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Conserved domains on  [gi|490874292|ref|WP_004736293|]
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MULTISPECIES: lactoylglutathione lyase [Vibrio]

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 ...
 3-125 9.75e-68

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 TIGR00068:

Pssm-ID: 472697  Cd Length: 150  Bit Score: 200.80  E-value: 9.75e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490874292    3 FLHTMIRVTDLDKSIEFYTKVLGMKELERHENKDYRYTLVFVGYEQG--GTTIELTYNWDTNEYEMGSAFGHLALGVDDI 80
Cdd:TIGR00068  18 LLHTMLRVGDLDKSLDFYTEVLGMKLLRKRDFPEMKFSLAFLGYGDEtsAAVIELTHNWGTEKYDLGNGFGHIAIGVDDV 97

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 490874292   81 YAACDKIKSLGGNVTREAGPVKGGSTHIAFITDPDGYQIELIQLG 125
Cdd:TIGR00068  98 YKACERVRALGGNVVREPGPVKGGTTVIAFVEDPDGYKIELIQRK 142
 
Name Accession Description Interval E-value
glyox_I TIGR00068
lactoylglutathione lyase; Lactoylglutathione lyase is also known as aldoketomutase and ...
 3-125 9.75e-68

lactoylglutathione lyase; Lactoylglutathione lyase is also known as aldoketomutase and glyoxalase I. Glyoxylase I is a homodimer in many species. In some eukaryotes, including yeasts and plants, the orthologous protein carries a tandem duplication, is twice as long, and hits this model twice. [Central intermediary metabolism, Amino sugars, Energy metabolism, Other]


Pssm-ID: 272886  Cd Length: 150  Bit Score: 200.80  E-value: 9.75e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490874292    3 FLHTMIRVTDLDKSIEFYTKVLGMKELERHENKDYRYTLVFVGYEQG--GTTIELTYNWDTNEYEMGSAFGHLALGVDDI 80
Cdd:TIGR00068  18 LLHTMLRVGDLDKSLDFYTEVLGMKLLRKRDFPEMKFSLAFLGYGDEtsAAVIELTHNWGTEKYDLGNGFGHIAIGVDDV 97

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 490874292   81 YAACDKIKSLGGNVTREAGPVKGGSTHIAFITDPDGYQIELIQLG 125
Cdd:TIGR00068  98 YKACERVRALGGNVVREPGPVKGGTTVIAFVEDPDGYKIELIQRK 142
GlxI_Ni cd16358
Glyoxalase I that uses Ni(++) as cofactor; This family includes Escherichia coil and other ...
 4-122 1.12e-62

Glyoxalase I that uses Ni(++) as cofactor; This family includes Escherichia coil and other prokaryotic glyoxalase I that uses nickel as cofactor. Glyoxalase I (also known as lactoylglutathione lyase; EC 4.4.1.5) is part of the glyoxalase system, a two-step system for detoxifying methylglyoxal, a side product of glycolysis. This system is responsible for the conversion of reactive, acyclic alpha-oxoaldehydes into the corresponding alpha-hydroxyacids and involves 2 enzymes, glyoxalase I and II. Glyoxalase I catalyses an intramolecular redox reaction of the hemithioacetal (formed from methylglyoxal and glutathione) to form the thioester, S-D-lactoylglutathione. This reaction involves the transfer of two hydrogen atoms from C1 to C2 of the methylglyoxal, and proceeds via an ene-diol intermediate. Glyoxalase I has a requirement for bound metal ions for catalysis. Eukaryotic glyoxalase I prefers the divalent cation zinc as cofactor, whereas Escherichia coil and other prokaryotic glyoxalase I uses nickel. However, eukaryotic Trypanosomatid parasites also use nickel as a cofactor, which could possibly be explained by acquiring their GLOI gene by horizontal gene transfer. Human glyoxalase I is a two-domain enzyme and it has the structure of a domain-swapped dimer with two active sites located at the dimer interface. In yeast, in various plants, insects and Plasmodia, glyoxalase I is four-domain, possibly the result of a further gene duplication and an additional gene fusing event.


Pssm-ID: 319965 [Multi-domain]  Cd Length: 122  Bit Score: 186.83  E-value: 1.12e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490874292   4 LHTMIRVTDLDKSIEFYTKVLGMKELERHENKDYRYTLVFVGY--EQGGTTIELTYNWDTNEYEMGSAFGHLALGVDDIY 81
Cdd:cd16358    2 LHTMLRVGDLDRSIKFYTEVLGMKLLRKRDYPEGKYTLAFVGYgdEDENTVLELTYNWGVDKYDLGTAYGHIAIGVEDVY 81

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 490874292  82 AACDKIKSLGGNVTREAGPVKGGSTHIAFITDPDGYQIELI 122
Cdd:cd16358   82 ETCERIRKKGGKVTREPGPMKGGTTVIAFVEDPDGYKIELI 122
PRK10291 PRK10291
glyoxalase I; Provisional
 7-123 2.17e-48

glyoxalase I; Provisional


Pssm-ID: 182358  Cd Length: 129  Bit Score: 151.33  E-value: 2.17e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490874292   7 MIRVTDLDKSIEFYTKVLGMKELERHENKDYRYTLVFVGY--EQGGTTIELTYNWDTNEYEMGSAFGHLALGVDDIYAAC 84
Cdd:PRK10291   1 MLRVGDLQRSIDFYTNVLGMKLLRTSENPEYKYSLAFVGYgpETEEAVIELTYNWGVDKYELGTAYGHIALSVDNAAEAC 80

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 490874292  85 DKIKSLGGNVTREAGPVKGGSTHIAFITDPDGYQIELIQ 123
Cdd:PRK10291  81 EKIRQNGGNVTREAGPVKGGTTVIAFVEDPDGYKIELIE 119
GloA COG0346
Catechol 2,3-dioxygenase or related enzyme, vicinal oxygen chelate (VOC) family [Secondary ...
 1-123 9.31e-41

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: 131.65  E-value: 9.31e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490874292   1 MKFLHTMIRVTDLDKSIEFYTKVLGMKELERHENKDYRYTLVFVGYEqGGTTIELTYNWDTNEYEMGSAFGHLALGVDDI 80
Cdd:COG0346    1 MGLHHVTLRVSDLEASLAFYTDVLGLELVKRTDFGDGGFGHAFLRLG-DGTELELFEAPGAAPAPGGGGLHHLAFRVDDL 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 490874292  81 YAACDKIKSLGGNVTREAGPVKGGsTHIAFITDPDGYQIELIQ 123
Cdd:COG0346   80 DAAYARLRAAGVEIEGEPRDRAYG-YRSAYFRDPDGNLIELVE 121
Glyoxalase pfam00903
Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;
2-121 5.43e-29

Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;


Pssm-ID: 395724 [Multi-domain]  Cd Length: 121  Bit Score: 101.76  E-value: 5.43e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490874292    2 KFLHTMIRVTDLDKSIEFYTKVLGMKELERHENKDYrYTLVFVGYEQGGTTIELTYNWDTNEYEMG---SAFGHLALGVD 78
Cdd:pfam00903   1 RIDHVALRVGDLEKSLDFYTDVLGFKLVEETDAGEE-GGLRSAFFLAGGRVLELLLNETPPPAAAGfggHHIAFIAFSVD 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 490874292   79 DIYAACDKIKSLGGNVTREAGPVKGGSThIAFITDPDGYQIEL 121
Cdd:pfam00903  80 DVDAAYDRLKAAGVEIVREPGRHGWGGR-YSYFRDPDGNLIEL 121
 
Name Accession Description Interval E-value
glyox_I TIGR00068
lactoylglutathione lyase; Lactoylglutathione lyase is also known as aldoketomutase and ...
 3-125 9.75e-68

lactoylglutathione lyase; Lactoylglutathione lyase is also known as aldoketomutase and glyoxalase I. Glyoxylase I is a homodimer in many species. In some eukaryotes, including yeasts and plants, the orthologous protein carries a tandem duplication, is twice as long, and hits this model twice. [Central intermediary metabolism, Amino sugars, Energy metabolism, Other]


Pssm-ID: 272886  Cd Length: 150  Bit Score: 200.80  E-value: 9.75e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490874292    3 FLHTMIRVTDLDKSIEFYTKVLGMKELERHENKDYRYTLVFVGYEQG--GTTIELTYNWDTNEYEMGSAFGHLALGVDDI 80
Cdd:TIGR00068  18 LLHTMLRVGDLDKSLDFYTEVLGMKLLRKRDFPEMKFSLAFLGYGDEtsAAVIELTHNWGTEKYDLGNGFGHIAIGVDDV 97

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 490874292   81 YAACDKIKSLGGNVTREAGPVKGGSTHIAFITDPDGYQIELIQLG 125
Cdd:TIGR00068  98 YKACERVRALGGNVVREPGPVKGGTTVIAFVEDPDGYKIELIQRK 142
GlxI_Ni cd16358
Glyoxalase I that uses Ni(++) as cofactor; This family includes Escherichia coil and other ...
 4-122 1.12e-62

Glyoxalase I that uses Ni(++) as cofactor; This family includes Escherichia coil and other prokaryotic glyoxalase I that uses nickel as cofactor. Glyoxalase I (also known as lactoylglutathione lyase; EC 4.4.1.5) is part of the glyoxalase system, a two-step system for detoxifying methylglyoxal, a side product of glycolysis. This system is responsible for the conversion of reactive, acyclic alpha-oxoaldehydes into the corresponding alpha-hydroxyacids and involves 2 enzymes, glyoxalase I and II. Glyoxalase I catalyses an intramolecular redox reaction of the hemithioacetal (formed from methylglyoxal and glutathione) to form the thioester, S-D-lactoylglutathione. This reaction involves the transfer of two hydrogen atoms from C1 to C2 of the methylglyoxal, and proceeds via an ene-diol intermediate. Glyoxalase I has a requirement for bound metal ions for catalysis. Eukaryotic glyoxalase I prefers the divalent cation zinc as cofactor, whereas Escherichia coil and other prokaryotic glyoxalase I uses nickel. However, eukaryotic Trypanosomatid parasites also use nickel as a cofactor, which could possibly be explained by acquiring their GLOI gene by horizontal gene transfer. Human glyoxalase I is a two-domain enzyme and it has the structure of a domain-swapped dimer with two active sites located at the dimer interface. In yeast, in various plants, insects and Plasmodia, glyoxalase I is four-domain, possibly the result of a further gene duplication and an additional gene fusing event.


Pssm-ID: 319965 [Multi-domain]  Cd Length: 122  Bit Score: 186.83  E-value: 1.12e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490874292   4 LHTMIRVTDLDKSIEFYTKVLGMKELERHENKDYRYTLVFVGY--EQGGTTIELTYNWDTNEYEMGSAFGHLALGVDDIY 81
Cdd:cd16358    2 LHTMLRVGDLDRSIKFYTEVLGMKLLRKRDYPEGKYTLAFVGYgdEDENTVLELTYNWGVDKYDLGTAYGHIAIGVEDVY 81

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 490874292  82 AACDKIKSLGGNVTREAGPVKGGSTHIAFITDPDGYQIELI 122
Cdd:cd16358   82 ETCERIRKKGGKVTREPGPMKGGTTVIAFVEDPDGYKIELI 122
PRK10291 PRK10291
glyoxalase I; Provisional
 7-123 2.17e-48

glyoxalase I; Provisional


Pssm-ID: 182358  Cd Length: 129  Bit Score: 151.33  E-value: 2.17e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490874292   7 MIRVTDLDKSIEFYTKVLGMKELERHENKDYRYTLVFVGY--EQGGTTIELTYNWDTNEYEMGSAFGHLALGVDDIYAAC 84
Cdd:PRK10291   1 MLRVGDLQRSIDFYTNVLGMKLLRTSENPEYKYSLAFVGYgpETEEAVIELTYNWGVDKYELGTAYGHIALSVDNAAEAC 80

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 490874292  85 DKIKSLGGNVTREAGPVKGGSTHIAFITDPDGYQIELIQ 123
Cdd:PRK10291  81 EKIRQNGGNVTREAGPVKGGTTVIAFVEDPDGYKIELIE 119
PLN02300 PLN02300
lactoylglutathione lyase
 2-125 1.73e-46

lactoylglutathione lyase


Pssm-ID: 215169 [Multi-domain]  Cd Length: 286  Bit Score: 151.47  E-value: 1.73e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490874292   2 KFLHTMIRVTDLDKSIEFYTKVLGMKELERHENKDYRYTLVFVGY--EQGGTTIELTYNWDTNEYEMGSAFGHLALGVDD 79
Cdd:PLN02300  24 RMLHVVYRVGDLDRTIKFYTECLGMKLLRKRDIPEEKYTNAFLGYgpEDSNFVVELTYNYGVDKYDIGTGFGHFGIAVED 103

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 490874292  80 IYAACDKIKSLGGNVTREAGPVKGGSTHIAFITDPDGYQIELIQLG 125
Cdd:PLN02300 104 VAKTVELVKAKGGKVTREPGPVKGGKSVIAFVKDPDGYKFELIQRG 149
GloA COG0346
Catechol 2,3-dioxygenase or related enzyme, vicinal oxygen chelate (VOC) family [Secondary ...
 1-123 9.31e-41

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: 131.65  E-value: 9.31e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490874292   1 MKFLHTMIRVTDLDKSIEFYTKVLGMKELERHENKDYRYTLVFVGYEqGGTTIELTYNWDTNEYEMGSAFGHLALGVDDI 80
Cdd:COG0346    1 MGLHHVTLRVSDLEASLAFYTDVLGLELVKRTDFGDGGFGHAFLRLG-DGTELELFEAPGAAPAPGGGGLHHLAFRVDDL 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 490874292  81 YAACDKIKSLGGNVTREAGPVKGGsTHIAFITDPDGYQIELIQ 123
Cdd:COG0346   80 DAAYARLRAAGVEIEGEPRDRAYG-YRSAYFRDPDGNLIELVE 121
GlxI_Zn cd07233
Glyoxalase I that uses Zn(++) as cofactor; This family includes eukaryotic glyoxalase I that ...
 3-122 1.20e-38

Glyoxalase I that uses Zn(++) as cofactor; This family includes eukaryotic glyoxalase I that prefers the divalent cation zinc as cofactor. Glyoxalase I (also known as lactoylglutathione lyase; EC 4.4.1.5) is part of the glyoxalase system, a two-step system for detoxifying methylglyoxal, a side product of glycolysis. This system is responsible for the conversion of reactive, acyclic alpha-oxoaldehydes into the corresponding alpha-hydroxyacids and involves 2 enzymes, glyoxalase I and II. Glyoxalase I catalyses an intramolecular redox reaction of the hemithioacetal (formed from methylglyoxal and glutathione) to form the thioester, S-D-lactoylglutathione. This reaction involves the transfer of two hydrogen atoms from C1 to C2 of the methylglyoxal, and proceeds via an ene-diol intermediate. Glyoxalase I has a requirement for bound metal ions for catalysis. Eukaryotic glyoxalase I prefers the divalent cation zinc as cofactor, whereas Escherichia coil and other prokaryotic glyoxalase I uses nickel. However, eukaryotic Trypanosomatid parasites also use nickel as a cofactor, which could possibly be explained by acquiring their GLOI gene by horizontal gene transfer. Human glyoxalase I is a two-domain enzyme and it has the structure of a domain-swapped dimer with two active sites located at the dimer interface. In yeast, in various plants, insects and Plasmodia, glyoxalase I is four-domain, possibly the result of a further gene duplication and an additional gene fusing event.


Pssm-ID: 319900 [Multi-domain]  Cd Length: 142  Bit Score: 126.67  E-value: 1.20e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490874292   3 FLHTMIRVTDLDKSIEFYTKVLGMKELERHENKDYRYTLVFVGYEQGGT---------------TIELTYNW-----DTN 62
Cdd:cd07233    1 FNHTMLRVKDPKKSLKFYTEVLGMKLLRKKDFPEMKFSLYFLGYEDPKDipkdprtawvfsregTLELTHNWgtendEDP 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490874292  63 EYEMGSA----FGHLALGVDDIYAACDKIKSLGgnVTREAGPVKGGSTHIAFITDPDGYQIELI 122
Cdd:cd07233   81 VYHNGNSdprgFGHIGIAVDDVYAACERFEELG--VKFKKKPDDGKMKGIAFIKDPDGYWIEIL 142
PLN02300 PLN02300
lactoylglutathione lyase
 3-122 1.71e-34

lactoylglutathione lyase


Pssm-ID: 215169 [Multi-domain]  Cd Length: 286  Bit Score: 120.27  E-value: 1.71e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490874292   3 FLHTMIRVTDLDKSIEFYTKVLGMKELERHENKDYRYTLVFVGY--EQGGTTIELTYNWDTNEYEMGSAFGHLALGVDDI 80
Cdd:PLN02300 155 LCQVMLRVGDLDRSIKFYEKAFGMKLLRKRDNPEYKYTIAMMGYgpEDKTTVLELTYNYGVTEYTKGNAYAQIAIGTDDV 234

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 490874292  81 YAACDKIKSLGGNVTREAGPVKGGSTHIAFITDPDGYQIELI 122
Cdd:PLN02300 235 YKTAEAIKLVGGKITREPGPLPGINTKITACLDPDGWKTVFV 276
PLN03042 PLN03042
Lactoylglutathione lyase; Provisional
 3-125 1.49e-30

Lactoylglutathione lyase; Provisional


Pssm-ID: 215548  Cd Length: 185  Bit Score: 107.60  E-value: 1.49e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490874292   3 FLHTMIRVTDLDKSIEFYTKVLGMKELERHENKDYRYTLVFVGYEQGGT-----------------TIELTYNWDTNE-- 63
Cdd:PLN03042  28 MQQTMFRIKDPKASLDFYSRVLGMSLLKRLDFPEMKFSLYFLGYEDSETaptdppertvwtfgrkaTIELTHNWGTESdp 107

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490874292  64 ----YEMGSA----FGHLALGVDDIYAACDKIKSLGgnVTREAGPVKGGSTHIAFITDPDGYQIELIQLG 125
Cdd:PLN03042 108 efkgYHNGNSdprgFGHIGITVDDVYKACERFEKLG--VEFVKKPDDGKMKGLAFIKDPDGYWIEIFDLK 175
Glyoxalase pfam00903
Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;
2-121 5.43e-29

Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;


Pssm-ID: 395724 [Multi-domain]  Cd Length: 121  Bit Score: 101.76  E-value: 5.43e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490874292    2 KFLHTMIRVTDLDKSIEFYTKVLGMKELERHENKDYrYTLVFVGYEQGGTTIELTYNWDTNEYEMG---SAFGHLALGVD 78
Cdd:pfam00903   1 RIDHVALRVGDLEKSLDFYTDVLGFKLVEETDAGEE-GGLRSAFFLAGGRVLELLLNETPPPAAAGfggHHIAFIAFSVD 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 490874292   79 DIYAACDKIKSLGGNVTREAGPVKGGSThIAFITDPDGYQIEL 121
Cdd:pfam00903  80 DVDAAYDRLKAAGVEIVREPGRHGWGGR-YSYFRDPDGNLIEL 121
PLN02367 PLN02367
lactoylglutathione lyase
 5-124 8.36e-29

lactoylglutathione lyase


Pssm-ID: 177995  Cd Length: 233  Bit Score: 104.31  E-value: 8.36e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490874292   5 HTMIRVTDLDKSIEFYTKVLGMKELERHENKDYRYTLVFVGYEQGGT-----------------TIELTYNWDTNE---- 63
Cdd:PLN02367  78 QTMYRIKDPKASLDFYSRVLGMSLLKRLDFPEMKFSLYFMGYEDTASaptdptertvwtfgqkaTIELTHNWGTESdpdf 157

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490874292  64 --YEMGSA----FGHLALGVDDIYAACDKIKSLGGNVTREagPVKGGSTHIAFITDPDGYQIELIQL 124
Cdd:PLN02367 158 kgYHNGNSeprgFGHIGITVDDVYKACERFEELGVEFVKK--PNDGKMKGIAFIKDPDGYWIEIFDL 222
VOC cd06587
vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate (VOC) superfamily is composed ...
 5-121 1.69e-21

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: 82.19  E-value: 1.69e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490874292   5 HTMIRVTDLDKSIEFYTKVLGMKELERHENKDYrytlVFVGYEqGGTTIELTYnWDTNEYEMGSAFGHLALGVDDIYAAC 84
Cdd:cd06587    1 HVALRVPDLDASVAFYEEVLGFEVVSRNEGGGF----AFLRLG-PGLRLALLE-GPEPERPGGGGLFHLAFEVDDVDEVD 74

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 490874292  85 DKIKSLGGNVTREAGPV-KGGSTHIAFITDPDGYQIEL 121
Cdd:cd06587   75 ERLREAGAEGELVAPPVdDPWGGRSFYFRDPDGNLIEF 112
VOC COG3324
Lactoylglutathione lyase-related enzyme, vicinal oxygen chelate (VOC) family [General function ...
 1-123 1.83e-20

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


Pssm-ID: 442553 [Multi-domain]  Cd Length: 119  Bit Score: 79.68  E-value: 1.83e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490874292   1 MKFLHTMIRVTDLDKSIEFYTKVLGMkELERHENKDYRYTLVFVGyeqGGTTIELTynwdTNEYEMGSAFGHLALGVDDI 80
Cdd:COG3324    3 GTIVWVELPVDDLERAKAFYEEVFGW-TFEDDAGPGGDYAEFDTD---GGQVGGLM----PGAEEPGGPGWLLYFAVDDL 74

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 490874292  81 YAACDKIKSLGGNVTREAGPVKGGStHIAFITDPDGYQIELIQ 123
Cdd:COG3324   75 DAAVARVEAAGGTVLRPPTDIPPWG-RFAVFRDPEGNRFGLWQ 116
GLOD4_N cd08358
N-terminal domain of human glyoxalase domain-containing protein 4 and similar proteins; ...
 4-122 6.00e-15

N-terminal domain of human glyoxalase domain-containing protein 4 and similar proteins; Uncharacterized subfamily of the vicinal oxygen chelate (VOC) superfamily contains human glyoxalase domain-containing protein 4 and similar proteins. VOC 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: 319946  Cd Length: 127  Bit Score: 65.85  E-value: 6.00e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490874292   4 LHTMIRVTDLDKSIEFYTKVLGMKELeRHE----------NKDY--RYTLVFVGY--EQGGTTIELTYNWDTNEYEMGSA 69
Cdd:cd08358    4 LHFVFKVGDRNKTIKFYREILGMKVL-RHEefeegckaacNGPYdgKWSKTMVGYgpEDDHFVVELTYNYGIGDYELGND 82

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 490874292  70 FGHLALGVDDIYAACDKIKSlggnvtreagPVKGGSTHIAFITDPDGYQIELI 122
Cdd:cd08358   83 FLGITIHSKQAVSRAKKHNW----------PVTQVGDGVYEVKAPGGYKFYLI 125
CatE COG2514
Catechol-2,3-dioxygenase [Secondary metabolites biosynthesis, transport and catabolism];
1-122 2.76e-14

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


Pssm-ID: 442004 [Multi-domain]  Cd Length: 141  Bit Score: 64.59  E-value: 2.76e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490874292   1 MKFLHTMIRVTDLDKSIEFYTKVLGMKELERHENkdyrytLVFVGYEQGGTTIELTYNWDTNEYEMGSAFGHLALGVD-- 78
Cdd:COG2514    2 TRLGHVTLRVRDLERSAAFYTDVLGLEVVEREGG------RVYLRADGGEHLLVLEEAPGAPPRPGAAGLDHVAFRVPsr 75

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 490874292  79 -DIYAACDKIKSLGGNVTreaGPVKGGSTHIAFITDPDGYQIELI 122
Cdd:COG2514   76 aDLDAALARLAAAGVPVE---GAVDHGVGESLYFRDPDGNLIELY 117
PhnB COG2764
Zn-dependent glyoxalase, PhnB family [Energy production and conversion];
4-123 5.10e-13

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


Pssm-ID: 442048 [Multi-domain]  Cd Length: 118  Bit Score: 60.64  E-value: 5.10e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490874292   4 LHTMIRVTDLDKSIEFYTKVLGMKELERHENKDYRytLVFVGYEQGGTTIELTYNWDTNEYEMGSAFgHLALGVDDIYAA 83
Cdd:COG2764    2 VTPYLVVDDAEEALEFYEDVFGFEVVFRMTDPDGK--IMHAELRIGGSVLMLSDAPPDSPAAEGNGV-SLSLYVDDVDAL 78

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 490874292  84 CDKIKSLGGNVTREAGPVKGGSTHiAFITDPDGYQIELIQ 123
Cdd:COG2764   79 FARLVAAGATVVMPLQDTFWGDRF-GMVRDPFGVLWMINT 117
VOC_like cd07263
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 5-123 5.71e-13

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: 60.77  E-value: 5.71e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490874292   5 HTMIRVTDLDKSIEFYTKVLGMKELERHENKDYRyTLVFVGYEQGGTTIELTYN-WDTNEYEMGSAFGHLA---LGVDDI 80
Cdd:cd07263    1 QVMLYVDDQDKALDFYVEKLGFEVVEDVPMGGMR-WVTVAPPGSPGTSLLLEPKaHPAQMPQSPEAAGGTPgilLATDDI 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 490874292  81 YAACDKIKSLGGNVTREagPVKGGSTHIAFITDPDGYQIELIQ 123
Cdd:cd07263   80 DATYERLTAAGVTFVQE--PTQMGGGRVANFRDPDGNLFALME 120
VOC_like cd07264
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 3-121 7.67e-12

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: 57.73  E-value: 7.67e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490874292   3 FLHTMIRVTDLDKSIEFYTKVLGMKelERHENKDYRYTLVFVgyeqGGTTIELTYN----WDTNEYEMGSAFgHLALGVD 78
Cdd:cd07264    1 IAYIVLYVDDFAASLRFYRDVLGLP--PRFLHEEGEYAEFDT----GETKLALFSRkemaRSGGPDRRGSAF-ELGFEVD 73

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 490874292  79 DIYAACDKIKSLGGNVTREAgPVKGGSTHIAFITDPDGYQIEL 121
Cdd:cd07264   74 DVEATVEELVERGAEFVREP-ANKPWGQTVAYVRDPDGNLIEI 115
MMCE cd07249
Methylmalonyl-CoA epimerase (MMCE); MMCE, also called methylmalonyl-CoA racemase (EC 5.1.99.1) ...
 5-123 1.13e-11

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: 57.59  E-value: 1.13e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490874292   5 HTMIRVTDLDKSIEFYTKVLGMKELERHENKDYRYTLVFVGYeqGGTTIEL------TYNWDTNEYEMGSAFGHLALGVD 78
Cdd:cd07249    3 HIGIAVPDLDEALKFYEDVLGVKVSEPEELEEQGVRVAFLEL--GNTQIELleplgeDSPIAKFLDKKGGGLHHIAFEVD 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 490874292  79 DIYAACDKIKSLGGNVTREAGPVKGGSTHIAFI--TDPDGYQIELIQ 123
Cdd:cd07249   81 DIDAAVEELKAQGVRLLSEGPRIGAHGKRVAFLhpKDTGGVLIELVE 127
metmalonyl_epim TIGR03081
methylmalonyl-CoA epimerase; Members of this protein family are the enzyme methylmalonyl-CoA ...
 2-123 4.02e-11

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: 56.18  E-value: 4.02e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490874292    2 KFLHTMIRVTDLDKSIEFYTKVLGMKELERHENKDYRYTLVFVgyEQGGTTIELTYNWDTNE------YEMGSAFGHLAL 75
Cdd:TIGR03081   1 RIDHVGIAVPDLEEAAKFYEDVLGAQVSEIEELPEQGVKVVFI--ALGNTKVELLEPLGEDSpiakflEKNGGGIHHIAI 78

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 490874292   76 GVDDIYAACDKIKSLGGNVTREAGPVKGGSTHIAFI--TDPDGYQIELIQ 123
Cdd:TIGR03081  79 EVDDIEAALETLKEKGVRLIDEEPRIGAHGKPVAFLhpKSTGGVLIELEQ 128
ED_TypeI_classII_N cd16360
N-terminal domain of type I, class II extradiol dioxygenases; This family contains the ...
 5-122 1.11e-10

N-terminal domain of type I, class II extradiol dioxygenases; This family contains the N-terminal non-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: 319967  Cd Length: 111  Bit Score: 54.63  E-value: 1.11e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490874292   5 HTMIRVTDLDKSIEFYTKVLGMKELERHENKDYrytlvFVGYEqggttielTYNWDTNEYE-MGSAFGHLALGV---DDI 80
Cdd:cd16360    1 YAELGVPDLEKALEFYTDVLGLQVAKRDGNSVY-----LRGYE--------DEHHSLVLYEaPEAGLKHFAFEVaseEDL 67

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 490874292  81 YAACDKIKSLGGNVTR-EAGPVKGGSTHIAFiTDPDGYQIELI 122
Cdd:cd16360   68 ERAAASLTALGCDVTWgPDGEVPGGGKGFRF-QDPSGHLLELF 109
Glyoxalase_4 pfam13669
Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;
5-110 1.84e-10

Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;


Pssm-ID: 463951 [Multi-domain]  Cd Length: 109  Bit Score: 53.82  E-value: 1.84e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490874292    5 HTMIRVTDLDKSIEFYTKVLGMKELERHENKDYRYTLVFVGYEQGGTTIELTYNWDTNEY--EMGSAFGHLALGVDDIYA 82
Cdd:pfam13669   2 HVGIAVPDLDRALALWGALLGLGPEGDYRSEPQNVDLAFALLGDGPVEVELIQPLDGDSPlaRHGPGLHHLAYWVDDLDA 81

                          90       100
                  ....*....|....*....|....*...
gi 490874292   83 ACDKIKSLGGNVTREAGPVKGGSTHIAF 110
Cdd:pfam13669  82 AVARLLDQGYRVAPKGPRAGAAGRRVAF 109
VOC_ShValD_like cd16361
vicinal oxygen chelate (VOC) family protein similar to Streptomyces hygroscopicus ValD protein; ...
 2-124 1.97e-10

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: 54.64  E-value: 1.97e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490874292   2 KFLHTMIRVTDLDKSIEFYTKVLGMK--------ELERHENKDYRYTLVFVGYEQ---------GGTTIEL-TY--NWDT 61
Cdd:cd16361    1 GVNHVGITVPDLDAAVEFYTDVLGAEvvyrstplAEGDRGGGEMRAAGFVPGFARariamlrlgPGPGIELfEYkgPEQR 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490874292  62 NEYEMGSAFG--HLALGVDDIYAACDKIKSLGGNV------TREAGPVKGgsTHIAFITDPDGYQIELIQL 124
Cdd:cd16361   81 APVPRNSDVGifHFALQVDDVEAAAERLAAAGGKVlmgpreIPDGGPGKG--NRMVYLRDPWGTLIELVSH 149
VOC_like cd07245
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 3-121 4.42e-10

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: 53.09  E-value: 4.42e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490874292   3 FLHTMIRVTDLDKSIEFYTKVLGMKELERHENKDYRYTLVFVGYEQGGTTIELTYNWDTNEYEMGSAFGHLALGVDDIYA 82
Cdd:cd07245    1 LDHVALACPDLERARRFYTDVLGLEEVPRPPFLKFGGAWLYLGGGQQIHLVVEQNPSELPRPEHPGRDRHPSFSVPDLDA 80

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 490874292  83 ACDKIKSLGGNVTREAGPVkGGSTHIaFITDPDGYQIEL 121
Cdd:cd07245   81 LKQRLKEAGIPYTESTSPG-GGVTQL-FFRDPDGNRLEF 117
GLOD4_C cd16357
C-terminal domain of human glyoxalase domain-containing protein 4 and similar proteins; ...
 7-119 1.68e-09

C-terminal domain of human glyoxalase domain-containing protein 4 and similar proteins; Uncharacterized subfamily of the vicinal oxygen chelate (VOC) superfamily contains human glyoxalase domain-containing protein 4 and similar proteins. VOC 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: 319964  Cd Length: 114  Bit Score: 51.40  E-value: 1.68e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490874292   7 MIRVTDLDKSIEFYTKVLGMKELERHENKdyrytlVFVGYEQGGTTIELTynwDTNE-YEMGSAFGHLALgvddiyaAC- 84
Cdd:cd16357    3 SLAVSDLEKSIDYWSDLLGMKVFEKSEKS------ALLGYGEDQAKLELV---DIPEpVDHGTAFGRIAF-------SCp 66

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 490874292  85 --------DKIKSLGGNVTREagPVK----GGST-HIAFITDPDGYQI 119
Cdd:cd16357   67 adelppieEKVKAAGQTILTP--LVSldtpGKATvQVVILADPDGHEI 112
HppD COG3185
4-hydroxyphenylpyruvate dioxygenase and related hemolysins [Amino acid transport and ...
 12-117 2.15e-09

4-hydroxyphenylpyruvate dioxygenase and related hemolysins [Amino acid transport and metabolism, General function prediction only];


Pssm-ID: 442418 [Multi-domain]  Cd Length: 333  Bit Score: 53.36  E-value: 2.15e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490874292  12 DLDKSIEFYTKVLGMKELERHENKDyRYTLV---FVGYEQGGTTIELtyNWDTN---------EYEMGSAFGHLALGVDD 79
Cdd:COG3185  158 DLDEWVLFYEDVLGFEEIREEDIED-PYQGVrsaVLQSPDGKVRIPL--NEPTSpdsqiaeflEKYRGEGIQHIAFATDD 234

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 490874292  80 IYAACDKIKSLGgnvtreagpvkggsthIAFITDPDGY 117
Cdd:COG3185  235 IEATVAALRARG----------------VRFLDIPDNY 256
SgaA_N_like cd07247
N-terminal domain of Streptomyces griseus SgaA and similar domains; SgaA suppresses the growth ...
 10-123 2.49e-09

N-terminal domain of Streptomyces griseus SgaA and similar domains; SgaA suppresses the growth disturbances caused by high osmolarity and a high concentration of A-factor, a microbial hormone, during the early growth phase in Streptomyces griseus. A-factor (2-isocapryloyl-3R-hydroxymethyl-gamma-butyrolactone) controls morphological differentiation and secondary metabolism in Streptomyces griseus. It is a chemical signaling molecule that at a very low concentration acts as a switch for yellow pigment production, aerial mycelium formation, streptomycin production, and streptomycin resistance. The structure and amino acid sequence of SgaA are closely related to a group of antibiotics resistance proteins, including bleomycin resistance protein, mitomycin resistance protein, and fosfomycin resistance proteins. SgaA might also function as a streptomycin resistance protein.


Pssm-ID: 319911 [Multi-domain]  Cd Length: 114  Bit Score: 51.11  E-value: 2.49e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490874292  10 VTDLDKSIEFYTKVLG--MKELERHENkdyRYTLVFVGYEQGGTTIELTYNWDtneyEMGSAFgHLALGVDDIYAACDKI 87
Cdd:cd07247    8 TTDLERAKAFYGAVFGwtFEDEGDGGG---DYALFTAGGGAVGGLMRAPEEVA----GAPPGW-LIYFAVDDLDAALARV 79

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 490874292  88 KSLGGNVTREAGPVkGGSTHIAFITDPDGYQIELIQ 123
Cdd:cd07247   80 EAAGGKVVVPPTDI-PGGGRFAVFADPEGNRFGLWS 114
VOC_like cd07251
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 10-121 1.77e-08

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: 319914 [Multi-domain]  Cd Length: 120  Bit Score: 48.83  E-value: 1.77e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490874292  10 VTDLDKSIEFYTKvLGMKELERHENKdyrytlvFVGYEQGGTTIELtYNWDTNEYEMGSAFGH-------LALGV---DD 79
Cdd:cd07251    6 VRDLERSARFYEA-LGWKPNLDPNDG-------VVFFQLGGTVLAL-YPRDALAEDAGVSVTGagfsgvtLAHNVrsrEE 76

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 490874292  80 IYAACDKIKSLGGNVTREAGPVKGGSTHiAFITDPDGYQIEL 121
Cdd:cd07251   77 VDQLLAKAVAAGGKILKPPQEVFWGGYS-GYFADPDGHIWEV 117
COG3607 COG3607
Lactoylglutathione lyase-related enzyme, vicinal oxygen chelate (VOC) family [General function ...
 10-123 3.07e-08

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


Pssm-ID: 442825  Cd Length: 126  Bit Score: 48.29  E-value: 3.07e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490874292  10 VTDLDKSIEFYTKvLGMKELERHENKDyrYTLVFVGyeqGGTTIEL----TYNWDTNEyEMGSAFGH----LALGVD--- 78
Cdd:COG3607   11 VADLERSRAFYEA-LGFTFNPQFSDEG--AACFVLG---EGIVLMLlpreKFATFTGK-PIADATGFtevlLALNVEsre 83

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 490874292  79 DIYAACDKIKSLGGNVTREAGPVKGGstHIAFITDPDGYQIELIQ 123
Cdd:COG3607   84 EVDALVAKALAAGGTVLKPPQDVGGM--YSGYFADPDGHLWEVAW 126
VOC_Bs_YwkD_like cd08352
vicinal oxygen chelate (VOC) family protein Bacillus subtilis YwkD and similar proteins; ...
 1-121 5.44e-08

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: 47.54  E-value: 5.44e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490874292   1 MKFLHTMIRVTDLDKSIEFYTKVLGMKELERH---ENKDYRYTLVFvgyeqGGTTIEL----------TYnwdtneyemG 67
Cdd:cd08352    1 KKIHHIAIICSDYEKSKDFYVDKLGFEIIREHyrpERNDIKLDLAL-----GGYQLELfikpdaparpSY---------P 66

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490874292  68 SAFG--HLALGVDDIYAACDKIKSLGgnVTREagPVK-----GgsTHIAFITDPDGYQIEL 121
Cdd:cd08352   67 EALGlrHLAFKVEDVEATVAELKSLG--IETE--PIRvddftG--KKFTFFFDPDGLPLEL 121
VOC_BsYqjT cd07242
vicinal oxygen chelate (VOC) family protein similar to Bacillus subtilis YqjT; The vicinal ...
 3-122 6.46e-08

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: 47.48  E-value: 6.46e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490874292   3 FLHTMIRVTDLDKSIEFYTKVLGM--KELER----HENKDYRYTLVFVGYEQGGTTIEltynwdtnEYEMGSAFGHLALG 76
Cdd:cd07242    2 VSHVELAVSDLHRSFKWFEWILGLgwKEYDTwsfgPSWKLSGGSLLVVQQTDEFATPE--------FDRARVGLNHLAFH 73

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 490874292  77 ------VDDIYAacdKIKSLGGNVT-REAGPVKGGSTH-IAFITDPDGYQIELI 122
Cdd:cd07242   74 aesreaVDELTE---KLAKIGGVRTyGDRHPFAGGPPHyAAFCEDPDGIKLELV 124
GLOD5 cd07253
Human glyoxalase domain-containing protein 5 and similar proteins; Uncharacterized subfamily ...
 5-121 3.59e-07

Human glyoxalase domain-containing protein 5 and similar proteins; Uncharacterized subfamily of VOC family contains human glyoxalase domain-containing protein 5 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: 319916 [Multi-domain]  Cd Length: 123  Bit Score: 45.68  E-value: 3.59e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490874292   5 HTMIRVTDLDKSIEFYTKVLGMKELERHENkdyRYTLVFvgyeqGGTTIELtynWDTnEYEMGSAFGHLALGVDDIyaaC 84
Cdd:cd07253    6 HLVLTVKDIERTIDFYTKVLGMTVVTFKEG---RKALRF-----GNQKINL---HQK-GKEFEPKASAPTPGSADL---C 70

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 490874292  85 DKIKSL---------GGNVTREAGPVKGGSTHIA----FITDPDGYQIEL 121
Cdd:cd07253   71 FITETPidevlehleACGVTIEEGPVKRTGALGPilsiYFRDPDGNLIEL 120
FosA cd07244
fosfomycin resistant protein subfamily FosA; This subfamily family contains FosA, a fosfomycin ...
 5-121 9.91e-07

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: 44.20  E-value: 9.91e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490874292   5 HTMIRVTDLDKSIEFYTKVLGMKELERHENKDYrytlvfvgYEQGGTTIELTYNwdtNEYEMGSAFGHLALGVD--DIYA 82
Cdd:cd07244    4 HITLAVSDLERSLAFYVDLLGFKPHVRWDKGAY--------LTAGDLWLCLSLD---PAAEPSPDYTHIAFTVSeeDFEE 72

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 490874292  83 ACDKIKSLGgnvtreagpVK--------GGSThiaFITDPDGYQIEL 121
Cdd:cd07244   73 LSERLRAAG---------VKiwqensseGDSL---YFLDPDGHKLEL 107
VOC_BsCatE_like_N cd07255
N-terminal of Bacillus subtilis CatE like protein; Uncharacterized subfamily of VOC ...
 9-121 2.35e-06

N-terminal of Bacillus subtilis CatE like protein; Uncharacterized subfamily of VOC superfamily contains Bacillus subtilis CatE and similar proteins. CatE is proposed to function as Catechol-2,3-dioxygenase. VOC 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: 319918  Cd Length: 124  Bit Score: 43.45  E-value: 2.35e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490874292   9 RVTDLDKSIEFYTKVLGMKELERHENKdyrytlVFVGYEQGGTTIELTYNWDTNEYEMgSAFG--HLALGVDDIYAACDK 86
Cdd:cd07255    9 KVADLERQSAFYQNVIGLSVLKQNASR------AYLGVDGKQVLLVLEAIPDAVLAPR-STTGlyHFAILLPDRKALGRA 81

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 490874292  87 IKSLGGNvtreaGPVKGGSTHI---AFI-TDPDGYQIEL 121
Cdd:cd07255   82 LAHLAEH-----GPLIGAADHGvseAIYlSDPEGNGIEI 115
FosB cd08363
fosfomycin resistant protein subfamily FosB; This subfamily family contains FosB, a fosfomycin ...
 5-121 5.63e-06

fosfomycin resistant protein subfamily FosB; This subfamily family contains FosB, a fosfomycin resistant protein. FosB is a Mg(2+)-dependent L-cysteine thiol transferase. Fosfomycin inhibits the enzyme UDP-nacetylglucosamine-3-enolpyruvyltransferase (MurA), which catalyzes the first committed step in bacterial cell wall biosynthesis. FosB catalyzes the Mg(II) dependent addition of L-cysteine to the epoxide ring of fosfomycin, (1R,2S)-epoxypropylphosphonic acid, rendering it inactive. FosB is evolutionarily related to glyoxalase I and type I extradiol dioxygenases.


Pssm-ID: 319951 [Multi-domain]  Cd Length: 131  Bit Score: 42.72  E-value: 5.63e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490874292   5 HTMIRVTDLDKSIEFYTKVLGMKELERHENKDYrytlvfvgYEQGGTTIELTYNWDTNEYEMGSAFGHLALGVD--DIYA 82
Cdd:cd08363    3 HITFSVSNLNKSIAFYKDVLDAKLLVLGEKTAY--------FDLNGLWLALNVQEDIPRNEISHSYTHIAFSIDeeDLDA 74

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 490874292  83 ACDKIKSLGGNVtreagpVKGGSTHIA-----FITDPDGYQIEL 121
Cdd:cd08363   75 FKERLKDNGVNI------LEGRKRDILegqsiYFTDPDGHLFEL 112
VOC_like cd07262
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 3-120 9.70e-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: 41.83  E-value: 9.70e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490874292   3 FLHTMIRVTDLDKSIEFYTKV---LGMKELERHENkdyrytlvFVGY-EQGGTTIELTYNWDTNEYEMGSAFgHLAL--- 75
Cdd:cd07262    1 ISHVTIGVNDLERSRAFYDAAlapLGYKRGFEDGG--------RVGYgLEGGPDFWVTEPFDGEPATAGNGT-HVAFaap 71

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 490874292  76 ---GVDDIYAACDKiksLGGNVTREAG--PVKGGSTHIAFITDPDGYQIE 120
Cdd:cd07262   72 sraAVDAFHAAALA---AGGTDNGAPGlrPHYHPGYYAAYVRDPDGNKIE 118
HPCD_N_class_II cd07266
N-terminal domain of 3,4-dihydroxyphenylacetate 2,3-dioxygenase (HPCD); This subfamily ...
 5-121 2.75e-05

N-terminal domain of 3,4-dihydroxyphenylacetate 2,3-dioxygenase (HPCD); This subfamily contains the N-terminal, non-catalytic, domain of HPCD. HPCD catalyses the second step in the degradation of 4-hydroxyphenylacetate to succinate and pyruvate. The aromatic ring of 4-hydroxyphenylacetate is opened by this dioxygenase to yield the 3,4-diol product, 2-hydroxy-5-carboxymethylmuconate semialdehyde. HPCD is a homotetramer and each monomer contains two structurally homologous barrel-shaped domains at the N- and C-terminus. The active-site metal is located in the C-terminal barrel and plays an essential role in the catalytic mechanism. Most extradiol dioxygenases contain Fe(II) in their active site, but HPCD can be activated by either Mn(II) or Fe(II). These enzymes belong to the type I class II family of extradiol dioxygenases. The class III 3,4-dihydroxyphenylacetate 2,3-dioxygenases belong to a different superfamily.


Pssm-ID: 319927  Cd Length: 118  Bit Score: 40.47  E-value: 2.75e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490874292   5 HTMIRVTDLDKSIEFYTKVLGMKELERHENKDYRYTLvfvgYEQGGTTIELTYNwdtneyeMGSAFGHLALGV---DDIY 81
Cdd:cd07266    7 HAELVVTDLAASREFYVDTLGLHVTDEDDNAIYLRGV----EEFIHHTLVLRKA-------PEAAVGHLGFRVrdeADLD 75

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 490874292  82 AACDKIKSLGGNVTREAGPVKGGSTHiafITDPDGYQIEL 121
Cdd:cd07266   76 KAAAFYKELGLPTEWREEPGQGRTLR---VEDPFGFPIEF 112
Fosfomycin_RP cd08345
Fosfomycin resistant protein; This family contains three types of fosfomycin resistant protein. ...
 5-121 3.15e-05

Fosfomycin resistant protein; This family contains three types of fosfomycin resistant protein. Fosfomycin inhibits the enzyme UDP-N-acetylglucosamine-3-enolpyruvyltransferase (MurA), which catalyzes the first committed step in bacterial cell wall biosynthesis. The three types of fosfomycin resistance proteins, employ different mechanisms to render fosfomycin [(1R,2S)-epoxypropylphosphonic acid] inactive. FosB catalyzes the addition of L-cysteine to the epoxide ring of fosfomycin. FosX catalyzes the addition of a water molecule to the C1 position of the antibiotic with inversion of configuration at C1. FosA catalyzes the addition of glutathione to the antibiotic fosfomycin, making it inactive. Catalytic activities of both FosX and FosA are Mn(II)-dependent, but FosB is activated by Mg(II). Fosfomycin resistant proteins are evolutionarily related to glyoxalase I and type I extradiol dioxygenases.


Pssm-ID: 319933  Cd Length: 118  Bit Score: 40.23  E-value: 3.15e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490874292   5 HTMIRVTDLDKSIEFYTKVLGMKELERHENKDY-----RYTL---VFVGYEQGGTTIELTYNwdtneyemgsafgHLALG 76
Cdd:cd08345    1 HITLIVRDLEKSTAFLQDIFGAREVYSSGDKTFslskeKFFLlggLWIALMEGESLQERSYT-------------HIAFQ 67

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 490874292  77 VD----DIYAAcdKIKSLGGNVTREAGPVKGGSTHIAFiTDPDGYQIEL 121
Cdd:cd08345   68 IQsedfDRYAE--RLGALGVEMRPPRPRVEGEGRSIYF-YDPDNHLFEL 113
PRK04101 PRK04101
metallothiol transferase FosB;
5-121 5.78e-05

metallothiol transferase FosB;


Pssm-ID: 179740  Cd Length: 139  Bit Score: 39.93  E-value: 5.78e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490874292   5 HTMIRVTDLDKSIEFYTKVLGMKELERHENKDYrytlvfvgYEQGGTTIELTYNWDTNEYEMGSAFGHLALGVD--DIYA 82
Cdd:PRK04101   7 HICFSVSNLEKSIEFYEKVLGAKLLVKGRKTAY--------FDLNGLWIALNEEKDIPRNEIHQSYTHIAFSIEeeDFDH 78

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 490874292  83 ACDKIKSLGGNVtreagpVKGGSTHIA-----FITDPDGYQIEL 121
Cdd:PRK04101  79 WYQRLKENDVNI------LPGRERDERdkksiYFTDPDGHKFEF 116
VOC_like cd07254
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 2-120 8.53e-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: 319917 [Multi-domain]  Cd Length: 120  Bit Score: 39.37  E-value: 8.53e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490874292   2 KFLHTMIRVTDLDKSIEFYTKVLGMKELERHEnkDYRYTLV------FVGYEQGGTTieltynwdtneyemGSAFGHLAL 75
Cdd:cd07254    1 KRFHLSLNVTDLERSIRFYSDLFGAEPAKRKA--DYAKFMLedpplnLALLVNDRKE--------------PYGLNHLGI 64

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 490874292  76 GVDDIYAACDKIKSL--GGNVTREAGPVK--GGSTHIAFITDPDGYQIE 120
Cdd:cd07254   65 QVDSKEEVAALKARAeaAGLPVRKEPRTTccYAVQDKFWLTDPDGNAWE 113
PRK11478 PRK11478
VOC family protein;
5-123 1.02e-04

VOC family protein;


Pssm-ID: 183156 [Multi-domain]  Cd Length: 129  Bit Score: 39.11  E-value: 1.02e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490874292   5 HTMIRVTDLDKSIEFYTKVLG---MKELERHENKDYRYTLVFvgyeQGGTTIEL-TYNWDTNEYEMGSAFG--HLALGVD 78
Cdd:PRK11478   9 HIAIIATDYAVSKAFYCDILGftlQSEVYREARDSWKGDLAL----NGQYVIELfSFPFPPERPSRPEACGlrHLAFSVD 84

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 490874292  79 DIYAACDKIKSLGgnVTREA---GPVKGgsTHIAFITDPDGYQIELIQ 123
Cdd:PRK11478  85 DIDAAVAHLESHN--VKCEAirvDPYTQ--KRFTFFNDPDGLPLELYE 128
2_3_CTD_N cd07265
N-terminal domain of catechol 2,3-dioxygenase; This subfamily contains the N-terminal, ...
 5-31 2.74e-04

N-terminal domain of catechol 2,3-dioxygenase; This subfamily contains the N-terminal, non-catalytic, domain of catechol 2,3-dioxygenase. Catechol 2,3-dioxygenase (2,3-CTD, catechol:oxygen 2,3-oxidoreductase) catalyzes an extradiol cleavage of catechol to form 2-hydroxymuconate semialdehyde with the insertion of two atoms of oxygen. The enzyme is a homotetramer and contains catalytically essential Fe(II) . The reaction proceeds by an ordered bi-unit mechanism. First, catechol binds to the enzyme, this is then followed by the binding of dioxygen to form a tertiary complex, and then the aromatic ring is cleaved to produce 2-hydroxymuconate semialdehyde. Catechol 2,3-dioxygenase belongs to the type I extradiol dioxygenase family. The subunit comprises 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. This subfamily represents the N-terminal domain.


Pssm-ID: 319926  Cd Length: 122  Bit Score: 37.71  E-value: 2.74e-04
                         10        20
                 ....*....|....*....|....*..
gi 490874292   5 HTMIRVTDLDKSIEFYTKVLGMKELER 31
Cdd:cd07265    7 HVQLRVLDLEEAIKHYREVLGLVETGR 33
Glyoxalase_2 pfam12681
Glyoxalase-like domain; This domain is related to the Glyoxalase domain pfam00903.
 3-121 7.01e-04

Glyoxalase-like domain; This domain is related to the Glyoxalase domain pfam00903.


Pssm-ID: 403776  Cd Length: 118  Bit Score: 36.62  E-value: 7.01e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490874292    3 FLHTMIRVTDLDKSIEFYTKVLGMKELERHENkdyrytlvFVGYEqGGTTIELTYNWDTN----EYEMGSAFgHLALGVD 78
Cdd:pfam12681   1 FKCPLLVVKDINISRKFYEDVLDQKIKLDFGE--------NVSFE-GGFAIQSDFKELIGidlsIAEQSNNF-ELYFEVA 70

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 490874292   79 DIYAACDKIKSLGG-NVTREAGPVKGGSThIAFITDPDGYQIEL 121
Cdd:pfam12681  71 DVDAFLQKIKEIGNiEYLHELKEQPWGQR-VFRFYDPDGHIIEI 113
VOC_like cd09011
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 1-121 1.60e-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: 319953  Cd Length: 122  Bit Score: 35.91  E-value: 1.60e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490874292   1 MKFLHTMIRVTDLDKSIEFYTKVLGMKELErhenkDYRYTLVFvgyeQGGTTIELTYNWDT--NEYEMGSAFG----HLA 74
Cdd:cd09011    1 MKFVNPLLVVKDIEKSKKFYEDVLGQKILL-----DFGENVVF----EGGFALQEKKSWLEtiIISDLSIKQQsnnfELY 71

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 490874292  75 LGVDDIYAACDKIKSLGG-NVTREAGPVKGGSTHIAFItDPDGYQIEL 121
Cdd:cd09011   72 FEVDDFDAFFEKLNPHKDiEFIHPILEHPWGQRVFRFY-DPDGHIIEI 118
VOC_like cd07246
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 10-117 1.63e-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: 319910 [Multi-domain]  Cd Length: 124  Bit Score: 35.74  E-value: 1.63e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490874292  10 VTDLDKSIEFYTKVLGMKELERHENKDYRytLVFVGYEQGGTTIELTynwDTNEyEMGSAFGH--------LALGVDDIY 81
Cdd:cd07246    9 VEDAAAAIAFYKKAFGAEELGRTTQEDGR--VGHAELRIGGTVVMVA---DENP-ERGALSPTklggtpviFHLYVEDVD 82

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 490874292  82 AACDKIKSLGGNVTREAgPVKGGSTHIAFITDPDGY 117
Cdd:cd07246   83 ATFARAVAAGAVVVEPV-EDQFWGDRVGKVKDPFGH 117
PpCmtC_N cd08361
N-terminal domain of 2,3-dihydroxy-p-cumate-3,4-dioxygenase (PpCmtC); This subfamily contains ...
 12-122 3.70e-03

N-terminal domain of 2,3-dihydroxy-p-cumate-3,4-dioxygenase (PpCmtC); This subfamily contains the N-terminal, non-catalytic, domain of PpCmtC. 2,3-dihydroxy-p-cumate-3,4-dioxygenase (CmtC of Pseudomonas putida F1) is a dioxygenase involved in the eight-step catabolism pathway of p-cymene. CmtC acts upon the reaction intermediate 2,3-dihydroxy-p-cumate, yielding 2-hydroxy-3-carboxy-6-oxo-7-methylocta-2,4-dienoate. The CmtC belongs to the type I family of extradiol dioxygenases. Fe2+ was suggested as a cofactor, same as other enzymes in the family. The type I family of extradiol dioxygenases contains two structurally homologous barrel-shaped domains at the N- and C-terminal. The active-site metal is located in the C-terminal barrel and plays an essential role in the catalytic mechanism.


Pssm-ID: 319949  Cd Length: 124  Bit Score: 34.88  E-value: 3.70e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490874292  12 DLDKSIEFYTKVLGMKELERHENK-----DYRY-TLVFVGYEQGGTTI--ELtynwdTNEYEMGSAFGHL-ALGVddiya 82
Cdd:cd08361   16 DLEEAVRFATDILGLELVRREGGAayfrsDDRDhTLCYFEGDPAEQTSgfEV-----RDPAELDAAAAELeSAGI----- 85

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 490874292  83 acdkikslggnvtreagPVKGGST------HI-AFIT--DPDGYQIELI 122
Cdd:cd08361   86 -----------------AVRRGTAeeceqrRVrAFISfrDPSGNRIELV 117
BLMA_like cd08349
Bleomycin binding protein (BLMA) and similar proteins; BLMA also called Bleomycin resistance ...
 9-37 7.67e-03

Bleomycin binding protein (BLMA) and similar proteins; BLMA also called Bleomycin resistance protein, confers Bm resistance by directly binding to Bm. Bm is a glycopeptide antibiotic produced naturally by actinomycetes. It is a potent anti-cancer drug, which acts as a strong DNA-cutting agent, thereby causing cell death. BLMA is produced by actinomycetes to protect themselves against their own lethal compound. BLMA has two identically-folded subdomains, with the same alpha/beta fold; these two halves have no sequence similarity. BLMAs are dimers and each dimer binds to two Bm molecules at the Bm-binding pockets formed at the dimer interface; two Bm molecules are bound per dimer. BLMA 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. As for the larger superfamily, this family contains members with or without domain swapping.


Pssm-ID: 319937 [Multi-domain]  Cd Length: 114  Bit Score: 33.74  E-value: 7.67e-03
                         10        20
                 ....*....|....*....|....*....
gi 490874292   9 RVTDLDKSIEFYTKVLGMKELERHENKDY 37
Cdd:cd08349    5 PVRDIDKTLAFYVDVLGFEVDYERPPPGY 33
 
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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