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Conserved domains on  [gi|1224755297|ref|WP_092773085|]
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VOC family protein [Agrobacterium fabrum]

Protein Classification

VOC family protein( domain architecture ID 50733)

vicinal oxygen chelate (VOC) family protein uses a metal center to coordinate a substrate, intermediate, or transition state through vicinal oxygen atoms

CATH:  3.10.180.10
Gene Ontology:  GO:0046872|GO:0003824
PubMed:  21820381|11076500

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 ...
 153-305 8.95e-53

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 cd08347:

Pssm-ID: 472697  Cd Length: 157  Bit Score: 170.12  E-value: 8.95e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224755297 153 GFSGARFNLNDTTATEELLR-FMGYERADAEGNVTRYVIPGGNGADTIDLATLPNTPFARQGAGSVHHVAFAVENREKQL 231
Cdd:cd08347     1 GLHGVTLTVREPEETDAFLTnVFGFTEVGEEGDLVRLFAGGNGSGGVVDVLDDPDLPSAQQGYGTVHHVAFRVADDEEQA 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1224755297 232 EVRKALMDTGYQVTPVIDRDYFWAIYFRTPGGILFEIATNEPGFDRDEDTAHLGEALKLPSRYEPFRNQIEANL 305
Cdd:cd08347    81 AWKERLEELGFDNSGIVDRFYFESLYFREPGGVLFEIATDGPGFTVDEPPEELGEKLKLPPFLEPRRAEIEAAL 154
VOC super family cl14632
vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate (VOC) superfamily is composed ...
 7-130 2.90e-46

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 cd08346:

Pssm-ID: 472697  Cd Length: 124  Bit Score: 152.44  E-value: 2.90e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224755297   7 GLHHVTSMASDARQNNSFFTDTLGLRRVKKTVNFDEPSVYHLYYGDETGTPGTVMTYFPFDHMVAGRPGVGEVGETQFSI 86
Cdd:cd08346     1 GIHHITAITGDAQENVDFYVKVLGLRLVKKTVNQDDPPMYHLYYGDELGSPGTLLTFFPWPLGGPGRRGTGQISRIGLRV 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1224755297  87 PKGAMGFWKDRLIAKGAAGIQADTVFGANRLRFTGPDGDGLALI 130
Cdd:cd08346    81 PKGSLSFWAERLEKFGVPHSEVVTRFGEKYLRFEDPDGTRLFLV 124
 
Name Accession Description Interval E-value
PcpA_C_like cd08347
C-terminal domain of Sphingobium chlorophenolicum 2,6-dichloro-p-hydroquinone 1,2-dioxygenase ...
 153-305 8.95e-53

C-terminal domain of Sphingobium chlorophenolicum 2,6-dichloro-p-hydroquinone 1,2-dioxygenase (PcpA), and similar proteins; The C-terminal domain of Sphingobium chlorophenolicum (formerly Sphingomonas chlorophenolica) 2,6-dichloro-p-hydroquinone 1,2-dioxygenase (PcpA), and similar proteins. PcpA is a key enzyme in the pentachlorophenol (PCP) degradation pathway, catalyzing the conversion of 2,6-dichloro-p-hydroquinone to 2-chloromaleylacetate. This domain belongs to a conserved domain superfamily that is found in a variety of structurally related metalloproteins, including the bleomycin resistance protein, glyoxalase I, and type I ring-cleaving dioxygenases.


Pssm-ID: 319935  Cd Length: 157  Bit Score: 170.12  E-value: 8.95e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224755297 153 GFSGARFNLNDTTATEELLR-FMGYERADAEGNVTRYVIPGGNGADTIDLATLPNTPFARQGAGSVHHVAFAVENREKQL 231
Cdd:cd08347     1 GLHGVTLTVREPEETDAFLTnVFGFTEVGEEGDLVRLFAGGNGSGGVVDVLDDPDLPSAQQGYGTVHHVAFRVADDEEQA 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1224755297 232 EVRKALMDTGYQVTPVIDRDYFWAIYFRTPGGILFEIATNEPGFDRDEDTAHLGEALKLPSRYEPFRNQIEANL 305
Cdd:cd08347    81 AWKERLEELGFDNSGIVDRFYFESLYFREPGGVLFEIATDGPGFTVDEPPEELGEKLKLPPFLEPRRAEIEAAL 154
PcpA_N_like cd08346
N-terminal domain of Sphingobium chlorophenolicum 2,6-dichloro-p-hydroquinone 1,2-dioxygenase ...
 7-130 2.90e-46

N-terminal domain of Sphingobium chlorophenolicum 2,6-dichloro-p-hydroquinone 1,2-dioxygenase (PcpA), and similar proteins; The N-terminal domain of Sphingobium chlorophenolicum (formerly Sphingomonas chlorophenolica) 2,6-dichloro-p-hydroquinone1,2-dioxygenase (PcpA), and similar proteins. PcpA is a key enzyme in the pentachlorophenol (PCP) degradation pathway, catalyzing the conversion of 2,6-dichloro-p-hydroquinone to 2-chloromaleylacetate. This domain belongs to a conserved domain superfamily that is found in a variety of structurally related metalloproteins, including the bleomycin resistance protein, glyoxalase I, and type I ring-cleaving dioxygenases.


Pssm-ID: 319934  Cd Length: 124  Bit Score: 152.44  E-value: 2.90e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224755297   7 GLHHVTSMASDARQNNSFFTDTLGLRRVKKTVNFDEPSVYHLYYGDETGTPGTVMTYFPFDHMVAGRPGVGEVGETQFSI 86
Cdd:cd08346     1 GIHHITAITGDAQENVDFYVKVLGLRLVKKTVNQDDPPMYHLYYGDELGSPGTLLTFFPWPLGGPGRRGTGQISRIGLRV 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1224755297  87 PKGAMGFWKDRLIAKGAAGIQADTVFGANRLRFTGPDGDGLALI 130
Cdd:cd08346    81 PKGSLSFWAERLEKFGVPHSEVVTRFGEKYLRFEDPDGTRLFLV 124
CatE COG2514
Catechol-2,3-dioxygenase [Secondary metabolites biosynthesis, transport and catabolism];
168-291 6.66e-22

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


Pssm-ID: 442004 [Multi-domain]  Cd Length: 141  Bit Score: 89.25  E-value: 6.66e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224755297 168 EELLRF----MGYERADAEGNVTRYVIPGGNgaDTIDLATLPNTPfARQGAGSVHHVAFAVENREKQLEVRKALMDTGYQ 243
Cdd:COG2514    15 ERSAAFytdvLGLEVVEREGGRVYLRADGGE--HLLVLEEAPGAP-PRPGAAGLDHVAFRVPSRADLDAALARLAAAGVP 91

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1224755297 244 VTPVIDRDYFWAIYFRTPGGILFEIATNEPGFDR--DEDTAHLGEALKLP 291
Cdd:COG2514    92 VEGAVDHGVGESLYFRDPDGNLIELYTDRPRFEHvgDLETDVLGFRLSDP 141
GloA COG0346
Catechol 2,3-dioxygenase or related enzyme, vicinal oxygen chelate (VOC) family [Secondary ...
 6-135 3.27e-11

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: 59.62  E-value: 3.27e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224755297   6 KGLHHVTSMASDARQNNSFFTDTLGLRRVKKTvNFDEPSVYHLYYGDETGTpGTVMTYFPFDHMVAGRPGVGEVGetqFS 85
Cdd:COG0346     1 MGLHHVTLRVSDLEASLAFYTDVLGLELVKRT-DFGDGGFGHAFLRLGDGT-ELELFEAPGAAPAPGGGGLHHLA---FR 75

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1224755297  86 IPkgAMGFWKDRLIAKGAAGIQA--DTVFGANRLRFTGPDGDGLALIETAND 135
Cdd:COG0346    76 VD--DLDAAYARLRAAGVEIEGEprDRAYGYRSAYFRDPDGNLIELVEPPPG 125
Glyoxalase pfam00903
Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;
177-268 1.93e-04

Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;


Pssm-ID: 395724 [Multi-domain]  Cd Length: 121  Bit Score: 40.51  E-value: 1.93e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224755297 177 ERADAEGNVTRYVIPGGNGADTIDLATLPNTPFARQGAGsVHHVAFAVENREKQLEVRKALMDTGYQVTPVIDRDYFW-- 254
Cdd:pfam00903  29 EETDAGEEGGLRSAFFLAGGRVLELLLNETPPPAAAGFG-GHHIAFIAFSVDDVDAAYDRLKAAGVEIVREPGRHGWGgr 107

                          90
                  ....*....|....
gi 1224755297 255 AIYFRTPGGILFEI 268
Cdd:pfam00903 108 YSYFRDPDGNLIEL 121
Glyoxalase pfam00903
Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;
7-124 1.51e-03

Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;


Pssm-ID: 395724 [Multi-domain]  Cd Length: 121  Bit Score: 37.81  E-value: 1.51e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224755297   7 GLHHVTSMASDARQNNSFFTDTLGLRRVKKTVNFDEPSVYHLYYGDETG--------TPGTVMTYFPFDHMVAGRPGVGE 78
Cdd:pfam00903   1 RIDHVALRVGDLEKSLDFYTDVLGFKLVEETDAGEEGGLRSAFFLAGGRvlelllneTPPPAAAGFGGHHIAFIAFSVDD 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1224755297  79 VGETQfsipkgamgfwkDRLIAKGAAGIQA--DTVFGANRLRFTGPDG 124
Cdd:pfam00903  81 VDAAY------------DRLKAAGVEIVREpgRHGWGGRYSYFRDPDG 116
 
Name Accession Description Interval E-value
PcpA_C_like cd08347
C-terminal domain of Sphingobium chlorophenolicum 2,6-dichloro-p-hydroquinone 1,2-dioxygenase ...
 153-305 8.95e-53

C-terminal domain of Sphingobium chlorophenolicum 2,6-dichloro-p-hydroquinone 1,2-dioxygenase (PcpA), and similar proteins; The C-terminal domain of Sphingobium chlorophenolicum (formerly Sphingomonas chlorophenolica) 2,6-dichloro-p-hydroquinone 1,2-dioxygenase (PcpA), and similar proteins. PcpA is a key enzyme in the pentachlorophenol (PCP) degradation pathway, catalyzing the conversion of 2,6-dichloro-p-hydroquinone to 2-chloromaleylacetate. This domain belongs to a conserved domain superfamily that is found in a variety of structurally related metalloproteins, including the bleomycin resistance protein, glyoxalase I, and type I ring-cleaving dioxygenases.


Pssm-ID: 319935  Cd Length: 157  Bit Score: 170.12  E-value: 8.95e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224755297 153 GFSGARFNLNDTTATEELLR-FMGYERADAEGNVTRYVIPGGNGADTIDLATLPNTPFARQGAGSVHHVAFAVENREKQL 231
Cdd:cd08347     1 GLHGVTLTVREPEETDAFLTnVFGFTEVGEEGDLVRLFAGGNGSGGVVDVLDDPDLPSAQQGYGTVHHVAFRVADDEEQA 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1224755297 232 EVRKALMDTGYQVTPVIDRDYFWAIYFRTPGGILFEIATNEPGFDRDEDTAHLGEALKLPSRYEPFRNQIEANL 305
Cdd:cd08347    81 AWKERLEELGFDNSGIVDRFYFESLYFREPGGVLFEIATDGPGFTVDEPPEELGEKLKLPPFLEPRRAEIEAAL 154
PcpA_N_like cd08346
N-terminal domain of Sphingobium chlorophenolicum 2,6-dichloro-p-hydroquinone 1,2-dioxygenase ...
 7-130 2.90e-46

N-terminal domain of Sphingobium chlorophenolicum 2,6-dichloro-p-hydroquinone 1,2-dioxygenase (PcpA), and similar proteins; The N-terminal domain of Sphingobium chlorophenolicum (formerly Sphingomonas chlorophenolica) 2,6-dichloro-p-hydroquinone1,2-dioxygenase (PcpA), and similar proteins. PcpA is a key enzyme in the pentachlorophenol (PCP) degradation pathway, catalyzing the conversion of 2,6-dichloro-p-hydroquinone to 2-chloromaleylacetate. This domain belongs to a conserved domain superfamily that is found in a variety of structurally related metalloproteins, including the bleomycin resistance protein, glyoxalase I, and type I ring-cleaving dioxygenases.


Pssm-ID: 319934  Cd Length: 124  Bit Score: 152.44  E-value: 2.90e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224755297   7 GLHHVTSMASDARQNNSFFTDTLGLRRVKKTVNFDEPSVYHLYYGDETGTPGTVMTYFPFDHMVAGRPGVGEVGETQFSI 86
Cdd:cd08346     1 GIHHITAITGDAQENVDFYVKVLGLRLVKKTVNQDDPPMYHLYYGDELGSPGTLLTFFPWPLGGPGRRGTGQISRIGLRV 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1224755297  87 PKGAMGFWKDRLIAKGAAGIQADTVFGANRLRFTGPDGDGLALI 130
Cdd:cd08346    81 PKGSLSFWAERLEKFGVPHSEVVTRFGEKYLRFEDPDGTRLFLV 124
CatE COG2514
Catechol-2,3-dioxygenase [Secondary metabolites biosynthesis, transport and catabolism];
168-291 6.66e-22

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


Pssm-ID: 442004 [Multi-domain]  Cd Length: 141  Bit Score: 89.25  E-value: 6.66e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224755297 168 EELLRF----MGYERADAEGNVTRYVIPGGNgaDTIDLATLPNTPfARQGAGSVHHVAFAVENREKQLEVRKALMDTGYQ 243
Cdd:COG2514    15 ERSAAFytdvLGLEVVEREGGRVYLRADGGE--HLLVLEEAPGAP-PRPGAAGLDHVAFRVPSRADLDAALARLAAAGVP 91

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1224755297 244 VTPVIDRDYFWAIYFRTPGGILFEIATNEPGFDR--DEDTAHLGEALKLP 291
Cdd:COG2514    92 VEGAVDHGVGESLYFRDPDGNLIELYTDRPRFEHvgDLETDVLGFRLSDP 141
GloA COG0346
Catechol 2,3-dioxygenase or related enzyme, vicinal oxygen chelate (VOC) family [Secondary ...
 6-135 3.27e-11

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: 59.62  E-value: 3.27e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224755297   6 KGLHHVTSMASDARQNNSFFTDTLGLRRVKKTvNFDEPSVYHLYYGDETGTpGTVMTYFPFDHMVAGRPGVGEVGetqFS 85
Cdd:COG0346     1 MGLHHVTLRVSDLEASLAFYTDVLGLELVKRT-DFGDGGFGHAFLRLGDGT-ELELFEAPGAAPAPGGGGLHHLA---FR 75

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1224755297  86 IPkgAMGFWKDRLIAKGAAGIQA--DTVFGANRLRFTGPDGDGLALIETAND 135
Cdd:COG0346    76 VD--DLDAAYARLRAAGVEIEGEprDRAYGYRSAYFRDPDGNLIELVEPPPG 125
GloA COG0346
Catechol 2,3-dioxygenase or related enzyme, vicinal oxygen chelate (VOC) family [Secondary ...
 168-274 4.96e-08

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: 50.76  E-value: 4.96e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224755297 168 EELLRFMGYERAD-AEGNVTRYVIPGGNGAdTIDLATLPNTPFARqGAGSVHHVAFAVENREkqlEVRKALMDTGYQVT- 245
Cdd:COG0346    21 TDVLGLELVKRTDfGDGGFGHAFLRLGDGT-ELELFEAPGAAPAP-GGGGLHHLAFRVDDLD---AAYARLRAAGVEIEg 95

                          90       100       110
                  ....*....|....*....|....*....|
gi 1224755297 246 -PVIDRDYFWAIYFRTPGGILFEIATNEPG 274
Cdd:COG0346    96 ePRDRAYGYRSAYFRDPDGNLIELVEPPPG 125
VOC cd06587
vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate (VOC) superfamily is composed ...
 196-268 5.39e-05

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: 41.74  E-value: 5.39e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1224755297 196 ADTIDLATLPNTPFARQGAGSVHHVAFAVENREKQLEVRKALMDTGYQVT-PVIDRDYFWAIYFRTPGGILFEI 268
Cdd:cd06587    39 GPGLRLALLEGPEPERPGGGGLFHLAFEVDDVDEVDERLREAGAEGELVApPVDDPWGGRSFYFRDPDGNLIEF 112
Glyoxalase pfam00903
Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;
177-268 1.93e-04

Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;


Pssm-ID: 395724 [Multi-domain]  Cd Length: 121  Bit Score: 40.51  E-value: 1.93e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224755297 177 ERADAEGNVTRYVIPGGNGADTIDLATLPNTPFARQGAGsVHHVAFAVENREKQLEVRKALMDTGYQVTPVIDRDYFW-- 254
Cdd:pfam00903  29 EETDAGEEGGLRSAFFLAGGRVLELLLNETPPPAAAGFG-GHHIAFIAFSVDDVDAAYDRLKAAGVEIVREPGRHGWGgr 107

                          90
                  ....*....|....
gi 1224755297 255 AIYFRTPGGILFEI 268
Cdd:pfam00903 108 YSYFRDPDGNLIEL 121
Glyoxalase pfam00903
Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;
7-124 1.51e-03

Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;


Pssm-ID: 395724 [Multi-domain]  Cd Length: 121  Bit Score: 37.81  E-value: 1.51e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224755297   7 GLHHVTSMASDARQNNSFFTDTLGLRRVKKTVNFDEPSVYHLYYGDETG--------TPGTVMTYFPFDHMVAGRPGVGE 78
Cdd:pfam00903   1 RIDHVALRVGDLEKSLDFYTDVLGFKLVEETDAGEEGGLRSAFFLAGGRvlelllneTPPPAAAGFGGHHIAFIAFSVDD 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1224755297  79 VGETQfsipkgamgfwkDRLIAKGAAGIQA--DTVFGANRLRFTGPDG 124
Cdd:pfam00903  81 VDAAY------------DRLKAAGVEIVREpgRHGWGGRYSYFRDPDG 116
 
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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