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Conserved domains on  [gi|495006367|ref|WP_007732381|]
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MULTISPECIES: MBL fold metallo-hydrolase [Rhodococcus]

Protein Classification

MBL fold metallo-hydrolase( domain architecture ID 14427473)

MBL fold metallo-hydrolase is most likely a hydrolytic enzyme that may have substrate towards phosphotriesters, esters, and/or lactones

CATH:  3.60.15.10
EC:  3.-.-.-
Gene Ontology:  GO:0016787|GO:0046872
PubMed:  17597585|12177301|11471246|11513844
SCOP:  3001057

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
metallo-hydrolase-like_MBL-fold cd16278
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 18-195 3.78e-62

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: 193.48  E-value: 3.78e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495006367  18 ASVLLENNPGMMTLDGTNTWILHAPGsvECVVVDPGDNDEEHLQRVAGI---GPVALTLITHRHYDHTGGVDRFHELTSA 94
Cdd:cd16278    2 VRRVLAPNPSPMTLDGTNTYLLGAPD--GVVVIDPGPDDPAHLDALLAAlggGRVSAILVTHTHRDHSPGAARLAERTGA 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495006367  95 PVRSVDPTFLRG------GASALVDGEVIEVAGLKLRILATPGHTADSVSIVIENDASVLTGDTILGRGTAVLDDSDGDL 168
Cdd:cd16278   80 PVRAFGPHRAGGqdtdfaPDRPLADGEVIEGGGLRLTVLHTPGHTSDHLCFALEDEGALFTGDHVMGWSTTVIAPPDGDL 159

                        170       180
                 ....*....|....*....|....*..
gi 495006367 169 GDYLTSLRSLAALGEGLtVLPGHGPDL 195
Cdd:cd16278  160 GDYLASLERLLALDDRL-LLPGHGPPI 185
BLACT_WH super family cl38958
Beta-lactamase associated winged helix domain; This winged helix domain is found at the ...
 228-261 6.11e-03

Beta-lactamase associated winged helix domain; This winged helix domain is found at the C-terminus of some beta lactamase enzymes.


The actual alignment was detected with superfamily member pfam17778:

Pssm-ID: 407650  Cd Length: 46  Bit Score: 34.13  E-value: 6.11e-03
                          10        20        30
                  ....*....|....*....|....*....|....
gi 495006367  228 SVRDVVEHVYSDVDPKLWPVAEKSVNVQLAYLRR 261
Cdd:pfam17778   1 TAMELVKVIYKDVPESLHPAAERGVLAHLEKLEA 34
 
Name Accession Description Interval E-value
metallo-hydrolase-like_MBL-fold cd16278
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 18-195 3.78e-62

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: 193.48  E-value: 3.78e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495006367  18 ASVLLENNPGMMTLDGTNTWILHAPGsvECVVVDPGDNDEEHLQRVAGI---GPVALTLITHRHYDHTGGVDRFHELTSA 94
Cdd:cd16278    2 VRRVLAPNPSPMTLDGTNTYLLGAPD--GVVVIDPGPDDPAHLDALLAAlggGRVSAILVTHTHRDHSPGAARLAERTGA 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495006367  95 PVRSVDPTFLRG------GASALVDGEVIEVAGLKLRILATPGHTADSVSIVIENDASVLTGDTILGRGTAVLDDSDGDL 168
Cdd:cd16278   80 PVRAFGPHRAGGqdtdfaPDRPLADGEVIEGGGLRLTVLHTPGHTSDHLCFALEDEGALFTGDHVMGWSTTVIAPPDGDL 159

                        170       180
                 ....*....|....*....|....*..
gi 495006367 169 GDYLTSLRSLAALGEGLtVLPGHGPDL 195
Cdd:cd16278  160 GDYLASLERLLALDDRL-LLPGHGPPI 185
GloB COG0491
Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General ...
 26-220 1.31e-30

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: 113.25  E-value: 1.31e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495006367  26 PGMMTLDGTNTWILHAPGsvECVVVDPGDNDEEH---LQRVAGIG-PVALTLITHRHYDHTGGVDRFHELTSAPVR--SV 99
Cdd:COG0491    7 GTPGAGLGVNSYLIVGGD--GAVLIDTGLGPADAealLAALAALGlDIKAVLLTHLHPDHVGGLAALAEAFGAPVYahAA 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495006367 100 DPTFLRGGASA-------------LVDGEVIEVAGLKLRILATPGHTADSVSIVIENDASVLTGDTILGRGTAVLDDSDG 166
Cdd:COG0491   85 EAEALEAPAAGalfgrepvppdrtLEDGDTLELGGPGLEVIHTPGHTPGHVSFYVPDEKVLFTGDALFSGGVGRPDLPDG 164

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 495006367 167 DLGDYLTSLRSLAALgEGLTVLPGHGPDLPdlqaisqqylAHREERLDQVRAAL 220
Cdd:COG0491  165 DLAQWLASLERLLAL-PPDLVIPGHGPPTT----------AEAIDYLEELLAAL 207
GSH_gloB TIGR03413
hydroxyacylglutathione hydrolase; Members of this protein family are hydroxyacylglutathione ...
 37-225 7.59e-22

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: 91.06  E-value: 7.59e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495006367   37 WILHAPGSvECVVVDPGDND--EEHLQRvAGIGPVALtLITHRHYDHTGGVDRFHELTSAPVRSVDPTFLRGGASALVDG 114
Cdd:TIGR03413  13 WLLHDPDG-QAAVVDPGEAEpvLDALEA-RGLTLTAI-LLTHHHHDHVGGVAELLEAFPAPVYGPAEERIPGITHPVKDG 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495006367  115 EVIEVAGLKLRILATPGHTADSVSIVIENDASVLTGDTIL----GR---GTAvlddsdgdlGDYLTSLRSLAALGEGLTV 187
Cdd:TIGR03413  90 DTVTLGGLEFEVLAVPGHTLGHIAYYLPDSPALFCGDTLFsagcGRlfeGTP---------EQMYDSLQRLAALPDDTLV 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 495006367  188 LPGH-------------GPDLPDLqaisQQYLAHREERLDQVRAAL-STLGE 225
Cdd:TIGR03413 161 YCAHeytlsnlrfaltvEPDNPAL----QERLKEVEALRAQGQPTLpSTLGL 208
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 35-191 1.98e-21

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: 87.99  E-value: 1.98e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495006367    35 NTWILHAPGsvECVVVDPGDNDEEHLQRVA---GIGPVALTLITHRHYDHTGGVDRFHELTSAPVRS--------VDPTF 103
Cdd:smart00849   1 NSYLVRDDG--GAILIDTGPGEAEDLLAELkklGPKKIDAIILTHGHPDHIGGLPELLEAPGAPVYApegtaellKDLLA 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495006367   104 LRGGASA----------LVDGEVIEVAGLKLRILATPGHTADSVSIVIENDASVLTGDTILGRGTAVLDD--SDGDLGDY 171
Cdd:smart00849  79 LLGELGAeaepappdrtLKDGDELDLGGGELEVIHTPGHTPGSIVLYLPEGKILFTGDLLFAGGDGRTLVdgGDAAASDA 158

                          170       180
                   ....*....|....*....|
gi 495006367   172 LTSLRSLAALGEGlTVLPGH 191
Cdd:smart00849 159 LESLLKLLKLLPK-LVVPGH 177
Lactamase_B pfam00753
Metallo-beta-lactamase superfamily;
29-191 6.88e-11

Metallo-beta-lactamase superfamily;


Pssm-ID: 425851 [Multi-domain]  Cd Length: 196  Bit Score: 60.07  E-value: 6.88e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495006367   29 MTLDGTNTWILHAPGsvECVVVDPGDNDEE------HLQRVAGIGPVALtLITHRHYDHTGGVDRFHELTSAPVRSVDPT 102
Cdd:pfam00753   1 LGPGQVNSYLIEGGG--GAVLIDTGGSAEAalllllAALGLGPKDIDAV-ILTHGHFDHIGGLGELAEATDVPVIVVAEE 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495006367  103 FLRGGASALV-----------------------DGEVIEVAGLKLRILATPGHTADSVSIVIENDASVLTGDTILGRGTA 159
Cdd:pfam00753  78 ARELLDEELGlaasrlglpgppvvplppdvvleEGDGILGGGLGLLVTHGPGHGPGHVVVYYGGGKVLFTGDLLFAGEIG 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 495006367  160 VLDDSDGDLGD--------YLTSLRSLAALGEgLTVLPGH 191
Cdd:pfam00753 158 RLDLPLGGLLVlhpssaesSLESLLKLAKLKA-AVIVPGH 196
PRK10241 PRK10241
hydroxyacylglutathione hydrolase; Provisional
 47-133 3.40e-10

hydroxyacylglutathione hydrolase; Provisional


Pssm-ID: 182327 [Multi-domain]  Cd Length: 251  Bit Score: 58.68  E-value: 3.40e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495006367  47 CVVVDPGDNdEEHLQRVA--GIGPVALtLITHRHYDHTGGV----DRFHELTS-APVRSVDPtflrgGASALV-DGEVIE 118
Cdd:PRK10241  24 CLIVDPGEA-EPVLNAIAenNWQPEAI-FLTHHHHDHVGGVkelvEKFPQIVVyGPQETQDK-----GTTQVVkDGETAF 96

                         90
                 ....*....|....*
gi 495006367 119 VAGLKLRILATPGHT 133
Cdd:PRK10241  97 VLGHEFSVFATPGHT 111
BLACT_WH pfam17778
Beta-lactamase associated winged helix domain; This winged helix domain is found at the ...
 228-261 6.11e-03

Beta-lactamase associated winged helix domain; This winged helix domain is found at the C-terminus of some beta lactamase enzymes.


Pssm-ID: 407650  Cd Length: 46  Bit Score: 34.13  E-value: 6.11e-03
                          10        20        30
                  ....*....|....*....|....*....|....
gi 495006367  228 SVRDVVEHVYSDVDPKLWPVAEKSVNVQLAYLRR 261
Cdd:pfam17778   1 TAMELVKVIYKDVPESLHPAAERGVLAHLEKLEA 34
 
Name Accession Description Interval E-value
metallo-hydrolase-like_MBL-fold cd16278
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 18-195 3.78e-62

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: 193.48  E-value: 3.78e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495006367  18 ASVLLENNPGMMTLDGTNTWILHAPGsvECVVVDPGDNDEEHLQRVAGI---GPVALTLITHRHYDHTGGVDRFHELTSA 94
Cdd:cd16278    2 VRRVLAPNPSPMTLDGTNTYLLGAPD--GVVVIDPGPDDPAHLDALLAAlggGRVSAILVTHTHRDHSPGAARLAERTGA 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495006367  95 PVRSVDPTFLRG------GASALVDGEVIEVAGLKLRILATPGHTADSVSIVIENDASVLTGDTILGRGTAVLDDSDGDL 168
Cdd:cd16278   80 PVRAFGPHRAGGqdtdfaPDRPLADGEVIEGGGLRLTVLHTPGHTSDHLCFALEDEGALFTGDHVMGWSTTVIAPPDGDL 159

                        170       180
                 ....*....|....*....|....*..
gi 495006367 169 GDYLTSLRSLAALGEGLtVLPGHGPDL 195
Cdd:cd16278  160 GDYLASLERLLALDDRL-LLPGHGPPI 185
LACTB2-like_MBL-fold cd07722
uncharacterized subgroup which includes human lactamase beta 2 and related proteins; MBL-fold ...
 13-193 8.35e-36

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: 126.11  E-value: 8.35e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495006367  13 RVTDIasvlLENNPGMMTLDGTNTWILHAPGSVecVVVDPGDNDE---EHLQRV---AGIGPVALTLITHRHYDHTGGVD 86
Cdd:cd07722    1 RVIRI----LGQNPGPFTLQGTNTYLVGTGKRR--ILIDTGEGRPsyiPLLKSVldsEGNATISDILLTHWHHDHVGGLP 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495006367  87 RFHELTSAPVRSV----------DPTFLRGGASALVDGEVIEVAGLKLRILATPGHTADSVSIVIENDASVLTGDTILGR 156
Cdd:cd07722   75 DVLDLLRGPSPRVykfprpeedeDPDEDGGDIHDLQDGQVFKVEGATLRVIHTPGHTTDHVCFLLEEENALFTGDCVLGH 154

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 495006367 157 GTAVlddsDGDLGDYLTSLRSLAALGEGlTVLPGHGP 193
Cdd:cd07722  155 GTAV----FEDLAAYMASLKKLLSLGPG-RIYPGHGP 186
metallo-hydrolase-like_MBL-fold cd06262
mainly hydrolytic enzymes and related proteins which carry out various biological functions; ...
 33-191 1.23e-30

mainly hydrolytic enzymes and related proteins which carry out various biological functions; MBL-fold metallohydrolase domain; Members of the MBL-fold metallohydrolase superfamily are mainly hydrolytic enzymes which carry out a variety of biological functions. The class B metal beta-lactamases (MBLs) for which this fold was named perform only a small fraction of the activities included in this superfamily. Activities carried out by superfamily members include class B beta-lactamases which can catalyze the hydrolysis of a wide range of beta-lactam antibiotics, hydroxyacylglutathione hydrolases (also called glyoxalase II) which hydrolyze S-d-lactoylglutathione to d-lactate in the second step of the glycoxlase system, AHL lactonases which catalyze the hydrolysis and opening of the homoserine lactone rings of acyl homoserine lactones (AHLs), persulfide dioxygenase which catalyze the oxidation of glutathione persulfide to glutathione and persulfite in the mitochondria, flavodiiron proteins which catalyze the reduction of oxygen and/or nitric oxide to water or nitrous oxide respectively, cleavage and polyadenylation specificity factors such as the Int9 and Int11 subunits of Integrator, Sdsa1-like and AtsA-like arylsulfatases, 5'-exonucleases human SNM1A and yeast Pso2p, ribonuclease J which has both 5'-3' exoribonucleolytic and endonucleolytic activity and ribonuclease Z which catalyzes the endonucleolytic removal of the 3' extension of the majority of tRNA precursors, cyclic nucleotide phosphodiesterases which decompose cyclic adenosine and guanosine 3', 5'-monophosphate (cAMP and cGMP) respectively, insecticide hydrolases, and proteins required for natural transformation competence. The diversity of biological roles is reflected in variations in the active site metallo-chemistry, for example classical members of the superfamily are di-, or less commonly mono-, zinc-ion-dependent hydrolases, human persulfide dioxygenase ETHE1 is a mono-iron binding member of the superfamily; Arabidopsis thaliana hydroxyacylglutathione hydrolases incorporates iron, manganese, and zinc in its dinuclear metal binding site, and flavodiiron proteins contains a diiron site.


Pssm-ID: 293792 [Multi-domain]  Cd Length: 188  Bit Score: 112.76  E-value: 1.23e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495006367  33 GTNTWILHAPGSvECVVVDPGDNDEEHLQRVAGIGPVALT--LITHRHYDHTGGVDRFHELTSAPV----------RSVD 100
Cdd:cd06262    9 QTNCYLVSDEEG-EAILIDPGAGALEKILEAIEELGLKIKaiLLTHGHFDHIGGLAELKEAPGAPVyiheadaellEDPE 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495006367 101 PTFLRGGASALV---------DGEVIEVAGLKLRILATPGHTADSVSIVIENDASVLTGDTILGRGTAVLDDSDGDLGDY 171
Cdd:cd06262   88 LNLAFFGGGPLPppepdilleDGDTIELGGLELEVIHTPGHTPGSVCFYIEEEGVLFTGDTLFAGSIGRTDLPGGDPEQL 167

                        170       180
                 ....*....|....*....|.
gi 495006367 172 LTSLRS-LAALGEGLTVLPGH 191
Cdd:cd06262  168 IESIKKlLLLLPDDTVVYPGH 188
GloB COG0491
Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General ...
 26-220 1.31e-30

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: 113.25  E-value: 1.31e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495006367  26 PGMMTLDGTNTWILHAPGsvECVVVDPGDNDEEH---LQRVAGIG-PVALTLITHRHYDHTGGVDRFHELTSAPVR--SV 99
Cdd:COG0491    7 GTPGAGLGVNSYLIVGGD--GAVLIDTGLGPADAealLAALAALGlDIKAVLLTHLHPDHVGGLAALAEAFGAPVYahAA 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495006367 100 DPTFLRGGASA-------------LVDGEVIEVAGLKLRILATPGHTADSVSIVIENDASVLTGDTILGRGTAVLDDSDG 166
Cdd:COG0491   85 EAEALEAPAAGalfgrepvppdrtLEDGDTLELGGPGLEVIHTPGHTPGHVSFYVPDEKVLFTGDALFSGGVGRPDLPDG 164

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 495006367 167 DLGDYLTSLRSLAALgEGLTVLPGHGPDLPdlqaisqqylAHREERLDQVRAAL 220
Cdd:COG0491  165 DLAQWLASLERLLAL-PPDLVIPGHGPPTT----------AEAIDYLEELLAAL 207
hydroxyacylglutathione_hydrolase_MBL-fold cd07723
hydroxyacylglutathione hydrolase, MBL-fold metallo-hydrolase domain; hydroxyacylglutathione ...
 37-191 2.15e-28

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: 106.01  E-value: 2.15e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495006367  37 WILHAPGSVECVVVDPGDNDE--EHLQRvAGIGPVALtLITHRHYDHTGGVDRFHELT-SAPVRSVDPTFLRGGASALVD 113
Cdd:cd07723   12 YLIVDEATGEAAVVDPGEAEPvlAALEK-NGLTLTAI-LTTHHHWDHTGGNAELKALFpDAPVYGPAEDRIPGLDHPVKD 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495006367 114 GEVIEVAGLKLRILATPGHTADSVSIVIENDASVLTGDTIL----GR---GTAvlddsdgdlGDYLTSLRSLAALGEGLT 186
Cdd:cd07723   90 GDEIKLGGLEVKVLHTPGHTLGHICYYVPDEPALFTGDTLFsggcGRffeGTA---------EQMYASLQKLLALPDDTL 160


                 ....*
gi 495006367 187 VLPGH 191
Cdd:cd07723  161 VYCGH 165
GSH_gloB TIGR03413
hydroxyacylglutathione hydrolase; Members of this protein family are hydroxyacylglutathione ...
 37-225 7.59e-22

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: 91.06  E-value: 7.59e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495006367   37 WILHAPGSvECVVVDPGDND--EEHLQRvAGIGPVALtLITHRHYDHTGGVDRFHELTSAPVRSVDPTFLRGGASALVDG 114
Cdd:TIGR03413  13 WLLHDPDG-QAAVVDPGEAEpvLDALEA-RGLTLTAI-LLTHHHHDHVGGVAELLEAFPAPVYGPAEERIPGITHPVKDG 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495006367  115 EVIEVAGLKLRILATPGHTADSVSIVIENDASVLTGDTIL----GR---GTAvlddsdgdlGDYLTSLRSLAALGEGLTV 187
Cdd:TIGR03413  90 DTVTLGGLEFEVLAVPGHTLGHIAYYLPDSPALFCGDTLFsagcGRlfeGTP---------EQMYDSLQRLAALPDDTLV 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 495006367  188 LPGH-------------GPDLPDLqaisQQYLAHREERLDQVRAAL-STLGE 225
Cdd:TIGR03413 161 YCAHeytlsnlrfaltvEPDNPAL----QERLKEVEALRAQGQPTLpSTLGL 208
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 35-191 1.98e-21

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: 87.99  E-value: 1.98e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495006367    35 NTWILHAPGsvECVVVDPGDNDEEHLQRVA---GIGPVALTLITHRHYDHTGGVDRFHELTSAPVRS--------VDPTF 103
Cdd:smart00849   1 NSYLVRDDG--GAILIDTGPGEAEDLLAELkklGPKKIDAIILTHGHPDHIGGLPELLEAPGAPVYApegtaellKDLLA 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495006367   104 LRGGASA----------LVDGEVIEVAGLKLRILATPGHTADSVSIVIENDASVLTGDTILGRGTAVLDD--SDGDLGDY 171
Cdd:smart00849  79 LLGELGAeaepappdrtLKDGDELDLGGGELEVIHTPGHTPGSIVLYLPEGKILFTGDLLFAGGDGRTLVdgGDAAASDA 158

                          170       180
                   ....*....|....*....|
gi 495006367   172 LTSLRSLAALGEGlTVLPGH 191
Cdd:smart00849 159 LESLLKLLKLLPK-LVVPGH 177
POD-like_MBL-fold cd07724
ETHE1 (PDO type I), persulfide dioxygenase A (PDOA, PDO type II) and related proteins; ...
 33-192 7.43e-21

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: 86.68  E-value: 7.43e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495006367  33 GTNTWILHAPGSVECVVVDPG-DNDEEHLQRVAGIGpvaLTLI----THRHYDHTGGVDRFHELTSAPV---RSVDPTFl 104
Cdd:cd07724   11 GTLSYLVGDPETGEAAVIDPVrDSVDRYLDLAAELG---LKITyvleTHVHADHVSGARELAERTGAPIvigEGAPASF- 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495006367 105 rgGASALVDGEVIEVAGLKLRILATPGHTADSVSIVIENDASVLTGDTILGRGTA----VLDDSDGDLGDYLTSLRSLAA 180
Cdd:cd07724   87 --FDRLLKDGDVLELGNLTLEVLHTPGHTPESVSYLVGDPDAVFTGDTLFVGDVGrpdlPGEAEGLARQLYDSLQRKLLL 164

                        170
                 ....*....|..
gi 495006367 181 LGEGLTVLPGHG 192
Cdd:cd07724  165 LPDETLVYPGHD 176
TTHA1623-like_MBL-fold cd16322
uncharacterized Thermus thermophilus TTHA1623 and related proteins; MBL-fold metallo hydrolase ...
 35-193 7.50e-21

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: 87.40  E-value: 7.50e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495006367  35 NTWILHAPGSVECVVVDPGDNDEEHLQRVAGIGP-VALTLITHRHYDHTGGVDRFHELTSAPV--RSVDPTFLRGGASA- 110
Cdd:cd16322   12 NTYLVADEGGGEAVLVDPGDESEKLLARFGTTGLtLLYILLTHAHFDHVGGVADLRRHPGAPVylHPDDLPLYEAADLGa 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495006367 111 ----------------LVDGEVIEVAGLKLRILATPGHTADSVSIVIENDASVLTGDTILGRGTAVLDDSDGDLGDYLTS 174
Cdd:cd16322   92 kafglgieplpppdrlLEDGQTLTLGGLEFKVLHTPGHSPGHVCFYVEEEGLLFSGDLLFQGSIGRTDLPGGDPKAMAAS 171

                        170
                 ....*....|....*....
gi 495006367 175 LRSLAALGEGLTVLPGHGP 193
Cdd:cd16322  172 LRRLLTLPDETRVFPGHGP 190
TTHA1429-like_MBL-fold cd07725
uncharacterized Thermus thermophilus TTHA1429 and related proteins; MBL-fold metallo hydrolase ...
 73-192 2.28e-20

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: 85.43  E-value: 2.28e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495006367  73 LITHRHYDHTGGVDRFHELTSAPVRSVDPTFLRggasalvDGEVIEVAGLKLRILATPGHTADSVSIVIENDASVLTGDT 152
Cdd:cd07725   60 LLTHHHPDHIGLAGKLQEKSGATVYILDVTPVK-------DGDKIDLGGLRLKVIETPGHTPGHIVLYDEDRRELFVGDA 132

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 495006367 153 ILGRGTAVLDDSDGDL----GDYLTSLRSLAALgEGLTVLPGHG 192
Cdd:cd07725  133 VLPKITPNVSLWAVRVedplGAYLESLDKLEKL-DVDLAYPGHG 175
BaeB-like_MBL-fold cd16275
Bacillus amyloliquefaciens BaeB and related proteins; MBL-fold metallo hydrolase domain; ...
 46-153 2.36e-19

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: 82.58  E-value: 2.36e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495006367  46 ECVVVDPG-------DNDEEHLQRVAGIgpvaltLITHRHYDHTGGVDRFHELTSAPV--RSVDPTFLRGGASALV---D 113
Cdd:cd16275   24 EAAVVDPAwdiekilAKLNELGLTLTGI------LLTHSHFDHVNLVEPLLAKYDAPVymSKEEIDYYGFRCPNLIpleD 97

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 495006367 114 GEVIEVAGLKLRILATPGHTADSVSIVIENdaSVLTGDTI 153
Cdd:cd16275   98 GDTIKIGDTEITCLLTPGHTPGSMCYLLGD--SLFTGDTL 135
yflN-like_MBL-fold cd07721
uncharacterized subgroup which includes Bacillus subtilis yflN; MBL-fold metallo hydrolase ...
 35-192 3.89e-17

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


Pssm-ID: 293807 [Multi-domain]  Cd Length: 202  Bit Score: 77.26  E-value: 3.89e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495006367  35 NTWILHAPGSVecVVVDPGD-NDEEHLQRVA-----GIGPVALTLITHRHYDHTGGVDRFHELTSAPV------------ 96
Cdd:cd07721   12 NAYLIEDDDGL--TLIDTGLpGSAKRILKALrelglSPKDIRRILLTHGHIDHIGSLAALKEAPGAPVyahereapyleg 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495006367  97 ----------------RSVDPTFLRGGASALVDGEVIEVAGlKLRILATPGHTADSVSIVIENDASVLTGDTILGRGTAV 160
Cdd:cd07721   90 ekpypppvrlgllgllSPLLPVKPVPVDRTLEDGDTLDLAG-GLRVIHTPGHTPGHISLYLEEDGVLIAGDALVTVGGEL 168

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 495006367 161 LDDSDGDLGDYLTSLRSLAALGEgL---TVLPGHG 192
Cdd:cd07721  169 VPPPPPFTWDMEEALESLRKLAE-LdpeVLAPGHG 202
YcbL-like_MBL-fold cd07737
Salmonella enterica serovar typhimurium YcbL and related proteins; MBL-fold metallo hydrolase ...
 46-191 1.59e-12

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: 64.50  E-value: 1.59e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495006367  46 ECVVVDPGDNDEEHLQRVA--GIGPVALtLITHRHYDHTGGVDRFHELTSAPV--RSVDPTFL----------RGGASA- 110
Cdd:cd07737   23 EAAVIDPGGDADKILQAIEdlGLTLKKI-LLTHGHLDHVGGAAELAEHYGVPIigPHKEDKFLlenlpeqsqmFGFPPAe 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495006367 111 -------LVDGEVIEVAGLKLRILATPGHTADSVSIVIENDASVLTGDTI---------LGRGTavlddsdgdLGDYLTS 174
Cdd:cd07737  102 aftpdrwLEEGDTVTVGNLTLEVLHCPGHTPGHVVFFNRESKLAIVGDVLfkgsigrtdFPGGN---------HAQLIAS 172

                        170
                 ....*....|....*...
gi 495006367 175 LRS-LAALGEGLTVLPGH 191
Cdd:cd07737  173 IKEkLLPLGDDVTFIPGH 190
MBLAC2-like_MBL-fold cd07712
uncharacterized human metallo-beta-lactamase domain-containing protein 2 and related proteins; ...
 32-191 5.10e-11

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: 59.95  E-value: 5.10e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495006367  32 DGTNTWILHapGSVECVVVDPGDNDEEHLQRVAGIGPVALTLI-THRHYDHTGGVDRF---------------HELTSAP 95
Cdd:cd07712    7 DRVNIYLLR--GRDRALLIDTGLGIGDLKEYVRTLTDLPLLVVaTHGHFDHIGGLHEFeevyvhpadaeilaaPDNFETL 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495006367  96 VRSVDPTFLRGGASALV--DGEVIEVAGLKLRILATPGHTADSVSIVIENDASVLTGDTIlGRGTAVLDDSDGDLGDYLT 173
Cdd:cd07712   85 TWDAATYSVPPAGPTLPlrDGDVIDLGDRQLEVIHTPGHTPGSIALLDRANRLLFSGDVV-YDGPLIMDLPHSDLDDYLA 163

                        170
                 ....*....|....*....
gi 495006367 174 SLRSLAAL-GEGLTVLPGH 191
Cdd:cd07712  164 SLEKLSKLpDEFDKVLPGH 182
Lactamase_B pfam00753
Metallo-beta-lactamase superfamily;
29-191 6.88e-11

Metallo-beta-lactamase superfamily;


Pssm-ID: 425851 [Multi-domain]  Cd Length: 196  Bit Score: 60.07  E-value: 6.88e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495006367   29 MTLDGTNTWILHAPGsvECVVVDPGDNDEE------HLQRVAGIGPVALtLITHRHYDHTGGVDRFHELTSAPVRSVDPT 102
Cdd:pfam00753   1 LGPGQVNSYLIEGGG--GAVLIDTGGSAEAalllllAALGLGPKDIDAV-ILTHGHFDHIGGLGELAEATDVPVIVVAEE 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495006367  103 FLRGGASALV-----------------------DGEVIEVAGLKLRILATPGHTADSVSIVIENDASVLTGDTILGRGTA 159
Cdd:pfam00753  78 ARELLDEELGlaasrlglpgppvvplppdvvleEGDGILGGGLGLLVTHGPGHGPGHVVVYYGGGKVLFTGDLLFAGEIG 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 495006367  160 VLDDSDGDLGD--------YLTSLRSLAALGEgLTVLPGH 191
Cdd:pfam00753 158 RLDLPLGGLLVlhpssaesSLESLLKLAKLKA-AVIVPGH 196
PRK10241 PRK10241
hydroxyacylglutathione hydrolase; Provisional
 47-133 3.40e-10

hydroxyacylglutathione hydrolase; Provisional


Pssm-ID: 182327 [Multi-domain]  Cd Length: 251  Bit Score: 58.68  E-value: 3.40e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495006367  47 CVVVDPGDNdEEHLQRVA--GIGPVALtLITHRHYDHTGGV----DRFHELTS-APVRSVDPtflrgGASALV-DGEVIE 118
Cdd:PRK10241  24 CLIVDPGEA-EPVLNAIAenNWQPEAI-FLTHHHHDHVGGVkelvEKFPQIVVyGPQETQDK-----GTTQVVkDGETAF 96

                         90
                 ....*....|....*
gi 495006367 119 VAGLKLRILATPGHT 133
Cdd:PRK10241  97 VLGHEFSVFATPGHT 111
metallo-hydrolase-like_MBL-fold cd07743
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 46-158 4.83e-10

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: 57.54  E-value: 4.83e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495006367  46 ECVVVDPGdNDEEHLQRV------AGIGPVALtLITHRHYDHTGGVDRFHELTSAPVRS------------VDPTFLRGG 107
Cdd:cd07743   19 EALLIDSG-LDEDAGRKIrkileeLGWKLKAI-INTHSHADHIGGNAYLQKKTGCKVYApkiekafienplLEPSYLGGA 96

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 495006367 108 -----------------ASALVDGEVIEVAGLKLRILATPGHTADSVSIVIENDasVL-TGDTILGRGT 158
Cdd:cd07743   97 yppkelrnkflmakpskVDDIIEEGELELGGVGLEIIPLPGHSFGQIGILTPDG--VLfAGDALFGEEV 163
MBLAC1-like_MBL-fold cd07711
uncharacterized human metallo-beta-lactamase domain-containing protein 1 and related proteins; ...
 48-193 1.56e-09

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: 56.05  E-value: 1.56e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495006367  48 VVVDPGD-NDEEHL-QRVA--GIGP--VALTLITHRHYDHTGGVD-----RFHELTSAPVRSVDPTFLRGGASALVDGEV 116
Cdd:cd07711   34 ILVDTGTpWDRDLLlKALAehGLSPedIDYVVLTHGHPDHIGNLNlfpnaTVIVGWDICGDSYDDHSLEEGDGYEIDENV 113

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495006367 117 ievaglklRILATPGHTADSVSIVIENDAS---VLTGDTILGRGTAVLDDSDGDLGDYLTSLRS-------LAALgeglt 186
Cdd:cd07711  114 --------EVIPTPGHTPEDVSVLVETEKKgtvAVAGDLFEREEDLEDPILWDPLSEDPELQEEsrkrilaLADW----- 180


                 ....*..
gi 495006367 187 VLPGHGP 193
Cdd:cd07711  181 IIPGHGP 187
PLN02398 PLN02398
hydroxyacylglutathione hydrolase
 71-208 1.97e-09

hydroxyacylglutathione hydrolase


Pssm-ID: 215223 [Multi-domain]  Cd Length: 329  Bit Score: 57.16  E-value: 1.97e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495006367  71 LTLI--THRHYDHTGGVDRFHELTSAPV--RSVDPTFLRGGASALVDGEVIEVAGLKLRILATPGHTADSVSIVIENDAS 146
Cdd:PLN02398 122 LTYIlnTHHHYDHTGGNLELKARYGAKVigSAVDKDRIPGIDIVLKDGDKWMFAGHEVLVMETPGHTRGHISFYFPGSGA 201

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 495006367 147 VLTGDTI-------LGRGTAvlddsdgdlGDYLTSLRSLAALGEGLTVLPGHGPDLPDLQ-AIS--------QQYLAH 208
Cdd:PLN02398 202 IFTGDTLfslscgkLFEGTP---------EQMLSSLQKIISLPDDTNIYCGHEYTLSNSKfALSiepnnevlQSYAAH 270
AHL_lactonase_MBL-fold cd07729
quorum-quenching N-acyl-homoserine lactonase, MBL-fold metallo-hydrolase domain; Acyl ...
 57-191 2.71e-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: 56.07  E-value: 2.71e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495006367  57 EEHLQRVaGIGP--VALTLITHRHYDHTGGVDRF---------HELTSA-----------PVRSVDPTFLRGGASALVDG 114
Cdd:cd07729   76 EEQLARL-GLDPedIDYVILSHLHFDHAGGLDLFpnatiivqrAELEYAtgpdplaagyyEDVLALDDDLPGGRVRLVDG 154

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495006367 115 EViEVAGlKLRILATPGHTADSVSIVIENDAS--VLTGDTI-----LGRGtaVLDDSDGDLGDYLTSLRSLAAL--GEGL 185
Cdd:cd07729  155 DY-DLFP-GVTLIPTPGHTPGHQSVLVRLPEGtvLLAGDAAytyenLEEG--RPPGINYDPEAALASLERLKALaeREGA 230


                 ....*.
gi 495006367 186 TVLPGH 191
Cdd:cd07729  231 RVIPGH 236
MBL-B3-like cd07708
metallo-beta-lactamases, subclass B3; MBL-fold metallo-hydrolase domain; MBLs (class B of the ...
 16-138 4.41e-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: 55.63  E-value: 4.41e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495006367  16 DIASVLLENNPGMMTLDGT---NTWILHApgSVECVVVDPGDndeehlqrvagigpVALTLITHRHYDHTGGVDRFHELT 92
Cdd:cd07708   21 DLAAYLIVTPQGNILIDGDmeqNAPMIKA--NIKKLGFKFSD--------------TKLILISHAHFDHAGGSAEIKKQT 84

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 495006367  93 SAPVRSVD---PTFLRGGAS-------------------ALVDGEVIEVAGLKLRILATPGHTADSVS 138
Cdd:cd07708   85 GAKVMAGAedvSLLLSGGSSdfhyandsstyfpqstvdrAVHDGERVTLGGTVLTAHATPGHTPGCTT 152
SMB-1-like_MBL-B3 cd16313
SMB-1, THIN-B and related metallo-beta-lactamases, subclass B3; MBL-fold metallo-hydrolase ...
 17-138 1.90e-07

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


Pssm-ID: 293871 [Multi-domain]  Cd Length: 254  Bit Score: 50.63  E-value: 1.90e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495006367  17 IASVLLENNPGMMTLDGTntwilhAPGSVECVVVDpgdndeehlQRVAGIGP--VALTLITHRHYDHTGGVDRFHELTSA 94
Cdd:cd16313   22 ISAVLITSPQGHILIDGG------FPKSPEQIAAS---------IRQLGFKLedVKYILSSHDHWDHAGGIAALQKLTGA 86

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 495006367  95 PV----------RS-----VDPTF-----LRGGAS--ALVDGEVIEVAGLKLRILATPGHTADSVS 138
Cdd:cd16313   87 QVlaspatvavlRSgsmgkDDPQFggltpMPPVASvrAVRDGEVVKLGPLAVTAHATPGHTTGGTS 152
metallo-hydrolase-like_MBL-fold cd16280
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 73-142 2.88e-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: 293838 [Multi-domain]  Cd Length: 251  Bit Score: 50.28  E-value: 2.88e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495006367  73 LITHRHYDHTGGVDRFHELTSAPV--------RSVDPTFLRGGASA---------LVDGEVIEVAGLKLRILATPGHTAD 135
Cdd:cd16280   66 LITHGHGDHYGGAAYLKDLYGAKVvmseadwdMMEEPPEEGDNPRWgppperdivIKDGDTLTLGDTTITVYLTPGHTPG 145


                 ....*..
gi 495006367 136 SVSIVIE 142
Cdd:cd16280  146 TLSLIFP 152
metallo-hydrolase-like_MBL-fold cd16282
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 47-193 1.11e-06

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


Pssm-ID: 293840 [Multi-domain]  Cd Length: 209  Bit Score: 47.95  E-value: 1.11e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495006367  47 CVVVDPGDND---EEHLQRVAGI--GPVALTLITHRHYDHTGGVDRF---------HELTSAPVRSVDPTFLR------- 105
Cdd:cd16282   26 VVVIDTGASPrlaRALLAAIRKVtdKPVRYVVNTHYHGDHTLGNAAFadagapiiaHENTREELAARGEAYLElmrrlgg 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495006367 106 --GGASALV-------DGEVIEVAGLKLRILAT-PGHTADSVSIVIENDASVLTGDTILGRGTAVldDSDGDLGDYLTSL 175
Cdd:cd16282  106 daMAGTELVlpdrtfdDGLTLDLGGRTVELIHLgPAHTPGDLVVWLPEEGVLFAGDLVFNGRIPF--LPDGSLAGWIAAL 183

                        170
                 ....*....|....*...
gi 495006367 176 RSLAALGEGlTVLPGHGP 193
Cdd:cd16282  184 DRLLALDAT-VVVPGHGP 200
GOB1-like_MBL-B3 cd16308
Elizabethkingia meningoseptica GOB-1 and related metallo-beta-lactamases, subclass B3; ...
 73-142 1.96e-06

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: 47.85  E-value: 1.96e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495006367  73 LITHRHYDHTGGVDRFHELTSAP--VRSVDPTFLR-GGAS------------------ALVDGEVIEVAGLKLRILATPG 131
Cdd:cd16308   65 LTTQAHYDHVGAMAAIKQQTGAKmmVDEKDAKVLAdGGKSdyemggygstfapvkadkLLHDGDTIKLGGTKLTLLHHPG 144

                         90
                 ....*....|.
gi 495006367 132 HTADSVSIVIE 142
Cdd:cd16308  145 HTKGSCSFLFD 155
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 ...
 17-138 2.02e-06

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


Pssm-ID: 293848 [Multi-domain]  Cd Length: 256  Bit Score: 47.73  E-value: 2.02e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495006367  17 IASVLLENNPGMMTLDGTntwilhAPGSVECVvvdpgdndEEHLQRVA-GIGPVALTLITHRHYDHTGGVDRFHELTSAP 95
Cdd:cd16290   22 LSAVLITSPQGLILIDGA------LPQSAPQI--------EANIRALGfRLEDVKLILNSHAHFDHAGGIAALQRDSGAT 87

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 495006367  96 VRSVDP--TFLRGGAS--------------------ALVDGEVIEVAGLKLRILATPGHTADSVS 138
Cdd:cd16290   88 VAASPAgaAALRSGGVdpddpqagaadpfppvakvrVVADGEVVKLGPLAVTAHATPGHTPGGTS 152
ST1585-like_MBL-fold cd07726
uncharacterized subgroup which includes Sulfolobus tokodaii ST1585 protein; MBL-fold metallo ...
 36-152 2.92e-06

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: 46.72  E-value: 2.92e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495006367  36 TWILHAPGsvECVVVDPG-----DNDEEHLQRvAGIGPVALT--LITHRHYDHTGGVDRFHE-LTSAPVR--------SV 99
Cdd:cd07726   18 SYLLDGEG--RPALIDTGpsssvPRLLAALEA-LGIAPEDVDyiILTHIHLDHAGGAGLLAEaLPNAKVYvhprgarhLI 94

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 495006367 100 DPTFLRGGASALV-----------------------DGEVIEVAGLKLRILATPGHTADSVSIVIENDASVLTGDT 152
Cdd:cd07726   95 DPSKLWASARAVYgdeadrlggeilpvpeervivleDGETLDLGGRTLEVIDTPGHAPHHLSFLDEESDGLFTGDA 170
AIM-1-like_MBL-B3 cd16314
Pseudomonas Aeruginosa AIM-1 and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 62-138 2.95e-06

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: 47.19  E-value: 2.95e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495006367  62 RVAGIGPVALTLI--THRHYDHTGGVDRFHELTSAPV----------------RSvDPTFLRGGASALV-------DGEV 116
Cdd:cd16314   52 RALGFRPEDVRYIvsSHEHFDHAGGIARLQRATGAPVvarepaattlergrsdRS-DPQFLVVEKFPPVasvqrigDGEV 130

                         90       100
                 ....*....|....*....|..
gi 495006367 117 IEVAGLKLRILATPGHTADSVS 138
Cdd:cd16314  131 LRVGPLALTAHATPGHTPGGTS 152
arylsulfatase_Sdsa1-like_MBL-fold cd07710
Pseudomonas aeruginosa arylsulfatase SdsA1, Pseudomonas sp. DSM6611 arylsulfatase Pisa1, and ...
 48-160 1.06e-05

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: 45.57  E-value: 1.06e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495006367  48 VVVDPGDNDE------EHLQRVAGIGPVALTLITHRHYDHTGGVDRF-------------HE------------------ 90
Cdd:cd07710   30 IIIDTLESAEaakaalELFRKHTGDKPVKAIIYTHSHPDHFGGAGGFveeedsgkvpiiaPEgfmeeavsenvlagnams 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495006367  91 ----------LTSAPVRSVD----PTFLRGGASAL-------VDGEVIEVAGLKLRILATPGHTADSVSIVIENDASVLT 149
Cdd:cd07710  110 rraayqfgalLPKGEKGQVGaglgPGLSTGTVGFIpptititETGETLTIDGVELEFQHAPGEAPDEMMVWLPDYKVLFC 189

                        170
                 ....*....|....*....
gi 495006367 150 GDTILG--------RGTAV 160
Cdd:cd07710  190 ADNVYHtfpnlytlRGAKY 208
EVM-1-like_MBL-B3 cd16315
Erythrobacter vulgaris EVM-1 and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 69-138 2.19e-05

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: 44.65  E-value: 2.19e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495006367  69 VALTLITHRHYDHTGGVDRFHELTSAPVRSV---------------DPTFlrGGASA---------LVDGEVIEVAGLKL 124
Cdd:cd16315   61 VRWLLSSHEHFDHVGGLAALQRATGARVAASaaaapvlesgkpapdDPQA--GLHEPfppvrvdriVEDGDTVALGSLRL 138

                         90
                 ....*....|....
gi 495006367 125 RILATPGHTADSVS 138
Cdd:cd16315  139 TAHATPGHTPGALS 152
PLN02469 PLN02469
hydroxyacylglutathione hydrolase
 22-153 2.69e-05

hydroxyacylglutathione hydrolase


Pssm-ID: 178088 [Multi-domain]  Cd Length: 258  Bit Score: 44.37  E-value: 2.69e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495006367  22 LENNPGMMTLDGTntwilhapgSVECVVVDPGDNDEehLQRVAGIGPVALTLI--THRHYDHTGGVDRFHELTSA-PVR- 97
Cdd:PLN02469   9 LEDNYAYLIIDES---------TKDAAVVDPVDPEK--VLQAAHEHGAKIKLVltTHHHWDHAGGNEKIKKLVPGiKVYg 77

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 495006367  98 -SVDPtfLRGGASALVDGEVIEVaGLKLRILA--TPGHTADSVSIVIEN----DASVLTGDTI 153
Cdd:PLN02469  78 gSLDN--VKGCTHPVENGDKLSL-GKDVNILAlhTPCHTKGHISYYVTGkegeDPAVFTGDTL 137
NDM_FIM-like_MBL-B1 cd16300
NDM-1, FIM-1 and related metallo-beta-lactamases, subclass B1; MBL-fold metallo-hydrolase ...
 48-193 6.55e-05

NDM-1, FIM-1 and related metallo-beta-lactamases, subclass B1; MBL-fold metallo-hydrolase domain; Includes the ISCR-mediated MBLs NDM-1 (NDM (New Delhi metallo-beta-lactamase) and FIM-1 (Florence imipenemase). MBLs (class B of the Ambler beta-lactamase classification) are a diverse group of metallo-enzymes that are capable of catalyzing the hydrolysis of a wide range of beta-lactam antibiotics. MBLs have been divided into three subclasses B1, B2 and B3, based on sequence/structural relationships and substrates, with the B1 and B2 MBLs being most closely related to each other. This subgroup of MBLs belongs to the B1 subclass. B1 enzymes are most active with two zinc ions bound in the active site, and have a broad-spectrum substrate profile.


Pssm-ID: 293858  Cd Length: 214  Bit Score: 42.88  E-value: 6.55e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495006367  48 VVVDPGDNDEEHLQRVAGIG-----PVALTLITHRHYDHTGGVDRFHEL-----------TSAPVRSVDP-----TFLRG 106
Cdd:cd16300   39 LLVDTAWTDDQTAQILNWAKqelnlPVRLAVVTHAHQDKMGGMDALHAAgiatyanalsnQLAPQEGLVPaqhslTFAAE 118

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495006367 107 GASALVDGEVIEVAGlklrilatPGHTADSVSIVIENDASVLTGDTIL-GRGTAVLDDSDGDLGDYLTSLRSLA-ALGEG 184
Cdd:cd16300  119 PSTAPNFPLKVFYPG--------PGHTRDNIVVGIDGTGIAFGGCLIRpSKATSLGNLADADTEHWAASARAFGaAFPDA 190


                 ....*....
gi 495006367 185 LTVLPGHGP 193
Cdd:cd16300  191 SMIVPSHGA 199
BJP-1_FEZ-1-like_MBL-B3 cd16288
BJP-1, FEZ-1, GOB-1, Mbl1b and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 15-133 1.05e-04

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: 42.69  E-value: 1.05e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495006367  15 TDIASVLLENNPGMMTLDG---TNTWILHApgSVECVVVDPGDndeehlqrvagigpVALTLITHRHYDHTGGVDRFHEL 91
Cdd:cd16288   20 SGLASYLITTPQGLILIDTgleSSAPMIKA--NIRKLGFKPSD--------------IKILLNSHAHLDHAGGLAALKKL 83

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 495006367  92 TSAPVRSVD---PTFLRGGAS------------------ALVDGEVIEVAGLKLRILATPGHT 133
Cdd:cd16288   84 TGAKLMASAedaALLASGGKSdfhygddslafppvkvdrVLKDGDRVTLGGTTLTAHLTPGHT 146
YmaE-like_MBL-fold cd07727
uncharacterized subgroup which includes Bacillus subtilis YmaE and related proteins; MBL-fold ...
 33-192 1.19e-04

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: 41.80  E-value: 1.19e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495006367  33 GTNTWILHAPGSVecVVVDPGDNDEEHLQRVAGIGPVALTLITHRHY--DHTGGVDRF------HEL-TSAPVRSVDPTF 103
Cdd:cd07727   14 GAASYLILRPEGN--ILVDSPRYSPPLAKRIEALGGIRYIFLTHRDDvaDHAKWAERFgakriiHEDdVNAVTRPDEVIV 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495006367 104 LRGGASALVDGEVievaglklRILATPGHTADSVSIVIENDASVLTGDTI-----LGRGTAVLDDSDGDLGDYLTSLRSL 178
Cdd:cd07727   92 LWGGDPWELDPDL--------TLIPVPGHTRGSVVLLYKEKGVLFTGDHLawsrrRGWLSAFRYVCWYSWPEQAESVERL 163

                        170
                 ....*....|....
gi 495006367 179 AALGEgLTVLPGHG 192
Cdd:cd07727  164 ADLDF-EWVLPGHG 176
BJP-1-like_MBL-B3 cd16309
Bradyrhizobium diazoefficiens BJP-1 and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 69-133 2.31e-04

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: 41.32  E-value: 2.31e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495006367  69 VALTLITHRHYDHTGGVDRFHELTSAPV--RSVDPTFLRGGA-----------------SALVDGEVIEVAGLKLRILAT 129
Cdd:cd16309   61 VKYLLNTHAHFDHAGGLAELKKATGAQLvaSAADKPLLESGYvgsgdtknlqfppvrvdRVIGDGDKVTLGGTTLTAHLT 140


                 ....
gi 495006367 130 PGHT 133
Cdd:cd16309  141 PGHS 144
PLN02962 PLN02962
hydroxyacylglutathione hydrolase
 48-157 5.94e-04

hydroxyacylglutathione hydrolase


Pssm-ID: 178547 [Multi-domain]  Cd Length: 251  Bit Score: 40.17  E-value: 5.94e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495006367  48 VVVDPGDNDEEhlQRVAGIGPVALTLI----THRHYDHTGGVDRFHelTSAP-VRSVDPTFLRGGASALVD-GEVIEVAG 121
Cdd:PLN02962  39 LLIDPVDKTVD--RDLSLVKELGLKLIyamnTHVHADHVTGTGLLK--TKLPgVKSIISKASGSKADLFVEpGDKIYFGD 114

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 495006367 122 LKLRILATPGHTADSVSIVIENDAS------VLTGDTILGRG 157
Cdd:PLN02962 115 LYLEVRATPGHTAGCVTYVTGEGPDqpqprmAFTGDALLIRG 156
metallo-hydrolase-like_MBL-fold cd16277
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 58-153 6.62e-04

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


Pssm-ID: 293835 [Multi-domain]  Cd Length: 222  Bit Score: 39.81  E-value: 6.62e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495006367  58 EHLQRvAGIGP--VALTLITHRHYDHTG------------------------GVDRFHELTSAPVR-------SVDPTFL 104
Cdd:cd16277   52 ERLAA-AGVRPedVDYVLCTHLHVDHVGwntrlvdgrwvptfpnarylfsraEYDHWSSPDAGGPPnrgvfedSVLPVIE 130

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 495006367 105 RGGASALVDGEVIeVAGLklRILATPGHTADSVSIVIEN--DASVLTGDTI 153
Cdd:cd16277  131 AGLADLVDDDHEI-LDGI--RLEPTPGHTPGHVSVELESggERALFTGDVM 178
Mbl1b-like_MBL-B3 cd16310
Caulobacter crescentus Mbl1b and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 69-133 1.01e-03

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: 39.74  E-value: 1.01e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495006367  69 VALTLITHRHYDHTGGVDRFHELTSAPVRSVDP--TFLRGGASA------------------LVDGEVIEVAGLKLRILA 128
Cdd:cd16310   61 IKIIINTHAHYDHAGGLAQLKADTGAKLWASRGdrPALEAGKHIgdnitqpapfpavkvdriLGDGEKIKLGDITLTATL 140


                 ....*
gi 495006367 129 TPGHT 133
Cdd:cd16310  141 TPGHT 145
UlaG COG2220
L-ascorbate lactonase UlaG, metallo-beta-lactamase superfamily [Carbohydrate transport and ...
 26-157 1.60e-03

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


Pssm-ID: 441822 [Multi-domain]  Cd Length: 224  Bit Score: 38.74  E-value: 1.60e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495006367  26 PGMMTLD--GTNTWILHAPGSVecVVVDPGDNDEEHLQRVAGIGPVALT-----LITHRHYDHtggvdrFHELTSAPVRS 98
Cdd:COG2220    1 PGGMKITwlGHATFLIETGGKR--ILIDPVFSGRASPVNPLPLDPEDLPkidavLVTHDHYDH------LDDATLRALKR 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495006367  99 VDPTFL--RGGASALVD-----------GEVIEVAGLKLRilATPGH---------TADSVSIVIENDASVL--TGDTIL 154
Cdd:COG2220   73 TGATVVapLGVAAWLRAwgfprvteldwGESVELGGLTVT--AVPARhssgrpdrnGGLWVGFVIETDGKTIyhAGDTGY 150


                 ...
gi 495006367 155 GRG 157
Cdd:COG2220  151 FPE 153
ComA-like_MBL-fold cd07731
Competence protein ComA, ComEC and related proteins; MBL-fold metallo hydrolase domain; This ...
 48-151 1.73e-03

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: 38.27  E-value: 1.73e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495006367  48 VVVDPGDNDEEHLQRVA------GIGPVALTLITHRHYDHTGGVD----RF--HELTSAPVRSVDPTFLR---------G 106
Cdd:cd07731   22 ILIDTGPRDSFGEDVVVpylkarGIKKLDYLILTHPDADHIGGLDavlkNFpvKEVYMPGVTHTTKTYEDlldaikekgI 101

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 495006367 107 GASALVDGEVIEVAGLKLRILATPGHTADSV---SIVIE---NDASVL-TGD 151
Cdd:cd07731  102 PVTPCKAGDRWQLGGVSFEVLSPPKDDYDDLnnnSCVLRltyGGTSFLlTGD 153
L1_POM-1-like_MBL-B3 cd16289
Stenotrophomonas maltophilia L1, Pseudomonas otitidis POM-1 and related ...
 62-138 2.93e-03

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: 38.26  E-value: 2.93e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495006367  62 RVAGIGPVALTLI--THRHYDHTGGVDRFHELTSAPVRSVDPT---FLRGGAS-----------------ALVDGEVIEV 119
Cdd:cd16289   52 RALGVAPGDLKLIlhSHAHADHAGPLAALKRATGARVAANAESavlLARGGSDdihfgdgitfppvqadrIVMDGEVVTL 131

                         90
                 ....*....|....*....
gi 495006367 120 AGLKLRILATPGHTADSVS 138
Cdd:cd16289  132 GGVTFTAHFTPGHTPGSTS 150
PhnP COG1235
Phosphoribosyl 1,2-cyclic phosphate phosphodiesterase [Inorganic ion transport and metabolism]; ...
 73-144 3.07e-03

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


Pssm-ID: 440848 [Multi-domain]  Cd Length: 259  Bit Score: 37.95  E-value: 3.07e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495006367  73 LITHRHYDHTGGVDRF-------------HELTSAPVRSVDPTFLRGGASAL-----VDGEVIEVAGLKLRILATPGHTA 134
Cdd:COG1235   73 LLTHEHADHIAGLDDLrprygpnpipvyaTPGTLEALERRFPYLFAPYPGKLefheiEPGEPFEIGGLTVTPFPVPHDAG 152

                         90
                 ....*....|
gi 495006367 135 DSVSIVIEND 144
Cdd:COG1235  153 DPVGYRIEDG 162
THIN-B2-like_MBL-B3 cd16311
Janthinobacterium lividum THIN-B2 and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 66-138 4.07e-03

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: 37.66  E-value: 4.07e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495006367  66 IGPVALTLITHRHYDHTGGVDRFHELTSAPVrSVDPTFLRGGASALV-----------------------DGEVIEVAGL 122
Cdd:cd16311   58 IEDVKLILNSHGHIDHAGGLAELQRRSGALV-AASPSAALDLASGEVgpddpqyhalpkyppvkdmrlarDGGQFNVGPV 136

                         90
                 ....*....|....*.
gi 495006367 123 KLRILATPGHTADSVS 138
Cdd:cd16311  137 SLTAHATPGHTPGGLS 152
Lactamase_B_2 pfam12706
Beta-lactamase superfamily domain; This family is part of the beta-lactamase superfamily and ...
 59-132 5.61e-03

Beta-lactamase superfamily domain; This family is part of the beta-lactamase superfamily and is related to pfam00753.


Pssm-ID: 432732 [Multi-domain]  Cd Length: 196  Bit Score: 36.90  E-value: 5.61e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495006367   59 HLQRVAGIGPVALTLITHRHYDHTGGVDRFHELTSAPV------------RSVDPTFLRGGASALVD---GEVIEVAGLK 123
Cdd:pfam12706  19 LQPGRLRDDPIDAVLLTHDHYDHLAGLLDLREGRPRPLyaplgvlahlrrNFPYLFLLEHYGVRVHEidwGESFTVGDGG 98


                  ....*....
gi 495006367  124 LRILATPGH 132
Cdd:pfam12706  99 LTVTATPAR 107
BLACT_WH pfam17778
Beta-lactamase associated winged helix domain; This winged helix domain is found at the ...
 228-261 6.11e-03

Beta-lactamase associated winged helix domain; This winged helix domain is found at the C-terminus of some beta lactamase enzymes.


Pssm-ID: 407650  Cd Length: 46  Bit Score: 34.13  E-value: 6.11e-03
                          10        20        30
                  ....*....|....*....|....*....|....
gi 495006367  228 SVRDVVEHVYSDVDPKLWPVAEKSVNVQLAYLRR 261
Cdd:pfam17778   1 TAMELVKVIYKDVPESLHPAAERGVLAHLEKLEA 34
 
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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