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Conserved domains on  [gi|30682443|ref|NP_849643|]
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glyoxalase/bleomycin resistance protein/dioxygenase superfamily protein [Arabidopsis thaliana]

Protein Classification

lactoylglutathione lyase( domain architecture ID 11476608)

lactoylglutathione lyase, a critical enzyme in methylglyoxal detoxification, catalyzes the conversion of of hemimercaptal, formed from methylglyoxal and glutathione, to S-lactoylglutathione

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PLN02300 PLN02300
lactoylglutathione lyase
 1-283 0e+00

lactoylglutathione lyase


:

Pssm-ID: 215169 [Multi-domain]  Cd Length: 286  Bit Score: 557.86  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682443    1 MAEASDLLEWPKKDNRRFLHVVYRVGDLDRTIEFYTEVFGMKLLRKRDIPEEKYSNAFLGFGPETSNFVVELTYNYGVSS 80
Cdd:PLN02300   8 AAEAEDLLEWPKKDKRRMLHVVYRVGDLDRTIKFYTECLGMKLLRKRDIPEEKYTNAFLGYGPEDSNFVVELTYNYGVDK 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682443   81 YDIGTGFGHFAISTQDVSKLVENVRAKGGNVTREPGPVKGGGSVIAFVKDPDGYTFELIQRGPTPEPFCQVMLRVGDLDR 160
Cdd:PLN02300  88 YDIGTGFGHFGIAVEDVAKTVELVKAKGGKVTREPGPVKGGKSVIAFVKDPDGYKFELIQRGPTPEPLCQVMLRVGDLDR 167

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682443  161 AIKFYEKALGMRLLRKIERPEYKYTIGMMGYAEEYESIVLELTYNYDVTEYTKGNAYAQIAIGTDDVYKSGEVIKIVnqe 240
Cdd:PLN02300 168 SIKFYEKAFGMKLLRKRDNPEYKYTIAMMGYGPEDKTTVLELTYNYGVTEYTKGNAYAQIAIGTDDVYKTAEAIKLV--- 244

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 30682443  241 lGGKITREAGPLPGLGTKIVSFLDPDGWKTVLVDNKDFLKELE 283
Cdd:PLN02300 245 -GGKITREPGPLPGINTKITACLDPDGWKTVFVDNIDFLKELE 286
 
Name Accession Description Interval E-value
PLN02300 PLN02300
lactoylglutathione lyase
 1-283 0e+00

lactoylglutathione lyase


Pssm-ID: 215169 [Multi-domain]  Cd Length: 286  Bit Score: 557.86  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682443    1 MAEASDLLEWPKKDNRRFLHVVYRVGDLDRTIEFYTEVFGMKLLRKRDIPEEKYSNAFLGFGPETSNFVVELTYNYGVSS 80
Cdd:PLN02300   8 AAEAEDLLEWPKKDKRRMLHVVYRVGDLDRTIKFYTECLGMKLLRKRDIPEEKYTNAFLGYGPEDSNFVVELTYNYGVDK 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682443   81 YDIGTGFGHFAISTQDVSKLVENVRAKGGNVTREPGPVKGGGSVIAFVKDPDGYTFELIQRGPTPEPFCQVMLRVGDLDR 160
Cdd:PLN02300  88 YDIGTGFGHFGIAVEDVAKTVELVKAKGGKVTREPGPVKGGKSVIAFVKDPDGYKFELIQRGPTPEPLCQVMLRVGDLDR 167

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682443  161 AIKFYEKALGMRLLRKIERPEYKYTIGMMGYAEEYESIVLELTYNYDVTEYTKGNAYAQIAIGTDDVYKSGEVIKIVnqe 240
Cdd:PLN02300 168 SIKFYEKAFGMKLLRKRDNPEYKYTIAMMGYGPEDKTTVLELTYNYGVTEYTKGNAYAQIAIGTDDVYKTAEAIKLV--- 244

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 30682443  241 lGGKITREAGPLPGLGTKIVSFLDPDGWKTVLVDNKDFLKELE 283
Cdd:PLN02300 245 -GGKITREPGPLPGINTKITACLDPDGWKTVFVDNIDFLKELE 286
glyox_I TIGR00068
lactoylglutathione lyase; Lactoylglutathione lyase is also known as aldoketomutase and ...
 1-150 3.75e-89

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: 261.66  E-value: 3.75e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682443     1 MAEASDLLEWPKKDNRRFLHVVYRVGDLDRTIEFYTEVFGMKLLRKRDIPEEKYSNAFLGFGPETSNFVVELTYNYGVSS 80
Cdd:TIGR00068   1 MAESGDLVADPKTKKRRLLHTMLRVGDLDKSLDFYTEVLGMKLLRKRDFPEMKFSLAFLGYGDETSAAVIELTHNWGTEK 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682443    81 YDIGTGFGHFAISTQDVSKLVENVRAKGGNVTREPGPVKGGGSVIAFVKDPDGYTFELIQRGPTPEPFCQ 150
Cdd:TIGR00068  81 YDLGNGFGHIAIGVDDVYKACERVRALGGNVVREPGPVKGGTTVIAFVEDPDGYKIELIQRKSTKDGLGN 150
GlxI_Ni cd16358
Glyoxalase I that uses Ni(++) as cofactor; This family includes Escherichia coil and other ...
 19-139 7.74e-71

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: 214.18  E-value: 7.74e-71
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682443  19 LHVVYRVGDLDRTIEFYTEVFGMKLLRKRDIPEEKYSNAFLGFGPETSNFVVELTYNYGVSSYDIGTGFGHFAISTQDVS 98
Cdd:cd16358   2 LHTMLRVGDLDRSIKFYTEVLGMKLLRKRDYPEGKYTLAFVGYGDEDENTVLELTYNWGVDKYDLGTAYGHIAIGVEDVY 81

                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 30682443  99 KLVENVRAKGGNVTREPGPVKGGGSVIAFVKDPDGYTFELI 139
Cdd:cd16358  82 ETCERIRKKGGKVTREPGPMKGGTTVIAFVEDPDGYKIELI 122
GloA COG0346
Catechol 2,3-dioxygenase or related enzyme, vicinal oxygen chelate (VOC) family [Secondary ...
 16-143 9.73e-35

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: 122.02  E-value: 9.73e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682443  16 RRFLHVVYRVGDLDRTIEFYTEVFGMKLLRKRDIPEEKYSNAFLGFGpetSNFVVELTYNYGVSSYDIGTGFGHFAISTQ 95
Cdd:COG0346   1 MGLHHVTLRVSDLEASLAFYTDVLGLELVKRTDFGDGGFGHAFLRLG---DGTELELFEAPGAAPAPGGGGLHHLAFRVD 77

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
gi 30682443  96 DVSKLVENVRAKGGNVTREPGPVkGGGSVIAFVKDPDGYTFELIQRGP 143
Cdd:COG0346  78 DLDAAYARLRAAGVEIEGEPRDR-AYGYRSAYFRDPDGNLIELVEPPP 124
Glyoxalase pfam00903
Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;
17-138 4.58e-28

Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;


Pssm-ID: 395724 [Multi-domain]  Cd Length: 121  Bit Score: 104.45  E-value: 4.58e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682443    17 RFLHVVYRVGDLDRTIEFYTEVFGMKLLRKRDIPEEKYSNAFLGFGPETsnfVVELTYNYGVSSYDIGT---GFGHFAIS 93
Cdd:pfam00903   1 RIDHVALRVGDLEKSLDFYTDVLGFKLVEETDAGEEGGLRSAFFLAGGR---VLELLLNETPPPAAAGFgghHIAFIAFS 77

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 30682443    94 TQDVSKLVENVRAKGGNVTREPGPVKGGGSVIaFVKDPDGYTFEL 138
Cdd:pfam00903  78 VDDVDAAYDRLKAAGVEIVREPGRHGWGGRYS-YFRDPDGNLIEL 121
 
Name Accession Description Interval E-value
PLN02300 PLN02300
lactoylglutathione lyase
 1-283 0e+00

lactoylglutathione lyase


Pssm-ID: 215169 [Multi-domain]  Cd Length: 286  Bit Score: 557.86  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682443    1 MAEASDLLEWPKKDNRRFLHVVYRVGDLDRTIEFYTEVFGMKLLRKRDIPEEKYSNAFLGFGPETSNFVVELTYNYGVSS 80
Cdd:PLN02300   8 AAEAEDLLEWPKKDKRRMLHVVYRVGDLDRTIKFYTECLGMKLLRKRDIPEEKYTNAFLGYGPEDSNFVVELTYNYGVDK 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682443   81 YDIGTGFGHFAISTQDVSKLVENVRAKGGNVTREPGPVKGGGSVIAFVKDPDGYTFELIQRGPTPEPFCQVMLRVGDLDR 160
Cdd:PLN02300  88 YDIGTGFGHFGIAVEDVAKTVELVKAKGGKVTREPGPVKGGKSVIAFVKDPDGYKFELIQRGPTPEPLCQVMLRVGDLDR 167

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682443  161 AIKFYEKALGMRLLRKIERPEYKYTIGMMGYAEEYESIVLELTYNYDVTEYTKGNAYAQIAIGTDDVYKSGEVIKIVnqe 240
Cdd:PLN02300 168 SIKFYEKAFGMKLLRKRDNPEYKYTIAMMGYGPEDKTTVLELTYNYGVTEYTKGNAYAQIAIGTDDVYKTAEAIKLV--- 244

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 30682443  241 lGGKITREAGPLPGLGTKIVSFLDPDGWKTVLVDNKDFLKELE 283
Cdd:PLN02300 245 -GGKITREPGPLPGINTKITACLDPDGWKTVFVDNIDFLKELE 286
glyox_I TIGR00068
lactoylglutathione lyase; Lactoylglutathione lyase is also known as aldoketomutase and ...
 1-150 3.75e-89

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: 261.66  E-value: 3.75e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682443     1 MAEASDLLEWPKKDNRRFLHVVYRVGDLDRTIEFYTEVFGMKLLRKRDIPEEKYSNAFLGFGPETSNFVVELTYNYGVSS 80
Cdd:TIGR00068   1 MAESGDLVADPKTKKRRLLHTMLRVGDLDKSLDFYTEVLGMKLLRKRDFPEMKFSLAFLGYGDETSAAVIELTHNWGTEK 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682443    81 YDIGTGFGHFAISTQDVSKLVENVRAKGGNVTREPGPVKGGGSVIAFVKDPDGYTFELIQRGPTPEPFCQ 150
Cdd:TIGR00068  81 YDLGNGFGHIAIGVDDVYKACERVRALGGNVVREPGPVKGGTTVIAFVEDPDGYKIELIQRKSTKDGLGN 150
GlxI_Ni cd16358
Glyoxalase I that uses Ni(++) as cofactor; This family includes Escherichia coil and other ...
 19-139 7.74e-71

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: 214.18  E-value: 7.74e-71
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682443  19 LHVVYRVGDLDRTIEFYTEVFGMKLLRKRDIPEEKYSNAFLGFGPETSNFVVELTYNYGVSSYDIGTGFGHFAISTQDVS 98
Cdd:cd16358   2 LHTMLRVGDLDRSIKFYTEVLGMKLLRKRDYPEGKYTLAFVGYGDEDENTVLELTYNWGVDKYDLGTAYGHIAIGVEDVY 81

                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 30682443  99 KLVENVRAKGGNVTREPGPVKGGGSVIAFVKDPDGYTFELI 139
Cdd:cd16358  82 ETCERIRKKGGKVTREPGPMKGGTTVIAFVEDPDGYKIELI 122
GlxI_Ni cd16358
Glyoxalase I that uses Ni(++) as cofactor; This family includes Escherichia coil and other ...
 149-273 1.05e-54

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: 172.97  E-value: 1.05e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682443 149 CQVMLRVGDLDRAIKFYEKALGMRLLRKIERPEYKYTIGMMGYAEEYESIVLELTYNYDVTEYTKGNAYAQIAIGTDDVY 228
Cdd:cd16358   2 LHTMLRVGDLDRSIKFYTEVLGMKLLRKRDYPEGKYTLAFVGYGDEDENTVLELTYNWGVDKYDLGTAYGHIAIGVEDVY 81

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 30682443 229 KSGEVIKivnqELGGKITREAGPLPGLGTKIVSFLDPDGWKTVLV 273
Cdd:cd16358  82 ETCERIR----KKGGKVTREPGPMKGGTTVIAFVEDPDGYKIELI 122
PRK10291 PRK10291
glyoxalase I; Provisional
 24-140 4.16e-47

glyoxalase I; Provisional


Pssm-ID: 182358  Cd Length: 129  Bit Score: 154.03  E-value: 4.16e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682443   24 RVGDLDRTIEFYTEVFGMKLLRKRDIPEEKYSNAFLGFGPETSNFVVELTYNYGVSSYDIGTGFGHFAISTQDVSKLVEN 103
Cdd:PRK10291   3 RVGDLQRSIDFYTNVLGMKLLRTSENPEYKYSLAFVGYGPETEEAVIELTYNWGVDKYELGTAYGHIALSVDNAAEACEK 82

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 30682443  104 VRAKGGNVTREPGPVKGGGSVIAFVKDPDGYTFELIQ 140
Cdd:PRK10291  83 IRQNGGNVTREAGPVKGGTTVIAFVEDPDGYKIELIE 119
glyox_I TIGR00068
lactoylglutathione lyase; Lactoylglutathione lyase is also known as aldoketomutase and ...
 150-277 7.65e-47

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: 153.81  E-value: 7.65e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682443   150 QVMLRVGDLDRAIKFYEKALGMRLLRKIERPEYKYTIGMMGYAEEYESIVLELTYNYDVTEYTKGNAYAQIAIGTDDVYK 229
Cdd:TIGR00068  20 HTMLRVGDLDKSLDFYTEVLGMKLLRKRDFPEMKFSLAFLGYGDETSAAVIELTHNWGTEKYDLGNGFGHIAIGVDDVYK 99

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 30682443   230 SGEVIKivnqELGGKITREAGPLPGlGTKIVSFL-DPDGWKTVLVDNKD 277
Cdd:TIGR00068 100 ACERVR----ALGGNVVREPGPVKG-GTTVIAFVeDPDGYKIELIQRKS 143
GloA COG0346
Catechol 2,3-dioxygenase or related enzyme, vicinal oxygen chelate (VOC) family [Secondary ...
 16-143 9.73e-35

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: 122.02  E-value: 9.73e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682443  16 RRFLHVVYRVGDLDRTIEFYTEVFGMKLLRKRDIPEEKYSNAFLGFGpetSNFVVELTYNYGVSSYDIGTGFGHFAISTQ 95
Cdd:COG0346   1 MGLHHVTLRVSDLEASLAFYTDVLGLELVKRTDFGDGGFGHAFLRLG---DGTELELFEAPGAAPAPGGGGLHHLAFRVD 77

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
gi 30682443  96 DVSKLVENVRAKGGNVTREPGPVkGGGSVIAFVKDPDGYTFELIQRGP 143
Cdd:COG0346  78 DLDAAYARLRAAGVEIEGEPRDR-AYGYRSAYFRDPDGNLIELVEPPP 124
PRK10291 PRK10291
glyoxalase I; Provisional
 152-277 9.04e-34

glyoxalase I; Provisional


Pssm-ID: 182358  Cd Length: 129  Bit Score: 119.74  E-value: 9.04e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682443  152 MLRVGDLDRAIKFYEKALGMRLLRKIERPEYKYTIGMMGYAEEYESIVLELTYNYDVTEYTKGNAYAQIAIGTDDVYKSG 231
Cdd:PRK10291   1 MLRVGDLQRSIDFYTNVLGMKLLRTSENPEYKYSLAFVGYGPETEEAVIELTYNWGVDKYELGTAYGHIALSVDNAAEAC 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 30682443  232 EVIKivnqELGGKITREAGPLPGlGTKIVSFL-DPDGWKTVLVDNKD 277
Cdd:PRK10291  81 EKIR----QNGGNVTREAGPVKG-GTTVIAFVeDPDGYKIELIEEKD 122
Glyoxalase pfam00903
Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;
17-138 4.58e-28

Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;


Pssm-ID: 395724 [Multi-domain]  Cd Length: 121  Bit Score: 104.45  E-value: 4.58e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682443    17 RFLHVVYRVGDLDRTIEFYTEVFGMKLLRKRDIPEEKYSNAFLGFGPETsnfVVELTYNYGVSSYDIGT---GFGHFAIS 93
Cdd:pfam00903   1 RIDHVALRVGDLEKSLDFYTDVLGFKLVEETDAGEEGGLRSAFFLAGGR---VLELLLNETPPPAAAGFgghHIAFIAFS 77

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 30682443    94 TQDVSKLVENVRAKGGNVTREPGPVKGGGSVIaFVKDPDGYTFEL 138
Cdd:pfam00903  78 VDDVDAAYDRLKAAGVEIVREPGRHGWGGRYS-YFRDPDGNLIEL 121
GLOD4_N cd08358
N-terminal domain of human glyoxalase domain-containing protein 4 and similar proteins; ...
 16-141 8.17e-28

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: 103.98  E-value: 8.17e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682443  16 RRFLHVVYRVGDLDRTIEFYTEVFGMKLLRKRDIPE-----------EKYSNAFLGFGPETSNFVVELTYNYGVSSYDIG 84
Cdd:cd08358   1 RRALHFVFKVGDRNKTIKFYREILGMKVLRHEEFEEgckaacngpydGKWSKTMVGYGPEDDHFVVELTYNYGIGDYELG 80

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 30682443  85 TGFGHFAISTQDVsklVENVRakggnvtREPGPVKGGGSVIAFVKDPDGYTFELIQR 141
Cdd:cd08358  81 NDFLGITIHSKQA---VSRAK-------KHNWPVTQVGDGVYEVKAPGGYKFYLIDK 127
GlxI_Zn cd07233
Glyoxalase I that uses Zn(++) as cofactor; This family includes eukaryotic glyoxalase I that ...
 18-139 1.32e-27

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: 103.95  E-value: 1.32e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682443  18 FLHVVYRVGDLDRTIEFYTEVFGMKLLRKRDIPEEKYSNAFLGFG-PETSNF------------VVELTYNYGV-----S 79
Cdd:cd07233   1 FNHTMLRVKDPKKSLKFYTEVLGMKLLRKKDFPEMKFSLYFLGYEdPKDIPKdprtawvfsregTLELTHNWGTendedP 80

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 30682443  80 SYDIG----TGFGHFAISTQDVSKLVENVRAKGGNVTREP--GPVKGggsvIAFVKDPDGYTFELI 139
Cdd:cd07233  81 VYHNGnsdpRGFGHIGIAVDDVYAACERFEELGVKFKKKPddGKMKG----IAFIKDPDGYWIEIL 142
VOC cd06587
vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate (VOC) superfamily is composed ...
 20-138 5.79e-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: 82.96  E-value: 5.79e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682443  20 HVVYRVGDLDRTIEFYTEVFGMKLLRKRDIPEEkysnAFLGFGPETsnfVVELTYNYGVsSYDIGTGFGHFAISTQDVSK 99
Cdd:cd06587   1 HVALRVPDLDASVAFYEEVLGFEVVSRNEGGGF----AFLRLGPGL---RLALLEGPEP-ERPGGGGLFHLAFEVDDVDE 72

                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 30682443 100 LVE-NVRAKGGNVTREPGPVKGGGSVIAFVKDPDGYTFEL 138
Cdd:cd06587  73 VDErLREAGAEGELVAPPVDDPWGGRSFYFRDPDGNLIEF 112
PLN03042 PLN03042
Lactoylglutathione lyase; Provisional
 22-139 6.55e-20

Lactoylglutathione lyase; Provisional


Pssm-ID: 215548  Cd Length: 185  Bit Score: 84.87  E-value: 6.55e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682443   22 VYRVGDLDRTIEFYTEVFGMKLLRKRDIPEEKYSNAFLGF---------GPETSNFV------VELTYNYGVSS------ 80
Cdd:PLN03042  32 MFRIKDPKASLDFYSRVLGMSLLKRLDFPEMKFSLYFLGYedsetaptdPPERTVWTfgrkatIELTHNWGTESdpefkg 111

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 30682443   81 YDIG----TGFGHFAISTQDVSKLVENVRAKGGNVTREP--GPVKGggsvIAFVKDPDGYTFELI 139
Cdd:PLN03042 112 YHNGnsdpRGFGHIGITVDDVYKACERFEKLGVEFVKKPddGKMKG----LAFIKDPDGYWIEIF 172
PLN02367 PLN02367
lactoylglutathione lyase
 22-138 9.28e-20

lactoylglutathione lyase


Pssm-ID: 177995  Cd Length: 233  Bit Score: 85.44  E-value: 9.28e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682443   22 VYRVGDLDRTIEFYTEVFGMKLLRKRDIPEEKYSNAFLGFGPETS---------------NFVVELTYNYGVSS------ 80
Cdd:PLN02367  80 MYRIKDPKASLDFYSRVLGMSLLKRLDFPEMKFSLYFMGYEDTASaptdptertvwtfgqKATIELTHNWGTESdpdfkg 159

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 30682443   81 YDIGT----GFGHFAISTQDVSKLVENVRAKGGNVTREP--GPVKGggsvIAFVKDPDGYTFEL 138
Cdd:PLN02367 160 YHNGNseprGFGHIGITVDDVYKACERFEELGVEFVKKPndGKMKG----IAFIKDPDGYWIEI 219
GloA COG0346
Catechol 2,3-dioxygenase or related enzyme, vicinal oxygen chelate (VOC) family [Secondary ...
 151-267 1.49e-19

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: 81.96  E-value: 1.49e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682443 151 VMLRVGDLDRAIKFYEKALGMRLLRKIERPEYKYTIGMMGYAEEYEsivLELTYNYDVTEYTKGNAYAQIAIGTDDVYKS 230
Cdd:COG0346   6 VTLRVSDLEASLAFYTDVLGLELVKRTDFGDGGFGHAFLRLGDGTE---LELFEAPGAAPAPGGGGLHHLAFRVDDLDAA 82

                        90       100       110
                ....*....|....*....|....*....|....*..
gi 30682443 231 GEVIKivnqELGGKITREAGPLPGlGTKIVSFLDPDG 267
Cdd:COG0346  83 YARLR----AAGVEIEGEPRDRAY-GYRSAYFRDPDG 114
CatE COG2514
Catechol-2,3-dioxygenase [Secondary metabolites biosynthesis, transport and catabolism];
16-173 1.60e-17

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


Pssm-ID: 442004 [Multi-domain]  Cd Length: 141  Bit Score: 77.31  E-value: 1.60e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682443  16 RRFLHVVYRVGDLDRTIEFYTEVFGMKLLRKRDipeekySNAFLGFGPETSnfVVELTYNYGVSSYDIGTGFGHFAI--- 92
Cdd:COG2514   2 TRLGHVTLRVRDLERSAAFYTDVLGLEVVEREG------GRVYLRADGGEH--LLVLEEAPGAPPRPGAAGLDHVAFrvp 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682443  93 STQDVSKLVENVRAKGgnvTREPGPVKGGGSVIAFVKDPDGYTFELIQRGPTPEpfcqvmlRVGDLDRaikfyeKALGMR 172
Cdd:COG2514  74 SRADLDAALARLAAAG---VPVEGAVDHGVGESLYFRDPDGNLIELYTDRPRFE-------HVGDLET------DVLGFR 137


                .
gi 30682443 173 L 173
Cdd:COG2514 138 L 138
VOC COG3324
Lactoylglutathione lyase-related enzyme, vicinal oxygen chelate (VOC) family [General function ...
 17-143 4.56e-16

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


Pssm-ID: 442553 [Multi-domain]  Cd Length: 119  Bit Score: 72.75  E-value: 4.56e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682443  17 RFLHVVYRVGDLDRTIEFYTEVFGMKLLRKRDiPEEKYsnAFLGFGPETSNFVVEltynygvSSYDIGTGFGHFAISTQD 96
Cdd:COG3324   4 TIVWVELPVDDLERAKAFYEEVFGWTFEDDAG-PGGDY--AEFDTDGGQVGGLMP-------GAEEPGGPGWLLYFAVDD 73

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 30682443  97 VSKLVENVRAKGGNVTREPGPVKGGGsVIAFVKDPDGYTFELIQRGP 143
Cdd:COG3324  74 LDAAVARVEAAGGTVLRPPTDIPPWG-RFAVFRDPEGNRFGLWQPAA 119
Glyoxalase pfam00903
Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;
150-269 4.94e-16

Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;


Pssm-ID: 395724 [Multi-domain]  Cd Length: 121  Bit Score: 72.48  E-value: 4.94e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682443   150 QVMLRVGDLDRAIKFYEKALGMRLLRKIERPEYKYTIGMMGYAEEYesiVLELTYNYDVTEYTKGNA---YAQIAIGTDD 226
Cdd:pfam00903   4 HVALRVGDLEKSLDFYTDVLGFKLVEETDAGEEGGLRSAFFLAGGR---VLELLLNETPPPAAAGFGghhIAFIAFSVDD 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 30682443   227 VYKSGEVIKivnqELGGKITREAGPLPGlGTKIVSFLDPDGWK 269
Cdd:pfam00903  81 VDAAYDRLK----AAGVEIVREPGRHGW-GGRYSYFRDPDGNL 118
GlxI_Zn cd07233
Glyoxalase I that uses Zn(++) as cofactor; This family includes eukaryotic glyoxalase I that ...
 148-268 7.30e-16

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: 72.74  E-value: 7.30e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682443 148 FCQVMLRVGDLDRAIKFYEKALGMRLLRKIERPEYKYTIGMMGY-------AEEYESI------VLELTYNY-----DVT 209
Cdd:cd07233   1 FNHTMLRVKDPKKSLKFYTEVLGMKLLRKKDFPEMKFSLYFLGYedpkdipKDPRTAWvfsregTLELTHNWgtendEDP 80

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 30682443 210 EYTKGNAYAQ----IAIGTDDVYKSGEVIKivnqELGGKITReaGPLPGLGTKIVSFLDPDGW 268
Cdd:cd07233  81 VYHNGNSDPRgfghIGIAVDDVYAACERFE----ELGVKFKK--KPDDGKMKGIAFIKDPDGY 137
GLOD4_N cd08358
N-terminal domain of human glyoxalase domain-containing protein 4 and similar proteins; ...
 153-274 1.16e-13

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: 66.23  E-value: 1.16e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682443 153 LRVGDLDRAIKFYEKALGMRLLRKIERPE---------Y--KYTIGMMGYAEEYESIVLELTYNYDVTEYTKGNAYAQIA 221
Cdd:cd08358   8 FKVGDRNKTIKFYREILGMKVLRHEEFEEgckaacngpYdgKWSKTMVGYGPEDDHFVVELTYNYGIGDYELGNDFLGIT 87

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|...
gi 30682443 222 IGTDDVYKsgevikivnqelggKITREAGPLPGLGTKIVSFLDPDGWKTVLVD 274
Cdd:cd08358  88 IHSKQAVS--------------RAKKHNWPVTQVGDGVYEVKAPGGYKFYLID 126
PLN02367 PLN02367
lactoylglutathione lyase
 150-276 5.81e-13

lactoylglutathione lyase


Pssm-ID: 177995  Cd Length: 233  Bit Score: 66.95  E-value: 5.81e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682443  150 QVMLRVGDLDRAIKFYEKALGMRLLRKIERPEYKYTIGMMGY-------AEEYESIV--------LELTYNY------DV 208
Cdd:PLN02367  78 QTMYRIKDPKASLDFYSRVLGMSLLKRLDFPEMKFSLYFMGYedtasapTDPTERTVwtfgqkatIELTHNWgtesdpDF 157

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 30682443  209 TEYTKGNA----YAQIAIGTDDVYKSGEVIKivnqELGGKITREagPLPGLGTKIVSFLDPDGWKTVLVDNK 276
Cdd:PLN02367 158 KGYHNGNSeprgFGHIGITVDDVYKACERFE----ELGVEFVKK--PNDGKMKGIAFIKDPDGYWIEIFDLK 223
PLN03042 PLN03042
Lactoylglutathione lyase; Provisional
 150-268 5.39e-12

Lactoylglutathione lyase; Provisional


Pssm-ID: 215548  Cd Length: 185  Bit Score: 63.30  E-value: 5.39e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682443  150 QVMLRVGDLDRAIKFYEKALGMRLLRKIERPEYKYTIGMMGYaEEYESI----------------VLELTYNY------D 207
Cdd:PLN03042  30 QTMFRIKDPKASLDFYSRVLGMSLLKRLDFPEMKFSLYFLGY-EDSETAptdppertvwtfgrkaTIELTHNWgtesdpE 108

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 30682443  208 VTEYTKGNA----YAQIAIGTDDVYKSGEVIkivnQELGGKITREagPLPGlGTKIVSFL-DPDGW 268
Cdd:PLN03042 109 FKGYHNGNSdprgFGHIGITVDDVYKACERF----EKLGVEFVKK--PDDG-KMKGLAFIkDPDGY 167
VOC cd06587
vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate (VOC) superfamily is composed ...
 151-269 9.69e-12

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: 60.62  E-value: 9.69e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682443 151 VMLRVGDLDRAIKFYEKALGMRLLRKIERPEYKytigMMGYAEEyesIVLELTYNYDVtEYTKGNAYAQIAIGTDDVYks 230
Cdd:cd06587   2 VALRVPDLDASVAFYEEVLGFEVVSRNEGGGFA----FLRLGPG---LRLALLEGPEP-ERPGGGGLFHLAFEVDDVD-- 71

                        90       100       110
                ....*....|....*....|....*....|....*....
gi 30682443 231 gEVIKIVNQELGGKITREAGPLPGLGTKIVSFLDPDGWK 269
Cdd:cd06587  72 -EVDERLREAGAEGELVAPPVDDPWGGRSFYFRDPDGNL 109
PhnB COG2764
Zn-dependent glyoxalase, PhnB family [Energy production and conversion];
24-141 7.78e-10

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


Pssm-ID: 442048 [Multi-domain]  Cd Length: 118  Bit Score: 55.25  E-value: 7.78e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682443  24 RVGDLDRTIEFYTEVFGMKLLRKRDIPEEKYSNAFLGFGpetsNFVVELTYNYGVSSYDIGTGFgHFAISTQDVSKLVEN 103
Cdd:COG2764   7 VVDDAEEALEFYEDVFGFEVVFRMTDPDGKIMHAELRIG----GSVLMLSDAPPDSPAAEGNGV-SLSLYVDDVDALFAR 81

                        90       100       110
                ....*....|....*....|....*....|....*...
gi 30682443 104 VRAKGGNVTREPGPvKGGGSVIAFVKDPDGYTFELIQR 141
Cdd:COG2764  82 LVAAGATVVMPLQD-TFWGDRFGMVRDPFGVLWMINTP 118
MMCE cd07249
Methylmalonyl-CoA epimerase (MMCE); MMCE, also called methylmalonyl-CoA racemase (EC 5.1.99.1) ...
 20-140 9.01e-10

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: 55.66  E-value: 9.01e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682443  20 HVVYRVGDLDRTIEFYTEVFGMKLLRKRDIPEEKYSNAFLGFGP----------ETSNFVVELTYNygvssydiGTGFGH 89
Cdd:cd07249   3 HIGIAVPDLDEALKFYEDVLGVKVSEPEELEEQGVRVAFLELGNtqielleplgEDSPIAKFLDKK--------GGGLHH 74

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|...
gi 30682443  90 FAISTQDVSKLVENVRAKGGNVTREPGPVKGGGSVIAFV--KDPDGYTFELIQ 140
Cdd:cd07249  75 IAFEVDDIDAAVEELKAQGVRLLSEGPRIGAHGKRVAFLhpKDTGGVLIELVE 127
SgaA_N_like cd07247
N-terminal domain of Streptomyces griseus SgaA and similar domains; SgaA suppresses the growth ...
 25-140 1.65e-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: 54.58  E-value: 1.65e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682443  25 VGDLDRTIEFYTEVFGmklLRKRDIPEEKYSNAFLGFGPETSNFVVELTynygvssYDIGTGFGHFAI--STQDVSKLVE 102
Cdd:cd07247   8 TTDLERAKAFYGAVFG---WTFEDEGDGGGDYALFTAGGGAVGGLMRAP-------EEVAGAPPGWLIyfAVDDLDAALA 77

                        90       100       110
                ....*....|....*....|....*....|....*...
gi 30682443 103 NVRAKGGNVTREPGPVKGGGsVIAFVKDPDGYTFELIQ 140
Cdd:cd07247  78 RVEAAGGKVVVPPTDIPGGG-RFAVFADPEGNRFGLWS 114
VOC_like cd07251
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 25-138 1.87e-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: 319914 [Multi-domain]  Cd Length: 120  Bit Score: 54.61  E-value: 1.87e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682443  25 VGDLDRTIEFYTEVfGMKLLRKrdiPEEKYSNAFLGfgpetsNFVVELtYNYGVSSYDIG-----TGFGHFAI-----ST 94
Cdd:cd07251   6 VRDLERSARFYEAL-GWKPNLD---PNDGVVFFQLG------GTVLAL-YPRDALAEDAGvsvtgAGFSGVTLahnvrSR 74

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 30682443  95 QDVSKLVENVRAKGGNVTREPGPVKGGGsVIAFVKDPDGYTFEL 138
Cdd:cd07251  75 EEVDQLLAKAVAAGGKILKPPQEVFWGG-YSGYFADPDGHIWEV 117
BphC5-RrK37_N_like cd08362
N-terminal, non-catalytic, domain of BphC5 (2,3-dihydroxybiphenyl 1,2-dioxygenase) from ...
 20-139 3.78e-09

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: 53.41  E-value: 3.78e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682443  20 HVVYRVGDLDRTIEFYTEVFGMKLLrkrdipEEKYSNAFL-GFGPEtsNFVVELTynygvSSYDIGTGFGHFAIST-QDV 97
Cdd:cd08362   6 YVALGVPDLAAEREFYTEVWGLEEV------AEDDDVVYLrAEGSE--HHVLRLR-----QSDENRLDLIAFAAATrADV 72

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 30682443  98 SKLVENVRAKGGNVTREPGPVK--GGGSVIAFVkDPDGYTFELI 139
Cdd:cd08362  73 DALAARLAAAGVRILSEPGPLDdpGGGYGFRFF-DPDGRTIEVS 115
ED_TypeI_classII_N cd16360
N-terminal domain of type I, class II extradiol dioxygenases; This family contains the ...
 20-139 3.86e-09

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: 53.47  E-value: 3.86e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682443  20 HVVYRVGDLDRTIEFYTEVFGMKLLRkrdipEEKYSNAFLGFGPETSNFVVeltYNygvssyDIGTGFGHFAI---STQD 96
Cdd:cd16360   1 YAELGVPDLEKALEFYTDVLGLQVAK-----RDGNSVYLRGYEDEHHSLVL---YE------APEAGLKHFAFevaSEED 66

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 30682443  97 VSKLVENVRAKGGNVTREPGP-VKGGGSVIAFvKDPDGYTFELI 139
Cdd:cd16360  67 LERAAASLTALGCDVTWGPDGeVPGGGKGFRF-QDPSGHLLELF 109
VOC_ShValD_like cd16361
vicinal oxygen chelate (VOC) family protein similar to Streptomyces hygroscopicus ValD protein; ...
 20-140 7.73e-09

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: 53.49  E-value: 7.73e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682443  20 HVVYRVGDLDRTIEFYTEVFGMKLL--------RKRDIPEEKYSN----------AFLGFGPETSnfvVEL-TYNYGVSS 80
Cdd:cd16361   4 HVGITVPDLDAAVEFYTDVLGAEVVyrstplaeGDRGGGEMRAAGfvpgfarariAMLRLGPGPG---IELfEYKGPEQR 80

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682443  81 YDI----GTGFGHFAISTQDVSKLVENVRAKGGNVTREP------GPVKGGGSViaFVKDPDGYTFELIQ 140
Cdd:cd16361  81 APVprnsDVGIFHFALQVDDVEAAAERLAAAGGKVLMGPreipdgGPGKGNRMV--YLRDPWGTLIELVS 148
VOC COG3324
Lactoylglutathione lyase-related enzyme, vicinal oxygen chelate (VOC) family [General function ...
 145-267 1.19e-08

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


Pssm-ID: 442553 [Multi-domain]  Cd Length: 119  Bit Score: 52.33  E-value: 1.19e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682443 145 PEPFCQVMLRVGDLDRAIKFYEKALGMRLLRKIErPEYKYTIgmmgyAEEYESIVLELTynydVTEYTKGNAYAQIAIGT 224
Cdd:COG3324   2 PGTIVWVELPVDDLERAKAFYEEVFGWTFEDDAG-PGGDYAE-----FDTDGGQVGGLM----PGAEEPGGPGWLLYFAV 71

                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
gi 30682443 225 DDVykSGEVIKIVnqELGGKITREAGPLPGLGtKIVSFLDPDG 267
Cdd:COG3324  72 DDL--DAAVARVE--AAGGTVLRPPTDIPPWG-RFAVFRDPEG 109
Glyoxalase_4 pfam13669
Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;
20-127 1.96e-08

Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;


Pssm-ID: 463951 [Multi-domain]  Cd Length: 109  Bit Score: 51.13  E-value: 1.96e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682443    20 HVVYRVGDLDRTIEFYTEVFGMKLLRKRDIPEEKYSNAFLGFGpeTSNFVVELTYNYGVSSY--DIGTGFGHFAISTQDV 97
Cdd:pfam13669   2 HVGIAVPDLDRALALWGALLGLGPEGDYRSEPQNVDLAFALLG--DGPVEVELIQPLDGDSPlaRHGPGLHHLAYWVDDL 79

                          90       100       110
                  ....*....|....*....|....*....|
gi 30682443    98 SKLVENVRAKGGNVTREPGPVKGGGSVIAF 127
Cdd:pfam13669  80 DAAVARLLDQGYRVAPKGPRAGAAGRRVAF 109
VOC_like cd07264
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 18-138 1.24e-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: 49.25  E-value: 1.24e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682443  18 FLHVVYRVGDLDRTIEFYTEVFGmkLLRKRDIPEEKYSNAFLGfGPETSNFVVELTYNYGVSsyDIGTGFGHFAISTQDV 97
Cdd:cd07264   1 IAYIVLYVDDFAASLRFYRDVLG--LPPRFLHEEGEYAEFDTG-ETKLALFSRKEMARSGGP--DRRGSAFELGFEVDDV 75

                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 30682443  98 SKLVENVRAKGGNVTREPGPVKGGGSViAFVKDPDGYTFEL 138
Cdd:cd07264  76 EATVEELVERGAEFVREPANKPWGQTV-AYVRDPDGNLIEI 115
VOC_like cd07245
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 18-138 1.45e-07

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


Pssm-ID: 319909 [Multi-domain]  Cd Length: 117  Bit Score: 49.24  E-value: 1.45e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682443  18 FLHVVYRVGDLDRTIEFYTEVFGMKLLRKRdiPEEKYSNAFLGFGPETSNFVVELTyNYGVSSYDIGTGFG-HFAISTQD 96
Cdd:cd07245   1 LDHVALACPDLERARRFYTDVLGLEEVPRP--PFLKFGGAWLYLGGGQQIHLVVEQ-NPSELPRPEHPGRDrHPSFSVPD 77

                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 30682443  97 VSKLVENVRAKGGNVTREpgPVKGGGSVIAFVKDPDGYTFEL 138
Cdd:cd07245  78 LDALKQRLKEAGIPYTES--TSPGGGVTQLFFRDPDGNRLEF 117
GLOD4_C cd16357
C-terminal domain of human glyoxalase domain-containing protein 4 and similar proteins; ...
 20-134 2.54e-07

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: 48.32  E-value: 2.54e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682443  20 HVVYRVGDLDRTIEFYTEVFGMKLLRKRDipeekySNAFLGFGPEtsNFVVELtyNYGVSSYDIGTGFGH--FAISTQDV 97
Cdd:cd16357   1 KVSLAVSDLEKSIDYWSDLLGMKVFEKSE------KSALLGYGED--QAKLEL--VDIPEPVDHGTAFGRiaFSCPADEL 70

                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 30682443  98 SKLVENVRAKGGNVTREP----GPVKGGGSVIaFVKDPDGY 134
Cdd:cd16357  71 PPIEEKVKAAGQTILTPLvsldTPGKATVQVV-ILADPDGH 110
COG3607 COG3607
Lactoylglutathione lyase-related enzyme, vicinal oxygen chelate (VOC) family [General function ...
 25-140 4.76e-07

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


Pssm-ID: 442825  Cd Length: 126  Bit Score: 47.90  E-value: 4.76e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682443  25 VGDLDRTIEFYTEvFGMKllRKRDIPEEKYsnAFLGFGPetsNFVVEL-TYNY-----GVSSYDiGTGFG-----HFAIS 93
Cdd:COG3607  11 VADLERSRAFYEA-LGFT--FNPQFSDEGA--ACFVLGE---GIVLMLlPREKfatftGKPIAD-ATGFTevllaLNVES 81

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 30682443  94 TQDVSKLVENVRAKGGNVTREPGPVKGGGSviAFVKDPDGYTFELIQ 140
Cdd:COG3607  82 REEVDALVAKALAAGGTVLKPPQDVGGMYS--GYFADPDGHLWEVAW 126
GLOD5 cd07253
Human glyoxalase domain-containing protein 5 and similar proteins; Uncharacterized subfamily ...
 20-138 5.55e-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: 47.61  E-value: 5.55e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682443  20 HVVYRVGDLDRTIEFYTEVFGMKLLRKRdipEEKYSnafLGFGPETSNfVVELTYNYGVSSYDIGTGFGHFAISTQ-DVS 98
Cdd:cd07253   6 HLVLTVKDIERTIDFYTKVLGMTVVTFK---EGRKA---LRFGNQKIN-LHQKGKEFEPKASAPTPGSADLCFITEtPID 78

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
gi 30682443  99 KLVENVRAKGgnVTREPGPVKGGG------SViaFVKDPDGYTFEL 138
Cdd:cd07253  79 EVLEHLEACG--VTIEEGPVKRTGalgpilSI--YFRDPDGNLIEL 120
VOC_BsYqjT cd07242
vicinal oxygen chelate (VOC) family protein similar to Bacillus subtilis YqjT; The vicinal ...
 18-139 8.47e-07

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: 47.10  E-value: 8.47e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682443  18 FLHVVYRVGDLDRTIEFYTEVFGMKLlrkRDIpeEKYSNAFLGFGPETSNFVVELTYNYGVSSYD-IGTGFGHFAI---S 93
Cdd:cd07242   2 VSHVELAVSDLHRSFKWFEWILGLGW---KEY--DTWSFGPSWKLSGGSLLVVQQTDEFATPEFDrARVGLNHLAFhaeS 76

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
gi 30682443  94 TQDVSKLVENVRAKGGNVT-REPGPVKGG-GSVIAFVKDPDGYTFELI 139
Cdd:cd07242  77 REAVDELTEKLAKIGGVRTyGDRHPFAGGpPHYAAFCEDPDGIKLELV 124
HppD COG3185
4-hydroxyphenylpyruvate dioxygenase and related hemolysins [Amino acid transport and ...
 84-175 4.59e-06

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: 47.19  E-value: 4.59e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682443  84 GTGFGHFAISTQDVSKLVENVRAKGGNVTREPGP-------VKG-GGSVIAFVkDPDGYT------FELIQRGPTPEPfc 149
Cdd:COG3185  65 GPGVCAIAFRVDDAAAAYERALALGAEPFEGPGPgelripaIRGiGGSLHYFV-DRYGYGgiydpdFEPLPGDAAPAG-- 141

                        90       100       110
                ....*....|....*....|....*....|....*.
gi 30682443 150 qVML----------RVGDLDRAIKFYEKALGMRLLR 175
Cdd:COG3185 142 -AGLtridhigiavPRGDLDEWVLFYEDVLGFEEIR 176
VOC_like cd07246
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 25-141 8.15e-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: 319910 [Multi-domain]  Cd Length: 124  Bit Score: 44.21  E-value: 8.15e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682443  25 VGDLDRTIEFYTEVFGMKLLRKRDIPEEKYSNAFLGFGpETSNFVVELTYNYGVSSYDIGTGFG-HFAISTQDVSKLVEN 103
Cdd:cd07246   9 VEDAAAAIAFYKKAFGAEELGRTTQEDGRVGHAELRIG-GTVVMVADENPERGALSPTKLGGTPvIFHLYVEDVDATFAR 87

                        90       100       110
                ....*....|....*....|....*....|....*...
gi 30682443 104 VRAKGGNVTREPgPVKGGGSVIAFVKDPDGYTFELIQR 141
Cdd:cd07246  88 AVAAGAVVVEPV-EDQFWGDRVGKVKDPFGHVWWLATP 124
Fosfomycin_RP cd08345
Fosfomycin resistant protein; This family contains three types of fosfomycin resistant protein. ...
 20-138 2.17e-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: 42.93  E-value: 2.17e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682443  20 HVVYRVGDLDRTIEFYTEVFGMKLLRKRDIPEEKYSN-AFLGFGPetsnfvVELTYNYGVSSydIGTGFGH--FAISTQD 96
Cdd:cd08345   1 HITLIVRDLEKSTAFLQDIFGAREVYSSGDKTFSLSKeKFFLLGG------LWIALMEGESL--QERSYTHiaFQIQSED 72

                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 30682443  97 VSKLVENVRAKGGNVTREPGPVKGGGSVIAFVkDPDGYTFEL 138
Cdd:cd08345  73 FDRYAERLGALGVEMRPPRPRVEGEGRSIYFY-DPDNHLFEL 113
VOC_like cd08354
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 22-138 9.50e-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: 9.50e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682443  22 VYrVGDLDRTIEFYTEVFGMKLLRKRDipeekySNAFLGFGPEtsnfvVELTYNYGVSSYDI---------GTGFGH--F 90
Cdd:cd08354   6 LY-ADDLDAAEAFYEDVLGLKPMLRSG------RHAFFRLGPQ-----VLLVFDPGATSKDVrtgevpghgASGHGHfaF 73

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
gi 30682443  91 AISTQDVSKLVENVRAKGGNVTREPGPVKGGGSViaFVKDPDGYTFEL 138
Cdd:cd08354  74 AVPTEELAAWEARLEAKGVPIESYTQWPEGGKSL--YFRDPAGNLVEL 119
VOC_like cd07254
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 16-141 1.25e-04

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


Pssm-ID: 319917 [Multi-domain]  Cd Length: 120  Bit Score: 40.91  E-value: 1.25e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682443  16 RRFlHVVYRVGDLDRTIEFYTEVFGMKllrkrdiPEEKYsnaflgfgPETSNFVVE---LTYNYGVSSYDIGTGFGHFAI 92
Cdd:cd07254   1 KRF-HLSLNVTDLERSIRFYSDLFGAE-------PAKRK--------ADYAKFMLEdppLNLALLVNDRKEPYGLNHLGI 64

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|...
gi 30682443  93 STQDVSKL-VENVRA-KGGNVTREPGPVKGGGSVI--AFVKDPDGYTFELIQR 141
Cdd:cd07254  65 QVDSKEEVaALKARAeAAGLPVRKEPRTTCCYAVQdkFWLTDPDGNAWEFYAT 117
SgaA_N_like cd07247
N-terminal domain of Streptomyces griseus SgaA and similar domains; SgaA suppresses the growth ...
 155-267 1.43e-04

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: 40.33  E-value: 1.43e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682443 155 VGDLDRAIKFYEKALGMRLLRkierpeykYTIGMMGYAeeyesivlELTYN-------YDVTEYTKG-NAYAQIAIGTDD 226
Cdd:cd07247   8 TTDLERAKAFYGAVFGWTFED--------EGDGGGDYA--------LFTAGggavgglMRAPEEVAGaPPGWLIYFAVDD 71

                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 30682443 227 VyksGEVIKIVnQELGGKITREAGPLPGLGTKIVsFLDPDG 267
Cdd:cd07247  72 L---DAALARV-EAAGGKVVVPPTDIPGGGRFAV-FADPEG 107
MMCE cd07249
Methylmalonyl-CoA epimerase (MMCE); MMCE, also called methylmalonyl-CoA racemase (EC 5.1.99.1) ...
 149-273 1.86e-04

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: 40.25  E-value: 1.86e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682443 149 CQVMLRVGDLDRAIKFYEKALGMRLLRKIERPEYKYTIGMMGYAEeyesIVLEL------TYNYDVTEYTKGNAYAQIAI 222
Cdd:cd07249   2 DHIGIAVPDLDEALKFYEDVLGVKVSEPEELEEQGVRVAFLELGN----TQIELleplgeDSPIAKFLDKKGGGLHHIAF 77

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 30682443 223 GTDDVYKSGEVIKivnqELGGKITREaGPLPGLGTKIVSFLDPDGWKTVLV 273
Cdd:cd07249  78 EVDDIDAAVEELK----AQGVRLLSE-GPRIGAHGKRVAFLHPKDTGGVLI 123
CatE COG2514
Catechol-2,3-dioxygenase [Secondary metabolites biosynthesis, transport and catabolism];
151-267 1.98e-04

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


Pssm-ID: 442004 [Multi-domain]  Cd Length: 141  Bit Score: 40.71  E-value: 1.98e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682443 151 VMLRVGDLDRAIKFYEKALGMRLlrkIERPEYKYTIGMMGyaeeyESIVLELTYNYDVTEYTKGNAYAQIAIGTDDVYKS 230
Cdd:COG2514   7 VTLRVRDLERSAAFYTDVLGLEV---VEREGGRVYLRADG-----GEHLLVLEEAPGAPPRPGAAGLDHVAFRVPSRADL 78

                        90       100       110
                ....*....|....*....|....*....|....*..
gi 30682443 231 GEVIKIVnQELGGKITreaGPLPGLGTKIVSFLDPDG 267
Cdd:COG2514  79 DAALARL-AAAGVPVE---GAVDHGVGESLYFRDPDG 111
FosA cd07244
fosfomycin resistant protein subfamily FosA; This subfamily family contains FosA, a fosfomycin ...
 20-138 2.87e-04

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: 39.57  E-value: 2.87e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682443  20 HVVYRVGDLDRTIEFYTEVFGMKLLRKRDipeekySNAFLGFGpetsNFVVELTY-NYGVSSYDigtgFGHFA--ISTQD 96
Cdd:cd07244   4 HITLAVSDLERSLAFYVDLLGFKPHVRWD------KGAYLTAG----DLWLCLSLdPAAEPSPD----YTHIAftVSEED 69

                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 30682443  97 VSKLVENVRAKGGNVTREPgpvKGGGSVIAFVkDPDGYTFEL 138
Cdd:cd07244  70 FEELSERLRAAGVKIWQEN---SSEGDSLYFL-DPDGHKLEL 107
VOC_BsYyaH cd07241
vicinal oxygen chelate (VOC) family protein similar to Bacillus subtilis YyaH; The vicinal ...
 20-138 4.78e-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: 39.31  E-value: 4.78e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682443  20 HVVYRVGDLDRTIEFYTEVFGMKLLRKRDIPEEKYSNAFLGFGpetSNFVVELTYNYGVSSYDIG---TGFGHFAIST-- 94
Cdd:cd07241   4 HVALWTNDLERMKDFYVKYFGAESNDIYHNKKKGFRSYFLTFD---SGARLELMSRPDVTDPDKEverTGLAHIAFSVgs 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 30682443  95 -QDVSKLVENVRAKGGNVTREPgPVKGGGSVIAFVKDPDGYTFEL 138
Cdd:cd07241  81 kEAVDELTERLRADGYAVVGGP-RTTGDGYYESVILDPEGNRIEI 124
VOC_like cd07262
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 151-269 1.85e-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: 319923 [Multi-domain]  Cd Length: 121  Bit Score: 37.59  E-value: 1.85e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682443 151 VMLRVGDLDRAIKFYEKA---LGMRLLRKIErpeykytiGMMGYAEEyESIVLELTYNYDVTEYTKGNAyAQIAIGTDDv 227
Cdd:cd07262   4 VTIGVNDLERSRAFYDAAlapLGYKRGFEDG--------GRVGYGLE-GGPDFWVTEPFDGEPATAGNG-THVAFAAPS- 72

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
gi 30682443 228 ykSGEV----IKIVnqELGGKITREAGPLPGLGTKI-VSFL-DPDGWK 269
Cdd:cd07262  73 --RAAVdafhAAAL--AAGGTDNGAPGLRPHYHPGYyAAYVrDPDGNK 116
PhnB COG2764
Zn-dependent glyoxalase, PhnB family [Energy production and conversion];
153-227 2.48e-03

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


Pssm-ID: 442048 [Multi-domain]  Cd Length: 118  Bit Score: 37.14  E-value: 2.48e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 30682443 153 LRVGDLDRAIKFYEKALGMRLLRKIERPEykytiGMMGYAE-EYESIVLELTYNYDVTEYTKGNAYAqIAIGTDDV 227
Cdd:COG2764   6 LVVDDAEEALEFYEDVFGFEVVFRMTDPD-----GKIMHAElRIGGSVLMLSDAPPDSPAAEGNGVS-LSLYVDDV 75
THT_Oxygenase_N cd07267
N-terminal domain of 2,4,5-trihydroxytoluene (THT) oxygenase; This subfamily contains the ...
 20-139 4.65e-03

N-terminal domain of 2,4,5-trihydroxytoluene (THT) oxygenase; This subfamily contains the N-terminal, non-catalytic, domain of THT oxygenase. THT oxygenase is an extradiol dioxygenase in the 2,4-dinitrotoluene (DNT) degradation pathway. It catalyzes the conversion of 2,4,5-trihydroxytoluene to an unstable ring fission product, 2,4-dihydroxy-5-methyl-6-oxo-2,4-hexadienoic acid. The native protein was determined to be a dimer by gel filtration. The enzyme belongs to the type I family of extradiol dioxygenases which contains two structurally homologous barrel-shaped domains at the N- and C-terminus of each monomer. The active-site metal is located in the C-terminal barrel. Fe(II) is required for its catalytic activity.


Pssm-ID: 319928  Cd Length: 113  Bit Score: 36.10  E-value: 4.65e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682443  20 HVVYRVGDLDRTIEFYTEvFGMKLLRKRDipEEKYsnaFLGFGPETSNFVVELTYNygvssydigTGFGHFAISTQDVSK 99
Cdd:cd07267   6 HVVYEHPDLEKAERFLTD-FGLIVAYRTG--EEIY---YRGYGTDPYVYVARKSSR---------SRFLGAAFVAASRAD 70

                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 30682443 100 LVENVRAKGGnVTREPGPVKGGGSVIAFvKDPDGYTFELI 139
Cdd:cd07267  71 LEKAATLPGA-SPIEDLEAPGGGKVVTL-TDPDGFPVHLV 108
BLMA_like cd08349
Bleomycin binding protein (BLMA) and similar proteins; BLMA also called Bleomycin resistance ...
 22-134 5.15e-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: 36.05  E-value: 5.15e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682443  22 VYRVGDLDRTIEFYTEVFGMKLLRKRdiPEEKYsnAFLGFGPETSNFvveltynYGVSSYDIGTGFGHFAISTQDVSKLV 101
Cdd:cd08349   3 ILPVRDIDKTLAFYVDVLGFEVDYER--PPPGY--AILSRGGVELHL-------FEHPGLDPAGSGVAAYIRVEDIDALH 71

                        90       100       110
                ....*....|....*....|....*....|....*...
gi 30682443 102 ENVRAKGGNVTREP-----GPVKGGGSVIAfVKDPDGY 134
Cdd:cd08349  72 AELKAAGLPLFGIPritpiEDKPWGMREFA-VVDPDGN 108
VOC_like cd07262
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 18-133 7.49e-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: 319923 [Multi-domain]  Cd Length: 121  Bit Score: 35.67  E-value: 7.49e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682443  18 FLHVVYRVGDLDRTIEFYTEVF---GMKLLRKRDipeekysnAFLGFGPE-TSNFVVELTYNYGVSSydiGTGFGHFAIS 93
Cdd:cd07262   1 ISHVTIGVNDLERSRAFYDAALaplGYKRGFEDG--------GRVGYGLEgGPDFWVTEPFDGEPAT---AGNGTHVAFA 69

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
gi 30682443  94 TQDvSKLVENVRAK----GGNVTREPG--PVKGGGSVIAFVKDPDG 133
Cdd:cd07262  70 APS-RAAVDAFHAAalaaGGTDNGAPGlrPHYHPGYYAAYVRDPDG 114
VOC_like cd07251
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 151-267 9.67e-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: 35.35  E-value: 9.67e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682443 151 VMLRVGDLDRAIKFYEkALGMRLLRKIERPEYKYTIGmmgyaeeyeSIVLEL----TYNYDVTEYTKGNAYAQIAIGTdD 226
Cdd:cd07251   2 ITLGVRDLERSARFYE-ALGWKPNLDPNDGVVFFQLG---------GTVLALyprdALAEDAGVSVTGAGFSGVTLAH-N 70

                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
gi 30682443 227 VYKSGEVIKIVNQ--ELGGKITREAGPLPGLGTkIVSFLDPDG 267
Cdd:cd07251  71 VRSREEVDQLLAKavAAGGKILKPPQEVFWGGY-SGYFADPDG 112
PRK04101 PRK04101
metallothiol transferase FosB;
20-46 9.88e-03

metallothiol transferase FosB;


Pssm-ID: 179740  Cd Length: 139  Bit Score: 35.69  E-value: 9.88e-03
                         10        20
                 ....*....|....*....|....*..
gi 30682443   20 HVVYRVGDLDRTIEFYTEVFGMKLLRK 46
Cdd:PRK04101   7 HICFSVSNLEKSIEFYEKVLGAKLLVK 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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