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Conserved domains on  [gi|446613816|ref|WP_000691162|]
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MULTISPECIES: MBL fold metallo-hydrolase [Bacillus]

Protein Classification

MBL fold metallo-hydrolase( domain architecture ID 10869930)

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

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
yflN-like_MBL-fold cd07721
uncharacterized subgroup which includes Bacillus subtilis yflN; MBL-fold metallo hydrolase ...
 19-223 1.04e-56

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: 178.95  E-value: 1.04e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446613816  19 IYPSLIILHNELTLVDTGYPSFLPLIENAILKHGYEMKNLKNIIITHYDDDHLGSVYDFKvKYPQINVIASEIESNYISG 98
Cdd:cd07721   11 VNAYLIEDDDGLTLIDTGLPGSAKRILKALRELGLSPKDIRRILLTHGHIDHIGSLAALK-EAPGAPVYAHEREAPYLEG 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446613816  99 DIKSERLVQAEEMLermsneekefgkwFIQQLKNIKHISVDEKVHDGQMI-LDNECQIVATPGHTSGHISLYFPNLDCVI 177
Cdd:cd07721   90 EKPYPPPVRLGLLG-------------LLSPLLPVKPVPVDRTLEDGDTLdLAGGLRVIHTPGHTPGHISLYLEEDGVLI 156

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 446613816 178 TGDAAVQENRELVIANPNFCLDIEKAKQSLNRIKSFKAAEYYCYHG 223
Cdd:cd07721  157 AGDALVTVGGELVPPPPPFTWDMEEALESLRKLAELDPEVLAPGHG 202
 
Name Accession Description Interval E-value
yflN-like_MBL-fold cd07721
uncharacterized subgroup which includes Bacillus subtilis yflN; MBL-fold metallo hydrolase ...
 19-223 1.04e-56

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: 178.95  E-value: 1.04e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446613816  19 IYPSLIILHNELTLVDTGYPSFLPLIENAILKHGYEMKNLKNIIITHYDDDHLGSVYDFKvKYPQINVIASEIESNYISG 98
Cdd:cd07721   11 VNAYLIEDDDGLTLIDTGLPGSAKRILKALRELGLSPKDIRRILLTHGHIDHIGSLAALK-EAPGAPVYAHEREAPYLEG 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446613816  99 DIKSERLVQAEEMLermsneekefgkwFIQQLKNIKHISVDEKVHDGQMI-LDNECQIVATPGHTSGHISLYFPNLDCVI 177
Cdd:cd07721   90 EKPYPPPVRLGLLG-------------LLSPLLPVKPVPVDRTLEDGDTLdLAGGLRVIHTPGHTPGHISLYLEEDGVLI 156

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 446613816 178 TGDAAVQENRELVIANPNFCLDIEKAKQSLNRIKSFKAAEYYCYHG 223
Cdd:cd07721  157 AGDALVTVGGELVPPPPPFTWDMEEALESLRKLAELDPEVLAPGHG 202
GloB COG0491
Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General ...
 19-227 2.87e-25

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: 98.22  E-value: 2.87e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446613816  19 IYPSLIILHNELTLVDTGY-PSFLPLIENAILKHGyemKNLKNIIITHYDDDHLGSVYDFKVKYpQINVIASEIESNYIS 97
Cdd:COG0491   15 VNSYLIVGGDGAVLIDTGLgPADAEALLAALAALG---LDIKAVLLTHLHPDHVGGLAALAEAF-GAPVYAHAAEAEALE 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446613816  98 GDIKSERLVQaeemlermsneekefgkwfiqqlkniKHISVDEKVHDGQMI--LDNECQIVATPGHTSGHISLYFPNLDC 175
Cdd:COG0491   91 APAAGALFGR--------------------------EPVPPDRTLEDGDTLelGGPGLEVIHTPGHTPGHVSFYVPDEKV 144

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 446613816 176 VITGDAAVQENRELVIAnpnFCLDIEKAKQSLNRIKSFKAAEYYCYHGGKLT 227
Cdd:COG0491  145 LFTGDALFSGGVGRPDL---PDGDLAQWLASLERLLALPPDLVIPGHGPPTT 193
Lactamase_B pfam00753
Metallo-beta-lactamase superfamily;
23-222 5.26e-20

Metallo-beta-lactamase superfamily;


Pssm-ID: 425851 [Multi-domain]  Cd Length: 196  Bit Score: 83.96  E-value: 5.26e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446613816   23 LIILHNELTLVDTGYPSFLPLIEnAILKHGYEMKNLKNIIITHYDDDHLGSVYDFKVKYPQINVIASEIesnyisgdiks 102
Cdd:pfam00753  10 LIEGGGGAVLIDTGGSAEAALLL-LLAALGLGPKDIDAVILTHGHFDHIGGLGELAEATDVPVIVVAEE----------- 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446613816  103 erlvqaeemLERMSNEEKEFGKWFIQQLKNIKHISVDEKVHDGQMILDNECQ---IVATPGHTSGHISLYFPNLDCVITG 179
Cdd:pfam00753  78 ---------ARELLDEELGLAASRLGLPGPPVVPLPPDVVLEEGDGILGGGLgllVTHGPGHGPGHVVVYYGGGKVLFTG 148

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 446613816  180 DAAVQENRELVIANPNFCLDI-----EKAKQSLNRIKSFKAAEYYCYH 222
Cdd:pfam00753 149 DLLFAGEIGRLDLPLGGLLVLhpssaESSLESLLKLAKLKAAVIVPGH 196
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 23-222 6.31e-20

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: 83.37  E-value: 6.31e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446613816    23 LIILHNELTLVDTGYPSFLPLIEnAILKHGyeMKNLKNIIITHYDDDHLGSVYDFKvKYPQINVIASEIESNYIsgdiks 102
Cdd:smart00849   4 LVRDDGGAILIDTGPGEAEDLLA-ELKKLG--PKKIDAIILTHGHPDHIGGLPELL-EAPGAPVYAPEGTAELL------ 73

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446613816   103 erlvqaeemlermsneeKEFGKWFIQQLKNIKHISVDEKVHDGQM--ILDNECQIVATPGHTSGHISLYFPNLDCVITGD 180
Cdd:smart00849  74 -----------------KDLLALLGELGAEAEPAPPDRTLKDGDEldLGGGELEVIHTPGHTPGSIVLYLPEGKILFTGD 136

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 446613816   181 AAVQENRELVIANPNFClDIEKAKQSLNRIKSFKAAEYYCYH 222
Cdd:smart00849 137 LLFAGGDGRTLVDGGDA-AASDALESLLKLLKLLPKLVVPGH 177
PLN02398 PLN02398
hydroxyacylglutathione hydrolase
 25-180 3.67e-11

hydroxyacylglutathione hydrolase


Pssm-ID: 215223 [Multi-domain]  Cd Length: 329  Bit Score: 61.40  E-value: 3.67e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446613816  25 ILHNEltlvDTGY-----PSFLPLIENAILKHGyemKNLKNIIITHYDDDHLGSVYDFKVKYPQiNVIASEIESNYISG- 98
Cdd:PLN02398  91 LLHDE----DTGTvgvvdPSEAVPVIDALSRKN---RNLTYILNTHHHYDHTGGNLELKARYGA-KVIGSAVDKDRIPGi 162

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446613816  99 DIKSerlvqaeemlermsneeKEFGKWfiqqlknikhisvdekvhdgqMILDNECQIVATPGHTSGHISLYFPNLDCVIT 178
Cdd:PLN02398 163 DIVL-----------------KDGDKW---------------------MFAGHEVLVMETPGHTRGHISFYFPGSGAIFT 204


                 ..
gi 446613816 179 GD 180
Cdd:PLN02398 205 GD 206
GSH_gloB TIGR03413
hydroxyacylglutathione hydrolase; Members of this protein family are hydroxyacylglutathione ...
 25-180 1.41e-08

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: 53.31  E-value: 1.41e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446613816   25 ILHNELT---LVDTGYPSflPLIEnAILKHGYemkNLKNIIITHYDDDHLGSVYDFKVKYPqINVIASEiesnyisgdik 101
Cdd:TIGR03413  14 LLHDPDGqaaVVDPGEAE--PVLD-ALEARGL---TLTAILLTHHHHDHVGGVAELLEAFP-APVYGPA----------- 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446613816  102 serlvqaeemlermsnEEKefgkwfiqqlknIKHIsvDEKVHDGQ--MILDNECQIVATPGHTSGHISLYFPNLDCVITG 179
Cdd:TIGR03413  76 ----------------EER------------IPGI--THPVKDGDtvTLGGLEFEVLAVPGHTLGHIAYYLPDSPALFCG 125


                  .
gi 446613816  180 D 180
Cdd:TIGR03413 126 D 126
 
Name Accession Description Interval E-value
yflN-like_MBL-fold cd07721
uncharacterized subgroup which includes Bacillus subtilis yflN; MBL-fold metallo hydrolase ...
 19-223 1.04e-56

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: 178.95  E-value: 1.04e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446613816  19 IYPSLIILHNELTLVDTGYPSFLPLIENAILKHGYEMKNLKNIIITHYDDDHLGSVYDFKvKYPQINVIASEIESNYISG 98
Cdd:cd07721   11 VNAYLIEDDDGLTLIDTGLPGSAKRILKALRELGLSPKDIRRILLTHGHIDHIGSLAALK-EAPGAPVYAHEREAPYLEG 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446613816  99 DIKSERLVQAEEMLermsneekefgkwFIQQLKNIKHISVDEKVHDGQMI-LDNECQIVATPGHTSGHISLYFPNLDCVI 177
Cdd:cd07721   90 EKPYPPPVRLGLLG-------------LLSPLLPVKPVPVDRTLEDGDTLdLAGGLRVIHTPGHTPGHISLYLEEDGVLI 156

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 446613816 178 TGDAAVQENRELVIANPNFCLDIEKAKQSLNRIKSFKAAEYYCYHG 223
Cdd:cd07721  157 AGDALVTVGGELVPPPPPFTWDMEEALESLRKLAELDPEVLAPGHG 202
GloB COG0491
Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General ...
 19-227 2.87e-25

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: 98.22  E-value: 2.87e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446613816  19 IYPSLIILHNELTLVDTGY-PSFLPLIENAILKHGyemKNLKNIIITHYDDDHLGSVYDFKVKYpQINVIASEIESNYIS 97
Cdd:COG0491   15 VNSYLIVGGDGAVLIDTGLgPADAEALLAALAALG---LDIKAVLLTHLHPDHVGGLAALAEAF-GAPVYAHAAEAEALE 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446613816  98 GDIKSERLVQaeemlermsneekefgkwfiqqlkniKHISVDEKVHDGQMI--LDNECQIVATPGHTSGHISLYFPNLDC 175
Cdd:COG0491   91 APAAGALFGR--------------------------EPVPPDRTLEDGDTLelGGPGLEVIHTPGHTPGHVSFYVPDEKV 144

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 446613816 176 VITGDAAVQENRELVIAnpnFCLDIEKAKQSLNRIKSFKAAEYYCYHGGKLT 227
Cdd:COG0491  145 LFTGDALFSGGVGRPDL---PDGDLAQWLASLERLLALPPDLVIPGHGPPTT 193
Lactamase_B pfam00753
Metallo-beta-lactamase superfamily;
23-222 5.26e-20

Metallo-beta-lactamase superfamily;


Pssm-ID: 425851 [Multi-domain]  Cd Length: 196  Bit Score: 83.96  E-value: 5.26e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446613816   23 LIILHNELTLVDTGYPSFLPLIEnAILKHGYEMKNLKNIIITHYDDDHLGSVYDFKVKYPQINVIASEIesnyisgdiks 102
Cdd:pfam00753  10 LIEGGGGAVLIDTGGSAEAALLL-LLAALGLGPKDIDAVILTHGHFDHIGGLGELAEATDVPVIVVAEE----------- 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446613816  103 erlvqaeemLERMSNEEKEFGKWFIQQLKNIKHISVDEKVHDGQMILDNECQ---IVATPGHTSGHISLYFPNLDCVITG 179
Cdd:pfam00753  78 ---------ARELLDEELGLAASRLGLPGPPVVPLPPDVVLEEGDGILGGGLgllVTHGPGHGPGHVVVYYGGGKVLFTG 148

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 446613816  180 DAAVQENRELVIANPNFCLDI-----EKAKQSLNRIKSFKAAEYYCYH 222
Cdd:pfam00753 149 DLLFAGEIGRLDLPLGGLLVLhpssaESSLESLLKLAKLKAAVIVPGH 196
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 23-222 6.31e-20

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: 83.37  E-value: 6.31e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446613816    23 LIILHNELTLVDTGYPSFLPLIEnAILKHGyeMKNLKNIIITHYDDDHLGSVYDFKvKYPQINVIASEIESNYIsgdiks 102
Cdd:smart00849   4 LVRDDGGAILIDTGPGEAEDLLA-ELKKLG--PKKIDAIILTHGHPDHIGGLPELL-EAPGAPVYAPEGTAELL------ 73

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446613816   103 erlvqaeemlermsneeKEFGKWFIQQLKNIKHISVDEKVHDGQM--ILDNECQIVATPGHTSGHISLYFPNLDCVITGD 180
Cdd:smart00849  74 -----------------KDLLALLGELGAEAEPAPPDRTLKDGDEldLGGGELEVIHTPGHTPGSIVLYLPEGKILFTGD 136

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 446613816   181 AAVQENRELVIANPNFClDIEKAKQSLNRIKSFKAAEYYCYH 222
Cdd:smart00849 137 LLFAGGDGRTLVDGGDA-AASDALESLLKLLKLLPKLVVPGH 177
metallo-hydrolase-like_MBL-fold cd06262
mainly hydrolytic enzymes and related proteins which carry out various biological functions; ...
 28-223 1.39e-18

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: 80.02  E-value: 1.39e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446613816  28 NELTLVDTGYPSFLPLIEnAILKHGyemKNLKNIIITHYDDDHLGSVYDFKvKYPQINVIASEIEsnyisgdikserlvq 107
Cdd:cd06262   20 GEAILIDPGAGALEKILE-AIEELG---LKIKAILLTHGHFDHIGGLAELK-EAPGAPVYIHEAD--------------- 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446613816 108 aEEMLERMSNEEKEFGkwfiqqLKNIKHISVDEKVHDGQMIL--DNECQIVATPGHTSGHISLYFPNLDCVITGDAAVqe 185
Cdd:cd06262   80 -AELLEDPELNLAFFG------GGPLPPPEPDILLEDGDTIElgGLELEVIHTPGHTPGSVCFYIEEEGVLFTGDTLF-- 150

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 446613816 186 nRELVIANPNFCLDIEKAKQSLNRIKSFKAAEYYCYHG 223
Cdd:cd06262  151 -AGSIGRTDLPGGDPEQLIESIKKLLLLLPDDTVVYPG 187
ST1585-like_MBL-fold cd07726
uncharacterized subgroup which includes Sulfolobus tokodaii ST1585 protein; MBL-fold metallo ...
 23-221 1.00e-16

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: 75.61  E-value: 1.00e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446613816  23 LIILHNELTLVDTGYPSFLPLIENAILKHGYEMKNLKNIIITHYDDDHLGSVYDFKVKYPQINVIASEIESNYIsgdIKS 102
Cdd:cd07726   20 LLDGEGRPALIDTGPSSSVPRLLAALEALGIAPEDVDYIILTHIHLDHAGGAGLLAEALPNAKVYVHPRGARHL---IDP 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446613816 103 ERLVQAEEML--ERMsneEKEFGKwfiqqlknIkhISVDEK----VHDGQM--ILDNECQIVATPGHTSGHISLYFPNLD 174
Cdd:cd07726   97 SKLWASARAVygDEA---DRLGGE--------I--LPVPEErvivLEDGETldLGGRTLEVIDTPGHAPHHLSFLDEESD 163

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 446613816 175 CVITGDAAVQENRELVIANPNFC----LDIEKAKQSLNRIKSFKaAEYYCY 221
Cdd:cd07726  164 GLFTGDAAGVRYPELDVVGPPSTpppdFDPEAWLESLDRLLSLK-PERIYL 213
hydroxyacylglutathione_hydrolase_MBL-fold cd07723
hydroxyacylglutathione hydrolase, MBL-fold metallo-hydrolase domain; hydroxyacylglutathione ...
 25-180 3.36e-16

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: 73.26  E-value: 3.36e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446613816  25 ILHNELT----LVDTGYPSflpLIENAILKHGYEmknLKNIIITHYDDDHLGSVYDFKVKYPQINVIASeiesnyisgdi 100
Cdd:cd07723   13 LIVDEATgeaaVVDPGEAE---PVLAALEKNGLT---LTAILTTHHHWDHTGGNAELKALFPDAPVYGP----------- 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446613816 101 kserlvqaeemlermsneekefgkwfiqqlKNIKHISVDEKVHDGQMI--LDNECQIVATPGHTSGHISLYFPNLDCVIT 178
Cdd:cd07723   76 ------------------------------AEDRIPGLDHPVKDGDEIklGGLEVKVLHTPGHTLGHICYYVPDEPALFT 125


                 ..
gi 446613816 179 GD 180
Cdd:cd07723  126 GD 127
AHL_lactonase_MBL-fold cd07729
quorum-quenching N-acyl-homoserine lactonase, MBL-fold metallo-hydrolase domain; Acyl ...
 20-217 1.77e-15

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: 72.63  E-value: 1.77e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446613816  20 YPSLIILHNELT-LVDTGYPSFLP------------------LIENAILKHGYEMKNLKNIIITHYDDDHLGSVYDFkvk 80
Cdd:cd07729   32 VYAYLIEHPEGTiLVDTGFHPDAAddpgglelafppgvteeqTLEEQLARLGLDPEDIDYVILSHLHFDHAGGLDLF--- 108

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446613816  81 yPQINVIASEIESNYISGDIkserlvqaeeMLERMSNEEKEFGKWFIQQLkNIKHISVDEKVHDGqmildneCQIVATPG 160
Cdd:cd07729  109 -PNATIIVQRAELEYATGPD----------PLAAGYYEDVLALDDDLPGG-RVRLVDGDYDLFPG-------VTLIPTPG 169

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 446613816 161 HTSGHISLYF--PNLDCVITGDAA-VQENRELVIAnPNFCLDIEKAKQSLNRIKSFKAAE 217
Cdd:cd07729  170 HTPGHQSVLVrlPEGTVLLAGDAAyTYENLEEGRP-PGINYDPEAALASLERLKALAERE 228
metallo-hydrolase-like_MBL-fold cd16280
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 30-171 8.23e-14

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: 68.38  E-value: 8.23e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446613816  30 LTLVDTGY-PSFLPLIENAILKHGYEMKNLKNIIITHYDDDHLGSVYDFKVKYpQINVIASEiesnyisgdikserlvQA 108
Cdd:cd16280   33 LILIDALNnNEAADLIVDGLEKLGLDPADIKYILITHGHGDHYGGAAYLKDLY-GAKVVMSE----------------AD 95

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446613816 109 EEMLERMsNEEKEFGKWFiqqlkniKHISVDEKVHDGQMIL--DNECQIVATPGHTSGHISLYFP 171
Cdd:cd16280   96 WDMMEEP-PEEGDNPRWG-------PPPERDIVIKDGDTLTlgDTTITVYLTPGHTPGTLSLIFP 152
PLN02398 PLN02398
hydroxyacylglutathione hydrolase
 25-180 3.67e-11

hydroxyacylglutathione hydrolase


Pssm-ID: 215223 [Multi-domain]  Cd Length: 329  Bit Score: 61.40  E-value: 3.67e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446613816  25 ILHNEltlvDTGY-----PSFLPLIENAILKHGyemKNLKNIIITHYDDDHLGSVYDFKVKYPQiNVIASEIESNYISG- 98
Cdd:PLN02398  91 LLHDE----DTGTvgvvdPSEAVPVIDALSRKN---RNLTYILNTHHHYDHTGGNLELKARYGA-KVIGSAVDKDRIPGi 162

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446613816  99 DIKSerlvqaeemlermsneeKEFGKWfiqqlknikhisvdekvhdgqMILDNECQIVATPGHTSGHISLYFPNLDCVIT 178
Cdd:PLN02398 163 DIVL-----------------KDGDKW---------------------MFAGHEVLVMETPGHTRGHISFYFPGSGAIFT 204


                 ..
gi 446613816 179 GD 180
Cdd:PLN02398 205 GD 206
metallo-hydrolase-like_MBL-fold cd07743
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 28-219 6.61e-10

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


Pssm-ID: 293829 [Multi-domain]  Cd Length: 197  Bit Score: 56.77  E-value: 6.61e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446613816  28 NELTLVDTGYPSFLPLIENAILKHGYEmkNLKNIIITHYDDDHLGSVYDFKvKYPQINVIASEIESNYIsgdiksERLVQ 107
Cdd:cd07743   18 KEALLIDSGLDEDAGRKIRKILEELGW--KLKAIINTHSHADHIGGNAYLQ-KKTGCKVYAPKIEKAFI------ENPLL 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446613816 108 AEEMLermsneekeFGKWFIQQLKN----IKHISVDEKVHDGQMILDNEC-QIVATPGHTSGHISLYFPNlDCVITGDAA 182
Cdd:cd07743   89 EPSYL---------GGAYPPKELRNkflmAKPSKVDDIIEEGELELGGVGlEIIPLPGHSFGQIGILTPD-GVLFAGDAL 158

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 446613816 183 VQENrelVIAN--PNFCLDIEKAKQSLNRIKSFKaAEYY 219
Cdd:cd07743  159 FGEE---VLEKygIPFLYDVEEQLETLEKLEELD-ADYY 193
MBLAC1-like_MBL-fold cd07711
uncharacterized human metallo-beta-lactamase domain-containing protein 1 and related proteins; ...
 32-210 6.91e-10

uncharacterized human metallo-beta-lactamase domain-containing protein 1 and related proteins; MBL-fold metallo hydrolase domain; Includes the MBL-fold metallo hydrolase domain of uncharacterized human MBLAC1 and related proteins. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions.


Pssm-ID: 293797 [Multi-domain]  Cd Length: 190  Bit Score: 56.44  E-value: 6.91e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446613816  32 LVDTGYPSFLPLIENAILKHGYEMKNLKNIIITHYDDDHLGSVYDFkvkyPQINVIASEIESNYisgdikserlvqaeem 111
Cdd:cd07711   35 LVDTGTPWDRDLLLKALAEHGLSPEDIDYVVLTHGHPDHIGNLNLF----PNATVIVGWDICGD---------------- 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446613816 112 lermsneekEFGKWfiqqlknikhisvDEKVHDGqMILDNECQIVATPGHTSGHISLYFPNLD---CVITGDA-AVQENR 187
Cdd:cd07711   95 ---------SYDDH-------------SLEEGDG-YEIDENVEVIPTPGHTPEDVSVLVETEKkgtVAVAGDLfEREEDL 151

                        170       180
                 ....*....|....*....|...
gi 446613816 188 ELVIANPNFCLDIEKAKQSLNRI 210
Cdd:cd07711  152 EDPILWDPLSEDPELQEESRKRI 174
GSH_gloB TIGR03413
hydroxyacylglutathione hydrolase; Members of this protein family are hydroxyacylglutathione ...
 25-180 1.41e-08

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: 53.31  E-value: 1.41e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446613816   25 ILHNELT---LVDTGYPSflPLIEnAILKHGYemkNLKNIIITHYDDDHLGSVYDFKVKYPqINVIASEiesnyisgdik 101
Cdd:TIGR03413  14 LLHDPDGqaaVVDPGEAE--PVLD-ALEARGL---TLTAILLTHHHHDHVGGVAELLEAFP-APVYGPA----------- 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446613816  102 serlvqaeemlermsnEEKefgkwfiqqlknIKHIsvDEKVHDGQ--MILDNECQIVATPGHTSGHISLYFPNLDCVITG 179
Cdd:TIGR03413  76 ----------------EER------------IPGI--THPVKDGDtvTLGGLEFEVLAVPGHTLGHIAYYLPDSPALFCG 125


                  .
gi 446613816  180 D 180
Cdd:TIGR03413 126 D 126
POD-like_MBL-fold cd07724
ETHE1 (PDO type I), persulfide dioxygenase A (PDOA, PDO type II) and related proteins; ...
 138-181 1.02e-07

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: 50.09  E-value: 1.02e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 446613816 138 VDEKVHDGQMI-LDN-ECQIVATPGHTSGHISLYFPNLDCVITGDA 181
Cdd:cd07724   87 FDRLLKDGDVLeLGNlTLEVLHTPGHTPESVSYLVGDPDAVFTGDT 132
LACTB2-like_MBL-fold cd07722
uncharacterized subgroup which includes human lactamase beta 2 and related proteins; MBL-fold ...
 32-223 1.26e-07

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: 50.22  E-value: 1.26e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446613816  32 LVDTG--YPSFLPLIENAILKHGYEMknLKNIIITHYDDDHLGSVydfkvkypqinviaSEIESNYISGDIKserlvqae 109
Cdd:cd07722   31 LIDTGegRPSYIPLLKSVLDSEGNAT--ISDILLTHWHHDHVGGL--------------PDVLDLLRGPSPR-------- 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446613816 110 eMLERMSNEEKEFGKWFIQQLKNIkhisvdekvHDGQMI------LdnecQIVATPGHTSGHISLYFPNLDCVITGDA-- 181
Cdd:cd07722   87 -VYKFPRPEEDEDPDEDGGDIHDL---------QDGQVFkvegatL----RVIHTPGHTTDHVCFLLEEENALFTGDCvl 152

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 446613816 182 ----AVQEN-RELVianpnfcldiekakQSLNRIKSFKAAEYYCYHG 223
Cdd:cd07722  153 ghgtAVFEDlAAYM--------------ASLKKLLSLGPGRIYPGHG 185
BJP-1_FEZ-1-like_MBL-B3 cd16288
BJP-1, FEZ-1, GOB-1, Mbl1b and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 30-211 6.93e-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: 48.47  E-value: 6.93e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446613816  30 LTLVDTGYPSFLPLIENAILKHGYEMKNLKNIIITHYDDDHLGSVYDFKvKYPQINVIASEiesnyisGDIkserlvqae 109
Cdd:cd16288   33 LILIDTGLESSAPMIKANIRKLGFKPSDIKILLNSHAHLDHAGGLAALK-KLTGAKLMASA-------EDA--------- 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446613816 110 EMLERMSNEEKEFG-KWFIQQlknikHISVDEKVHDGQMILDNECQIVA--TPGHTSGHISLYFP------NLDCVITGD 180
Cdd:cd16288   96 ALLASGGKSDFHYGdDSLAFP-----PVKVDRVLKDGDRVTLGGTTLTAhlTPGHTRGCTTWTMTvkddgkVYQVVFADS 170

                        170       180       190
                 ....*....|....*....|....*....|...
gi 446613816 181 AAVQENRELV--IANPNFCLDIEKAKQSLNRIK 211
Cdd:cd16288  171 LTVNPGYKLVgnPTYPGIAEDYRHSFATLRALQ 203
TTHA1623-like_MBL-fold cd16322
uncharacterized Thermus thermophilus TTHA1623 and related proteins; MBL-fold metallo hydrolase ...
 32-228 7.59e-07

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: 48.11  E-value: 7.59e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446613816  32 LVDTGYPSflpliENAILKHGYEMKNLKNIIITHYDDDHLGSVYDFKvKYPQINVIASEIESnyisgdikserlvqaeem 111
Cdd:cd16322   26 LVDPGDES-----EKLLARFGTTGLTLLYILLTHAHFDHVGGVADLR-RHPGAPVYLHPDDL------------------ 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446613816 112 leRMSNEEKEFGKWFiqQLKNIKHISVDEKVHDGQMI-LDN-ECQIVATPGHTSGHISLYFPNLDCVITGDAAVQENrel 189
Cdd:cd16322   82 --PLYEAADLGAKAF--GLGIEPLPPPDRLLEDGQTLtLGGlEFKVLHTPGHSPGHVCFYVEEEGLLFSGDLLFQGS--- 154

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 446613816 190 vIANPNFCLDIEKA-KQSLNRI-KSFKAAEYYCYHGGKLTV 228
Cdd:cd16322  155 -IGRTDLPGGDPKAmAASLRRLlTLPDETRVFPGHGPPTTL 194
BaeB-like_MBL-fold cd16275
Bacillus amyloliquefaciens BaeB and related proteins; MBL-fold metallo hydrolase domain; ...
 44-180 3.67e-06

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: 45.61  E-value: 3.67e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446613816  44 IENAILKHGYEMKNLKNIIITHYDDDHLGSVyDFKVKYPQINVIASEIESNYiSGdIKSERLVQaeemlermsneekefg 123
Cdd:cd16275   34 IEKILAKLNELGLTLTGILLTHSHFDHVNLV-EPLLAKYDAPVYMSKEEIDY-YG-FRCPNLIP---------------- 94

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 446613816 124 kwfiqqlknikhisvdekVHDGQMIL--DNECQIVATPGHTSGHISLYFPnlDCVITGD 180
Cdd:cd16275   95 ------------------LEDGDTIKigDTEITCLLTPGHTPGSMCYLLG--DSLFTGD 133
metallo-hydrolase-like_MBL-fold cd16278
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 139-180 7.06e-06

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


Pssm-ID: 293836 [Multi-domain]  Cd Length: 185  Bit Score: 45.17  E-value: 7.06e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 446613816 139 DEKVHDGQMILDNECQI--VATPGHTSGHISLYFPNLDCVITGD 180
Cdd:cd16278   99 DRPLADGEVIEGGGLRLtvLHTPGHTSDHLCFALEDEGALFTGD 142
TTHA1429-like_MBL-fold cd07725
uncharacterized Thermus thermophilus TTHA1429 and related proteins; MBL-fold metallo hydrolase ...
 28-181 9.60e-06

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: 44.60  E-value: 9.60e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446613816  28 NELTLVDTGYPSFL--PLIENAILKHGYEMKNLKNIIITHYDDDHLGsvydfkvkypqinvIASEIESnyisgdiKSERL 105
Cdd:cd07725   24 DETTLIDTGLATEEdaEALWEGLKELGLKPSDIDRVLLTHHHPDHIG--------------LAGKLQE-------KSGAT 82

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446613816 106 VqaeemlerMSNEEKEFGkwfiqqlknikhisvdekvhDGQMI--LDNECQIVATPGHTSGHISLYFPNLDCVITGDA 181
Cdd:cd07725   83 V--------YILDVTPVK--------------------DGDKIdlGGLRLKVIETPGHTPGHIVLYDEDRRELFVGDA 132
YmaE-like_MBL-fold cd07727
uncharacterized subgroup which includes Bacillus subtilis YmaE and related proteins; MBL-fold ...
 149-224 1.65e-05

uncharacterized subgroup which includes Bacillus subtilis YmaE and related proteins; MBL-fold metallo hydrolase domain; Includes the uncharacterized Bacillus subtilis YmaE and Nostoc all1228 proteins.Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions. The class B metal beta-lactamases (MBLs) from which this fold was named are only a small fraction of the activities which are included in this superfamily. Activities carried out by superfamily members include class B beta-lactamases, hydroxyacylglutathione hydrolases, AHL (acyl homoserine lactone) lactonases, persulfide dioxygenases, flavodiiron proteins, cleavage and polyadenylation specificity factors such as the Int9 and Int11 subunits of Integrator, Sdsa1-like and AtsA-like arylsulfatases, 5'-exonucleases human SNM1A and yeast Pso2p, ribonuclease J and ribonuclease Z, cyclic nucleotide phosphodiesterases, insecticide hydrolases, and proteins required for natural transformation competence. Classical members of the superfamily are di-, or less commonly mono-, zinc-ion-dependent hydrolases, however the diversity of biological roles is reflected in variations in the active site metallo-chemistry.


Pssm-ID: 293813 [Multi-domain]  Cd Length: 181  Bit Score: 43.72  E-value: 1.65e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446613816 149 LDNECQIVATPGHTSGHISLYFPNLDCVITGDA-AVQENRELVIANPNFCL-DIEKAKQSLNRIKSFKAAEYYCYHGG 224
Cdd:cd07727  100 LDPDLTLIPVPGHTRGSVVLLYKEKGVLFTGDHlAWSRRRGWLSAFRYVCWySWPEQAESVERLADLDFEWVLPGHGR 177
MBL-B3-like cd07708
metallo-beta-lactamases, subclass B3; MBL-fold metallo-hydrolase domain; MBLs (class B of the ...
 30-167 2.32e-05

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: 44.07  E-value: 2.32e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446613816  30 LTLVDTGYPSFLPLIENAILKHGYEMKNLKNIIITHYDDDHLGSVYDFKvkypqinviaSEIESNYISGDikserlvQAE 109
Cdd:cd07708   33 NILIDGDMEQNAPMIKANIKKLGFKFSDTKLILISHAHFDHAGGSAEIK----------KQTGAKVMAGA-------EDV 95

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 446613816 110 EMLERMSNEEKEFGKwfiQQLKNIKHISVDEKVHDGQMILDNECQIVA--TPGHTSGHIS 167
Cdd:cd07708   96 SLLLSGGSSDFHYAN---DSSTYFPQSTVDRAVHDGERVTLGGTVLTAhaTPGHTPGCTT 152
YcbL-like_MBL-fold cd07737
Salmonella enterica serovar typhimurium YcbL and related proteins; MBL-fold metallo hydrolase ...
 41-180 2.42e-05

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: 43.70  E-value: 2.42e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446613816  41 LPLIENAILKHGYEmknLKNIIITHYDDDHLGSVYDFKVKYpQINVIASEIESNYisgdikserlvqaeeMLERMSNEEK 120
Cdd:cd07737   33 ADKILQAIEDLGLT---LKKILLTHGHLDHVGGAAELAEHY-GVPIIGPHKEDKF---------------LLENLPEQSQ 93

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446613816 121 EFGkwfiqqLKNIKHISVDEKVHDGQMIL--DNECQIVATPGHTSGHISLYFPNLDCVITGD 180
Cdd:cd07737   94 MFG------FPPAEAFTPDRWLEEGDTVTvgNLTLEVLHCPGHTPGHVVFFNRESKLAIVGD 149
GOB1-like_MBL-B3 cd16308
Elizabethkingia meningoseptica GOB-1 and related metallo-beta-lactamases, subclass B3; ...
 32-174 3.25e-05

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


Pssm-ID: 293866 [Multi-domain]  Cd Length: 254  Bit Score: 43.61  E-value: 3.25e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446613816  32 LVDTGYPSFLPLIENAILKHGYEMKNLKNIIITHYDDDHLGSVYDFKvKYPQINVIASEiesnyisGDIKserlvqaeeM 111
Cdd:cd16308   35 LINTGLAESVPLIKKNIQALGFKFKDIKILLTTQAHYDHVGAMAAIK-QQTGAKMMVDE-------KDAK---------V 97

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446613816 112 LERMSNEEKEFGKWFIqqlkNIKHISVDEKVHDGQMILDNECQIVAT--PGHTSGHISLYFPNLD 174
Cdd:cd16308   98 LADGGKSDYEMGGYGS----TFAPVKADKLLHDGDTIKLGGTKLTLLhhPGHTKGSCSFLFDVKD 158
metallo-hydrolase-like_MBL-fold cd07730
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 14-217 3.38e-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) 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. Some members of this subgroup are annotated as GumP protein.


Pssm-ID: 293816 [Multi-domain]  Cd Length: 250  Bit Score: 43.41  E-value: 3.38e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446613816  14 GQKQCIYPSL--IILHNELT--LVDTGY--------PSFLPLIEN------------AIL-KHGYEMKNLKNIIITHYDD 68
Cdd:cd07730   15 PLKRVTFPALafLIEHPTGGkiLFDLGYrkdfeeytPRVPERLYRtpvpleveedvaEQLaAGGIDPEDIDAVILSHLHW 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446613816  69 DHLGSVYDFkvkyPQINVIASE------IESNYISGDIKSerlVQAEEMLERMSNEEKEFGKWfiqqlkniKHISVDEKV 142
Cdd:cd07730   95 DHIGGLSDF----PNARLIVGPgakealRPPGYPSGFLPE---LLPSDFEGRLVRWEEDDFLW--------VPLGPFPRA 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446613816 143 HD--GqmilDNECQIVATPGHTSGHISLYFPNL---------DCVITGDAAVQENRELVIANPNFCLDIEKAKQSLNRIK 211
Cdd:cd07730  160 LDlfG----DGSLYLVDLPGHAPGHLGLLARTTsgtwvflagDACHHRIGLLRPSPLLPLPDLDDGADREAARETLARLR 235


                 ....*.
gi 446613816 212 SFKAAE 217
Cdd:cd07730  236 ELDAAP 241
NorV COG0426
Flavorubredoxin [Energy production and conversion];
20-91 3.52e-05

Flavorubredoxin [Energy production and conversion];


Pssm-ID: 440195 [Multi-domain]  Cd Length: 390  Bit Score: 44.05  E-value: 3.52e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446613816  20 YPSLIILHNELTLVDTGYPSFLP-LIENaiLKHGYEMKNLKNIIITHYDDDHLGSVYDFKVKYPQINVIASEI 91
Cdd:COG0426   34 YNSYLIVDEKTALIDTVGESFFEeFLEN--LSKVIDPKKIDYIIVNHQEPDHSGSLPELLELAPNAKIVCSKK 104
metallo-hydrolase-like_MBL-fold cd07739
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 22-181 4.34e-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: 42.87  E-value: 4.34e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446613816  22 SLIILHNELTLVDTGYpsflpLIENA------ILKHGyemKNLKNIIITHYDDDHLGSVYDFKVKYPQINVIAseiesny 95
Cdd:cd07739   19 TLIYGETEAVLVDAQF-----TRADAerladwIKASG---KTLTTIYITHGHPDHYFGLEVLLEAFPDAKVVA------- 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446613816  96 isgdikserlvqAEEMLERMSNE-EKEFGKWFIQQLKNI-KHISVDEKVHDGQMILDNE-CQIVATPGHTSGHIS-LYFP 171
Cdd:cd07739   84 ------------TPAVVAHIKAQlEPKLAFWGPLLGGNApARLVVPEPLDGDTLTLEGHpLEIVGVGGGDTDDTTyLWIP 151

                        170
                 ....*....|
gi 446613816 172 NLDCVITGDA 181
Cdd:cd07739  152 SLKTVVAGDV 161
PRK10241 PRK10241
hydroxyacylglutathione hydrolase; Provisional
 46-175 4.85e-05

hydroxyacylglutathione hydrolase; Provisional


Pssm-ID: 182327 [Multi-domain]  Cd Length: 251  Bit Score: 43.27  E-value: 4.85e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446613816  46 NAILKHGYEMKNlknIIITHYDDDHLGSVYDFKVKYPQINVIASEiESnyisgdikserlvqaeemlermsneekefgkw 125
Cdd:PRK10241  37 NAIAENNWQPEA---IFLTHHHHDHVGGVKELVEKFPQIVVYGPQ-ET-------------------------------- 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 446613816 126 fiqQLKNIKHIsvdekVHDGQ--MILDNECQIVATPGHTSGHISLY-FPNLDC 175
Cdd:PRK10241  81 ---QDKGTTQV-----VKDGEtaFVLGHEFSVFATPGHTLGHICYFsKPYLFC 125
flavodiiron_proteins_MBL-fold cd07709
catalytic domain of flavodiiron proteins (FDPs) and related proteins; MBL-fold ...
 24-91 5.94e-05

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


Pssm-ID: 293795 [Multi-domain]  Cd Length: 238  Bit Score: 42.86  E-value: 5.94e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446613816  24 IILHNELTLVDTGYPSFLPLIENAILKHGyEMKNLKNIIITHYDDDHLGSVYDFKVKYPQINVIASEI 91
Cdd:cd07709   36 LIKDEKTALIDTVKEPFFDEFLENLEEVI-DPRKIDYIVVNHQEPDHSGSLPELLELAPNAKIVCSKK 102
metallo-hydrolase-like_MBL-fold cd16282
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 32-180 6.42e-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) 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: 42.55  E-value: 6.42e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446613816  32 LVDTGYPsflPLIENAILKhgyEMKNLKN-----IIITHYDDDH-LGSVYdFKVKYPQInvIASEIesnyisgdikserl 105
Cdd:cd16282   28 VIDTGAS---PRLARALLA---AIRKVTDkpvryVVNTHYHGDHtLGNAA-FADAGAPI--IAHEN-------------- 84

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446613816 106 vQAEEMLERMSNEEKEFGKWFIQQLKNIKHISVDEKVhDGQMILD---NECQIVAT-PGHTSGHISLYFPNLDCVITGD 180
Cdd:cd16282   85 -TREELAARGEAYLELMRRLGGDAMAGTELVLPDRTF-DDGLTLDlggRTVELIHLgPAHTPGDLVVWLPEEGVLFAGD 161
BJP-1-like_MBL-B3 cd16309
Bradyrhizobium diazoefficiens BJP-1 and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 23-164 7.64e-05

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: 42.47  E-value: 7.64e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446613816  23 LIILHNELTLVDTGYPSFLPLIENAILKHGYEMKNLKNIIITHYDDDHLGSVYDFKvKYPQINVIASEIESNYISGdiks 102
Cdd:cd16309   26 LITTPEGHILIDGAMPQSTPLIKDNIKKLGFDVKDVKYLLNTHAHFDHAGGLAELK-KATGAQLVASAADKPLLES---- 100

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446613816 103 erlvqaeemlermsneekefGKWFIQQLKNIKH--ISVDEKVHDGQMILDNECQIVA--TPGHTSG 164
Cdd:cd16309  101 --------------------GYVGSGDTKNLQFppVRVDRVIGDGDKVTLGGTTLTAhlTPGHSPG 146
Mbl1b-like_MBL-B3 cd16310
Caulobacter crescentus Mbl1b and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 23-164 8.35e-05

Caulobacter crescentus Mbl1b and related metallo-beta-lactamases, subclass B3; MBL-fold metallo-hydrolase domain; MBLs (class B of the Ambler beta-lactamase classification) are a diverse group of metallo-enzymes that are capable of catalyzing the hydrolysis of a wide range of beta-lactam antibiotics. MBLs have been divided into three subclasses B1, B2 and B3, based on sequence/structural relationships and substrates, with the B1 and B2 MBLs being most closely related to each other. This subgroup of Mbl1b-like MBLs belongs to the B3 subclass. Subclass B3 enzymes are most active with two zinc ions bound in the active site, and have a broad-spectrum substrate profile. These B3 enzymes have a modified Zn2/DCH site (Asp-His-His).


Pssm-ID: 293868  Cd Length: 252  Bit Score: 42.44  E-value: 8.35e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446613816  23 LIILHNELTLVDTGYPSFLPLIENAILKHGYEMKNLKNIIITHYDDDHLGSVYDFKvKYPQINVIASEiesnyisGDIKS 102
Cdd:cd16310   26 LITSNHGAILLDGGLEENAALIEQNIKALGFKLSDIKIIINTHAHYDHAGGLAQLK-ADTGAKLWASR-------GDRPA 97

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446613816 103 erlvqaeemlermsneeKEFGKWF---IQQLKNIKHISVDEKVHDGQMILDNECQIVA--TPGHTSG 164
Cdd:cd16310   98 -----------------LEAGKHIgdnITQPAPFPAVKVDRILGDGEKIKLGDITLTAtlTPGHTKG 147
ComA-like_MBL-fold cd07731
Competence protein ComA, ComEC and related proteins; MBL-fold metallo hydrolase domain; This ...
 14-94 2.37e-04

Competence protein ComA, ComEC and related proteins; MBL-fold metallo hydrolase domain; This subgroup includes proteins required for natural transformation competence including Neisseria gonorrhoeae ComA, Pseudomonas stutzeri ComA, Bacillus subtilis ComEC (also known as ComE operon protein 3) and Haemophilus influenza ORF2 encoded by the rec-2 gene, as well as Escherichia coli YcaI which does not mediate spontaneous plasmid transformation on nutrient-containing agar plates. It also includes the phosphorylcholine esterase (Pce) domain of choline-binding protein e from streptococcus pneumonia. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions.


Pssm-ID: 293817 [Multi-domain]  Cd Length: 179  Bit Score: 40.58  E-value: 2.37e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446613816  14 GQKQCIypsLIILHNELTLVDTG--YPSFLPLIENAILKHGYemKNLKNIIITHYDDDHLGSVYD----FKVKypqiNVI 87
Cdd:cd07731    8 GQGDAI---LIQTPGKTILIDTGprDSFGEDVVVPYLKARGI--KKLDYLILTHPDADHIGGLDAvlknFPVK----EVY 78


                 ....*..
gi 446613816  88 ASEIESN 94
Cdd:cd07731   79 MPGVTHT 85
PhnP COG1235
Phosphoribosyl 1,2-cyclic phosphate phosphodiesterase [Inorganic ion transport and metabolism]; ...
 28-90 5.65e-03

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


Pssm-ID: 440848 [Multi-domain]  Cd Length: 259  Bit Score: 36.80  E-value: 5.65e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446613816  28 NELTLVDTGyPSFLPLIENAILKhgyeMKNLKNIIITHYDDDHLGSVYDFKVKYPQ--INVIASE 90
Cdd:COG1235   44 GTRLLIDAG-PDLREQLLRLGLD----PSKIDAILLTHEHADHIAGLDDLRPRYGPnpIPVYATP 103
 
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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