavin mononucleotide-binding flavodoxin-like domain. Although some FDPs are able to reduce NO or O2 with similar catalytic efficiencies others are selective for either NO or O2, such as Escherichia coli flavorubredoxin which is selective toward NO and G. intestinalis FDP which is selective toward O2. 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. Some members of this subgroup are single domain.


Pssm-ID: 293795 [Multi-domain]  Cd Length: 238  Bit Score: 49.02  E-value: 3.66e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296123  26 AALVDPGGDAKT------IKQEVAASGVTlmQILLTHGHLDHVGAAAELAEHY-GVPIIGPEKedefWLQGLPAqsrMFG 98
Cdd:cd07709   42 TALIDTVKEPFFdeflenLEEVIDPRKID--YIVVNHQEPDHSGSLPELLELApNAKIVCSKK----AARFLKH---FYP 112

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296123  99 LDDcqplTPDRWLNEDDRVNVGNVTLQVLHCPG-HTPGHIVFFDDVSRLLISGDvIFkGGVGRS----DFPRGDH----- 168
Cdd:cd07709  113 GID----ERFVVVKDGDTLDLGKHTLKFIPAPMlHWPDTMVTYDPEDKILFSGD-AF-GAHGASgelfDDEVEDYleear 186

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 823296123 169 ----------GQLIQSIKQKLLPLgdDVTFI-PGHGPM 195
Cdd:cd07709  187 ryyanimgpfSKQVRKALEKLEAL--DIKMIaPSHGPI 222
metallo-hydrolase-like_MBL-fold cd16277
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 43-153 5.01e-07

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: 48.67  E-value: 5.01e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296123  43 AASGVTLMQI---LLTHGHLDHVGAAAELAEHYGVPIIG------PEKEDEFWLQGLPAQSRMFGL--DDCQPLtPD--- 108
Cdd:cd16277   55 AAAGVRPEDVdyvLCTHLHVDHVGWNTRLVDGRWVPTFPnarylfSRAEYDHWSSPDAGGPPNRGVfeDSVLPV-IEagl 133

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 823296123 109 -RWLNEDDRVNVGnvtLQVLHCPGHTPGH--IVFFDDVSRLLISGDVI 153
Cdd:cd16277  134 aDLVDDDHEILDG---IRLEPTPGHTPGHvsVELESGGERALFTGDVM 178
metallo-hydrolase-like_MBL-fold cd16276
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 28-194 5.26e-07

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: 293834 [Multi-domain]  Cd Length: 188  Bit Score: 47.96  E-value: 5.26e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296123  28 LVD-PGGDAKTIKQEVAAsgVTLMQI---LLTHGHLDHVGAAAELAEHyGVPIIGPEKEDEfWLQGLPaqsrmfgldDCQ 103
Cdd:cd16276   23 VVDaPPSLGENLLAAIRK--VTDKPVthvVYSHNHADHIGGASIFKDE-GATIIAHEATAE-LLKRNP---------DPK 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296123 104 PLTPDRWLNEDDRVNVGNVTLQ-VLHCPGHTPGHIVFFDDVSRLLISGDVIFKGGVGRSDFPRGDH-GQLIQSIKQkLLP 181
Cdd:cd16276   90 RPVPTVTFDDEYTLEVGGQTLElSYFGPNHGPGNIVIYLPKQKVLMAVDLINPGWVPFFNFAGSEDiPGYIEALDE-LLE 168

                        170
                 ....*....|...
gi 823296123 182 LgDDVTFIPGHGP 194
Cdd:cd16276  169 Y-DFDTFVGGHGN 180
L1_POM-1-like_MBL-B3 cd16289
Stenotrophomonas maltophilia L1, Pseudomonas otitidis POM-1 and related ...
 26-137 6.20e-07

Stenotrophomonas maltophilia L1, Pseudomonas otitidis POM-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 L1- and Pom-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: 293847  Cd Length: 239  Bit Score: 48.66  E-value: 6.20e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296123  26 AALVDPG--GDAKTIKQEVAASGVT---LMQILLTHGHLDHVGAAAELAEHYGVPIIGpEKEDEFWLQGLPAQSRMFGlD 100
Cdd:cd16289   33 AVLLDGGmpQAADMLLDNMRALGVApgdLKLILHSHAHADHAGPLAALKRATGARVAA-NAESAVLLARGGSDDIHFG-D 110

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 823296123 101 DC--QPLTPDRWLNEDDRVNVGNVTLQVLHCPGHTPGHI 137
Cdd:cd16289  111 GItfPPVQADRIVMDGEVVTLGGVTFTAHFTPGHTPGST 149
THIN-B2-like_MBL-B3 cd16311
Janthinobacterium lividum THIN-B2 and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 52-135 7.90e-07

Janthinobacterium lividum THIN-B2 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 THIN-B2-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: 293869  Cd Length: 257  Bit Score: 48.44  E-value: 7.90e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296123  52 ILLTHGHLDHVGAAAELAEHYGVpIIGPEKEDEFWLqglpaQSRMFGLDDCQ-------PLTPD-RWLNEDDRVNVGNVT 123
Cdd:cd16311   64 ILNSHGHIDHAGGLAELQRRSGA-LVAASPSAALDL-----ASGEVGPDDPQyhalpkyPPVKDmRLARDGGQFNVGPVS 137

                         90
                 ....*....|..
gi 823296123 124 LQVLHCPGHTPG 135
Cdd:cd16311  138 LTAHATPGHTPG 149
arylsulfatase_Sdsa1-like_MBL-fold cd07710
Pseudomonas aeruginosa arylsulfatase SdsA1, Pseudomonas sp. DSM6611 arylsulfatase Pisa1, and ...
 52-155 1.61e-06

Pseudomonas aeruginosa arylsulfatase SdsA1, Pseudomonas sp. DSM6611 arylsulfatase Pisa1, and related proteins; MBL-fold metallo-hydrolase domain; Arylsulfatase (also known as aryl-sulfate sulfohydrolase, EC 3.1.6.1). Pseudomonas aeruginosa SdsA1 is a secreted SDS hydrolase that allows the bacterium to use primary sulfates such as the detergent SDS common in commercial personal hygiene products as a sole carbon or sulfur source. Pseudomonas inverting secondary alkylsulfatase 1 (Pisa1) is specific for secondary alkyl sulfates. 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: 293796 [Multi-domain]  Cd Length: 239  Bit Score: 47.11  E-value: 1.61e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296123  52 ILLTHGHLDHVGAA---AELAEHYGVPIIGPEK-----EDEFWLQGlPAQSR----MFG--LDDCQP------------- 104
Cdd:cd07710   60 IIYTHSHPDHFGGAggfVEEEDSGKVPIIAPEGfmeeaVSENVLAG-NAMSRraayQFGalLPKGEKgqvgaglgpglst 138

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 823296123 105 -----LTPDRWLNEDD-RVNVGNVTLQVLHCPGHTPGHIVFF--DDvsRLLISGDVIFK 155
Cdd:cd07710  139 gtvgfIPPTITITETGeTLTIDGVELEFQHAPGEAPDEMMVWlpDY--KVLFCADNVYH 195
ComEC COG2333
DNA uptake channel protein ComEC C-terminal domain, metallo-beta-lactamase superfamily ...
 26-151 2.07e-06

DNA uptake channel protein ComEC C-terminal domain, metallo-beta-lactamase superfamily [Intracellular trafficking, secretion, and vesicular transport];


Pssm-ID: 441904 [Multi-domain]  Cd Length: 253  Bit Score: 47.16  E-value: 2.07e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296123  26 AALVDPGGD------AKTIKQEVAASGVT-LMQILLTHGHLDHVGAAAELAEHYGVP--IIGPEKEDEFWLQGLPAQSRM 96
Cdd:COG2333   23 TILIDTGPRpsfdagERVVLPYLRALGIRrLDLLVLTHPDADHIGGLAAVLEAFPVGrvLVSGPPDTSETYERLLEALKE 102

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 823296123  97 FGlddcqplTPDRWLNEDDRVNVGNVTLQVLHCPGHTPGH-------IVF---FDDVSrLLISGD 151
Cdd:COG2333  103 KG-------IPVRPCRAGDTWQLGGVRFEVLWPPEDLLEGsdennnsLVLrltYGGFS-FLLTGD 159
RNaseJ_MBL-fold cd07714
RNAaseJ, MBL-fold metallo-hydrolase domain; RNase J, also called Ribonuclease J, is a ...
 52-80 3.93e-06

RNAaseJ, MBL-fold metallo-hydrolase domain; RNase J, also called Ribonuclease J, is a prokaryotic ribonuclease which plays a key part in RNA processing and in RNA degradation. It can act as an endonuclease which is specific for single-stranded regions of RNA irrespective of their sequence or location, and as a processive 5' exonuclease which only acts on substrates having a single phosphate or a hydroxyl at the 5' end. Many bacterial species have only one RNase J, but some, such as Bacillus subtilis, have two. 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: 293800 [Multi-domain]  Cd Length: 248  Bit Score: 46.25  E-value: 3.93e-06
                         10        20
                 ....*....|....*....|....*....
gi 823296123  52 ILLTHGHLDHVGAAAELAEHYGVPIIGPE 80
Cdd:cd07714   59 IFITHGHEDHIGALPYLLPELNVPIYATP 87
PRK00685 PRK00685
metal-dependent hydrolase; Provisional
 52-79 1.23e-05

metal-dependent hydrolase; Provisional


Pssm-ID: 234811 [Multi-domain]  Cd Length: 228  Bit Score: 44.42  E-value: 1.23e-05
                         10        20
                 ....*....|....*....|....*...
gi 823296123  52 ILLTHGHLDHVGAAAELAEHYGVPIIGP 79
Cdd:PRK00685  44 ILLTHGHGDHLGDTVEIAKRTGATVIAN 71
AIM-1-like_MBL-B3 cd16314
Pseudomonas Aeruginosa AIM-1 and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 52-135 2.35e-05

Pseudomonas Aeruginosa AIM-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 AIM-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: 293872 [Multi-domain]  Cd Length: 255  Bit Score: 44.11  E-value: 2.35e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296123  52 ILLTHGHLDHVGAAAELAEHYGVPIIGPEKEDEFWLQGLPAQS--RMFGLDDCQPLTPDRWLNEDDRVNVGNVTLQVLHC 129
Cdd:cd16314   64 IVSSHEHFDHAGGIARLQRATGAPVVAREPAATTLERGRSDRSdpQFLVVEKFPPVASVQRIGDGEVLRVGPLALTAHAT 143


                 ....*.
gi 823296123 130 PGHTPG 135
Cdd:cd16314  144 PGHTPG 149
ComA-like_MBL-fold cd07731
Competence protein ComA, ComEC and related proteins; MBL-fold metallo hydrolase domain; This ...
 15-128 2.79e-05

Competence protein ComA, ComEC and related proteins; MBL-fold metallo hydrolase domain; This subgroup includes proteins required for natural transformation competence including Neisseria gonorrhoeae ComA, Pseudomonas stutzeri ComA, Bacillus subtilis ComEC (also known as ComE operon protein 3) and Haemophilus influenza ORF2 encoded by the rec-2 gene, as well as Escherichia coli YcaI which does not mediate spontaneous plasmid transformation on nutrient-containing agar plates. It also includes the phosphorylcholine esterase (Pce) domain of choline-binding protein e from streptococcus pneumonia. 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: 293817 [Multi-domain]  Cd Length: 179  Bit Score: 42.89  E-value: 2.79e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296123  15 CSLIWCEQTklAALVDPGGDAKTIKQEVA----ASGVT-LMQILLTHGHLDHVGAAAELAEHYGVpiigpekeDEFWLQG 89
Cdd:cd07731   12 AILIQTPGK--TILIDTGPRDSFGEDVVVpylkARGIKkLDYLILTHPDADHIGGLDAVLKNFPV--------KEVYMPG 81

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 823296123  90 LPAQSRMFG--LDDC-QPLTPDRWLNEDDRVNVGNVTLQVLH 128
Cdd:cd07731   82 VTHTTKTYEdlLDAIkEKGIPVTPCKAGDRWQLGGVSFEVLS 123
RnjA COG0595
mRNA degradation ribonuclease J1/J2 [Translation, ribosomal structure and biogenesis];
52-155 4.51e-05

mRNA degradation ribonuclease J1/J2 [Translation, ribosomal structure and biogenesis];


Pssm-ID: 440360 [Multi-domain]  Cd Length: 553  Bit Score: 43.51  E-value: 4.51e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296123  52 ILLTHGHLDHVGAAAELAEHYGVPIIGPekedEFWLqGLpAQSRM--FGLDDCQPLTPdrwLNEDDRVNVGNVTLQVLH- 128
Cdd:COG0595   67 IVLTHGHEDHIGALPYLLKELNVPVYGT----PLTL-AL-LEAKLkeHGLLKKVKLHV---VKPGDRIKFGPFKVEFFRv 137

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 823296123 129 ---CPG------HTP-GHIVFfddvsrlliSGDviFK 155
Cdd:COG0595  138 thsIPDslglaiRTPaGTIVH---------TGD--FK 163
UlaG COG2220
L-ascorbate lactonase UlaG, metallo-beta-lactamase superfamily [Carbohydrate transport and ...
 52-151 1.08e-04

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


Pssm-ID: 441822 [Multi-domain]  Cd Length: 224  Bit Score: 41.83  E-value: 1.08e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296123  52 ILLTHGHLDHVGAAAELA-EHYGVPIIGPEkEDEFWLQGLpaqsrmfGLDDCQPltpdrwLNEDDRVNVGNVTLQVL--- 127
Cdd:COG2220   52 VLVTHDHYDHLDDATLRAlKRTGATVVAPL-GVAAWLRAW-------GFPRVTE------LDWGESVELGGLTVTAVpar 117

                         90       100       110
                 ....*....|....*....|....*....|
gi 823296123 128 HCPGHTPGH------IVFFDDVSRLLISGD 151
Cdd:COG2220  118 HSSGRPDRNgglwvgFVIETDGKTIYHAGD 147
YSH1 COG1236
RNA processing exonuclease, beta-lactamase fold, Cft2 family [Translation, ribosomal structure ...
 52-152 1.31e-03

RNA processing exonuclease, beta-lactamase fold, Cft2 family [Translation, ribosomal structure and biogenesis];


Pssm-ID: 440849 [Multi-domain]  Cd Length: 404  Bit Score: 39.01  E-value: 1.31e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296123  52 ILLTHGHLDHVGAAAEL-AEHYGVPIIGPE--------------KEDEFWLQGLPaqsrMFGLDD-------CQPLTPDR 109
Cdd:COG1236   54 VVLTHAHLDHSGALPLLvKEGFRGPIYATPatadlarillgdsaKIQEEEAEAEP----LYTEEDaeralelFQTVDYGE 129

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 823296123 110 WlneddrVNVGNVTLQvLHCPGHTPG--HIVFFDDVSRLLISGDV 152
Cdd:COG1236  130 P------FEIGGVRVT-FHPAGHILGsaQVELEVGGKRIVFSGDY 167
FEZ-1-like_MBL-B3 cd16307
Fluoribacter gormanii FEZ-1 and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 52-135 2.89e-03

Fluoribacter gormanii FEZ-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 FEZ-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: 293865  Cd Length: 255  Bit Score: 37.81  E-value: 2.89e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296123  52 ILLTHGHLDHVGAAAELAEHYGVPIIGPEKEDEFWLQGlpAQSRMFGLDDC----QPLTPDRWLNEDDRVNVGNVTLQVL 127
Cdd:cd16307   64 LLISHAHFDHAAGSALIKRETHAKYMVMDGDVDVVESG--GKSDFFYGNDPstyfPPAHVDKVLHDGEQVELGGTVLTAH 141


                 ....*...
gi 823296123 128 HCPGHTPG 135
Cdd:cd16307  142 LTAGHTKG 149
ElaC COG1234
Ribonuclease BN, tRNA processing enzyme [Translation, ribosomal structure and biogenesis];
13-86 5.18e-03

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


Pssm-ID: 440847 [Multi-domain]  Cd Length: 250  Bit Score: 36.71  E-value: 5.18e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296123  13 QNCSLIWCEQTKLaaLVDPGGDakTIKQeVAASGVTLMQ---ILLTHGHLDHVGAAAELAEHYG-------VPIIGPEKE 82
Cdd:COG1234   19 TSSYLLEAGGERL--LIDCGEG--TQRQ-LLRAGLDPRDidaIFITHLHGDHIAGLPGLLSTRSlagrekpLTIYGPPGT 93


                 ....
gi 823296123  83 DEFW 86
Cdd:COG1234   94 KEFL 97
BcII-like_MBL-B1 cd16304
Bacillus cereus Beta-lactamase 2 and related metallo-beta-lactamases, subclass B1; MBL-fold ...
 21-150 5.29e-03

Bacillus cereus Beta-lactamase 2 and related metallo-beta-lactamases, subclass B1; MBL-fold metallo-hydrolase domain; Bacillus cereus Beta-lactamase 2, also called BcII. 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 being most closely related to each other. BcII is a chromosome-encoded B1 MBL. B1 enzymes are most active with two zinc ions bound in the active site, and have a broad-spectrum substrate profile.


Pssm-ID: 293862 [Multi-domain]  Cd Length: 212  Bit Score: 36.49  E-value: 5.29e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296123  21 EQTK-LAALVdpggdAKTIKQEVaasgvtlMQILLTHGHLDHVGAAAELAEHyGVPIIGPEkedefwlqgLPAQ-SRMFG 98
Cdd:cd16304   47 EQTEeLLDWI-----KKKLKKPV-------TLAIVTHAHDDRIGGIKALQKR-GIPVYSTK---------LTAQlAKKQG 104

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 823296123  99 LDdcqplTPDRWLNEDDRVNVGNVTLQVLHC-PGHTPGHIVFFDDVSRLLISG 150
Cdd:cd16304  105 YP-----SPDGILKDDTTLKFGNTKIETFYPgEGHTADNIVVWLPQSKILFGG 152
 
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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