NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1534627144|gb|RSI88302|]
View 

Lactoylglutathione lyase [Streptococcus mitis]

Protein Classification

VOC family protein( domain architecture ID 10001243)

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
GloA COG0346
Catechol 2,3-dioxygenase or related enzyme, vicinal oxygen chelate (VOC) family [Secondary ...
 4-123 7.55e-37

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: 121.64  E-value: 7.55e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1534627144   4 KMLHTCLRVENLEKSIAFYQDAFGFKELRRRDFPDHAFTIVYLGLeGDDYELELTYNYDHGPYVVGDGFAHIALSTPDLE 83
Cdd:COG0346     2 GLHHVTLRVSDLEASLAFYTDVLGLELVKRTDFGDGGFGHAFLRL-GDGTELELFEAPGAAPAPGGGGLHHLAFRVDDLD 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1534627144  84 ALHQEHSAKGYEVTEPNGLPGTAPNYYFVKDPDGYKVEVI 123
Cdd:COG0346    81 AAYARLRAAGVEIEGEPRDRAYGYRSAYFRDPDGNLIELV 120
 
Name Accession Description Interval E-value
GloA COG0346
Catechol 2,3-dioxygenase or related enzyme, vicinal oxygen chelate (VOC) family [Secondary ...
 4-123 7.55e-37

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: 121.64  E-value: 7.55e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1534627144   4 KMLHTCLRVENLEKSIAFYQDAFGFKELRRRDFPDHAFTIVYLGLeGDDYELELTYNYDHGPYVVGDGFAHIALSTPDLE 83
Cdd:COG0346     2 GLHHVTLRVSDLEASLAFYTDVLGLELVKRTDFGDGGFGHAFLRL-GDGTELELFEAPGAAPAPGGGGLHHLAFRVDDLD 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1534627144  84 ALHQEHSAKGYEVTEPNGLPGTAPNYYFVKDPDGYKVEVI 123
Cdd:COG0346    81 AAYARLRAAGVEIEGEPRDRAYGYRSAYFRDPDGNLIELV 120
GlxI_Ni cd16358
Glyoxalase I that uses Ni(++) as cofactor; This family includes Escherichia coil and other ...
 5-123 5.87e-36

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: 119.42  E-value: 5.87e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1534627144   5 MLHTCLRVENLEKSIAFYQDAFGFKELRRRDFPDHAFTIVYLGL--EGDDYELELTYNYDHGPYVVGDGFAHIALSTPDL 82
Cdd:cd16358     1 MLHTMLRVGDLDRSIKFYTEVLGMKLLRKRDYPEGKYTLAFVGYgdEDENTVLELTYNWGVDKYDLGTAYGHIAIGVEDV 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1534627144  83 EALHQEHSAKGYEVT-EPNGLPGTAPNYYFVKDPDGYKVEVI 123
Cdd:cd16358    81 YETCERIRKKGGKVTrEPGPMKGGTTVIAFVEDPDGYKIELI 122
glyox_I TIGR00068
lactoylglutathione lyase; Lactoylglutathione lyase is also known as aldoketomutase and ...
 5-126 2.69e-35

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: 118.76  E-value: 2.69e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1534627144   5 MLHTCLRVENLEKSIAFYQDAFGFKELRRRDFPDHAFTIVYLGL--EGDDYELELTYNYDHGPYVVGDGFAHIALSTPDL 82
Cdd:TIGR00068  18 LLHTMLRVGDLDKSLDFYTEVLGMKLLRKRDFPEMKFSLAFLGYgdETSAAVIELTHNWGTEKYDLGNGFGHIAIGVDDV 97

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1534627144  83 EALHQEHSAKGYEVT-EPNGLPGTAPNYYFVKDPDGYKVEVIREK 126
Cdd:TIGR00068  98 YKACERVRALGGNVVrEPGPVKGGTTVIAFVEDPDGYKIELIQRK 142
PLN02300 PLN02300
lactoylglutathione lyase
 4-126 3.11e-29

lactoylglutathione lyase


Pssm-ID: 215169 [Multi-domain]  Cd Length: 286  Bit Score: 106.79  E-value: 3.11e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1534627144   4 KMLHTCLRVENLEKSIAFYQDAFGFKELRRRDFPDHAFTIVYLGL--EGDDYELELTYNYDHGPYVVGDGFAHIALSTPD 81
Cdd:PLN02300   24 RMLHVVYRVGDLDRTIKFYTECLGMKLLRKRDIPEEKYTNAFLGYgpEDSNFVVELTYNYGVDKYDIGTGFGHFGIAVED 103

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1534627144  82 LEALHQEHSAKGYEVT-EPNGLPGTAPNYYFVKDPDGYKVEVIREK 126
Cdd:PLN02300  104 VAKTVELVKAKGGKVTrEPGPVKGGKSVIAFVKDPDGYKFELIQRG 149
Glyoxalase pfam00903
Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;
4-122 4.91e-23

Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;


Pssm-ID: 395724 [Multi-domain]  Cd Length: 121  Bit Score: 86.73  E-value: 4.91e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1534627144   4 KMLHTCLRVENLEKSIAFYQDAFGFKELRRRDFPDHAfTIVYLGLEGDDYELELTYNY---DHGPYVVGDGFAHIALSTP 80
Cdd:pfam00903   1 RIDHVALRVGDLEKSLDFYTDVLGFKLVEETDAGEEG-GLRSAFFLAGGRVLELLLNEtppPAAAGFGGHHIAFIAFSVD 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1534627144  81 DLEALHQEHSAKGYEVTEPNGLPGTAPNYYFVKDPDGYKVEV 122
Cdd:pfam00903  80 DVDAAYDRLKAAGVEIVREPGRHGWGGRYSYFRDPDGNLIEL 121
 
Name Accession Description Interval E-value
GloA COG0346
Catechol 2,3-dioxygenase or related enzyme, vicinal oxygen chelate (VOC) family [Secondary ...
 4-123 7.55e-37

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: 121.64  E-value: 7.55e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1534627144   4 KMLHTCLRVENLEKSIAFYQDAFGFKELRRRDFPDHAFTIVYLGLeGDDYELELTYNYDHGPYVVGDGFAHIALSTPDLE 83
Cdd:COG0346     2 GLHHVTLRVSDLEASLAFYTDVLGLELVKRTDFGDGGFGHAFLRL-GDGTELELFEAPGAAPAPGGGGLHHLAFRVDDLD 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1534627144  84 ALHQEHSAKGYEVTEPNGLPGTAPNYYFVKDPDGYKVEVI 123
Cdd:COG0346    81 AAYARLRAAGVEIEGEPRDRAYGYRSAYFRDPDGNLIELV 120
GlxI_Ni cd16358
Glyoxalase I that uses Ni(++) as cofactor; This family includes Escherichia coil and other ...
 5-123 5.87e-36

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: 119.42  E-value: 5.87e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1534627144   5 MLHTCLRVENLEKSIAFYQDAFGFKELRRRDFPDHAFTIVYLGL--EGDDYELELTYNYDHGPYVVGDGFAHIALSTPDL 82
Cdd:cd16358     1 MLHTMLRVGDLDRSIKFYTEVLGMKLLRKRDYPEGKYTLAFVGYgdEDENTVLELTYNWGVDKYDLGTAYGHIAIGVEDV 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1534627144  83 EALHQEHSAKGYEVT-EPNGLPGTAPNYYFVKDPDGYKVEVI 123
Cdd:cd16358    81 YETCERIRKKGGKVTrEPGPMKGGTTVIAFVEDPDGYKIELI 122
glyox_I TIGR00068
lactoylglutathione lyase; Lactoylglutathione lyase is also known as aldoketomutase and ...
 5-126 2.69e-35

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: 118.76  E-value: 2.69e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1534627144   5 MLHTCLRVENLEKSIAFYQDAFGFKELRRRDFPDHAFTIVYLGL--EGDDYELELTYNYDHGPYVVGDGFAHIALSTPDL 82
Cdd:TIGR00068  18 LLHTMLRVGDLDKSLDFYTEVLGMKLLRKRDFPEMKFSLAFLGYgdETSAAVIELTHNWGTEKYDLGNGFGHIAIGVDDV 97

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1534627144  83 EALHQEHSAKGYEVT-EPNGLPGTAPNYYFVKDPDGYKVEVIREK 126
Cdd:TIGR00068  98 YKACERVRALGGNVVrEPGPVKGGTTVIAFVEDPDGYKIELIQRK 142
PLN02300 PLN02300
lactoylglutathione lyase
 4-126 3.11e-29

lactoylglutathione lyase


Pssm-ID: 215169 [Multi-domain]  Cd Length: 286  Bit Score: 106.79  E-value: 3.11e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1534627144   4 KMLHTCLRVENLEKSIAFYQDAFGFKELRRRDFPDHAFTIVYLGL--EGDDYELELTYNYDHGPYVVGDGFAHIALSTPD 81
Cdd:PLN02300   24 RMLHVVYRVGDLDRTIKFYTECLGMKLLRKRDIPEEKYTNAFLGYgpEDSNFVVELTYNYGVDKYDIGTGFGHFGIAVED 103

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1534627144  82 LEALHQEHSAKGYEVT-EPNGLPGTAPNYYFVKDPDGYKVEVIREK 126
Cdd:PLN02300  104 VAKTVELVKAKGGKVTrEPGPVKGGKSVIAFVKDPDGYKFELIQRG 149
GlxI_Zn cd07233
Glyoxalase I that uses Zn(++) as cofactor; This family includes eukaryotic glyoxalase I that ...
 5-123 3.56e-28

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: 100.09  E-value: 3.56e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1534627144   5 MLHTCLRVENLEKSIAFYQDAFGFKELRRRDFPDHAFTIVYLGLEGDDYE---------------LELTYNY----DHGP 65
Cdd:cd07233     1 FNHTMLRVKDPKKSLKFYTEVLGMKLLRKKDFPEMKFSLYFLGYEDPKDIpkdprtawvfsregtLELTHNWgtenDEDP 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1534627144  66 -YVVGD----GFAHIALSTPDLEALHQEHSAKGYE-VTEPNGlpGTAPNYYFVKDPDGYKVEVI 123
Cdd:cd07233    81 vYHNGNsdprGFGHIGIAVDDVYAACERFEELGVKfKKKPDD--GKMKGIAFIKDPDGYWIEIL 142
PLN02300 PLN02300
lactoylglutathione lyase
 10-119 5.34e-24

lactoylglutathione lyase


Pssm-ID: 215169 [Multi-domain]  Cd Length: 286  Bit Score: 92.92  E-value: 5.34e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1534627144  10 LRVENLEKSIAFYQDAFGFKELRRRDFPDHAFTIVYLGLeGDDYE---LELTYNYDHGPYVVGDGFAHIALSTPDL---- 82
Cdd:PLN02300  160 LRVGDLDRSIKFYEKAFGMKLLRKRDNPEYKYTIAMMGY-GPEDKttvLELTYNYGVTEYTKGNAYAQIAIGTDDVykta 238

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1534627144  83 EALHQEHsakGYEVTEPNGLPGTAPNYYFVKDPDGYK 119
Cdd:PLN02300  239 EAIKLVG---GKITREPGPLPGINTKITACLDPDGWK 272
Glyoxalase pfam00903
Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;
4-122 4.91e-23

Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;


Pssm-ID: 395724 [Multi-domain]  Cd Length: 121  Bit Score: 86.73  E-value: 4.91e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1534627144   4 KMLHTCLRVENLEKSIAFYQDAFGFKELRRRDFPDHAfTIVYLGLEGDDYELELTYNY---DHGPYVVGDGFAHIALSTP 80
Cdd:pfam00903   1 RIDHVALRVGDLEKSLDFYTDVLGFKLVEETDAGEEG-GLRSAFFLAGGRVLELLLNEtppPAAAGFGGHHIAFIAFSVD 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1534627144  81 DLEALHQEHSAKGYEVTEPNGLPGTAPNYYFVKDPDGYKVEV 122
Cdd:pfam00903  80 DVDAAYDRLKAAGVEIVREPGRHGWGGRYSYFRDPDGNLIEL 121
VOC cd06587
vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate (VOC) superfamily is composed ...
 7-122 1.22e-20

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: 80.26  E-value: 1.22e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1534627144   7 HTCLRVENLEKSIAFYQDAFGFKELRRRDFPDHAFtivyLGLeGDDYELELTYNYDHgPYVVGDGFAHIALSTPDLEALH 86
Cdd:cd06587     1 HVALRVPDLDASVAFYEEVLGFEVVSRNEGGGFAF----LRL-GPGLRLALLEGPEP-ERPGGGGLFHLAFEVDDVDEVD 74

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1534627144  87 QEHSAKGYEVTEPNGLPGTAPNYY--FVKDPDGYKVEV 122
Cdd:cd06587    75 ERLREAGAEGELVAPPVDDPWGGRsfYFRDPDGNLIEF 112
CatE COG2514
Catechol-2,3-dioxygenase [Secondary metabolites biosynthesis, transport and catabolism];
4-126 9.85e-20

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


Pssm-ID: 442004 [Multi-domain]  Cd Length: 141  Bit Score: 78.46  E-value: 9.85e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1534627144   4 KMLHTCLRVENLEKSIAFYQDAFGFKELRRRDfpdhafTIVYLGLEGDDYELELTYNYDHGPYVVGDGFAHIALSTP--- 80
Cdd:COG2514     3 RLGHVTLRVRDLERSAAFYTDVLGLEVVEREG------GRVYLRADGGEHLLVLEEAPGAPPRPGAAGLDHVAFRVPsra 76

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1534627144  81 DLEALHQEHSAKGYEVTEPnGLPGTAPNYYFvKDPDGYKVEVIREK 126
Cdd:COG2514    77 DLDAALARLAAAGVPVEGA-VDHGVGESLYF-RDPDGNLIELYTDR 120
PRK10291 PRK10291
glyoxalase I; Provisional
 10-126 1.87e-18

glyoxalase I; Provisional


Pssm-ID: 182358  Cd Length: 129  Bit Score: 75.06  E-value: 1.87e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1534627144  10 LRVENLEKSIAFYQDAFGFKELRRRDFPDHAFTIVYLGL--EGDDYELELTYNYDHGPYVVGDGFAHIALSTPDLEALHQ 87
Cdd:PRK10291    2 LRVGDLQRSIDFYTNVLGMKLLRTSENPEYKYSLAFVGYgpETEEAVIELTYNWGVDKYELGTAYGHIALSVDNAAEACE 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1534627144  88 EHSAKGYEVTEPNG-LPGTAPNYYFVKDPDGYKVEVIREK 126
Cdd:PRK10291   82 KIRQNGGNVTREAGpVKGGTTVIAFVEDPDGYKIELIEEK 121
PhnB COG2764
Zn-dependent glyoxalase, PhnB family [Energy production and conversion];
6-122 1.81e-17

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


Pssm-ID: 442048 [Multi-domain]  Cd Length: 118  Bit Score: 72.20  E-value: 1.81e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1534627144   6 LHTCLRVENLEKSIAFYQDAFGFKELRRRDFPDHAftIVYLGLEGDDYELELTYNYDHGPYVVGDGFaHIALSTPDLEAL 85
Cdd:COG2764     2 VTPYLVVDDAEEALEFYEDVFGFEVVFRMTDPDGK--IMHAELRIGGSVLMLSDAPPDSPAAEGNGV-SLSLYVDDVDAL 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1534627144  86 HQEHSAKGYEVTEPnglPGTAP---NYYFVKDPDGYKVEV 122
Cdd:COG2764    79 FARLVAAGATVVMP---LQDTFwgdRFGMVRDPFGVLWMI 115
PLN03042 PLN03042
Lactoylglutathione lyase; Provisional
 5-123 3.88e-14

Lactoylglutathione lyase; Provisional


Pssm-ID: 215548  Cd Length: 185  Bit Score: 65.23  E-value: 3.88e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1534627144   5 MLHTCLRVENLEKSIAFYQDAFGFKELRRRDFPDHAFTIVYLGLE------GDDYE-----------LELTYNY------ 61
Cdd:PLN03042   28 MQQTMFRIKDPKASLDFYSRVLGMSLLKRLDFPEMKFSLYFLGYEdsetapTDPPErtvwtfgrkatIELTHNWgtesdp 107

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1534627144  62 DHGPYVVGD----GFAHIALSTPDLEALHQEHSAKGYE-VTEPN--GLPGTApnyyFVKDPDGYKVEVI 123
Cdd:PLN03042  108 EFKGYHNGNsdprGFGHIGITVDDVYKACERFEKLGVEfVKKPDdgKMKGLA----FIKDPDGYWIEIF 172
VOC COG3324
Lactoylglutathione lyase-related enzyme, vicinal oxygen chelate (VOC) family [General function ...
 1-126 6.00e-13

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


Pssm-ID: 442553 [Multi-domain]  Cd Length: 119  Bit Score: 60.42  E-value: 6.00e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1534627144   1 MASKMLHTCLRVENLEKSIAFYQDAFGFkELRRRDFPDHAFTIVYLGlEGDDYELEltynydHGPYVVGDGFAHIALSTP 80
Cdd:COG3324     1 MPGTIVWVELPVDDLERAKAFYEEVFGW-TFEDDAGPGGDYAEFDTD-GGQVGGLM------PGAEEPGGPGWLLYFAVD 72

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1534627144  81 DLEALHQEHSAKGYEVTEPnglPGTAPNY---YFVKDPDGYKVEVIREK 126
Cdd:COG3324    73 DLDAAVARVEAAGGTVLRP---PTDIPPWgrfAVFRDPEGNRFGLWQPA 118
PLN02367 PLN02367
lactoylglutathione lyase
 5-122 7.26e-13

lactoylglutathione lyase


Pssm-ID: 177995  Cd Length: 233  Bit Score: 62.71  E-value: 7.26e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1534627144   5 MLHTCLRVENLEKSIAFYQDAFGFKELRRRDFPDHAFTIVYLGLE-----------------GDDYELELTYNY------ 61
Cdd:PLN02367   76 MQQTMYRIKDPKASLDFYSRVLGMSLLKRLDFPEMKFSLYFMGYEdtasaptdptertvwtfGQKATIELTHNWgtesdp 155

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1534627144  62 DHGPYVVGD----GFAHIALSTPDLEALHQEHSAKGYE-VTEPNGlpGTAPNYYFVKDPDGYKVEV 122
Cdd:PLN02367  156 DFKGYHNGNseprGFGHIGITVDDVYKACERFEELGVEfVKKPND--GKMKGIAFIKDPDGYWIEI 219
VOC_like cd07245
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 7-122 1.09e-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: 319909 [Multi-domain]  Cd Length: 117  Bit Score: 60.02  E-value: 1.09e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1534627144   7 HTCLRVENLEKSIAFYQDAFGFKELRRRDFPDhaFTIVYLGLeGDDYELELTY--NYDHGPYVVGDGF-AHIALSTPDLE 83
Cdd:cd07245     3 HVALACPDLERARRFYTDVLGLEEVPRPPFLK--FGGAWLYL-GGGQQIHLVVeqNPSELPRPEHPGRdRHPSFSVPDLD 79

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1534627144  84 ALHQEHSAKGYEVTEpNGLPGTAPNYYFVKDPDGYKVEV 122
Cdd:cd07245    80 ALKQRLKEAGIPYTE-STSPGGGVTQLFFRDPDGNRLEF 117
VOC_like cd07262
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 7-123 1.22e-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: 319923 [Multi-domain]  Cd Length: 121  Bit Score: 57.24  E-value: 1.22e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1534627144   7 HTCLRVENLEKSIAFYQDAFGFKELRRRDFPDHAftiVYLGLEGDDyELELTYNYDHGPYVVGDGfAHIALSTPDLEALH 86
Cdd:cd07262     3 HVTIGVNDLERSRAFYDAALAPLGYKRGFEDGGR---VGYGLEGGP-DFWVTEPFDGEPATAGNG-THVAFAAPSRAAVD 77

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1534627144  87 QEHSAK----GYEVTEPNGLPGTAPNYY--FVKDPDGYKVEVI 123
Cdd:cd07262    78 AFHAAAlaagGTDNGAPGLRPHYHPGYYaaYVRDPDGNKIEAV 120
BLMA_like cd08349
Bleomycin binding protein (BLMA) and similar proteins; BLMA also called Bleomycin resistance ...
 10-120 1.23e-11

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: 56.85  E-value: 1.23e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1534627144  10 LRVENLEKSIAFYQDAFGFKELRRRDFPDhaftivYLGLEGDDYELELTYNYDHGPYvvGDGFAhIALSTPDLEALHQEH 89
Cdd:cd08349     4 LPVRDIDKTLAFYVDVLGFEVDYERPPPG------YAILSRGGVELHLFEHPGLDPA--GSGVA-AYIRVEDIDALHAEL 74

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1534627144  90 SAKGY--EVTEPNGLPGTAPnYYF----VKDPDGYKV 120
Cdd:cd08349    75 KAAGLplFGIPRITPIEDKP-WGMrefaVVDPDGNLL 110
Glyoxalase_4 pfam13669
Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;
7-97 6.99e-11

Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;


Pssm-ID: 463951 [Multi-domain]  Cd Length: 109  Bit Score: 54.98  E-value: 6.99e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1534627144   7 HTCLRVENLEKSIAFYQDAFGFKELRRRDFPDHAFTIVYLGLEGDDYELEL-------TYNYDHGPyvvgdGFAHIALST 79
Cdd:pfam13669   2 HVGIAVPDLDRALALWGALLGLGPEGDYRSEPQNVDLAFALLGDGPVEVELiqpldgdSPLARHGP-----GLHHLAYWV 76

                          90
                  ....*....|....*...
gi 1534627144  80 PDLEALHQEHSAKGYEVT 97
Cdd:pfam13669  77 DDLDAAVARLLDQGYRVA 94
VOC_like cd07254
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 4-122 1.45e-09

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: 51.69  E-value: 1.45e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1534627144   4 KMLHTCLRVENLEKSIAFYQDAFGFKELRRRdfPDHAFTIVylglegDDYELELTYNYDHGPyvVGDGFAHIALSTPDLE 83
Cdd:cd07254     1 KRFHLSLNVTDLERSIRFYSDLFGAEPAKRK--ADYAKFML------EDPPLNLALLVNDRK--EPYGLNHLGIQVDSKE 70

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1534627144  84 ALHQEHS---AKGYEVTEPNGLP--GTAPNYYFVKDPDGYKVEV 122
Cdd:cd07254    71 EVAALKAraeAAGLPVRKEPRTTccYAVQDKFWLTDPDGNAWEF 114
GLOD4_N cd08358
N-terminal domain of human glyoxalase domain-containing protein 4 and similar proteins; ...
 6-125 1.55e-09

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: 51.98  E-value: 1.55e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1534627144   6 LHTCLRVENLEKSIAFYQDAFGFKELRRRDFPDH-------------AFTIVYLGLEGDDYELELTYNYDHGPYVVGDGF 72
Cdd:cd08358     4 LHFVFKVGDRNKTIKFYREILGMKVLRHEEFEEGckaacngpydgkwSKTMVGYGPEDDHFVVELTYNYGIGDYELGNDF 83

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1534627144  73 AHIALSTPDLEALHQEHSakgYEVTEpnglpgTAPNYYFVKDPDGYKVEVIRE 125
Cdd:cd08358    84 LGITIHSKQAVSRAKKHN---WPVTQ------VGDGVYEVKAPGGYKFYLIDK 127
VOC_Bs_YwkD_like cd08352
vicinal oxygen chelate (VOC) family protein Bacillus subtilis YwkD and similar proteins; ...
 7-122 2.70e-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: 48.69  E-value: 2.70e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1534627144   7 HTCLRVENLEKSIAFYQDAFGFKELRRRDFPDHAFTIvyLGLEGDDYELELTYNYD---HGPYVVGDGFAHIALSTPDLE 83
Cdd:cd08352     5 HIAIICSDYEKSKDFYVDKLGFEIIREHYRPERNDIK--LDLALGGYQLELFIKPDapaRPSYPEALGLRHLAFKVEDVE 82

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1534627144  84 ALHQEHSAKGYEVTEPNGLPGTAPNYYFVKDPDGYKVEV 122
Cdd:cd08352    83 ATVAELKSLGIETEPIRVDDFTGKKFTFFFDPDGLPLEL 121
metmalonyl_epim TIGR03081
methylmalonyl-CoA epimerase; Members of this protein family are the enzyme methylmalonyl-CoA ...
 7-95 8.37e-08

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: 47.32  E-value: 8.37e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1534627144   7 HTCLRVENLEKSIAFYQDAFGFKELRRRDFPDHAFTIVYLGLEGDDYELeLTYNYDHGPYVV-----GDGFAHIALSTPD 81
Cdd:TIGR03081   4 HVGIAVPDLEEAAKFYEDVLGAQVSEIEELPEQGVKVVFIALGNTKVEL-LEPLGEDSPIAKfleknGGGIHHIAIEVDD 82

                          90
                  ....*....|....
gi 1534627144  82 LEALHQEHSAKGYE 95
Cdd:TIGR03081  83 IEAALETLKEKGVR 96
MMCE cd07249
Methylmalonyl-CoA epimerase (MMCE); MMCE, also called methylmalonyl-CoA racemase (EC 5.1.99.1) ...
 7-105 8.47e-08

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


Pssm-ID: 319912 [Multi-domain]  Cd Length: 127  Bit Score: 47.19  E-value: 8.47e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1534627144   7 HTCLRVENLEKSIAFYQDAFGFKELRRRDFPDHAFTIVYLGLegDDYELELTYNYDHGPYVV------GDGFAHIALSTP 80
Cdd:cd07249     3 HIGIAVPDLDEALKFYEDVLGVKVSEPEELEEQGVRVAFLEL--GNTQIELLEPLGEDSPIAkfldkkGGGLHHIAFEVD 80

                          90       100
                  ....*....|....*....|....*
gi 1534627144  81 DLEALHQEHSAKGYEVTEPNGLPGT 105
Cdd:cd07249    81 DIDAAVEELKAQGVRLLSEGPRIGA 105
VOC_like cd07263
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 7-117 1.48e-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: 319924 [Multi-domain]  Cd Length: 120  Bit Score: 46.52  E-value: 1.48e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1534627144   7 HTCLRVENLEKSIAFYQDAFGFKELRRRDFPDHAF-TIVYLGLEGDDYELELTYNYDHGPY--VVGDGFAHIALSTPDLE 83
Cdd:cd07263     1 QVMLYVDDQDKALDFYVEKLGFEVVEDVPMGGMRWvTVAPPGSPGTSLLLEPKAHPAQMPQspEAAGGTPGILLATDDID 80

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1534627144  84 ALHQEHSAKGYEVTEPNGLPGTAPNYYFvKDPDG 117
Cdd:cd07263    81 ATYERLTAAGVTFVQEPTQMGGGRVANF-RDPDG 113
VOC_like cd07264
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 5-122 5.07e-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: 319925 [Multi-domain]  Cd Length: 118  Bit Score: 45.02  E-value: 5.07e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1534627144   5 MLHTCLRVENLEKSIAFYQDAFGFKelRRRDFPDHaftiVYLGLEGDDYELELTYNYDHGPYVVGDGFAH---IALSTPD 81
Cdd:cd07264     1 IAYIVLYVDDFAASLRFYRDVLGLP--PRFLHEEG----EYAEFDTGETKLALFSRKEMARSGGPDRRGSafeLGFEVDD 74

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1534627144  82 LEALHQEHSAKGYEVTEPnglPGTAP---NYYFVKDPDGYKVEV 122
Cdd:cd07264    75 VEATVEELVERGAEFVRE---PANKPwgqTVAYVRDPDGNLIEI 115
FosA cd07244
fosfomycin resistant protein subfamily FosA; This subfamily family contains FosA, a fosfomycin ...
 7-122 7.34e-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: 44.58  E-value: 7.34e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1534627144   7 HTCLRVENLEKSIAFYQDAFGFKELRRRDfpdhafTIVYLgLEGDDYeleLTYNYDHGPYVVGDgFAHIALS--TPDLEA 84
Cdd:cd07244     4 HITLAVSDLERSLAFYVDLLGFKPHVRWD------KGAYL-TAGDLW---LCLSLDPAAEPSPD-YTHIAFTvsEEDFEE 72

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1534627144  85 LHQEHSAKGYEVTEPNGLPGtaPNYYFVkDPDGYKVEV 122
Cdd:cd07244    73 LSERLRAAGVKIWQENSSEG--DSLYFL-DPDGHKLEL 107
VOC_like cd16355
uncharacterized subfamily of vicinal oxygen chelate (VOC) superfamily; The vicinal oxygen ...
 10-122 1.44e-06

uncharacterized subfamily of vicinal oxygen chelate (VOC) superfamily; 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: 319962  Cd Length: 121  Bit Score: 44.02  E-value: 1.44e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1534627144  10 LRVENLEKSIAFYQDAFGFKELRRRDFPDHAFTI------VYLGLEGDDYELELtynyDHGPYVVGDGFAHIALSTPDLE 83
Cdd:cd16355     5 LNVSDIPASFAWFEKVLGFQKDWDWGDPPTFGSVgsgeceIFLCQGGQGGSLRL----GPCGDALPSYGAWMSVWVDDVD 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1534627144  84 ALHQEHSAKGYEVTEPnglPGTAP---NYYFVKDPDGYKVEV 122
Cdd:cd16355    81 ALHRECRARGADIRQP---PTDMPwgmREMHVRHPDGHRFRV 119
COG3607 COG3607
Lactoylglutathione lyase-related enzyme, vicinal oxygen chelate (VOC) family [General function ...
 10-122 3.72e-06

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


Pssm-ID: 442825  Cd Length: 126  Bit Score: 42.89  E-value: 3.72e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1534627144  10 LRVENLEKSIAFYQdAFGFKELRRRDFPDHAFTIV----YLGLEGDDYELELTynydHGPYVVGDGF--AHIALSTP--- 80
Cdd:COG3607     9 LPVADLERSRAFYE-ALGFTFNPQFSDEGAACFVLgegiVLMLLPREKFATFT----GKPIADATGFteVLLALNVEsre 83

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1534627144  81 DLEALHQEHSAKGYEVTEPnglPGTAPNYY--FVKDPDGYKVEV 122
Cdd:COG3607    84 EVDALVAKALAAGGTVLKP---PQDVGGMYsgYFADPDGHLWEV 124
BphC-JF8_N_like cd09013
N-terminal, non-catalytic, domain of BphC_JF8, (2,3-dihydroxybiphenyl 1,2-dioxygenase) from ...
 3-125 4.69e-06

N-terminal, non-catalytic, domain of BphC_JF8, (2,3-dihydroxybiphenyl 1,2-dioxygenase) from Bacillus sp. JF8, and similar proteins; 2,3-dihydroxybiphenyl 1,2-dioxygenase (BphC) catalyzes the extradiol ring cleavage reaction of 2,3-dihydroxybiphenyl, a key step in the polychlorinated biphenyls (PCBs) degradation pathway (bph pathway). BphC belongs to the type I extradiol dioxygenase family, which requires a metal ion in the active site in its catalytic mechanism. Polychlorinated biphenyl degrading bacteria demonstrate a multiplicity of BphCs. This subfamily of BphC is represented by the enzyme purified from the thermophilic biphenyl and naphthalene degrader, Bacillus sp. JF8. The members in this family of BphC enzymes may use either Mn(II) or Fe(II) as cofactors. The enzyme purified from Bacillus sp. JF8 is Mn(II)-dependent, however, the enzyme from Rhodococcus jostii RHAI has Fe(II) bound to it. BphC_JF8 is thermostable and its optimum activity is at 85 degrees C. The enzymes in this family have an internal duplication. This family represents the N-terminal repeat.


Pssm-ID: 319955  Cd Length: 121  Bit Score: 42.72  E-value: 4.69e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1534627144   3 SKMLHTCLRVENLEKSIAFYQDAFGFKELRRRDfpdhafTIVYLGLEGD--DYELELTYnydhGPYVvgdGFAHIAL--- 77
Cdd:cd09013     5 AQLAHVELLTPKPEESLWFFTDVLGLEETHREG------QSVYLRAWGDweHHTLKLTE----SPEA---GLGHIAWras 71

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1534627144  78 STPDLEALHQEHSAKGYEVTEPNGLPGTAPNYYFvKDPDGYKVEVIRE 125
Cdd:cd09013    72 SPEALERRVAALEASGVGIGWIDGDLGQGPAYRF-QSPDGHPMEIYWE 118
Fosfomycin_RP cd08345
Fosfomycin resistant protein; This family contains three types of fosfomycin resistant protein. ...
 7-121 5.17e-06

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: 42.55  E-value: 5.17e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1534627144   7 HTCLRVENLEKSIAFYQDAFGFKELRRRDfpDHAFTI----------VYLGL-EGDDYElELTYNydhgpyvvgdgfaHI 75
Cdd:cd08345     1 HITLIVRDLEKSTAFLQDIFGAREVYSSG--DKTFSLskekffllggLWIALmEGESLQ-ERSYT-------------HI 64

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1534627144  76 A--LSTPDLEALHQEHSAKGYEVTEPN-GLPGTAPNYYFVkDPDGYKVE 121
Cdd:cd08345    65 AfqIQSEDFDRYAERLGALGVEMRPPRpRVEGEGRSIYFY-DPDNHLFE 112
GLOD5 cd07253
Human glyoxalase domain-containing protein 5 and similar proteins; Uncharacterized subfamily ...
 3-122 1.01e-05

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: 41.83  E-value: 1.01e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1534627144   3 SKMLHTCLRVENLEKSIAFYQDAFGFKELR-RRDFPDHAFTIVYLGLegddyeleLTYNYDHGPYVV--GDGFAHIALST 79
Cdd:cd07253     2 KRLDHLVLTVKDIERTIDFYTKVLGMTVVTfKEGRKALRFGNQKINL--------HQKGKEFEPKASapTPGSADLCFIT 73

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1534627144  80 -PDLEALHQEHSAKGYEVTEP----NGLPGTAPNYYFvKDPDGYKVEV 122
Cdd:cd07253    74 eTPIDEVLEHLEACGVTIEEGpvkrTGALGPILSIYF-RDPDGNLIEL 120
VOC_like cd08354
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 5-122 1.43e-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: 319942  Cd Length: 122  Bit Score: 41.20  E-value: 1.43e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1534627144   5 MLHTCLRVENLEKSIAFYQDAFGFKELRRRdfPDHAF--------TIVYLGLEGDDYELeltynyDHGPYVVGDGFAHIA 76
Cdd:cd08354     1 ILETCLYADDLDAAEAFYEDVLGLKPMLRS--GRHAFfrlgpqvlLVFDPGATSKDVRT------GEVPGHGASGHGHFA 72

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1534627144  77 LSTPD--LEALHQEHSAKGYEVTEPNGLPGTAPNYYFvKDPDGYKVEV 122
Cdd:cd08354    73 FAVPTeeLAAWEARLEAKGVPIESYTQWPEGGKSLYF-RDPAGNLVEL 119
BphC2-C3-RGP6_C_like cd08348
The single-domain 2,3-dihydroxybiphenyl 1,2-dioxygenases; This subfamily contains Rhodococcus ...
 4-122 3.25e-05

The single-domain 2,3-dihydroxybiphenyl 1,2-dioxygenases; This subfamily contains Rhodococcus globerulus P6 BphC2-RGP6 and BphC3-RGP6, and similar proteins. BphC catalyzes the extradiol ring cleavage reaction of 2,3-dihydroxybiphenyl, yielding 2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoic acid. This is 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. Most type I extradiol dioxygenases are activated by Fe(II). 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. BphC2-RGP6 and BphC3-RGP6 are one-domain dioxygenases, which form hexamers. BphC1-RGP6 has an internal duplication, it is a two-domain dioxygenase which forms octamers, its two domains do not belong to this subfamily.


Pssm-ID: 319936  Cd Length: 137  Bit Score: 40.58  E-value: 3.25e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1534627144   4 KMLHTCLRV--ENLEKSIAFYQDAFGFKELRRRDFpdhaftIVYLGLEGDDYELELTYNYDHGPYV----VGDGFAHIAL 77
Cdd:cd08348     1 KLAHFVLRTnpEKFEAMVQWYLDILGARIVARNAK------GCFLSFDEEHHRIAIFGAPGGAQPPdkrpTRVGLAHIAF 74

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1534627144  78 STPDLEALHQEH---SAKGYEVTEPNGLPGTAPNYYFvkDPDGYKVEV 122
Cdd:cd08348    75 TYASLDDLARNYaqlKERGIKPVWPVNHGVTTSIYYR--DPDGNMLEM 120
PRK04101 PRK04101
metallothiol transferase FosB;
7-122 4.30e-05

metallothiol transferase FosB;


Pssm-ID: 179740  Cd Length: 139  Bit Score: 40.31  E-value: 4.30e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1534627144   7 HTCLRVENLEKSIAFYQDAFGFKEL---RRRDFPDHAFTIVYLGLEGDDYELELTYNYdhgpyvvgdgfAHIALSTPDLE 83
Cdd:PRK04101    7 HICFSVSNLEKSIEFYEKVLGAKLLvkgRKTAYFDLNGLWIALNEEKDIPRNEIHQSY-----------THIAFSIEEED 75

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1534627144  84 ALHQEHSAKGYEVtepNGLPGTAPN------YYFVkDPDGYKVEV 122
Cdd:PRK04101   76 FDHWYQRLKENDV---NILPGRERDerdkksIYFT-DPDGHKFEF 116
VOC_like cd07246
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 10-118 5.19e-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: 319910 [Multi-domain]  Cd Length: 124  Bit Score: 39.97  E-value: 5.19e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1534627144  10 LRVENLEKSIAFYQDAFGFKELRRRDFPD----HA-FTI----VYLGLEGDDYELELTynYDHGPYVVgdgfaHIALSTP 80
Cdd:cd07246     7 LVVEDAAAAIAFYKKAFGAEELGRTTQEDgrvgHAeLRIggtvVMVADENPERGALSP--TKLGGTPV-----IFHLYVE 79

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1534627144  81 DLEALHQEHSAKGYEVTEPNGLPGTAPNYYFVKDPDGY 118
Cdd:cd07246    80 DVDATFARAVAAGAVVVEPVEDQFWGDRVGKVKDPFGH 117
FosB cd08363
fosfomycin resistant protein subfamily FosB; This subfamily family contains FosB, a fosfomycin ...
 7-122 6.11e-05

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: 39.64  E-value: 6.11e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1534627144   7 HTCLRVENLEKSIAFYQDAFGFKEL---RRRDFPDHAFTIVYLGLEGDDYELELTYNYdhgpyvvgdgfAHIALST--PD 81
Cdd:cd08363     3 HITFSVSNLNKSIAFYKDVLDAKLLvlgEKTAYFDLNGLWLALNVQEDIPRNEISHSY-----------THIAFSIdeED 71

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1534627144  82 LEALHQEHSAKGYEVTEpnGLP---GTAPNYYFvKDPDGYKVEV 122
Cdd:cd08363    72 LDAFKERLKDNGVNILE--GRKrdiLEGQSIYF-TDPDGHLFEL 112
VOC_BsCatE_like_N cd07255
N-terminal of Bacillus subtilis CatE like protein; Uncharacterized subfamily of VOC ...
 10-85 9.44e-05

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: 39.22  E-value: 9.44e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1534627144  10 LRVENLEKSIAFYQDAFGFKELRRRDfpdhafTIVYLGLEGDDYELELTYNYDHG-PYVVGDGFAHIALSTPDLEAL 85
Cdd:cd07255     8 LKVADLERQSAFYQNVIGLSVLKQNA------SRAYLGVDGKQVLLVLEAIPDAVlAPRSTTGLYHFAILLPDRKAL 78
VOC_BsYyaH cd07241
vicinal oxygen chelate (VOC) family protein similar to Bacillus subtilis YyaH; The vicinal ...
 4-122 1.64e-04

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


Pssm-ID: 319905  Cd Length: 125  Bit Score: 38.54  E-value: 1.64e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1534627144   4 KMLHTCLRVENLEKSIAFYQDAFGFK-----ELRRRDFPDHAFTIvylgleGDDYELEL---TYNYDHGPYVVGDGFAHI 75
Cdd:cd07241     1 KIEHVALWTNDLERMKDFYVKYFGAEsndiyHNKKKGFRSYFLTF------DSGARLELmsrPDVTDPDKEVERTGLAHI 74

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1534627144  76 ALSTPDLEA---LHQEHSAKGYEVTepnGLPGTAPNYYF---VKDPDGYKVEV 122
Cdd:cd07241    75 AFSVGSKEAvdeLTERLRADGYAVV---GGPRTTGDGYYesvILDPEGNRIEI 124
GLOD4_C cd16357
C-terminal domain of human glyoxalase domain-containing protein 4 and similar proteins; ...
 9-118 1.87e-04

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: 38.31  E-value: 1.87e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1534627144   9 CLRVENLEKSIAFYQDAFGFKELRRRDfpdhafTIVYLGLEGDDYELEL---TYNYDHgpyvvGDGFAHIALSTP--DLE 83
Cdd:cd16357     3 SLAVSDLEKSIDYWSDLLGMKVFEKSE------KSALLGYGEDQAKLELvdiPEPVDH-----GTAFGRIAFSCPadELP 71

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1534627144  84 ALHQEHSAKGYEV-TEPNGL--PGTAPnyyfVK-----DPDGY 118
Cdd:cd16357    72 PIEEKVKAAGQTIlTPLVSLdtPGKAT----VQvvilaDPDGH 110
BphC5-RrK37_N_like cd08362
N-terminal, non-catalytic, domain of BphC5 (2,3-dihydroxybiphenyl 1,2-dioxygenase) from ...
 7-125 2.98e-04

N-terminal, non-catalytic, domain of BphC5 (2,3-dihydroxybiphenyl 1,2-dioxygenase) from Rhodococcus rhodochrous K37, and similar proteins; 2,3-dihydroxybiphenyl 1,2-dioxygenase (BphC) catalyzes the extradiol ring cleavage reaction of 2,3-dihydroxybiphenyl, the third step in the polychlorinated biphenyls (PCBs) degradation pathway (bph pathway). The enzyme contains a N-terminal and a C-terminal domain of similar structure fold, resulting from an ancient gene duplication. BphC belongs to the type I extradiol dioxygenase family, which requires a metal in the active site for its catalytic activity. Polychlorinated biphenyl degrading bacteria demonstrate multiplicity of BphCs. Bacterium Rhodococcus rhodochrous K37 has eight genes encoding BphC enzymes. This family includes the N-terminal domain of BphC5-RrK37. The crystal structure of the protein from Novosphingobium aromaticivorans has a Mn(II)in the active site, although most proteins of type I extradiol dioxygenases are activated by Fe(II).


Pssm-ID: 319950 [Multi-domain]  Cd Length: 120  Bit Score: 37.61  E-value: 2.98e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1534627144   7 HTCLRVENLEKSIAFYQDAFGFKELRRRDfpdhafTIVYLGLEGDD-YELELTYNYDHGPYVVgdGFAhiALSTPDLEAL 85
Cdd:cd08362     6 YVALGVPDLAAEREFYTEVWGLEEVAEDD------DVVYLRAEGSEhHVLRLRQSDENRLDLI--AFA--AATRADVDAL 75

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1534627144  86 HQEHSAKGYE-VTEPNGLPGTAPNYYF-VKDPDGYKVEVIRE 125
Cdd:cd08362    76 AARLAAAGVRiLSEPGPLDDPGGGYGFrFFDPDGRTIEVSAD 117
VOC_ShValD_like cd16361
vicinal oxygen chelate (VOC) family protein similar to Streptomyces hygroscopicus ValD protein; ...
 4-124 1.10e-03

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: 36.54  E-value: 1.10e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1534627144   4 KMLHTCLRVENLEKSIAFYQDAFGFK---------------ELRRRDFPDHAFT---IVYLGLeGDDYELEL-TY-NYDH 63
Cdd:cd16361     1 GVNHVGITVPDLDAAVEFYTDVLGAEvvyrstplaegdrggGEMRAAGFVPGFArarIAMLRL-GPGPGIELfEYkGPEQ 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1534627144  64 GPYVVGD---GFAHIALSTPDLEALHQEHSAKGYEV-TEPNGLPGTAPN----YYFVKDPDGYKVEVIR 124
Cdd:cd16361    80 RAPVPRNsdvGIFHFALQVDDVEAAAERLAAAGGKVlMGPREIPDGGPGkgnrMVYLRDPWGTLIELVS 148
VOC_BsYqjT cd07242
vicinal oxygen chelate (VOC) family protein similar to Bacillus subtilis YqjT; The vicinal ...
 7-123 1.46e-03

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: 35.93  E-value: 1.46e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1534627144   7 HTCLRVENLEKSIAFYQD--AFGFKELRRRDFpDHAFTI---VYLGLEGDDyelELTYNYDHGPYVvgdGFAHIALSTPD 81
Cdd:cd07242     4 HVELAVSDLHRSFKWFEWilGLGWKEYDTWSF-GPSWKLsggSLLVVQQTD---EFATPEFDRARV---GLNHLAFHAES 76

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1534627144  82 LEAL---HQEHSAKGYEVTEPNGLPGTA-PNYY--FVKDPDGYKVEVI 123
Cdd:cd07242    77 REAVdelTEKLAKIGGVRTYGDRHPFAGgPPHYaaFCEDPDGIKLELV 124
Glyoxalase_3 pfam13468
Glyoxalase-like domain; This domain is related to the Glyoxalase domain pfam00903.
 7-105 1.91e-03

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


Pssm-ID: 433233  Cd Length: 175  Bit Score: 36.16  E-value: 1.91e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1534627144   7 HTCLRVENLEKSIAFYQDAFGFK------------ELRRRDFPDHaftivYLGLEGDDYELELTynydHGPYVV------ 68
Cdd:pfam13468   3 HVVLAVPDLDEAAARFARALGFTvtpggrhpgmgtANALIMFGDG-----YLELLAVDPEAPAP----PRGRWFgldrla 73

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1534627144  69 -GDGFAHIALSTPDLEALHQEHSAKGYEVTEPNGLPGT 105
Cdd:pfam13468  74 dGEGLLGWALRTDDIDAVAARLRAAGVEPGRRVRPDGG 111
HppD COG3185
4-hydroxyphenylpyruvate dioxygenase and related hemolysins [Amino acid transport and ...
 9-126 2.13e-03

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: 36.41  E-value: 2.13e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1534627144   9 CLRVENLEKSIAFYQDAFGFKELRRRDFPDHA----------------FTIvylgLEGDDyeleltynyDHGP---YV-- 67
Cdd:COG3185   153 AVPRGDLDEWVLFYEDVLGFEEIREEDIEDPYqgvrsavlqspdgkvrIPL----NEPTS---------PDSQiaeFLek 219

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1534627144  68 -VGDGFAHIALSTPDLEALHQEHSAKGYEVtepngLPgTAPNYYFVKDP----DGYKVEVIREK 126
Cdd:COG3185   220 yRGEGIQHIAFATDDIEATVAALRARGVRF-----LD-IPDNYYDDLEPrvgaHGEDVAFLHPK 277
TioX_like cd08355
Micromonospora sp. TioX and similar proteins; Micromonospora sp. TioX is encoded by a gene of ...
 6-118 6.62e-03

Micromonospora sp. TioX and similar proteins; Micromonospora sp. TioX is encoded by a gene of the thiocoraline biosynthetic gene cluster. Thiocoraline is a thiodepsipeptide with potent antitumor activity. TioX may be involved in thiocoraline resistance or secretion. TioX belongs to vicinal oxygen chelate (VOC) superfamily that 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: 319943  Cd Length: 123  Bit Score: 34.32  E-value: 6.62e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1534627144   6 LHTCLRVENLEKSIAFYQDAFGFKELRRRDFPD----HA-----FTIVYLGLEGDDYELEltYNYDHGPyVVGDGfAHIA 76
Cdd:cd08355     1 VVPTLRYRDAVAAIDWLVEAFGFEERMVVPGDEgtihHAeltfgGGGVMVGSVRDEARPD--RPADAGG-HGTQS-VYVA 76

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1534627144  77 LSTPDleALHQEHSAKGYEVTEPnglPGTAP--NY-YFVKDPDGY 118
Cdd:cd08355    77 VADPD--AHYERARAAGAEIVME---PTDTDygSRdYSARDPEGH 116
VOC_like cd07251
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 9-122 9.34e-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: 319914 [Multi-domain]  Cd Length: 120  Bit Score: 33.81  E-value: 9.34e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1534627144   9 CLRVENLEKSIAFYQdAFGFKELRRRDFPDHAFTI--VYLGLegddYELELtYNYDHGPYVVGDGF-----AHIALSTPD 81
Cdd:cd07251     3 TLGVRDLERSARFYE-ALGWKPNLDPNDGVVFFQLggTVLAL----YPRDA-LAEDAGVSVTGAGFsgvtlAHNVRSREE 76

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1534627144  82 LEALHQEHSAKGYEVT-EPNGLPGTAPNYYFvKDPDGYKVEV 122
Cdd:cd07251    77 VDQLLAKAVAAGGKILkPPQEVFWGGYSGYF-ADPDGHIWEV 117
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH