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Conserved domains on  [gi|2427034038|ref|WP_270260229|]
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VOC family protein [Kocuria marina]

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 ...
 9-157 1.45e-48

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 cd16361:

Pssm-ID: 472697  Cd Length: 150  Bit Score: 154.41  E-value: 1.45e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2427034038   9 GIQHIGVTVPDLDAATRFLVEGLGAEVVYDgLTAEDEPRQGAEVERQLGLPKGAAIHKQRMIRMGNGPNLEVFEISGEQR 88
Cdd:cd16361     1 GVNHVGITVPDLDAAVEFYTDVLGAEVVYR-STPLAEGDRGGGEMRAAGFVPGFARARIAMLRLGPGPGIELFEYKGPEQ 79

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2427034038  89 AAA--GLADLGLNHMCFYCDDIDSALTRLMAAGGQALSEVHENSRHEDSEGNGSVYVKAPWGMLVELQTIP 157
Cdd:cd16361    80 RAPvpRNSDVGIFHFALQVDDVEAAAERLAAAGGKVLMGPREIPDGGPGKGNRMVYLRDPWGTLIELVSHP 150
 
Name Accession Description Interval E-value
VOC_ShValD_like cd16361
vicinal oxygen chelate (VOC) family protein similar to Streptomyces hygroscopicus ValD protein; ...
 9-157 1.45e-48

vicinal oxygen chelate (VOC) family protein similar to Streptomyces hygroscopicus ValD protein; This subfamily of vicinal oxygen chelate (VOC) family protein includes Streptomyces hygroscopicus ValD protein and similar proteins. ValD protein functions in validamycin biosynthetic pathway. 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: 319968  Cd Length: 150  Bit Score: 154.41  E-value: 1.45e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2427034038   9 GIQHIGVTVPDLDAATRFLVEGLGAEVVYDgLTAEDEPRQGAEVERQLGLPKGAAIHKQRMIRMGNGPNLEVFEISGEQR 88
Cdd:cd16361     1 GVNHVGITVPDLDAAVEFYTDVLGAEVVYR-STPLAEGDRGGGEMRAAGFVPGFARARIAMLRLGPGPGIELFEYKGPEQ 79

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2427034038  89 AAA--GLADLGLNHMCFYCDDIDSALTRLMAAGGQALSEVHENSRHEDSEGNGSVYVKAPWGMLVELQTIP 157
Cdd:cd16361    80 RAPvpRNSDVGIFHFALQVDDVEAAAERLAAAGGKVLMGPREIPDGGPGKGNRMVYLRDPWGTLIELVSHP 150
GloA COG0346
Catechol 2,3-dioxygenase or related enzyme, vicinal oxygen chelate (VOC) family [Secondary ...
 8-159 2.97e-23

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: 88.90  E-value: 2.97e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2427034038   8 RGIQHIGVTVPDLDAATRFLVEGLGAEVVYDgltaedeprqgaeverqlgLPKGAAIHKQRMIRMGNGPNLEVFEISGEQ 87
Cdd:COG0346     1 MGLHHVTLRVSDLEASLAFYTDVLGLELVKR-------------------TDFGDGGFGHAFLRLGDGTELELFEAPGAA 61

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2427034038  88 RAAAGladLGLNHMCFYCDDIDSALTRLMAAGGQALSEVhensrHEDSEGNGSVYVKAPWGMLVELQTIPAG 159
Cdd:COG0346    62 PAPGG---GGLHHLAFRVDDLDAAYARLRAAGVEIEGEP-----RDRAYGYRSAYFRDPDGNLIELVEPPPG 125
Glyoxalase pfam00903
Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;
9-153 5.24e-12

Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;


Pssm-ID: 395724 [Multi-domain]  Cd Length: 121  Bit Score: 59.77  E-value: 5.24e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2427034038   9 GIQHIGVTVPDLDAATRFLVEGLGAEVVYDGLTAEDEprqgaeverqlglpkgaaihKQRMIRMGNGPN-LEVFEISGEQ 87
Cdd:pfam00903   1 RIDHVALRVGDLEKSLDFYTDVLGFKLVEETDAGEEG--------------------GLRSAFFLAGGRvLELLLNETPP 60

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2427034038  88 RAAAGLADLGLNHMCFYCDDIDSALTRLMAAGGqalSEVHENSRHEDseGNGSVYVKAPWGMLVEL 153
Cdd:pfam00903  61 PAAAGFGGHHIAFIAFSVDDVDAAYDRLKAAGV---EIVREPGRHGW--GGRYSYFRDPDGNLIEL 121
metmalonyl_epim TIGR03081
methylmalonyl-CoA epimerase; Members of this protein family are the enzyme methylmalonyl-CoA ...
 10-153 6.85e-10

methylmalonyl-CoA epimerase; Members of this protein family are the enzyme methylmalonyl-CoA epimerase (EC 5.1.99.1), also called methylmalonyl-CoA racemase. This enzyme converts (2R)-methylmalonyl-CoA to (2S)-methylmalonyl-CoA, which is then a substrate for methylmalonyl-CoA mutase (TIGR00642). It is known in bacteria, archaea, and as a mitochondrial protein in animals. It is closely related to lactoylglutathione lyase (TIGR00068), which is also called glyoxylase I, and is also a homodimer.


Pssm-ID: 213772 [Multi-domain]  Cd Length: 128  Bit Score: 54.25  E-value: 6.85e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2427034038  10 IQHIGVTVPDLDAATRFLVEGLGAEVvydgLTAEDEPRQGAEVErqlglpkgaaihkqrMIRMGNGpNLEVFEISGEQRA 89
Cdd:TIGR03081   2 IDHVGIAVPDLEEAAKFYEDVLGAQV----SEIEELPEQGVKVV---------------FIALGNT-KVELLEPLGEDSP 61

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2427034038  90 AAGLADL---GLNHMCFYCDDIDSALTRLMAAGGQALSEVHENSRHedseGNGSVYV--KAPWGMLVEL 153
Cdd:TIGR03081  62 IAKFLEKnggGIHHIAIEVDDIEAALETLKEKGVRLIDEEPRIGAH----GKPVAFLhpKSTGGVLIEL 126
 
Name Accession Description Interval E-value
VOC_ShValD_like cd16361
vicinal oxygen chelate (VOC) family protein similar to Streptomyces hygroscopicus ValD protein; ...
 9-157 1.45e-48

vicinal oxygen chelate (VOC) family protein similar to Streptomyces hygroscopicus ValD protein; This subfamily of vicinal oxygen chelate (VOC) family protein includes Streptomyces hygroscopicus ValD protein and similar proteins. ValD protein functions in validamycin biosynthetic pathway. 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: 319968  Cd Length: 150  Bit Score: 154.41  E-value: 1.45e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2427034038   9 GIQHIGVTVPDLDAATRFLVEGLGAEVVYDgLTAEDEPRQGAEVERQLGLPKGAAIHKQRMIRMGNGPNLEVFEISGEQR 88
Cdd:cd16361     1 GVNHVGITVPDLDAAVEFYTDVLGAEVVYR-STPLAEGDRGGGEMRAAGFVPGFARARIAMLRLGPGPGIELFEYKGPEQ 79

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2427034038  89 AAA--GLADLGLNHMCFYCDDIDSALTRLMAAGGQALSEVHENSRHEDSEGNGSVYVKAPWGMLVELQTIP 157
Cdd:cd16361    80 RAPvpRNSDVGIFHFALQVDDVEAAAERLAAAGGKVLMGPREIPDGGPGKGNRMVYLRDPWGTLIELVSHP 150
GloA COG0346
Catechol 2,3-dioxygenase or related enzyme, vicinal oxygen chelate (VOC) family [Secondary ...
 8-159 2.97e-23

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: 88.90  E-value: 2.97e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2427034038   8 RGIQHIGVTVPDLDAATRFLVEGLGAEVVYDgltaedeprqgaeverqlgLPKGAAIHKQRMIRMGNGPNLEVFEISGEQ 87
Cdd:COG0346     1 MGLHHVTLRVSDLEASLAFYTDVLGLELVKR-------------------TDFGDGGFGHAFLRLGDGTELELFEAPGAA 61

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2427034038  88 RAAAGladLGLNHMCFYCDDIDSALTRLMAAGGQALSEVhensrHEDSEGNGSVYVKAPWGMLVELQTIPAG 159
Cdd:COG0346    62 PAPGG---GGLHHLAFRVDDLDAAYARLRAAGVEIEGEP-----RDRAYGYRSAYFRDPDGNLIELVEPPPG 125
VOC cd06587
vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate (VOC) superfamily is composed ...
 12-153 2.87e-15

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: 2.87e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2427034038  12 HIGVTVPDLDAATRFLVEGLGAEVVYdgltaEDEPRQGAEVerqlglpkgaaihkqrmiRMGNGPNLEVFEISGEQRAAA 91
Cdd:cd06587     1 HVALRVPDLDASVAFYEEVLGFEVVS-----RNEGGGFAFL------------------RLGPGLRLALLEGPEPERPGG 57

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2427034038  92 GladlGLNHMCFYCDDIDSALTRLMAAGGQALSEVHensRHEDSEGNGSVYVKAPWGMLVEL 153
Cdd:cd06587    58 G----GLFHLAFEVDDVDEVDERLREAGAEGELVAP---PVDDPWGGRSFYFRDPDGNLIEF 112
MMCE cd07249
Methylmalonyl-CoA epimerase (MMCE); MMCE, also called methylmalonyl-CoA racemase (EC 5.1.99.1) ...
 10-153 8.74e-13

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: 61.82  E-value: 8.74e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2427034038  10 IQHIGVTVPDLDAATRFLVEGLGAEVVYDgltaEDEPRQGAEVerqlglpkgaaihkqRMIRMGNGPnLEVFEISGEQRA 89
Cdd:cd07249     1 LDHIGIAVPDLDEALKFYEDVLGVKVSEP----EELEEQGVRV---------------AFLELGNTQ-IELLEPLGEDSP 60

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2427034038  90 AAGLADL---GLNHMCFYCDDIDSALTRLMAAGGQALSEVhensRHEDSEGNGSVYV--KAPWGMLVEL 153
Cdd:cd07249    61 IAKFLDKkggGLHHIAFEVDDIDAAVEELKAQGVRLLSEG----PRIGAHGKRVAFLhpKDTGGVLIEL 125
Glyoxalase pfam00903
Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;
9-153 5.24e-12

Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;


Pssm-ID: 395724 [Multi-domain]  Cd Length: 121  Bit Score: 59.77  E-value: 5.24e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2427034038   9 GIQHIGVTVPDLDAATRFLVEGLGAEVVYDGLTAEDEprqgaeverqlglpkgaaihKQRMIRMGNGPN-LEVFEISGEQ 87
Cdd:pfam00903   1 RIDHVALRVGDLEKSLDFYTDVLGFKLVEETDAGEEG--------------------GLRSAFFLAGGRvLELLLNETPP 60

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2427034038  88 RAAAGLADLGLNHMCFYCDDIDSALTRLMAAGGqalSEVHENSRHEDseGNGSVYVKAPWGMLVEL 153
Cdd:pfam00903  61 PAAAGFGGHHIAFIAFSVDDVDAAYDRLKAAGV---EIVREPGRHGW--GGRYSYFRDPDGNLIEL 121
VOC_like cd08353
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 10-153 1.33e-11

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: 59.13  E-value: 1.33e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2427034038  10 IQHIGVTVPDLDAATRFLVEgLGAEVvyDGLTaedePRQGAEVERQLGLpkgaaiHKQR----MIRMGNG-PNLEVFE-- 82
Cdd:cd08353     4 MDHVGIVVEDLDAAIAFFTE-LGLEL--EGRM----TVEGEWADRVVGL------DGVRveiaMLRTPDGhGRLELSKfl 70

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2427034038  83 ----ISGEQRAAAGlaDLGLNHMCFYCDDIDSALTRLMAAGGQALSEVHEnsrHEDSEgnGSVYVKAPWGMLVEL 153
Cdd:cd08353    71 tpaaIPGHRPAPAN--ALGLRHVAFAVDDIDAVVARLRKHGAELVGEVVQ---YEDSY--RLCYVRGPEGIIVEL 138
metmalonyl_epim TIGR03081
methylmalonyl-CoA epimerase; Members of this protein family are the enzyme methylmalonyl-CoA ...
 10-153 6.85e-10

methylmalonyl-CoA epimerase; Members of this protein family are the enzyme methylmalonyl-CoA epimerase (EC 5.1.99.1), also called methylmalonyl-CoA racemase. This enzyme converts (2R)-methylmalonyl-CoA to (2S)-methylmalonyl-CoA, which is then a substrate for methylmalonyl-CoA mutase (TIGR00642). It is known in bacteria, archaea, and as a mitochondrial protein in animals. It is closely related to lactoylglutathione lyase (TIGR00068), which is also called glyoxylase I, and is also a homodimer.


Pssm-ID: 213772 [Multi-domain]  Cd Length: 128  Bit Score: 54.25  E-value: 6.85e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2427034038  10 IQHIGVTVPDLDAATRFLVEGLGAEVvydgLTAEDEPRQGAEVErqlglpkgaaihkqrMIRMGNGpNLEVFEISGEQRA 89
Cdd:TIGR03081   2 IDHVGIAVPDLEEAAKFYEDVLGAQV----SEIEELPEQGVKVV---------------FIALGNT-KVELLEPLGEDSP 61

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2427034038  90 AAGLADL---GLNHMCFYCDDIDSALTRLMAAGGQALSEVHENSRHedseGNGSVYV--KAPWGMLVEL 153
Cdd:TIGR03081  62 IAKFLEKnggGIHHIAIEVDDIEAALETLKEKGVRLIDEEPRIGAH----GKPVAFLhpKSTGGVLIEL 126
CatE COG2514
Catechol-2,3-dioxygenase [Secondary metabolites biosynthesis, transport and catabolism];
7-155 2.79e-08

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


Pssm-ID: 442004 [Multi-domain]  Cd Length: 141  Bit Score: 50.34  E-value: 2.79e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2427034038   7 PRGIQHIGVTVPDLDAATRFLVEGLGAEVVYdgltaedepRQGAEVerqlglpkgaaihkqRMIRMGNGPNLEVFEISGe 86
Cdd:COG2514     1 ITRLGHVTLRVRDLERSAAFYTDVLGLEVVE---------REGGRV---------------YLRADGGEHLLVLEEAPG- 55

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2427034038  87 qrAAAGLADLGLNHMCFYCD---DIDSALTRLMAAGgqalsevHENSRHEDSEGNGSVYVKAPWGMLVELQT 155
Cdd:COG2514    56 --APPRPGAAGLDHVAFRVPsraDLDAALARLAAAG-------VPVEGAVDHGVGESLYFRDPDGNLIELYT 118
VOC_like cd07245
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 10-153 2.43e-07

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: 47.31  E-value: 2.43e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2427034038  10 IQHIGVTVPDLDAATRFLVEGLGAEVVydgltaedePRqgaeveRQLGLPKGAAIHkqrmirMGNGPNLEVFEISGEQRA 89
Cdd:cd07245     1 LDHVALACPDLERARRFYTDVLGLEEV---------PR------PPFLKFGGAWLY------LGGGQQIHLVVEQNPSEL 59

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2427034038  90 AAGLADLGLNHMCFYCDDIDSALTRLMAAGgqalseVHENSRHEDSEGNGSVYVKAPWGMLVEL 153
Cdd:cd07245    60 PRPEHPGRDRHPSFSVPDLDALKQRLKEAG------IPYTESTSPGGGVTQLFFRDPDGNRLEF 117
Glyoxalase_4 pfam13669
Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;
11-119 4.33e-07

Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;


Pssm-ID: 463951 [Multi-domain]  Cd Length: 109  Bit Score: 46.12  E-value: 4.33e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2427034038  11 QHIGVTVPDLDAATRFLVEGLGAEVVYDgltaEDEPRQGAEVerqlglpkgaaihkqRMIRMGNGPnLEVFEISGEQRA- 89
Cdd:pfam13669   1 HHVGIAVPDLDRALALWGALLGLGPEGD----YRSEPQNVDL---------------AFALLGDGP-VEVELIQPLDGDs 60

                          90       100       110
                  ....*....|....*....|....*....|..
gi 2427034038  90 --AAGLAdlGLNHMCFYCDDIDSALTRLMAAG 119
Cdd:pfam13669  61 plARHGP--GLHHLAYWVDDLDAAVARLLDQG 90
VOC COG3324
Lactoylglutathione lyase-related enzyme, vicinal oxygen chelate (VOC) family [General function ...
 7-138 5.39e-07

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


Pssm-ID: 442553 [Multi-domain]  Cd Length: 119  Bit Score: 46.17  E-value: 5.39e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2427034038   7 PRGIQHIGVTVPDLDAATRFLVEGLGAEVVYDgltaEDEPRQGAEVERQLGLpkGAAIHKQRMIRMGNGPnlevfeisge 86
Cdd:COG3324     2 PGTIVWVELPVDDLERAKAFYEEVFGWTFEDD----AGPGGDYAEFDTDGGQ--VGGLMPGAEEPGGPGW---------- 65

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2427034038  87 qraaagladlglnHMCFYCDDIDSALTRLMAAGGQALSEVHENSRH------EDSEGN 138
Cdd:COG3324    66 -------------LLYFAVDDLDAAVARVEAAGGTVLRPPTDIPPWgrfavfRDPEGN 110
FosX cd08364
fosfomycin resistant protein subfamily FosX; This subfamily family contains FosX, a fosfomycin ...
 7-38 1.53e-05

fosfomycin resistant protein subfamily FosX; This subfamily family contains FosX, a fosfomycin resistant protein. FosX is a Mn(II)-dependent fosfomycin-specific epoxide hydrolase. Fosfomycin inhibits the enzyme UDP-Nacetylglucosamine-3-enolpyruvyltransferase (MurA), which catalyzes the first committed step in bacterial cell wall biosynthesis. FosX catalyzes the addition of a water molecule to the C1 position of the antibiotic with inversion of the configuration at C1 in the presence of Mn(II). The hydrated fosfomycin loses the inhibition activity. FosX is evolutionarily related to glyoxalase I and type I extradiol dioxygenases.


Pssm-ID: 319952  Cd Length: 130  Bit Score: 42.65  E-value: 1.53e-05
                          10        20        30
                  ....*....|....*....|....*....|..
gi 2427034038   7 PRGIQHIGVTVPDLDAATRFLVEGLGAEVVYD 38
Cdd:cd08364     1 IEGISHITFIVKDLDRTAAFLTEIFGAEEVYD 32
VOC_Bs_YwkD_like cd08352
vicinal oxygen chelate (VOC) family protein Bacillus subtilis YwkD and similar proteins; ...
 8-119 2.95e-05

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: 41.38  E-value: 2.95e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2427034038   8 RGIQHIGVTVPDLDAATRFLVEGLGAEVVydgltaedeprqgAEVERQLglpkgaaihKQR---MIRMGNGpNLEVFEIS 84
Cdd:cd08352     1 KKIHHIAIICSDYEKSKDFYVDKLGFEII-------------REHYRPE---------RNDiklDLALGGY-QLELFIKP 57

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 2427034038  85 GEQRAAAGLADLGLNHMCFYCDDIDSALTRLMAAG 119
Cdd:cd08352    58 DAPARPSYPEALGLRHLAFKVEDVEATVAELKSLG 92
PhnB COG2764
Zn-dependent glyoxalase, PhnB family [Energy production and conversion];
15-128 4.02e-04

Zn-dependent glyoxalase, PhnB family [Energy production and conversion];


Pssm-ID: 442048 [Multi-domain]  Cd Length: 118  Bit Score: 38.30  E-value: 4.02e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2427034038  15 VTVPDLDAATRFLVEGLGAEVVYDgltaedeprqgaeverqLGLPKGAAIHKQrmIRMGNGpNLEVFEISGEQRAAAGla 94
Cdd:COG2764     6 LVVDDAEEALEFYEDVFGFEVVFR-----------------MTDPDGKIMHAE--LRIGGS-VLMLSDAPPDSPAAEG-- 63

                          90       100       110
                  ....*....|....*....|....*....|....
gi 2427034038  95 dlGLNHMCFYCDDIDSALTRLMAAGGQALSEVHE 128
Cdd:COG2764    64 --NGVSLSLYVDDVDALFARLVAAGATVVMPLQD 95
VOC_like cd07263
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 12-126 8.29e-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: 319924 [Multi-domain]  Cd Length: 120  Bit Score: 37.66  E-value: 8.29e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2427034038  12 HIGVTVPDLDAATRFLVEGLGAEVVydgltaEDEPRQGA---EVErqlglPKGAAihkqrMIRMGNGPNlevfeISGEQR 88
Cdd:cd07263     1 QVMLYVDDQDKALDFYVEKLGFEVV------EDVPMGGMrwvTVA-----PPGSP-----GTSLLLEPK-----AHPAQM 59

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 2427034038  89 AAAGLADLGLNHMCFYCDDIDSALTRLMAAGGQALSEV 126
Cdd:cd07263    60 PQSPEAAGGTPGILLATDDIDATYERLTAAGVTFVQEP 97
BphC1-RGP6_C_like cd07237
C-terminal domain of 2,3-dihydroxybiphenyl 1,2-dioxygenase; This subfamily contains the ...
 8-153 3.44e-03

C-terminal domain of 2,3-dihydroxybiphenyl 1,2-dioxygenase; This subfamily contains the C-terminal, catalytic, domain of BphC1-RGP6 and similar proteins. BphC catalyzes the extradiol ring cleavage reaction of 2,3-dihydroxybiphenyl, the third step in the polychlorinated biphenyls (PCBs) degradation pathway (bph pathway). This subfamily of BphCs belongs to the type I extradiol dioxygenase family, which require a metal in the active site in its catalytic mechanism. Polychlorinated biphenyl degrading bacteria demonstrate a multiplicity of BphCs. For example, three types of BphC enzymes have been found in Rhodococcus globerulus (BphC1-RGP6 - BphC3-RGP6), all three enzymes are type I extradiol dioxygenases. BphC1-RGP6 has an internal duplication, it is a two-domain dioxygenase which forms octamers, and has Fe(II) at the catalytic site. Its C-terminal repeat is represented in this subfamily. BphC2-RGP6 and BphC3-RGP6 are one-domain dioxygenases, they belong to a different subfamily of the ED_TypeI_classII_C (C-terminal domain of type I, class II extradiol dioxygenases) family.


Pssm-ID: 319902  Cd Length: 153  Bit Score: 36.10  E-value: 3.44e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2427034038   8 RGIQHIGVTVPDLDAATRFLVEGLGAE--VVYDGltaedeprqgaeverQLGLPKGAAIH------KQRMIRMGNGPnle 79
Cdd:cd07237     8 QGLGHVVLIVPDVDEALAFYTDVLGFRlsDEIRI---------------PLPPGVTARLHflhcngRHHSLAFGAGP--- 69

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2427034038  80 vfeisgeqraaaglADLGLNHMCFYCDDIDS---ALTRLMAAGGQALSEV--HENSRHEdsegngSVYVKAPWGMLVEL 153
Cdd:cd07237    70 --------------GPKRLHHLMLEVTSLDDvgrAYDRVRKRGIPIAMTLgrHTNDKML------SFYVATPSGFLIEY 128
Glyoxalase_6 pfam18029
Glyoxalase-like domain; This entry comprises a diverse set of domains related to the ...
 12-138 8.68e-03

Glyoxalase-like domain; This entry comprises a diverse set of domains related to the Glyoxalase domain. The exact specificity of these proteins is uncertain.


Pssm-ID: 436220  Cd Length: 110  Bit Score: 34.28  E-value: 8.68e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2427034038  12 HIGVTVPDLDAATRFLVEGLGAEVVYDGLTAEDEPRQGAEVERQLGL----PKGAAIHKQRMirmgngpnlevfeisgeq 87
Cdd:pfam18029   1 AVVLDCADPAALAAFWSAALGWEVVPDDTALPDPDGGGPIGGGGPRLlfqrVPEPKPGKNRV------------------ 62

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2427034038  88 raaagladlglnHMCFYCDDIDSALTRLMAAGGQALSEVHENSRHE----DSEGN 138
Cdd:pfam18029  63 ------------HLDLAVDDLEAAVARLVALGATVLDDGDDPDGGRwvlaDPEGN 105
 
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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