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Conserved domains on  [gi|2558033678|gb|WLF37895|]
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subclass B1 metallo-beta-lactamase NDM-5 (plasmid) [Klebsiella pneumoniae]

Protein Classification

NDM family subclass B1 metallo-beta-lactamase( domain architecture ID 10888856)

NDM (New Delhi metallo-beta-lactamase) family subclass B1 metallo-beta-lactamase hydrolyzes the beta-lactam ring of beta-lactam antibiotics such as penicillin, cephalosporin and carbapenem, resulting in antibiotic resistance

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
NDM_FIM-like_MBL-B1 cd16300
NDM-1, FIM-1 and related metallo-beta-lactamases, subclass B1; MBL-fold metallo-hydrolase ...
 49-267 2.11e-126

NDM-1, FIM-1 and related metallo-beta-lactamases, subclass B1; MBL-fold metallo-hydrolase domain; Includes the ISCR-mediated MBLs NDM-1 (NDM (New Delhi metallo-beta-lactamase) and FIM-1 (Florence imipenemase). 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 MBLs belongs to the B1 subclass. B1 enzymes are most active with two zinc ions bound in the active site, and have a broad-spectrum substrate profile.


:

Pssm-ID: 293858  Cd Length: 214  Bit Score: 357.98  E-value: 2.11e-126
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2558033678  49 LVFRQLAPNVWQHTSYLDMPGFGAVASNGLIVRDGGRVLLVDTAWTDDQTAQILNWIKQEINLPVALAVVTHAHQDKMGG 128
Cdd:cd16300     1 VVFRQLAPGVWMHTSYLDMPGFGAVPSNGLIVRDGDRVLLVDTAWTDDQTAQILNWAKQELNLPVRLAVVTHAHQDKMGG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2558033678 129 MDALHAAGIATYANALSNQLAPQEGLVAAQHSLTFAAngwvEPATAPNFgPLKVFYPGPGHTSDNITVGIDGTDIAFGGC 208
Cdd:cd16300    81 MDALHAAGIATYANALSNQLAPQEGLVPAQHSLTFAA----EPSTAPNF-PLKVFYPGPGHTRDNIVVGIDGTGIAFGGC 155

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2558033678 209 LIKDSKAKSLGNLGDADTEHYAASARAFGAAFPKASMIVMSHSAPDSRAAITHTARMAD 267
Cdd:cd16300   156 LIRPSKATSLGNLADADTEHWAASARAFGAAFPDASMIVPSHGAPDGRAAITHTARLAD 214
 
Name Accession Description Interval E-value
NDM_FIM-like_MBL-B1 cd16300
NDM-1, FIM-1 and related metallo-beta-lactamases, subclass B1; MBL-fold metallo-hydrolase ...
 49-267 2.11e-126

NDM-1, FIM-1 and related metallo-beta-lactamases, subclass B1; MBL-fold metallo-hydrolase domain; Includes the ISCR-mediated MBLs NDM-1 (NDM (New Delhi metallo-beta-lactamase) and FIM-1 (Florence imipenemase). 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 MBLs belongs to the B1 subclass. B1 enzymes are most active with two zinc ions bound in the active site, and have a broad-spectrum substrate profile.


Pssm-ID: 293858  Cd Length: 214  Bit Score: 357.98  E-value: 2.11e-126
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2558033678  49 LVFRQLAPNVWQHTSYLDMPGFGAVASNGLIVRDGGRVLLVDTAWTDDQTAQILNWIKQEINLPVALAVVTHAHQDKMGG 128
Cdd:cd16300     1 VVFRQLAPGVWMHTSYLDMPGFGAVPSNGLIVRDGDRVLLVDTAWTDDQTAQILNWAKQELNLPVRLAVVTHAHQDKMGG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2558033678 129 MDALHAAGIATYANALSNQLAPQEGLVAAQHSLTFAAngwvEPATAPNFgPLKVFYPGPGHTSDNITVGIDGTDIAFGGC 208
Cdd:cd16300    81 MDALHAAGIATYANALSNQLAPQEGLVPAQHSLTFAA----EPSTAPNF-PLKVFYPGPGHTRDNIVVGIDGTGIAFGGC 155

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2558033678 209 LIKDSKAKSLGNLGDADTEHYAASARAFGAAFPKASMIVMSHSAPDSRAAITHTARMAD 267
Cdd:cd16300   156 LIRPSKATSLGNLADADTEHWAASARAFGAAFPDASMIVPSHGAPDGRAAITHTARLAD 214
GloB COG0491
Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General ...
 58-210 2.68e-17

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: 78.19  E-value: 2.68e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2558033678  58 VWQHTSYLDMPGFGavaSNGLIVRDGGRVLLVDTAWTDDQTAQILNWIKqEINLPVALAVVTHAHQDKMGGMDALHAA-G 136
Cdd:COG0491     1 VYVLPGGTPGAGLG---VNSYLIVGGDGAVLIDTGLGPADAEALLAALA-ALGLDIKAVLLTHLHPDHVGGLAALAEAfG 76

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2558033678 137 IATYANALSNQLAPQEGLVAAQHSLTFAANGWVEPATAPNFGPLKV-FYPGPGHTSDNITVGIDGTDIAFGGCLI 210
Cdd:COG0491    77 APVYAHAAEAEALEAPAAGALFGREPVPPDRTLEDGDTLELGGPGLeVIHTPGHTPGHVSFYVPDEKVLFTGDAL 151
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 76-250 2.09e-13

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: 66.81  E-value: 2.09e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2558033678   76 NGLIVRDGGRVLLVDTAWTDDQtaQILNWIKQEINLPVALAVVTHAHQDKMGGMDALHAA-GIATYANALSNQLAPQEGL 154
Cdd:smart00849   1 NSYLVRDDGGAILIDTGPGEAE--DLLAELKKLGPKKIDAIILTHGHPDHIGGLPELLEApGAPVYAPEGTAELLKDLLA 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2558033678  155 VAAQHSLTFAANG---WVEPATAPNFGPLKV-FYPGPGHTSDNITVGIDGTDIAFGGCLIKDSKAKSLGNLGDaDTEHYA 230
Cdd:smart00849  79 LLGELGAEAEPAPpdrTLKDGDELDLGGGELeVIHTPGHTPGSIVLYLPEGKILFTGDLLFAGGDGRTLVDGG-DAAASD 157

                          170       180
                   ....*....|....*....|
gi 2558033678  231 ASARAFGAAFPKASMIVMSH 250
Cdd:smart00849 158 ALESLLKLLKLLPKLVVPGH 177
Lactamase_B pfam00753
Metallo-beta-lactamase superfamily;
71-210 2.23e-10

Metallo-beta-lactamase superfamily;


Pssm-ID: 425851 [Multi-domain]  Cd Length: 196  Bit Score: 58.53  E-value: 2.23e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2558033678  71 GAVASNGLIVRDGGRVLLVDTAWTDDQTAQILNWIKQEINLPVALAVVTHAHQDKMGGMDAL-HAAGIATYANAL-SNQL 148
Cdd:pfam00753   2 GPGQVNSYLIEGGGGAVLIDTGGSAEAALLLLLAALGLGPKDIDAVILTHGHFDHIGGLGELaEATDVPVIVVAEeAREL 81

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2558033678 149 APQEGLVAAQHSLTFAANGWVEP--------ATAPNFGPLKVFYPGPGHTSDNITVGIDGTDIAFGGCLI 210
Cdd:pfam00753  82 LDEELGLAASRLGLPGPPVVPLPpdvvleegDGILGGGLGLLVTHGPGHGPGHVVVYYGGGKVLFTGDLL 151
 
Name Accession Description Interval E-value
NDM_FIM-like_MBL-B1 cd16300
NDM-1, FIM-1 and related metallo-beta-lactamases, subclass B1; MBL-fold metallo-hydrolase ...
 49-267 2.11e-126

NDM-1, FIM-1 and related metallo-beta-lactamases, subclass B1; MBL-fold metallo-hydrolase domain; Includes the ISCR-mediated MBLs NDM-1 (NDM (New Delhi metallo-beta-lactamase) and FIM-1 (Florence imipenemase). 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 MBLs belongs to the B1 subclass. B1 enzymes are most active with two zinc ions bound in the active site, and have a broad-spectrum substrate profile.


Pssm-ID: 293858  Cd Length: 214  Bit Score: 357.98  E-value: 2.11e-126
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2558033678  49 LVFRQLAPNVWQHTSYLDMPGFGAVASNGLIVRDGGRVLLVDTAWTDDQTAQILNWIKQEINLPVALAVVTHAHQDKMGG 128
Cdd:cd16300     1 VVFRQLAPGVWMHTSYLDMPGFGAVPSNGLIVRDGDRVLLVDTAWTDDQTAQILNWAKQELNLPVRLAVVTHAHQDKMGG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2558033678 129 MDALHAAGIATYANALSNQLAPQEGLVAAQHSLTFAAngwvEPATAPNFgPLKVFYPGPGHTSDNITVGIDGTDIAFGGC 208
Cdd:cd16300    81 MDALHAAGIATYANALSNQLAPQEGLVPAQHSLTFAA----EPSTAPNF-PLKVFYPGPGHTRDNIVVGIDGTGIAFGGC 155

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2558033678 209 LIKDSKAKSLGNLGDADTEHYAASARAFGAAFPKASMIVMSHSAPDSRAAITHTARMAD 267
Cdd:cd16300   156 LIRPSKATSLGNLADADTEHWAASARAFGAAFPDASMIVPSHGAPDGRAAITHTARLAD 214
MBL-B1 cd16285
metallo-beta-lactamases, subclass B1; MBL-fold metallo-hydrolase domain; MBLs (class B of the ...
 49-267 4.03e-100

metallo-beta-lactamases, subclass B1; 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 B1 enzymes are most active with two zinc ions bound in the active site, and have a broad-spectrum substrate profile. Includes chromosomally-encoded MBLs such as Bacillus cereus BcII, Bacteroides fragilis CcrA, and Elizabethkingia meningoseptica (Chryseobacterium meningosepticum) BlaB and acquired MBLs including IMP-1, VIM-1, VIM-2, GIM-1, NDM-1 and FIM-1.


Pssm-ID: 293843 [Multi-domain]  Cd Length: 210  Bit Score: 291.11  E-value: 4.03e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2558033678  49 LVFRQLAPNVWQHTSYLDMPGfGAVASNGLIVRDGGRVLLVDTAWTDDQTAQILNWIKQEINLPVALAVVTHAHQDKMGG 128
Cdd:cd16285     1 LRIRPLADNVWVHTSLAEFNG-GAVPSNGLIVIDGKGLVLIDTPWTEAQTATLLDWIEKKLGKPVTAAISTHSHDDRTGG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2558033678 129 MDALHAAGIATYANALSNQLAPQEGLVAAQHSLTFaangwvepATAPNFGPLKVFYPGPGHTSDNITVGIDGTDIAFGGC 208
Cdd:cd16285    80 IKALNARGIPTYATALTNELAKKEGKPVPTHSLKG--------ALTLGFGPLEVFYPGPGHTPDNIVVWLPKSKILFGGC 151

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2558033678 209 LIKDSKAKSLGNLGDADTEHYAASARAFGAAFPKASMIVMSHSAPDSRAAITHTARMAD 267
Cdd:cd16285   152 LVKSASATSLGNVGDADVEAWPKSIENLKAKYPEARMVVPGHGAPGGTELLDHTLDLAK 210
BcII-like_MBL-B1 cd16304
Bacillus cereus Beta-lactamase 2 and related metallo-beta-lactamases, subclass B1; MBL-fold ...
 49-262 4.22e-65

Bacillus cereus Beta-lactamase 2 and related metallo-beta-lactamases, subclass B1; MBL-fold metallo-hydrolase domain; Bacillus cereus Beta-lactamase 2, also called BcII. MBLs (class B of the Ambler beta-lactamase classification) 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. BcII is a chromosome-encoded B1 MBL. B1 enzymes are most active with two zinc ions bound in the active site, and have a broad-spectrum substrate profile.


Pssm-ID: 293862 [Multi-domain]  Cd Length: 212  Bit Score: 202.13  E-value: 4.22e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2558033678  49 LVFRQLAPNVWQHTSYLDMPGfGAVASNGLIVRDGGRVLLVDTAWTDDQTAQILNWIKQEINLPVALAVVTHAHQDKMGG 128
Cdd:cd16304     1 LEVTKLNKNVWVHTSYGLFNG-TPVPSNGLIVETSKGVVLIDTPWDDEQTEELLDWIKKKLKKPVTLAIVTHAHDDRIGG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2558033678 129 MDALHAAGIATYANALSNQLAPQEGLVAAQHSLtfaangwvEPATAPNFG--PLKVFYPGPGHTSDNITVGIDGTDIAFG 206
Cdd:cd16304    80 IKALQKRGIPVYSTKLTAQLAKKQGYPSPDGIL--------KDDTTLKFGntKIETFYPGEGHTADNIVVWLPQSKILFG 151

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2558033678 207 GCLIKDSKAKSLGNLGDADTEHYAASARAFGAAFPKASMIVMSHSAPDSRAAITHT 262
Cdd:cd16304   152 GCLVKSLEAKDLGNTADANLKEWPTSIRNVLKRYPNAEIVVPGHGEWGDKQLLRHT 207
VIM_type_MBL-B1 cd16303
VIM-type metallo-beta-lactamases, subclass B1; MBL-fold metallo-hydrolase domain; VIM (Verona ...
 47-253 2.68e-61

VIM-type metallo-beta-lactamases, subclass B1; MBL-fold metallo-hydrolase domain; VIM (Verona integron-encoded metallo-beta-lactamase)-type MBLs are integron-associated and are widely distributed acquired MBLs. MBLs (class B of the Ambler beta-lactamase classification) 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 VIM-type MBLs belongs to the B1 subclass. B1 enzymes are most active with two zinc ions bound in the active site, and have a broad-spectrum substrate profile.


Pssm-ID: 293861 [Multi-domain]  Cd Length: 218  Bit Score: 192.77  E-value: 2.68e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2558033678  47 GDLVFRQLAPNVWQHTSYLDMPGfGAVASNGLIVRDGGRVLLVDTAWTDDQTAQILNWIKQEINLPVALAVVTHAHQDKM 126
Cdd:cd16303     1 GEVRLYQIADGVWSHIATQSFDG-AVYPSNGLIVRDGDELLLIDTAWGAKNTAALLAEIEKQIGLPVTRAVSTHFHDDRV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2558033678 127 GGMDALHAAGIATYANALSNQLAPQEGLVAAQHSLTfaanGWVEPATAPNFGPLKVFYPGPGHTSDNITVGIDGTDIAFG 206
Cdd:cd16303    80 GGVDVLRAAGVATYASPSTRRLAEAEGNEIPTHSLE----GLSSSGDAVRFGPVELFYPGAAHSTDNLVVYVPSARVLYG 155

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 2558033678 207 GCLIKDSKAKSLGNLGDADTEHYAASARAFGAAFPKASMIVMSHSAP 253
Cdd:cd16303   156 GCAVRELSSTSAGNVADADLAEWPTSIERIQKHYPEAEFVIPGHGLP 202
IMP_DIM-like_MBL-B1 cd16301
IMP-1, DIM-1, GIM-1, SIM-1, TMB-1 and related metallo-beta-lactamases, subclass B1; MBL-fold ...
 48-268 3.36e-61

IMP-1, DIM-1, GIM-1, SIM-1, TMB-1 and related metallo-beta-lactamases, subclass B1; MBL-fold metallo-hydrolase domain; Includes the acquired MBLs IMP-1(a beta-lactamase that is active on imipenem), DIM-1 (Dutch imipenemase), GIM-1 (German imipenemase), KHM-1 (Kyorin Health Science MBL 1), SIM-1 (Seoul imipenemase), and TMB-1 (Tripoli metallo-beta-lactamase). IMP-1, DIM-1, GIM-1, SIM-1, and TMB-1 are Class 1 integron-mediated MBLs, KMH-1 is plasmid-mediated. 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 acquired MBLs belongs to the B1 subclass. B1 enzymes are most active with two zinc ions bound in the active site, and have a broad-spectrum substrate profile.


Pssm-ID: 293859 [Multi-domain]  Cd Length: 215  Bit Score: 192.50  E-value: 3.36e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2558033678  48 DLVFRQLAPNVWQHTSYLDMPGFGAVASNGLIVRDGGRVLLVDTAWTDDQTAQILNWIKQEiNLPVALAVVTHAHQDKMG 127
Cdd:cd16301     2 KLKIEKLSDGVYLHTSYKEVEGWGLVDANGLVVVDGKEAYLIDTPWSESDTEKLVEWIKAQ-GLTLKASISTHFHEDRTG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2558033678 128 GMDALHAAGIATYANALSNQLAPQEGLVAAQHSLTFA----ANGWVEpatapnfgplkVFYPGPGHTSDNITVGIDGTDI 203
Cdd:cd16301    81 GIGYLNSHSIPTYASELTNQLLKKNGKELATHSFSGDefwlLKGKIE-----------VFYPGAGHTKDNLVVWLPKEKI 149

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2558033678 204 AFGGCLIKDSKAKSLGNLGDADTEHYAASARAFGAAFPKASMIVMSHSAPDSRAAITHTARMADK 268
Cdd:cd16301   150 LFGGCLVKSLESKGLGNTGDASISQWPASAQKVLSKYPNAKLVVPGHGKVGDVSLLEHTRKLAKK 214
CcrA-like_MBL-B1 cd16302
Bacteroides fragilis CcrA and related metallo-beta-lactamases, subclass B1; MBL-fold ...
 49-265 1.46e-60

Bacteroides fragilis CcrA and related metallo-beta-lactamases, subclass B1; 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 MBLs belongs to the B1 subclass. B1 enzymes are most active with two zinc ions bound in the active site, and have a broad-spectrum substrate profile.


Pssm-ID: 293860  Cd Length: 212  Bit Score: 190.53  E-value: 1.46e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2558033678  49 LVFRQLAPNVWQHTSYLDMPGFGAVASNGLIVRDGGRVLLVDTAWTDDQTAQILNWIKQEINLPVALAVVTHAHQDKMGG 128
Cdd:cd16302     1 LEIIKLSDHVYVHVSYLETETFGKVPCNGMIVINGGEAVVFDTPTNDSQSEELIDWIENSLKAKVKAVVPTHFHDDCLGG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2558033678 129 MDALHAAGIATYANALSNQLAPQEGLVAAQH----SLTFAANGwvepatapnfGPLKVFYPGPGHTSDNITVGIDGTDIA 204
Cdd:cd16302    81 LKAFHRRGIPSYANQKTIALAKEKGLPVPQHgfsdSLTLKLGG----------KKIVCRYFGEGHTKDNIVVYFPSEKVL 150

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2558033678 205 FGGCLIKDSKAkSLGNLGDADTEHYAASARAFGAAFPKASMIVMSHSAPDSRAAITHTARM 265
Cdd:cd16302   151 FGGCMVKSLGA-GKGNLEDANVEAWPKTVEKVKAKYPDVKIVIPGHGKIGGSELLDYTIDL 210
MBL-B1-B2-like cd07707
metallo-beta-lactamases; subclasses B1 and B2 and related proteins; MBL-fold metallo-hydrolase ...
 53-262 6.28e-44

metallo-beta-lactamases; subclasses B1 and B2 and related proteins; 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 B1 enzymes are most active with two zinc ions bound in the active site, and have a broad-spectrum substrate profile. B1 MBls include chromosomally-encoded MBLs such as Bacillus cereus BcII, Bacteroides fragilis CcrA, and Elizabethkingia meningoseptica (Chryseobacterium meningosepticum) BlaB and acquired MBLs including IMP-1, VIM-1, VIM-2, GIM-1, NDM-1 and FIM-1. B2 MBLs have a narrow substrate profile that includes carbapenems, and they are active with one zinc ion bound in the Asp-Cys-His site, binding of a second zinc ion in the modified 3H site (Asn-His-His) inhibits catalysis. B2 MBLs include Aeromonas hydrophyla CphA, Aeromonas veronii ImiS, and Serratia fonticola Sfh-I.


Pssm-ID: 293793 [Multi-domain]  Cd Length: 219  Bit Score: 148.46  E-value: 6.28e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2558033678  53 QLAPNVWQHTSYldmpgfGAVASNGLIVRDGGRVLLVDTAWTDDQTAQILNWIKQEINLPVALAVVTHAHQDKMGGMDAL 132
Cdd:cd07707     5 QINGPVWVVTDL------GSVPSNGLVYNGSKGLVLVDSTWTPKTTKELIKEIEKVSQKPVTEVINTHFHTDRAGGNAYL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2558033678 133 HAAGIATYANALSNQLAPQEG----LVAAQHSLTFAANGWVEP------ATAPNFGPLKVFYPGPGHTSDNITVGIDGTD 202
Cdd:cd07707    79 KERGAKTVSTALTRDLAKSEWaeivAFTRKGLPEYPDLGYELPdgvldgDFNLQFGKVEAFYPGPAHTPDNIVVYFPQEN 158

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2558033678 203 IAFGGCLIKDskaKSLGNLGDADTEHYAASARAFGAAFPKASMIVMSHSAPDSRAAITHT 262
Cdd:cd07707   159 VLYGGCIIKE---TDLGNVADADVKEWPTSIERLKKRYRNIKAVIPGHGEVGGPELLDHT 215
MUS_TUS_MBL-B1 cd16318
Myroides odoratimimus MUS-1, MUS-2, TUS-1 and related metallo-beta-lactamases, subclass B1; ...
 49-265 1.53e-34

Myroides odoratimimus MUS-1, MUS-2, TUS-1 and related metallo-beta-lactamases, subclass B1; MBL-fold metallo-hydrolase domain; Includes the chromosome-encoded MBLs Myroides odoratimimus MUS-1 and related MBLs. 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 MBLs belongs to the B1 subclass. B1 enzymes are most active with two zinc ions bound in the active site, and have a broad-spectrum substrate profile.


Pssm-ID: 293876  Cd Length: 214  Bit Score: 124.00  E-value: 1.53e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2558033678  49 LVFRQLAPNVWQHTSYLDMPGFgAVASNGLIVRDGGRVLLVDTAWTDDQTAQILNWIKQEINLPVALAVVTHAHQDKMGG 128
Cdd:cd16318     1 LKIKQLNDNMYIYTTYQEFQGV-TYSSNSMYVLTDEGVILIDTPWDKDQYEPLLEYIRSNHNKEVKWVITTHFHEDRSGG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2558033678 129 MDALHAAGIATYANALSNQLAPQEGLVAAQHSLTfaangwvePATAPNFG--PLKVFYPGPGHTSDNITVGIDGTDIAFG 206
Cdd:cd16318    80 LGYFNSIGAQTYTYALTNEILKERNEPQAQFSFN--------KEKQFTFGneKLAVYFLGEGHSLDNTVVWFPKEEVLYG 151

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2558033678 207 GCLIKDSKAKSLGNLGDADTEHYAASARAFGAAFPKASMIVMSHSAPDSRAAITHTARM 265
Cdd:cd16318   152 GCLIKSAEATTIGNIADGNVIAWPKTIEAVKQKFKNAKVIIPGHDEWDMSGHIENTERI 210
IND_BlaB-like_MBL-B1 cd16299
IND1, IND2, BlaB-1 and related metallo-beta-lactamases, subclass B1; MBL-fold ...
 49-265 3.90e-34

IND1, IND2, BlaB-1 and related metallo-beta-lactamases, subclass B1; MBL-fold metallo-hydrolase domain; Includes the chromosome-encoded metallo-beta-lactamases Chryseobacterium indologenes IND-1, IND-2, and IND-7, Elizabethkingia meningoseptica (Chryseobacterium meningosepticum) BlaB, Chryseobacterium gleum CGB-1, and Empedobacter brevis EBR-1. 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 MBLs belongs to the B1 subclass. B1 enzymes are most active with two zinc ions bound in the active site, and have a broad-spectrum substrate profile.


Pssm-ID: 293857  Cd Length: 212  Bit Score: 122.55  E-value: 3.90e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2558033678  49 LVFRQLAPNVWQHTSYLDMPGFGAVASNGLIVRDGGrVLLVDTAWTDDQTAQILNWIKQEINLPVALAVVTHAHQDKMGG 128
Cdd:cd16299     1 LKIEKLNDNLYIYTTYNEFNGVKYSANAMYLVTKKG-VILFDTPWDKDQYQPLLDSIRKKHNLPVIAVIATHSHEDRAGG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2558033678 129 MDALHAAGIATYANALSNQLAPQEGLVAAQHSltfaangwVEPATAPNFG--PLKVFYPGPGHTSDNITVGIDGTDIAFG 206
Cdd:cd16299    80 LGYFNKIGIPTYATAMTNSILKKENKPQATYL--------IETDKTYKIGgeKFVVYFFGEGHTADNVVVWFPKEKVLDG 151

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2558033678 207 GCLIKDSKAKSLGNLGDADTEHYAASARAFGAAFPKASMIVMSHSAPDSRAAITHTARM 265
Cdd:cd16299   152 GCLIKSAEATDLGYIGEANVKEWPKTIHKLKQKFKKAKVVIPGHDEWKDQGHIENTLKL 210
BlaB-like_MBL-B1 cd16316
Elizabethkingia meningoseptica (Chryseobacterium meningosepticum) BlaB and related ...
 53-269 1.00e-33

Elizabethkingia meningoseptica (Chryseobacterium meningosepticum) BlaB and related metallo-beta-lactamases, subclass B1; MBL-fold metallo-hydrolase domain; Includes the chromosome-encoded MBL Elizabethkingia meningoseptica (Chryseobacterium meningosepticum) BlaB and related MBLs. 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 MBLs belongs to the B1 subclass. B1 enzymes are most active with two zinc ions bound in the active site, and have a broad-spectrum substrate profile.


Pssm-ID: 293874  Cd Length: 214  Bit Score: 121.80  E-value: 1.00e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2558033678  53 QLAPNVWQHTSYLDMPGFGAVASNGLIVRDGGrVLLVDTAWTDDQTAQILNWIKQEINLPVALAVVTHAHQDKMGGMDAL 132
Cdd:cd16316     5 HLTGDLYVYTTYNTYKGTKTAANAVYVVTDKG-VVVIDAPWDETQFQPFLDSIQKKHHKKVIMNIATHSHDDRAGGLEYF 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2558033678 133 HAAGIATYANALSNQLAPQEGLVAAQHSLTFAANGWVEPATapnfgpLKVFYPGPGHTSDNITVGIDGTDIAFGGCLIKD 212
Cdd:cd16316    84 GKKGAKTYTTKLTDSILKKNNKPRAEYTFDNDTTFKVGKYE------FQVYYPGKGHTADNIVVWFPKEKVLYGGCLIKS 157

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2558033678 213 SKAKSLGNLGDADTEHYAASARAFGAAFPKASMIVMSHSAPDSRAAITHTARMADKL 269
Cdd:cd16316   158 ADAKDLGYLGEAYVNDWTQSIHNIQQKFPNPQYVIAGHDDWKDQTSLQHTLKLISEY 214
IND_MBL-B1 cd16317
Chryseobacterium indologenes IND-1, IND-2, IND-7and related metallo-beta-lactamases, subclass ...
 53-268 1.99e-22

Chryseobacterium indologenes IND-1, IND-2, IND-7and related metallo-beta-lactamases, subclass B1; MBL-fold metallo-hydrolase domain; Includes the chromosome-encoded MBLs Chryseobacterium indologenes IND-1, IND-2, and IND-7 and related MBLs. 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 MBLs belongs to the B1 subclass. B1 enzymes are most active with two zinc ions bound in the active site, and have a broad-spectrum substrate profile.


Pssm-ID: 293875  Cd Length: 215  Bit Score: 92.00  E-value: 1.99e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2558033678  53 QLAPNVWQHTSYlDMPGFGAVASNGLIVRDGGRVLLVDTAWTDDQTAQILNWIKQEINLPVALAVVTHAHQDKMGGMDAL 132
Cdd:cd16317     7 PIKPNLYIYKTF-GVFGGKEYSANAVYLVTKKGVVLFDVPWQKVQYQSLMDTIQKRHHLPVIAVFATHSHDDRAGDLSFY 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2558033678 133 HAAGIATYANALSNQLAPQEGLVAaqhSLTFAANGWVEPATAPNFgplKVFYPGPGHTSDNITVGIDGTDIAFGGCLIKD 212
Cdd:cd16317    86 NNKGIKTYATAKTNEFLKKDGKAT---STEIIKTGKPYRIGGEEF---VVDFLGEGHTADNVVVWFPKYKVLDGGCLVKS 159

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2558033678 213 SKAKSLGNLGDADTEHYAASARAFGAAFPKASMIVMSHSAPDSRAAITHTARMADK 268
Cdd:cd16317   160 NSATDLGYTGEANVEQWPKTMNKLKAKYAQATLIIPGHDEWKGGGHVEHTLDLLNK 215
SPM-1-like_MBL-B1-B2-like cd16286
Pseudomonas areoginosa SPM-1 and related metallo-beta-lactamases, subclasses B1 and B2 like; ...
 48-225 1.89e-21

Pseudomonas areoginosa SPM-1 and related metallo-beta-lactamases, subclasses B1 and B2 like; MBL-fold metallo-hydrolase domain; SPM-1 was first identified in a Pseudomonas aeruginosa strain from a paediatric leukaemia patient and is a major clinical problem. MBLs (class B of the Ambler beta-lactamase classification) have been divided into three subclasses B1, B2 and B3, based on sequence/structural relationships and substrates, with the B1 and B2 MBLs are most closely related to each other. SPM-1 appears to be a hybrid B1/B2 MBL.


Pssm-ID: 293844 [Multi-domain]  Cd Length: 236  Bit Score: 89.90  E-value: 1.89e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2558033678  48 DLVFRQLAPNVWQHTSYLDMpgfgavASNGLIVRDG-GRVLLVDTAWTDDQTAQILNWIKQEINLPVALAVVTHAHQDKM 126
Cdd:cd16286     6 NLTAREIDPDVFVITHRDPW------SSNVLVVKMLdGTVVIVDSPYTNLATQTVLDWIAKTMGPRKVVAINTHFHLDGT 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2558033678 127 GGMDALHAAGIATYANALSNQLAPQEGLVAAQHSLTFAANGWV------EPATAPN------------FG--PLKVFYPG 186
Cdd:cd16286    80 GGNEALKKRGIPTWGSDLTKQLLLERGKADRIKAAEFLKNEDLkrriesSPPVPPDnvfdlkegkvfsFGneLVEVSFPG 159

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 2558033678 187 PGHTSDNITVGIDGTDIAFGGCLIKdsKAKSLGNLGDAD 225
Cdd:cd16286   160 PAHAPDNVVVYFPERKILFGGCMIK--PGKELGNLGDAN 196
GloB COG0491
Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General ...
 58-210 2.68e-17

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: 78.19  E-value: 2.68e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2558033678  58 VWQHTSYLDMPGFGavaSNGLIVRDGGRVLLVDTAWTDDQTAQILNWIKqEINLPVALAVVTHAHQDKMGGMDALHAA-G 136
Cdd:COG0491     1 VYVLPGGTPGAGLG---VNSYLIVGGDGAVLIDTGLGPADAEALLAALA-ALGLDIKAVLLTHLHPDHVGGLAALAEAfG 76

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2558033678 137 IATYANALSNQLAPQEGLVAAQHSLTFAANGWVEPATAPNFGPLKV-FYPGPGHTSDNITVGIDGTDIAFGGCLI 210
Cdd:COG0491    77 APVYAHAAEAEALEAPAAGALFGREPVPPDRTLEDGDTLELGGPGLeVIHTPGHTPGHVSFYVPDEKVLFTGDAL 151
metallo-hydrolase-like_MBL-fold cd16282
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 68-207 7.39e-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: 293840 [Multi-domain]  Cd Length: 209  Bit Score: 68.75  E-value: 7.39e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2558033678  68 PGFGAVASNGLIVRDGGrVLLVDTAWTDDQTAQILNWIKQEINLPVALAVVTHAHQDKMGGMDALHAAGIATYA--NALS 145
Cdd:cd16282     9 DGGGFISNIGFIVGDDG-VVVIDTGASPRLARALLAAIRKVTDKPVRYVVNTHYHGDHTLGNAAFADAGAPIIAheNTRE 87

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2558033678 146 NQLAPQEGLVAAQHSLTFAANGWVEPaTAPN----------FG--PLKVFYPGPGHTSDNITVGIDGTDIAFGG 207
Cdd:cd16282    88 ELAARGEAYLELMRRLGGDAMAGTEL-VLPDrtfddgltldLGgrTVELIHLGPAHTPGDLVVWLPEEGVLFAG 160
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 76-250 2.09e-13

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: 66.81  E-value: 2.09e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2558033678   76 NGLIVRDGGRVLLVDTAWTDDQtaQILNWIKQEINLPVALAVVTHAHQDKMGGMDALHAA-GIATYANALSNQLAPQEGL 154
Cdd:smart00849   1 NSYLVRDDGGAILIDTGPGEAE--DLLAELKKLGPKKIDAIILTHGHPDHIGGLPELLEApGAPVYAPEGTAELLKDLLA 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2558033678  155 VAAQHSLTFAANG---WVEPATAPNFGPLKV-FYPGPGHTSDNITVGIDGTDIAFGGCLIKDSKAKSLGNLGDaDTEHYA 230
Cdd:smart00849  79 LLGELGAEAEPAPpdrTLKDGDELDLGGGELeVIHTPGHTPGSIVLYLPEGKILFTGDLLFAGGDGRTLVDGG-DAAASD 157

                          170       180
                   ....*....|....*....|
gi 2558033678  231 ASARAFGAAFPKASMIVMSH 250
Cdd:smart00849 158 ALESLLKLLKLLPKLVVPGH 177
Lactamase_B pfam00753
Metallo-beta-lactamase superfamily;
71-210 2.23e-10

Metallo-beta-lactamase superfamily;


Pssm-ID: 425851 [Multi-domain]  Cd Length: 196  Bit Score: 58.53  E-value: 2.23e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2558033678  71 GAVASNGLIVRDGGRVLLVDTAWTDDQTAQILNWIKQEINLPVALAVVTHAHQDKMGGMDAL-HAAGIATYANAL-SNQL 148
Cdd:pfam00753   2 GPGQVNSYLIEGGGGAVLIDTGGSAEAALLLLLAALGLGPKDIDAVILTHGHFDHIGGLGELaEATDVPVIVVAEeAREL 81

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2558033678 149 APQEGLVAAQHSLTFAANGWVEP--------ATAPNFGPLKVFYPGPGHTSDNITVGIDGTDIAFGGCLI 210
Cdd:pfam00753  82 LDEELGLAASRLGLPGPPVVPLPpdvvleegDGILGGGLGLLVTHGPGHGPGHVVVYYGGGKVLFTGDLL 151
CphS_ImiS-like_MBL-B2 cd16287
metallo-beta-lactamases, subclass B2; MBL-fold metallo-hydrolase domain; Includes Aeromonas ...
 73-229 4.24e-10

metallo-beta-lactamases, subclass B2; MBL-fold metallo-hydrolase domain; Includes Aeromonas hydrophyla CphA, Aeromonas veronii ImiS, and Serratia fonticola Sfh-I. 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. B2 MBLs have a narrow substrate profile relative to subclass B1 MBLs that includes carbapenems, and they are active with one zinc ion bound in the Asp-Cys-His site, binding of a second zinc ion in the modified 3H site (Asn-His-His) inhibits catalysis.


Pssm-ID: 293845  Cd Length: 226  Bit Score: 58.21  E-value: 4.24e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2558033678  73 VASNGLIVRDGGRVLLVDTAWTDDQTAQILNWIKQEINLPVALAVVTHAHQDKMGGMDALHAAGIATYANALSNQLAPQE 152
Cdd:cd16287    19 VQENSMVYIGTDGITIIGATWTPETAETLYKEIRKVSPLPINEVINTNYHTDRAGGNAYWKTLGAKIVATQMTYDLQKSQ 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2558033678 153 GlvaaQHSLTFAANGWVE----PATAPNF----------GPLKVFYPGPGHTSDNITVGIDGTDIAFGGCLIKDskakSL 218
Cdd:cd16287    99 W----GSIVNFTRQGNNKypnlEKSLPDTvfpgdfnlqnGSIRAMYLGEAHTKDGIFVYFPAERVLYGNCILKE----NL 170

                         170
                  ....*....|.
gi 2558033678 219 GNLGDADTEHY 229
Cdd:cd16287   171 GNMSFANRTEY 181
CphA_ImiS-like_MBL-B2 cd16306
Aeromonas hydrophyla CphA, Aeromonas veronii ImiS, and related metallo-beta-lactamases, ...
 73-229 1.03e-09

Aeromonas hydrophyla CphA, Aeromonas veronii ImiS, and related metallo-beta-lactamases, subclass B2; 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. B2 MBLs have a narrow substrate profile relative to subclass B1 MBLs that includes carbapenems, and they are active with one zinc ion bound in the Asp-Cys-His site, binding of a second zinc ion in the modified 3H site (Asn-His-His) inhibits catalysis.


Pssm-ID: 293864  Cd Length: 222  Bit Score: 57.27  E-value: 1.03e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2558033678  73 VASNGLIVRDGGRVLLVDTAWTDDQTAQILNWIKQEINLPVALAVVTHAHQDKMGGMDALHAAGiatyANALSNQLAPQE 152
Cdd:cd16306    19 VQENSMVYFGAKGVTVVGATWTPDTARELHKLIKRVSRKPVLEVINTNYHTDRAGGNAYWKSIG----AKVVSTRQTRDL 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2558033678 153 GLVAAQHSLTFAANGWVE----PATAPNF----------GPLKVFYPGPGHTSDNITVGIDGTDIAFGGCLIKdskaKSL 218
Cdd:cd16306    95 MKSDWAEIVAFTRKGLPEypdlPLVLPNVvhdgdftlqeGKVRAFYLGPAHTPDGIFVYFPDEQVLYGNCILK----EKL 170

                         170
                  ....*....|.
gi 2558033678 219 GNLGDADTEHY 229
Cdd:cd16306   171 GNLSFADVKAY 181
metallo-hydrolase-like_MBL-fold cd06262
mainly hydrolytic enzymes and related proteins which carry out various biological functions; ...
 69-210 9.82e-09

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: 53.83  E-value: 9.82e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2558033678  69 GFGAVASNGLIVRDG-GRVLLVDTAwtDDQTAQILNWIKqEINLPVALAVVTHAHQDKMGGMDALHAA-GIATYANALSN 146
Cdd:cd06262     4 PVGPLQTNCYLVSDEeGEAILIDPG--AGALEKILEAIE-ELGLKIKAILLTHGHFDHIGGLAELKEApGAPVYIHEADA 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2558033678 147 QLAPQEGLVAA----QHSLTFAANGWVEPATAPNFGPLKV-FYPGPGHTSDNITVGIDGTDIAFGGCLI 210
Cdd:cd06262    81 ELLEDPELNLAffggGPLPPPEPDILLEDGDTIELGGLELeVIHTPGHTPGSVCFYIEEEGVLFTGDTL 149
yflN-like_MBL-fold cd07721
uncharacterized subgroup which includes Bacillus subtilis yflN; MBL-fold metallo hydrolase ...
 79-191 9.65e-05

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: 42.21  E-value: 9.65e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2558033678  79 IVRDGGRVLLVDTAWTDdQTAQILNWIKqEINL---PVALAVVTHAHQDKMGGMDALHAA-GIATYANA-----LSNQLA 149
Cdd:cd07721    15 LIEDDDGLTLIDTGLPG-SAKRILKALR-ELGLspkDIRRILLTHGHIDHIGSLAALKEApGAPVYAHEreapyLEGEKP 92

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2558033678 150 PQEGLVAAQHSLTFaangWVEPATA-------------PNFGPLKVFY-PG--PGHTS 191
Cdd:cd07721    93 YPPPVRLGLLGLLS----PLLPVKPvpvdrtledgdtlDLAGGLRVIHtPGhtPGHIS 146
ComA-like_MBL-fold cd07731
Competence protein ComA, ComEC and related proteins; MBL-fold metallo hydrolase domain; This ...
 79-132 5.45e-04

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


Pssm-ID: 293817 [Multi-domain]  Cd Length: 179  Bit Score: 39.81  E-value: 5.45e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2558033678  79 IVRDGGRVLLVDTAWTDDQTAQ-ILNWIKQEINLPVALAVVTHAHQDKMGGMDAL 132
Cdd:cd07731    14 LIQTPGKTILIDTGPRDSFGEDvVVPYLKARGIKKLDYLILTHPDADHIGGLDAV 68
metallo-hydrolase-like_MBL-fold cd07743
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 77-145 5.92e-04

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: 39.82  E-value: 5.92e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2558033678  77 GLIVRDGGRVLLVDTAWTDDQTAQILNWIKqEINLPVALAVVTHAHQDKMGGMDALHAA-GIATYANALS 145
Cdd:cd07743    11 GVYVFGDKEALLIDSGLDEDAGRKIRKILE-ELGWKLKAIINTHSHADHIGGNAYLQKKtGCKVYAPKIE 79
TTHA1429-like_MBL-fold cd07725
uncharacterized Thermus thermophilus TTHA1429 and related proteins; MBL-fold metallo hydrolase ...
 76-207 2.00e-03

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: 38.05  E-value: 2.00e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2558033678  76 NGLIVRDGGRVLLVDTA-WTDDQTAQILNWIKQeinLPVALA-----VVTHAHQDKMGGMDALHAAGIATYANALSNQLA 149
Cdd:cd07725    16 NVYLLRDGDETTLIDTGlATEEDAEALWEGLKE---LGLKPSdidrvLLTHHHPDHIGLAGKLQEKSGATVYILDVTPVK 92

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2558033678 150 PQEGLVAAQHSLTFAangwvepatapnfgplkvfyPGPGHTSDNITVGIDGTDIAFGG 207
Cdd:cd07725    93 DGDKIDLGGLRLKVI--------------------ETPGHTPGHIVLYDEDRRELFVG 130
ComEC COG2333
DNA uptake channel protein ComEC C-terminal domain, metallo-beta-lactamase superfamily ...
 78-135 2.86e-03

DNA uptake channel protein ComEC C-terminal domain, metallo-beta-lactamase superfamily [Intracellular trafficking, secretion, and vesicular transport];


Pssm-ID: 441904 [Multi-domain]  Cd Length: 253  Bit Score: 38.30  E-value: 2.86e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2558033678  78 LIVRDGGRVLLVDT--AWTDDQTAQ-ILNWIKQE-INlPVALAVVTHAHQDKMGGMDALHAA 135
Cdd:COG2333    15 LIRTPDGKTILIDTgpRPSFDAGERvVLPYLRALgIR-RLDLLVLTHPDADHIGGLAAVLEA 75
arylsulfatase_Sdsa1-like_MBL-fold cd07710
Pseudomonas aeruginosa arylsulfatase SdsA1, Pseudomonas sp. DSM6611 arylsulfatase Pisa1, and ...
 53-156 7.25e-03

Pseudomonas aeruginosa arylsulfatase SdsA1, Pseudomonas sp. DSM6611 arylsulfatase Pisa1, and related proteins; MBL-fold metallo-hydrolase domain; Arylsulfatase (also known as aryl-sulfate sulfohydrolase, EC 3.1.6.1). Pseudomonas aeruginosa SdsA1 is a secreted SDS hydrolase that allows the bacterium to use primary sulfates such as the detergent SDS common in commercial personal hygiene products as a sole carbon or sulfur source. Pseudomonas inverting secondary alkylsulfatase 1 (Pisa1) is specific for secondary alkyl sulfates. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions.


Pssm-ID: 293796 [Multi-domain]  Cd Length: 239  Bit Score: 37.09  E-value: 7.25e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2558033678  53 QLAPNVWQhtsyldMPGFGaVASNGLIVRDGGrVLLVDTAWTDDQTAQILNWIKQE-INLPVAlAVV-THAHQDKMGGMD 130
Cdd:cd07710     4 EVTDGVYQ------VRGYD-LSNMTFIEGDTG-LIIIDTLESAEAAKAALELFRKHtGDKPVK-AIIyTHSHPDHFGGAG 74

                          90       100       110
                  ....*....|....*....|....*....|
gi 2558033678 131 AL----HAAGIATYANALSNQLAPQEGLVA 156
Cdd:cd07710    75 GFveeeDSGKVPIIAPEGFMEEAVSENVLA 104
 
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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