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Conserved domains on  [gi|16128199|ref|NP_414748|]
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hydroxyacylglutathione hydrolase GloB [Escherichia coli str. K-12 substr. MG1655]

Protein Classification

hydroxyacylglutathione hydrolase( domain architecture ID 11484625)

hydroxyacylglutathione hydrolase is a type II glyoxalase that catalyzes the hydrolysis of (R)-S-lactoylglutathione to (R)-lactate and glutathione

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK10241 PRK10241
hydroxyacylglutathione hydrolase; Provisional
 1-251 0e+00

hydroxyacylglutathione hydrolase; Provisional


:

Pssm-ID: 182327 [Multi-domain]  Cd Length: 251  Bit Score: 549.81  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128199    1 MNLNSIPAFDDNYIWVLNDEAGRCLIVDPGDAEPVLNAIAANNWQPEAIFLTHHHHDHVGGVKELVEKFPQIVVYGPQET 80
Cdd:PRK10241   1 MNLNSIPAFDDNYIWVLNDEAGRCLIVDPGEAEPVLNAIAENNWQPEAIFLTHHHHDHVGGVKELVEKFPQIVVYGPQET 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128199   81 QDKGTTQVVKDGETAFVLGHEFSVIATPGHTLGHICYFSKPYLFCGDTLFSGGCGRLFEGTASQMYQSLKKLSALPDDTL 160
Cdd:PRK10241  81 QDKGTTQVVKDGETAFVLGHEFSVFATPGHTLGHICYFSKPYLFCGDTLFSGGCGRLFEGTASQMYQSLKKINALPDDTL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128199  161 VCCAHEYTLSNMKFALSILPHDLSINDYYRKVKELRAKNQITLPVILKNERQINVFLRTEDIDLINVINEETLLQQPEER 240
Cdd:PRK10241 161 ICCAHEYTLSNMKFALSILPHDLSINDYYRKVKELRAKNQITLPVILKNERQINLFLRTEDIDLINVINEETLLQQPEER 240

                        250
                 ....*....|.
gi 16128199  241 FAWLRSKKDRF 251
Cdd:PRK10241 241 FAWLRSKKDRF 251
 
Name Accession Description Interval E-value
PRK10241 PRK10241
hydroxyacylglutathione hydrolase; Provisional
 1-251 0e+00

hydroxyacylglutathione hydrolase; Provisional


Pssm-ID: 182327 [Multi-domain]  Cd Length: 251  Bit Score: 549.81  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128199    1 MNLNSIPAFDDNYIWVLNDEAGRCLIVDPGDAEPVLNAIAANNWQPEAIFLTHHHHDHVGGVKELVEKFPQIVVYGPQET 80
Cdd:PRK10241   1 MNLNSIPAFDDNYIWVLNDEAGRCLIVDPGEAEPVLNAIAENNWQPEAIFLTHHHHDHVGGVKELVEKFPQIVVYGPQET 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128199   81 QDKGTTQVVKDGETAFVLGHEFSVIATPGHTLGHICYFSKPYLFCGDTLFSGGCGRLFEGTASQMYQSLKKLSALPDDTL 160
Cdd:PRK10241  81 QDKGTTQVVKDGETAFVLGHEFSVFATPGHTLGHICYFSKPYLFCGDTLFSGGCGRLFEGTASQMYQSLKKINALPDDTL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128199  161 VCCAHEYTLSNMKFALSILPHDLSINDYYRKVKELRAKNQITLPVILKNERQINVFLRTEDIDLINVINEETLLQQPEER 240
Cdd:PRK10241 161 ICCAHEYTLSNMKFALSILPHDLSINDYYRKVKELRAKNQITLPVILKNERQINLFLRTEDIDLINVINEETLLQQPEER 240

                        250
                 ....*....|.
gi 16128199  241 FAWLRSKKDRF 251
Cdd:PRK10241 241 FAWLRSKKDRF 251
GSH_gloB TIGR03413
hydroxyacylglutathione hydrolase; Members of this protein family are hydroxyacylglutathione ...
 3-251 1.52e-142

hydroxyacylglutathione hydrolase; Members of this protein family are hydroxyacylglutathione hydrolase, a detoxification enzyme known as glyoxalase II. It follows lactoylglutathione lyase, or glyoxalase I, and acts to remove the toxic metabolite methylglyoxal and related compounds. This protein belongs to the broader metallo-beta-lactamase family (pfam00753). [Cellular processes, Detoxification]


Pssm-ID: 274569 [Multi-domain]  Cd Length: 248  Bit Score: 399.22  E-value: 1.52e-142
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128199     3 LNSIPAFDDNYIWVLNDEAGRCLIVDPGDAEPVLNAIAANNWQPEAIFLTHHHHDHVGGVKELVEKFPqIVVYGPQETQD 82
Cdd:TIGR03413   1 IIPIPALSDNYIWLLHDPDGQAAVVDPGEAEPVLDALEARGLTLTAILLTHHHHDHVGGVAELLEAFP-APVYGPAEERI 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128199    83 KGTTQVVKDGETAFVLGHEFSVIATPGHTLGHICYFS--KPYLFCGDTLFSGGCGRLFEGTASQMYQSLKKLSALPDDTL 160
Cdd:TIGR03413  80 PGITHPVKDGDTVTLGGLEFEVLAVPGHTLGHIAYYLpdSPALFCGDTLFSAGCGRLFEGTPEQMYDSLQRLAALPDDTL 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128199   161 VCCAHEYTLSNMKFALSILPHDLSINDYYRKVKELRAKNQITLPVILKNERQINVFLRTEDIDLINVINEEtlLQQPEER 240
Cdd:TIGR03413 160 VYCAHEYTLSNLRFALTVEPDNPALQERLKEVEALRAQGQPTLPSTLGLERATNPFLRADDPAVRAALGSQ--GADPVEV 237

                         250
                  ....*....|.
gi 16128199   241 FAWLRSKKDRF 251
Cdd:TIGR03413 238 FAALRAWKDNF 248
hydroxyacylglutathione_hydrolase_MBL-fold cd07723
hydroxyacylglutathione hydrolase, MBL-fold metallo-hydrolase domain; hydroxyacylglutathione ...
 6-165 1.71e-86

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: 253.92  E-value: 1.71e-86
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128199   6 IPAFDDNYIWVLNDEA-GRCLIVDPGDAEPVLNAIAANNWQPEAIFLTHHHHDHVGGVKELVEKFPQIVVYGPQETQDKG 84
Cdd:cd07723   3 IPALSDNYIYLIVDEAtGEAAVVDPGEAEPVLAALEKNGLTLTAILTTHHHWDHTGGNAELKALFPDAPVYGPAEDRIPG 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128199  85 TTQVVKDGETAFVLGHEFSVIATPGHTLGHICYF--SKPYLFCGDTLFSGGCGRLFEGTASQMYQSLKKLSALPDDTLVC 162
Cdd:cd07723  83 LDHPVKDGDEIKLGGLEVKVLHTPGHTLGHICYYvpDEPALFTGDTLFSGGCGRFFEGTAEQMYASLQKLLALPDDTLVY 162


                ...
gi 16128199 163 CAH 165
Cdd:cd07723 163 CGH 165
GloB COG0491
Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General ...
 7-170 1.44e-39

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: 136.36  E-value: 1.44e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128199   7 PAFDDNYIWVLNDEaGRCLIVDPG----DAEPVLNAIAANNWQPEAIFLTHHHHDHVGGVKELVEKFpQIVVYGPQETQD 82
Cdd:COG0491  10 GAGLGVNSYLIVGG-DGAVLIDTGlgpaDAEALLAALAALGLDIKAVLLTHLHPDHVGGLAALAEAF-GAPVYAHAAEAE 87

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128199  83 KGT---------------TQVVKDGETAFVLGHEFSVIATPGHTLGHICYF--SKPYLFCGDTLFSGGCGR--LFEGTAS 143
Cdd:COG0491  88 ALEapaagalfgrepvppDRTLEDGDTLELGGPGLEVIHTPGHTPGHVSFYvpDEKVLFTGDALFSGGVGRpdLPDGDLA 167

                       170       180
                ....*....|....*....|....*..
gi 16128199 144 QMYQSLKKLSALPDDtLVCCAHEYTLS 170
Cdd:COG0491 168 QWLASLERLLALPPD-LVIPGHGPPTT 193
HAGH_C pfam16123
Hydroxyacylglutathione hydrolase C-terminus; This domain is found at the C-terminus of ...
 166-251 1.08e-29

Hydroxyacylglutathione hydrolase C-terminus; This domain is found at the C-terminus of hydroxyacylglutathione hydrolase enzymes. Substrate binding occurs at the interface between this domain and the catalytic domain (pfam00753).


Pssm-ID: 465030 [Multi-domain]  Cd Length: 82  Bit Score: 106.37  E-value: 1.08e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128199   166 EYTLSNMKFALSILPHDLSINDYYRKVKELRAKNQITLPVILKNERQINVFLRTEDIDLINVINEETllqqPEERFAWLR 245
Cdd:pfam16123   1 EYTLSNLKFALSVEPDNEALQKRLAWVEALRAAGEPTVPSTLGDEKATNPFLRVDDPAVQKATGETD----PVEVFAALR 76


                  ....*.
gi 16128199   246 SKKDRF 251
Cdd:pfam16123  77 ELKDNF 82
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 13-165 3.02e-25

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: 98.01  E-value: 3.02e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128199     13 YIWVLNDEaGRCLIVDPG--DAEPVLNAIAANNW-QPEAIFLTHHHHDHVGGVKELVEKfPQIVVYGPQETQD------- 82
Cdd:smart00849   1 NSYLVRDD-GGAILIDTGpgEAEDLLAELKKLGPkKIDAIILTHGHPDHIGGLPELLEA-PGAPVYAPEGTAEllkdlla 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128199     83 -----------KGTTQVVKDGETAFVLGHEFSVIATPGHTLGHICYF--SKPYLFCGDTLFSGGCGRLF-EGTASQMYQS 148
Cdd:smart00849  79 llgelgaeaepAPPDRTLKDGDELDLGGGELEVIHTPGHTPGSIVLYlpEGKILFTGDLLFAGGDGRTLvDGGDAAASDA 158

                          170
                   ....*....|....*....
gi 16128199    149 LKKLSAL--PDDTLVCCAH 165
Cdd:smart00849 159 LESLLKLlkLLPKLVVPGH 177
 
Name Accession Description Interval E-value
PRK10241 PRK10241
hydroxyacylglutathione hydrolase; Provisional
 1-251 0e+00

hydroxyacylglutathione hydrolase; Provisional


Pssm-ID: 182327 [Multi-domain]  Cd Length: 251  Bit Score: 549.81  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128199    1 MNLNSIPAFDDNYIWVLNDEAGRCLIVDPGDAEPVLNAIAANNWQPEAIFLTHHHHDHVGGVKELVEKFPQIVVYGPQET 80
Cdd:PRK10241   1 MNLNSIPAFDDNYIWVLNDEAGRCLIVDPGEAEPVLNAIAENNWQPEAIFLTHHHHDHVGGVKELVEKFPQIVVYGPQET 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128199   81 QDKGTTQVVKDGETAFVLGHEFSVIATPGHTLGHICYFSKPYLFCGDTLFSGGCGRLFEGTASQMYQSLKKLSALPDDTL 160
Cdd:PRK10241  81 QDKGTTQVVKDGETAFVLGHEFSVFATPGHTLGHICYFSKPYLFCGDTLFSGGCGRLFEGTASQMYQSLKKINALPDDTL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128199  161 VCCAHEYTLSNMKFALSILPHDLSINDYYRKVKELRAKNQITLPVILKNERQINVFLRTEDIDLINVINEETLLQQPEER 240
Cdd:PRK10241 161 ICCAHEYTLSNMKFALSILPHDLSINDYYRKVKELRAKNQITLPVILKNERQINLFLRTEDIDLINVINEETLLQQPEER 240

                        250
                 ....*....|.
gi 16128199  241 FAWLRSKKDRF 251
Cdd:PRK10241 241 FAWLRSKKDRF 251
GSH_gloB TIGR03413
hydroxyacylglutathione hydrolase; Members of this protein family are hydroxyacylglutathione ...
 3-251 1.52e-142

hydroxyacylglutathione hydrolase; Members of this protein family are hydroxyacylglutathione hydrolase, a detoxification enzyme known as glyoxalase II. It follows lactoylglutathione lyase, or glyoxalase I, and acts to remove the toxic metabolite methylglyoxal and related compounds. This protein belongs to the broader metallo-beta-lactamase family (pfam00753). [Cellular processes, Detoxification]


Pssm-ID: 274569 [Multi-domain]  Cd Length: 248  Bit Score: 399.22  E-value: 1.52e-142
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128199     3 LNSIPAFDDNYIWVLNDEAGRCLIVDPGDAEPVLNAIAANNWQPEAIFLTHHHHDHVGGVKELVEKFPqIVVYGPQETQD 82
Cdd:TIGR03413   1 IIPIPALSDNYIWLLHDPDGQAAVVDPGEAEPVLDALEARGLTLTAILLTHHHHDHVGGVAELLEAFP-APVYGPAEERI 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128199    83 KGTTQVVKDGETAFVLGHEFSVIATPGHTLGHICYFS--KPYLFCGDTLFSGGCGRLFEGTASQMYQSLKKLSALPDDTL 160
Cdd:TIGR03413  80 PGITHPVKDGDTVTLGGLEFEVLAVPGHTLGHIAYYLpdSPALFCGDTLFSAGCGRLFEGTPEQMYDSLQRLAALPDDTL 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128199   161 VCCAHEYTLSNMKFALSILPHDLSINDYYRKVKELRAKNQITLPVILKNERQINVFLRTEDIDLINVINEEtlLQQPEER 240
Cdd:TIGR03413 160 VYCAHEYTLSNLRFALTVEPDNPALQERLKEVEALRAQGQPTLPSTLGLERATNPFLRADDPAVRAALGSQ--GADPVEV 237

                         250
                  ....*....|.
gi 16128199   241 FAWLRSKKDRF 251
Cdd:TIGR03413 238 FAALRAWKDNF 248
hydroxyacylglutathione_hydrolase_MBL-fold cd07723
hydroxyacylglutathione hydrolase, MBL-fold metallo-hydrolase domain; hydroxyacylglutathione ...
 6-165 1.71e-86

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: 253.92  E-value: 1.71e-86
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128199   6 IPAFDDNYIWVLNDEA-GRCLIVDPGDAEPVLNAIAANNWQPEAIFLTHHHHDHVGGVKELVEKFPQIVVYGPQETQDKG 84
Cdd:cd07723   3 IPALSDNYIYLIVDEAtGEAAVVDPGEAEPVLAALEKNGLTLTAILTTHHHWDHTGGNAELKALFPDAPVYGPAEDRIPG 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128199  85 TTQVVKDGETAFVLGHEFSVIATPGHTLGHICYF--SKPYLFCGDTLFSGGCGRLFEGTASQMYQSLKKLSALPDDTLVC 162
Cdd:cd07723  83 LDHPVKDGDEIKLGGLEVKVLHTPGHTLGHICYYvpDEPALFTGDTLFSGGCGRFFEGTAEQMYASLQKLLALPDDTLVY 162


                ...
gi 16128199 163 CAH 165
Cdd:cd07723 163 CGH 165
PLN02398 PLN02398
hydroxyacylglutathione hydrolase
 6-251 1.13e-64

hydroxyacylglutathione hydrolase


Pssm-ID: 215223 [Multi-domain]  Cd Length: 329  Bit Score: 204.31  E-value: 1.13e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128199    6 IPAFDDNYIWVLNDE-AGRCLIVDPGDAEPVLNAIAANNWQPEAIFLTHHHHDHVGGVKELVEKFPQIVVyGPQETQDK- 83
Cdd:PLN02398  81 VPCLKDNYAYLLHDEdTGTVGVVDPSEAVPVIDALSRKNRNLTYILNTHHHYDHTGGNLELKARYGAKVI-GSAVDKDRi 159

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128199   84 -GTTQVVKDGETAFVLGHEFSVIATPGHTLGHICYF--SKPYLFCGDTLFSGGCGRLFEGTASQMYQSLKKLSALPDDTL 160
Cdd:PLN02398 160 pGIDIVLKDGDKWMFAGHEVLVMETPGHTRGHISFYfpGSGAIFTGDTLFSLSCGKLFEGTPEQMLSSLQKIISLPDDTN 239

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128199  161 VCCAHEYTLSNMKFALSILPHDLSINDYYRKVKELRAKNQITLPVILKNERQINVFLRTEDIDLINVINEETLLQQpEER 240
Cdd:PLN02398 240 IYCGHEYTLSNSKFALSIEPNNEVLQSYAAHVAHLRSKGLPTIPTTVKMEKACNPFLRTSSTDIRKSLSIPDTADE-AEA 318

                        250
                 ....*....|.
gi 16128199  241 FAWLRSKKDRF 251
Cdd:PLN02398 319 LGIIRRAKDNF 329
PLN02469 PLN02469
hydroxyacylglutathione hydrolase
 1-251 7.44e-56

hydroxyacylglutathione hydrolase


Pssm-ID: 178088 [Multi-domain]  Cd Length: 258  Bit Score: 179.57  E-value: 7.44e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128199    1 MNLNSIPAFDDNYIWVLNDEA-GRCLIVDPGDAEPVLNAIAANNWQPEAIFLTHHHHDHVGGVKELVEKFPQIVVYGPQE 79
Cdd:PLN02469   1 MKIIPVPCLEDNYAYLIIDEStKDAAVVDPVDPEKVLQAAHEHGAKIKLVLTTHHHWDHAGGNEKIKKLVPGIKVYGGSL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128199   80 TQDKGTTQVVKDGETaFVLGHEFSVIA--TPGHTLGHICYF------SKPYLFCGDTLFSGGCGRLFEGTASQMYQSL-K 150
Cdd:PLN02469  81 DNVKGCTHPVENGDK-LSLGKDVNILAlhTPCHTKGHISYYvtgkegEDPAVFTGDTLFIAGCGKFFEGTAEQMYQSLcV 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128199  151 KLSALPDDTLVCCAHEYTLSNMKFALSILPHDLSINDYYRKVKELRAKNQITLPVILKNERQINVFLRtedIDLINvINE 230
Cdd:PLN02469 160 TLGSLPKPTQVYCGHEYTVKNLKFALTVEPDNEKLKQKLEWAEKQRQAGLPTVPSTIEEELETNPFMR---VDLPE-IQE 235

                        250       260
                 ....*....|....*....|.
gi 16128199  231 ETLLQQPEERFAWLRSKKDRF 251
Cdd:PLN02469 236 KVGCESPVEALREVRKMKDNW 256
GloB COG0491
Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General ...
 7-170 1.44e-39

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: 136.36  E-value: 1.44e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128199   7 PAFDDNYIWVLNDEaGRCLIVDPG----DAEPVLNAIAANNWQPEAIFLTHHHHDHVGGVKELVEKFpQIVVYGPQETQD 82
Cdd:COG0491  10 GAGLGVNSYLIVGG-DGAVLIDTGlgpaDAEALLAALAALGLDIKAVLLTHLHPDHVGGLAALAEAF-GAPVYAHAAEAE 87

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128199  83 KGT---------------TQVVKDGETAFVLGHEFSVIATPGHTLGHICYF--SKPYLFCGDTLFSGGCGR--LFEGTAS 143
Cdd:COG0491  88 ALEapaagalfgrepvppDRTLEDGDTLELGGPGLEVIHTPGHTPGHVSFYvpDEKVLFTGDALFSGGVGRpdLPDGDLA 167

                       170       180
                ....*....|....*....|....*..
gi 16128199 144 QMYQSLKKLSALPDDtLVCCAHEYTLS 170
Cdd:COG0491 168 QWLASLERLLALPPD-LVIPGHGPPTT 193
metallo-hydrolase-like_MBL-fold cd06262
mainly hydrolytic enzymes and related proteins which carry out various biological functions; ...
 15-165 8.02e-35

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: 123.16  E-value: 8.02e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128199  15 WVLNDEAGRCLIVDPGD--AEPVLNAIAANNWQPEAIFLTHHHHDHVGGVKELVEKfPQIVVYGPQETQD---------- 82
Cdd:cd06262  13 YLVSDEEGEAILIDPGAgaLEKILEAIEELGLKIKAILLTHGHFDHIGGLAELKEA-PGAPVYIHEADAElledpelnla 91

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128199  83 ---------KGTTQVVKDGETAFVLGHEFSVIATPGHTLGHICYF--SKPYLFCGDTLFSGGCGR--LFEGTASQMYQSL 149
Cdd:cd06262  92 ffgggplppPEPDILLEDGDTIELGGLELEVIHTPGHTPGSVCFYieEEGVLFTGDTLFAGSIGRtdLPGGDPEQLIESI 171

                       170
                ....*....|....*..
gi 16128199 150 KK-LSALPDDTLVCCAH 165
Cdd:cd06262 172 KKlLLLLPDDTVVYPGH 188
POD-like_MBL-fold cd07724
ETHE1 (PDO type I), persulfide dioxygenase A (PDOA, PDO type II) and related proteins; ...
 13-167 5.53e-32

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: 115.57  E-value: 5.53e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128199  13 YIwVLNDEAGRCLIVDP--GDAEPVLNAIAANNWQPEAIFLTHHHHDHVGGVKELVEKfPQIVVYGPQETQDKGTTQVVK 90
Cdd:cd07724  15 YL-VGDPETGEAAVIDPvrDSVDRYLDLAAELGLKITYVLETHVHADHVSGARELAER-TGAPIVIGEGAPASFFDRLLK 92

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128199  91 DGETaFVLGH-EFSVIATPGHTLGHICY--FSKPYLFCGDTLFSGGCGR-----LFEGTASQMYQSL-KKLSALPDDTLV 161
Cdd:cd07724  93 DGDV-LELGNlTLEVLHTPGHTPESVSYlvGDPDAVFTGDTLFVGDVGRpdlpgEAEGLARQLYDSLqRKLLLLPDETLV 171


                ....*.
gi 16128199 162 CCAHEY 167
Cdd:cd07724 172 YPGHDY 177
HAGH_C pfam16123
Hydroxyacylglutathione hydrolase C-terminus; This domain is found at the C-terminus of ...
 166-251 1.08e-29

Hydroxyacylglutathione hydrolase C-terminus; This domain is found at the C-terminus of hydroxyacylglutathione hydrolase enzymes. Substrate binding occurs at the interface between this domain and the catalytic domain (pfam00753).


Pssm-ID: 465030 [Multi-domain]  Cd Length: 82  Bit Score: 106.37  E-value: 1.08e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128199   166 EYTLSNMKFALSILPHDLSINDYYRKVKELRAKNQITLPVILKNERQINVFLRTEDIDLINVINEETllqqPEERFAWLR 245
Cdd:pfam16123   1 EYTLSNLKFALSVEPDNEALQKRLAWVEALRAAGEPTVPSTLGDEKATNPFLRVDDPAVQKATGETD----PVEVFAALR 76


                  ....*.
gi 16128199   246 SKKDRF 251
Cdd:pfam16123  77 ELKDNF 82
YcbL-like_MBL-fold cd07737
Salmonella enterica serovar typhimurium YcbL and related proteins; MBL-fold metallo hydrolase ...
 14-165 1.97e-29

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: 109.18  E-value: 1.97e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128199  14 IWvlNDEAGRCLIVDPG-DAEPVLNAIAANNWQPEAIFLTHHHHDHVGGVKELVEKFpQIVVYGPQ-------------- 78
Cdd:cd07737  16 IW--CEETKEAAVIDPGgDADKILQAIEDLGLTLKKILLTHGHLDHVGGAAELAEHY-GVPIIGPHkedkfllenlpeqs 92

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128199  79 ------ETQDKGTTQVVKDGETAFVLGHEFSVIATPGHTLGHICYFSKP--YLFCGDTLFSGGCGR--LFEGTASQMYQS 148
Cdd:cd07737  93 qmfgfpPAEAFTPDRWLEEGDTVTVGNLTLEVLHCPGHTPGHVVFFNREskLAIVGDVLFKGSIGRtdFPGGNHAQLIAS 172

                       170
                ....*....|....*...
gi 16128199 149 LK-KLSALPDDTLVCCAH 165
Cdd:cd07737 173 IKeKLLPLGDDVTFIPGH 190
BaeB-like_MBL-fold cd16275
Bacillus amyloliquefaciens BaeB and related proteins; MBL-fold metallo hydrolase domain; ...
 11-158 1.13e-26

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: 101.46  E-value: 1.13e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128199  11 DNYIWVLNDEAGR-CLIVDPG-DAEPVLNAIAANNWQPEAIFLTHHHHDHVGGVKELVEKFpQIVVYGPQETQD-----K 83
Cdd:cd16275  11 INYSYIIIDKATReAAVVDPAwDIEKILAKLNELGLTLTGILLTHSHFDHVNLVEPLLAKY-DAPVYMSKEEIDyygfrC 89

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16128199  84 GTTQVVKDGETAFVLGHEFSVIATPGHTLGHICYFSKPYLFCGDTLFSGGCGR--LFEGTASQMYQSLKKLSALPDD 158
Cdd:cd16275  90 PNLIPLEDGDTIKIGDTEITCLLTPGHTPGSMCYLLGDSLFTGDTLFIEGCGRcdLPGGDPEEMYESLQRLKKLPPP 166
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 13-165 3.02e-25

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: 98.01  E-value: 3.02e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128199     13 YIWVLNDEaGRCLIVDPG--DAEPVLNAIAANNW-QPEAIFLTHHHHDHVGGVKELVEKfPQIVVYGPQETQD------- 82
Cdd:smart00849   1 NSYLVRDD-GGAILIDTGpgEAEDLLAELKKLGPkKIDAIILTHGHPDHIGGLPELLEA-PGAPVYAPEGTAEllkdlla 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128199     83 -----------KGTTQVVKDGETAFVLGHEFSVIATPGHTLGHICYF--SKPYLFCGDTLFSGGCGRLF-EGTASQMYQS 148
Cdd:smart00849  79 llgelgaeaepAPPDRTLKDGDELDLGGGELEVIHTPGHTPGSIVLYlpEGKILFTGDLLFAGGDGRTLvDGGDAAASDA 158

                          170
                   ....*....|....*....
gi 16128199    149 LKKLSAL--PDDTLVCCAH 165
Cdd:smart00849 159 LESLLKLlkLLPKLVVPGH 177
TTHA1623-like_MBL-fold cd16322
uncharacterized Thermus thermophilus TTHA1623 and related proteins; MBL-fold metallo hydrolase ...
 5-165 5.39e-24

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: 95.49  E-value: 5.39e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128199   5 SIPAFDDNYIWVLNDEAGRCLIVDPGDAEP-VLNAIAANNWQPEAIFLTHHHHDHVGGVKELVEKfPQIVVYGPQETQ-- 81
Cdd:cd16322   5 TLGPLQENTYLVADEGGGEAVLVDPGDESEkLLARFGTTGLTLLYILLTHAHFDHVGGVADLRRH-PGAPVYLHPDDLpl 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128199  82 -DKGTTQV----------------VKDGETAFVLGHEFSVIATPGHTLGHICYF--SKPYLFCGDTLFSGGCGR--LFEG 140
Cdd:cd16322  84 yEAADLGAkafglgieplpppdrlLEDGQTLTLGGLEFKVLHTPGHSPGHVCFYveEEGLLFSGDLLFQGSIGRtdLPGG 163

                       170       180
                ....*....|....*....|....*
gi 16128199 141 TASQMYQSLKKLSALPDDTLVCCAH 165
Cdd:cd16322 164 DPKAMAASLRRLLTLPDETRVFPGH 188
yflN-like_MBL-fold cd07721
uncharacterized subgroup which includes Bacillus subtilis yflN; MBL-fold metallo hydrolase ...
 13-165 1.36e-18

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: 81.11  E-value: 1.36e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128199  13 YIWVLNDEAGRCLIvD---PGDAEPVLNAIAANNWQPE---AIFLTHHHHDHVGGVKELVEKfPQIVVY-GPQE------ 79
Cdd:cd07721  12 NAYLIEDDDGLTLI-DtglPGSAKRILKALRELGLSPKdirRILLTHGHIDHIGSLAALKEA-PGAPVYaHEREapyleg 89

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128199  80 ---------------------TQDKGTTQVVKDGETAFVLGhEFSVIATPGHTLGHICYFSKPY--LFCGDTLFSGGcGR 136
Cdd:cd07721  90 ekpypppvrlgllgllspllpVKPVPVDRTLEDGDTLDLAG-GLRVIHTPGHTPGHISLYLEEDgvLIAGDALVTVG-GE 167

                       170       180       190
                ....*....|....*....|....*....|....*
gi 16128199 137 LFEGTA------SQMYQSLKKLSALPDDTlVCCAH 165
Cdd:cd07721 168 LVPPPPpftwdmEEALESLRKLAELDPEV-LAPGH 201
TTHA1429-like_MBL-fold cd07725
uncharacterized Thermus thermophilus TTHA1429 and related proteins; MBL-fold metallo hydrolase ...
 17-160 9.46e-15

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: 70.02  E-value: 9.46e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128199  17 LNDEAGRCLIVDPG-----DAEPVLNAIAANNW---QPEAIFLTHHHHDHVGGVKELVEKFpQIVVYGPqetqdkgTTQV 88
Cdd:cd07725  19 LLRDGDETTLIDTGlateeDAEALWEGLKELGLkpsDIDRVLLTHHHPDHIGLAGKLQEKS-GATVYIL-------DVTP 90

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128199  89 VKDGETAFVLGHEFSVIATPGHTLGHICYFSKPY--LFCGDTLFS------GGCGRLFEGTASQMYQSLKKLSALPDDTL 160
Cdd:cd07725  91 VKDGDKIDLGGLRLKVIETPGHTPGHIVLYDEDRreLFVGDAVLPkitpnvSLWAVRVEDPLGAYLESLDKLEKLDVDLA 170
metallo-hydrolase-like_MBL-fold cd16278
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 15-165 1.66e-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: 69.44  E-value: 1.66e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128199  15 WVLNDEAGrCLIVDPGDAEP-----VLNAIAANNwqPEAIFLTHHHHDHVGGVKELVEKFP-QIVVYGPQETQDKGTT-- 86
Cdd:cd16278  21 YLLGAPDG-VVVIDPGPDDPahldaLLAALGGGR--VSAILVTHTHRDHSPGAARLAERTGaPVRAFGPHRAGGQDTDfa 97

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128199  87 --QVVKDGETAFVLGHEFSVIATPGHTLGHICYF--SKPYLFCGDTLFSGGCGRLF--EGTASQMYQSLKKLSALPDDTL 160
Cdd:cd16278  98 pdRPLADGEVIEGGGLRLTVLHTPGHTSDHLCFAleDEGALFTGDHVMGWSTTVIAppDGDLGDYLASLERLLALDDRLL 177


                ....*
gi 16128199 161 vCCAH 165
Cdd:cd16278 178 -LPGH 181
Lactamase_B pfam00753
Metallo-beta-lactamase superfamily;
13-165 2.29e-12

Metallo-beta-lactamase superfamily;


Pssm-ID: 425851 [Multi-domain]  Cd Length: 196  Bit Score: 63.93  E-value: 2.29e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128199    13 YIWVLNDEaGRCLIVDPG-----DAEPVLNAIAANNWQPEAIFLTHHHHDHVGGVKELVEKFPqIVVYGPQET------- 80
Cdd:pfam00753   7 NSYLIEGG-GGAVLIDTGgsaeaALLLLLAALGLGPKDIDAVILTHGHFDHIGGLGELAEATD-VPVIVVAEEarellde 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128199    81 ------------------QDKGTTQVVKDGETAFVLGHEFSVIATPGHTLGHICYFSKPYLFCGDTLFSGGCGR------ 136
Cdd:pfam00753  85 elglaasrlglpgppvvpLPPDVVLEEGDGILGGGLGLLVTHGPGHGPGHVVVYYGGGKVLFTGDLLFAGEIGRldlplg 164

                         170       180       190
                  ....*....|....*....|....*....|...
gi 16128199   137 ----LFEGTASQMYQSLKKLsALPDDTLVCCAH 165
Cdd:pfam00753 165 gllvLHPSSAESSLESLLKL-AKLKAAVIVPGH 196
MBLAC2-like_MBL-fold cd07712
uncharacterized human metallo-beta-lactamase domain-containing protein 2 and related proteins; ...
 79-165 3.22e-10

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: 57.64  E-value: 3.22e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128199  79 ETQDKGTTQVVKDGETaFVLG-HEFSVIATPGHTLGHICYFSKP--YLFCGDTLFSGGCGRLFEGT-ASQMYQSLKKLSA 154
Cdd:cd07712  92 SVPPAGPTLPLRDGDV-IDLGdRQLEVIHTPGHTPGSIALLDRAnrLLFSGDVVYDGPLIMDLPHSdLDDYLASLEKLSK 170

                        90
                ....*....|..
gi 16128199 155 LPDD-TLVCCAH 165
Cdd:cd07712 171 LPDEfDKVLPGH 182
LACTB2-like_MBL-fold cd07722
uncharacterized subgroup which includes human lactamase beta 2 and related proteins; MBL-fold ...
 48-165 1.09e-09

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: 56.39  E-value: 1.09e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128199  48 AIFLTHHHHDHVGGVKELVEKF--PQIVVY-------GPQETQDKGTTQVVKDGETAFVLGHEFSVIATPGHTLGHICYf 118
Cdd:cd07722  59 DILLTHWHHDHVGGLPDVLDLLrgPSPRVYkfprpeeDEDPDEDGGDIHDLQDGQVFKVEGATLRVIHTPGHTTDHVCF- 137

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|...
gi 16128199 119 skpYLFCGDTLFSGGCgRLFEGTA------SQMyQSLKKLSALPDDTLvCCAH 165
Cdd:cd07722 138 ---LLEEENALFTGDC-VLGHGTAvfedlaAYM-ASLKKLLSLGPGRI-YPGH 184
PLN02962 PLN02962
hydroxyacylglutathione hydrolase
 104-167 1.66e-09

hydroxyacylglutathione hydrolase


Pssm-ID: 178547 [Multi-domain]  Cd Length: 251  Bit Score: 56.73  E-value: 1.66e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16128199  104 VIATPGHTLGHICYFS-----KPY---LFCGDTLFSGGCGRL-FE-GTASQMYQSL-KKLSALPDDTLVCCAHEY 167
Cdd:PLN02962 119 VRATPGHTAGCVTYVTgegpdQPQprmAFTGDALLIRGCGRTdFQgGSSDQLYKSVhSQIFTLPKDTLIYPAHDY 193
ST1585-like_MBL-fold cd07726
uncharacterized subgroup which includes Sulfolobus tokodaii ST1585 protein; MBL-fold metallo ...
 15-165 2.40e-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: 55.58  E-value: 2.40e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128199  15 WVLNDEaGRCLIVDPG---DAEPVLNAIAANNWQPE---AIFLTHhhhdhV-----GGVKELVEKFPQIVVY-------- 75
Cdd:cd07726  19 YLLDGE-GRPALIDTGpssSVPRLLAALEALGIAPEdvdYIILTH-----IhldhaGGAGLLAEALPNAKVYvhprgarh 92

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128199  76 -----------------------GPQETQDKGTTQVVKDGETAFVLGHEFSVIATPGHTLGHICYFSKP--YLFCGDT-- 128
Cdd:cd07726  93 lidpsklwasaravygdeadrlgGEILPVPEERVIVLEDGETLDLGGRTLEVIDTPGHAPHHLSFLDEEsdGLFTGDAag 172

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 16128199 129 LFSGGCGRLFEGTAS-------QMYQSLKKLSALPDDTLvCCAH 165
Cdd:cd07726 173 VRYPELDVVGPPSTPppdfdpeAWLESLDRLLSLKPERI-YLTH 215
metallo-hydrolase-like_MBL-fold cd07743
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 14-131 1.43e-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: 47.53  E-value: 1.43e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128199  14 IWVLNDeaGRCLIVDPGDAEPVLNAIA----ANNWQPEAIFLTHHHHDHVGGVKELVEKfPQIVVY-------------- 75
Cdd:cd07743  12 VYVFGD--KEALLIDSGLDEDAGRKIRkileELGWKLKAIINTHSHADHIGGNAYLQKK-TGCKVYapkiekafienpll 88

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16128199  76 ---------GPQETQDKG-------TTQVVKDGETAFvLGHEFSVIATPGHTLGHICYFSKP-YLFCGDTLFS 131
Cdd:cd07743  89 epsylggayPPKELRNKFlmakpskVDDIIEEGELEL-GGVGLEIIPLPGHSFGQIGILTPDgVLFAGDALFG 160
YmaE-like_MBL-fold cd07727
uncharacterized subgroup which includes Bacillus subtilis YmaE and related proteins; MBL-fold ...
 91-130 8.08e-06

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


Pssm-ID: 293813 [Multi-domain]  Cd Length: 181  Bit Score: 44.88  E-value: 8.08e-06
                        10        20        30        40
                ....*....|....*....|....*....|....*....|..
gi 16128199  91 DGETAFVLGHEFSVIATPGHTLGHICYFSKP--YLFCGDTLF 130
Cdd:cd07727  93 WGGDPWELDPDLTLIPVPGHTRGSVVLLYKEkgVLFTGDHLA 134
metallo-hydrolase-like_MBL-fold cd16282
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 86-161 2.05e-03

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: 38.32  E-value: 2.05e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128199  86 TQVVKDGETAFVLGHEFSVIAT-PGHTLGHIC-YF--SKpYLFCGDTLFSGGCGRLFEGTASQMYQSLKKLSALPDDTLV 161
Cdd:cd16282 117 DRTFDDGLTLDLGGRTVELIHLgPAHTPGDLVvWLpeEG-VLFAGDLVFNGRIPFLPDGSLAGWIAALDRLLALDATVVV 195
metallo-hydrolase-like_MBL-fold cd16280
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 59-118 2.59e-03

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: 38.33  E-value: 2.59e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128199  59 VGGVKELVEKF-PQIV-------------------VYGPQETQDKgttqVVKDGETaFVLG-HEFSVIATPGHTLGHICY 117
Cdd:cd16280  75 YGGAAYLKDLYgAKVVmseadwdmmeeppeegdnpRWGPPPERDI----VIKDGDT-LTLGdTTITVYLTPGHTPGTLSL 149


                .
gi 16128199 118 F 118
Cdd:cd16280 150 I 150
metallo-hydrolase-like_MBL-fold cd07730
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 104-166 3.45e-03

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


Pssm-ID: 293816 [Multi-domain]  Cd Length: 250  Bit Score: 37.63  E-value: 3.45e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128199 104 VIATPGHTLGHICYF-----SKPYLFCGDTlfsggC---GRLFEGTAS-------------QMYQSLKKLSAL--PDDTL 160
Cdd:cd07730 170 LVDLPGHAPGHLGLLarttsGTWVFLAGDA-----ChhrIGLLRPSPLlplpdlddgadreAARETLARLRELdaAPDVR 244


                ....*.
gi 16128199 161 VCCAHE 166
Cdd:cd07730 245 VVLAHD 250
metallo-hydrolase-like_MBL-fold cd16277
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 96-131 7.71e-03

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: 293835 [Multi-domain]  Cd Length: 222  Bit Score: 36.73  E-value: 7.71e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|
gi 16128199  96 FVLGHEFSVIATPGHTLGHICYF----SKPYLFCGDTLFS 131
Cdd:cd16277 141 HEILDGIRLEPTPGHTPGHVSVElesgGERALFTGDVMHH 180
 
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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