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Conserved domains on  [gi|1395168515|ref|NP_001350943|]
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persulfide dioxygenase ETHE1, mitochondrial precursor [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PLN02962 super family cl30130
hydroxyacylglutathione hydrolase
 13-254 4.91e-127

hydroxyacylglutathione hydrolase


The actual alignment was detected with superfamily member PLN02962:

Pssm-ID: 178547 [Multi-domain]  Cd Length: 251  Bit Score: 360.27  E-value: 4.91e-127
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168515  13 LSQQSASGAPVLLRQMFEPKSCTYTYLLGD--RESREAVLIDPVLETAHRDAQLIKELGLKLLYAVNTHCHADHITGTGV 90
Cdd:PLN02962    1 SSSSSSSSSKLLFRQLFEKESSTYTYLLADvsHPDKPALLIDPVDKTVDRDLSLVKELGLKLIYAMNTHVHADHVTGTGL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168515  91 LRSLLPGCQSVISRLSGAQADLHIGEGDSIRFGRFALETRASPGHTPGCVTFVLNDQS------MAFTGDALLIRGCGRT 164
Cdd:PLN02962   81 LKTKLPGVKSIISKASGSKADLFVEPGDKIYFGDLYLEVRATPGHTAGCVTYVTGEGPdqpqprMAFTGDALLIRGCGRT 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168515 165 DFQQGCAKTLYHSVHEKIFTLPGNCLIYPAHDYHGLTVSTVEEERTLNPRLTLSCEEFIKVMDNLNLPKPQQIDIAVPAN 244
Cdd:PLN02962  161 DFQGGSSDQLYKSVHSQIFTLPKDTLIYPAHDYKGFTVSTVGEEMLYNPRLTKDEETFKTIMENLNLPYPKMIDVAVPAN 240

                         250
                  ....*....|
gi 1395168515 245 MRCGVQTPPS 254
Cdd:PLN02962  241 MVCGLQDPPA 250
 
Name Accession Description Interval E-value
PLN02962 PLN02962
hydroxyacylglutathione hydrolase
 13-254 4.91e-127

hydroxyacylglutathione hydrolase


Pssm-ID: 178547 [Multi-domain]  Cd Length: 251  Bit Score: 360.27  E-value: 4.91e-127
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168515  13 LSQQSASGAPVLLRQMFEPKSCTYTYLLGD--RESREAVLIDPVLETAHRDAQLIKELGLKLLYAVNTHCHADHITGTGV 90
Cdd:PLN02962    1 SSSSSSSSSKLLFRQLFEKESSTYTYLLADvsHPDKPALLIDPVDKTVDRDLSLVKELGLKLIYAMNTHVHADHVTGTGL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168515  91 LRSLLPGCQSVISRLSGAQADLHIGEGDSIRFGRFALETRASPGHTPGCVTFVLNDQS------MAFTGDALLIRGCGRT 164
Cdd:PLN02962   81 LKTKLPGVKSIISKASGSKADLFVEPGDKIYFGDLYLEVRATPGHTAGCVTYVTGEGPdqpqprMAFTGDALLIRGCGRT 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168515 165 DFQQGCAKTLYHSVHEKIFTLPGNCLIYPAHDYHGLTVSTVEEERTLNPRLTLSCEEFIKVMDNLNLPKPQQIDIAVPAN 244
Cdd:PLN02962  161 DFQGGSSDQLYKSVHSQIFTLPKDTLIYPAHDYKGFTVSTVGEEMLYNPRLTKDEETFKTIMENLNLPYPKMIDVAVPAN 240

                         250
                  ....*....|
gi 1395168515 245 MRCGVQTPPS 254
Cdd:PLN02962  241 MVCGLQDPPA 250
POD-like_MBL-fold cd07724
ETHE1 (PDO type I), persulfide dioxygenase A (PDOA, PDO type II) and related proteins; ...
 24-197 1.96e-82

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: 244.23  E-value: 1.96e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168515  24 LLRQMFEPKSCTYTYLLGDRESREAVLIDPVLETAHRDAQLIKELGLKLLYAVNTHCHADHITGTGVLRSLLpGCQSVIS 103
Cdd:cd07724     1 IFRQFFDPGLGTLSYLVGDPETGEAAVIDPVRDSVDRYLDLAAELGLKITYVLETHVHADHVSGARELAERT-GAPIVIG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168515 104 RLSGA-QADLHIGEGDSIRFGRFALETRASPGHTPGCVTFVLNDQSMAFTGDALLIRGCGRTDFQQ---GCAKTLYHSVH 179
Cdd:cd07724    80 EGAPAsFFDRLLKDGDVLELGNLTLEVLHTPGHTPESVSYLVGDPDAVFTGDTLFVGDVGRPDLPGeaeGLARQLYDSLQ 159

                         170
                  ....*....|....*...
gi 1395168515 180 EKIFTLPGNCLIYPAHDY 197
Cdd:cd07724   160 RKLLLLPDETLVYPGHDY 177
GloB COG0491
Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General ...
 35-197 1.75e-38

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: 133.66  E-value: 1.75e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168515  35 TYTYLLGDreSREAVLIDPVLETAHRDA--QLIKELGLKLLYAVNTHCHADHITGTGVLRSLLpGCQSVISR-------- 104
Cdd:COG0491    15 VNSYLIVG--GDGAVLIDTGLGPADAEAllAALAALGLDIKAVLLTHLHPDHVGGLAALAEAF-GAPVYAHAaeaealea 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168515 105 --------LSGAQADLHIGEGDSIRFGRFALETRASPGHTPGCVTFVLNDQSMAFTGDALLIRGCGRTDFQQGCAKTLYH 176
Cdd:COG0491    92 paagalfgREPVPPDRTLEDGDTLELGGPGLEVIHTPGHTPGHVSFYVPDEKVLFTGDALFSGGVGRPDLPDGDLAQWLA 171

                         170       180
                  ....*....|....*....|.
gi 1395168515 177 SVhEKIFTLPGNcLIYPAHDY 197
Cdd:COG0491   172 SL-ERLLALPPD-LVIPGHGP 190
GSH_gloB TIGR03413
hydroxyacylglutathione hydrolase; Members of this protein family are hydroxyacylglutathione ...
 36-197 2.49e-25

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: 99.92  E-value: 2.49e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168515  36 YTYLLGDrESREAVLID-----PVLETahrdaqlIKELGLKLLYAVNTHCHADHITGTGVLRSLLPgCQsVI----SRLS 106
Cdd:TIGR03413  11 YIWLLHD-PDGQAAVVDpgeaePVLDA-------LEARGLTLTAILLTHHHHDHVGGVAELLEAFP-AP-VYgpaeERIP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168515 107 GAqaDLHIGEGDSIRFGRFALETRASPGHTPGCVTFVLNDQSMAFTGDALLIRGCGRTdFqQGCAKTLYHSVhEKIFTLP 186
Cdd:TIGR03413  81 GI--THPVKDGDTVTLGGLEFEVLAVPGHTLGHIAYYLPDSPALFCGDTLFSAGCGRL-F-EGTPEQMYDSL-QRLAALP 155

                         170
                  ....*....|.
gi 1395168515 187 GNCLIYPAHDY 197
Cdd:TIGR03413 156 DDTLVYCAHEY 166
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 36-195 1.74e-24

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: 96.08  E-value: 1.74e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168515   36 YTYLLGDREsrEAVLIDPVLETAHRDAQLIKELGL-KLLYAVNTHCHADHITGTGVL------------------RSLLP 96
Cdd:smart00849   1 NSYLVRDDG--GAILIDTGPGEAEDLLAELKKLGPkKIDAIILTHGHPDHIGGLPELleapgapvyapegtaellKDLLA 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168515   97 GCQSVISRLSGAQADLHIGEGDSIRFGRFALETRASPGHTPGCVTFVLNDQSMAFTGDALLIRGCGRTDFQQG-CAKTLY 175
Cdd:smart00849  79 LLGELGAEAEPAPPDRTLKDGDELDLGGGELEVIHTPGHTPGSIVLYLPEGKILFTGDLLFAGGDGRTLVDGGdAAASDA 158

                          170       180
                   ....*....|....*....|
gi 1395168515  176 HSVHEKIFTLPGNcLIYPAH 195
Cdd:smart00849 159 LESLLKLLKLLPK-LVVPGH 177
Lactamase_B pfam00753
Metallo-beta-lactamase superfamily;
35-195 1.54e-18

Metallo-beta-lactamase superfamily;


Pssm-ID: 425851 [Multi-domain]  Cd Length: 196  Bit Score: 80.88  E-value: 1.54e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168515  35 TYTYLLGDREsrEAVLIDPVLETAHRDAQLIKELGLKLL---YAVNTHCHADHITGTGVLRSLLPGCQSVISRLSGAQAD 111
Cdd:pfam00753   6 VNSYLIEGGG--GAVLIDTGGSAEAALLLLLAALGLGPKdidAVILTHGHFDHIGGLGELAEATDVPVIVVAEEARELLD 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168515 112 LH-----------------------IGEGDSIRFGRFALETRASPGHTPGCVTFVLNDQSMAFTGDALLIRGCGRTDFQQ 168
Cdd:pfam00753  84 EElglaasrlglpgppvvplppdvvLEEGDGILGGGLGLLVTHGPGHGPGHVVVYYGGGKVLFTGDLLFAGEIGRLDLPL 163

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1395168515 169 GCAKTLYHSVHEK------IFTLPGNCLIYPAH 195
Cdd:pfam00753 164 GGLLVLHPSSAESslesllKLAKLKAAVIVPGH 196
B3_Acin_new1 NF033184
putative subclass B3 metallo-beta-lactamase; This is one of two families of putative ...
 13-142 4.52e-07

putative subclass B3 metallo-beta-lactamase; This is one of two families of putative metallo-beta-lactamases of subclass B3 that are restricted to the genus Acinetobacter, and undescribed as of January 2017.


Pssm-ID: 439394  Cd Length: 283  Bit Score: 49.72  E-value: 4.52e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168515  13 LSQQSASGAPVLL-------RQMFEPKSCTY--------TYLLGdrESREAVLIDPVL-ETAHRDAQLIKELGLKLL--- 73
Cdd:NF033184   12 LTSLSTSAAPLKLpddwtqnTQPFQITENIYyvgthglaAYLLA--SGHQALLIDTGLpENTEQIEQNIKQLGFKLSdvk 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168515  74 YAVNTHCHADHITGTGVLRsllpgcQSVISRLSGAQADLH-------IGE-------------------GDSIRFGRFAL 127
Cdd:NF033184   90 IMVTSHAHWDHVGALARIK------QDTGAKLIAMQQDVKaleigkpIGEntfqtipftpvkvdkvihdGEVVKLGKFKL 163

                         170
                  ....*....|....*
gi 1395168515 128 ETRASPGHTPGCVTF 142
Cdd:NF033184  164 KATLTPGHTPGCTTW 178
 
Name Accession Description Interval E-value
PLN02962 PLN02962
hydroxyacylglutathione hydrolase
 13-254 4.91e-127

hydroxyacylglutathione hydrolase


Pssm-ID: 178547 [Multi-domain]  Cd Length: 251  Bit Score: 360.27  E-value: 4.91e-127
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168515  13 LSQQSASGAPVLLRQMFEPKSCTYTYLLGD--RESREAVLIDPVLETAHRDAQLIKELGLKLLYAVNTHCHADHITGTGV 90
Cdd:PLN02962    1 SSSSSSSSSKLLFRQLFEKESSTYTYLLADvsHPDKPALLIDPVDKTVDRDLSLVKELGLKLIYAMNTHVHADHVTGTGL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168515  91 LRSLLPGCQSVISRLSGAQADLHIGEGDSIRFGRFALETRASPGHTPGCVTFVLNDQS------MAFTGDALLIRGCGRT 164
Cdd:PLN02962   81 LKTKLPGVKSIISKASGSKADLFVEPGDKIYFGDLYLEVRATPGHTAGCVTYVTGEGPdqpqprMAFTGDALLIRGCGRT 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168515 165 DFQQGCAKTLYHSVHEKIFTLPGNCLIYPAHDYHGLTVSTVEEERTLNPRLTLSCEEFIKVMDNLNLPKPQQIDIAVPAN 244
Cdd:PLN02962  161 DFQGGSSDQLYKSVHSQIFTLPKDTLIYPAHDYKGFTVSTVGEEMLYNPRLTKDEETFKTIMENLNLPYPKMIDVAVPAN 240

                         250
                  ....*....|
gi 1395168515 245 MRCGVQTPPS 254
Cdd:PLN02962  241 MVCGLQDPPA 250
POD-like_MBL-fold cd07724
ETHE1 (PDO type I), persulfide dioxygenase A (PDOA, PDO type II) and related proteins; ...
 24-197 1.96e-82

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: 244.23  E-value: 1.96e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168515  24 LLRQMFEPKSCTYTYLLGDRESREAVLIDPVLETAHRDAQLIKELGLKLLYAVNTHCHADHITGTGVLRSLLpGCQSVIS 103
Cdd:cd07724     1 IFRQFFDPGLGTLSYLVGDPETGEAAVIDPVRDSVDRYLDLAAELGLKITYVLETHVHADHVSGARELAERT-GAPIVIG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168515 104 RLSGA-QADLHIGEGDSIRFGRFALETRASPGHTPGCVTFVLNDQSMAFTGDALLIRGCGRTDFQQ---GCAKTLYHSVH 179
Cdd:cd07724    80 EGAPAsFFDRLLKDGDVLELGNLTLEVLHTPGHTPESVSYLVGDPDAVFTGDTLFVGDVGRPDLPGeaeGLARQLYDSLQ 159

                         170
                  ....*....|....*...
gi 1395168515 180 EKIFTLPGNCLIYPAHDY 197
Cdd:cd07724   160 RKLLLLPDETLVYPGHDY 177
metallo-hydrolase-like_MBL-fold cd06262
mainly hydrolytic enzymes and related proteins which carry out various biological functions; ...
 35-195 1.09e-42

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: 143.58  E-value: 1.09e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168515  35 TYTYLLGDrESREAVLIDPVLETAHRDAQLIKELGLKLLYAVNTHCHADHITGTGVLRSLlPGCQSVISR---------- 104
Cdd:cd06262    10 TNCYLVSD-EEGEAILIDPGAGALEKILEAIEELGLKIKAILLTHGHFDHIGGLAELKEA-PGAPVYIHEadaelledpe 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168515 105 ----------LSGAQADLHIGEGDSIRFGRFALETRASPGHTPGCVTFVLNDQSMAFTGDALLIRGCGRTDFQQGCAKTL 174
Cdd:cd06262    88 lnlaffgggpLPPPEPDILLEDGDTIELGGLELEVIHTPGHTPGSVCFYIEEEGVLFTGDTLFAGSIGRTDLPGGDPEQL 167

                         170       180
                  ....*....|....*....|.
gi 1395168515 175 YHSVHEKIFTLPGNCLIYPAH 195
Cdd:cd06262   168 IESIKKLLLLLPDDTVVYPGH 188
hydroxyacylglutathione_hydrolase_MBL-fold cd07723
hydroxyacylglutathione hydrolase, MBL-fold metallo-hydrolase domain; hydroxyacylglutathione ...
 36-195 6.02e-39

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: 132.97  E-value: 6.02e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168515  36 YTYLLGDRESREAVLIDPVletahrDAQLI----KELGLKLLYAVNTHCHADHITGTGVLRSLLPGCQsVI----SRLSG 107
Cdd:cd07723    10 YIYLIVDEATGEAAVVDPG------EAEPVlaalEKNGLTLTAILTTHHHWDHTGGNAELKALFPDAP-VYgpaeDRIPG 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168515 108 AqaDLHIGEGDSIRFGRFALETRASPGHTPGCVTFVLNDQSMAFTGDALLIRGCGRtdFQQGCAKTLYHSvHEKIFTLPG 187
Cdd:cd07723    83 L--DHPVKDGDEIKLGGLEVKVLHTPGHTLGHICYYVPDEPALFTGDTLFSGGCGR--FFEGTAEQMYAS-LQKLLALPD 157


                  ....*...
gi 1395168515 188 NCLIYPAH 195
Cdd:cd07723   158 DTLVYCGH 165
GloB COG0491
Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General ...
 35-197 1.75e-38

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: 133.66  E-value: 1.75e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168515  35 TYTYLLGDreSREAVLIDPVLETAHRDA--QLIKELGLKLLYAVNTHCHADHITGTGVLRSLLpGCQSVISR-------- 104
Cdd:COG0491    15 VNSYLIVG--GDGAVLIDTGLGPADAEAllAALAALGLDIKAVLLTHLHPDHVGGLAALAEAF-GAPVYAHAaeaealea 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168515 105 --------LSGAQADLHIGEGDSIRFGRFALETRASPGHTPGCVTFVLNDQSMAFTGDALLIRGCGRTDFQQGCAKTLYH 176
Cdd:COG0491    92 paagalfgREPVPPDRTLEDGDTLELGGPGLEVIHTPGHTPGHVSFYVPDEKVLFTGDALFSGGVGRPDLPDGDLAQWLA 171

                         170       180
                  ....*....|....*....|.
gi 1395168515 177 SVhEKIFTLPGNcLIYPAHDY 197
Cdd:COG0491   172 SL-ERLLALPPD-LVIPGHGP 190
BaeB-like_MBL-fold cd16275
Bacillus amyloliquefaciens BaeB and related proteins; MBL-fold metallo hydrolase domain; ...
 36-195 5.13e-34

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: 120.72  E-value: 5.13e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168515  36 YTYLLGDRESREAVLIDPV--LETAhrdAQLIKELGLKLLYAVNTHCHADHITGTGVLRSLlPGCQSVISR----LSGAQ 109
Cdd:cd16275    13 YSYIIIDKATREAAVVDPAwdIEKI---LAKLNELGLTLTGILLTHSHFDHVNLVEPLLAK-YDAPVYMSKeeidYYGFR 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168515 110 A-DLH-IGEGDSIRFGRFALETRASPGHTPGCVTFVLNDQsmAFTGDALLIRGCGRTDFQQGCAKTLYHSVHEKIFTLPG 187
Cdd:cd16275    89 CpNLIpLEDGDTIKIGDTEITCLLTPGHTPGSMCYLLGDS--LFTGDTLFIEGCGRCDLPGGDPEEMYESLQRLKKLPPP 166


                  ....*...
gi 1395168515 188 NCLIYPAH 195
Cdd:cd16275   167 NTRVYPGH 174
TTHA1623-like_MBL-fold cd16322
uncharacterized Thermus thermophilus TTHA1623 and related proteins; MBL-fold metallo hydrolase ...
 37-215 1.50e-29

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: 110.13  E-value: 1.50e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168515  37 TYLLGDRESREAVLIDPVLEtAHRDAQLIKELGLKLLYAVNTHCHADHITGTGVLRsLLPGCQSVISRL---------SG 107
Cdd:cd16322    13 TYLVADEGGGEAVLVDPGDE-SEKLLARFGTTGLTLLYILLTHAHFDHVGGVADLR-RHPGAPVYLHPDdlplyeaadLG 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168515 108 AQA-----------DLHIGEGDSIRFGRFALETRASPGHTPGCVTFVLNDQSMAFTGDALLIRGCGRTDFqQGCAKTLYH 176
Cdd:cd16322    91 AKAfglgieplpppDRLLEDGQTLTLGGLEFKVLHTPGHSPGHVCFYVEEEGLLFSGDLLFQGSIGRTDL-PGGDPKAMA 169

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1395168515 177 SVHEKIFTLPGNCLIYPAHdyhgLTVSTVEEERTLNPRL 215
Cdd:cd16322   170 ASLRRLLTLPDETRVFPGH----GPPTTLGEERRTNPFL 204
GSH_gloB TIGR03413
hydroxyacylglutathione hydrolase; Members of this protein family are hydroxyacylglutathione ...
 36-197 2.49e-25

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: 99.92  E-value: 2.49e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168515  36 YTYLLGDrESREAVLID-----PVLETahrdaqlIKELGLKLLYAVNTHCHADHITGTGVLRSLLPgCQsVI----SRLS 106
Cdd:TIGR03413  11 YIWLLHD-PDGQAAVVDpgeaePVLDA-------LEARGLTLTAILLTHHHHDHVGGVAELLEAFP-AP-VYgpaeERIP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168515 107 GAqaDLHIGEGDSIRFGRFALETRASPGHTPGCVTFVLNDQSMAFTGDALLIRGCGRTdFqQGCAKTLYHSVhEKIFTLP 186
Cdd:TIGR03413  81 GI--THPVKDGDTVTLGGLEFEVLAVPGHTLGHIAYYLPDSPALFCGDTLFSAGCGRL-F-EGTPEQMYDSL-QRLAALP 155

                         170
                  ....*....|.
gi 1395168515 187 GNCLIYPAHDY 197
Cdd:TIGR03413 156 DDTLVYCAHEY 166
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 36-195 1.74e-24

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: 96.08  E-value: 1.74e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168515   36 YTYLLGDREsrEAVLIDPVLETAHRDAQLIKELGL-KLLYAVNTHCHADHITGTGVL------------------RSLLP 96
Cdd:smart00849   1 NSYLVRDDG--GAILIDTGPGEAEDLLAELKKLGPkKIDAIILTHGHPDHIGGLPELleapgapvyapegtaellKDLLA 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168515   97 GCQSVISRLSGAQADLHIGEGDSIRFGRFALETRASPGHTPGCVTFVLNDQSMAFTGDALLIRGCGRTDFQQG-CAKTLY 175
Cdd:smart00849  79 LLGELGAEAEPAPPDRTLKDGDELDLGGGELEVIHTPGHTPGSIVLYLPEGKILFTGDLLFAGGDGRTLVDGGdAAASDA 158

                          170       180
                   ....*....|....*....|
gi 1395168515  176 HSVHEKIFTLPGNcLIYPAH 195
Cdd:smart00849 159 LESLLKLLKLLPK-LVVPGH 177
YcbL-like_MBL-fold cd07737
Salmonella enterica serovar typhimurium YcbL and related proteins; MBL-fold metallo hydrolase ...
 34-195 3.37e-24

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: 95.70  E-value: 3.37e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168515  34 CTytyLLGDRESREAVLIDPVLEtAHRDAQLIKELGLKLLYAVNTHCHADHITGTGVLRSL------------------L 95
Cdd:cd07737    13 CS---LIWCEETKEAAVIDPGGD-ADKILQAIEDLGLTLKKILLTHGHLDHVGGAAELAEHygvpiigphkedkfllenL 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168515  96 PGcQSVISRLSGAQA---DLHIGEGDSIRFGRFALETRASPGHTPGCVTFVLNDQSMAFTGDALLIRGCGRTDFQQGCAK 172
Cdd:cd07737    89 PE-QSQMFGFPPAEAftpDRWLEEGDTVTVGNLTLEVLHCPGHTPGHVVFFNRESKLAIVGDVLFKGSIGRTDFPGGNHA 167

                         170       180
                  ....*....|....*....|...
gi 1395168515 173 TLYHSVHEKIFTLPGNCLIYPAH 195
Cdd:cd07737   168 QLIASIKEKLLPLGDDVTFIPGH 190
PLN02469 PLN02469
hydroxyacylglutathione hydrolase
 36-213 7.91e-20

hydroxyacylglutathione hydrolase


Pssm-ID: 178088 [Multi-domain]  Cd Length: 258  Bit Score: 85.58  E-value: 7.91e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168515  36 YTYLLGDRESREAVLIDPV-----LETAHrdaqlikELGLKLLYAVNTHCHADHITGTGVLRSLLPGCQSVISRLSGAQA 110
Cdd:PLN02469   13 YAYLIIDESTKDAAVVDPVdpekvLQAAH-------EHGAKIKLVLTTHHHWDHAGGNEKIKKLVPGIKVYGGSLDNVKG 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168515 111 DLH-IGEGDSIRFGR----FALETrasPGHTPGCVTFVL----NDQSMAFTGDALLIRGCGRtdFQQGCAKTLYHSVHEK 181
Cdd:PLN02469   86 CTHpVENGDKLSLGKdvniLALHT---PCHTKGHISYYVtgkeGEDPAVFTGDTLFIAGCGK--FFEGTAEQMYQSLCVT 160

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1395168515 182 IFTLPGNCLIYPAHDYhglTVSTVEEERTLNP 213
Cdd:PLN02469  161 LGSLPKPTQVYCGHEY---TVKNLKFALTVEP 189
Lactamase_B pfam00753
Metallo-beta-lactamase superfamily;
35-195 1.54e-18

Metallo-beta-lactamase superfamily;


Pssm-ID: 425851 [Multi-domain]  Cd Length: 196  Bit Score: 80.88  E-value: 1.54e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168515  35 TYTYLLGDREsrEAVLIDPVLETAHRDAQLIKELGLKLL---YAVNTHCHADHITGTGVLRSLLPGCQSVISRLSGAQAD 111
Cdd:pfam00753   6 VNSYLIEGGG--GAVLIDTGGSAEAALLLLLAALGLGPKdidAVILTHGHFDHIGGLGELAEATDVPVIVVAEEARELLD 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168515 112 LH-----------------------IGEGDSIRFGRFALETRASPGHTPGCVTFVLNDQSMAFTGDALLIRGCGRTDFQQ 168
Cdd:pfam00753  84 EElglaasrlglpgppvvplppdvvLEEGDGILGGGLGLLVTHGPGHGPGHVVVYYGGGKVLFTGDLLFAGEIGRLDLPL 163

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1395168515 169 GCAKTLYHSVHEK------IFTLPGNCLIYPAH 195
Cdd:pfam00753 164 GGLLVLHPSSAESslesllKLAKLKAAVIVPGH 196
metallo-hydrolase-like_MBL-fold cd07743
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 44-156 6.96e-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: 6.96e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168515  44 ESREAVLIDPVL--ETAHRDAQLIKELGLKLLYAVNTHCHADHITGTGVLRSlLPGCQSVISR---------------LS 106
Cdd:cd07743    16 GDKEALLIDSGLdeDAGRKIRKILEELGWKLKAIINTHSHADHIGGNAYLQK-KTGCKVYAPKiekafienpllepsyLG 94

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1395168515 107 GA----------------QADlHIGEGDSIRFGRFALETRASPGHTPGCVTfVLNDQSMAFTGDAL 156
Cdd:cd07743    95 GAyppkelrnkflmakpsKVD-DIIEEGELELGGVGLEIIPLPGHSFGQIG-ILTPDGVLFAGDAL 158
PLN02398 PLN02398
hydroxyacylglutathione hydrolase
 36-197 2.81e-12

hydroxyacylglutathione hydrolase


Pssm-ID: 215223 [Multi-domain]  Cd Length: 329  Bit Score: 65.25  E-value: 2.81e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168515  36 YTYLLGDRESREAVLIDPVLETAHRDAqlIKELGLKLLYAVNTHCHADHITGTGVLRSLLpGCQSVIS-----RLSGAqa 110
Cdd:PLN02398   88 YAYLLHDEDTGTVGVVDPSEAVPVIDA--LSRKNRNLTYILNTHHHYDHTGGNLELKARY-GAKVIGSavdkdRIPGI-- 162

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168515 111 DLHIGEGDSIRFGRFALETRASPGHTPGCVTFVLNDQSMAFTGDALLIRGCGRtdFQQGCAKTLYHSVhEKIFTLPGNCL 190
Cdd:PLN02398  163 DIVLKDGDKWMFAGHEVLVMETPGHTRGHISFYFPGSGAIFTGDTLFSLSCGK--LFEGTPEQMLSSL-QKIISLPDDTN 239


                  ....*..
gi 1395168515 191 IYPAHDY 197
Cdd:PLN02398  240 IYCGHEY 246
TTHA1429-like_MBL-fold cd07725
uncharacterized Thermus thermophilus TTHA1429 and related proteins; MBL-fold metallo hydrolase ...
 38-159 5.30e-12

uncharacterized Thermus thermophilus TTHA1429 and related proteins; MBL-fold metallo hydrolase domain; Includes the MBL-fold metallo hydrolase domain of uncharacterized Thermus thermophilus TTHA1429 and related proteins. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions.


Pssm-ID: 293811 [Multi-domain]  Cd Length: 184  Bit Score: 62.70  E-value: 5.30e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168515  38 YLLGDREsrEAVLIDPVLETaHRDAQL----IKELGLKLL---YAVNTHCHADHITGTGVLRSLLpGCQSVISRLSGaqa 110
Cdd:cd07725    18 YLLRDGD--ETTLIDTGLAT-EEDAEAlwegLKELGLKPSdidRVLLTHHHPDHIGLAGKLQEKS-GATVYILDVTP--- 90

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1395168515 111 dlhIGEGDSIRFGRFALETRASPGHTPGCVTFVLNDQSMAFTGDALLIR 159
Cdd:cd07725    91 ---VKDGDKIDLGGLRLKVIETPGHTPGHIVLYDEDRRELFVGDAVLPK 136
metallo-hydrolase-like_MBL-fold cd16278
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 35-160 1.38e-11

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: 61.35  E-value: 1.38e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168515  35 TYTYLLGDREsrEAVLIDP-VLETAHRDAQLIKELGLKLLYAVNTHCHADHITGTGVLRSLL------PGCQSVISRLSG 107
Cdd:cd16278    18 TNTYLLGAPD--GVVVIDPgPDDPAHLDALLAALGGGRVSAILVTHTHRDHSPGAARLAERTgapvraFGPHRAGGQDTD 95

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1395168515 108 AQADLHIGEGDSIRFGRFALETRASPGHTPGCVTFVLNDQSMAFTGDALLIRG 160
Cdd:cd16278    96 FAPDRPLADGEVIEGGGLRLTVLHTPGHTSDHLCFALEDEGALFTGDHVMGWS 148
metallo-hydrolase-like_MBL-fold cd16280
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 49-143 1.55e-09

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: 56.82  E-value: 1.55e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168515  49 VLIDpVLETAHRDAQL---IKELGLK---LLYAVNTHCHADHITGTGVLRSLlPGCQSVISR----LSGAQA-------- 110
Cdd:cd16280    34 ILID-ALNNNEAADLIvdgLEKLGLDpadIKYILITHGHGDHYGGAAYLKDL-YGAKVVMSEadwdMMEEPPeegdnprw 111

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1395168515 111 ------DLHIGEGDSIRFGRFALETRASPGHTPGCVTFV 143
Cdd:cd16280   112 gppperDIVIKDGDTLTLGDTTITVYLTPGHTPGTLSLI 150
Mbl1b-like_MBL-B3 cd16310
Caulobacter crescentus Mbl1b and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 37-142 1.89e-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: 1.89e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168515  37 TYLLGdrESREAVLIDPVL-ETAHRDAQLIKELGLKLL---YAVNTHCHADHITGTGVLRSlLPGCQSVISR-------- 104
Cdd:cd16310    24 SYLIT--SNHGAILLDGGLeENAALIEQNIKALGFKLSdikIIINTHAHYDHAGGLAQLKA-DTGAKLWASRgdrpalea 100

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1395168515 105 -------------LSGAQADLHIGEGDSIRFGRFALETRASPGHTPGCVTF 142
Cdd:cd16310   101 gkhigdnitqpapFPAVKVDRILGDGEKIKLGDITLTATLTPGHTKGCTTW 151
MBLAC2-like_MBL-fold cd07712
uncharacterized human metallo-beta-lactamase domain-containing protein 2 and related proteins; ...
 35-195 2.75e-09

uncharacterized human metallo-beta-lactamase domain-containing protein 2 and related proteins; MBL-fold metallo hydrolase domain; Includes the MBL-fold metallo hydrolase domain of uncharacterized human MBLAC2 and related proteins. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions.


Pssm-ID: 293798 [Multi-domain]  Cd Length: 182  Bit Score: 54.94  E-value: 2.75e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168515  35 TYTYLLgdRESREAVLIDPVLETAHRDaQLIKELGLKLLYAVNTHCHADHITG-------------TGVLRSLLPGCQSV 101
Cdd:cd07712     9 VNIYLL--RGRDRALLIDTGLGIGDLK-EYVRTLTDLPLLVVATHGHFDHIGGlhefeevyvhpadAEILAAPDNFETLT 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168515 102 IS----RLSGAQADLHIGEGDSIRFGRFALETRASPGHTPGCVTFVLNDQSMAFTGDAL----LIRGCGRTDFqqgcakT 173
Cdd:cd07712    86 WDaatySVPPAGPTLPLRDGDVIDLGDRQLEVIHTPGHTPGSIALLDRANRLLFSGDVVydgpLIMDLPHSDL------D 159

                         170       180
                  ....*....|....*....|...
gi 1395168515 174 LYHSVHEKIFTLPGNC-LIYPAH 195
Cdd:cd07712   160 DYLASLEKLSKLPDEFdKVLPGH 182
MBL-B3-like cd07708
metallo-beta-lactamases, subclass B3; MBL-fold metallo-hydrolase domain; MBLs (class B of the ...
 45-146 4.89e-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: 55.24  E-value: 4.89e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168515  45 SREAVLIDPVLE--TAHRDAQlIKELGLKLL---YAVNTHCHADHITGTGVLR-----SLLPGCQSVISRLSGAQADLHI 114
Cdd:cd07708    30 PQGNILIDGDMEqnAPMIKAN-IKKLGFKFSdtkLILISHAHFDHAGGSAEIKkqtgaKVMAGAEDVSLLLSGGSSDFHY 108

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1395168515 115 G-----------------EGDSIRFGRFALETRASPGHTPGCVTFVLND 146
Cdd:cd07708   109 AndsstyfpqstvdravhDGERVTLGGTVLTAHATPGHTPGCTTWTMTL 157
BJP-1-like_MBL-B3 cd16309
Bradyrhizobium diazoefficiens BJP-1 and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 65-144 7.32e-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: 51.72  E-value: 7.32e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168515  65 IKELGLK---LLYAVNTHCHADHITGTGVLRSLlPGCQSVISRL-----------SGAQADLH---------IGEGDSIR 121
Cdd:cd16309    51 IKKLGFDvkdVKYLLNTHAHFDHAGGLAELKKA-TGAQLVASAAdkpllesgyvgSGDTKNLQfppvrvdrvIGDGDKVT 129

                          90       100
                  ....*....|....*....|...
gi 1395168515 122 FGRFALETRASPGHTPGCVTFVL 144
Cdd:cd16309   130 LGGTTLTAHLTPGHSPGCTSWTT 152
LACTB2-like_MBL-fold cd07722
uncharacterized subgroup which includes human lactamase beta 2 and related proteins; MBL-fold ...
 35-195 9.26e-08

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: 50.61  E-value: 9.26e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168515  35 TYTYLLGDRESReaVLID---------PVLETAhrdaqlIKELGLKLL-YAVNTHCHADHITGTGVLRSLLPGCQSVISR 104
Cdd:cd07722    18 TNTYLVGTGKRR--ILIDtgegrpsyiPLLKSV------LDSEGNATIsDILLTHWHHDHVGGLPDVLDLLRGPSPRVYK 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168515 105 L------------SGAQADLHigEGDSIRFGRFALETRASPGHTPGCVTFVLNDQSMAFTGDALLirGCGRTDFQqgCAK 172
Cdd:cd07722    90 FprpeededpdedGGDIHDLQ--DGQVFKVEGATLRVIHTPGHTTDHVCFLLEEENALFTGDCVL--GHGTAVFE--DLA 163

                         170       180
                  ....*....|....*....|...
gi 1395168515 173 TLYHSVHeKIFTLpGNCLIYPAH 195
Cdd:cd07722   164 AYMASLK-KLLSL-GPGRIYPGH 184
yflN-like_MBL-fold cd07721
uncharacterized subgroup which includes Bacillus subtilis yflN; MBL-fold metallo hydrolase ...
 36-160 1.27e-07

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: 50.68  E-value: 1.27e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168515  36 YTYLLGDreSREAVLIDP-VLETAHRDAQLIKELGLK-------LLyavnTHCHADHITG-------------------- 87
Cdd:cd07721    12 NAYLIED--DDGLTLIDTgLPGSAKRILKALRELGLSpkdirriLL----THGHIDHIGSlaalkeapgapvyahereap 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168515  88 --TGVLRSLLPGCQSVISRLSG------AQADLHIGEGDSIRFGrFALETRASPGHTPGCVTFVLNDQSMAFTGDALLIR 159
Cdd:cd07721    86 ylEGEKPYPPPVRLGLLGLLSPllpvkpVPVDRTLEDGDTLDLA-GGLRVIHTPGHTPGHISLYLEEDGVLIAGDALVTV 164


                  .
gi 1395168515 160 G 160
Cdd:cd07721   165 G 165
B3_Acin_new1 NF033184
putative subclass B3 metallo-beta-lactamase; This is one of two families of putative ...
 13-142 4.52e-07

putative subclass B3 metallo-beta-lactamase; This is one of two families of putative metallo-beta-lactamases of subclass B3 that are restricted to the genus Acinetobacter, and undescribed as of January 2017.


Pssm-ID: 439394  Cd Length: 283  Bit Score: 49.72  E-value: 4.52e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168515  13 LSQQSASGAPVLL-------RQMFEPKSCTY--------TYLLGdrESREAVLIDPVL-ETAHRDAQLIKELGLKLL--- 73
Cdd:NF033184   12 LTSLSTSAAPLKLpddwtqnTQPFQITENIYyvgthglaAYLLA--SGHQALLIDTGLpENTEQIEQNIKQLGFKLSdvk 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168515  74 YAVNTHCHADHITGTGVLRsllpgcQSVISRLSGAQADLH-------IGE-------------------GDSIRFGRFAL 127
Cdd:NF033184   90 IMVTSHAHWDHVGALARIK------QDTGAKLIAMQQDVKaleigkpIGEntfqtipftpvkvdkvihdGEVVKLGKFKL 163

                         170
                  ....*....|....*
gi 1395168515 128 ETRASPGHTPGCVTF 142
Cdd:NF033184  164 KATLTPGHTPGCTTW 178
ST1585-like_MBL-fold cd07726
uncharacterized subgroup which includes Sulfolobus tokodaii ST1585 protein; MBL-fold metallo ...
 35-162 6.11e-07

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: 48.64  E-value: 6.11e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168515  35 TYTYLLgdRESREAVLIDP-VLETAHRDAQLIKELGLKLL---YAVNTHCHADHITGTGVLRSLLPGCQSVI-------- 102
Cdd:cd07726    16 IASYLL--DGEGRPALIDTgPSSSVPRLLAALEALGIAPEdvdYIILTHIHLDHAGGAGLLAEALPNAKVYVhprgarhl 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168515 103 ---SRL-------SGAQADLHIGE--------------GDSIRFGRFALETRASPGHTPGCVTFVLNDQSMAFTGDALLI 158
Cdd:cd07726    94 idpSKLwasaravYGDEADRLGGEilpvpeervivledGETLDLGGRTLEVIDTPGHAPHHLSFLDEESDGLFTGDAAGV 173


                  ....
gi 1395168515 159 RGCG 162
Cdd:cd07726   174 RYPE 177
BJP-1_FEZ-1-like_MBL-B3 cd16288
BJP-1, FEZ-1, GOB-1, Mbl1b and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 49-145 6.67e-07

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: 48.86  E-value: 6.67e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168515  49 VLIDPVLE-TAHRDAQLIKELGLK---LLYAVNTHCHADHITGTGVLRSLlPGCQSVISR------LSGAQADLHIG--- 115
Cdd:cd16288    34 ILIDTGLEsSAPMIKANIRKLGFKpsdIKILLNSHAHLDHAGGLAALKKL-TGAKLMASAedaallASGGKSDFHYGdds 112

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1395168515 116 -------------EGDSIRFGRFALETRASPGHTPGCVTFVLN 145
Cdd:cd16288   113 lafppvkvdrvlkDGDRVTLGGTTLTAHLTPGHTRGCTTWTMT 155
VIM_type_MBL-B1 cd16303
VIM-type metallo-beta-lactamases, subclass B1; MBL-fold metallo-hydrolase domain; VIM (Verona ...
 43-164 2.07e-06

VIM-type metallo-beta-lactamases, subclass B1; MBL-fold metallo-hydrolase domain; VIM (Verona integron-encoded metallo-beta-lactamase)-type MBLs are integron-associated and are widely distributed acquired MBLs. 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. This subgroup of VIM-type 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: 293861 [Multi-domain]  Cd Length: 218  Bit Score: 47.16  E-value: 2.07e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168515  43 RESREAVLIDPV---LETAHRDAQLIKELGLKLLYAVNTHCHADHITGTGVLRS------LLPGCQSvISRLSGAQADLH 113
Cdd:cd16303    34 RDGDELLLIDTAwgaKNTAALLAEIEKQIGLPVTRAVSTHFHDDRVGGVDVLRAagvatyASPSTRR-LAEAEGNEIPTH 112

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1395168515 114 IGE-----GDSIRFGRFALeTRASPGHTPGCVTFVLNDQSMAFTGDAllIRGCGRT 164
Cdd:cd16303   113 SLEglsssGDAVRFGPVEL-FYPGAAHSTDNLVVYVPSARVLYGGCA--VRELSST 165
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 ...
 49-141 3.08e-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: 46.96  E-value: 3.08e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168515  49 VLIDPVLE-TAHRDAQLIKELGLKL---LYAVNTHCHADHITGTGVLRSLlPGCQsVISRLSGAQA-------------- 110
Cdd:cd16290    34 ILIDGALPqSAPQIEANIRALGFRLedvKLILNSHAHFDHAGGIAALQRD-SGAT-VAASPAGAAAlrsggvdpddpqag 111

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1395168515 111 ----------DLHIGEGDSIRFGRFALETRASPGHTPGCVT 141
Cdd:cd16290   112 aadpfppvakVRVVADGEVVKLGPLAVTAHATPGHTPGGTS 152
metallo-hydrolase-like_MBL-fold cd07739
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 45-97 1.33e-05

uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo hydrolase domain; Members of the MBL-fold metallohydrolase superfamily are mainly hydrolytic enzymes which carry out a variety of biological functions. The class B metal beta-lactamases (MBLs) 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: 44.80  E-value: 1.33e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1395168515  45 SREAVLIDP--VLETAHRDAQLIKELGLKLLYAVNTHCHADHITGTGVLRSLLPG 97
Cdd:cd07739    24 ETEAVLVDAqfTRADAERLADWIKASGKTLTTIYITHGHPDHYFGLEVLLEAFPD 78
EVM-1-like_MBL-B3 cd16315
Erythrobacter vulgaris EVM-1 and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 49-138 4.42e-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: 43.49  E-value: 4.42e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168515  49 VLIDPVLETAhrdAQL----IKELGLKLL---YAVNTHCHADHITGTGVLRSL-------LPGCQSVISR---------- 104
Cdd:cd16315    34 VLIDSGTEEA---APLvlanIRKLGFDPKdvrWLLSSHEHFDHVGGLAALQRAtgarvaaSAAAAPVLESgkpapddpqa 110

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1395168515 105 -----LSGAQADLHIGEGDSIRFGRFALETRASPGHTPG 138
Cdd:cd16315   111 glhepFPPVRVDRIVEDGDTVALGSLRLTAHATPGHTPG 149
MBLAC1-like_MBL-fold cd07711
uncharacterized human metallo-beta-lactamase domain-containing protein 1 and related proteins; ...
 33-155 2.17e-03

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: 37.95  E-value: 2.17e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168515  33 SCTYTYLLGDRESreaVLIDPvleTAHRDAQLI----KELGLKLL---YAVNTHCHADHITGTGvlrsLLPGCQSVISR- 104
Cdd:cd07711    21 SSTVTLIKDGGKN---ILVDT---GTPWDRDLLlkalAEHGLSPEdidYVVLTHGHPDHIGNLN----LFPNATVIVGWd 90

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1395168515 105 LSGAQADLHIGE-------GDSIRFgrfaLETrasPGHTPGCVTFVLNDQSM---AFTGDA 155
Cdd:cd07711    91 ICGDSYDDHSLEegdgyeiDENVEV----IPT---PGHTPEDVSVLVETEKKgtvAVAGDL 144
 
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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