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Conserved domains on  [gi|492459440|ref|WP_005852038|]
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MULTISPECIES: GNAT family N-acetyltransferase [Phocaeicola]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
VOC super family cl14632
vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate (VOC) superfamily is composed ...
 2-126 8.28e-67

vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate (VOC) superfamily is composed of structurally related proteins with paired beta.alpha.beta.beta.beta motifs that provide a metal coordination environment with two or three open or readily accessible coordination sites to promote direct electrophilic participation of the metal ion in catalysis. VOC is found in a variety of structurally related metalloproteins, including the type I extradiol dioxygenases, glyoxalase I and a group of antibiotic resistance proteins. A bound metal ion is required for protein activities for the members of this superfamily. A variety of metal ions have been found in the catalytic centers of these proteins including Fe(II), Mn(II), Zn(II), Ni(II) and Mg(II). Type I extradiol dioxygenases catalyze the incorporation of both atoms of molecular oxygen into aromatic substrates, which results in the cleavage of aromatic rings. They are key enzymes in the degradation of aromatic compounds. Type I extradiol dioxygenases include class I and class II enzymes. Class I and II enzymes show sequence similarity; the two-domain class II enzymes evolved from a class I enzyme through gene duplication. Glyoxylase I catalyzes the glutathione-dependent inactivation of toxic methylglyoxal, requiring zinc or nickel ions for activity. The antibiotic resistance proteins in this family use a variety of mechanisms to block the function of antibiotics. Bleomycin resistance protein (BLMA) sequesters bleomycin's activity by directly binding to it. Whereas, three types of fosfomycin resistance proteins employ different mechanisms to render fosfomycin inactive by modifying the fosfomycin molecule. Although the proteins in this superfamily are functionally distinct, their structures are similar. The difference among the three dimensional structures of the three types of proteins in this superfamily is interesting from an evolutionary perspective. Both glyoxalase I and BLMA show domain swapping between subunits. However, there is no domain swapping for type 1 extradiol dioxygenases.


The actual alignment was detected with superfamily member cd07241:

Pssm-ID: 472697  Cd Length: 125  Bit Score: 204.95  E-value: 8.28e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492459440   2 KIHHIAIWTFHLEKLREFYTRYFNGTSNEKYINSQKGFESYFISFESGATLELMSRIDVQNIPIEENRPGLTHLAFSFES 81
Cdd:cd07241    1 KIEHVALWTNDLERMKDFYVKYFGAESNDIYHNKKKGFRSYFLTFDSGARLELMSRPDVTDPDKEVERTGLAHIAFSVGS 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 492459440  82 QEAVLSLTEQLRTKGYHIVGEPRISGDGYFESVILDPDGNRIECV 126
Cdd:cd07241   81 KEAVDELTERLRADGYAVVGGPRTTGDGYYESVILDPEGNRIEIT 125
RimL COG1670
Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, ...
 140-309 1.32e-48

Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, Posttranslational modification, protein turnover, chaperones];


:

Pssm-ID: 441276 [Multi-domain]  Cd Length: 173  Bit Score: 160.16  E-value: 1.32e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492459440 140 VIETERLILRPFTENDTEAVFNCCQNPNLGNNAGWKPHdTLEESLKILQTIFIPQKD----TWAITRKEDRLLIGAIGIL 215
Cdd:COG1670    2 TLETERLRLRPLRPEDAEALAELLNDPEVARYLPGPPY-SLEEARAWLERLLADWADggalPFAIEDKEDGELIGVVGLY 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492459440 216 PDPKRENSnaGMIGYWLDEAQWGKGYMSEAVCAVLDYGFNKLGLTLISANCYPQNKRSQRVLEKMGFTYEGILHQAEVsY 295
Cdd:COG1670   81 DIDRANRS--AEIGYWLAPAYWGKGYATEALRALLDYAFEELGLHRVEAEVDPDNTASIRVLEKLGFRLEGTLRDALV-I 157

                        170
                 ....*....|....
gi 492459440 296 DDKIYDHLCYYLEK 309
Cdd:COG1670  158 DGRYRDHVLYSLLR 171
 
Name Accession Description Interval E-value
VOC_BsYyaH cd07241
vicinal oxygen chelate (VOC) family protein similar to Bacillus subtilis YyaH; The vicinal ...
 2-126 8.28e-67

vicinal oxygen chelate (VOC) family protein similar to Bacillus subtilis YyaH; The vicinal oxygen chelate (VOC) superfamily is composed of structurally related proteins with paired beta.alpha.beta.beta.beta motifs that provide a metal coordination environment with two or three open or readily accessible coordination sites to promote direct electrophilic participation of the metal ion in catalysis. VOC domain is found in a variety of structurally related metalloproteins, including the bleomycin resistance protein, glyoxalase I, and type I ring-cleaving dioxygenases. A bound metal ion is required for protein activities for the members of this superfamily. A variety of metal ions have been found in the catalytic centers of these proteins including Fe(II), Mn(II), Zn(II), Ni(II) and Mg(II). The protein superfamily contains members with or without domain swapping. The proteins of this family share three conserved metal binding amino acids with the type I extradiol dioxygenases, which shows no domain swapping.


Pssm-ID: 319905  Cd Length: 125  Bit Score: 204.95  E-value: 8.28e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492459440   2 KIHHIAIWTFHLEKLREFYTRYFNGTSNEKYINSQKGFESYFISFESGATLELMSRIDVQNIPIEENRPGLTHLAFSFES 81
Cdd:cd07241    1 KIEHVALWTNDLERMKDFYVKYFGAESNDIYHNKKKGFRSYFLTFDSGARLELMSRPDVTDPDKEVERTGLAHIAFSVGS 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 492459440  82 QEAVLSLTEQLRTKGYHIVGEPRISGDGYFESVILDPDGNRIECV 126
Cdd:cd07241   81 KEAVDELTERLRADGYAVVGGPRTTGDGYYESVILDPEGNRIEIT 125
RimL COG1670
Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, ...
 140-309 1.32e-48

Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 441276 [Multi-domain]  Cd Length: 173  Bit Score: 160.16  E-value: 1.32e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492459440 140 VIETERLILRPFTENDTEAVFNCCQNPNLGNNAGWKPHdTLEESLKILQTIFIPQKD----TWAITRKEDRLLIGAIGIL 215
Cdd:COG1670    2 TLETERLRLRPLRPEDAEALAELLNDPEVARYLPGPPY-SLEEARAWLERLLADWADggalPFAIEDKEDGELIGVVGLY 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492459440 216 PDPKRENSnaGMIGYWLDEAQWGKGYMSEAVCAVLDYGFNKLGLTLISANCYPQNKRSQRVLEKMGFTYEGILHQAEVsY 295
Cdd:COG1670   81 DIDRANRS--AEIGYWLAPAYWGKGYATEALRALLDYAFEELGLHRVEAEVDPDNTASIRVLEKLGFRLEGTLRDALV-I 157

                        170
                 ....*....|....
gi 492459440 296 DDKIYDHLCYYLEK 309
Cdd:COG1670  158 DGRYRDHVLYSLLR 171
Acetyltransf_3 pfam13302
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 145-283 2.44e-37

Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.


Pssm-ID: 379112 [Multi-domain]  Cd Length: 139  Bit Score: 129.77  E-value: 2.44e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492459440  145 RLILRPFTENDTEAVFNCCQNPNLgnNAGWKPHD-TLEESLKILQTIFIPQKD----TWAITRKEDRLlIGAIGIlpDPK 219
Cdd:pfam13302   1 RLLLRPLTEEDAEALFELLSDPEV--MRYGVPWPlTLEEAREWLARIWAADEAergyGWAIELKDTGF-IGSIGL--YDI 75

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 492459440  220 RENSNAGMIGYWLDEAQWGKGYMSEAVCAVLDYGFNKLGLTLISANCYPQNKRSQRVLEKMGFT 283
Cdd:pfam13302  76 DGEPERAELGYWLGPDYWGKGYATEAVRALLEYAFEELGLPRLVARIDPENTASRRVLEKLGFK 139
GloA COG0346
Catechol 2,3-dioxygenase or related enzyme, vicinal oxygen chelate (VOC) family [Secondary ...
 1-130 4.32e-25

Catechol 2,3-dioxygenase or related enzyme, vicinal oxygen chelate (VOC) family [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 440115 [Multi-domain]  Cd Length: 125  Bit Score: 97.37  E-value: 4.32e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492459440   1 MKIHHIAIWTFHLEKLREFYTRYFNGTSNEKYINSQKGFESYFISFESGATLELMSRIDVQNIPieeNRPGLTHLAFSFE 80
Cdd:COG0346    1 MGLHHVTLRVSDLEASLAFYTDVLGLELVKRTDFGDGGFGHAFLRLGDGTELELFEAPGAAPAP---GGGGLHHLAFRVD 77

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 492459440  81 SQEAVLsltEQLRTKGYHIVGEPRISGDGYFESVILDPDGNRIECVYKKE 130
Cdd:COG0346   78 DLDAAY---ARLRAAGVEIEGEPRDRAYGYRSAYFRDPDGNLIELVEPPP 124
Glyoxalase pfam00903
Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;
2-124 2.38e-17

Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;


Pssm-ID: 395724 [Multi-domain]  Cd Length: 121  Bit Score: 76.72  E-value: 2.38e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492459440    2 KIHHIAIWTFHLEKLREFYTRYFNGTSNEKYINSQKGFESYFISFESGATLELMSRidvQNIPIEENRPGLTHLAFSFES 81
Cdd:pfam00903   1 RIDHVALRVGDLEKSLDFYTDVLGFKLVEETDAGEEGGLRSAFFLAGGRVLELLLN---ETPPPAAAGFGGHHIAFIAFS 77

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 492459440   82 QEAVLSLTEQLRTKGYHIVGEPRISGDGYFESVILDPDGNRIE 124
Cdd:pfam00903  78 VDDVDAAYDRLKAAGVEIVREPGRHGWGGRYSYFRDPDGNLIE 120
PRK10151 PRK10151
50S ribosomal protein L7/L12-serine acetyltransferase;
225-297 3.47e-09

50S ribosomal protein L7/L12-serine acetyltransferase;


Pssm-ID: 182270  Cd Length: 179  Bit Score: 55.15  E-value: 3.47e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 492459440 225 AGMIGYWLDEAQWGKGYMSEAVCAVLDYGFNKLGLTLISANCYPQNKRSQRVLEKMGFTYEGILHQAEV---SYDD 297
Cdd:PRK10151  93 TAYIGYWLDESHQGQGIISQALQALIHHYAQSGELRRFVIKCRVDNPASNQVALRNGFTLEGCLKQAEYlngAYDD 168
 
Name Accession Description Interval E-value
VOC_BsYyaH cd07241
vicinal oxygen chelate (VOC) family protein similar to Bacillus subtilis YyaH; The vicinal ...
 2-126 8.28e-67

vicinal oxygen chelate (VOC) family protein similar to Bacillus subtilis YyaH; The vicinal oxygen chelate (VOC) superfamily is composed of structurally related proteins with paired beta.alpha.beta.beta.beta motifs that provide a metal coordination environment with two or three open or readily accessible coordination sites to promote direct electrophilic participation of the metal ion in catalysis. VOC domain is found in a variety of structurally related metalloproteins, including the bleomycin resistance protein, glyoxalase I, and type I ring-cleaving dioxygenases. A bound metal ion is required for protein activities for the members of this superfamily. A variety of metal ions have been found in the catalytic centers of these proteins including Fe(II), Mn(II), Zn(II), Ni(II) and Mg(II). The protein superfamily contains members with or without domain swapping. The proteins of this family share three conserved metal binding amino acids with the type I extradiol dioxygenases, which shows no domain swapping.


Pssm-ID: 319905  Cd Length: 125  Bit Score: 204.95  E-value: 8.28e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492459440   2 KIHHIAIWTFHLEKLREFYTRYFNGTSNEKYINSQKGFESYFISFESGATLELMSRIDVQNIPIEENRPGLTHLAFSFES 81
Cdd:cd07241    1 KIEHVALWTNDLERMKDFYVKYFGAESNDIYHNKKKGFRSYFLTFDSGARLELMSRPDVTDPDKEVERTGLAHIAFSVGS 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 492459440  82 QEAVLSLTEQLRTKGYHIVGEPRISGDGYFESVILDPDGNRIECV 126
Cdd:cd07241   81 KEAVDELTERLRADGYAVVGGPRTTGDGYYESVILDPEGNRIEIT 125
RimL COG1670
Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, ...
 140-309 1.32e-48

Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 441276 [Multi-domain]  Cd Length: 173  Bit Score: 160.16  E-value: 1.32e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492459440 140 VIETERLILRPFTENDTEAVFNCCQNPNLGNNAGWKPHdTLEESLKILQTIFIPQKD----TWAITRKEDRLLIGAIGIL 215
Cdd:COG1670    2 TLETERLRLRPLRPEDAEALAELLNDPEVARYLPGPPY-SLEEARAWLERLLADWADggalPFAIEDKEDGELIGVVGLY 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492459440 216 PDPKRENSnaGMIGYWLDEAQWGKGYMSEAVCAVLDYGFNKLGLTLISANCYPQNKRSQRVLEKMGFTYEGILHQAEVsY 295
Cdd:COG1670   81 DIDRANRS--AEIGYWLAPAYWGKGYATEALRALLDYAFEELGLHRVEAEVDPDNTASIRVLEKLGFRLEGTLRDALV-I 157

                        170
                 ....*....|....
gi 492459440 296 DDKIYDHLCYYLEK 309
Cdd:COG1670  158 DGRYRDHVLYSLLR 171
Acetyltransf_3 pfam13302
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 145-283 2.44e-37

Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.


Pssm-ID: 379112 [Multi-domain]  Cd Length: 139  Bit Score: 129.77  E-value: 2.44e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492459440  145 RLILRPFTENDTEAVFNCCQNPNLgnNAGWKPHD-TLEESLKILQTIFIPQKD----TWAITRKEDRLlIGAIGIlpDPK 219
Cdd:pfam13302   1 RLLLRPLTEEDAEALFELLSDPEV--MRYGVPWPlTLEEAREWLARIWAADEAergyGWAIELKDTGF-IGSIGL--YDI 75

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 492459440  220 RENSNAGMIGYWLDEAQWGKGYMSEAVCAVLDYGFNKLGLTLISANCYPQNKRSQRVLEKMGFT 283
Cdd:pfam13302  76 DGEPERAELGYWLGPDYWGKGYATEAVRALLEYAFEELGLPRLVARIDPENTASRRVLEKLGFK 139
GloA COG0346
Catechol 2,3-dioxygenase or related enzyme, vicinal oxygen chelate (VOC) family [Secondary ...
 1-130 4.32e-25

Catechol 2,3-dioxygenase or related enzyme, vicinal oxygen chelate (VOC) family [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 440115 [Multi-domain]  Cd Length: 125  Bit Score: 97.37  E-value: 4.32e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492459440   1 MKIHHIAIWTFHLEKLREFYTRYFNGTSNEKYINSQKGFESYFISFESGATLELMSRIDVQNIPieeNRPGLTHLAFSFE 80
Cdd:COG0346    1 MGLHHVTLRVSDLEASLAFYTDVLGLELVKRTDFGDGGFGHAFLRLGDGTELELFEAPGAAPAP---GGGGLHHLAFRVD 77

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 492459440  81 SQEAVLsltEQLRTKGYHIVGEPRISGDGYFESVILDPDGNRIECVYKKE 130
Cdd:COG0346   78 DLDAAY---ARLRAAGVEIEGEPRDRAYGYRSAYFRDPDGNLIELVEPPP 124
Glyoxalase pfam00903
Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;
2-124 2.38e-17

Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;


Pssm-ID: 395724 [Multi-domain]  Cd Length: 121  Bit Score: 76.72  E-value: 2.38e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492459440    2 KIHHIAIWTFHLEKLREFYTRYFNGTSNEKYINSQKGFESYFISFESGATLELMSRidvQNIPIEENRPGLTHLAFSFES 81
Cdd:pfam00903   1 RIDHVALRVGDLEKSLDFYTDVLGFKLVEETDAGEEGGLRSAFFLAGGRVLELLLN---ETPPPAAAGFGGHHIAFIAFS 77

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 492459440   82 QEAVLSLTEQLRTKGYHIVGEPRISGDGYFESVILDPDGNRIE 124
Cdd:pfam00903  78 VDDVDAAYDRLKAAGVEIVREPGRHGWGGRYSYFRDPDGNLIE 120
VOC cd06587
vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate (VOC) superfamily is composed ...
 5-124 3.13e-14

vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate (VOC) superfamily is composed of structurally related proteins with paired beta.alpha.beta.beta.beta motifs that provide a metal coordination environment with two or three open or readily accessible coordination sites to promote direct electrophilic participation of the metal ion in catalysis. VOC is found in a variety of structurally related metalloproteins, including the type I extradiol dioxygenases, glyoxalase I and a group of antibiotic resistance proteins. A bound metal ion is required for protein activities for the members of this superfamily. A variety of metal ions have been found in the catalytic centers of these proteins including Fe(II), Mn(II), Zn(II), Ni(II) and Mg(II). Type I extradiol dioxygenases catalyze the incorporation of both atoms of molecular oxygen into aromatic substrates, which results in the cleavage of aromatic rings. They are key enzymes in the degradation of aromatic compounds. Type I extradiol dioxygenases include class I and class II enzymes. Class I and II enzymes show sequence similarity; the two-domain class II enzymes evolved from a class I enzyme through gene duplication. Glyoxylase I catalyzes the glutathione-dependent inactivation of toxic methylglyoxal, requiring zinc or nickel ions for activity. The antibiotic resistance proteins in this family use a variety of mechanisms to block the function of antibiotics. Bleomycin resistance protein (BLMA) sequesters bleomycin's activity by directly binding to it. Whereas, three types of fosfomycin resistance proteins employ different mechanisms to render fosfomycin inactive by modifying the fosfomycin molecule. Although the proteins in this superfamily are functionally distinct, their structures are similar. The difference among the three dimensional structures of the three types of proteins in this superfamily is interesting from an evolutionary perspective. Both glyoxalase I and BLMA show domain swapping between subunits. However, there is no domain swapping for type 1 extradiol dioxygenases.


Pssm-ID: 319898 [Multi-domain]  Cd Length: 112  Bit Score: 67.94  E-value: 3.13e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492459440   5 HIAIWTFHLEKLREFYTRYFNGTSNEKYinsqKGFESYFISFESGATLELMSRIDVQnipiEENRPGLTHLAFSFESQEA 84
Cdd:cd06587    1 HVALRVPDLDASVAFYEEVLGFEVVSRN----EGGGFAFLRLGPGLRLALLEGPEPE----RPGGGGLFHLAFEVDDVDE 72

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 492459440  85 VLSLTEQLRTKGYhIVGEPRISGDGYFESVILDPDGNRIE 124
Cdd:cd06587   73 VDERLREAGAEGE-LVAPPVDDPWGGRSFYFRDPDGNLIE 111
CatE COG2514
Catechol-2,3-dioxygenase [Secondary metabolites biosynthesis, transport and catabolism];
1-124 1.26e-13

Catechol-2,3-dioxygenase [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 442004 [Multi-domain]  Cd Length: 141  Bit Score: 66.91  E-value: 1.26e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492459440   1 MKIHHIAIWTFHLEKLREFYTRYFngtsnekyinsqkGFE--------SYFISFESGATLELmsrIDVQNIPIEENRPGL 72
Cdd:COG2514    2 TRLGHVTLRVRDLERSAAFYTDVL-------------GLEvvereggrVYLRADGGEHLLVL---EEAPGAPPRPGAAGL 65

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 492459440  73 THLAFSFESQEAVLSLTEQLRTKGYHIVGEpriSGDGYFESV-ILDPDGNRIE 124
Cdd:COG2514   66 DHVAFRVPSRADLDAALARLAAAGVPVEGA---VDHGVGESLyFRDPDGNLIE 115
PRK10151 PRK10151
50S ribosomal protein L7/L12-serine acetyltransferase;
225-297 3.47e-09

50S ribosomal protein L7/L12-serine acetyltransferase;


Pssm-ID: 182270  Cd Length: 179  Bit Score: 55.15  E-value: 3.47e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 492459440 225 AGMIGYWLDEAQWGKGYMSEAVCAVLDYGFNKLGLTLISANCYPQNKRSQRVLEKMGFTYEGILHQAEV---SYDD 297
Cdd:PRK10151  93 TAYIGYWLDESHQGQGIISQALQALIHHYAQSGELRRFVIKCRVDNPASNQVALRNGFTLEGCLKQAEYlngAYDD 168
VOC_BsYqjT cd07242
vicinal oxygen chelate (VOC) family protein similar to Bacillus subtilis YqjT; The vicinal ...
 3-126 7.28e-09

vicinal oxygen chelate (VOC) family protein similar to Bacillus subtilis YqjT; The vicinal oxygen chelate (VOC) superfamily is composed of structurally related proteins with paired beta.alpha.beta.beta.beta motifs that provide a metal coordination environment with two or three open or readily accessible coordination sites to promote direct electrophilic participation of the metal ion in catalysis. VOC domain is found in a variety of structurally related metalloproteins, including the bleomycin resistance protein, glyoxalase I, and type I ring-cleaving dioxygenases. A bound metal ion is required for protein activities for the members of this superfamily. A variety of metal ions have been found in the catalytic centers of these proteins including Fe(II), Mn(II), Zn(II), Ni(II) and Mg(II). The protein superfamily contains members with or without domain swapping. The proteins of this family share three conserved metal binding amino acids with the type I extradiol dioxygenases, which shows no domain swapping.


Pssm-ID: 319906  Cd Length: 126  Bit Score: 53.26  E-value: 7.28e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492459440   3 IHHIAIWTFHLEKLREFYTRY-FNGtsnekYINSQKGfeSYFISFESGATLELMSRI-DVQNIPI-EENRPGLTHLAFSF 79
Cdd:cd07242    2 VSHVELAVSDLHRSFKWFEWIlGLG-----WKEYDTW--SFGPSWKLSGGSLLVVQQtDEFATPEfDRARVGLNHLAFHA 74

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 492459440  80 ESQEAVLSLTEQLRTKGYHIV---GEPRISGDGYFESVILDPDGNRIECV 126
Cdd:cd07242   75 ESREAVDELTEKLAKIGGVRTygdRHPFAGGPPHYAAFCEDPDGIKLELV 124
VOC COG3324
Lactoylglutathione lyase-related enzyme, vicinal oxygen chelate (VOC) family [General function ...
 1-124 9.39e-09

Lactoylglutathione lyase-related enzyme, vicinal oxygen chelate (VOC) family [General function prediction only];


Pssm-ID: 442553 [Multi-domain]  Cd Length: 119  Bit Score: 52.72  E-value: 9.39e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492459440   1 MKIHHIAIWTFHLEKLREFYTRYFNGTSNEKYinsQKGFESYFISFESGATLELMSRIdvqnipiEENRPGLTHLAFSFE 80
Cdd:COG3324    3 GTIVWVELPVDDLERAKAFYEEVFGWTFEDDA---GPGGDYAEFDTDGGQVGGLMPGA-------EEPGGPGWLLYFAVD 72

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 492459440  81 SQEAVLsltEQLRTKGYHIVGEPR-ISGDGYFeSVILDPDGNRIE 124
Cdd:COG3324   73 DLDAAV---ARVEAAGGTVLRPPTdIPPWGRF-AVFRDPEGNRFG 113
ED_TypeI_classII_C cd08343
C-terminal domain of type I, class II extradiol dioxygenases, catalytic domain; This family ...
 5-125 2.08e-07

C-terminal domain of type I, class II extradiol dioxygenases, catalytic domain; This family contains the C-terminal, catalytic domain of type I, class II extradiol dioxygenases. Dioxygenases catalyze the incorporation of both atoms of molecular oxygen into substrates using a variety of reaction mechanisms, resulting in the cleavage of aromatic rings. Two major groups of dioxygenases have been identified according to the cleavage site; extradiol enzymes cleave the aromatic ring between a hydroxylated carbon and an adjacent non-hydroxylated carbon, whereas intradiol enzymes cleave the aromatic ring between two hydroxyl groups. Extradiol dioxygenases are classified into type I and type II enzymes. Type I extradiol dioxygenases include class I and class II enzymes. These two classes of enzymes show sequence similarity; the two-domain class II enzymes evolved from a class I enzyme through gene duplication. The extradiol dioxygenases represented in this family are type I, class II enzymes, and are composed of the N- and C-terminal domains of similar structure fold, resulting from an ancient gene duplication. The active site is located in a funnel-shaped space of the C-terminal domain. A catalytically essential metal, Fe(II) or Mn(II), presents in all the enzymes in this family.


Pssm-ID: 319931  Cd Length: 132  Bit Score: 49.24  E-value: 2.08e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492459440   5 HIAIWTFHLEKLREFYTRYFNGTSNEKYINSQKGFesyfISFESGATLELMSRIDVQNIPieenRPGLTHLAFSFESQEA 84
Cdd:cd08343    2 HVVLCSPDVEASRDFYTDVLGFRVSDRIVDPGVDG----GAFLHCDRGTDHHTVALAGGP----HPGLHHVAFEVHDLDD 73

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 492459440  85 VLSLTEQLRTKGYHIV-GEPR-ISGDGYFeSVILDPDGNRIEC 125
Cdd:cd08343   74 VGRGHDRLREKGYKIEwGPGRhGLGSQVF-DYWFDPSGNRVEY 115
VOC_Bs_YwkD_like cd08352
vicinal oxygen chelate (VOC) family protein Bacillus subtilis YwkD and similar proteins; ...
 1-124 2.66e-07

vicinal oxygen chelate (VOC) family protein Bacillus subtilis YwkD and similar proteins; uncharacterized subfamily of vicinal oxygen chelate (VOC) family contains Bacillus subtilis YwkD and similar proteins. The vicinal oxygen chelate (VOC) superfamily is composed of structurally related proteins with paired beta.alpha.beta.beta.beta motifs that provide a metal coordination environment with two or three open or readily accessible coordination sites to promote direct electrophilic participation of the metal ion in catalysis. VOC domain is found in a variety of structurally related metalloproteins, including the bleomycin resistance protein, glyoxalase I, and type I ring-cleaving dioxygenases. A bound metal ion is required for protein activities for the members of this superfamily. A variety of metal ions have been found in the catalytic centers of these proteins including Fe(II), Mn(II), Zn(II), Ni(II) and Mg(II). The protein superfamily contains members with or without domain swapping. The proteins of this family share three conserved metal binding amino acids with the type I extradiol dioxygenases, which shows no domain swapping.


Pssm-ID: 319940 [Multi-domain]  Cd Length: 123  Bit Score: 48.69  E-value: 2.66e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492459440   1 MKIHHIAIWTFHLEKLREFYTRYFNGTSNEKYINSQKGfeSYFISFESG-ATLELMSRIDVQNIPIEENRPGLTHLAFSF 79
Cdd:cd08352    1 KKIHHIAIICSDYEKSKDFYVDKLGFEIIREHYRPERN--DIKLDLALGgYQLELFIKPDAPARPSYPEALGLRHLAFKV 78

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 492459440  80 ESQEAVLsltEQLRTKGyhIVGEP----RISGDGYFesVILDPDGNRIE 124
Cdd:cd08352   79 EDVEATV---AELKSLG--IETEPirvdDFTGKKFT--FFFDPDGLPLE 120
MMCE cd07249
Methylmalonyl-CoA epimerase (MMCE); MMCE, also called methylmalonyl-CoA racemase (EC 5.1.99.1) ...
 3-118 1.04e-06

Methylmalonyl-CoA epimerase (MMCE); MMCE, also called methylmalonyl-CoA racemase (EC 5.1.99.1) interconverts (2R)-methylmalonyl-CoA and (2S)-methylmalonyl-CoA. MMCE has been found in bacteria, archaea, and in animals. In eukaryotes, MMCE is an essential enzyme in a pathway that converts propionyl-CoA to succinyl-CoA, and is important in the breakdown of odd-chain length fatty acids, branched-chain amino acids, and other metabolites. In bacteria, MMCE participates in the reverse pathway for propionate fermentation, glyoxylate regeneration, and the biosynthesis of polyketide antibiotics. MMCE is closely related to glyoxalase I and type I extradiol dioxygenases.


Pssm-ID: 319912 [Multi-domain]  Cd Length: 127  Bit Score: 47.19  E-value: 1.04e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492459440   3 IHHIAIWTFHLEKLREFYTRYFnGTSNEKYINSQKgFESYFISFESGAT-LELMSRIDVQNIP---IEENRPGLTHLAFS 78
Cdd:cd07249    1 LDHIGIAVPDLDEALKFYEDVL-GVKVSEPEELEE-QGVRVAFLELGNTqIELLEPLGEDSPIakfLDKKGGGLHHIAFE 78

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 492459440  79 FESQEAVLsltEQLRTKGYHIVGEPRISGDGYFESVILDP 118
Cdd:cd07249   79 VDDIDAAV---EELKAQGVRLLSEGPRIGAHGKRVAFLHP 115
EhpR_like cd07261
phenazine resistance protein, EhpR; Phenazine resistance protein (EhpR) in Enterobacter ...
 14-123 1.29e-06

phenazine resistance protein, EhpR; Phenazine resistance protein (EhpR) in Enterobacter agglomerans confers resistance by binding D-alanyl-griseoluteic acid and acting as a chaperone involved in exporting the antibiotic rather than by altering it chemically. EhpR is evolutionarily related to glyoxalase I and type I extradiol dioxygenases.


Pssm-ID: 319922  Cd Length: 114  Bit Score: 46.62  E-value: 1.29e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492459440  14 EKLREFYTRYFNgtsnEKYINSQKGFESYfiSFESGATLELMSRIDVQNIPIEEnrPGLTHLAFSFESQEAVLSLTEQLR 93
Cdd:cd07261   10 ERSTEFYRFLLG----KEPVESSPTFASF--VLSGGAKLGLWSSEEVEPKVAVT--GGGAELSFMVPSGEQVDEVYAEWK 81

                         90       100       110
                 ....*....|....*....|....*....|.
gi 492459440  94 TKGYHIVGEPRISGDGY-FesVILDPDGNRI 123
Cdd:cd07261   82 AMGIPIIQEPTTMDFGYtF--VATDPDGHRL 110
VOC_like cd07262
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 3-127 1.68e-06

uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate (VOC) superfamily is composed of structurally related proteins with paired beta.alpha.beta.beta.beta motifs that provide a metal coordination environment with two or three open or readily accessible coordination sites to promote direct electrophilic participation of the metal ion in catalysis. VOC domain is found in a variety of structurally related metalloproteins, including the bleomycin resistance protein, glyoxalase I, and type I ring-cleaving dioxygenases. A bound metal ion is required for protein activities for the members of this superfamily. A variety of metal ions have been found in the catalytic centers of these proteins including Fe(II), Mn(II), Zn(II), Ni(II) and Mg(II). The protein superfamily contains members with or without domain swapping. The proteins of this family share three conserved metal binding amino acids with the type I extradiol dioxygenases, which shows no domain swapping.


Pssm-ID: 319923 [Multi-domain]  Cd Length: 121  Bit Score: 46.45  E-value: 1.68e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492459440   3 IHHIAIWTFHLEKLREFYTRYFngtsnEKYINSQKGFESYFISFESGATLELMSridVQNIPIEENRPGL-THLAFSFES 81
Cdd:cd07262    1 ISHVTIGVNDLERSRAFYDAAL-----APLGYKRGFEDGGRVGYGLEGGPDFWV---TEPFDGEPATAGNgTHVAFAAPS 72

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 492459440  82 QEAVLSLTEQLRTKGYHIVGEPRI---SGDGYFESVILDPDGNRIECVY 127
Cdd:cd07262   73 RAAVDAFHAAALAAGGTDNGAPGLrphYHPGYYAAYVRDPDGNKIEAVC 121
PRK10809 PRK10809
30S ribosomal protein S5 alanine N-acetyltransferase;
224-286 3.09e-06

30S ribosomal protein S5 alanine N-acetyltransferase;


Pssm-ID: 182749  Cd Length: 194  Bit Score: 47.04  E-value: 3.09e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 492459440 224 NAGMIGYWLDEAQWGKGYMSEAVCAVLDYGFNKLGLTLISANCYPQNKRSQRVLEKMGFTYEG 286
Cdd:PRK10809 103 HACYLGYSLGQKWQGQGLMFEALQAAIRYMQRQQHMHRIMANYMPHNKRSGDLLARLGFEKEG 165
COG3607 COG3607
Lactoylglutathione lyase-related enzyme, vicinal oxygen chelate (VOC) family [General function ...
 13-127 5.57e-06

Lactoylglutathione lyase-related enzyme, vicinal oxygen chelate (VOC) family [General function prediction only];


Pssm-ID: 442825  Cd Length: 126  Bit Score: 44.82  E-value: 5.57e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492459440  13 LEKLREFYTRY---FNGT-SNEKYInsqkgfesyFISFESGATLELMSRI----DVQNIPIEENRPGLTHLAFSFESQEA 84
Cdd:COG3607   14 LERSRAFYEALgftFNPQfSDEGAA---------CFVLGEGIVLMLLPREkfatFTGKPIADATGFTEVLLALNVESREE 84

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 492459440  85 VLSLTEQLRTKGYHIVGEPRISGDGY---FEsvilDPDGNRIECVY 127
Cdd:COG3607   85 VDALVAKALAAGGTVLKPPQDVGGMYsgyFA----DPDGHLWEVAW 126
VOC_like cd07245
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 3-125 2.87e-05

uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate (VOC) superfamily is composed of structurally related proteins with paired beta.alpha.beta.beta.beta motifs that provide a metal coordination environment with two or three open or readily accessible coordination sites to promote direct electrophilic participation of the metal ion in catalysis. VOC domain is found in a variety of structurally related metalloproteins, including the bleomycin resistance protein, glyoxalase I, and type I ring-cleaving dioxygenases. A bound metal ion is required for protein activities for the members of this superfamily. A variety of metal ions have been found in the catalytic centers of these proteins including Fe(II), Mn(II), Zn(II), Ni(II) and Mg(II). The protein superfamily contains members with or without domain swapping. The proteins of this family share three conserved metal binding amino acids with the type I extradiol dioxygenases, which shows no domain swapping.


Pssm-ID: 319909 [Multi-domain]  Cd Length: 117  Bit Score: 42.69  E-value: 2.87e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492459440   3 IHHIAIWTFHLEKLREFYTRYFNGTSNEKYiNSQKgFESYFISFESGATLELMSRIDVQNIPIEENRPGLTHLAFSFESq 82
Cdd:cd07245    1 LDHVALACPDLERARRFYTDVLGLEEVPRP-PFLK-FGGAWLYLGGGQQIHLVVEQNPSELPRPEHPGRDRHPSFSVPD- 77

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 492459440  83 eaVLSLTEQLRTKGYHIVgePRISGDGYFESVIL-DPDGNRIEC 125
Cdd:cd07245   78 --LDALKQRLKEAGIPYT--ESTSPGGGVTQLFFrDPDGNRLEF 117
VOC_like cd07264
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 3-124 3.45e-04

uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate (VOC) superfamily is composed of structurally related proteins with paired beta.alpha.beta.beta.beta motifs that provide a metal coordination environment with two or three open or readily accessible coordination sites to promote direct electrophilic participation of the metal ion in catalysis. VOC domain is found in a variety of structurally related metalloproteins, including the bleomycin resistance protein, glyoxalase I, and type I ring-cleaving dioxygenases. A bound metal ion is required for protein activities for the members of this superfamily. A variety of metal ions have been found in the catalytic centers of these proteins including Fe(II), Mn(II), Zn(II), Ni(II) and Mg(II). The protein superfamily contains members with or without domain swapping. The proteins of this family share three conserved metal binding amino acids with the type I extradiol dioxygenases, which shows no domain swapping.


Pssm-ID: 319925 [Multi-domain]  Cd Length: 118  Bit Score: 39.62  E-value: 3.45e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492459440   3 IHHIAIWTFHLEKLREFYTRYFNGTSNEKYINSQkgfesyFISFESGAT-LELMSRIDVQNIPIEENRPGLTHLAFSFES 81
Cdd:cd07264    1 IAYIVLYVDDFAASLRFYRDVLGLPPRFLHEEGE------YAEFDTGETkLALFSRKEMARSGGPDRRGSAFELGFEVDD 74

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 492459440  82 QEAVLsltEQLRTKGYHIVGEPRISGDGYFESVILDPDGNRIE 124
Cdd:cd07264   75 VEATV---EELVERGAEFVREPANKPWGQTVAYVRDPDGNLIE 114
Glyoxalase_4 pfam13669
Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;
4-109 4.69e-04

Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;


Pssm-ID: 463951 [Multi-domain]  Cd Length: 109  Bit Score: 39.18  E-value: 4.69e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492459440    4 HHIAIWTFHLEKLREFYTRYFN-GTSNEKYINSQkGFESYFISFESGA-TLELMSRIDVqNIPIEENRPGLTHLAFSFES 81
Cdd:pfam13669   1 HHVGIAVPDLDRALALWGALLGlGPEGDYRSEPQ-NVDLAFALLGDGPvEVELIQPLDG-DSPLARHGPGLHHLAYWVDD 78

                          90       100
                  ....*....|....*....|....*....
gi 492459440   82 QEAVLsltEQLRTKGYHIV-GEPRISGDG 109
Cdd:pfam13669  79 LDAAV---ARLLDQGYRVApKGPRAGAAG 104
FosA cd07244
fosfomycin resistant protein subfamily FosA; This subfamily family contains FosA, a fosfomycin ...
 64-124 2.41e-03

fosfomycin resistant protein subfamily FosA; This subfamily family contains FosA, a fosfomycin resistant protein. FosA is a Mn(II) and K(+)-dependent glutathione transferase. Fosfomycin inhibits the enzyme UDP-N-acetylglucosamine-3-enolpyruvyltransferase (MurA), which catalyzes the first committed step in bacterial cell wall biosynthesis. FosA, catalyzes the addition of glutathione to the antibiotic fosfomycin, (1R,2S)-epoxypropylphosphonic acid, making it inactive. FosA is a Mn(II) dependent enzyme. It is evolutionarily related to glyoxalase I and type I extradiol dioxygenases.


Pssm-ID: 319908 [Multi-domain]  Cd Length: 121  Bit Score: 37.26  E-value: 2.41e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 492459440  64 PIEENRPGLTHLAFSFeSQEAVLSLTEQLRTKGYHIVGEPRISGDG-YFesviLDPDGNRIE 124
Cdd:cd07244   50 PAAEPSPDYTHIAFTV-SEEDFEELSERLRAAGVKIWQENSSEGDSlYF----LDPDGHKLE 106
PsjN_like cd16356
Burkholderia Phytofirmans glyoxalase/bleomycin resistance protein/dioxygenase family enzyme ...
 75-123 3.07e-03

Burkholderia Phytofirmans glyoxalase/bleomycin resistance protein/dioxygenase family enzyme and similar proteins; Burkholderia Phytofirmans glyoxalase/bleomycin resistance protein/dioxygenase family enzyme and similar proteins. The vicinal oxygen chelate (VOC) superfamily is composed of structurally related proteins with paired beta.alpha.beta.beta.beta motifs that provide a metal coordination environment with two or three open or readily accessible coordination sites to promote direct electrophilic participation of the metal ion in catalysis. VOC domain is found in a variety of structurally related metalloproteins, including the bleomycin resistance protein, glyoxalase I, and type I ring-cleaving dioxygenases. A bound metal ion is required for protein activities for the members of this superfamily. A variety of metal ions have been found in the catalytic centers of these proteins including Fe(II), Mn(II), Zn(II), Ni(II) and Mg(II). The protein superfamily contains members with or without domain swapping. The proteins of this family share three conserved metal binding amino acids with the type I extradiol dioxygenases, which shows no domain swapping.


Pssm-ID: 319963  Cd Length: 119  Bit Score: 37.02  E-value: 3.07e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 492459440  75 LAFSFESQEAVLSLTEQLRTKGYHIVGEPRISGDGYFESVILDPDGN--RI 123
Cdd:cd16356   69 LTFDVDDVEAVDRLVPRAAALGATLIKPPYDTYYGWYQAVLLDPEGNvfRI 119
VOC_like cd08353
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 68-102 6.06e-03

uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate (VOC) superfamily is composed of structurally related proteins with paired beta.alpha.beta.beta.beta motifs that provide a metal coordination environment with two or three open or readily accessible coordination sites to promote direct electrophilic participation of the metal ion in catalysis. VOC domain is found in a variety of structurally related metalloproteins, including the bleomycin resistance protein, glyoxalase I, and type I ring-cleaving dioxygenases. A bound metal ion is required for protein activities for the members of this superfamily. A variety of metal ions have been found in the catalytic centers of these proteins including Fe(II), Mn(II), Zn(II), Ni(II) and Mg(II). The protein superfamily contains members with or without domain swapping. The proteins of this family share three conserved metal binding amino acids with the type I extradiol dioxygenases, which shows no domain swapping.


Pssm-ID: 319941  Cd Length: 142  Bit Score: 36.40  E-value: 6.06e-03
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 492459440  68 NRPGLTHLAFSFESQEAVLsltEQLRTKGYHIVGE 102
Cdd:cd08353   84 NALGLRHVAFAVDDIDAVV---ARLRKHGAELVGE 115
 
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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