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Conserved domains on  [gi|2568418062|ref|WP_306575298|]
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MBL fold metallo-hydrolase [Oligella urethralis]

Protein Classification

MBL fold metallo-hydrolase( domain architecture ID 581040)

MBL fold metallo-hydrolase is most likely a hydrolytic enzyme

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
metallo-hydrolase-like_MBL-fold super family cl23716
mainly hydrolytic enzymes and related proteins which carry out various biological functions; ...
 32-275 9.61e-36

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.


The actual alignment was detected with superfamily member cd07725:

Pssm-ID: 451500 [Multi-domain]  Cd Length: 184  Bit Score: 128.19  E-value: 9.61e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2568418062  32 IRLPLPFALDHINCWLIADEyegqKGWTMVDCGINKP-VVREVWEQIFANELDGLPIVRVMVTHMHPDHVGLAGWHCSRW 110
Cdd:cd07725     4 LSLPLPGPLGHVNVYLLRDG----DETTLIDTGLATEeDAEALWEGLKELGLKPSDIDRVLLTHHHPDHIGLAGKLQEKS 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2568418062 111 NvslwmsmtdyfvaccwtmdtkgagtggqgavahfarhglldkdsqqkileranyypGLVYPPPssFNRLIDERVIDIGG 190
Cdd:cd07725    80 G--------------------------------------------------------ATVYILD--VTPVKDGDKIDLGG 101

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2568418062 191 HAWTLISGYGHAPEHISLYCPDLAVLISGDMLLPRISTNVSVFDFePEANPLPLYLNSVVKFLDLPDDtLVLPSHGRPFK 270
Cdd:cd07725   102 LRLKVIETPGHTPGHIVLYDEDRRELFVGDAVLPKITPNVSLWAV-RVEDPLGAYLESLDKLEKLDVD-LAYPGHGGPIK 179


                  ....*
gi 2568418062 271 GIKER 275
Cdd:cd07725   180 DPKAR 184
 
Name Accession Description Interval E-value
TTHA1429-like_MBL-fold cd07725
uncharacterized Thermus thermophilus TTHA1429 and related proteins; MBL-fold metallo hydrolase ...
 32-275 9.61e-36

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: 128.19  E-value: 9.61e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2568418062  32 IRLPLPFALDHINCWLIADEyegqKGWTMVDCGINKP-VVREVWEQIFANELDGLPIVRVMVTHMHPDHVGLAGWHCSRW 110
Cdd:cd07725     4 LSLPLPGPLGHVNVYLLRDG----DETTLIDTGLATEeDAEALWEGLKELGLKPSDIDRVLLTHHHPDHIGLAGKLQEKS 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2568418062 111 NvslwmsmtdyfvaccwtmdtkgagtggqgavahfarhglldkdsqqkileranyypGLVYPPPssFNRLIDERVIDIGG 190
Cdd:cd07725    80 G--------------------------------------------------------ATVYILD--VTPVKDGDKIDLGG 101

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2568418062 191 HAWTLISGYGHAPEHISLYCPDLAVLISGDMLLPRISTNVSVFDFePEANPLPLYLNSVVKFLDLPDDtLVLPSHGRPFK 270
Cdd:cd07725   102 LRLKVIETPGHTPGHIVLYDEDRRELFVGDAVLPKITPNVSLWAV-RVEDPLGAYLESLDKLEKLDVD-LAYPGHGGPIK 179


                  ....*
gi 2568418062 271 GIKER 275
Cdd:cd07725   180 DPKAR 184
GloB COG0491
Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General ...
 29-269 1.14e-33

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


Pssm-ID: 440257 [Multi-domain]  Cd Length: 215  Bit Score: 123.65  E-value: 1.14e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2568418062  29 VKWIRLPLPFALDHINCWLIADEyegqKGWTMVDCGINKPVVREVWEQIFANeldGLPIVRVMVTHMHPDHVGLAGWHCS 108
Cdd:COG0491     1 VYVLPGGTPGAGLGVNSYLIVGG----DGAVLIDTGLGPADAEALLAALAAL---GLDIKAVLLTHLHPDHVGGLAALAE 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2568418062 109 RWNVSLWMSmtdyfvaccwtmdtkgagtggqGAVAHFARHGlldkdsqqkilERANYYPGLVYPPpssfNRLIDER-VID 187
Cdd:COG0491    74 AFGAPVYAH----------------------AAEAEALEAP-----------AAGALFGREPVPP----DRTLEDGdTLE 116

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2568418062 188 IGGHAWTLISGYGHAPEHISLYCPDLAVLISGDMLLPRISTNVSVFDFEPEAnplplYLNSVVKFLDLPDDtLVLPSHGR 267
Cdd:COG0491   117 LGGPGLEVIHTPGHTPGHVSFYVPDEKVLFTGDALFSGGVGRPDLPDGDLAQ-----WLASLERLLALPPD-LVIPGHGP 190


                  ..
gi 2568418062 268 PF 269
Cdd:COG0491   191 PT 192
Lactamase_B pfam00753
Metallo-beta-lactamase superfamily;
40-265 1.35e-19

Metallo-beta-lactamase superfamily;


Pssm-ID: 425851 [Multi-domain]  Cd Length: 196  Bit Score: 85.50  E-value: 1.35e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2568418062  40 LDHINCWLIadeyEGQKGWTMVDCGINKPVVREVWeqIFANELDGLPIVRVMVTHMHPDHVGLAGWHCSRWNVSLWMSMT 119
Cdd:pfam00753   3 PGQVNSYLI----EGGGGAVLIDTGGSAEAALLLL--LAALGLGPKDIDAVILTHGHFDHIGGLGELAEATDVPVIVVAE 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2568418062 120 DYFVAccwtmdtkgagtggqgavahfarhglldKDSQQKILERANYYPGLVYPPPSSFNRLIDERVIDIGGHAWTLISGY 199
Cdd:pfam00753  77 EAREL----------------------------LDEELGLAASRLGLPGPPVVPLPPDVVLEEGDGILGGGLGLLVTHGP 128

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2568418062 200 GHAPEHISLYCPDLAVLISGDMLLPRISTNVSVFDFEPEANPLPLYLNSVVKFLDL--PDDTLVLPSH 265
Cdd:pfam00753 129 GHGPGHVVVYYGGGKVLFTGDLLFAGEIGRLDLPLGGLLVLHPSSAESSLESLLKLakLKAAVIVPGH 196
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 44-265 1.28e-18

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: 82.22  E-value: 1.28e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2568418062   44 NCWLIADEyegqKGWTMVDCGINKPVVREVWEQifanELDGLPIVRVMVTHMHPDHVGLAGWHCSRWNVSLWMSMTDYFV 123
Cdd:smart00849   1 NSYLVRDD----GGAILIDTGPGEAEDLLAELK----KLGPKKIDAIILTHGHPDHIGGLPELLEAPGAPVYAPEGTAEL 72

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2568418062  124 AccwtmdtkgagtggqgavahfarhglldkdsqqKILERANYYPGLVYPPPSSFNRLIDERVIDIGGHAWTLISGYGHAP 203
Cdd:smart00849  73 L---------------------------------KDLLALLGELGAEAEPAPPDRTLKDGDELDLGGGELEVIHTPGHTP 119

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2568418062  204 EHISLYCPDLAVLISGDMLLPRIstnVSVFDFEPEANPLPLYLNSVVKFLDlPDDTLVLPSH 265
Cdd:smart00849 120 GSIVLYLPEGKILFTGDLLFAGG---DGRTLVDGGDAAASDALESLLKLLK-LLPKLVVPGH 177
SoxH_rel_PQQ_2 TIGR04559
quinoprotein relay system zinc metallohydrolase 2; By homology, members are Zn ...
 54-100 7.83e-03

quinoprotein relay system zinc metallohydrolase 2; By homology, members are Zn metallohydrolases in the same family as the SoxH protein associated with sulfate metabolism, Bacillus cereus beta-lactamase II (see PDB:1bc2), and, more distantly, hydroxyacylglutathione hydrolase (glyoxalase II). All members occur in genomes with both PQQ biosynthesis and a PQQ-dependent (quinoprotein) dehydrogenase that has a motif of two consecutive Cys residues (see TIGR03075). The Cys-Cys motif is associated with electron transfer by specialized cytochromes such as c551. All these genomes also include a fusion protein (TIGR04557) whose domains resemble SoxY and SoxZ from thiosulfate oxidation. A conserved Cys in this fusion protein aligns to the Cys residue in SoxY that carries sulfur cycle intermediates. In many genomes, the genes for PQQ biosynthesis enzymes, PQQ-dependent enzymes, their associated cytochromes, and members of this family are clustered. Note that one to three closely related Zn metallohydrolases may occur; this family represents a specific clade among them. Some members of this family have a short additional N-terminal domain with four conserved Cys residues. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 275352  Cd Length: 283  Bit Score: 37.56  E-value: 7.83e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 2568418062  54 GQKGWTMVDCGINKPVVREVWEQIfaNELDGLPIVRVMVTHMHPDHV 100
Cdd:TIGR04559  37 GEDAVAVIDTGGSRAEGEALLAAI--RQRTDLPIRYVINTHVHPDHI 81
 
Name Accession Description Interval E-value
TTHA1429-like_MBL-fold cd07725
uncharacterized Thermus thermophilus TTHA1429 and related proteins; MBL-fold metallo hydrolase ...
 32-275 9.61e-36

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: 128.19  E-value: 9.61e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2568418062  32 IRLPLPFALDHINCWLIADEyegqKGWTMVDCGINKP-VVREVWEQIFANELDGLPIVRVMVTHMHPDHVGLAGWHCSRW 110
Cdd:cd07725     4 LSLPLPGPLGHVNVYLLRDG----DETTLIDTGLATEeDAEALWEGLKELGLKPSDIDRVLLTHHHPDHIGLAGKLQEKS 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2568418062 111 NvslwmsmtdyfvaccwtmdtkgagtggqgavahfarhglldkdsqqkileranyypGLVYPPPssFNRLIDERVIDIGG 190
Cdd:cd07725    80 G--------------------------------------------------------ATVYILD--VTPVKDGDKIDLGG 101

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2568418062 191 HAWTLISGYGHAPEHISLYCPDLAVLISGDMLLPRISTNVSVFDFePEANPLPLYLNSVVKFLDLPDDtLVLPSHGRPFK 270
Cdd:cd07725   102 LRLKVIETPGHTPGHIVLYDEDRRELFVGDAVLPKITPNVSLWAV-RVEDPLGAYLESLDKLEKLDVD-LAYPGHGGPIK 179


                  ....*
gi 2568418062 271 GIKER 275
Cdd:cd07725   180 DPKAR 184
GloB COG0491
Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General ...
 29-269 1.14e-33

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


Pssm-ID: 440257 [Multi-domain]  Cd Length: 215  Bit Score: 123.65  E-value: 1.14e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2568418062  29 VKWIRLPLPFALDHINCWLIADEyegqKGWTMVDCGINKPVVREVWEQIFANeldGLPIVRVMVTHMHPDHVGLAGWHCS 108
Cdd:COG0491     1 VYVLPGGTPGAGLGVNSYLIVGG----DGAVLIDTGLGPADAEALLAALAAL---GLDIKAVLLTHLHPDHVGGLAALAE 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2568418062 109 RWNVSLWMSmtdyfvaccwtmdtkgagtggqGAVAHFARHGlldkdsqqkilERANYYPGLVYPPpssfNRLIDER-VID 187
Cdd:COG0491    74 AFGAPVYAH----------------------AAEAEALEAP-----------AAGALFGREPVPP----DRTLEDGdTLE 116

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2568418062 188 IGGHAWTLISGYGHAPEHISLYCPDLAVLISGDMLLPRISTNVSVFDFEPEAnplplYLNSVVKFLDLPDDtLVLPSHGR 267
Cdd:COG0491   117 LGGPGLEVIHTPGHTPGHVSFYVPDEKVLFTGDALFSGGVGRPDLPDGDLAQ-----WLASLERLLALPPD-LVIPGHGP 190


                  ..
gi 2568418062 268 PF 269
Cdd:COG0491   191 PT 192
metallo-hydrolase-like_MBL-fold cd06262
mainly hydrolytic enzymes and related proteins which carry out various biological functions; ...
 44-265 5.39e-20

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: 86.19  E-value: 5.39e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2568418062  44 NCWLIADEyegQKGWTMVDCGInkpvvrEVWEQIFA-NELDGLPIVRVMVTHMHPDHVGLAGWHCSRWNVSLWMSMTDYF 122
Cdd:cd06262    11 NCYLVSDE---EGEAILIDPGA------GALEKILEaIEELGLKIKAILLTHGHFDHIGGLAELKEAPGAPVYIHEADAE 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2568418062 123 vaccwtmdtkgagtggqgavahfarhgLLDKDSqqkilERANYYPGLVYPPPSSFNRLIDERVIDIGGHAWTLISGYGHA 202
Cdd:cd06262    82 ---------------------------LLEDPE-----LNLAFFGGGPLPPPEPDILLEDGDTIELGGLELEVIHTPGHT 129

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2568418062 203 PEHISLYCPDLAVLISGDMLLPRistnvSVF--DFePEANPLPLYLNSVVKFLDLPDDTLVLPSH 265
Cdd:cd06262   130 PGSVCFYIEEEGVLFTGDTLFAG-----SIGrtDL-PGGDPEQLIESIKKLLLLLPDDTVVYPGH 188
Lactamase_B pfam00753
Metallo-beta-lactamase superfamily;
40-265 1.35e-19

Metallo-beta-lactamase superfamily;


Pssm-ID: 425851 [Multi-domain]  Cd Length: 196  Bit Score: 85.50  E-value: 1.35e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2568418062  40 LDHINCWLIadeyEGQKGWTMVDCGINKPVVREVWeqIFANELDGLPIVRVMVTHMHPDHVGLAGWHCSRWNVSLWMSMT 119
Cdd:pfam00753   3 PGQVNSYLI----EGGGGAVLIDTGGSAEAALLLL--LAALGLGPKDIDAVILTHGHFDHIGGLGELAEATDVPVIVVAE 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2568418062 120 DYFVAccwtmdtkgagtggqgavahfarhglldKDSQQKILERANYYPGLVYPPPSSFNRLIDERVIDIGGHAWTLISGY 199
Cdd:pfam00753  77 EAREL----------------------------LDEELGLAASRLGLPGPPVVPLPPDVVLEEGDGILGGGLGLLVTHGP 128

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2568418062 200 GHAPEHISLYCPDLAVLISGDMLLPRISTNVSVFDFEPEANPLPLYLNSVVKFLDL--PDDTLVLPSH 265
Cdd:pfam00753 129 GHGPGHVVVYYGGGKVLFTGDLLFAGEIGRLDLPLGGLLVLHPSSAESSLESLLKLakLKAAVIVPGH 196
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 44-265 1.28e-18

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: 82.22  E-value: 1.28e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2568418062   44 NCWLIADEyegqKGWTMVDCGINKPVVREVWEQifanELDGLPIVRVMVTHMHPDHVGLAGWHCSRWNVSLWMSMTDYFV 123
Cdd:smart00849   1 NSYLVRDD----GGAILIDTGPGEAEDLLAELK----KLGPKKIDAIILTHGHPDHIGGLPELLEAPGAPVYAPEGTAEL 72

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2568418062  124 AccwtmdtkgagtggqgavahfarhglldkdsqqKILERANYYPGLVYPPPSSFNRLIDERVIDIGGHAWTLISGYGHAP 203
Cdd:smart00849  73 L---------------------------------KDLLALLGELGAEAEPAPPDRTLKDGDELDLGGGELEVIHTPGHTP 119

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2568418062  204 EHISLYCPDLAVLISGDMLLPRIstnVSVFDFEPEANPLPLYLNSVVKFLDlPDDTLVLPSH 265
Cdd:smart00849 120 GSIVLYLPEGKILFTGDLLFAGG---DGRTLVDGGDAAASDALESLLKLLK-LLPKLVVPGH 177
yflN-like_MBL-fold cd07721
uncharacterized subgroup which includes Bacillus subtilis yflN; MBL-fold metallo hydrolase ...
 28-266 1.84e-15

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: 74.18  E-value: 1.84e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2568418062  28 GVKWIRLPLPfaldhINCWLIADEyegqKGWTMVDCGINKPVvREVWEQIFANELDGLPIVRVMVTHMHPDHVGLAGWHC 107
Cdd:cd07721     1 GVYQLPLLPP-----VNAYLIEDD----DGLTLIDTGLPGSA-KRILKALRELGLSPKDIRRILLTHGHIDHIGSLAALK 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2568418062 108 SRWNVSLWMSMTDyfvaccwtmdtkgagtggqgavAHFARHGLLDKDSQQKILeRANYYPGLVYPPPSSFNRLIDERVID 187
Cdd:cd07721    71 EAPGAPVYAHERE----------------------APYLEGEKPYPPPVRLGL-LGLLSPLLPVKPVPVDRTLEDGDTLD 127

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2568418062 188 IGGhAWTLISGYGHAPEHISLYCPDLAVLISGDMLlprISTNVSVFDFEPEANP-LPLYLNSVVKFLDLPDDTlVLPSHG 266
Cdd:cd07721   128 LAG-GLRVIHTPGHTPGHISLYLEEDGVLIAGDAL---VTVGGELVPPPPPFTWdMEEALESLRKLAELDPEV-LAPGHG 202
TTHA1623-like_MBL-fold cd16322
uncharacterized Thermus thermophilus TTHA1623 and related proteins; MBL-fold metallo hydrolase ...
 44-277 1.89e-15

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: 73.92  E-value: 1.89e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2568418062  44 NCWLIADEyeGQKGWTMVDCGINKpvvrevwEQIFAN-ELDGLPIVRVMVTHMHPDHVGLAGWHCSRWNVSLWMSMTDYF 122
Cdd:cd16322    12 NTYLVADE--GGGEAVLVDPGDES-------EKLLARfGTTGLTLLYILLTHAHFDHVGGVADLRRHPGAPVYLHPDDLP 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2568418062 123 VAccwtmdtkgagtggqGAVAHFARHGLLDkdsqqkileranyypglVYPPPSSFNRLIDERVIDIGGHAWTLISGYGHA 202
Cdd:cd16322    83 LY---------------EAADLGAKAFGLG-----------------IEPLPPPDRLLEDGQTLTLGGLEFKVLHTPGHS 130

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2568418062 203 PEHISLYCPDLAVLISGDMLLPRistNVSVFDFePEANPLPLYlNSVVKFLDLPDDTLVLPSHGRPFKGIKERVT 277
Cdd:cd16322   131 PGHVCFYVEEEGLLFSGDLLFQG---SIGRTDL-PGGDPKAMA-ASLRRLLTLPDETRVFPGHGPPTTLGEERRT 200
metallo-hydrolase-like_MBL-fold cd16282
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 54-268 9.01e-12

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


Pssm-ID: 293840 [Multi-domain]  Cd Length: 209  Bit Score: 63.74  E-value: 9.01e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2568418062  54 GQKGWTMVDCGINKPVVREVWEQIfaNELDGLPIVRVMVTHMHPDHVGlagwhcsrWNvslwmsmtDYFvaccwtmdtKG 133
Cdd:cd16282    22 GDDGVVVIDTGASPRLARALLAAI--RKVTDKPVRYVVNTHYHGDHTL--------GN--------AAF---------AD 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2568418062 134 AGT---GGQGAVAHFARHGLLDKDSQQKILERANYYPGLVYPppssfNRLIDER-VIDIGGHAWTLIS-GYGHAPEHISL 208
Cdd:cd16282    75 AGApiiAHENTREELAARGEAYLELMRRLGGDAMAGTELVLP-----DRTFDDGlTLDLGGRTVELIHlGPAHTPGDLVV 149

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2568418062 209 YCPDLAVLISGDMLLpristnVSVFDFEPEANPLPlYLNSVVKFLDLPDDTLVlPSHGRP 268
Cdd:cd16282   150 WLPEEGVLFAGDLVF------NGRIPFLPDGSLAG-WIAALDRLLALDATVVV-PGHGPV 201
metallo-hydrolase-like_MBL-fold cd16278
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 35-268 9.24e-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: 293836 [Multi-domain]  Cd Length: 185  Bit Score: 54.42  E-value: 9.24e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2568418062  35 PLPFALDHINCWLIADEyegqKGWTMVDCGinkPVVREVWEQIfANELDGLPIVRVMVTHMHPDHVGLAGWhcsrwnvsl 114
Cdd:cd16278    10 PSPMTLDGTNTYLLGAP----DGVVVIDPG---PDDPAHLDAL-LAALGGGRVSAILVTHTHRDHSPGAAR--------- 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2568418062 115 WMSMTdyfvaccwtmdtkGAGTGGQGAvahfARHGLLDKDsqqkileranyypglvyPPPSSfnRLIDERVIDIGGHAWT 194
Cdd:cd16278    73 LAERT-------------GAPVRAFGP----HRAGGQDTD-----------------FAPDR--PLADGEVIEGGGLRLT 116

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2568418062 195 LISGYGHAPEHISLYCPDLAVLISGDMLLPRISTNVSvfdfEPEANpLPLYLNSVVKFLDLPDDTLvLPSHGRP 268
Cdd:cd16278   117 VLHTPGHTSDHLCFALEDEGALFTGDHVMGWSTTVIA----PPDGD-LGDYLASLERLLALDDRLL-LPGHGPP 184
MBLAC2-like_MBL-fold cd07712
uncharacterized human metallo-beta-lactamase domain-containing protein 2 and related proteins; ...
 81-265 9.16e-08

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: 51.48  E-value: 9.16e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2568418062  81 ELDGLPIVrVMVTHMHPDHVGlagwhcsrwnvslwmsMTDYFvACCWtmdtkgagtggqgavAHFARHGLL-DKDSQQKI 159
Cdd:cd07712    38 TLTDLPLL-VVATHGHFDHIG----------------GLHEF-EEVY---------------VHPADAEILaAPDNFETL 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2568418062 160 LERANYYPGlvyPPPSSFNRLIDERVIDIGGHAWTLISGYGHAPEHISLYCPDLAVLISGDmllprISTNVSVFDFePEA 239
Cdd:cd07712    85 TWDAATYSV---PPAGPTLPLRDGDVIDLGDRQLEVIHTPGHTPGSIALLDRANRLLFSGD-----VVYDGPLIMD-LPH 155

                         170       180
                  ....*....|....*....|....*..
gi 2568418062 240 NPLPLYLNSVVKFLDLPDD-TLVLPSH 265
Cdd:cd07712   156 SDLDDYLASLEKLSKLPDEfDKVLPGH 182
YcbL-like_MBL-fold cd07737
Salmonella enterica serovar typhimurium YcbL and related proteins; MBL-fold metallo hydrolase ...
 44-265 1.11e-07

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: 51.40  E-value: 1.11e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2568418062  44 NCWLIADEYEGQKgwTMVDCG--INKpVVREVWEQifaneldGLPIVRVMVTHMHPDHVGLAGWHCSRWNVSLWMSmtdy 121
Cdd:cd07737    12 NCSLIWCEETKEA--AVIDPGgdADK-ILQAIEDL-------GLTLKKILLTHGHLDHVGGAAELAEHYGVPIIGP---- 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2568418062 122 fvaccwtmdtkgagtggqgavaHFARHGLLDKDSQQkilERANYYPGLVYPPPSSFnrLIDERVIDIGGHAWTLISGYGH 201
Cdd:cd07737    78 ----------------------HKEDKFLLENLPEQ---SQMFGFPPAEAFTPDRW--LEEGDTVTVGNLTLEVLHCPGH 130

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2568418062 202 APEHISLYCPDLAVLISGDMLLpristNVSV--FDFePEANPLPLYLNSVVKFLDLPDDTLVLPSH 265
Cdd:cd07737   131 TPGHVVFFNRESKLAIVGDVLF-----KGSIgrTDF-PGGNHAQLIASIKEKLLPLGDDVTFIPGH 190
hydroxyacylglutathione_hydrolase_MBL-fold cd07723
hydroxyacylglutathione hydrolase, MBL-fold metallo-hydrolase domain; hydroxyacylglutathione ...
 35-265 8.76e-07

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: 48.23  E-value: 8.76e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2568418062  35 PLPFALDhiN-CWLIADEyEGQKGWtMVDCGINKPVVRevweqiFANELdGLPIVRVMVTHMHPDHvglagwhcsrwnvs 113
Cdd:cd07723     2 PIPALSD--NyIYLIVDE-ATGEAA-VVDPGEAEPVLA------ALEKN-GLTLTAILTTHHHWDH-------------- 56

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2568418062 114 lwmsmtdyfvaccwtmdtkgagTGGqgavahfarhglldkdsqqkILERANYYPGL-VYPPPSSFNRLIDERV-----ID 187
Cdd:cd07723    57 ----------------------TGG--------------------NAELKALFPDApVYGPAEDRIPGLDHPVkdgdeIK 94

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2568418062 188 IGGHAWTLISGYGHAPEHISLYCPDLAVLISGDMLLpristnVS----VFdfepEANPlPLYLNSVVKFLDLPDDTLVLP 263
Cdd:cd07723    95 LGGLEVKVLHTPGHTLGHICYYVPDEPALFTGDTLF------SGgcgrFF----EGTA-EQMYASLQKLLALPDDTLVYC 163


                  ..
gi 2568418062 264 SH 265
Cdd:cd07723   164 GH 165
ST1585-like_MBL-fold cd07726
uncharacterized subgroup which includes Sulfolobus tokodaii ST1585 protein; MBL-fold metallo ...
 45-263 2.25e-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: 47.87  E-value: 2.25e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2568418062  45 CWLIadeyEGQKGWTMVDCGINK--PVVREVWEQ--IFANELDglpivRVMVTHMHPDHVGLAGwhcsrwnvslwmsmtd 120
Cdd:cd07726    18 SYLL----DGEGRPALIDTGPSSsvPRLLAALEAlgIAPEDVD-----YIILTHIHLDHAGGAG---------------- 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2568418062 121 YFVACCwtmdtkgagtggQGA--VAH--FARHgLLD----KDSQQKIL-ERANYYPGLVYPPPSSfnRLI---DERVIDI 188
Cdd:cd07726    73 LLAEAL------------PNAkvYVHprGARH-LIDpsklWASARAVYgDEADRLGGEILPVPEE--RVIvleDGETLDL 137

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2568418062 189 GGHAWTLISGYGHAPEHISLYCPDLAVLISGD---MLLPRISTNVSVF----DFEPEAnplplYLNSVVKFLDLPDDTLV 261
Cdd:cd07726   138 GGRTLEVIDTPGHAPHHLSFLDEESDGLFTGDaagVRYPELDVVGPPStpppDFDPEA-----WLESLDRLLSLKPERIY 212


                  ..
gi 2568418062 262 LP 263
Cdd:cd07726   213 LT 214
POD-like_MBL-fold cd07724
ETHE1 (PDO type I), persulfide dioxygenase A (PDOA, PDO type II) and related proteins; ...
 200-266 1.09e-05

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: 45.47  E-value: 1.09e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2568418062 200 GHAPEHISLYCPDLAVLISGDMLLPRiSTNVSvfDFEPEANPLP--LYlNSV-VKFLDLPDDTLVLPSHG 266
Cdd:cd07724   111 GHTPESVSYLVGDPDAVFTGDTLFVG-DVGRP--DLPGEAEGLArqLY-DSLqRKLLLLPDETLVYPGHD 176
arylsulfatase_Sdsa1-like_MBL-fold cd07710
Pseudomonas aeruginosa arylsulfatase SdsA1, Pseudomonas sp. DSM6611 arylsulfatase Pisa1, and ...
 23-101 1.98e-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: 45.18  E-value: 1.98e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2568418062  23 IEVAPGVKWIRlplpfALDHINCWLIadeyEGQKGWTMVDCGINKPVVREVWEQiFANELDGLPIVRVMVTHMHPDHVG 101
Cdd:cd07710     3 FEVTDGVYQVR-----GYDLSNMTFI----EGDTGLIIIDTLESAEAAKAALEL-FRKHTGDKPVKAIIYTHSHPDHFG 71
BaeB-like_MBL-fold cd16275
Bacillus amyloliquefaciens BaeB and related proteins; MBL-fold metallo hydrolase domain; ...
 38-117 2.42e-05

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: 44.06  E-value: 2.42e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2568418062  38 FALDHIN-CWLIADEYEGQkgwtmvdCGINKPVvrevW--EQIFA-NELDGLPIVRVMVTHMHPDHVGLAGWHCSRWNVS 113
Cdd:cd16275     6 KAGPMINySYIIIDKATRE-------AAVVDPA----WdiEKILAkLNELGLTLTGILLTHSHFDHVNLVEPLLAKYDAP 74


                  ....
gi 2568418062 114 LWMS 117
Cdd:cd16275    75 VYMS 78
AHL_lactonase_MBL-fold cd07729
quorum-quenching N-acyl-homoserine lactonase, MBL-fold metallo-hydrolase domain; Acyl ...
 30-101 5.96e-04

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: 40.66  E-value: 5.96e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2568418062  30 KWIRLPlpfaldhINCWLIadeyEGQKGWTMVDCGINKPVVREVWEQIFANELDGLPIVR-----------------VMV 92
Cdd:cd07729    26 EPIDLP-------VYAYLI----EHPEGTILVDTGFHPDAADDPGGLELAFPPGVTEEQTleeqlarlgldpedidyVIL 94


                  ....*....
gi 2568418062  93 THMHPDHVG 101
Cdd:cd07729    95 SHLHFDHAG 103
BDS1 COG2015
Alkyl sulfatase BDS1 and related hydrolases, metallo-beta-lactamase superfamily [Secondary ...
 24-101 1.05e-03

Alkyl sulfatase BDS1 and related hydrolases, metallo-beta-lactamase superfamily [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 441618 [Multi-domain]  Cd Length: 629  Bit Score: 40.98  E-value: 1.05e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2568418062  24 EVAPGVKWIRlplpfALDHINCWLIadeyEGQKGWTMVDCGINKPVVREVWEqiFANE-LDGLPIVRVMVTHMHPDHVG 101
Cdd:COG2015    89 EVTDGIYQVR-----GFDLANMTFI----EGDTGWIVIDPLTSVETAAAALA--LYRKhLGDRPVKAVIYTHSHVDHFG 156
LACTB2-like_MBL-fold cd07722
uncharacterized subgroup which includes human lactamase beta 2 and related proteins; MBL-fold ...
 60-266 2.06e-03

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: 38.67  E-value: 2.06e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2568418062  60 MVDCGINKPVvrevWEQIFANELDGLPIVR---VMVTHMHPDHVG-----LAgwHCSRWNVSLWMSMTDYfvaccwtmdt 131
Cdd:cd07722    31 LIDTGEGRPS----YIPLLKSVLDSEGNATisdILLTHWHHDHVGglpdvLD--LLRGPSPRVYKFPRPE---------- 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2568418062 132 kgagtggqgavahfarhglldkdsqqkileranyYPGLVYPPPSSFNRLIDERVIDIGGHAWTLISGYGHAPEHISLYCP 211
Cdd:cd07722    95 ----------------------------------EDEDPDEDGGDIHDLQDGQVFKVEGATLRVIHTPGHTTDHVCFLLE 140

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2568418062 212 DLAVLISGDMLLpriSTNVSVFDfepeanPLPLYLNSVVKFLDLPDDTLvLPSHG 266
Cdd:cd07722   141 EENALFTGDCVL---GHGTAVFE------DLAAYMASLKKLLSLGPGRI-YPGHG 185
SoxH_rel_PQQ_2 TIGR04559
quinoprotein relay system zinc metallohydrolase 2; By homology, members are Zn ...
 54-100 7.83e-03

quinoprotein relay system zinc metallohydrolase 2; By homology, members are Zn metallohydrolases in the same family as the SoxH protein associated with sulfate metabolism, Bacillus cereus beta-lactamase II (see PDB:1bc2), and, more distantly, hydroxyacylglutathione hydrolase (glyoxalase II). All members occur in genomes with both PQQ biosynthesis and a PQQ-dependent (quinoprotein) dehydrogenase that has a motif of two consecutive Cys residues (see TIGR03075). The Cys-Cys motif is associated with electron transfer by specialized cytochromes such as c551. All these genomes also include a fusion protein (TIGR04557) whose domains resemble SoxY and SoxZ from thiosulfate oxidation. A conserved Cys in this fusion protein aligns to the Cys residue in SoxY that carries sulfur cycle intermediates. In many genomes, the genes for PQQ biosynthesis enzymes, PQQ-dependent enzymes, their associated cytochromes, and members of this family are clustered. Note that one to three closely related Zn metallohydrolases may occur; this family represents a specific clade among them. Some members of this family have a short additional N-terminal domain with four conserved Cys residues. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 275352  Cd Length: 283  Bit Score: 37.56  E-value: 7.83e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 2568418062  54 GQKGWTMVDCGINKPVVREVWEQIfaNELDGLPIVRVMVTHMHPDHV 100
Cdd:TIGR04559  37 GEDAVAVIDTGGSRAEGEALLAAI--RQRTDLPIRYVINTHVHPDHI 81
 
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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