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Conserved domains on  [gi|521005756|gb|AGP38759|]
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beta-lactamase [Sorangium cellulosum So0157-2]

Protein Classification

MBL fold metallo-hydrolase( domain architecture ID 10888684)

MBL fold metallo-hydrolase is most likely a hydrolytic enzyme

Gene Ontology:  GO:0016787
PubMed:  17597585

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
metallo-hydrolase-like_MBL-fold cd16282
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 7-232 5.16e-67

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: 208.57  E-value: 5.16e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521005756   7 GCFAYLQPAGTWGLSNAGLVTSDGEALLVDTLFDLKRTREMLDAMRAATPAaaRIGTVVNTHANGDHCYGNALV--EGAT 84
Cdd:cd16282    1 GVYALIGPDGGGFISNIGFIVGDDGVVVIDTGASPRLARALLAAIRKVTDK--PVRYVVNTHYHGDHTLGNAAFadAGAP 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521005756  85 IIATRASAAEMDEVPAPMLAMLMRqarsgaagalgdylvhcFGAFDFDGIAPTAPTRVFEGELTVTVGAKEVRLLEVGPS 164
Cdd:cd16282   79 IIAHENTREELAARGEAYLELMRR-----------------LGGDAMAGTELVLPDRTFDDGLTLDLGGRTVELIHLGPA 141

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 521005756 165 HTKGDLLVHVPADRAIYTGDILFIDVTPILWAGPVGNWLKACDTILALDVDVIVPGHGPITDRAGVRA 232
Cdd:cd16282  142 HTPGDLVVWLPEEGVLFAGDLVFNGRIPFLPDGSLAGWIAALDRLLALDATVVVPGHGPVGDKADLRA 209
 
Name Accession Description Interval E-value
metallo-hydrolase-like_MBL-fold cd16282
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 7-232 5.16e-67

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: 208.57  E-value: 5.16e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521005756   7 GCFAYLQPAGTWGLSNAGLVTSDGEALLVDTLFDLKRTREMLDAMRAATPAaaRIGTVVNTHANGDHCYGNALV--EGAT 84
Cdd:cd16282    1 GVYALIGPDGGGFISNIGFIVGDDGVVVIDTGASPRLARALLAAIRKVTDK--PVRYVVNTHYHGDHTLGNAAFadAGAP 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521005756  85 IIATRASAAEMDEVPAPMLAMLMRqarsgaagalgdylvhcFGAFDFDGIAPTAPTRVFEGELTVTVGAKEVRLLEVGPS 164
Cdd:cd16282   79 IIAHENTREELAARGEAYLELMRR-----------------LGGDAMAGTELVLPDRTFDDGLTLDLGGRTVELIHLGPA 141

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 521005756 165 HTKGDLLVHVPADRAIYTGDILFIDVTPILWAGPVGNWLKACDTILALDVDVIVPGHGPITDRAGVRA 232
Cdd:cd16282  142 HTPGDLVVWLPEEGVLFAGDLVFNGRIPFLPDGSLAGWIAALDRLLALDATVVVPGHGPVGDKADLRA 209
GloB COG0491
Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General ...
 21-244 2.56e-28

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: 108.62  E-value: 2.56e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521005756  21 SNAGLVTSDGEALLVDTLFDLKRTREMLDAMRAATPaaaRIGTVVNTHANGDHCYGNALVE---GATIIATRASAAEMDE 97
Cdd:COG0491   15 VNSYLIVGGDGAVLIDTGLGPADAEALLAALAALGL---DIKAVLLTHLHPDHVGGLAALAeafGAPVYAHAAEAEALEA 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521005756  98 VPApmlamlmrqarsgaagalgdylvhcfgaFDFDGIAPTAPTRVFEGELTVTVGAKEVRLLEvGPSHTKGDLLVHVPAD 177
Cdd:COG0491   92 PAA----------------------------GALFGREPVPPDRTLEDGDTLELGGPGLEVIH-TPGHTPGHVSFYVPDE 142

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 521005756 178 RAIYTGDILFIDVT--PILWAGPVGNWLKACDTILALDVDVIVPGHGPITDRAGVRAVRDYLVYIRDEA 244
Cdd:COG0491  143 KVLFTGDALFSGGVgrPDLPDGDLAQWLASLERLLALPPDLVIPGHGPPTTAEAIDYLEELLAALGERA 211
SoxH_rel_PQQ_2 TIGR04559
quinoprotein relay system zinc metallohydrolase 2; By homology, members are Zn ...
 61-285 1.11e-25

quinoprotein relay system zinc metallohydrolase 2; By homology, members are Zn metallohydrolases in the same family as the SoxH protein associated with sulfate metabolism, Bacillus cereus beta-lactamase II (see PDB:1bc2), and, more distantly, hydroxyacylglutathione hydrolase (glyoxalase II). All members occur in genomes with both PQQ biosynthesis and a PQQ-dependent (quinoprotein) dehydrogenase that has a motif of two consecutive Cys residues (see TIGR03075). The Cys-Cys motif is associated with electron transfer by specialized cytochromes such as c551. All these genomes also include a fusion protein (TIGR04557) whose domains resemble SoxY and SoxZ from thiosulfate oxidation. A conserved Cys in this fusion protein aligns to the Cys residue in SoxY that carries sulfur cycle intermediates. In many genomes, the genes for PQQ biosynthesis enzymes, PQQ-dependent enzymes, their associated cytochromes, and members of this family are clustered. Note that one to three closely related Zn metallohydrolases may occur; this family represents a specific clade among them. Some members of this family have a short additional N-terminal domain with four conserved Cys residues. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 275352  Cd Length: 283  Bit Score: 103.43  E-value: 1.11e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521005756   61 IGTVVNTHANGDHCYGNA--LVEGATIIATRASAAEMDEVPAPMLAMLMRQarsgaagaLGDylvhcfgafDFDGIAPTA 138
Cdd:TIGR04559  68 IRYVINTHVHPDHIFGNAafREDGAEFVGHAKLPRALAARGEFYLASFARL--------LGE---------AFLGTEIVP 130

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521005756  139 PTRVFEGELTVTVGAKEVRLLEVGPSHTKGDLLVHVPADRAIYTGDILFIDVTPILwAGPVGNWLKACDTILALDVDVIV 218
Cdd:TIGR04559 131 PTRLVADPLELDLGGRVLELTAWPTAHTDNDLTVFDEKTGTLFTGDLLFVEHIPVL-DGSLLGWLAVLDRLKARPAARVV 209

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521005756  219 PGHGPIT--DRAGVRAVRDYLVYIRDEARRRYDAGMPPADAARDIALADYASWSDAERI-AVNVHTLYRE 285
Cdd:TIGR04559 210 PGHGPVSldWPAALAPQRRYLETLRDDVRAAIKDGLPLEEAVETAAQSEKGKWALFDEYnRRNVTAAYAE 279
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 22-221 9.00e-18

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: 79.13  E-value: 9.00e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521005756    22 NAGLVTSDGEALLVDTLFDlkrtREMLDAMRAATPAAARIGTVVNTHANGDHCYGNALVEGATIIATRASAAEMDEVPAP 101
Cdd:smart00849   1 NSYLVRDDGGAILIDTGPG----EAEDLLAELKKLGPKKIDAIILTHGHPDHIGGLPELLEAPGAPVYAPEGTAELLKDL 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521005756   102 MLAMlmrqarsgaagalgdylvhcfGAFDFDGIAPTAPTRVFEGElTVTVGAKEVRLLEVgPSHTKGDLLVHVPADRAIY 181
Cdd:smart00849  77 LALL---------------------GELGAEAEPAPPDRTLKDGD-ELDLGGGELEVIHT-PGHTPGSIVLYLPEGKILF 133

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 521005756   182 TGDILFIDVTPILWAGPVG----NWLKACDTILALDVDVIVPGH 221
Cdd:smart00849 134 TGDLLFAGGDGRTLVDGGDaaasDALESLLKLLKLLPKLVVPGH 177
Lactamase_B pfam00753
Metallo-beta-lactamase superfamily;
16-221 6.70e-17

Metallo-beta-lactamase superfamily;


Pssm-ID: 425851 [Multi-domain]  Cd Length: 196  Bit Score: 77.41  E-value: 6.70e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521005756   16 GTWGLSNAGLVTSDGEALLVDTLFDLKRTREMLdaMRAATPAAARIGTVVNTHANGDHCYGNALVEGATIIATRASAAEm 95
Cdd:pfam00753   1 LGPGQVNSYLIEGGGGAVLIDTGGSAEAALLLL--LAALGLGPKDIDAVILTHGHFDHIGGLGELAEATDVPVIVVAEE- 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521005756   96 devpapmlamlmrqARSGAAGALGDYLVHcfgAFDFDGIAPTAPTRVFEGELTVTVGAKEVRLLEVGPSHTKGDLLVHVP 175
Cdd:pfam00753  78 --------------ARELLDEELGLAASR---LGLPGPPVVPLPPDVVLEEGDGILGGGLGLLVTHGPGHGPGHVVVYYG 140

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 521005756  176 ADRAIYTGDILFIDVTPILW----------AGPVGNWLKACDTILALDVDVIVPGH 221
Cdd:pfam00753 141 GGKVLFTGDLLFAGEIGRLDlplggllvlhPSSAESSLESLLKLAKLKAAVIVPGH 196
PLN02398 PLN02398
hydroxyacylglutathione hydrolase
 64-187 2.73e-04

hydroxyacylglutathione hydrolase


Pssm-ID: 215223 [Multi-domain]  Cd Length: 329  Bit Score: 42.14  E-value: 2.73e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521005756  64 VVNTHANGDHCYGNALVE---GATIIAtraSAAEMDEVPapmlamlmrqarsGAAGALGDylvhcfgafdfdgiaptAPT 140
Cdd:PLN02398 125 ILNTHHHYDHTGGNLELKaryGAKVIG---SAVDKDRIP-------------GIDIVLKD-----------------GDK 171

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 521005756 141 RVFEGEltvtvgakEVRLLEVgPSHTKGDLLVHVPADRAIYTGDILF 187
Cdd:PLN02398 172 WMFAGH--------EVLVMET-PGHTRGHISFYFPGSGAIFTGDTLF 209
 
Name Accession Description Interval E-value
metallo-hydrolase-like_MBL-fold cd16282
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 7-232 5.16e-67

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: 208.57  E-value: 5.16e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521005756   7 GCFAYLQPAGTWGLSNAGLVTSDGEALLVDTLFDLKRTREMLDAMRAATPAaaRIGTVVNTHANGDHCYGNALV--EGAT 84
Cdd:cd16282    1 GVYALIGPDGGGFISNIGFIVGDDGVVVIDTGASPRLARALLAAIRKVTDK--PVRYVVNTHYHGDHTLGNAAFadAGAP 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521005756  85 IIATRASAAEMDEVPAPMLAMLMRqarsgaagalgdylvhcFGAFDFDGIAPTAPTRVFEGELTVTVGAKEVRLLEVGPS 164
Cdd:cd16282   79 IIAHENTREELAARGEAYLELMRR-----------------LGGDAMAGTELVLPDRTFDDGLTLDLGGRTVELIHLGPA 141

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 521005756 165 HTKGDLLVHVPADRAIYTGDILFIDVTPILWAGPVGNWLKACDTILALDVDVIVPGHGPITDRAGVRA 232
Cdd:cd16282  142 HTPGDLVVWLPEEGVLFAGDLVFNGRIPFLPDGSLAGWIAALDRLLALDATVVVPGHGPVGDKADLRA 209
GloB COG0491
Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General ...
 21-244 2.56e-28

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: 108.62  E-value: 2.56e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521005756  21 SNAGLVTSDGEALLVDTLFDLKRTREMLDAMRAATPaaaRIGTVVNTHANGDHCYGNALVE---GATIIATRASAAEMDE 97
Cdd:COG0491   15 VNSYLIVGGDGAVLIDTGLGPADAEALLAALAALGL---DIKAVLLTHLHPDHVGGLAALAeafGAPVYAHAAEAEALEA 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521005756  98 VPApmlamlmrqarsgaagalgdylvhcfgaFDFDGIAPTAPTRVFEGELTVTVGAKEVRLLEvGPSHTKGDLLVHVPAD 177
Cdd:COG0491   92 PAA----------------------------GALFGREPVPPDRTLEDGDTLELGGPGLEVIH-TPGHTPGHVSFYVPDE 142

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 521005756 178 RAIYTGDILFIDVT--PILWAGPVGNWLKACDTILALDVDVIVPGHGPITDRAGVRAVRDYLVYIRDEA 244
Cdd:COG0491  143 KVLFTGDALFSGGVgrPDLPDGDLAQWLASLERLLALPPDLVIPGHGPPTTAEAIDYLEELLAALGERA 211
SoxH_rel_PQQ_2 TIGR04559
quinoprotein relay system zinc metallohydrolase 2; By homology, members are Zn ...
 61-285 1.11e-25

quinoprotein relay system zinc metallohydrolase 2; By homology, members are Zn metallohydrolases in the same family as the SoxH protein associated with sulfate metabolism, Bacillus cereus beta-lactamase II (see PDB:1bc2), and, more distantly, hydroxyacylglutathione hydrolase (glyoxalase II). All members occur in genomes with both PQQ biosynthesis and a PQQ-dependent (quinoprotein) dehydrogenase that has a motif of two consecutive Cys residues (see TIGR03075). The Cys-Cys motif is associated with electron transfer by specialized cytochromes such as c551. All these genomes also include a fusion protein (TIGR04557) whose domains resemble SoxY and SoxZ from thiosulfate oxidation. A conserved Cys in this fusion protein aligns to the Cys residue in SoxY that carries sulfur cycle intermediates. In many genomes, the genes for PQQ biosynthesis enzymes, PQQ-dependent enzymes, their associated cytochromes, and members of this family are clustered. Note that one to three closely related Zn metallohydrolases may occur; this family represents a specific clade among them. Some members of this family have a short additional N-terminal domain with four conserved Cys residues. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 275352  Cd Length: 283  Bit Score: 103.43  E-value: 1.11e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521005756   61 IGTVVNTHANGDHCYGNA--LVEGATIIATRASAAEMDEVPAPMLAMLMRQarsgaagaLGDylvhcfgafDFDGIAPTA 138
Cdd:TIGR04559  68 IRYVINTHVHPDHIFGNAafREDGAEFVGHAKLPRALAARGEFYLASFARL--------LGE---------AFLGTEIVP 130

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521005756  139 PTRVFEGELTVTVGAKEVRLLEVGPSHTKGDLLVHVPADRAIYTGDILFIDVTPILwAGPVGNWLKACDTILALDVDVIV 218
Cdd:TIGR04559 131 PTRLVADPLELDLGGRVLELTAWPTAHTDNDLTVFDEKTGTLFTGDLLFVEHIPVL-DGSLLGWLAVLDRLKARPAARVV 209

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521005756  219 PGHGPIT--DRAGVRAVRDYLVYIRDEARRRYDAGMPPADAARDIALADYASWSDAERI-AVNVHTLYRE 285
Cdd:TIGR04559 210 PGHGPVSldWPAALAPQRRYLETLRDDVRAAIKDGLPLEEAVETAAQSEKGKWALFDEYnRRNVTAAYAE 279
SoxH_rel_PQQ_1 TIGR04558
quinoprotein relay system zinc metallohydrolase 1; By homology, members are Zn ...
 61-266 2.82e-19

quinoprotein relay system zinc metallohydrolase 1; By homology, members are Zn metallohydrolases in the same family as the SoxH protein associated with sulfate metabolism, Bacillus cereus beta-lactamase II (see PDB:1bc2), and, more distantly, hydroxyacylglutathione hydrolase (glyoxalase II). All members occur in genomes with both PQQ biosynthesis and a PQQ-dependent (quinoprotein) dehydrogenase that has a motif of two consecutive Cys residues (see TIGR03075). The Cys-Cys motif is associated with electron transfer by specialized cytochromes such as c551. All these genomes also include a fusion protein (TIGR04557) whose domains resemble SoxY and SoxZ from thiosulfate oxidation. A conserved Cys in this fusion protein aligns to the Cys residue in SoxY that carries sulfur cycle intermediates. In many genomes, the genes for PQQ biosynthesis enzymes, PQQ-dependent enzymes, their associated cytochromes, and members of this family are clustered. Note that one to three closely related Zn metallohydrolases may occur; this family represents a specific clade among them. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 275351 [Multi-domain]  Cd Length: 285  Bit Score: 85.78  E-value: 2.82e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521005756   61 IGTVVNTHANGDHCYGNALVEGATIIATRASAAEMDEVPAPMLAMLMRqarsgaagALGDYLvhcfgafdfDGIAPTAPT 140
Cdd:TIGR04558  72 VRRVLNTHHHPDHFLGNQAFADVPIAALPATIAGIRAEGDAYADNMYR--------LVGDWM---------RGTEPVPPN 134

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521005756  141 RVFEGElTVTVGAKEVRLLEVgPSHTKGDLLVHVPADRAIYTGDILFIDVTPILWAGPVGNWLKACDTILALDVDVIVPG 220
Cdd:TIGR04558 135 EALEAG-PLTIGGRRLELLAL-SGHTGADLVILDEATGVLFAGDLVFLDRAPTTPHADLADWLASLDRLEALPAKVLVPG 212

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 521005756  221 HGPIT-DRAGVRAVRDYLVY----IRDEARRRYDA----GMPPADAARDIALADY 266
Cdd:TIGR04558 213 HGPVDrDGAGIAQTRDYLAWldatLRDAAERGLDMtevmALPIPERFAGLAAAPA 267
metallo-hydrolase-like_MBL-fold cd16276
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 61-232 1.63e-18

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: 81.48  E-value: 1.63e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521005756  61 IGTVVNTHANGDHCYGNALV--EGATIIATRASAAEMDEVPAPMLAMlmrqarsgaagalgdylvhcfgafdfdgiapta 138
Cdd:cd16276   46 VTHVVYSHNHADHIGGASIFkdEGATIIAHEATAELLKRNPDPKRPV--------------------------------- 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521005756 139 PTRVFEGELTVTVGAKEVRLLEVGPSHTKGDLLVHVPADRAIYTGDILFIDVTPILWAGP---VGNWLKACDTILALDVD 215
Cdd:cd16276   93 PTVTFDDEYTLEVGGQTLELSYFGPNHGPGNIVIYLPKQKVLMAVDLINPGWVPFFNFAGsedIPGYIEALDELLEYDFD 172

                        170
                 ....*....|....*..
gi 521005756 216 VIVPGHGPitdRAGVRA 232
Cdd:cd16276  173 TFVGGHGN---RLGTRE 186
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 22-221 9.00e-18

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: 79.13  E-value: 9.00e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521005756    22 NAGLVTSDGEALLVDTLFDlkrtREMLDAMRAATPAAARIGTVVNTHANGDHCYGNALVEGATIIATRASAAEMDEVPAP 101
Cdd:smart00849   1 NSYLVRDDGGAILIDTGPG----EAEDLLAELKKLGPKKIDAIILTHGHPDHIGGLPELLEAPGAPVYAPEGTAELLKDL 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521005756   102 MLAMlmrqarsgaagalgdylvhcfGAFDFDGIAPTAPTRVFEGElTVTVGAKEVRLLEVgPSHTKGDLLVHVPADRAIY 181
Cdd:smart00849  77 LALL---------------------GELGAEAEPAPPDRTLKDGD-ELDLGGGELEVIHT-PGHTPGSIVLYLPEGKILF 133

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 521005756   182 TGDILFIDVTPILWAGPVG----NWLKACDTILALDVDVIVPGH 221
Cdd:smart00849 134 TGDLLFAGGDGRTLVDGGDaaasDALESLLKLLKLLPKLVVPGH 177
Lactamase_B pfam00753
Metallo-beta-lactamase superfamily;
16-221 6.70e-17

Metallo-beta-lactamase superfamily;


Pssm-ID: 425851 [Multi-domain]  Cd Length: 196  Bit Score: 77.41  E-value: 6.70e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521005756   16 GTWGLSNAGLVTSDGEALLVDTLFDLKRTREMLdaMRAATPAAARIGTVVNTHANGDHCYGNALVEGATIIATRASAAEm 95
Cdd:pfam00753   1 LGPGQVNSYLIEGGGGAVLIDTGGSAEAALLLL--LAALGLGPKDIDAVILTHGHFDHIGGLGELAEATDVPVIVVAEE- 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521005756   96 devpapmlamlmrqARSGAAGALGDYLVHcfgAFDFDGIAPTAPTRVFEGELTVTVGAKEVRLLEVGPSHTKGDLLVHVP 175
Cdd:pfam00753  78 --------------ARELLDEELGLAASR---LGLPGPPVVPLPPDVVLEEGDGILGGGLGLLVTHGPGHGPGHVVVYYG 140

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 521005756  176 ADRAIYTGDILFIDVTPILW----------AGPVGNWLKACDTILALDVDVIVPGH 221
Cdd:pfam00753 141 GGKVLFTGDLLFAGEIGRLDlplggllvlhPSSAESSLESLLKLAKLKAAVIVPGH 196
metallo-hydrolase-like_MBL-fold cd07739
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 14-221 5.60e-16

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: 74.85  E-value: 5.60e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521005756  14 PAGTWGLSNAGLVTSDGEALLVDTLFDLKRTREMLDAMRAATPaaaRIGTVVNTHANGDHCYG-NALVE---GATIIATR 89
Cdd:cd07739    9 PEISSFPVTSTLIYGETEAVLVDAQFTRADAERLADWIKASGK---TLTTIYITHGHPDHYFGlEVLLEafpDAKVVATP 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521005756  90 ASAAEMDEVPAPMLAmlmrqarsgaagalgdylvhcFGAFDFDGIAPTAPT--RVFEGElTVTVGAKEVRLLEVGPSHTK 167
Cdd:cd07739   86 AVVAHIKAQLEPKLA---------------------FWGPLLGGNAPARLVvpEPLDGD-TLTLEGHPLEIVGVGGGDTD 143

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 521005756 168 GDLLVHVPADRAIYTGDILFIDV--------TPILWAgpvgNWLKACDTILALDVDVIVPGH 221
Cdd:cd07739  144 DTTYLWIPSLKTVVAGDVVYNGVhvwladatTPELRA----AWLAALDKIEALNPETVVPGH 201
metallo-hydrolase-like_MBL-fold cd06262
mainly hydrolytic enzymes and related proteins which carry out various biological functions; ...
 21-221 4.62e-12

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: 63.84  E-value: 4.62e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521005756  21 SNAGLV-TSDGEALLVDTLFD-LKRTREMLDAMRAatpaaaRIGTVVNTHANGDHCYGNA-LVE--GATIIATRAsAAEM 95
Cdd:cd06262   10 TNCYLVsDEEGEAILIDPGAGaLEKILEAIEELGL------KIKAILLTHGHFDHIGGLAeLKEapGAPVYIHEA-DAEL 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521005756  96 DEVPAPMLAMLMrqarsgaagalgdylvhcfgafdFDGIAPTAPTRVFEGELTVTVGAKEVRLLEVgPSHTKGDLLVHVP 175
Cdd:cd06262   83 LEDPELNLAFFG-----------------------GGPLPPPEPDILLEDGDTIELGGLELEVIHT-PGHTPGSVCFYIE 138

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 521005756 176 ADRAIYTGDILFiDVTPILWAGPVGNWLKACDTILAL-----DVDVIVPGH 221
Cdd:cd06262  139 EEGVLFTGDTLF-AGSIGRTDLPGGDPEQLIESIKKLllllpDDTVVYPGH 188
MBL-B1-B2-like cd07707
metallo-beta-lactamases; subclasses B1 and B2 and related proteins; MBL-fold metallo-hydrolase ...
 21-226 3.44e-11

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: 61.79  E-value: 3.44e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521005756  21 SNAGLVTSDGEALLVDTLFDLKRTREMLDAMRAATPAaaRIGTVVNTHANGDHCYGNALVE--GATIIATRaSAAEMDEV 98
Cdd:cd07707   21 SNGLVYNGSKGLVLVDSTWTPKTTKELIKEIEKVSQK--PVTEVINTHFHTDRAGGNAYLKerGAKTVSTA-LTRDLAKS 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521005756  99 PAPMLAMLMRQarsgaagalgdylvhcfGAFDFDGIAPTAPTRVFEGEltVTVGAKEVRLLEVGPSHTKGDLLVHVPADR 178
Cdd:cd07707   98 EWAEIVAFTRK-----------------GLPEYPDLGYELPDGVLDGD--FNLQFGKVEAFYPGPAHTPDNIVVYFPQEN 158

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 521005756 179 AIYTGDILFIDVTPILWAGPVGNWLKACDTILALD--VDVIVPGHGPITD 226
Cdd:cd07707  159 VLYGGCIIKETDLGNVADADVKEWPTSIERLKKRYrnIKAVIPGHGEVGG 208
CphA_ImiS-like_MBL-B2 cd16306
Aeromonas hydrophyla CphA, Aeromonas veronii ImiS, and related metallo-beta-lactamases, ...
 61-221 3.26e-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: 56.11  E-value: 3.26e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521005756  61 IGTVVNTHANGDHCYGNALVE--GATIIATRASAAEM----DEVPApmlamLMRQarsgaagalgdylvhcfGAFDFDGI 134
Cdd:cd16306   59 VLEVINTNYHTDRAGGNAYWKsiGAKVVSTRQTRDLMksdwAEIVA-----FTRK-----------------GLPEYPDL 116

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521005756 135 APTAPTRVFEGELTVTVGakEVRLLEVGPSHTKGDLLVHVPADRAIYTGDILFIDVTPILWAGpVGNWLKACD--TILAL 212
Cdd:cd16306  117 PLVLPNVVHDGDFTLQEG--KVRAFYLGPAHTPDGIFVYFPDEQVLYGNCILKEKLGNLSFAD-VKAYPQTLErlKAMKL 193


                 ....*....
gi 521005756 213 DVDVIVPGH 221
Cdd:cd16306  194 PIKTVIGGH 202
metallo-hydrolase-like_MBL-fold cd07743
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 19-221 4.79e-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) 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: 55.23  E-value: 4.79e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521005756  19 GLSNAGL-VTSDGEALLVDTLFD---LKRTREMLDAMRAatpaaaRIGTVVNTHANGDHCYGNA-LVE--GATIIATRAS 91
Cdd:cd07743    6 GPTNIGVyVFGDKEALLIDSGLDedaGRKIRKILEELGW------KLKAIINTHSHADHIGGNAyLQKktGCKVYAPKIE 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521005756  92 AAEMDEvpaPMLAMLMRQARSGAAGALGDYLVhcfgafdfdgIAPTAPTRVFEgELTVTVGAKEVRLLEVgPSHTKGDLL 171
Cdd:cd07743   80 KAFIEN---PLLEPSYLGGAYPPKELRNKFLM----------AKPSKVDDIIE-EGELELGGVGLEIIPL-PGHSFGQIG 144

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 521005756 172 VHVPaDRAIYTGDILF----IDVTPILWAGPVGNWLKACDTILALDVDVIVPGH 221
Cdd:cd07743  145 ILTP-DGVLFAGDALFgeevLEKYGIPFLYDVEEQLETLEKLEELDADYYVPGH 197
AHL_lactonase_MBL-fold cd07729
quorum-quenching N-acyl-homoserine lactonase, MBL-fold metallo-hydrolase domain; Acyl ...
 61-221 1.78e-07

quorum-quenching N-acyl-homoserine lactonase, MBL-fold metallo-hydrolase domain; Acyl Homoserine Lactones (also known as AHLs) are signal molecules which coordinate gene expression in quorum sensing, in many Gram-negative bacteria. Quorum-quenching N-acyl-homoserine lactonase (also known as AHL lactonase, N-acyl-L-homoserine lactone hydrolase, EC 3.1.1.81) catalyzes the hydrolysis and opening of the homoserine lactone rings of AHLs, a reaction that can block quorum sensing. These enzymes belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions.


Pssm-ID: 293815 [Multi-domain]  Cd Length: 238  Bit Score: 51.06  E-value: 1.78e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521005756  61 IGTVVNTHANGDHCYGNALVEGATIIATRasaAEMDevpapmlamlmrQARSGAAGALGDYLVHCFGAFDFDGIaptaPT 140
Cdd:cd07729   89 IDYVILSHLHFDHAGGLDLFPNATIIVQR---AELE------------YATGPDPLAAGYYEDVLALDDDLPGG----RV 149

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521005756 141 RVFEGELTVTVGakeVRLLEVgPSHTKG--DLLVHVPADRAIYTGDI------LFIDVTPILWAGPVgNWLKACDTILAL 212
Cdd:cd07729  150 RLVDGDYDLFPG---VTLIPT-PGHTPGhqSVLVRLPEGTVLLAGDAaytyenLEEGRPPGINYDPE-AALASLERLKAL 224

                        170
                 ....*....|..
gi 521005756 213 ---DVDVIVPGH 221
Cdd:cd07729  225 aerEGARVIPGH 236
TTHA1623-like_MBL-fold cd16322
uncharacterized Thermus thermophilus TTHA1623 and related proteins; MBL-fold metallo hydrolase ...
 21-225 1.45e-06

uncharacterized Thermus thermophilus TTHA1623 and related proteins; MBL-fold metallo hydrolase domain; Includes the MBL-fold metallo hydrolase domain of uncharacterized Thermus thermophilus TTHA1623 and related proteins. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions. This family includes homologs present in a wide range of bacteria and archaea and some eukaryota. Members of the MBL-fold metallo-hydrolase superfamily exhibit a variety of active site metallo-chemistry, TTHA1623 exhibiting a uniquely shaped putative substrate-binding pocket with a glyoxalase II-type metal-coordination mode.


Pssm-ID: 293877 [Multi-domain]  Cd Length: 204  Bit Score: 48.11  E-value: 1.45e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521005756  21 SNAGLVTSD--GEALLVDTLFDlkrTREMLDAMRAATPaaaRIGTVVNTHANGDHCYGNALVEgatiiatRASAAEM--- 95
Cdd:cd16322   11 ENTYLVADEggGEAVLVDPGDE---SEKLLARFGTTGL---TLLYILLTHAHFDHVGGVADLR-------RHPGAPVylh 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521005756  96 -DEVPapmlamLMRQARSGAAgalgdylvhcfgAFDFDGIAPTAPTRVFEGELTVTVGAKEVRLLEVgPSHTKGDLLVHV 174
Cdd:cd16322   78 pDDLP------LYEAADLGAK------------AFGLGIEPLPPPDRLLEDGQTLTLGGLEFKVLHT-PGHSPGHVCFYV 138

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 521005756 175 PADRAIYTGDILFidvtpilwAGPVGNW-LKACD---------TILALDVDV-IVPGHGPIT 225
Cdd:cd16322  139 EEEGLLFSGDLLF--------QGSIGRTdLPGGDpkamaaslrRLLTLPDETrVFPGHGPPT 192
CcrA-like_MBL-B1 cd16302
Bacteroides fragilis CcrA and related metallo-beta-lactamases, subclass B1; MBL-fold ...
 10-226 2.30e-06

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: 47.62  E-value: 2.30e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521005756  10 AYLQpAGTWGL--SNAGLVTSDGEALLVDTLFDLKRTREMLDAMRAATPAaaRIGTVVNTHANGDhCYG--NALVEGAti 85
Cdd:cd16302   15 SYLE-TETFGKvpCNGMIVINGGEAVVFDTPTNDSQSEELIDWIENSLKA--KVKAVVPTHFHDD-CLGglKAFHRRG-- 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521005756  86 IATRASAaemdevpapMLAMLMRQarsgaagalgdylvhcfgafdfDGIAPtaPTRVFEGELTVTVGAKEVRLLEVGPSH 165
Cdd:cd16302   89 IPSYANQ---------KTIALAKE----------------------KGLPV--PQHGFSDSLTLKLGGKKIVCRYFGEGH 135

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 521005756 166 TKGDLLVHVPADraiytgDILF-------IDVTpilwAG-----PVGNWLKACDTILAL--DVDVIVPGHGPITD 226
Cdd:cd16302  136 TKDNIVVYFPSE------KVLFggcmvksLGAG----KGnledaNVEAWPKTVEKVKAKypDVKIVIPGHGKIGG 200
TTHA1429-like_MBL-fold cd07725
uncharacterized Thermus thermophilus TTHA1429 and related proteins; MBL-fold metallo hydrolase ...
 22-228 2.31e-06

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: 47.29  E-value: 2.31e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521005756  22 NAGLVTSDGEALLVDTLFDLKRTREML-DAMRAATPAAARIGTVVNTHANGDHCygnalvegatiiatrasaaemdevpa 100
Cdd:cd07725   16 NVYLLRDGDETTLIDTGLATEEDAEALwEGLKELGLKPSDIDRVLLTHHHPDHI-------------------------- 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521005756 101 pmlamlmrqarsGAAGalgdYLVHCFGAfdfDGIAPTaPTRVFEGElTVTVGAKEVRLLEVgPSHTKGDLLVHVPADRAI 180
Cdd:cd07725   70 ------------GLAG----KLQEKSGA---TVYILD-VTPVKDGD-KIDLGGLRLKVIET-PGHTPGHIVLYDEDRREL 127

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 521005756 181 YTGDILFIDVTP--ILWA----GPVGNWLKACDTILALDVDVIVPGHG-PITDRA 228
Cdd:cd07725  128 FVGDAVLPKITPnvSLWAvrveDPLGAYLESLDKLEKLDVDLAYPGHGgPIKDPK 182
MBLAC2-like_MBL-fold cd07712
uncharacterized human metallo-beta-lactamase domain-containing protein 2 and related proteins; ...
 25-221 4.33e-06

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: 46.47  E-value: 4.33e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521005756  25 LVTSDGEALLVDT---LFDLKR-TREMLDAMRaatpaaarigTVVNTHANGDHCYGNAlvegatiiatrasaaEMDEVpa 100
Cdd:cd07712   13 LLRGRDRALLIDTglgIGDLKEyVRTLTDLPL----------LVVATHGHFDHIGGLH---------------EFEEV-- 65

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521005756 101 pmlamLMRQARSGAAgALGDYLVHCFGAFDFDGIAPTAPTRVF-EGELtVTVGAKEVRLLEVgPSHTKGDLLVHVPADRA 179
Cdd:cd07712   66 -----YVHPADAEIL-AAPDNFETLTWDAATYSVPPAGPTLPLrDGDV-IDLGDRQLEVIHT-PGHTPGSIALLDRANRL 137

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 521005756 180 IYTGDIlFIDVTPILWAG--PVGNWLKACDTILAL--DVDVIVPGH 221
Cdd:cd07712  138 LFSGDV-VYDGPLIMDLPhsDLDDYLASLEKLSKLpdEFDKVLPGH 182
Sfh-1-like_MBL-B2 cd16305
Serratia fonticola Sfh-I and related metallo-beta-lactamases, subclass B2; MBL-fold ...
 61-242 5.39e-05

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: 43.83  E-value: 5.39e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521005756  61 IGTVVNTHANGDHCYGNALVE--GATIIATRASAaEMDEVPAPMLAMLMRQarsgaagalgdylvhcfGAFDFDGIAPTA 138
Cdd:cd16305   59 IKEVINTNYHTDRAGGNAYWKtlGASIVSTQMTY-DLEKSQWGSIVDFTRQ-----------------GNNKYPNLEKSL 120

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521005756 139 PTRVFEGELTVTVGakEVRLLEVGPSHTKGDLLVHVPADRAIYTGDILFIDVTPILWAG--PVGNWLKACDTILA---LD 213
Cdd:cd16305  121 PDTVYPGDFNLQNG--SVRALYLGEAHTEDGIFVYFPAERVLYGNCILKEKLGNMSFANrtEYPKTLKKLKGLIEqgeLK 198

                        170       180       190
                 ....*....|....*....|....*....|
gi 521005756 214 VDVIVPGHG-PITDragVRAVRDYLVYIRD 242
Cdd:cd16305  199 VESIIAGHDtPIHD---VELIDHYLTLLEK 225
hydroxyacylglutathione_hydrolase_MBL-fold cd07723
hydroxyacylglutathione hydrolase, MBL-fold metallo-hydrolase domain; hydroxyacylglutathione ...
 142-221 1.84e-04

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: 41.29  E-value: 1.84e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521005756 142 VFEGElTVTVGAKEVRLLEVgPSHTKGDLLVHVPADRAIYTGDILFIdvtpilwAGpVGNW--------LKACDTILALD 213
Cdd:cd07723   87 VKDGD-EIKLGGLEVKVLHT-PGHTLGHICYYVPDEPALFTGDTLFS-------GG-CGRFfegtaeqmYASLQKLLALP 156


                 ....*....
gi 521005756 214 VDVIV-PGH 221
Cdd:cd07723  157 DDTLVyCGH 165
arylsulfatase_Sdsa1-like_MBL-fold cd07710
Pseudomonas aeruginosa arylsulfatase SdsA1, Pseudomonas sp. DSM6611 arylsulfatase Pisa1, and ...
 18-222 2.34e-04

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: 41.72  E-value: 2.34e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521005756  18 WGLSNAGLVTSDGEALLVDTLFDLKRTREMLDAMRAATPAAArIGTVVNTHANGDHCYG-NALVEGAT-----IIAtras 91
Cdd:cd07710   15 YDLSNMTFIEGDTGLIIIDTLESAEAAKAALELFRKHTGDKP-VKAIIYTHSHPDHFGGaGGFVEEEDsgkvpIIA---- 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521005756  92 aaemdevPAPMLAMLMRQARsGAAGALGDYLVHCFGAF--------DFDGIAPT---------APTRVFEGE-LTVTVGA 153
Cdd:cd07710   90 -------PEGFMEEAVSENV-LAGNAMSRRAAYQFGALlpkgekgqVGAGLGPGlstgtvgfiPPTITITETgETLTIDG 161

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 521005756 154 KEVRLLEVgPSHTKGDLLVHVPADRAIYTGDIL---FIDVTPILWAGP--VGNWLKACDTILALDVDVIVPGHG 222
Cdd:cd07710  162 VELEFQHA-PGEAPDEMMVWLPDYKVLFCADNVyhtFPNLYTLRGAKYrdALAWAKSLDEAISLKAEVLFPSHT 234
PLN02398 PLN02398
hydroxyacylglutathione hydrolase
 64-187 2.73e-04

hydroxyacylglutathione hydrolase


Pssm-ID: 215223 [Multi-domain]  Cd Length: 329  Bit Score: 42.14  E-value: 2.73e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521005756  64 VVNTHANGDHCYGNALVE---GATIIAtraSAAEMDEVPapmlamlmrqarsGAAGALGDylvhcfgafdfdgiaptAPT 140
Cdd:PLN02398 125 ILNTHHHYDHTGGNLELKaryGAKVIG---SAVDKDRIP-------------GIDIVLKD-----------------GDK 171

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 521005756 141 RVFEGEltvtvgakEVRLLEVgPSHTKGDLLVHVPADRAIYTGDILF 187
Cdd:PLN02398 172 WMFAGH--------EVLVMET-PGHTRGHISFYFPGSGAIFTGDTLF 209
yflN-like_MBL-fold cd07721
uncharacterized subgroup which includes Bacillus subtilis yflN; MBL-fold metallo hydrolase ...
 21-222 3.75e-04

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: 40.67  E-value: 3.75e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521005756  21 SNAGLVTSDGEALLVDT--LFDLKRtreMLDAMRAATPAAARIGTVVNTHANGDHcYGNA--LVE--GATIIAtraSAAE 94
Cdd:cd07721   11 VNAYLIEDDDGLTLIDTglPGSAKR---ILKALRELGLSPKDIRRILLTHGHIDH-IGSLaaLKEapGAPVYA---HERE 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521005756  95 mdevpAPMLAmlmrqarsgaagalGD--YLVHCFGAFdFDGIAPTAPTRVFEGELTVTVGakeVRLLEVG-------PSH 165
Cdd:cd07721   84 -----APYLE--------------GEkpYPPPVRLGL-LGLLSPLLPVKPVPVDRTLEDG---DTLDLAGglrvihtPGH 140

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 521005756 166 TKGDLLVHVPADRAIYTGDILFIDVTPILWAGPVGNW-----LKACDTILALDVDVIVPGHG 222
Cdd:cd07721  141 TPGHISLYLEEDGVLIAGDALVTVGGELVPPPPPFTWdmeeaLESLRKLAELDPEVLAPGHG 202
CphS_ImiS-like_MBL-B2 cd16287
metallo-beta-lactamases, subclass B2; MBL-fold metallo-hydrolase domain; Includes Aeromonas ...
 64-186 6.53e-04

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: 40.49  E-value: 6.53e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521005756  64 VVNTHANGDHCYGNALVE--GATIIATRASAAEMDEVPAPMLAMLMRqarsgaagalgdylvhcfGAFDFDGIAPTAPTR 141
Cdd:cd16287   62 VINTNYHTDRAGGNAYWKtlGAKIVATQMTYDLQKSQWGSIVNFTRQ------------------GNNKYPNLEKSLPDT 123

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 521005756 142 VFEGELTVTVGakEVRLLEVGPSHTKGDLLVHVPADRAIYTGDIL 186
Cdd:cd16287  124 VFPGDFNLQNG--SIRAMYLGEAHTKDGIFVYFPAERVLYGNCIL 166
YmaE-like_MBL-fold cd07727
uncharacterized subgroup which includes Bacillus subtilis YmaE and related proteins; MBL-fold ...
 142-222 1.33e-03

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


Pssm-ID: 293813 [Multi-domain]  Cd Length: 181  Bit Score: 39.10  E-value: 1.33e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521005756 142 VFEGELTVTvGAKEVRLLEVgPSHTKGDLLVHVPADRAIYTGDIL-----------FIDVTPILWAGPVGNWLKacdtIL 210
Cdd:cd07727   91 VLWGGDPWE-LDPDLTLIPV-PGHTRGSVVLLYKEKGVLFTGDHLawsrrrgwlsaFRYVCWYSWPEQAESVER----LA 164

                         90
                 ....*....|..
gi 521005756 211 ALDVDVIVPGHG 222
Cdd:cd07727  165 DLDFEWVLPGHG 176
flavodiiron_proteins_MBL-fold cd07709
catalytic domain of flavodiiron proteins (FDPs) and related proteins; MBL-fold ...
 21-237 2.81e-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: 38.62  E-value: 2.81e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521005756  21 SNAGLVTsDGEALLVDT----LFD--LKRTREMLDAMraatpaaaRIGTVVNTHANGDHCYG-NALVE---GATIIATRA 90
Cdd:cd07709   32 YNSYLIK-DEKTALIDTvkepFFDefLENLEEVIDPR--------KIDYIVVNHQEPDHSGSlPELLElapNAKIVCSKK 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521005756  91 sAAEMdevpapmlamlmrqarsgaagalgdyLVHCFGAFDFDGIAptaptrVFEGElTVTVGAKEVRLLEVgPS-HTKGD 169
Cdd:cd07709  103 -AARF--------------------------LKHFYPGIDERFVV------VKDGD-TLDLGKHTLKFIPA-PMlHWPDT 147

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521005756 170 LLVHVPADRAIYTGDI---------LFIDVTPILWA----------GPVGNW-LKACDTILALDVDVIVPGHGPITDRAG 229
Cdd:cd07709  148 MVTYDPEDKILFSGDAfgahgasgeLFDDEVEDYLEearryyanimGPFSKQvRKALEKLEALDIKMIAPSHGPIWRKDP 227


                 ....*...
gi 521005756 230 VRAVRDYL 237
Cdd:cd07709  228 GEIIDLYR 235
 
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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