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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1325451167  17 DVYCFSVQ-IVNVVFLGNPkesNEFVLIDAGMPGAEEVIIgEAIKRFGENCKPL-GIVLTHGHFDHVGALQELINKWDVP 94
Cdd:cd07721     1 GVYQLPLLpPVNAYLIEDD---DGLTLIDTGLPGSAKRIL-KALRELGLSPKDIrRILLTHGHIDHIGSLAALKEAPGAP 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1325451167  95 VYAHPLEQPYLNGksDYPPPNPKAEGLVAKMSPLFPRHSIDIgshLQLLNGDGSVPCLPNWRYLHTPGHTPGHISLFRDS 174
Cdd:cd07721    77 VYAHEREAPYLEG--EKPYPPPVRLGLLGLLSPLLPVKPVPV---DRTLEDGDTLDLAGGLRVIHTPGHTPGHISLYLEE 151

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1325451167 175 DQFLIAGDAITTVeqeslydvitqKQEMHGPPAYFTQDWEAAEQSVKKIEALQPEATITGHG 236
Cdd:cd07721   152 DGVLIAGDALVTV-----------GGELVPPPPPFTWDMEEALESLRKLAELDPEVLAPGHG 202

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1325451167  17 DVYCFSVQ-IVNVVFLGNPkesNEFVLIDAGMPGAEEVIIgEAIKRFGENCKPL-GIVLTHGHFDHVGALQELINKWDVP 94
Cdd:cd07721     1 GVYQLPLLpPVNAYLIEDD---DGLTLIDTGLPGSAKRIL-KALRELGLSPKDIrRILLTHGHIDHIGSLAALKEAPGAP 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1325451167  95 VYAHPLEQPYLNGksDYPPPNPKAEGLVAKMSPLFPRHSIDIgshLQLLNGDGSVPCLPNWRYLHTPGHTPGHISLFRDS 174
Cdd:cd07721    77 VYAHEREAPYLEG--EKPYPPPVRLGLLGLLSPLLPVKPVPV---DRTLEDGDTLDLAGGLRVIHTPGHTPGHISLYLEE 151

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1325451167 175 DQFLIAGDAITTVeqeslydvitqKQEMHGPPAYFTQDWEAAEQSVKKIEALQPEATITGHG 236
Cdd:cd07721   152 DGVLIAGDALVTV-----------GGELVPPPPPFTWDMEEALESLRKLAELDPEVLAPGHG 202

Metallo-beta-lactamase superfamily;

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1325451167  25 IVNVVFLGNPKESnefVLIDAGMPGAEEVIIGEAIKRFGENcKPLGIVLTHGHFDHVGALQELINKWDVPVYAHPLEqpy 104
Cdd:pfam00753   5 QVNSYLIEGGGGA---VLIDTGGSAEAALLLLLAALGLGPK-DIDAVILTHGHFDHIGGLGELAEATDVPVIVVAEE--- 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1325451167 105 lngksdYPPPNPKAEGLVAKMSPLFPRHSIDIGSHLQLLNGDGSVPCLPNWRYLHTPGHTPGHISLFRDSDQFLIAGDAI 184
Cdd:pfam00753  78 ------ARELLDEELGLAASRLGLPGPPVVPLPPDVVLEEGDGILGGGLGLLVTHGPGHGPGHVVVYYGGGKVLFTGDLL 151

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1325451167 185 TTVEQESLYDvitqkqEMHGPPAYFTQDWEAAEQSVKKIEALQPEATITGH 235
Cdd:pfam00753 152 FAGEIGRLDL------PLGGLLVLHPSSAESSLESLLKLAKLKAAVIVPGH 196

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]

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1325451167  35 KESNEFVLIDAGMpgAEEVIigEAIKRfgENCKPLGIVLTHGHFDHVGALQELINKWDVPVYAhpleqpylngksdyppp 114
Cdd:TIGR03413  17 DPDGQAAVVDPGE--AEPVL--DALEA--RGLTLTAILLTHHHHDHVGGVAELLEAFPAPVYG----------------- 73

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1325451167 115 nPKAEGLvakmsPlFPRHSIDIGSHLQLLNGDGSVpclpnwryLHTPGHTPGHISLFRDSDQFLIAGD 182
Cdd:TIGR03413  74 -PAEERI-----P-GITHPVKDGDTVTLGGLEFEV--------LAVPGHTLGHIAYYLPDSPALFCGD 126

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1325451167  17 DVYCFSVQ-IVNVVFLGNPkesNEFVLIDAGMPGAEEVIIgEAIKRFGENCKPL-GIVLTHGHFDHVGALQELINKWDVP 94
Cdd:cd07721     1 GVYQLPLLpPVNAYLIEDD---DGLTLIDTGLPGSAKRIL-KALRELGLSPKDIrRILLTHGHIDHIGSLAALKEAPGAP 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1325451167  95 VYAHPLEQPYLNGksDYPPPNPKAEGLVAKMSPLFPRHSIDIgshLQLLNGDGSVPCLPNWRYLHTPGHTPGHISLFRDS 174
Cdd:cd07721    77 VYAHEREAPYLEG--EKPYPPPVRLGLLGLLSPLLPVKPVPV---DRTLEDGDTLDLAGGLRVIHTPGHTPGHISLYLEE 151

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1325451167 175 DQFLIAGDAITTVeqeslydvitqKQEMHGPPAYFTQDWEAAEQSVKKIEALQPEATITGHG 236
Cdd:cd07721   152 DGVLIAGDALVTV-----------GGELVPPPPPFTWDMEEALESLRKLAELDPEVLAPGHG 202

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1325451167  26 VNVVFLGNpkESNEFVLIDAGMPGAEEVIigEAIKRFGEncKPLGIVLTHGHFDHVGALQELINKWDVPVYAHPLEQPYL 105
Cdd:cd06262    10 TNCYLVSD--EEGEAILIDPGAGALEKIL--EAIEELGL--KIKAILLTHGHFDHIGGLAELKEAPGAPVYIHEADAELL 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1325451167 106 NGksdypPPNPKAEGLVAKMSPLFPRHSIDIGSHLQLLNGDgsvpclpnWRYLHTPGHTPGHISLFRDSDQFLIAGDAIT 185
Cdd:cd06262    84 ED-----PELNLAFFGGGPLPPPEPDILLEDGDTIELGGLE--------LEVIHTPGHTPGSVCFYIEEEGVLFTGDTLF 150

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1325451167 186 tveQESlydvitqkqemHGPPAYFTQDWEAAEQSVKKIEALQPEATI--TGH 235
Cdd:cd06262   151 ---AGS-----------IGRTDLPGGDPEQLIESIKKLLLLLPDDTVvyPGH 188

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.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1325451167   27 NVVFLGNPKESnefVLIDAGMPGAEEVIigEAIKRFGENcKPLGIVLTHGHFDHVGALQELINKWDVPVYAHPLEQPYLN 106
Cdd:smart00849   1 NSYLVRDDGGA---ILIDTGPGEAEDLL--AELKKLGPK-KIDAIILTHGHPDHIGGLPELLEAPGAPVYAPEGTAELLK 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1325451167  107 GKSDYPPPnpkaegLVAKMSPLFPRHSIDIGSHLQLLNGDgsvpclpnWRYLHTPGHTPGHISLFRDSDQFLIAGDAItt 186
Cdd:smart00849  75 DLLALLGE------LGAEAEPAPPDRTLKDGDELDLGGGE--------LEVIHTPGHTPGSIVLYLPEGKILFTGDLL-- 138

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1325451167  187 veqeslydvitqKQEMHGPPAYFTQDWEAAE--QSVKKIEALQPEATITGH 235
Cdd:smart00849 139 ------------FAGGDGRTLVDGGDAAASDalESLLKLLKLLPKLVVPGH 177

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1325451167  35 KESNEFVLIDAGmpGAEEVIIGEAIKRfgeNCKPLGIVLTHGHFDHVGALQELINKWDVPVYA-HPLEQPYLNGKsdypp 113
Cdd:cd07737    19 EETKEAAVIDPG--GDADKILQAIEDL---GLTLKKILLTHGHLDHVGGAAELAEHYGVPIIGpHKEDKFLLENL----- 88

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1325451167 114 PNPKAEGLVAKMSPLFPRHSIDIGSHLQLLNGDGSVpclpnwryLHTPGHTPGHISLFRDSDQFLIAGDAI 184
Cdd:cd07737    89 PEQSQMFGFPPAEAFTPDRWLEEGDTVTVGNLTLEV--------LHCPGHTPGHVVFFNRESKLAIVGDVL 151

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1325451167  37 SNEFVLIDAGMPGAEeviIGEAIKRFGEncKPLGIVLTHGHFDHVGALQELINkwdvpVYAHPLEQPYLNGKSDY----P 112
Cdd:cd07712    17 RDRALLIDTGLGIGD---LKEYVRTLTD--LPLLVVATHGHFDHIGGLHEFEE-----VYVHPADAEILAAPDNFetltW 86

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1325451167 113 PPNPKAEGLVAKMSPLFPRHSIDIGSHlqllngdgsvpCLpnwRYLHTPGHTPGHISLFRDSDQFLIAGDAI 184
Cdd:cd07712    87 DAATYSVPPAGPTLPLRDGDVIDLGDR-----------QL---EVIHTPGHTPGSIALLDRANRLLFSGDVV 144

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1325451167  41 VLIDAGMPGAEEVIIGEAIKRFGENCKP----------LGI--------VLTHGHFDHVGALQELINkwdVPVYAHPLEq 102
Cdd:cd07729    44 ILVDTGFHPDAADDPGGLELAFPPGVTEeqtleeqlarLGLdpedidyvILSHLHFDHAGGLDLFPN---ATIIVQRAE- 119

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1325451167 103 pYLNGKSDYPPPNPKAEGLVAkmsplfpRHSIDIGSHLQLLNGDGSVpcLPNWRYLHTPGHTPGHISLF--RDSDQFLIA 180
Cdd:cd07729   120 -LEYATGPDPLAAGYYEDVLA-------LDDDLPGGRVRLVDGDYDL--FPGVTLIPTPGHTPGHQSVLvrLPEGTVLLA 189

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1325451167 181 GDAITTVEQeslYDvitqkqemHGPPAYFTQDWEAAEQSVKKIEAL--QPEATI-TGH 235
Cdd:cd07729   190 GDAAYTYEN---LE--------EGRPPGINYDPEAALASLERLKALaeREGARViPGH 236

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1325451167  21 FSVQIVNVVFLGNPKEsneFVLIDAGmpgAEEVIIGEAIKRF--GENCKPL-GIVLTHGHFDHVG---ALQELINKWDVP 94
Cdd:cd07722    13 FTLQGTNTYLVGTGKR---RILIDTG---EGRPSYIPLLKSVldSEGNATIsDILLTHWHHDHVGglpDVLDLLRGPSPR 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1325451167  95 VYAHPLEQPYLNGKSDYPPPNPKAEGLVAKMSplfprhsidiGSHLQLLngdgsvpclpnwrylHTPGHTPGHISLFRDS 174
Cdd:cd07722    87 VYKFPRPEEDEDPDEDGGDIHDLQDGQVFKVE----------GATLRVI---------------HTPGHTTDHVCFLLEE 141

                         170       180
                  ....*....|....*....|....
gi 1325451167 175 DQFLIAGDAI----TTVeQESLYD 194
Cdd:cd07722   142 ENALFTGDCVlghgTAV-FEDLAA 164

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1325451167  70 GIVLTHGHFDHVGALQELINkwdVPVYAHP------LEQPYLNGK------SDYPPPNPKAEGLVAKMSPLFP-RHSIDi 136
Cdd:cd07730    86 AVILSHLHWDHIGGLSDFPN---ARLIVGPgakealRPPGYPSGFlpellpSDFEGRLVRWEEDDFLWVPLGPfPRALD- 161

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1325451167 137 gshlqlLNGDGSVpclpnwrYL-HTPGHTPGHISLF-RDSDQ--FLIAGDAittveQESLYDVITQKQEMHGPPAYFTQD 212
Cdd:cd07730   162 ------LFGDGSL-------YLvDLPGHAPGHLGLLaRTTSGtwVFLAGDA-----CHHRIGLLRPSPLLPLPDLDDGAD 223

                         170
                  ....*....|....*
gi 1325451167 213 WEAAEQSVKKIEALQ 227
Cdd:cd07730   224 REAARETLARLRELD 238

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1325451167  41 VLIDAGMPGAEEVIIgEAIKrfGENCKPLGI---VLTHGHFDHVG--ALQElinkwDVPVYAHPLEQPYLNGKSDYPPPN 115
Cdd:cd07711    34 ILVDTGTPWDRDLLL-KALA--EHGLSPEDIdyvVLTHGHPDHIGnlNLFP-----NATVIVGWDICGDSYDDHSLEEGD 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1325451167 116 PKAeglvakmsplfprhsidIGSHLQLLngdgsvpclpnwrylHTPGHTPGHISLFRDSDQF---LIAGDAITTVEQEsl 192
Cdd:cd07711   106 GYE-----------------IDENVEVI---------------PTPGHTPEDVSVLVETEKKgtvAVAGDLFEREEDL-- 151

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1325451167 193 ydvitqkQEMHGPPAYFTqDWEAAEQSVKKIEALqpeAT--ITGHGLP 238
Cdd:cd07711   152 -------EDPILWDPLSE-DPELQEESRKRILAL---ADwiIPGHGPP 188

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

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1325451167  41 VLIDAGMPGAEEVIIGEaIKRFGENCKPLGIVLT-HGHFDHVGALQELINKWDVPVYAHPLEQPYL-NGKSDypPPNPKA 118
Cdd:cd16315    34 VLIDSGTEEAAPLVLAN-IRKLGFDPKDVRWLLSsHEHFDHVGGLAALQRATGARVAASAAAAPVLeSGKPA--PDDPQA 110

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1325451167 119 eGLVAKMSPlfprhsIDIGSHLQllngDGSVPCLPNWR--YLHTPGHTPGHIS 169
Cdd:cd16315   111 -GLHEPFPP------VRVDRIVE----DGDTVALGSLRltAHATPGHTPGALS 152

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

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1325451167  38 NEFVLIDAG-------MPGAEEVI-----IgEAIKRfgencKPLGIVLTHGHFDHVGALQELINKWDVPVYAHPL 100
Cdd:COG0595    28 DDIIIVDCGlkfpedeMPGVDLVIpdisyL-EENKD-----KIKGIVLTHGHEDHIGALPYLLKELNVPVYGTPL 96

Pseudomonas pseudoalcaligenes organophosphorus hydrolase C2, and related proteins; MBL-fold metallo hydrolase domain; Pseudomonas pseudoalcaligenes OPHC2 is a thermostable organophosphorus hydrolase which a broad substrate activity spectrum: it hydrolyzes various phosphotriesters, esters, and a lactone. This subgroup also includes Pseudomonas oleovorans PoOPH which exhibits high lactonase and esterase activities, and latent PTE activity. However, double mutations His250Ile/Ile263Trp switch PoOPH into an efficient and thermostable PTE. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1325451167  41 VLIDAGMPGAeeviIGEAIKRFGENCKPLGI--------VLTHGHFDHVGALqelINKWDVP------VYAHPLE----- 101
Cdd:cd07720    61 ILVDTGAGGL----FGPTAGKLLANLAAAGIdpediddvLLTHLHPDHIGGL---VDAGGKPvfpnaeVHVSEAEwdfwl 133

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1325451167 102 -QPYLNGKSDYPPPNPKAegLVAKMSPLFPRHSIDIGSHLqllngdgsvpcLPNWRYLHTPGHTPGHiSLFR---DSDQF 177
Cdd:cd07720   134 dDANAAKAPEGAKRFFDA--ARDRLRPYAAAGRFEDGDEV-----------LPGITAVPAPGHTPGH-TGYRiesGGERL 199

                  ....*..
gi 1325451167 178 LIAGDAI 184
Cdd:cd07720   200 LIWGDIV 206

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1325451167  41 VLIDAGMP--GAEEVIigEAIKRFGEncKP-LGIVLTHGHFDHVGALQeLINKWDVPVYAHPL--------EQPYLNGKS 109
Cdd:cd16282    27 VVIDTGASprLARALL--AAIRKVTD--KPvRYVVNTHYHGDHTLGNA-AFADAGAPIIAHENtreelaarGEAYLELMR 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1325451167 110 DYPPPNPKAEGLVAKMSPLFPRHSIDIGSH-LQLLNgdgsvpclpnwrylHTPGHTPGHISLFRDSDQFLIAGDAIttve 188
Cdd:cd16282   102 RLGGDAMAGTELVLPDRTFDDGLTLDLGGRtVELIH--------------LGPAHTPGDLVVWLPEEGVLFAGDLV---- 163

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1325451167 189 qeslydvitqkqeMHGPPAYF----TQDWEAAeqsVKKIEALQPEATITGHGlPMTGKE 243
Cdd:cd16282   164 -------------FNGRIPFLpdgsLAGWIAA---LDRLLALDATVVVPGHG-PVGDKA 205

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1325451167 137 GSHLQLLNGDGSVPCLPNWRYLHTPGHTPGHISLFRDSDQFLIAGDAITTVEqeslydvitQKQEMHGPPAYFTQDWEAA 216
Cdd:cd07727    86 PDEVIVLWGGDPWELDPDLTLIPVPGHTRGSVVLLYKEKGVLFTGDHLAWSR---------RRGWLSAFRYVCWYSWPEQ 156

                          90       100
                  ....*....|....*....|..
gi 1325451167 217 EQSVKKIEALQPEATITGHGLP 238
Cdd:cd07727   157 AESVERLADLDFEWVLPGHGRR 178

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

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1325451167  41 VLIDAGmPGaeeviIGEAIKRFGENCKPL-GIVLTHGHFDHV---GALQELINKWDVPVYAHPLEQPYLNGKSDYpppnp 116
Cdd:COG1235    47 LLIDAG-PD-----LREQLLRLGLDPSKIdAILLTHEHADHIaglDDLRPRYGPNPIPVYATPGTLEALERRFPY----- 115

                          90       100
                  ....*....|....*....|....*.
gi 1325451167 117 kaegLVAKMSPLFPRHSIDIGSHLQL 142
Cdd:COG1235   116 ----LFAPYPGKLEFHEIEPGEPFEI 137

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

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1325451167  27 NVVFLGNPKESnefVLIDAGMPGAEeviIGEAIKRFGENCKPL-GIVLTHGHFDHVGALQELINKWDVPVYA 97
Cdd:cd07733    10 NCTYLETEDGK---LLIDAGLSGRK---ITGRLAEIGRDPEDIdAILVTHEHADHIKGLGVLARKYNVPIYA 75

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

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1325451167  41 VLIDAGMPGAEEVIIGeAIKRFGENCKPLGIVL-THGHFDHVGALQELINKWDVPVYAHPLEQPYL-NGKSDypPPNPKA 118
Cdd:cd16311    34 VLVDGGLPESAPKIIA-NIEALGFRIEDVKLILnSHGHIDHAGGLAELQRRSGALVAASPSAALDLaSGEVG--PDDPQY 110

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1325451167 119 EglvakMSPLFPRHsidigSHLQLLNGDGSVPCLPNWRYLH-TPGHTPGHIS 169
Cdd:cd16311   111 H-----ALPKYPPV-----KDMRLARDGGQFNVGPVSLTAHaTPGHTPGGLS 152

Methanocaldococcus jannaschii dihydropteroate synthase, Thermoanaerobacter tengcongensis Tflp, and related proteins; MBL-fold metallo hydrolase domain; This subgroup includes Methanocaldococcus jannaschii 7,8-dihydropterin-6-methyl-4-(beta-D-ribofuranosyl)-aminobenzene-5'-phosphate synthase (EC 2.5.1.15), a folate biosynthetic enzyme also known as dihydropteroate synthase and 7,8 dihydropteroate synthase. Thermoanaerobacter tengcongensis Tflp is a ferredoxin-like member. 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.

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1325451167  41 VLIDAGmpgAEEVIIgeaikrfgENCKPLGI--------VLTHGHFDHVGALQELINKW-DVPVYAHP 99
Cdd:cd07713    32 ILFDTG---QSGVLL--------HNAKKLGIdlsdidavVLSHGHYDHTGGLKALLELNpKAPVYAHP 88

Thermus thermophilus TTHA0252 and related cleavage and polyadenylation specificity factors; MBL-fold metallo-hydrolase domain; Includes the archaeal cleavage and polyadenylation specificity factors (CPSFs) such as Methanothermobacter thermautotrophicus MTH1203, and Pyrococcus horikoshii PH1404. In addition to the MBL-fold metallo-hydrolase nuclease and the beta-CASP domains, members of this subgroup contain two contiguous KH domains. 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.

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1325451167  41 VLIDAGM-PGAEEVIIGEAiKRFGENCKPL-GIVLTHGHFDHVGALQELINK-WDVPVYAHP 99
Cdd:cd16295    24 ILLDCGLfQGGKELEELNN-EPFPFDPKEIdAVILTHAHLDHSGRLPLLVKEgFRGPIYATP 84