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Conserved domains on  [gi|748407574|gb|AJE51090|]
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ring-cleaving dioxygenase [Paenibacillus polymyxa]

Protein Classification

ring-cleaving dioxygenase( domain architecture ID 10327061)

ring-cleaving dioxygenase is a vicinal oxygen chelate (VOC) family protein that uses a metal center to coordinate a substrate, intermediate, or transition state through vicinal oxygen atoms; similar to Sphingobium indicum chlorohydroquinone/hydroquinone 1,2-dioxygenase that cleaves aromatic rings with two hydroxyl groups at para positions with consumption of O(2)

CATH:  3.10.180.10
Gene Ontology:  GO:0046872|GO:0051213
PubMed:  21820381

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PcpA_C_like cd08347
C-terminal domain of Sphingobium chlorophenolicum 2,6-dichloro-p-hydroquinone 1,2-dioxygenase ...
 152-308 1.55e-59

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: 187.45  E-value: 1.55e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748407574 152 GFGGAVLYSADSKHTQGVLENVLGMTPIGEDaDAGYIRYQTTGDLGNLIDIPV-KDVPWGNGGAGTVHHIAWRAQDDTEH 230
Cdd:cd08347    1 GLHGVTLTVREPEETDAFLTNVFGFTEVGEE-GDLVRLFAGGNGSGGVVDVLDdPDLPSAQQGYGTVHHVAFRVADDEEQ 79

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 748407574 231 QAWNEWVRQHGFGTSGIVDRQYFNAVYFREQGGILFEIATDPPGFTVDEELNELGHKLMLPEWYEPQRAQIESNLVPI 308
Cdd:cd08347   80 AAWKERLEELGFDNSGIVDRFYFESLYFREPGGVLFEIATDGPGFTVDEPPEELGEKLKLPPFLEPRRAEIEAALPPL 157
VOC super family cl14632
vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate (VOC) superfamily is composed ...
 7-129 3.15e-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 cd08346:

Pssm-ID: 472697  Cd Length: 124  Bit Score: 170.16  E-value: 3.15e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748407574   7 GIHHITSFAGDPQGNVDFYAGVLGLRLIKKTINFDAPEVYHLYFGNEEGSPGTIITFFPAPGTRKGKIGGGQVGITTYVV 86
Cdd:cd08346    1 GIHHITAITGDAQENVDFYVKVLGLRLVKKTVNQDDPPMYHLYYGDELGSPGTLLTFFPWPLGGPGRRGTGQISRIGLRV 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 748407574  87 PLGSLDYWENRLHSLKVSFTK-ATRFGESFIQFRDNEGLHLELV 129
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 ...
 152-308 1.55e-59

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: 187.45  E-value: 1.55e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748407574 152 GFGGAVLYSADSKHTQGVLENVLGMTPIGEDaDAGYIRYQTTGDLGNLIDIPV-KDVPWGNGGAGTVHHIAWRAQDDTEH 230
Cdd:cd08347    1 GLHGVTLTVREPEETDAFLTNVFGFTEVGEE-GDLVRLFAGGNGSGGVVDVLDdPDLPSAQQGYGTVHHVAFRVADDEEQ 79

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 748407574 231 QAWNEWVRQHGFGTSGIVDRQYFNAVYFREQGGILFEIATDPPGFTVDEELNELGHKLMLPEWYEPQRAQIESNLVPI 308
Cdd:cd08347   80 AAWKERLEELGFDNSGIVDRFYFESLYFREPGGVLFEIATDGPGFTVDEPPEELGEKLKLPPFLEPRRAEIEAALPPL 157
PcpA_N_like cd08346
N-terminal domain of Sphingobium chlorophenolicum 2,6-dichloro-p-hydroquinone 1,2-dioxygenase ...
 7-129 3.15e-53

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: 170.16  E-value: 3.15e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748407574   7 GIHHITSFAGDPQGNVDFYAGVLGLRLIKKTINFDAPEVYHLYFGNEEGSPGTIITFFPAPGTRKGKIGGGQVGITTYVV 86
Cdd:cd08346    1 GIHHITAITGDAQENVDFYVKVLGLRLVKKTVNQDDPPMYHLYYGDELGSPGTLLTFFPWPLGGPGRRGTGQISRIGLRV 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 748407574  87 PLGSLDYWENRLHSLKVSFTK-ATRFGESFIQFRDNEGLHLELV 129
Cdd:cd08346   81 PKGSLSFWAERLEKFGVPHSEvVTRFGEKYLRFEDPDGTRLFLV 124
CatE COG2514
Catechol-2,3-dioxygenase [Secondary metabolites biosynthesis, transport and catabolism];
150-291 4.36e-24

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


Pssm-ID: 442004 [Multi-domain]  Cd Length: 141  Bit Score: 95.41  E-value: 4.36e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748407574 150 IKGFGGAVLYSADSKHTQGVLENVLGMTPIGEDADAgyIRYQTTGDLGNLIDIPVKDVPWGNGGAGtVHHIAWRAQDDTE 229
Cdd:COG2514    1 ITRLGHVTLRVRDLERSAAFYTDVLGLEVVEREGGR--VYLRADGGEHLLVLEEAPGAPPRPGAAG-LDHVAFRVPSRAD 77

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 748407574 230 HQAWNEWVRQHGFGTSGIVDRQYFNAVYFREQGGILFEIATDPPGF--TVDEELNELGHKLMLP 291
Cdd:COG2514   78 LDAALARLAAAGVPVEGAVDHGVGESLYFRDPDGNLIELYTDRPRFehVGDLETDVLGFRLSDP 141
GloA COG0346
Catechol 2,3-dioxygenase or related enzyme, vicinal oxygen chelate (VOC) family [Secondary ...
 7-134 1.31e-16

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: 74.64  E-value: 1.31e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748407574   7 GIHHITSFAGDPQGNVDFYAGVLGLRLIKKTiNFDAPEVYHLYFGNEEgspGTIITFFPAPGTRKGKiGGGQVGITTYVV 86
Cdd:COG0346    2 GLHHVTLRVSDLEASLAFYTDVLGLELVKRT-DFGDGGFGHAFLRLGD---GTELELFEAPGAAPAP-GGGGLHHLAFRV 76

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 748407574  87 PlgSLDYWENRLHSLKVSFTKATR---FGESFIQFRDNEGLHLELVEREEG 134
Cdd:COG0346   77 D--DLDAAYARLRAAGVEIEGEPRdraYGYRSAYFRDPDGNLIELVEPPPG 125
Glyoxalase pfam00903
Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;
7-128 3.61e-09

Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;


Pssm-ID: 395724 [Multi-domain]  Cd Length: 121  Bit Score: 53.99  E-value: 3.61e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748407574    7 GIHHITSFAGDPQGNVDFYAGVLGLRLIKKTINFDAPEVYHLYFGNeegsPGTIITFFPAPGTRKGKIGGGQVGITTYVV 86
Cdd:pfam00903   1 RIDHVALRVGDLEKSLDFYTDVLGFKLVEETDAGEEGGLRSAFFLA----GGRVLELLLNETPPPAAAGFGGHHIAFIAF 76

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 748407574   87 PLGSLDYWENRLHSLKVSFTKA---TRFGESFIQFRDNEGLHLEL 128
Cdd:pfam00903  77 SVDDVDAAYDRLKAAGVEIVREpgrHGWGGRYSYFRDPDGNLIEL 121
 
Name Accession Description Interval E-value
PcpA_C_like cd08347
C-terminal domain of Sphingobium chlorophenolicum 2,6-dichloro-p-hydroquinone 1,2-dioxygenase ...
 152-308 1.55e-59

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: 187.45  E-value: 1.55e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748407574 152 GFGGAVLYSADSKHTQGVLENVLGMTPIGEDaDAGYIRYQTTGDLGNLIDIPV-KDVPWGNGGAGTVHHIAWRAQDDTEH 230
Cdd:cd08347    1 GLHGVTLTVREPEETDAFLTNVFGFTEVGEE-GDLVRLFAGGNGSGGVVDVLDdPDLPSAQQGYGTVHHVAFRVADDEEQ 79

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 748407574 231 QAWNEWVRQHGFGTSGIVDRQYFNAVYFREQGGILFEIATDPPGFTVDEELNELGHKLMLPEWYEPQRAQIESNLVPI 308
Cdd:cd08347   80 AAWKERLEELGFDNSGIVDRFYFESLYFREPGGVLFEIATDGPGFTVDEPPEELGEKLKLPPFLEPRRAEIEAALPPL 157
PcpA_N_like cd08346
N-terminal domain of Sphingobium chlorophenolicum 2,6-dichloro-p-hydroquinone 1,2-dioxygenase ...
 7-129 3.15e-53

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: 170.16  E-value: 3.15e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748407574   7 GIHHITSFAGDPQGNVDFYAGVLGLRLIKKTINFDAPEVYHLYFGNEEGSPGTIITFFPAPGTRKGKIGGGQVGITTYVV 86
Cdd:cd08346    1 GIHHITAITGDAQENVDFYVKVLGLRLVKKTVNQDDPPMYHLYYGDELGSPGTLLTFFPWPLGGPGRRGTGQISRIGLRV 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 748407574  87 PLGSLDYWENRLHSLKVSFTK-ATRFGESFIQFRDNEGLHLELV 129
Cdd:cd08346   81 PKGSLSFWAERLEKFGVPHSEvVTRFGEKYLRFEDPDGTRLFLV 124
CatE COG2514
Catechol-2,3-dioxygenase [Secondary metabolites biosynthesis, transport and catabolism];
150-291 4.36e-24

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


Pssm-ID: 442004 [Multi-domain]  Cd Length: 141  Bit Score: 95.41  E-value: 4.36e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748407574 150 IKGFGGAVLYSADSKHTQGVLENVLGMTPIGEDADAgyIRYQTTGDLGNLIDIPVKDVPWGNGGAGtVHHIAWRAQDDTE 229
Cdd:COG2514    1 ITRLGHVTLRVRDLERSAAFYTDVLGLEVVEREGGR--VYLRADGGEHLLVLEEAPGAPPRPGAAG-LDHVAFRVPSRAD 77

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 748407574 230 HQAWNEWVRQHGFGTSGIVDRQYFNAVYFREQGGILFEIATDPPGF--TVDEELNELGHKLMLP 291
Cdd:COG2514   78 LDAALARLAAAGVPVEGAVDHGVGESLYFRDPDGNLIELYTDRPRFehVGDLETDVLGFRLSDP 141
GloA COG0346
Catechol 2,3-dioxygenase or related enzyme, vicinal oxygen chelate (VOC) family [Secondary ...
 7-134 1.31e-16

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: 74.64  E-value: 1.31e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748407574   7 GIHHITSFAGDPQGNVDFYAGVLGLRLIKKTiNFDAPEVYHLYFGNEEgspGTIITFFPAPGTRKGKiGGGQVGITTYVV 86
Cdd:COG0346    2 GLHHVTLRVSDLEASLAFYTDVLGLELVKRT-DFGDGGFGHAFLRLGD---GTELELFEAPGAAPAP-GGGGLHHLAFRV 76

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 748407574  87 PlgSLDYWENRLHSLKVSFTKATR---FGESFIQFRDNEGLHLELVEREEG 134
Cdd:COG0346   77 D--DLDAAYARLRAAGVEIEGEPRdraYGYRSAYFRDPDGNLIELVEPPPG 125
Glyoxalase pfam00903
Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;
7-128 3.61e-09

Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;


Pssm-ID: 395724 [Multi-domain]  Cd Length: 121  Bit Score: 53.99  E-value: 3.61e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748407574    7 GIHHITSFAGDPQGNVDFYAGVLGLRLIKKTINFDAPEVYHLYFGNeegsPGTIITFFPAPGTRKGKIGGGQVGITTYVV 86
Cdd:pfam00903   1 RIDHVALRVGDLEKSLDFYTDVLGFKLVEETDAGEEGGLRSAFFLA----GGRVLELLLNETPPPAAAGFGGHHIAFIAF 76

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 748407574   87 PLGSLDYWENRLHSLKVSFTKA---TRFGESFIQFRDNEGLHLEL 128
Cdd:pfam00903  77 SVDDVDAAYDRLKAAGVEIVREpgrHGWGGRYSYFRDPDGNLIEL 121
CatE COG2514
Catechol-2,3-dioxygenase [Secondary metabolites biosynthesis, transport and catabolism];
6-138 2.06e-06

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


Pssm-ID: 442004 [Multi-domain]  Cd Length: 141  Bit Score: 46.49  E-value: 2.06e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748407574   6 AGIHHITSFAGDPQGNVDFYAGVLGLRLIKKTinfdaPEVYHLYFGNEEgspgTIITFFPAPGTRKGKIGGGqVGITTYV 85
Cdd:COG2514    2 TRLGHVTLRVRDLERSAAFYTDVLGLEVVERE-----GGRVYLRADGGE----HLLVLEEAPGAPPRPGAAG-LDHVAFR 71

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 748407574  86 VP-LGSLDYWENRLHSLKVSFTKATRFGES-FIQFRDNEGLHLELVEREEGPVNT 138
Cdd:COG2514   72 VPsRADLDAALARLAAAGVPVEGAVDHGVGeSLYFRDPDGNLIELYTDRPRFEHV 126
VOC cd06587
vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate (VOC) superfamily is composed ...
 171-268 3.17e-04

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: 39.82  E-value: 3.17e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748407574 171 ENVLGMTPIGEDADAGYIRYQTTGDLGnlIDIPVKDVPWGNGGAGtVHHIAWRAQD-DTEHQAWNEWVRQHGFGTSGIVD 249
Cdd:cd06587   17 EEVLGFEVVSRNEGGGFAFLRLGPGLR--LALLEGPEPERPGGGG-LFHLAFEVDDvDEVDERLREAGAEGELVAPPVDD 93

                         90
                 ....*....|....*....
gi 748407574 250 RQYFNAVYFREQGGILFEI 268
Cdd:cd06587   94 PWGGRSFYFRDPDGNLIEF 112
GloA COG0346
Catechol 2,3-dioxygenase or related enzyme, vicinal oxygen chelate (VOC) family [Secondary ...
 171-274 1.13e-03

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: 38.43  E-value: 1.13e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748407574 171 ENVLGMTPIGE---DADAGYIRYQTTGDlGNLIDIPVKDVPWGNGGAGTVHHIAWRAqDDTEhqAWNEWVRQHGFG-TSG 246
Cdd:COG0346   21 TDVLGLELVKRtdfGDGGFGHAFLRLGD-GTELELFEAPGAAPAPGGGGLHHLAFRV-DDLD--AAYARLRAAGVEiEGE 96

                         90       100
                 ....*....|....*....|....*....
gi 748407574 247 IVDRQY-FNAVYFREQGGILFEIATDPPG 274
Cdd:COG0346   97 PRDRAYgYRSAYFRDPDGNLIELVEPPPG 125
VOC_like cd08354
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 24-131 1.77e-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: 319942  Cd Length: 122  Bit Score: 37.73  E-value: 1.77e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748407574  24 FYAGVLGLRLIKKT---INFDA-PEVYHLYFGNEEGSPGTIitffpAPGTRKGKIGGGQVgitTYVVPLGSLDYWENRLH 99
Cdd:cd08354   17 FYEDVLGLKPMLRSgrhAFFRLgPQVLLVFDPGATSKDVRT-----GEVPGHGASGHGHF---AFAVPTEELAAWEARLE 88

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 748407574 100 SLKVSFTKATRF---GESfIQFRDNEGLHLELVER 131
Cdd:cd08354   89 AKGVPIESYTQWpegGKS-LYFRDPAGNLVELASA 122
 
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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