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Conserved domains on  [gi|11513826|pdb|1DD6|A]
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Chain A, IMP-1 METALLO BETA-LACTAMASE

Protein Classification

DIM/GIM/SIM family subclass B1 metallo-beta-lactamase( domain architecture ID 10888857)

DIM/GIM/SIM 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
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 ...
 5-216 1.64e-127

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: 358.90  E-value: 1.64e-127
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DD6_A        5 PDLKIEKLDEGVYVHTSFEEVNGWGVVPKHGLVVLVNAEAYLIDTPFTAKDTEKLVTWFVERGYKIKGSISSHFHSDSTG 84
Cdd:cd16301   1 PKLKIEKLSDGVYLHTSYKEVEGWGLVDANGLVVVDGKEAYLIDTPWSESDTEKLVEWIKAQGLTLKASISTHFHEDRTG 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DD6_A       85 GIEWLNSRSIPTYASELTNELLKKDGKVQATNSFSGVNYWLVKNKIEVFYPGPGHTPDNVVVWLPERKILFGGCFIKP-- 162
Cdd:cd16301  81 GIGYLNSHSIPTYASELTNQLLKKNGKELATHSFSGDEFWLLKGKIEVFYPGAGHTKDNLVVWLPKEKILFGGCLVKSle 160

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
1DD6_A      163 -YGLGNLGDANIEAWPKSAKLLKSKYGKAKLVVPSHSEVGDASLLKLTLEQAVKG 216
Cdd:cd16301 161 sKGLGNTGDASISQWPASAQKVLSKYPNAKLVVPGHGKVGDVSLLEHTRKLAKKA 215
 
Name Accession Description Interval E-value
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 ...
 5-216 1.64e-127

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: 358.90  E-value: 1.64e-127
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DD6_A        5 PDLKIEKLDEGVYVHTSFEEVNGWGVVPKHGLVVLVNAEAYLIDTPFTAKDTEKLVTWFVERGYKIKGSISSHFHSDSTG 84
Cdd:cd16301   1 PKLKIEKLSDGVYLHTSYKEVEGWGLVDANGLVVVDGKEAYLIDTPWSESDTEKLVEWIKAQGLTLKASISTHFHEDRTG 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DD6_A       85 GIEWLNSRSIPTYASELTNELLKKDGKVQATNSFSGVNYWLVKNKIEVFYPGPGHTPDNVVVWLPERKILFGGCFIKP-- 162
Cdd:cd16301  81 GIGYLNSHSIPTYASELTNQLLKKNGKELATHSFSGDEFWLLKGKIEVFYPGAGHTKDNLVVWLPKEKILFGGCLVKSle 160

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
1DD6_A      163 -YGLGNLGDANIEAWPKSAKLLKSKYGKAKLVVPSHSEVGDASLLKLTLEQAVKG 216
Cdd:cd16301 161 sKGLGNTGDASISQWPASAQKVLSKYPNAKLVVPGHGKVGDVSLLEHTRKLAKKA 215
GloB COG0491
Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General ...
 16-223 3.11e-24

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: 95.53  E-value: 3.11e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DD6_A       16 VYVHTSFEEVNGWGVvpkHGLVVLVNAEAYLIDTPFTAKDTEKLVTWFVERGYKIKGSISSHFHSDSTGGIEWLNSRS-I 94
Cdd:COG0491   1 VYVLPGGTPGAGLGV---NSYLIVGGDGAVLIDTGLGPADAEALLAALAALGLDIKAVLLTHLHPDHVGGLAALAEAFgA 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DD6_A       95 PTYASELTNELLKKDGK--------VQATNSFS-GVNYWLVKNKIEVFYpGPGHTPDNVVVWLPERKILFGGCFIKPYGL 165
Cdd:COG0491  78 PVYAHAAEAEALEAPAAgalfgrepVPPDRTLEdGDTLELGGPGLEVIH-TPGHTPGHVSFYVPDEKVLFTGDALFSGGV 156

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
1DD6_A      166 GN--LGDANIEAWPKSAKLLKSKygKAKLVVPSHSEVGDASLLKLtLEQAVKGLNESKKP 223
Cdd:COG0491 157 GRpdLPDGDLAQWLASLERLLAL--PPDLVIPGHGPPTTAEAIDY-LEELLAALGERANP 213
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 37-197 7.08e-24

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: 93.77  E-value: 7.08e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DD6_A          37 VVLVNAEAYLIDTPFtaKDTEKLVTWFVERGY-KIKGSISSHFHSDSTGGIEWLNSRS-IPTYASELTNELLKKDGKVQA 114
Cdd:smart00849   4 LVRDDGGAILIDTGP--GEAEDLLAELKKLGPkKIDAIILTHGHPDHIGGLPELLEAPgAPVYAPEGTAELLKDLLALLG 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DD6_A         115 TNSFSGVNYWLVK------------NKIEVFYPgPGHTPDNVVVWLPERKILFGGCFIKPYGLGNLG--DANIEAWPKSA 180
Cdd:smart00849  82 ELGAEAEPAPPDRtlkdgdeldlggGELEVIHT-PGHTPGSIVLYLPEGKILFTGDLLFAGGDGRTLvdGGDAAASDALE 160

                          170
                   ....*....|....*..
1DD6_A         181 KLLKSKYGKAKLVVPSH 197
Cdd:smart00849 161 SLLKLLKLLPKLVVPGH 177
Lactamase_B pfam00753
Metallo-beta-lactamase superfamily;
37-197 2.40e-11

Metallo-beta-lactamase superfamily;


Pssm-ID: 425851 [Multi-domain]  Cd Length: 196  Bit Score: 60.85  E-value: 2.40e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DD6_A         37 VVLVNAEAYLIDT-PFTAKDTEKLVTWFVERGYKIKGSISSHFHSDSTGGIEWL-NSRSIPTYASELTNELLKKDGKVQA 114
Cdd:pfam00753  10 LIEGGGGAVLIDTgGSAEAALLLLLAALGLGPKDIDAVILTHGHFDHIGGLGELaEATDVPVIVVAEEARELLDEELGLA 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DD6_A        115 TNSFSGVNYWLVKNKIEV----------------FYPGPGHTPDNVVVWLPERKILFGGCFIKPYGLGNLGDANIEAWPK 178
Cdd:pfam00753  90 ASRLGLPGPPVVPLPPDVvleegdgilggglgllVTHGPGHGPGHVVVYYGGGKVLFTGDLLFAGEIGRLDLPLGGLLVL 169

                         170       180
                  ....*....|....*....|....*..
1DD6_A        179 S--------AKLLKSKYGKAKLVVPSH 197
Cdd:pfam00753 170 HpssaesslESLLKLAKLKAAVIVPGH 196
 
Name Accession Description Interval E-value
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 ...
 5-216 1.64e-127

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: 358.90  E-value: 1.64e-127
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DD6_A        5 PDLKIEKLDEGVYVHTSFEEVNGWGVVPKHGLVVLVNAEAYLIDTPFTAKDTEKLVTWFVERGYKIKGSISSHFHSDSTG 84
Cdd:cd16301   1 PKLKIEKLSDGVYLHTSYKEVEGWGLVDANGLVVVDGKEAYLIDTPWSESDTEKLVEWIKAQGLTLKASISTHFHEDRTG 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DD6_A       85 GIEWLNSRSIPTYASELTNELLKKDGKVQATNSFSGVNYWLVKNKIEVFYPGPGHTPDNVVVWLPERKILFGGCFIKP-- 162
Cdd:cd16301  81 GIGYLNSHSIPTYASELTNQLLKKNGKELATHSFSGDEFWLLKGKIEVFYPGAGHTKDNLVVWLPKEKILFGGCLVKSle 160

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
1DD6_A      163 -YGLGNLGDANIEAWPKSAKLLKSKYGKAKLVVPSHSEVGDASLLKLTLEQAVKG 216
Cdd:cd16301 161 sKGLGNTGDASISQWPASAQKVLSKYPNAKLVVPGHGKVGDVSLLEHTRKLAKKA 215
MBL-B1 cd16285
metallo-beta-lactamases, subclass B1; MBL-fold metallo-hydrolase domain; MBLs (class B of the ...
 7-211 2.37e-106

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: 304.98  E-value: 2.37e-106
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DD6_A        7 LKIEKLDEGVYVHTSFEEVNgWGVVPKHGLVVLVNAEAYLIDTPFTAKDTEKLVTWFVER-GYKIKGSISSHFHSDSTGG 85
Cdd:cd16285   1 LRIRPLADNVWVHTSLAEFN-GGAVPSNGLIVIDGKGLVLIDTPWTEAQTATLLDWIEKKlGKPVTAAISTHSHDDRTGG 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DD6_A       86 IEWLNSRSIPTYASELTNELLKKDGKVQATNSFSGvNYWLVKNKIEVFYPGPGHTPDNVVVWLPERKILFGGCFIKP--- 162
Cdd:cd16285  80 IKALNARGIPTYATALTNELAKKEGKPVPTHSLKG-ALTLGFGPLEVFYPGPGHTPDNIVVWLPKSKILFGGCLVKSasa 158

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
1DD6_A      163 YGLGNLGDANIEAWPKSAKLLKSKYGKAKLVVPSHSEVGDASLLKLTLE 211
Cdd:cd16285 159 TSLGNVGDADVEAWPKSIENLKAKYPEARMVVPGHGAPGGTELLDHTLD 207
CcrA-like_MBL-B1 cd16302
Bacteroides fragilis CcrA and related metallo-beta-lactamases, subclass B1; MBL-fold ...
 7-211 3.50e-73

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: 220.96  E-value: 3.50e-73
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DD6_A        7 LKIEKLDEGVYVHTSFEEVNGWGVVPKHGLVVLVNAEAYLIDTPFTAKDTEKLVTWfVER--GYKIKGSISSHFHSDSTG 84
Cdd:cd16302   1 LEIIKLSDHVYVHVSYLETETFGKVPCNGMIVINGGEAVVFDTPTNDSQSEELIDW-IENslKAKVKAVVPTHFHDDCLG 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DD6_A       85 GIEWLNSRSIPTYASELTNELLKKDGKVQATNSFSGVNYWLV-KNKIEVFYPGPGHTPDNVVVWLPERKILFGGCFIKPY 163
Cdd:cd16302  80 GLKAFHRRGIPSYANQKTIALAKEKGLPVPQHGFSDSLTLKLgGKKIVCRYFGEGHTKDNIVVYFPSEKVLFGGCMVKSL 159

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
1DD6_A      164 --GLGNLGDANIEAWPKSAKLLKSKYGKAKLVVPSHSEVGDASLLKLTLE 211
Cdd:cd16302 160 gaGKGNLEDANVEAWPKTVEKVKAKYPDVKIVIPGHGKIGGSELLDYTID 209
BcII-like_MBL-B1 cd16304
Bacillus cereus Beta-lactamase 2 and related metallo-beta-lactamases, subclass B1; MBL-fold ...
 7-211 2.86e-67

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: 205.98  E-value: 2.86e-67
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DD6_A        7 LKIEKLDEGVYVHTSFEEVNGwGVVPKHGLVVLVNAEAYLIDTPFTAKDTEKLVTWFVERGYK-IKGSISSHFHSDSTGG 85
Cdd:cd16304   1 LEVTKLNKNVWVHTSYGLFNG-TPVPSNGLIVETSKGVVLIDTPWDDEQTEELLDWIKKKLKKpVTLAIVTHAHDDRIGG 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DD6_A       86 IEWLNSRSIPTYASELTNELLKKDGKVQATNSFSGV-NYWLVKNKIEVFYPGPGHTPDNVVVWLPERKILFGGCFIKPY- 163
Cdd:cd16304  80 IKALQKRGIPVYSTKLTAQLAKKQGYPSPDGILKDDtTLKFGNTKIETFYPGEGHTADNIVVWLPQSKILFGGCLVKSLe 159

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
1DD6_A      164 --GLGNLGDANIEAWPKSAKLLKSKYGKAKLVVPSHSEVGDASLLKLTLE 211
Cdd:cd16304 160 akDLGNTADANLKEWPTSIRNVLKRYPNAEIVVPGHGEWGDKQLLRHTLD 209
NDM_FIM-like_MBL-B1 cd16300
NDM-1, FIM-1 and related metallo-beta-lactamases, subclass B1; MBL-fold metallo-hydrolase ...
 7-213 1.15e-55

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: 176.55  E-value: 1.15e-55
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DD6_A        7 LKIEKLDEGVYVHTSFEEVNGWGVVPKHGLVVLVNAEAYLIDTPFTAKDTEKLVTWFVERGYK-IKGSISSHFHSDSTGG 85
Cdd:cd16300   1 VVFRQLAPGVWMHTSYLDMPGFGAVPSNGLIVRDGDRVLLVDTAWTDDQTAQILNWAKQELNLpVRLAVVTHAHQDKMGG 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DD6_A       86 IEWLNSRSIPTYASELTNELLKKDGKVQATNS--FSGVNYWLVKNKIEVFYPGPGHTPDNVVVWLPERKILFGGCFIKPY 163
Cdd:cd16300  81 MDALHAAGIATYANALSNQLAPQEGLVPAQHSltFAAEPSTAPNFPLKVFYPGPGHTRDNIVVGIDGTGIAFGGCLIRPS 160

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
1DD6_A      164 G---LGNLGDANIEAWPKSAKLLKSKYGKAKLVVPSHSEVGDASLLKLTLEQA 213
Cdd:cd16300 161 KatsLGNLADADTEHWAASARAFGAAFPDASMIVPSHGAPDGRAAITHTARLA 213
MBL-B1-B2-like cd07707
metallo-beta-lactamases; subclasses B1 and B2 and related proteins; MBL-fold metallo-hydrolase ...
 7-210 4.82e-55

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: 175.43  E-value: 4.82e-55
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DD6_A        7 LKIEKLDEGVYVHTSFEEVngwgvvPKHGLVVLVNAEAYLIDTPFTAKDTEKLVTWfVER--GYKIKGSISSHFHSDSTG 84
Cdd:cd07707   1 LSLTQINGPVWVVTDLGSV------PSNGLVYNGSKGLVLVDSTWTPKTTKELIKE-IEKvsQKPVTEVINTHFHTDRAG 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DD6_A       85 GIEWLNSRSIPTYASELTNELLKKD------------------GKVQATNSFSGVnYWLVKNKIEVFYPGPGHTPDNVVV 146
Cdd:cd07707  74 GNAYLKERGAKTVSTALTRDLAKSEwaeivaftrkglpeypdlGYELPDGVLDGD-FNLQFGKVEAFYPGPAHTPDNIVV 152

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....
1DD6_A      147 WLPERKILFGGCFIKPYGLGNLGDANIEAWPKSAKLLKSKYGKAKLVVPSHSEVGDASLLKLTL 210
Cdd:cd07707 153 YFPQENVLYGGCIIKETDLGNVADADVKEWPTSIERLKKRYRNIKAVIPGHGEVGGPELLDHTL 216
MUS_TUS_MBL-B1 cd16318
Myroides odoratimimus MUS-1, MUS-2, TUS-1 and related metallo-beta-lactamases, subclass B1; ...
 7-199 1.22e-51

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: 166.37  E-value: 1.22e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DD6_A        7 LKIEKLDEGVYVHTSFEEVNGWgVVPKHGLVVLVNAEAYLIDTPFTAKDTEKLVTWF-VERGYKIKGSISSHFHSDSTGG 85
Cdd:cd16318   1 LKIKQLNDNMYIYTTYQEFQGV-TYSSNSMYVLTDEGVILIDTPWDKDQYEPLLEYIrSNHNKEVKWVITTHFHEDRSGG 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DD6_A       86 IEWLNSRSIPTYASELTNELLKKDGKVQATNSF-SGVNYWLVKNKIEVFYPGPGHTPDNVVVWLPERKILFGGCFIK--- 161
Cdd:cd16318  80 LGYFNSIGAQTYTYALTNEILKERNEPQAQFSFnKEKQFTFGNEKLAVYFLGEGHSLDNTVVWFPKEEVLYGGCLIKsae 159

                       170       180       190
                ....*....|....*....|....*....|....*...
1DD6_A      162 PYGLGNLGDANIEAWPKSAKLLKSKYGKAKLVVPSHSE 199
Cdd:cd16318 160 ATTIGNIADGNVIAWPKTIEAVKQKFKNAKVIIPGHDE 197
VIM_type_MBL-B1 cd16303
VIM-type metallo-beta-lactamases, subclass B1; MBL-fold metallo-hydrolase domain; VIM (Verona ...
 6-210 3.36e-51

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: 165.42  E-value: 3.36e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DD6_A        6 DLKIEKLDEGVYVHTSFEEVNGwGVVPKHGLVVLVNAEAYLIDTPFTAKDTEKLVTWF-VERGYKIKGSISSHFHSDSTG 84
Cdd:cd16303   2 EVRLYQIADGVWSHIATQSFDG-AVYPSNGLIVRDGDELLLIDTAWGAKNTAALLAEIeKQIGLPVTRAVSTHFHDDRVG 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DD6_A       85 GIEWLNSRSIPTYASELTNELLKKDGKVQATNSFSGVNYWLVKNK---IEVFYPGPGHTPDNVVVWLPERKILFGGCFIK 161
Cdd:cd16303  81 GVDVLRAAGVATYASPSTRRLAEAEGNEIPTHSLEGLSSSGDAVRfgpVELFYPGAAHSTDNLVVYVPSARVLYGGCAVR 160

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
1DD6_A      162 PY---GLGNLGDANIEAWPKSAKLLKSKYGKAKLVVPSHSEVGDASLLKLTL 210
Cdd:cd16303 161 ELsstSAGNVADADLAEWPTSIERIQKHYPEAEFVIPGHGLPGGLDLLHHTK 212
IND_BlaB-like_MBL-B1 cd16299
IND1, IND2, BlaB-1 and related metallo-beta-lactamases, subclass B1; MBL-fold ...
 7-211 1.24e-49

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: 161.07  E-value: 1.24e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DD6_A        7 LKIEKLDEGVYVHTSFEEVNGwGVVPKHGLVVLVNAEAYLIDTPFTAKDTEKLVTWFVER-GYKIKGSISSHFHSDSTGG 85
Cdd:cd16299   1 LKIEKLNDNLYIYTTYNEFNG-VKYSANAMYLVTKKGVILFDTPWDKDQYQPLLDSIRKKhNLPVIAVIATHSHEDRAGG 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DD6_A       86 IEWLNSRSIPTYASELTNELLKKDGKVQATNSF-SGVNYWLVKNKIEVFYPGPGHTPDNVVVWLPERKILFGGCFIK--- 161
Cdd:cd16299  80 LGYFNKIGIPTYATAMTNSILKKENKPQATYLIeTDKTYKIGGEKFVVYFFGEGHTADNVVVWFPKEKVLDGGCLIKsae 159

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
1DD6_A      162 PYGLGNLGDANIEAWPKSAKLLKSKYGKAKLVVPSHSEVGDASLLKLTLE 211
Cdd:cd16299 160 ATDLGYIGEANVKEWPKTIHKLKQKFKKAKVVIPGHDEWKDQGHIENTLK 209
BlaB-like_MBL-B1 cd16316
Elizabethkingia meningoseptica (Chryseobacterium meningosepticum) BlaB and related ...
 7-211 4.47e-48

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: 157.24  E-value: 4.47e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DD6_A        7 LKIEKLDEGVYVHTSFEEVNGwGVVPKHGLVVLVNAEAYLIDTPFTAKDTEKLV-TWFVERGYKIKGSISSHFHSDSTGG 85
Cdd:cd16316   1 LKISHLTGDLYVYTTYNTYKG-TKTAANAVYVVTDKGVVVIDAPWDETQFQPFLdSIQKKHHKKVIMNIATHSHDDRAGG 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DD6_A       86 IEWLNSRSIPTYASELTNELLKKDGKVQATNSFSGVNYWLV-KNKIEVFYPGPGHTPDNVVVWLPERKILFGGCFIKPYG 164
Cdd:cd16316  80 LEYFGKKGAKTYTTKLTDSILKKNNKPRAEYTFDNDTTFKVgKYEFQVYYPGKGHTADNIVVWFPKEKVLYGGCLIKSAD 159

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
1DD6_A      165 ---LGNLGDANIEAWPKSAKLLKSKYGKAKLVVPSHSEVGDASLLKLTLE 211
Cdd:cd16316 160 akdLGYLGEAYVNDWTQSIHNIQQKFPNPQYVIAGHDDWKDQTSLQHTLK 209
SPM-1-like_MBL-B1-B2-like cd16286
Pseudomonas areoginosa SPM-1 and related metallo-beta-lactamases, subclasses B1 and B2 like; ...
 6-210 1.53e-44

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: 148.83  E-value: 1.53e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DD6_A        6 DLKIEKLDEGVYVHTsfeEVNGWGvvpKHGLVVLV-NAEAYLIDTPFTAKDTEKLVTWfVERGYKIKG--SISSHFHSDS 82
Cdd:cd16286   6 NLTAREIDPDVFVIT---HRDPWS---SNVLVVKMlDGTVVIVDSPYTNLATQTVLDW-IAKTMGPRKvvAINTHFHLDG 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DD6_A       83 TGGIEWLNSRSIPTYASELTNELLKKDGK------------------------VQATNSF---SGVNYWLVKNKIEVFYP 135
Cdd:cd16286  79 TGGNEALKKRGIPTWGSDLTKQLLLERGKadrikaaeflknedlkrriessppVPPDNVFdlkEGKVFSFGNELVEVSFP 158

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
1DD6_A      136 GPGHTPDNVVVWLPERKILFGGCFIKPY-GLGNLGDANIEAWPKSAKLLKSKygKAKLVVPSHSEVGDASLLKLTL 210
Cdd:cd16286 159 GPAHAPDNVVVYFPERKILFGGCMIKPGkELGNLGDANMKAWPDSVRRLKKF--DAKIVIPGHGERGDPGMVNKTI 232
IND_MBL-B1 cd16317
Chryseobacterium indologenes IND-1, IND-2, IND-7and related metallo-beta-lactamases, subclass ...
 26-211 1.02e-34

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: 123.20  E-value: 1.02e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DD6_A       26 NGWGVVPKHGLVvlvnaeayLIDTPFTAKDTEKLVTWFVERGY-KIKGSISSHFHSDSTGGIEWLNSRSIPTYASELTNE 104
Cdd:cd16317  29 NAVYLVTKKGVV--------LFDVPWQKVQYQSLMDTIQKRHHlPVIAVFATHSHDDRAGDLSFYNNKGIKTYATAKTNE 100

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DD6_A      105 LLKKDGKVQATNSF-SGVNYWLVKNKIEVFYPGPGHTPDNVVVWLPERKILFGGCFIKPYG---LGNLGDANIEAWPKSA 180
Cdd:cd16317 101 FLKKDGKATSTEIIkTGKPYRIGGEEFVVDFLGEGHTADNVVVWFPKYKVLDGGCLVKSNSatdLGYTGEANVEQWPKTM 180

                       170       180       190
                ....*....|....*....|....*....|.
1DD6_A      181 KLLKSKYGKAKLVVPSHSEVGDASLLKLTLE 211
Cdd:cd16317 181 NKLKAKYAQATLIIPGHDEWKGGGHVEHTLD 211
GloB COG0491
Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General ...
 16-223 3.11e-24

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: 95.53  E-value: 3.11e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DD6_A       16 VYVHTSFEEVNGWGVvpkHGLVVLVNAEAYLIDTPFTAKDTEKLVTWFVERGYKIKGSISSHFHSDSTGGIEWLNSRS-I 94
Cdd:COG0491   1 VYVLPGGTPGAGLGV---NSYLIVGGDGAVLIDTGLGPADAEALLAALAALGLDIKAVLLTHLHPDHVGGLAALAEAFgA 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DD6_A       95 PTYASELTNELLKKDGK--------VQATNSFS-GVNYWLVKNKIEVFYpGPGHTPDNVVVWLPERKILFGGCFIKPYGL 165
Cdd:COG0491  78 PVYAHAAEAEALEAPAAgalfgrepVPPDRTLEdGDTLELGGPGLEVIH-TPGHTPGHVSFYVPDEKVLFTGDALFSGGV 156

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
1DD6_A      166 GN--LGDANIEAWPKSAKLLKSKygKAKLVVPSHSEVGDASLLKLtLEQAVKGLNESKKP 223
Cdd:COG0491 157 GRpdLPDGDLAQWLASLERLLAL--PPDLVIPGHGPPTTAEAIDY-LEELLAALGERANP 213
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 37-197 7.08e-24

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: 93.77  E-value: 7.08e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DD6_A          37 VVLVNAEAYLIDTPFtaKDTEKLVTWFVERGY-KIKGSISSHFHSDSTGGIEWLNSRS-IPTYASELTNELLKKDGKVQA 114
Cdd:smart00849   4 LVRDDGGAILIDTGP--GEAEDLLAELKKLGPkKIDAIILTHGHPDHIGGLPELLEAPgAPVYAPEGTAELLKDLLALLG 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DD6_A         115 TNSFSGVNYWLVK------------NKIEVFYPgPGHTPDNVVVWLPERKILFGGCFIKPYGLGNLG--DANIEAWPKSA 180
Cdd:smart00849  82 ELGAEAEPAPPDRtlkdgdeldlggGELEVIHT-PGHTPGSIVLYLPEGKILFTGDLLFAGGDGRTLvdGGDAAASDALE 160

                          170
                   ....*....|....*..
1DD6_A         181 KLLKSKYGKAKLVVPSH 197
Cdd:smart00849 161 SLLKLLKLLPKLVVPGH 177
metallo-hydrolase-like_MBL-fold cd16282
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 15-206 5.53e-19

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: 81.46  E-value: 5.53e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DD6_A       15 GVYVHTSFEEVNGWG----VVPKHGLVVlvnaeaylIDTPFTAKDTEKL------VT----WFVergykikgsISSHFHS 80
Cdd:cd16282   1 GVYALIGPDGGGFISnigfIVGDDGVVV--------IDTGASPRLARALlaairkVTdkpvRYV---------VNTHYHG 63

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DD6_A       81 DSTGGIEWLNSRSIPTYASELTNELLKKDGKVQATNSFSGVNYWLV--------------------KNKIEVFYPGPGHT 140
Cdd:cd16282  64 DHTLGNAAFADAGAPIIAHENTREELAARGEAYLELMRRLGGDAMAgtelvlpdrtfddgltldlgGRTVELIHLGPAHT 143

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
1DD6_A      141 PDNVVVWLPERKILFGGCFIKPYGLGNLGDANIEAWPKSAKLLKSKygKAKLVVPSHSEVGDASLL 206
Cdd:cd16282 144 PGDLVVWLPEEGVLFAGDLVFNGRIPFLPDGSLAGWIAALDRLLAL--DATVVVPGHGPVGDKADL 207
CphA_ImiS-like_MBL-B2 cd16306
Aeromonas hydrophyla CphA, Aeromonas veronii ImiS, and related metallo-beta-lactamases, ...
 49-197 2.86e-17

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: 77.30  E-value: 2.86e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DD6_A       49 TPFTAKDTEKLVTWFVERgyKIKGSISSHFHSDSTGGIEWLNSRSIPTYASELTNELLKKDGK----------------- 111
Cdd:cd16306  40 TPDTARELHKLIKRVSRK--PVLEVINTNYHTDRAGGNAYWKSIGAKVVSTRQTRDLMKSDWAeivaftrkglpeypdlp 117

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DD6_A      112 -VQATNSFSGvNYWLVKNKIEVFYPGPGHTPDNVVVWLPERKILFGGCFIKPyGLGNLGDANIEAWPKSAKLLKSKYGKA 190
Cdd:cd16306 118 lVLPNVVHDG-DFTLQEGKVRAFYLGPAHTPDGIFVYFPDEQVLYGNCILKE-KLGNLSFADVKAYPQTLERLKAMKLPI 195


                ....*..
1DD6_A      191 KLVVPSH 197
Cdd:cd16306 196 KTVIGGH 202
CphS_ImiS-like_MBL-B2 cd16287
metallo-beta-lactamases, subclass B2; MBL-fold metallo-hydrolase domain; Includes Aeromonas ...
 49-201 2.02e-16

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: 75.16  E-value: 2.02e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DD6_A       49 TPFTAKDTEKLVTWFVERgyKIKGSISSHFHSDSTGGIEWLNSRSIPTYASELTNELLKKDGKVQATNSFSGV------- 121
Cdd:cd16287  40 TPETAETLYKEIRKVSPL--PINEVINTNYHTDRAGGNAYWKTLGAKIVATQMTYDLQKSQWGSIVNFTRQGNnkypnle 117

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DD6_A      122 ----------NYWLVKNKIEVFYPGPGHTPDNVVVWLPERKILFGGCFIKPyGLGNLGDANIEAWPKSAKLLKSKygKAK 191
Cdd:cd16287 118 kslpdtvfpgDFNLQNGSIRAMYLGEAHTKDGIFVYFPAERVLYGNCILKE-NLGNMSFANRTEYPKTLEKLKGL--IEQ 194

                       170
                ....*....|
1DD6_A      192 LVVPSHSEVG 201
Cdd:cd16287 195 GELKVDSIIA 204
metallo-hydrolase-like_MBL-fold cd06262
mainly hydrolytic enzymes and related proteins which carry out various biological functions; ...
 43-197 6.01e-14

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: 67.70  E-value: 6.01e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DD6_A       43 EAYLIDTPFTAKdtEKLVTWFVERGYKIKGSISSHFHSDSTGGIEWLNSRS-IPTYASELTNELLKKDGKVQATNSFSGV 121
Cdd:cd06262  21 EAILIDPGAGAL--EKILEAIEELGLKIKAILLTHGHFDHIGGLAELKEAPgAPVYIHEADAELLEDPELNLAFFGGGPL 98

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DD6_A      122 NY-----WLVKN--------KIEVFYPgPGHTPDNVVVWLPERKILFGGCFIKPYGLGN--LGDANIEAWPKSAKLLKSK 186
Cdd:cd06262  99 PPpepdiLLEDGdtielgglELEVIHT-PGHTPGSVCFYIEEEGVLFTGDTLFAGSIGRtdLPGGDPEQLIESIKKLLLL 177

                       170
                ....*....|.
1DD6_A      187 YGKAKLVVPSH 197
Cdd:cd06262 178 LPDDTVVYPGH 188
Sfh-1-like_MBL-B2 cd16305
Serratia fonticola Sfh-I and related metallo-beta-lactamases, subclass B2; MBL-fold ...
 49-196 5.39e-12

Serratia fonticola Sfh-I 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: 293863  Cd Length: 226  Bit Score: 63.09  E-value: 5.39e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DD6_A       49 TPFTAKDTEKLVTWFveRGYKIKGSISSHFHSDSTGGIEWLNSRSIPTYASELTNELLKKDGKVQATNSFSGVNYW---- 124
Cdd:cd16305  40 TPETAETLEKEIRKV--SPLPIKEVINTNYHTDRAGGNAYWKTLGASIVSTQMTYDLEKSQWGSIVDFTRQGNNKYpnle 117

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DD6_A      125 -------------LVKNKIEVFYPGPGHTPDNVVVWLPERKILFGGCFIKPyGLGNLGDANIEAWPKSAKLLKSKYGKAK 191
Cdd:cd16305 118 kslpdtvypgdfnLQNGSVRALYLGEAHTEDGIFVYFPAERVLYGNCILKE-KLGNMSFANRTEYPKTLKKLKGLIEQGE 196


                ....*
1DD6_A      192 LVVPS 196
Cdd:cd16305 197 LKVES 201
Lactamase_B pfam00753
Metallo-beta-lactamase superfamily;
37-197 2.40e-11

Metallo-beta-lactamase superfamily;


Pssm-ID: 425851 [Multi-domain]  Cd Length: 196  Bit Score: 60.85  E-value: 2.40e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DD6_A         37 VVLVNAEAYLIDT-PFTAKDTEKLVTWFVERGYKIKGSISSHFHSDSTGGIEWL-NSRSIPTYASELTNELLKKDGKVQA 114
Cdd:pfam00753  10 LIEGGGGAVLIDTgGSAEAALLLLLAALGLGPKDIDAVILTHGHFDHIGGLGELaEATDVPVIVVAEEARELLDEELGLA 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DD6_A        115 TNSFSGVNYWLVKNKIEV----------------FYPGPGHTPDNVVVWLPERKILFGGCFIKPYGLGNLGDANIEAWPK 178
Cdd:pfam00753  90 ASRLGLPGPPVVPLPPDVvleegdgilggglgllVTHGPGHGPGHVVVYYGGGKVLFTGDLLFAGEIGRLDLPLGGLLVL 169

                         170       180
                  ....*....|....*....|....*..
1DD6_A        179 S--------AKLLKSKYGKAKLVVPSH 197
Cdd:pfam00753 170 HpssaesslESLLKLAKLKAAVIVPGH 196
metallo-hydrolase-like_MBL-fold cd16276
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 74-155 8.99e-09

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: 293834 [Multi-domain]  Cd Length: 188  Bit Score: 53.36  E-value: 8.99e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DD6_A       74 ISSHFHSDSTGGIEWLNSRSIPTYASELTNELLKKDGK---VQATNSFSGvNYWL-VKNK-IEVFYPGPGHTPDNVVVWL 148
Cdd:cd16276  50 VYSHNHADHIGGASIFKDEGATIIAHEATAELLKRNPDpkrPVPTVTFDD-EYTLeVGGQtLELSYFGPNHGPGNIVIYL 128


                ....*..
1DD6_A      149 PERKILF 155
Cdd:cd16276 129 PKQKVLM 135
metallo-hydrolase-like_MBL-fold cd07739
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 43-197 6.80e-08

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


Pssm-ID: 293825 [Multi-domain]  Cd Length: 201  Bit Score: 50.96  E-value: 6.80e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DD6_A       43 EAYLIDTPFTAKDTEKLVTWFVERGYKIKGSISSHFHSDSTGGIEWLNSR--SIPTYASELTNELLKK--DGKVQATNSF 118
Cdd:cd07739  26 EAVLVDAQFTRADAERLADWIKASGKTLTTIYITHGHPDHYFGLEVLLEAfpDAKVVATPAVVAHIKAqlEPKLAFWGPL 105

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DD6_A      119 SGVNywLVKN-----------------KIEVFYPGPGHTPDNVVVWLPERK------ILFGGCFikPYGLGNLGDANIEA 175
Cdd:cd07739 106 LGGN--APARlvvpepldgdtltleghPLEIVGVGGGDTDDTTYLWIPSLKtvvagdVVYNGVH--VWLADATTPELRAA 181

                       170       180
                ....*....|....*....|..
1DD6_A      176 WPKSAKLLKSKygKAKLVVPSH 197
Cdd:cd07739 182 WLAALDKIEAL--NPETVVPGH 201
arylsulfatase_Sdsa1-like_MBL-fold cd07710
Pseudomonas aeruginosa arylsulfatase SdsA1, Pseudomonas sp. DSM6611 arylsulfatase Pisa1, and ...
 8-198 2.37e-07

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: 49.81  E-value: 2.37e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DD6_A        8 KIEKLDEGVYVhtsfeeVNGWG------VVPKHGLVVlvnaeaylIDTPFTAKDTEKLVTWFVE-RGYK-IKGSISSHFH 79
Cdd:cd07710   1 GLFEVTDGVYQ------VRGYDlsnmtfIEGDTGLII--------IDTLESAEAAKAALELFRKhTGDKpVKAIIYTHSH 66

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DD6_A       80 SDSTGGIEWL----NSRSIPTYASELTNE-----------------------LLKKDGKVQ-----------ATNSFSGV 121
Cdd:cd07710  67 PDHFGGAGGFveeeDSGKVPIIAPEGFMEeavsenvlagnamsrraayqfgaLLPKGEKGQvgaglgpglstGTVGFIPP 146

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DD6_A      122 NYWLVKNKIEV--------FYPGPGHTPDNVVVWLPERKILFGG-----CFikPyglgNL----G----DANieAWPKSA 180
Cdd:cd07710 147 TITITETGETLtidgveleFQHAPGEAPDEMMVWLPDYKVLFCAdnvyhTF--P----NLytlrGakyrDAL--AWAKSL 218

                       250
                ....*....|....*...
1DD6_A      181 KLLKSKygKAKLVVPSHS 198
Cdd:cd07710 219 DEAISL--KAEVLFPSHT 234
yflN-like_MBL-fold cd07721
uncharacterized subgroup which includes Bacillus subtilis yflN; MBL-fold metallo hydrolase ...
 37-197 2.04e-06

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: 46.83  E-value: 2.04e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DD6_A       37 VVLVNAEAYLIDT--PFTAKDTEKLVTwfvERGYK---IKGSISSHFHSDSTGGIEWLNSRS-IPTYASELTNELLKKDG 110
Cdd:cd07721  15 LIEDDDGLTLIDTglPGSAKRILKALR---ELGLSpkdIRRILLTHGHIDHIGSLAALKEAPgAPVYAHEREAPYLEGEK 91

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DD6_A      111 KVQATNSFsgvnywLVKNKIEVFYPG--------------------------PGHTPDNVVVWLPERKILFGGCFIKPYG 164
Cdd:cd07721  92 PYPPPVRL------GLLGLLSPLLPVkpvpvdrtledgdtldlagglrvihtPGHTPGHISLYLEEDGVLIAGDALVTVG 165

                       170       180       190
                ....*....|....*....|....*....|....*...
1DD6_A      165 LGNLG-----DANIEAWPKSAKLLKSKygKAKLVVPSH 197
Cdd:cd07721 166 GELVPppppfTWDMEEALESLRKLAEL--DPEVLAPGH 201
hydroxyacylglutathione_hydrolase_MBL-fold cd07723
hydroxyacylglutathione hydrolase, MBL-fold metallo-hydrolase domain; hydroxyacylglutathione ...
 43-158 4.54e-05

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: 42.45  E-value: 4.54e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DD6_A       43 EAYLIDTPftakDTEKLVTWFVERGYKIKGSISSHFHSDSTGGIEWLNSR--SIPTYASE------LTNELlkKDGKVqa 114
Cdd:cd07723  21 EAAVVDPG----EAEPVLAALEKNGLTLTAILTTHHHWDHTGGNAELKALfpDAPVYGPAedripgLDHPV--KDGDE-- 92

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
1DD6_A      115 tnsfsgvnYWLVKNKIEVFYPgPGHTPDNVVVWLPERKILF-------GGC 158
Cdd:cd07723  93 --------IKLGGLEVKVLHT-PGHTLGHICYYVPDEPALFtgdtlfsGGC 134
TTHA1429-like_MBL-fold cd07725
uncharacterized Thermus thermophilus TTHA1429 and related proteins; MBL-fold metallo hydrolase ...
 41-157 6.19e-05

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: 42.29  E-value: 6.19e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DD6_A       41 NAEAYLIDT-PFTAKDTEKLVTWFVERGYKIkGSIS----SHFHSDSTGGIEWLNSRSIPTYASELTNELlkKDG-KVQA 114
Cdd:cd07725  23 GDETTLIDTgLATEEDAEALWEGLKELGLKP-SDIDrvllTHHHPDHIGLAGKLQEKSGATVYILDVTPV--KDGdKIDL 99

                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
1DD6_A      115 tnsfsGVNYWLVKnkievfyPGPGHTPDNVVVWLPERKILFGG 157
Cdd:cd07725 100 -----GGLRLKVI-------ETPGHTPGHIVLYDEDRRELFVG 130
RNaseJ_MBL-fold cd07714
RNAaseJ, MBL-fold metallo-hydrolase domain; RNase J, also called Ribonuclease J, is a ...
 61-108 2.04e-04

RNAaseJ, MBL-fold metallo-hydrolase domain; RNase J, also called Ribonuclease J, is a prokaryotic ribonuclease which plays a key part in RNA processing and in RNA degradation. It can act as an endonuclease which is specific for single-stranded regions of RNA irrespective of their sequence or location, and as a processive 5' exonuclease which only acts on substrates having a single phosphate or a hydroxyl at the 5' end. Many bacterial species have only one RNase J, but some, such as Bacillus subtilis, have two. 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: 293800 [Multi-domain]  Cd Length: 248  Bit Score: 41.24  E-value: 2.04e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*....
1DD6_A       61 TWFVERGYKIKGSISSHFHSDSTGGIEWL-NSRSIPTYASELTNELLKK 108
Cdd:cd07714  47 SYLEENKDKIKGIFITHGHEDHIGALPYLlPELNVPIYATPLTLALIKK 95
MBLAC2-like_MBL-fold cd07712
uncharacterized human metallo-beta-lactamase domain-containing protein 2 and related proteins; ...
 18-197 2.46e-04

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


Pssm-ID: 293798 [Multi-domain]  Cd Length: 182  Bit Score: 40.69  E-value: 2.46e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DD6_A       18 VHTSFEEVNGWGVVPKHglvvlvnaEAYLIDTPFTAKDTEKLVTWFVERGYKIkgsISSHFHSDSTGGIE-----WLNSR 92
Cdd:cd07712   2 FIEEDDRVNIYLLRGRD--------RALLIDTGLGIGDLKEYVRTLTDLPLLV---VATHGHFDHIGGLHefeevYVHPA 70

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DD6_A       93 SIPTYASELTNELLKKDgkVQATNSFSGVNYWLVKN---------KIEVFYPgPGHTPDNVVVWLPERKILFGGCFIkpy 163
Cdd:cd07712  71 DAEILAAPDNFETLTWD--AATYSVPPAGPTLPLRDgdvidlgdrQLEVIHT-PGHTPGSIALLDRANRLLFSGDVV--- 144

                       170       180       190
                ....*....|....*....|....*....|....*...
1DD6_A      164 GLGNL----GDANIEAWPKSAKLLKSKYGKAKLVVPSH 197
Cdd:cd07712 145 YDGPLimdlPHSDLDDYLASLEKLSKLPDEFDKVLPGH 182
flavodiiron_proteins_MBL-fold cd07709
catalytic domain of flavodiiron proteins (FDPs) and related proteins; MBL-fold ...
 69-181 2.54e-03

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


Pssm-ID: 293795 [Multi-domain]  Cd Length: 238  Bit Score: 37.85  E-value: 2.54e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DD6_A       69 KIKGSISSHFHSDSTGGIEWLNSR--SIPTYASELTNELLKKDGKVQATNsfsgvnYWLVKNKIEV--------FYPGPG 138
Cdd:cd07709  68 KIDYIVVNHQEPDHSGSLPELLELapNAKIVCSKKAARFLKHFYPGIDER------FVVVKDGDTLdlgkhtlkFIPAPM 141

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
1DD6_A      139 -HTPDNVVVWLPERKILF----GGCFikpYGLGNLGDANIEAWPKSAK 181
Cdd:cd07709 142 lHWPDTMVTYDPEDKILFsgdaFGAH---GASGELFDDEVEDYLEEAR 186
metallo-hydrolase-like_MBL-fold cd07743
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 35-197 6.59e-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) 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: 36.35  E-value: 6.59e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DD6_A       35 GLVVLVNAEAYLIDTPFTAKDTEKLVTWFVERGYKIKGSISSHFHSDSTGGIEWLNSRS-IPTYAS-------------- 99
Cdd:cd07743  11 GVYVFGDKEALLIDSGLDEDAGRKIRKILEELGWKLKAIINTHSHADHIGGNAYLQKKTgCKVYAPkiekafienpllep 90

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1DD6_A      100 ----------ELTNELLK-KDGKVQATNSfSGVNYWLVKnKIEVfYPGPGHTPDNVVVwLPERKILFggcfikpyglgnL 168
Cdd:cd07743  91 sylggayppkELRNKFLMaKPSKVDDIIE-EGELELGGV-GLEI-IPLPGHSFGQIGI-LTPDGVLF------------A 154

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
1DD6_A      169 GDA----------------NIEAWPKSAKLLKSKygKAKLVVPSH 197
Cdd:cd07743 155 GDAlfgeevlekygipflyDVEEQLETLEKLEEL--DADYYVPGH 197
 
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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