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Conserved domains on  [gi|15598111|ref|NP_251605|]
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hypothetical protein PA2915 [Pseudomonas aeruginosa PAO1]

Protein Classification

MBL fold metallo-hydrolase( domain architecture ID 10869981)

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

 Zoom to residue level

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List of domain hits

 Name Accession Description Interval E-value
bifunc_ST_SDO super family cl48920
bifunctional sulfur transferase/dioxygenase Blh;
3-288 7.08e-147

bifunctional sulfur transferase/dioxygenase Blh;


The actual alignment was detected with superfamily member NF040641:

Pssm-ID: 468609 [Multi-domain]  Cd Length: 423  Bit Score: 418.53  E-value: 7.08e-147
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598111    3 KPDITAFFDPATSTYSYVVRDPSSRACAIVDPVLDYDPAAGRTSHASAERLIAHVRQHDLQVEWLLETHVHADHLSAAIF 82
Cdd:NF040641 141 RPQVKGFFDPRTGSVQYVVSDPATRRCAIIDPVLDFDEKSGATSTTNADAILAYVAEEGLTVEWILDTHPHADHFSAAHY 220

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598111   83 LQRELGGCLAIGARITQVQAKFSGLFNLGEaFPVDGRQFEHLFEDGESFRIGALECRALHTPGHTPACMTYLVGDSAFVG 162
Cdd:NF040641 221 LKEKTGAPTAIGEHVVDVQKLWKGIYNWPD-LPTDGSQWDRLFADGDTFKVGSIDARVMFSPGHTLASITYVIGDAAFVH 299

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598111  163 DTLFMPDYGTARCDFPGGDARQLYRSIQRLFALPDATRLFMCHDYTAPGRdEHRCETSVGEQRRHNVHVReGVDEEAFVA 242
Cdd:NF040641 300 DTLFMPDSGTARADFPGGSARALWRSIQAILALPDETRLFTGHDYQPGGR-APRWESTVAEQKRSNPHLA-GQDEASFVA 377

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 15598111  243 MRQQRDATLGMPTLMLPAIQVNMRGGNLPPVEGNGVRYLKIPLDLF 288
Cdd:NF040641 378 LREARDKTLPMPKLILHALQVNIRGGRLPEPEANGRRYLKIPLDAL 423
 
Name Accession Description Interval E-value
bifunc_ST_SDO NF040641
bifunctional sulfur transferase/dioxygenase Blh;
3-288 7.08e-147

bifunctional sulfur transferase/dioxygenase Blh;


Pssm-ID: 468609 [Multi-domain]  Cd Length: 423  Bit Score: 418.53  E-value: 7.08e-147
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598111    3 KPDITAFFDPATSTYSYVVRDPSSRACAIVDPVLDYDPAAGRTSHASAERLIAHVRQHDLQVEWLLETHVHADHLSAAIF 82
Cdd:NF040641 141 RPQVKGFFDPRTGSVQYVVSDPATRRCAIIDPVLDFDEKSGATSTTNADAILAYVAEEGLTVEWILDTHPHADHFSAAHY 220

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598111   83 LQRELGGCLAIGARITQVQAKFSGLFNLGEaFPVDGRQFEHLFEDGESFRIGALECRALHTPGHTPACMTYLVGDSAFVG 162
Cdd:NF040641 221 LKEKTGAPTAIGEHVVDVQKLWKGIYNWPD-LPTDGSQWDRLFADGDTFKVGSIDARVMFSPGHTLASITYVIGDAAFVH 299

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598111  163 DTLFMPDYGTARCDFPGGDARQLYRSIQRLFALPDATRLFMCHDYTAPGRdEHRCETSVGEQRRHNVHVReGVDEEAFVA 242
Cdd:NF040641 300 DTLFMPDSGTARADFPGGSARALWRSIQAILALPDETRLFTGHDYQPGGR-APRWESTVAEQKRSNPHLA-GQDEASFVA 377

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 15598111  243 MRQQRDATLGMPTLMLPAIQVNMRGGNLPPVEGNGVRYLKIPLDLF 288
Cdd:NF040641 378 LREARDKTLPMPKLILHALQVNIRGGRLPEPEANGRRYLKIPLDAL 423
POD-like_MBL-fold cd07724
ETHE1 (PDO type I), persulfide dioxygenase A (PDOA, PDO type II) and related proteins; ...
 6-207 1.98e-74

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: 225.36  E-value: 1.98e-74
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598111   6 ITAFFDPATSTYSYVVRDPSSRACAIVDPVLDydpaagrtshaSAERLIAHVRQHDLQVEWLLETHVHADHLSAAIFLQR 85
Cdd:cd07724   2 FRQFFDPGLGTLSYLVGDPETGEAAVIDPVRD-----------SVDRYLDLAAELGLKITYVLETHVHADHVSGARELAE 70

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598111  86 ELGGCLAIGARItqvqakfsglfnlgeafpvDGRQFEHLFEDGESFRIGALECRALHTPGHTPACMTYLVGD--SAFVGD 163
Cdd:cd07724  71 RTGAPIVIGEGA-------------------PASFFDRLLKDGDVLELGNLTLEVLHTPGHTPESVSYLVGDpdAVFTGD 131

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 15598111 164 TLFMPDygTARCDFPG---GDARQLYRSIQRLFA-LPDATRLFMCHDY 207
Cdd:cd07724 132 TLFVGD--VGRPDLPGeaeGLARQLYDSLQRKLLlLPDETLVYPGHDY 177
GloB COG0491
Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General ...
 7-231 8.41e-43

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: 145.99  E-value: 8.41e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598111   7 TAFFDPATSTYSYVVRDPssRACAIVDPVLDYdpaagrtshASAERLIAHVRQHDLQVEWLLETHVHADHLSAAIFLQRE 86
Cdd:COG0491   6 GGTPGAGLGVNSYLIVGG--DGAVLIDTGLGP---------ADAEALLAALAALGLDIKAVLLTHLHPDHVGGLAALAEA 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598111  87 LGGCLAIGARITQVQAKFSGlfnlGEAFPVDGRQFEHLFEDGESFRIGALECRALHTPGHTPACMTYLVGDS--AFVGDT 164
Cdd:COG0491  75 FGAPVYAHAAEAEALEAPAA----GALFGREPVPPDRTLEDGDTLELGGPGLEVIHTPGHTPGHVSFYVPDEkvLFTGDA 150

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15598111 165 LFMPDYGtaRCDFPGGDARQLYRSIQRLFALPDaTRLFMCHDYTAPGRDEHRCETSVGE-QRRHNVHV 231
Cdd:COG0491 151 LFSGGVG--RPDLPDGDLAQWLASLERLLALPP-DLVIPGHGPPTTAEAIDYLEELLAAlGERANPFL 215
PLN02962 PLN02962
hydroxyacylglutathione hydrolase
 10-265 7.18e-30

hydroxyacylglutathione hydrolase


Pssm-ID: 178547 [Multi-domain]  Cd Length: 251  Bit Score: 112.97  E-value: 7.18e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598111   10 FDPATSTYSYVVRDPS--SRACAIVDPVldydpaaGRTshasAERLIAHVRQHDLQVEWLLETHVHADHLSAAIFLQREL 87
Cdd:PLN02962  17 FEKESSTYTYLLADVShpDKPALLIDPV-------DKT----VDRDLSLVKELGLKLIYAMNTHVHADHVTGTGLLKTKL 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598111   88 GGCLAIGARITQVQAkfsglfnlgeafpvdgrqfEHLFEDGESFRIGA--LECRAlhTPGHTPACMTYLVGDS------- 158
Cdd:PLN02962  86 PGVKSIISKASGSKA-------------------DLFVEPGDKIYFGDlyLEVRA--TPGHTAGCVTYVTGEGpdqpqpr 144

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598111  159 -AFVGDTLFMpdYGTARCDFPGGDARQLYRSIQ-RLFALPDATRLFMCHDYTApgrdeHRCETsVGEQRRHNvhVREGVD 236
Cdd:PLN02962 145 mAFTGDALLI--RGCGRTDFQGGSSDQLYKSVHsQIFTLPKDTLIYPAHDYKG-----FTVST-VGEEMLYN--PRLTKD 214

                        250       260
                 ....*....|....*....|....*....
gi 15598111  237 EEAFVAMRQqrDATLGMPTLMLPAIQVNM 265
Cdd:PLN02962 215 EETFKTIME--NLNLPYPKMIDVAVPANM 241
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 17-199 6.55e-23

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: 92.62  E-value: 6.55e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598111     17 YSYVVRDPSSraCAIVDPVLDYdpaagrtshasAERLIAHVRQHDL-QVEWLLETHVHADHLSAAIFLQRELGgCLAIGA 95
Cdd:smart00849   1 NSYLVRDDGG--AILIDTGPGE-----------AEDLLAELKKLGPkKIDAIILTHGHPDHIGGLPELLEAPG-APVYAP 66

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598111     96 RITQVQAKFSGLFNLGEAFPVDGRQFEHLFEDGESFRIGALECRALHTPGHTPACMTYLVGDS--AFVGDTLFMPDYGTA 173
Cdd:smart00849  67 EGTAELLKDLLALLGELGAEAEPAPPDRTLKDGDELDLGGGELEVIHTPGHTPGSIVLYLPEGkiLFTGDLLFAGGDGRT 146

                          170       180
                   ....*....|....*....|....*.
gi 15598111    174 RCDFPGGDARQLYRSIQRLFALPDAT 199
Cdd:smart00849 147 LVDGGDAAASDALESLLKLLKLLPKL 172
Lactamase_B pfam00753
Metallo-beta-lactamase superfamily;
15-205 1.55e-13

Metallo-beta-lactamase superfamily;


Pssm-ID: 425851 [Multi-domain]  Cd Length: 196  Bit Score: 67.78  E-value: 1.55e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598111    15 STYSYVVRDPssRACAIVDPvldydpaaGRTSHASAERLIAHVRQHDLQVEWLLETHVHADHLSAAIFLQRELGGCLAIG 94
Cdd:pfam00753   5 QVNSYLIEGG--GGAVLIDT--------GGSAEAALLLLLAALGLGPKDIDAVILTHGHFDHIGGLGELAEATDVPVIVV 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598111    95 ARIT---------QVQAKFSGLFNLGEAFPVDGRQFEHLFEDGESFRIGALECralHTPGHTPACMTYLVGDSAFVGDTL 165
Cdd:pfam00753  75 AEEArelldeelgLAASRLGLPGPPVVPLPPDVVLEEGDGILGGGLGLLVTHG---PGHGPGHVVVYYGGGKVLFTGDLL 151

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 15598111   166 FMPDygTARCDFPGGDARQLYRSIQ-------RLFALPDATRLFMCH 205
Cdd:pfam00753 152 FAGE--IGRLDLPLGGLLVLHPSSAessleslLKLAKLKAAVIVPGH 196
 
Name Accession Description Interval E-value
bifunc_ST_SDO NF040641
bifunctional sulfur transferase/dioxygenase Blh;
3-288 7.08e-147

bifunctional sulfur transferase/dioxygenase Blh;


Pssm-ID: 468609 [Multi-domain]  Cd Length: 423  Bit Score: 418.53  E-value: 7.08e-147
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598111    3 KPDITAFFDPATSTYSYVVRDPSSRACAIVDPVLDYDPAAGRTSHASAERLIAHVRQHDLQVEWLLETHVHADHLSAAIF 82
Cdd:NF040641 141 RPQVKGFFDPRTGSVQYVVSDPATRRCAIIDPVLDFDEKSGATSTTNADAILAYVAEEGLTVEWILDTHPHADHFSAAHY 220

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598111   83 LQRELGGCLAIGARITQVQAKFSGLFNLGEaFPVDGRQFEHLFEDGESFRIGALECRALHTPGHTPACMTYLVGDSAFVG 162
Cdd:NF040641 221 LKEKTGAPTAIGEHVVDVQKLWKGIYNWPD-LPTDGSQWDRLFADGDTFKVGSIDARVMFSPGHTLASITYVIGDAAFVH 299

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598111  163 DTLFMPDYGTARCDFPGGDARQLYRSIQRLFALPDATRLFMCHDYTAPGRdEHRCETSVGEQRRHNVHVReGVDEEAFVA 242
Cdd:NF040641 300 DTLFMPDSGTARADFPGGSARALWRSIQAILALPDETRLFTGHDYQPGGR-APRWESTVAEQKRSNPHLA-GQDEASFVA 377

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 15598111  243 MRQQRDATLGMPTLMLPAIQVNMRGGNLPPVEGNGVRYLKIPLDLF 288
Cdd:NF040641 378 LREARDKTLPMPKLILHALQVNIRGGRLPEPEANGRRYLKIPLDAL 423
POD-like_MBL-fold cd07724
ETHE1 (PDO type I), persulfide dioxygenase A (PDOA, PDO type II) and related proteins; ...
 6-207 1.98e-74

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: 225.36  E-value: 1.98e-74
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598111   6 ITAFFDPATSTYSYVVRDPSSRACAIVDPVLDydpaagrtshaSAERLIAHVRQHDLQVEWLLETHVHADHLSAAIFLQR 85
Cdd:cd07724   2 FRQFFDPGLGTLSYLVGDPETGEAAVIDPVRD-----------SVDRYLDLAAELGLKITYVLETHVHADHVSGARELAE 70

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598111  86 ELGGCLAIGARItqvqakfsglfnlgeafpvDGRQFEHLFEDGESFRIGALECRALHTPGHTPACMTYLVGD--SAFVGD 163
Cdd:cd07724  71 RTGAPIVIGEGA-------------------PASFFDRLLKDGDVLELGNLTLEVLHTPGHTPESVSYLVGDpdAVFTGD 131

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 15598111 164 TLFMPDygTARCDFPG---GDARQLYRSIQRLFA-LPDATRLFMCHDY 207
Cdd:cd07724 132 TLFVGD--VGRPDLPGeaeGLARQLYDSLQRKLLlLPDETLVYPGHDY 177
GloB COG0491
Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General ...
 7-231 8.41e-43

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: 145.99  E-value: 8.41e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598111   7 TAFFDPATSTYSYVVRDPssRACAIVDPVLDYdpaagrtshASAERLIAHVRQHDLQVEWLLETHVHADHLSAAIFLQRE 86
Cdd:COG0491   6 GGTPGAGLGVNSYLIVGG--DGAVLIDTGLGP---------ADAEALLAALAALGLDIKAVLLTHLHPDHVGGLAALAEA 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598111  87 LGGCLAIGARITQVQAKFSGlfnlGEAFPVDGRQFEHLFEDGESFRIGALECRALHTPGHTPACMTYLVGDS--AFVGDT 164
Cdd:COG0491  75 FGAPVYAHAAEAEALEAPAA----GALFGREPVPPDRTLEDGDTLELGGPGLEVIHTPGHTPGHVSFYVPDEkvLFTGDA 150

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15598111 165 LFMPDYGtaRCDFPGGDARQLYRSIQRLFALPDaTRLFMCHDYTAPGRDEHRCETSVGE-QRRHNVHV 231
Cdd:COG0491 151 LFSGGVG--RPDLPDGDLAQWLASLERLLALPP-DLVIPGHGPPTTAEAIDYLEELLAAlGERANPFL 215
BaeB-like_MBL-fold cd16275
Bacillus amyloliquefaciens BaeB and related proteins; MBL-fold metallo hydrolase domain; ...
 17-202 5.83e-40

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: 137.28  E-value: 5.83e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598111  17 YSYVVRDPSSRACAIVDPVLDydpaagrtshasAERLIAHVRQHDLQVEWLLETHVHADHLSAAIFLQRELGgclaIGAR 96
Cdd:cd16275  13 YSYIIIDKATREAAVVDPAWD------------IEKILAKLNELGLTLTGILLTHSHFDHVNLVEPLLAKYD----APVY 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598111  97 ITQVQAKFSGL--FNLgeafpvdgrqfeHLFEDGESFRIGALECRALHTPGHTPACMTYLVGDSAFVGDTLFMpdYGTAR 174
Cdd:cd16275  77 MSKEEIDYYGFrcPNL------------IPLEDGDTIKIGDTEITCLLTPGHTPGSMCYLLGDSLFTGDTLFI--EGCGR 142

                       170       180
                ....*....|....*....|....*....
gi 15598111 175 CDFPGGDARQLYRSIQRLFALPDA-TRLF 202
Cdd:cd16275 143 CDLPGGDPEEMYESLQRLKKLPPPnTRVY 171
metallo-hydrolase-like_MBL-fold cd06262
mainly hydrolytic enzymes and related proteins which carry out various biological functions; ...
 15-205 2.65e-37

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: 130.87  E-value: 2.65e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598111  15 STYSYVVRDPSSRaCAIVDPvldydpaagrtSHASAERLIAHVRQHDLQVEWLLETHVHADHLSAAIFLQRELGGCLAIG 94
Cdd:cd06262   9 QTNCYLVSDEEGE-AILIDP-----------GAGALEKILEAIEELGLKIKAILLTHGHFDHIGGLAELKEAPGAPVYIH 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598111  95 ARITQVQAKFSGLFNLGEAFPVDGRQFEHLFEDGESFRIGALECRALHTPGHTPACMTYLVGDS--AFVGDTLFMPDYGt 172
Cdd:cd06262  77 EADAELLEDPELNLAFFGGGPLPPPEPDILLEDGDTIELGGLELEVIHTPGHTPGSVCFYIEEEgvLFTGDTLFAGSIG- 155

                       170       180       190
                ....*....|....*....|....*....|....
gi 15598111 173 aRCDFPGGDARQLYRSIQR-LFALPDATRLFMCH 205
Cdd:cd06262 156 -RTDLPGGDPEQLIESIKKlLLLLPDDTVVYPGH 188
hydroxyacylglutathione_hydrolase_MBL-fold cd07723
hydroxyacylglutathione hydrolase, MBL-fold metallo-hydrolase domain; hydroxyacylglutathione ...
 17-202 2.68e-33

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: 119.49  E-value: 2.68e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598111  17 YSYVVRDPSSRACAIVDPvldydpaagrtshASAERLIAHVRQHDLQVEWLLETHVHADHLSAAIFLQRELGGCLAIGAR 96
Cdd:cd07723  10 YIYLIVDEATGEAAVVDP-------------GEAEPVLAALEKNGLTLTAILTTHHHWDHTGGNAELKALFPDAPVYGPA 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598111  97 ITQVQAkfsglfnlgeafpVDgrqfeHLFEDGESFRIGALECRALHTPGHTPACMTYLVGDS--AFVGDTLFMpdYGTAR 174
Cdd:cd07723  77 EDRIPG-------------LD-----HPVKDGDEIKLGGLEVKVLHTPGHTLGHICYYVPDEpaLFTGDTLFS--GGCGR 136

                       170       180
                ....*....|....*....|....*...
gi 15598111 175 CDfpGGDARQLYRSIQRLFALPDATRLF 202
Cdd:cd07723 137 FF--EGTAEQMYASLQKLLALPDDTLVY 162
TTHA1623-like_MBL-fold cd16322
uncharacterized Thermus thermophilus TTHA1623 and related proteins; MBL-fold metallo hydrolase ...
 19-228 2.16e-31

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: 115.91  E-value: 2.16e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598111  19 YVVRDPSSRACAIVDPVLDydpaagrtshasAERLIAHVRQHDLQVEWLLETHVHADHLSAAIFLQRELGGCLAI---GA 95
Cdd:cd16322  14 YLVADEGGGEAVLVDPGDE------------SEKLLARFGTTGLTLLYILLTHAHFDHVGGVADLRRHPGAPVYLhpdDL 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598111  96 RITQVQAKFSGLFNLGEAFPVDGrqfEHLFEDGESFRIGALECRALHTPGHTPACMTYLV--GDSAFVGDTLFMPDYGta 173
Cdd:cd16322  82 PLYEAADLGAKAFGLGIEPLPPP---DRLLEDGQTLTLGGLEFKVLHTPGHSPGHVCFYVeeEGLLFSGDLLFQGSIG-- 156

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 15598111 174 RCDFPGGDARQLYRSIQRLFALPDATRLFmchdytaPGrdeHRCETSVGEQRRHN 228
Cdd:cd16322 157 RTDLPGGDPKAMAASLRRLLTLPDETRVF-------PG---HGPPTTLGEERRTN 201
PLN02962 PLN02962
hydroxyacylglutathione hydrolase
 10-265 7.18e-30

hydroxyacylglutathione hydrolase


Pssm-ID: 178547 [Multi-domain]  Cd Length: 251  Bit Score: 112.97  E-value: 7.18e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598111   10 FDPATSTYSYVVRDPS--SRACAIVDPVldydpaaGRTshasAERLIAHVRQHDLQVEWLLETHVHADHLSAAIFLQREL 87
Cdd:PLN02962  17 FEKESSTYTYLLADVShpDKPALLIDPV-------DKT----VDRDLSLVKELGLKLIYAMNTHVHADHVTGTGLLKTKL 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598111   88 GGCLAIGARITQVQAkfsglfnlgeafpvdgrqfEHLFEDGESFRIGA--LECRAlhTPGHTPACMTYLVGDS------- 158
Cdd:PLN02962  86 PGVKSIISKASGSKA-------------------DLFVEPGDKIYFGDlyLEVRA--TPGHTAGCVTYVTGEGpdqpqpr 144

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598111  159 -AFVGDTLFMpdYGTARCDFPGGDARQLYRSIQ-RLFALPDATRLFMCHDYTApgrdeHRCETsVGEQRRHNvhVREGVD 236
Cdd:PLN02962 145 mAFTGDALLI--RGCGRTDFQGGSSDQLYKSVHsQIFTLPKDTLIYPAHDYKG-----FTVST-VGEEMLYN--PRLTKD 214

                        250       260
                 ....*....|....*....|....*....
gi 15598111  237 EEAFVAMRQqrDATLGMPTLMLPAIQVNM 265
Cdd:PLN02962 215 EETFKTIME--NLNLPYPKMIDVAVPANM 241
YcbL-like_MBL-fold cd07737
Salmonella enterica serovar typhimurium YcbL and related proteins; MBL-fold metallo hydrolase ...
 18-205 4.04e-23

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: 93.39  E-value: 4.04e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598111  18 SYVVRDPSSRACAIVDPVLDydpaagrtshasAERLIAHVRQHDLQVEWLLETHVHADHLSAAIFLqRELGGCLAIGARI 97
Cdd:cd07737  13 CSLIWCEETKEAAVIDPGGD------------ADKILQAIEDLGLTLKKILLTHGHLDHVGGAAEL-AEHYGVPIIGPHK 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598111  98 T--------QVQAKFSGlFNLGEAFPVDgrqfeHLFEDGESFRIGALECRALHTPGHTPACMTYLVGDS--AFVGDTLFm 167
Cdd:cd07737  80 EdkfllenlPEQSQMFG-FPPAEAFTPD-----RWLEEGDTVTVGNLTLEVLHCPGHTPGHVVFFNRESklAIVGDVLF- 152

                       170       180       190
                ....*....|....*....|....*....|....*....
gi 15598111 168 pDYGTARCDFPGGDARQLYRSIQR-LFALPDATRLFMCH 205
Cdd:cd07737 153 -KGSIGRTDFPGGNHAQLIASIKEkLLPLGDDVTFIPGH 190
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 17-199 6.55e-23

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: 92.62  E-value: 6.55e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598111     17 YSYVVRDPSSraCAIVDPVLDYdpaagrtshasAERLIAHVRQHDL-QVEWLLETHVHADHLSAAIFLQRELGgCLAIGA 95
Cdd:smart00849   1 NSYLVRDDGG--AILIDTGPGE-----------AEDLLAELKKLGPkKIDAIILTHGHPDHIGGLPELLEAPG-APVYAP 66

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598111     96 RITQVQAKFSGLFNLGEAFPVDGRQFEHLFEDGESFRIGALECRALHTPGHTPACMTYLVGDS--AFVGDTLFMPDYGTA 173
Cdd:smart00849  67 EGTAELLKDLLALLGELGAEAEPAPPDRTLKDGDELDLGGGELEVIHTPGHTPGSIVLYLPEGkiLFTGDLLFAGGDGRT 146

                          170       180
                   ....*....|....*....|....*.
gi 15598111    174 RCDFPGGDARQLYRSIQRLFALPDAT 199
Cdd:smart00849 147 LVDGGDAAASDALESLLKLLKLLPKL 172
PLN02469 PLN02469
hydroxyacylglutathione hydrolase
 17-209 1.47e-19

hydroxyacylglutathione hydrolase


Pssm-ID: 178088 [Multi-domain]  Cd Length: 258  Bit Score: 85.58  E-value: 1.47e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598111   17 YSYVVRDPSSRACAIVDPVldyDPaagrtshasaERLIAHVRQHDLQVEWLLETHVHADHLSAAIFLQRELGGCLAIGAR 96
Cdd:PLN02469  13 YAYLIIDESTKDAAVVDPV---DP----------EKVLQAAHEHGAKIKLVLTTHHHWDHAGGNEKIKKLVPGIKVYGGS 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598111   97 ITQVQakfsglfnlGEAFPVdgrqfehlfEDGESFRIGA-LECRALHTPGHTPACMTYLV-----GDSA-FVGDTLFMPD 169
Cdd:PLN02469  80 LDNVK---------GCTHPV---------ENGDKLSLGKdVNILALHTPCHTKGHISYYVtgkegEDPAvFTGDTLFIAG 141

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 15598111  170 YGtarcDFPGGDARQLYRSIQRLFA-LPDATRLFMCHDYTA 209
Cdd:PLN02469 142 CG----KFFEGTAEQMYQSLCVTLGsLPKPTQVYCGHEYTV 178
PRK10241 PRK10241
hydroxyacylglutathione hydrolase; Provisional
 6-208 7.66e-16

hydroxyacylglutathione hydrolase; Provisional


Pssm-ID: 182327 [Multi-domain]  Cd Length: 251  Bit Score: 75.25  E-value: 7.66e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598111    6 ITAFFDpatsTYSYVVRDPSSRaCAIVDPvldydpaagrtshASAERLIAHVRQHDLQVEWLLETHVHADHLsaaiflqr 85
Cdd:PRK10241   6 IPAFDD----NYIWVLNDEAGR-CLIVDP-------------GEAEPVLNAIAENNWQPEAIFLTHHHHDHV-------- 59

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598111   86 elGGclaigarITQVQAKFSGLFNLGEAFPVDgRQFEHLFEDGESFRIGALECRALHTPGHTPACMTYLVGDSAFVGDTL 165
Cdd:PRK10241  60 --GG-------VKELVEKFPQIVVYGPQETQD-KGTTQVVKDGETAFVLGHEFSVFATPGHTLGHICYFSKPYLFCGDTL 129

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 15598111  166 FmpDYGTARCdFPgGDARQLYRSIQRLFALPDATRLFMCHDYT 208
Cdd:PRK10241 130 F--SGGCGRL-FE-GTASQMYQSLKKINALPDDTLICCAHEYT 168
metallo-hydrolase-like_MBL-fold cd16278
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 16-199 1.68e-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: 293836 [Multi-domain]  Cd Length: 185  Bit Score: 70.21  E-value: 1.68e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598111  16 TYSYVVRDPssRACAIVDPVLDyDPAagrtsHAsaERLIAHVRqhDLQVEWLLETHVHADHLSAAIFLqRELGGCLAIGA 95
Cdd:cd16278  18 TNTYLLGAP--DGVVVIDPGPD-DPA-----HL--DALLAALG--GGRVSAILVTHTHRDHSPGAARL-AERTGAPVRAF 84

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598111  96 RITQVQAkfsglfnLGEAFPVDgrqfeHLFEDGESFRIGALECRALHTPGHTPACMTYLVGDSA--FVGDTLFmpDYGTA 173
Cdd:cd16278  85 GPHRAGG-------QDTDFAPD-----RPLADGEVIEGGGLRLTVLHTPGHTSDHLCFALEDEGalFTGDHVM--GWSTT 150

                       170       180
                ....*....|....*....|....*.
gi 15598111 174 RCDFPGGDARQLYRSIQRLFALPDAT 199
Cdd:cd16278 151 VIAPPDGDLGDYLASLERLLALDDRL 176
yflN-like_MBL-fold cd07721
uncharacterized subgroup which includes Bacillus subtilis yflN; MBL-fold metallo hydrolase ...
 49-205 2.93e-14

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: 69.94  E-value: 2.93e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598111  49 SAERLIAHVRQHDL---QVEWLLETHVHADHLSAAIFLQRELGGCLAIGAR----IT-----QVQAKFSGLFNLGEAFPV 116
Cdd:cd07721  32 SAKRILKALRELGLspkDIRRILLTHGHIDHIGSLAALKEAPGAPVYAHEReapyLEgekpyPPPVRLGLLGLLSPLLPV 111

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598111 117 DGRQFEHLFEDGESFRIGAlECRALHTPGHTPACMTYLVGDS--AFVGDTLF--------MPDYGTArcdfpggDARQLY 186
Cdd:cd07721 112 KPVPVDRTLEDGDTLDLAG-GLRVIHTPGHTPGHISLYLEEDgvLIAGDALVtvggelvpPPPPFTW-------DMEEAL 183

                       170
                ....*....|....*....
gi 15598111 187 RSIQRLFALpDATRLFMCH 205
Cdd:cd07721 184 ESLRKLAEL-DPEVLAPGH 201
Lactamase_B pfam00753
Metallo-beta-lactamase superfamily;
15-205 1.55e-13

Metallo-beta-lactamase superfamily;


Pssm-ID: 425851 [Multi-domain]  Cd Length: 196  Bit Score: 67.78  E-value: 1.55e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598111    15 STYSYVVRDPssRACAIVDPvldydpaaGRTSHASAERLIAHVRQHDLQVEWLLETHVHADHLSAAIFLQRELGGCLAIG 94
Cdd:pfam00753   5 QVNSYLIEGG--GGAVLIDT--------GGSAEAALLLLLAALGLGPKDIDAVILTHGHFDHIGGLGELAEATDVPVIVV 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598111    95 ARIT---------QVQAKFSGLFNLGEAFPVDGRQFEHLFEDGESFRIGALECralHTPGHTPACMTYLVGDSAFVGDTL 165
Cdd:pfam00753  75 AEEArelldeelgLAASRLGLPGPPVVPLPPDVVLEEGDGILGGGLGLLVTHG---PGHGPGHVVVYYGGGKVLFTGDLL 151

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 15598111   166 FMPDygTARCDFPGGDARQLYRSIQ-------RLFALPDATRLFMCH 205
Cdd:pfam00753 152 FAGE--IGRLDLPLGGLLVLHPSSAessleslLKLAKLKAAVIVPGH 196
PLN02398 PLN02398
hydroxyacylglutathione hydrolase
 17-209 3.02e-11

hydroxyacylglutathione hydrolase


Pssm-ID: 215223 [Multi-domain]  Cd Length: 329  Bit Score: 62.94  E-value: 3.02e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598111   17 YSYVVRDPSSRACAIVDPvldydpaagrtshASAERLIAHVRQHDLQVEWLLETHVHADHLsaaiflqrelGGCLAIGAR 96
Cdd:PLN02398  88 YAYLLHDEDTGTVGVVDP-------------SEAVPVIDALSRKNRNLTYILNTHHHYDHT----------GGNLELKAR 144

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598111   97 ITqvqAKFSGLFNLGEAFPvdgrQFEHLFEDGESFRIGALECRALHTPGHTPACMTYLVGDSA--FVGDTLFMPDYGTar 174
Cdd:PLN02398 145 YG---AKVIGSAVDKDRIP----GIDIVLKDGDKWMFAGHEVLVMETPGHTRGHISFYFPGSGaiFTGDTLFSLSCGK-- 215

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 15598111  175 cdFPGGDARQLYRSIQRLFALPDATRLFMCHDYTA 209
Cdd:PLN02398 216 --LFEGTPEQMLSSLQKIISLPDDTNIYCGHEYTL 248
ST1585-like_MBL-fold cd07726
uncharacterized subgroup which includes Sulfolobus tokodaii ST1585 protein; MBL-fold metallo ...
 7-205 4.39e-09

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: 55.19  E-value: 4.39e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598111   7 TAFFDPATSTYSYVVRDPSSraCAIVDPvldydpaaGrTSHaSAERLIAHVRQHDL---QVEWLLETHVHADHLSAAIFL 83
Cdd:cd07726   7 LGFLGFPGRIASYLLDGEGR--PALIDT--------G-PSS-SVPRLLAALEALGIapeDVDYIILTHIHLDHAGGAGLL 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598111  84 QRELGGC-----------------LAIGARitQVqakfsglfnLGEAF--------PVDGRQFEHLfEDGESFRIGALEC 138
Cdd:cd07726  75 AEALPNAkvyvhprgarhlidpskLWASAR--AV---------YGDEAdrlggeilPVPEERVIVL-EDGETLDLGGRTL 142

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15598111 139 RALHTPGHTPACMTYLVGDS--AFVGDT--LFMPDYGTARC------DFpggDARQLYRSIQRLFALpDATRLFMCH 205
Cdd:cd07726 143 EVIDTPGHAPHHLSFLDEESdgLFTGDAagVRYPELDVVGPpstpppDF---DPEAWLESLDRLLSL-KPERIYLTH 215
TTHA1429-like_MBL-fold cd07725
uncharacterized Thermus thermophilus TTHA1429 and related proteins; MBL-fold metallo hydrolase ...
 18-196 1.32e-08

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: 53.46  E-value: 1.32e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598111  18 SYVVRDPSSRAcaIVDPVLDYDPAAGrtshaSAERLIAHVRQHDLQVEWLLETHVHADHLSAAIFLQrELGGCLAIGARI 97
Cdd:cd07725  17 VYLLRDGDETT--LIDTGLATEEDAE-----ALWEGLKELGLKPSDIDRVLLTHHHPDHIGLAGKLQ-EKSGATVYILDV 88

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598111  98 TQVQakfsglfnlgeafpvdgrqfehlfeDGESFRIGALECRALHTPGHTP--ACMTYLVGDSAFVGDTLfMPDY---GT 172
Cdd:cd07725  89 TPVK-------------------------DGDKIDLGGLRLKVIETPGHTPghIVLYDEDRRELFVGDAV-LPKItpnVS 142

                       170       180
                ....*....|....*....|....
gi 15598111 173 ARCDFPGGDARQLYRSIQRLFALP 196
Cdd:cd07725 143 LWAVRVEDPLGAYLESLDKLEKLD 166
EVM-1-like_MBL-B3 cd16315
Erythrobacter vulgaris EVM-1 and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 64-159 1.48e-07

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


Pssm-ID: 293873 [Multi-domain]  Cd Length: 248  Bit Score: 51.20  E-value: 1.48e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598111  64 VEWLLETHVHADHLSAAIFLQRELGGCLAIGARITQV-----------QAkfsGLFNLGEAFPVDGrqfehLFEDGESFR 132
Cdd:cd16315  61 VRWLLSSHEHFDHVGGLAALQRATGARVAASAAAAPVlesgkpapddpQA---GLHEPFPPVRVDR-----IVEDGDTVA 132

                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 15598111 133 IGALECRALHTPGHTP-------------ACMTYLVGDSA 159
Cdd:cd16315 133 LGSLRLTAHATPGHTPgalswtwrscegaDCRTIVYADSL 172
BJP-1_FEZ-1-like_MBL-B3 cd16288
BJP-1, FEZ-1, GOB-1, Mbl1b and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 63-155 2.03e-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: 50.78  E-value: 2.03e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598111  63 QVEWLLETHVHADHLSAAIFLQRELGGCLAIGARITQVQAK-FSGLFNLGE---AFPvdGRQFEHLFEDGESFRIGALEC 138
Cdd:cd16288  60 DIKILLNSHAHLDHAGGLAALKKLTGAKLMASAEDAALLASgGKSDFHYGDdslAFP--PVKVDRVLKDGDRVTLGGTTL 137

                        90
                ....*....|....*..
gi 15598111 139 RALHTPGHTPACMTYLV 155
Cdd:cd16288 138 TAHLTPGHTRGCTTWTM 154
AIM-1_SMB-1-like_MBL-B3 cd16290
AIM-1, SMB-1, EVM-1, THIN-B and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 49-153 2.50e-07

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


Pssm-ID: 293848 [Multi-domain]  Cd Length: 256  Bit Score: 50.81  E-value: 2.50e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598111  49 SAERLIAHVRQ-----HDlqVEWLLETHVHADHLSAAIFLQRELGGCLAigARITQVQAKFSGLFN-----LGEAFPVDG 118
Cdd:cd16290  43 SAPQIEANIRAlgfrlED--VKLILNSHAHFDHAGGIAALQRDSGATVA--ASPAGAAALRSGGVDpddpqAGAADPFPP 118

                        90       100       110
                ....*....|....*....|....*....|....*
gi 15598111 119 RQFEHLFEDGESFRIGALECRALHTPGHTPACMTY 153
Cdd:cd16290 119 VAKVRVVADGEVVKLGPLAVTAHATPGHTPGGTSW 153
metallo-hydrolase-like_MBL-fold cd16282
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 46-199 4.51e-07

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


Pssm-ID: 293840 [Multi-domain]  Cd Length: 209  Bit Score: 49.49  E-value: 4.51e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598111  46 SHASAERLIAHVRQH-DLQVEWLLETHVHADH-LSAAIFlqrelggcLAIGARI--------TQVQAKFSGLFNLGEAFP 115
Cdd:cd16282  34 SPRLARALLAAIRKVtDKPVRYVVNTHYHGDHtLGNAAF--------ADAGAPIiahentreELAARGEAYLELMRRLGG 105

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598111 116 VDGRQFE-----HLFEDGESFRIGALECRALHT-PGHTPacmtylvGDSA---------FVGDTLFMPDYGTarcdFPGG 180
Cdd:cd16282 106 DAMAGTElvlpdRTFDDGLTLDLGGRTVELIHLgPAHTP-------GDLVvwlpeegvlFAGDLVFNGRIPF----LPDG 174

                       170
                ....*....|....*....
gi 15598111 181 DARQLYRSIQRLFALPDAT 199
Cdd:cd16282 175 SLAGWIAALDRLLALDATV 193
metallo-hydrolase-like_MBL-fold cd16280
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 64-154 9.55e-07

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


Pssm-ID: 293838 [Multi-domain]  Cd Length: 251  Bit Score: 48.74  E-value: 9.55e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598111  64 VEWLLETHVHADHLSAAIFLQRELGGCLA---IGARITQVQAKFSGLFNLGEAFPVDGrqfehLFEDGESFRIGALECRA 140
Cdd:cd16280  62 IKYILITHGHGDHYGGAAYLKDLYGAKVVmseADWDMMEEPPEEGDNPRWGPPPERDI-----VIKDGDTLTLGDTTITV 136

                        90
                ....*....|....
gi 15598111 141 LHTPGHTPACMTYL 154
Cdd:cd16280 137 YLTPGHTPGTLSLI 150
metallo-hydrolase-like_MBL-fold cd07743
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 18-166 1.09e-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) 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: 48.30  E-value: 1.09e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598111  18 SYVVRDPS--------SRACAIVDPVLDYDpaAGRTshasAERLIahvRQHDLQVEWLLETHVHADHLSAAIFLQRELgG 89
Cdd:cd07743   1 TYYIPGPTnigvyvfgDKEALLIDSGLDED--AGRK----IRKIL---EELGWKLKAIINTHSHADHIGGNAYLQKKT-G 70

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598111  90 CL----AIGARITQ---VQAKFSG----------LFNLGEAFPVDgrqfeHLFEDGEsFRIGALECRALHTPGHTPACMT 152
Cdd:cd07743  71 CKvyapKIEKAFIEnplLEPSYLGgayppkelrnKFLMAKPSKVD-----DIIEEGE-LELGGVGLEIIPLPGHSFGQIG 144

                       170
                ....*....|....*
gi 15598111 153 YLVGDS-AFVGDTLF 166
Cdd:cd07743 145 ILTPDGvLFAGDALF 159
GOB1-like_MBL-B3 cd16308
Elizabethkingia meningoseptica GOB-1 and related metallo-beta-lactamases, subclass B3; ...
 64-155 3.23e-06

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


Pssm-ID: 293866 [Multi-domain]  Cd Length: 254  Bit Score: 47.46  E-value: 3.23e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598111  64 VEWLLETHVHADHLSAAIFLQRELGGCLAIGARITQVQAkfSG---LFNLGEA----FPVDGRQfehLFEDGESFRIGAL 136
Cdd:cd16308  61 IKILLTTQAHYDHVGAMAAIKQQTGAKMMVDEKDAKVLA--DGgksDYEMGGYgstfAPVKADK---LLHDGDTIKLGGT 135

                        90
                ....*....|....*....
gi 15598111 137 ECRALHTPGHTPACMTYLV 155
Cdd:cd16308 136 KLTLLHHPGHTKGSCSFLF 154
MBL-B3-like cd07708
metallo-beta-lactamases, subclass B3; MBL-fold metallo-hydrolase domain; MBLs (class B of the ...
 64-153 4.24e-06

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: 47.15  E-value: 4.24e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598111  64 VEWLLETHVHADHLSAAIFLQRELGGCLAIGAR-----ITQVQAKFSGLFNLGEAFPvdGRQFEHLFEDGESFRIGALEC 138
Cdd:cd07708  61 TKLILISHAHFDHAGGSAEIKKQTGAKVMAGAEdvsllLSGGSSDFHYANDSSTYFP--QSTVDRAVHDGERVTLGGTVL 138

                        90
                ....*....|....*
gi 15598111 139 RALHTPGHTPACMTY 153
Cdd:cd07708 139 TAHATPGHTPGCTTW 153
L1_POM-1-like_MBL-B3 cd16289
Stenotrophomonas maltophilia L1, Pseudomonas otitidis POM-1 and related ...
 50-170 7.70e-06

Stenotrophomonas maltophilia L1, Pseudomonas otitidis POM-1 and related metallo-beta-lactamases, subclass B3; MBL-fold metallo-hydrolase domain; MBLs (class B of the Ambler beta-lactamase classification) are a diverse group of metallo-enzymes that are capable of catalyzing the hydrolysis of a wide range of beta-lactam antibiotics. MBLs have been divided into three subclasses B1, B2 and B3, based on sequence/structural relationships and substrates, with the B1 and B2 MBLs being most closely related to each other. This subgroup of L1- and Pom-1-like MBLs belongs to the B3 subclass. Subclass B3 enzymes are most active with two zinc ions bound in the active site, and have a broad-spectrum substrate profile. These B3 enzymes have a modified Zn2/DCH site (Asp-His-His).


Pssm-ID: 293847  Cd Length: 239  Bit Score: 45.96  E-value: 7.70e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598111  50 AERLIAHVRQ---HDLQVEWLLETHVHADHLSAAIFLQRELGGCLAIGARITQVQAKFSG---LFNLGEAFPvdGRQFEH 123
Cdd:cd16289  44 ADMLLDNMRAlgvAPGDLKLILHSHAHADHAGPLAALKRATGARVAANAESAVLLARGGSddiHFGDGITFP--PVQADR 121

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*
gi 15598111 124 LFEDGESFRIGALECRALHTPGHTPACMTYLVGDS--------AFVgDTLFMPDY 170
Cdd:cd16289 122 IVMDGEVVTLGGVTFTAHFTPGHTPGSTSWTWTDTrdgkpvriAYA-DSLSAPGY 175
Mbl1b-like_MBL-B3 cd16310
Caulobacter crescentus Mbl1b and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 64-153 9.76e-06

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: 45.90  E-value: 9.76e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598111  64 VEWLLETHVHADHLSAAIFLQRELGGCLAigARITQVQAKFSGLF---NLGEAFPVDGRQFEHLFEDGESFRIGALECRA 140
Cdd:cd16310  61 IKIIINTHAHYDHAGGLAQLKADTGAKLW--ASRGDRPALEAGKHigdNITQPAPFPAVKVDRILGDGEKIKLGDITLTA 138

                        90
                ....*....|...
gi 15598111 141 LHTPGHTPACMTY 153
Cdd:cd16310 139 TLTPGHTKGCTTW 151
LACTB2-like_MBL-fold cd07722
uncharacterized subgroup which includes human lactamase beta 2 and related proteins; MBL-fold ...
 70-164 2.51e-05

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: 44.06  E-value: 2.51e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598111  70 THVHADHLsaaiflqrelGGCLAIGARITQVQA---KFSGLFNLGEAFPVDGRQfeHLFEDGESFRIGALECRALHTPGH 146
Cdd:cd07722  63 THWHHDHV----------GGLPDVLDLLRGPSPrvyKFPRPEEDEDPDEDGGDI--HDLQDGQVFKVEGATLRVIHTPGH 130

                        90       100
                ....*....|....*....|
gi 15598111 147 TP--ACMTYLVGDSAFVGDT 164
Cdd:cd07722 131 TTdhVCFLLEEENALFTGDC 150
SMB-1-like_MBL-B3 cd16313
SMB-1, THIN-B and related metallo-beta-lactamases, subclass B3; MBL-fold metallo-hydrolase ...
 45-147 3.35e-05

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


Pssm-ID: 293871 [Multi-domain]  Cd Length: 254  Bit Score: 44.47  E-value: 3.35e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598111  45 TSHASAERLIAHVRQHDLQVE---WLLETHVHADHLSAAIFLQRELGGCLAIGAriTQVQAKFSGlfNLGEAFPvdgrQF 121
Cdd:cd16313  39 GFPKSPEQIAASIRQLGFKLEdvkYILSSHDHWDHAGGIAALQKLTGAQVLASP--ATVAVLRSG--SMGKDDP----QF 110

                        90       100       110
                ....*....|....*....|....*....|....*..
gi 15598111 122 EHL-----------FEDGESFRIGALECRALHTPGHT 147
Cdd:cd16313 111 GGLtpmppvasvraVRDGEVVKLGPLAVTAHATPGHT 147
BJP-1-like_MBL-B3 cd16309
Bradyrhizobium diazoefficiens BJP-1 and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 64-153 1.01e-04

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


Pssm-ID: 293867 [Multi-domain]  Cd Length: 252  Bit Score: 42.86  E-value: 1.01e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598111  64 VEWLLETHVHADHLSAAIFLQRELGGCLAIGARITQVQAkfSGLFNLGE----AFP---VDgrqfeHLFEDGESFRIGAL 136
Cdd:cd16309  61 VKYLLNTHAHFDHAGGLAELKKATGAQLVASAADKPLLE--SGYVGSGDtknlQFPpvrVD-----RVIGDGDKVTLGGT 133

                        90
                ....*....|....*..
gi 15598111 137 ECRALHTPGHTPACMTY 153
Cdd:cd16309 134 TLTAHLTPGHSPGCTSW 150
MBLAC1-like_MBL-fold cd07711
uncharacterized human metallo-beta-lactamase domain-containing protein 1 and related proteins; ...
 117-197 1.64e-04

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: 41.80  E-value: 1.64e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598111 117 DGRQFEHLFEDGESFRIGAlECRALHTPGHTPACMTYLV-----GDSAFVGDtLFM---PDYGTARCDFPGGDARQLYRS 188
Cdd:cd07711  93 GDSYDDHSLEEGDGYEIDE-NVEVIPTPGHTPEDVSVLVetekkGTVAVAGD-LFEreeDLEDPILWDPLSEDPELQEES 170


                ....*....
gi 15598111 189 IQRLFALPD 197
Cdd:cd07711 171 RKRILALAD 179
MBLAC2-like_MBL-fold cd07712
uncharacterized human metallo-beta-lactamase domain-containing protein 2 and related proteins; ...
 123-204 1.75e-04

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


Pssm-ID: 293798 [Multi-domain]  Cd Length: 182  Bit Score: 41.46  E-value: 1.75e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598111 123 HLFEDGESFRIGALECRALHTPGHTPACMTYLVGDS--AFVGDT-----LFMpdygtarcDFPGGDARQLYRSIQRLFAL 195
Cdd:cd07712 100 LPLRDGDVIDLGDRQLEVIHTPGHTPGSIALLDRANrlLFSGDVvydgpLIM--------DLPHSDLDDYLASLEKLSKL 171


                ....*....
gi 15598111 196 PDATRLFMC 204
Cdd:cd07712 172 PDEFDKVLP 180
AIM-1-like_MBL-B3 cd16314
Pseudomonas Aeruginosa AIM-1 and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 48-148 3.39e-04

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


Pssm-ID: 293872 [Multi-domain]  Cd Length: 255  Bit Score: 41.42  E-value: 3.39e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598111  48 ASAERLIAHVRQHDLQVE---WLLETHVHADHLSAAIFLQRELGGCLAigARITQVQAKFSGL-------FNLGEAF-PV 116
Cdd:cd16314  42 KAAPLIEANIRALGFRPEdvrYIVSSHEHFDHAGGIARLQRATGAPVV--AREPAATTLERGRsdrsdpqFLVVEKFpPV 119

                        90       100       110
                ....*....|....*....|....*....|..
gi 15598111 117 DGRQfehLFEDGESFRIGALECRALHTPGHTP 148
Cdd:cd16314 120 ASVQ---RIGDGEVLRVGPLALTAHATPGHTP 148
THIN-B2-like_MBL-B3 cd16311
Janthinobacterium lividum THIN-B2 and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 49-202 3.41e-04

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


Pssm-ID: 293869  Cd Length: 257  Bit Score: 41.13  E-value: 3.41e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598111  49 SAERLIAHVRQHDLQVE---WLLETHVHADHLSAAIFLQRELGGCLAigaritqvqAKFSGLFNL--GEAFPvDGRQFE- 122
Cdd:cd16311  43 SAPKIIANIEALGFRIEdvkLILNSHGHIDHAGGLAELQRRSGALVA---------ASPSAALDLasGEVGP-DDPQYHa 112

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598111 123 ----------HLFEDGESFRIGALECRALHTPGHTPA-------------CMTYLVGDSAfvgDTLFMPDYG-TARCDFP 178
Cdd:cd16311 113 lpkyppvkdmRLARDGGQFNVGPVSLTAHATPGHTPGglswtwqscdgprCLNMVYADSQ---NAVSRPGFKfSASSEYP 189

                       170       180       190
                ....*....|....*....|....*....|..
gi 15598111 179 GG--DARQLYRSIQRL------FALPDATRLF 202
Cdd:cd16311 190 NAvaDLRRSFETLEKLpcdvliSAHPEASQLW 221
THIN-B-like_MBL-B3 cd16312
Janthinobacterium lividum THIN-B and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 49-153 5.64e-04

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


Pssm-ID: 293870 [Multi-domain]  Cd Length: 258  Bit Score: 40.74  E-value: 5.64e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598111  49 SAERLIAHVRQHDLQVE---WLLETHVHADHLSAAIFLQRELGGCLAIGARITQV-QAKFSGL----FNLGEAFPVDGRQ 120
Cdd:cd16312  43 SAPLIIANIEALGFRIEdvkLILNSHAHWDHAGGIAALQKASGATVAASAHGAQVlQSGTNGKddpqYQAKPVVHVAKVA 122

                        90       100       110
                ....*....|....*....|....*....|...
gi 15598111 121 FEHLFEDGESFRIGALECRALHTPGHTPACMTY 153
Cdd:cd16312 123 KVKEVGEGDTLKVGPLRLTAHMTPGHTPGGTTW 155
AHL_lactonase_MBL-fold cd07729
quorum-quenching N-acyl-homoserine lactonase, MBL-fold metallo-hydrolase domain; Acyl ...
 70-206 2.86e-03

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: 38.35  E-value: 2.86e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598111  70 THVHADHLS-------AAIFLQR-ELGGCLAIGARitqvqAKFSGLFNLGEAFPVDGRQFEHLFEDGESFriGALECraL 141
Cdd:cd07729  95 SHLHFDHAGgldlfpnATIIVQRaELEYATGPDPL-----AAGYYEDVLALDDDLPGGRVRLVDGDYDLF--PGVTL--I 165

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15598111 142 HTPGHTPACMTYLV----GDSAFVGDTLFMPD-YGTARCDFPGGDARQLYRSIQRLFALPDAT--RLFMCHD 206
Cdd:cd07729 166 PTPGHTPGHQSVLVrlpeGTVLLAGDAAYTYEnLEEGRPPGINYDPEAALASLERLKALAEREgaRVIPGHD 237
metallo-hydrolase-like_MBL-fold cd16279
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo; ...
 70-169 5.77e-03

uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo; 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 named as octanoyltransferase (also known as lipoate-protein ligase B).


Pssm-ID: 293837 [Multi-domain]  Cd Length: 193  Bit Score: 37.07  E-value: 5.77e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598111  70 THVHADH------LSAAIFLQRELGGCLAIGARITQVQAKFSGLFNLGEAFPVDGRQFeHLFEDGESFRIGALECRAL-- 141
Cdd:cd16279  73 THAHADHihglddLRPFNRLQQRPIPVYASEETLDDLKRRFPYFFAATGGGGVPKLDL-HIIEPDEPFTIGGLEITPLpv 151

                        90       100
                ....*....|....*....|....*....
gi 15598111 142 -HtpGHTPaCMTYLVGDSAFVGDTLFMPD 169
Cdd:cd16279 152 lH--GKLP-SLGFRFGDFAYLTDVSEIPE 177
UlaG COG2220
L-ascorbate lactonase UlaG, metallo-beta-lactamase superfamily [Carbohydrate transport and ...
 31-178 6.16e-03

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


Pssm-ID: 441822 [Multi-domain]  Cd Length: 224  Bit Score: 37.20  E-value: 6.16e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598111  31 IVDPVLDYDPAAGRTSHASAERLiahvrqhdLQVEWLLETHVHADHLSAAIFlqrelggclaigARITQVQAKFSGLFNL 110
Cdd:COG2220  24 LIDPVFSGRASPVNPLPLDPEDL--------PKIDAVLVTHDHYDHLDDATL------------RALKRTGATVVAPLGV 83

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15598111 111 GEAFPVDGRQFEHLFEDGESFRIGALE---CRALHTPGHTPACMT----YLVGDSA----FVGDTLFMPDYGTARCDFP 178
Cdd:COG2220  84 AAWLRAWGFPRVTELDWGESVELGGLTvtaVPARHSSGRPDRNGGlwvgFVIETDGktiyHAGDTGYFPEMKEIGERFP 162
 
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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