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Conserved domains on  [gi|488139740|ref|WP_002210948|]
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lactoylglutathione lyase [Yersinia pestis]

Protein Classification

lactoylglutathione lyase( domain architecture ID 10794439)

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

EC:  4.4.1.5
Gene Ontology:  GO:0004462|GO:0046872
PubMed:  14641060

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
glyox_I TIGR00068
lactoylglutathione lyase; Lactoylglutathione lyase is also known as aldoketomutase and ...
 2-135 3.24e-85

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: 245.49  E-value: 3.24e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488139740    2 RLLHTMLRVGDLQRSIDFYTKVLGMRLLRTSENTEYKYSLAFVGYSDESKGSVIELTYNWGVDQYDMGTAFGHLALGVDD 81
Cdd:TIGR00068  17 RLLHTMLRVGDLDKSLDFYTEVLGMKLLRKRDFPEMKFSLAFLGYGDETSAAVIELTHNWGTEKYDLGNGFGHIAIGVDD 96

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 488139740   82 VAATCDQIRQAGGKVTREAGPVKGGNTIIAFVEDPDGYKIELIENKSAGDCLGN 135
Cdd:TIGR00068  97 VYKACERVRALGGNVVREPGPVKGGTTVIAFVEDPDGYKIELIQRKSTKDGLGN 150
 
Name Accession Description Interval E-value
glyox_I TIGR00068
lactoylglutathione lyase; Lactoylglutathione lyase is also known as aldoketomutase and ...
 2-135 3.24e-85

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: 245.49  E-value: 3.24e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488139740    2 RLLHTMLRVGDLQRSIDFYTKVLGMRLLRTSENTEYKYSLAFVGYSDESKGSVIELTYNWGVDQYDMGTAFGHLALGVDD 81
Cdd:TIGR00068  17 RLLHTMLRVGDLDKSLDFYTEVLGMKLLRKRDFPEMKFSLAFLGYGDETSAAVIELTHNWGTEKYDLGNGFGHIAIGVDD 96

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 488139740   82 VAATCDQIRQAGGKVTREAGPVKGGNTIIAFVEDPDGYKIELIENKSAGDCLGN 135
Cdd:TIGR00068  97 VYKACERVRALGGNVVREPGPVKGGTTVIAFVEDPDGYKIELIQRKSTKDGLGN 150
GlxI_Ni cd16358
Glyoxalase I that uses Ni(++) as cofactor; This family includes Escherichia coil and other ...
 3-124 1.58e-77

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: 224.97  E-value: 1.58e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488139740   3 LLHTMLRVGDLQRSIDFYTKVLGMRLLRTSENTEYKYSLAFVGYSDESKGSVIELTYNWGVDQYDMGTAFGHLALGVDDV 82
Cdd:cd16358    1 MLHTMLRVGDLDRSIKFYTEVLGMKLLRKRDYPEGKYTLAFVGYGDEDENTVLELTYNWGVDKYDLGTAYGHIAIGVEDV 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 488139740  83 AATCDQIRQAGGKVTREAGPVKGGNTIIAFVEDPDGYKIELI 124
Cdd:cd16358   81 YETCERIRKKGGKVTREPGPMKGGTTVIAFVEDPDGYKIELI 122
PRK10291 PRK10291
glyoxalase I; Provisional
 7-135 9.08e-70

glyoxalase I; Provisional


Pssm-ID: 182358  Cd Length: 129  Bit Score: 205.64  E-value: 9.08e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488139740   7 MLRVGDLQRSIDFYTKVLGMRLLRTSENTEYKYSLAFVGYSDESKGSVIELTYNWGVDQYDMGTAFGHLALGVDDVAATC 86
Cdd:PRK10291   1 MLRVGDLQRSIDFYTNVLGMKLLRTSENPEYKYSLAFVGYGPETEEAVIELTYNWGVDKYELGTAYGHIALSVDNAAEAC 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 488139740  87 DQIRQAGGKVTREAGPVKGGNTIIAFVEDPDGYKIELIENKSAGDCLGN 135
Cdd:PRK10291  81 EKIRQNGGNVTREAGPVKGGTTVIAFVEDPDGYKIELIEEKDAGRGLGN 129
GloA COG0346
Catechol 2,3-dioxygenase or related enzyme, vicinal oxygen chelate (VOC) family [Secondary ...
 1-129 1.77e-42

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: 136.28  E-value: 1.77e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488139740   1 MRLLHTMLRVGDLQRSIDFYTKVLGMRLLRTSENTEYKYSLAFVGYSDeskGSVIELTYNWGVDQYDMGTAFGHLALGVD 80
Cdd:COG0346    1 MGLHHVTLRVSDLEASLAFYTDVLGLELVKRTDFGDGGFGHAFLRLGD---GTELELFEAPGAAPAPGGGGLHHLAFRVD 77

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 488139740  81 DVAATCDQIRQAGGKVTREAGPVKGGNTiIAFVEDPDGYKIELIENKSA 129
Cdd:COG0346   78 DLDAAYARLRAAGVEIEGEPRDRAYGYR-SAYFRDPDGNLIELVEPPPG 125
Glyoxalase pfam00903
Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;
2-123 2.90e-31

Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;


Pssm-ID: 395724 [Multi-domain]  Cd Length: 121  Bit Score: 107.92  E-value: 2.90e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488139740    2 RLLHTMLRVGDLQRSIDFYTKVLGMRLLRTSENTEYKYSLAFVGYSDeskGSVIELTYNWGVDQYDMGTA---FGHLALG 78
Cdd:pfam00903   1 RIDHVALRVGDLEKSLDFYTDVLGFKLVEETDAGEEGGLRSAFFLAG---GRVLELLLNETPPPAAAGFGghhIAFIAFS 77

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 488139740   79 VDDVAATCDQIRQAGGKVTREAGPVKGGNTIIaFVEDPDGYKIEL 123
Cdd:pfam00903  78 VDDVDAAYDRLKAAGVEIVREPGRHGWGGRYS-YFRDPDGNLIEL 121
 
Name Accession Description Interval E-value
glyox_I TIGR00068
lactoylglutathione lyase; Lactoylglutathione lyase is also known as aldoketomutase and ...
 2-135 3.24e-85

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: 245.49  E-value: 3.24e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488139740    2 RLLHTMLRVGDLQRSIDFYTKVLGMRLLRTSENTEYKYSLAFVGYSDESKGSVIELTYNWGVDQYDMGTAFGHLALGVDD 81
Cdd:TIGR00068  17 RLLHTMLRVGDLDKSLDFYTEVLGMKLLRKRDFPEMKFSLAFLGYGDETSAAVIELTHNWGTEKYDLGNGFGHIAIGVDD 96

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 488139740   82 VAATCDQIRQAGGKVTREAGPVKGGNTIIAFVEDPDGYKIELIENKSAGDCLGN 135
Cdd:TIGR00068  97 VYKACERVRALGGNVVREPGPVKGGTTVIAFVEDPDGYKIELIQRKSTKDGLGN 150
GlxI_Ni cd16358
Glyoxalase I that uses Ni(++) as cofactor; This family includes Escherichia coil and other ...
 3-124 1.58e-77

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: 224.97  E-value: 1.58e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488139740   3 LLHTMLRVGDLQRSIDFYTKVLGMRLLRTSENTEYKYSLAFVGYSDESKGSVIELTYNWGVDQYDMGTAFGHLALGVDDV 82
Cdd:cd16358    1 MLHTMLRVGDLDRSIKFYTEVLGMKLLRKRDYPEGKYTLAFVGYGDEDENTVLELTYNWGVDKYDLGTAYGHIAIGVEDV 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 488139740  83 AATCDQIRQAGGKVTREAGPVKGGNTIIAFVEDPDGYKIELI 124
Cdd:cd16358   81 YETCERIRKKGGKVTREPGPMKGGTTVIAFVEDPDGYKIELI 122
PRK10291 PRK10291
glyoxalase I; Provisional
 7-135 9.08e-70

glyoxalase I; Provisional


Pssm-ID: 182358  Cd Length: 129  Bit Score: 205.64  E-value: 9.08e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488139740   7 MLRVGDLQRSIDFYTKVLGMRLLRTSENTEYKYSLAFVGYSDESKGSVIELTYNWGVDQYDMGTAFGHLALGVDDVAATC 86
Cdd:PRK10291   1 MLRVGDLQRSIDFYTNVLGMKLLRTSENPEYKYSLAFVGYGPETEEAVIELTYNWGVDKYELGTAYGHIALSVDNAAEAC 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 488139740  87 DQIRQAGGKVTREAGPVKGGNTIIAFVEDPDGYKIELIENKSAGDCLGN 135
Cdd:PRK10291  81 EKIRQNGGNVTREAGPVKGGTTVIAFVEDPDGYKIELIEEKDAGRGLGN 129
PLN02300 PLN02300
lactoylglutathione lyase
 2-127 3.39e-59

lactoylglutathione lyase


Pssm-ID: 215169 [Multi-domain]  Cd Length: 286  Bit Score: 184.21  E-value: 3.39e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488139740   2 RLLHTMLRVGDLQRSIDFYTKVLGMRLLRTSENTEYKYSLAFVGYSDESKGSVIELTYNWGVDQYDMGTAFGHLALGVDD 81
Cdd:PLN02300  24 RMLHVVYRVGDLDRTIKFYTECLGMKLLRKRDIPEEKYTNAFLGYGPEDSNFVVELTYNYGVDKYDIGTGFGHFGIAVED 103

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 488139740  82 VAATCDQIRQAGGKVTREAGPVKGGNTIIAFVEDPDGYKIELIENK 127
Cdd:PLN02300 104 VAKTVELVKAKGGKVTREPGPVKGGKSVIAFVKDPDGYKFELIQRG 149
PLN02300 PLN02300
lactoylglutathione lyase
 2-127 3.30e-47

lactoylglutathione lyase


Pssm-ID: 215169 [Multi-domain]  Cd Length: 286  Bit Score: 153.40  E-value: 3.30e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488139740   2 RLLHTMLRVGDLQRSIDFYTKVLGMRLLRTSENTEYKYSLAFVGYSDESKGSVIELTYNWGVDQYDMGTAFGHLALGVDD 81
Cdd:PLN02300 154 PLCQVMLRVGDLDRSIKFYEKAFGMKLLRKRDNPEYKYTIAMMGYGPEDKTTVLELTYNYGVTEYTKGNAYAQIAIGTDD 233

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 488139740  82 VAATCDQIRQAGGKVTREAGPVKGGNTIIAFVEDPDGYKIELIENK 127
Cdd:PLN02300 234 VYKTAEAIKLVGGKITREPGPLPGINTKITACLDPDGWKTVFVDNI 279
GloA COG0346
Catechol 2,3-dioxygenase or related enzyme, vicinal oxygen chelate (VOC) family [Secondary ...
 1-129 1.77e-42

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: 136.28  E-value: 1.77e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488139740   1 MRLLHTMLRVGDLQRSIDFYTKVLGMRLLRTSENTEYKYSLAFVGYSDeskGSVIELTYNWGVDQYDMGTAFGHLALGVD 80
Cdd:COG0346    1 MGLHHVTLRVSDLEASLAFYTDVLGLELVKRTDFGDGGFGHAFLRLGD---GTELELFEAPGAAPAPGGGGLHHLAFRVD 77

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 488139740  81 DVAATCDQIRQAGGKVTREAGPVKGGNTiIAFVEDPDGYKIELIENKSA 129
Cdd:COG0346   78 DLDAAYARLRAAGVEIEGEPRDRAYGYR-SAYFRDPDGNLIELVEPPPG 125
GlxI_Zn cd07233
Glyoxalase I that uses Zn(++) as cofactor; This family includes eukaryotic glyoxalase I that ...
 3-124 2.43e-37

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: 123.98  E-value: 2.43e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488139740   3 LLHTMLRVGDLQRSIDFYTKVLGMRLLRTSENTEYKYSLAFVGYSDE-------------SKGSVIELTYNWGVDQ---- 65
Cdd:cd07233    1 FNHTMLRVKDPKKSLKFYTEVLGMKLLRKKDFPEMKFSLYFLGYEDPkdipkdprtawvfSREGTLELTHNWGTENdedp 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488139740  66 -YDMGTA----FGHLALGVDDVAATCDQIRQAGGKVTR--EAGPVKGgntiIAFVEDPDGYKIELI 124
Cdd:cd07233   81 vYHNGNSdprgFGHIGIAVDDVYAACERFEELGVKFKKkpDDGKMKG----IAFIKDPDGYWIEIL 142
Glyoxalase pfam00903
Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;
2-123 2.90e-31

Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;


Pssm-ID: 395724 [Multi-domain]  Cd Length: 121  Bit Score: 107.92  E-value: 2.90e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488139740    2 RLLHTMLRVGDLQRSIDFYTKVLGMRLLRTSENTEYKYSLAFVGYSDeskGSVIELTYNWGVDQYDMGTA---FGHLALG 78
Cdd:pfam00903   1 RIDHVALRVGDLEKSLDFYTDVLGFKLVEETDAGEEGGLRSAFFLAG---GRVLELLLNETPPPAAAGFGghhIAFIAFS 77

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 488139740   79 VDDVAATCDQIRQAGGKVTREAGPVKGGNTIIaFVEDPDGYKIEL 123
Cdd:pfam00903  78 VDDVDAAYDRLKAAGVEIVREPGRHGWGGRYS-YFRDPDGNLIEL 121
PLN03042 PLN03042
Lactoylglutathione lyase; Provisional
 6-130 2.79e-29

Lactoylglutathione lyase; Provisional


Pssm-ID: 215548  Cd Length: 185  Bit Score: 104.90  E-value: 2.79e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488139740   6 TMLRVGDLQRSIDFYTKVLGMRLLRTSENTEYKYSLAFVGYSDES---------------KGSVIELTYNWGVDQ----- 65
Cdd:PLN03042  31 TMFRIKDPKASLDFYSRVLGMSLLKRLDFPEMKFSLYFLGYEDSEtaptdppertvwtfgRKATIELTHNWGTESdpefk 110

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488139740  66 -YDMGTA----FGHLALGVDDVAATCDQIRQAGgkVTREAGPVKGGNTIIAFVEDPDGYKIELIENKSAG 130
Cdd:PLN03042 111 gYHNGNSdprgFGHIGITVDDVYKACERFEKLG--VEFVKKPDDGKMKGLAFIKDPDGYWIEIFDLKRIG 178
PLN02367 PLN02367
lactoylglutathione lyase
 5-135 2.88e-28

lactoylglutathione lyase


Pssm-ID: 177995  Cd Length: 233  Bit Score: 103.54  E-value: 2.88e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488139740   5 HTMLRVGDLQRSIDFYTKVLGMRLLRTSENTEYKYSLAFVGYSDE---------------SKGSVIELTYNWGVDQ---- 65
Cdd:PLN02367  78 QTMYRIKDPKASLDFYSRVLGMSLLKRLDFPEMKFSLYFMGYEDTasaptdptertvwtfGQKATIELTHNWGTESdpdf 157

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488139740  66 --YDMGTA----FGHLALGVDDVAATCDQIRQAGGKVTR--EAGPVKGgntiIAFVEDPDGYKIELIENKSAGDCLGN 135
Cdd:PLN02367 158 kgYHNGNSeprgFGHIGITVDDVYKACERFEELGVEFVKkpNDGKMKG----IAFIKDPDGYWIEIFDLKTIGTTTVN 231
VOC cd06587
vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate (VOC) superfamily is composed ...
 5-123 1.74e-21

vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate (VOC) superfamily is composed of structurally related proteins with paired beta.alpha.beta.beta.beta motifs that provide a metal coordination environment with two or three open or readily accessible coordination sites to promote direct electrophilic participation of the metal ion in catalysis. VOC is found in a variety of structurally related metalloproteins, including the type I extradiol dioxygenases, glyoxalase I and a group of antibiotic resistance proteins. A bound metal ion is required for protein activities for the members of this superfamily. A variety of metal ions have been found in the catalytic centers of these proteins including Fe(II), Mn(II), Zn(II), Ni(II) and Mg(II). Type I extradiol dioxygenases catalyze the incorporation of both atoms of molecular oxygen into aromatic substrates, which results in the cleavage of aromatic rings. They are key enzymes in the degradation of aromatic compounds. Type I extradiol dioxygenases include class I and class II enzymes. Class I and II enzymes show sequence similarity; the two-domain class II enzymes evolved from a class I enzyme through gene duplication. Glyoxylase I catalyzes the glutathione-dependent inactivation of toxic methylglyoxal, requiring zinc or nickel ions for activity. The antibiotic resistance proteins in this family use a variety of mechanisms to block the function of antibiotics. Bleomycin resistance protein (BLMA) sequesters bleomycin's activity by directly binding to it. Whereas, three types of fosfomycin resistance proteins employ different mechanisms to render fosfomycin inactive by modifying the fosfomycin molecule. Although the proteins in this superfamily are functionally distinct, their structures are similar. The difference among the three dimensional structures of the three types of proteins in this superfamily is interesting from an evolutionary perspective. Both glyoxalase I and BLMA show domain swapping between subunits. However, there is no domain swapping for type 1 extradiol dioxygenases.


Pssm-ID: 319898 [Multi-domain]  Cd Length: 112  Bit Score: 82.57  E-value: 1.74e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488139740   5 HTMLRVGDLQRSIDFYTKVLGMRLLRTSENTEYkyslAFVGYSDeskGSVIELTYNWGVdQYDMGTAFGHLALGVDDVAA 84
Cdd:cd06587    1 HVALRVPDLDASVAFYEEVLGFEVVSRNEGGGF----AFLRLGP---GLRLALLEGPEP-ERPGGGGLFHLAFEVDDVDE 72

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 488139740  85 TCDQIRQAGGKVTREAGPV-KGGNTIIAFVEDPDGYKIEL 123
Cdd:cd06587   73 VDERLREAGAEGELVAPPVdDPWGGRSFYFRDPDGNLIEF 112
GLOD4_N cd08358
N-terminal domain of human glyoxalase domain-containing protein 4 and similar proteins; ...
 2-124 2.41e-21

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: 82.80  E-value: 2.41e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488139740   2 RLLHTMLRVGDLQRSIDFYTKVLGMRLLRTSE---------NTEY--KYSLAFVGYSDESKGSVIELTYNWGVDQYDMGT 70
Cdd:cd08358    2 RALHFVFKVGDRNKTIKFYREILGMKVLRHEEfeegckaacNGPYdgKWSKTMVGYGPEDDHFVVELTYNYGIGDYELGN 81

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 488139740  71 AFGHLALGVDDVAATCDQIRQaggkvtreagPVKGGNTIIAFVEDPDGYKIELI 124
Cdd:cd08358   82 DFLGITIHSKQAVSRAKKHNW----------PVTQVGDGVYEVKAPGGYKFYLI 125
VOC COG3324
Lactoylglutathione lyase-related enzyme, vicinal oxygen chelate (VOC) family [General function ...
 1-128 2.58e-18

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


Pssm-ID: 442553 [Multi-domain]  Cd Length: 119  Bit Score: 74.67  E-value: 2.58e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488139740   1 MRLLHTMLRVGDLQRSIDFYTKVLGMRLLRTSEnTEYKYSLAFVGysdesKGSVIELtynwGVDQYDMGTAFGHLALGVD 80
Cdd:COG3324    3 GTIVWVELPVDDLERAKAFYEEVFGWTFEDDAG-PGGDYAEFDTD-----GGQVGGL----MPGAEEPGGPGWLLYFAVD 72

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 488139740  81 DVAATCDQIRQAGGKVTREAGPVKGGNTiIAFVEDPDGYKIELIENKS 128
Cdd:COG3324   73 DLDAAVARVEAAGGTVLRPPTDIPPWGR-FAVFRDPEGNRFGLWQPAA 119
CatE COG2514
Catechol-2,3-dioxygenase [Secondary metabolites biosynthesis, transport and catabolism];
1-124 1.33e-13

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


Pssm-ID: 442004 [Multi-domain]  Cd Length: 141  Bit Score: 63.05  E-value: 1.33e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488139740   1 MRLLHTMLRVGDLQRSIDFYTKVLGMRLLRTSENTEYkysLAFVGysdesKGSVIELTYNWGVDQYDMGTAFGHLALGVD 80
Cdd:COG2514    2 TRLGHVTLRVRDLERSAAFYTDVLGLEVVEREGGRVY---LRADG-----GEHLLVLEEAPGAPPRPGAAGLDHVAFRVP 73

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 488139740  81 ---DVAATCDQIRQAGGKVTreaGPVKGGNTIIAFVEDPDGYKIELI 124
Cdd:COG2514   74 sraDLDAALARLAAAGVPVE---GAVDHGVGESLYFRDPDGNLIELY 117
VOC_like cd07264
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 3-125 1.75e-11

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


Pssm-ID: 319925 [Multi-domain]  Cd Length: 118  Bit Score: 56.96  E-value: 1.75e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488139740   3 LLHTMLRVGDLQRSIDFYTKVLGmrLLRTSENTEYKYSLAFVGysdeskGSVIELT-YNWG--VDQYDMGTAFGHLALGV 79
Cdd:cd07264    1 IAYIVLYVDDFAASLRFYRDVLG--LPPRFLHEEGEYAEFDTG------ETKLALFsRKEMarSGGPDRRGSAFELGFEV 72

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 488139740  80 DDVAATCDQIRQAGGKVTREAGPVKGGNTiIAFVEDPDGYKIELIE 125
Cdd:cd07264   73 DDVEATVEELVERGAEFVREPANKPWGQT-VAYVRDPDGNLIEICE 117
GLOD4_C cd16357
C-terminal domain of human glyoxalase domain-containing protein 4 and similar proteins; ...
 7-121 3.38e-09

C-terminal domain of human glyoxalase domain-containing protein 4 and similar proteins; Uncharacterized subfamily of the vicinal oxygen chelate (VOC) superfamily contains human glyoxalase domain-containing protein 4 and similar proteins. VOC is composed of structurally related proteins with paired beta.alpha.beta.beta.beta motifs that provide a metal coordination environment with two or three open or readily accessible coordination sites to promote direct electrophilic participation of the metal ion in catalysis. VOC domain is found in a variety of structurally related metalloproteins, including the bleomycin resistance protein, glyoxalase I, and type I ring-cleaving dioxygenases. A bound metal ion is required for protein activities for the members of this superfamily. A variety of metal ions have been found in the catalytic centers of these proteins including Fe(II), Mn(II), Zn(II), Ni(II) and Mg(II). The protein superfamily contains members with or without domain swapping. The proteins of this family share three conserved metal binding amino acids with the type I extradiol dioxygenases, which shows no domain swapping.


Pssm-ID: 319964  Cd Length: 114  Bit Score: 51.02  E-value: 3.38e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488139740   7 MLRVGDLQRSIDFYTKVLGMRLLRTSENTeykyslAFVGYSDESkgsvIELTYNWGVDQYDMGTAFGHLALGV--DDVAA 84
Cdd:cd16357    3 SLAVSDLEKSIDYWSDLLGMKVFEKSEKS------ALLGYGEDQ----AKLELVDIPEPVDHGTAFGRIAFSCpaDELPP 72

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 488139740  85 TCDQIRQAGGKVTREagPVK----GGNT----IIAfveDPDGYKI 121
Cdd:cd16357   73 IEEKVKAAGQTILTP--LVSldtpGKATvqvvILA---DPDGHEI 112
SgaA_N_like cd07247
N-terminal domain of Streptomyces griseus SgaA and similar domains; SgaA suppresses the growth ...
 10-125 5.32e-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: 50.34  E-value: 5.32e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488139740  10 VGDLQRSIDFYTKVLGMRLLRTSENT-EYkyslAFVGYSDESKGSVIELTYNWGvdqyDMGTAFgHLALGVDDVAATCDQ 88
Cdd:cd07247    8 TTDLERAKAFYGAVFGWTFEDEGDGGgDY----ALFTAGGGAVGGLMRAPEEVA----GAPPGW-LIYFAVDDLDAALAR 78

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 488139740  89 IRQAGGKVTREAGPVKGGNTiIAFVEDPDGYKIELIE 125
Cdd:cd07247   79 VEAAGGKVVVPPTDIPGGGR-FAVFADPEGNRFGLWS 114
PhnB COG2764
Zn-dependent glyoxalase, PhnB family [Energy production and conversion];
4-125 1.07e-08

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


Pssm-ID: 442048 [Multi-domain]  Cd Length: 118  Bit Score: 49.85  E-value: 1.07e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488139740   4 LHTMLRVGDLQRSIDFYTKVLGMRLLRTSENTEYKYSLAFVgysdESKGSVIELTYNWGVDQYDMGTAFgHLALGVDDVA 83
Cdd:COG2764    2 VTPYLVVDDAEEALEFYEDVFGFEVVFRMTDPDGKIMHAEL----RIGGSVLMLSDAPPDSPAAEGNGV-SLSLYVDDVD 76

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 488139740  84 ATCDQIRQAGGKVTREAGPVKGGNTiIAFVEDPDGYKIELIE 125
Cdd:COG2764   77 ALFARLVAAGATVVMPLQDTFWGDR-FGMVRDPFGVLWMINT 117
VOC_like cd07251
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 8-126 2.10e-08

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


Pssm-ID: 319914 [Multi-domain]  Cd Length: 120  Bit Score: 49.22  E-value: 2.10e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488139740   8 LRVGDLQRSIDFYTKvLGMRLLRTSENTeykyslaFVGYsdESKGSVIELtYNWG-----VDQYDMGTAFGHLALG---- 78
Cdd:cd07251    4 LGVRDLERSARFYEA-LGWKPNLDPNDG-------VVFF--QLGGTVLAL-YPRDalaedAGVSVTGAGFSGVTLAhnvr 72

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 488139740  79 -VDDVAATCDQIRQAGGKVTREAGPVKGGNTiIAFVEDPDGYKIELIEN 126
Cdd:cd07251   73 sREEVDQLLAKAVAAGGKILKPPQEVFWGGY-SGYFADPDGHIWEVAYN 120
COG3607 COG3607
Lactoylglutathione lyase-related enzyme, vicinal oxygen chelate (VOC) family [General function ...
 8-123 2.95e-08

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


Pssm-ID: 442825  Cd Length: 126  Bit Score: 48.67  E-value: 2.95e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488139740   8 LRVGDLQRSIDFYTKvLGMRLLRTSENTEykysLAFVGYSDeskGSVIELtynWGVDQY--DMG------TAFG--HLAL 77
Cdd:COG3607    9 LPVADLERSRAFYEA-LGFTFNPQFSDEG----AACFVLGE---GIVLML---LPREKFatFTGkpiadaTGFTevLLAL 77

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 488139740  78 GVD---DVAATCDQIRQAGGKVTREAGPVKGGNTiiAFVEDPDGYKIEL 123
Cdd:COG3607   78 NVEsreEVDALVAKALAAGGTVLKPPQDVGGMYS--GYFADPDGHLWEV 124
GLOD5 cd07253
Human glyoxalase domain-containing protein 5 and similar proteins; Uncharacterized subfamily ...
 2-123 4.81e-08

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: 47.99  E-value: 4.81e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488139740   2 RLLHTMLRVGDLQRSIDFYTKVLGMRLLRTSENteyKYSLAFvgysdeskGSV-IELtynwgvDQYDM--GTAFGHLALG 78
Cdd:cd07253    3 RLDHLVLTVKDIERTIDFYTKVLGMTVVTFKEG---RKALRF--------GNQkINL------HQKGKefEPKASAPTPG 65

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 488139740  79 VDD--------VAATCDQIRQAGgkVTREAGPVK--G--GNTIIAFVEDPDGYKIEL 123
Cdd:cd07253   66 SADlcfitetpIDEVLEHLEACG--VTIEEGPVKrtGalGPILSIYFRDPDGNLIEL 120
Glyoxalase_4 pfam13669
Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;
10-112 1.24e-07

Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;


Pssm-ID: 463951 [Multi-domain]  Cd Length: 109  Bit Score: 46.89  E-value: 1.24e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488139740   10 VGDLQRSIDFYTKVLGMRLLRT--SENTEYKYSLAFVGysdeSKGSVIELTYNWGVDQY--DMGTAFGHLALGVDDVAAT 85
Cdd:pfam13669   7 VPDLDRALALWGALLGLGPEGDyrSEPQNVDLAFALLG----DGPVEVELIQPLDGDSPlaRHGPGLHHLAYWVDDLDAA 82

                          90       100
                  ....*....|....*....|....*..
gi 488139740   86 CDQIRQAGGKVTREAGPVKGGNTIIAF 112
Cdd:pfam13669  83 VARLLDQGYRVAPKGPRAGAAGRRVAF 109
VOC_like cd07262
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 3-122 1.41e-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: 319923 [Multi-domain]  Cd Length: 121  Bit Score: 46.84  E-value: 1.41e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488139740   3 LLHTMLRVGDLQRSIDFYTKVLGmrllrTSENTEYKYSLAFVGYSDESKGSV-IELTYNwgvDQYDMGTAFGHLALgvdd 81
Cdd:cd07262    1 ISHVTIGVNDLERSRAFYDAALA-----PLGYKRGFEDGGRVGYGLEGGPDFwVTEPFD---GEPATAGNGTHVAF---- 68

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 488139740  82 VAATCDQIR-------QAGGKVTREAG--PVKGGNTIIAFVEDPDGYKIE 122
Cdd:cd07262   69 AAPSRAAVDafhaaalAAGGTDNGAPGlrPHYHPGYYAAYVRDPDGNKIE 118
ED_TypeI_classII_N cd16360
N-terminal domain of type I, class II extradiol dioxygenases; This family contains the ...
 5-124 1.62e-07

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: 46.54  E-value: 1.62e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488139740   5 HTMLRVGDLQRSIDFYTKVLGMRLLRTSENTEYkyslaFVGYSDEskgsvielTYNWGVDQYDmGTAFGHLALGV---DD 81
Cdd:cd16360    1 YAELGVPDLEKALEFYTDVLGLQVAKRDGNSVY-----LRGYEDE--------HHSLVLYEAP-EAGLKHFAFEVaseED 66

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 488139740  82 VAATCDQIRQAGGKVTR-EAGPVKGGNTIIAFvEDPDGYKIELI 124
Cdd:cd16360   67 LERAAASLTALGCDVTWgPDGEVPGGGKGFRF-QDPSGHLLELF 109
VOC_Bs_YwkD_like cd08352
vicinal oxygen chelate (VOC) family protein Bacillus subtilis YwkD and similar proteins; ...
 12-125 1.76e-07

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


Pssm-ID: 319940 [Multi-domain]  Cd Length: 123  Bit Score: 46.77  E-value: 1.76e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488139740  12 DLQRSIDFYTKVLGMRLLR---TSENTEYKYSLAFVGYSDE---SKGSVIELTYnwgvdqydmGTAFG--HLALGVDDVA 83
Cdd:cd08352   12 DYEKSKDFYVDKLGFEIIRehyRPERNDIKLDLALGGYQLElfiKPDAPARPSY---------PEALGlrHLAFKVEDVE 82

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 488139740  84 ATCDQIRQAGGKV--------TREAgpvkggntiIAFVEDPDGYKIELIE 125
Cdd:cd08352   83 ATVAELKSLGIETepirvddfTGKK---------FTFFFDPDGLPLELYE 123
FosA cd07244
fosfomycin resistant protein subfamily FosA; This subfamily family contains FosA, a fosfomycin ...
 5-123 2.88e-07

fosfomycin resistant protein subfamily FosA; This subfamily family contains FosA, a fosfomycin resistant protein. FosA is a Mn(II) and K(+)-dependent glutathione transferase. Fosfomycin inhibits the enzyme UDP-N-acetylglucosamine-3-enolpyruvyltransferase (MurA), which catalyzes the first committed step in bacterial cell wall biosynthesis. FosA, catalyzes the addition of glutathione to the antibiotic fosfomycin, (1R,2S)-epoxypropylphosphonic acid, making it inactive. FosA is a Mn(II) dependent enzyme. It is evolutionarily related to glyoxalase I and type I extradiol dioxygenases.


Pssm-ID: 319908 [Multi-domain]  Cd Length: 121  Bit Score: 46.12  E-value: 2.88e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488139740   5 HTMLRVGDLQRSIDFYTKVLGMRLLRTSEnteykyslafvgysdesKGSVIELTYNW---GVDQyDMGTA--FGHLALGV 79
Cdd:cd07244    4 HITLAVSDLERSLAFYVDLLGFKPHVRWD-----------------KGAYLTAGDLWlclSLDP-AAEPSpdYTHIAFTV 65

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 488139740  80 D--DVAATCDQIRQAGGKVTREAGpvKGGNTIiaFVEDPDGYKIEL 123
Cdd:cd07244   66 SeeDFEELSERLRAAGVKIWQENS--SEGDSL--YFLDPDGHKLEL 107
ED_TypeI_classII_C cd08343
C-terminal domain of type I, class II extradiol dioxygenases, catalytic domain; This family ...
 5-123 3.47e-07

C-terminal domain of type I, class II extradiol dioxygenases, catalytic domain; This family contains the C-terminal, 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: 319931  Cd Length: 132  Bit Score: 46.16  E-value: 3.47e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488139740   5 HTMLRVGDLQRSIDFYTKVLGMRL--------------LRTSENTEYkYSLAFVGYSdeskgsvieltynwgvdqydmGT 70
Cdd:cd08343    2 HVVLCSPDVEASRDFYTDVLGFRVsdrivdpgvdggafLHCDRGTDH-HTVALAGGP---------------------HP 59

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 488139740  71 AFGHLAL---GVDDVAATCDQIRQAGgkVTREAGPVK--GGNTIIAFVEDPDGYKIEL 123
Cdd:cd08343   60 GLHHVAFevhDLDDVGRGHDRLREKG--YKIEWGPGRhgLGSQVFDYWFDPSGNRVEY 115
MMCE cd07249
Methylmalonyl-CoA epimerase (MMCE); MMCE, also called methylmalonyl-CoA racemase (EC 5.1.99.1) ...
 10-125 3.70e-07

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: 46.03  E-value: 3.70e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488139740  10 VGDLQRSIDFYTKVLGMRLLRTSENTEYKYSLAFVGYSDeskgSVIEL------TYNWGVDQYDMGTAFGHLALGVDDVA 83
Cdd:cd07249    8 VPDLDEALKFYEDVLGVKVSEPEELEEQGVRVAFLELGN----TQIELleplgeDSPIAKFLDKKGGGLHHIAFEVDDID 83

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 488139740  84 ATCDQIRQAGGKVTREAGPVKGGNTIIAFVEDPDGYK--IELIE 125
Cdd:cd07249   84 AAVEELKAQGVRLLSEGPRIGAHGKRVAFLHPKDTGGvlIELVE 127
VOC_ShValD_like cd16361
vicinal oxygen chelate (VOC) family protein similar to Streptomyces hygroscopicus ValD protein; ...
 5-124 7.62e-07

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: 45.40  E-value: 7.62e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488139740   5 HTMLRVGDLQRSIDFYTKVLG----MRL----LRTSENTEYKYSLAFVGYSDESK-------GSVIELTYNWGVDQ---- 65
Cdd:cd16361    4 HVGITVPDLDAAVEFYTDVLGaevvYRStplaEGDRGGGEMRAAGFVPGFARARIamlrlgpGPGIELFEYKGPEQrapv 83

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488139740  66 ---YDMGTAfgHLALGVDDVAATCDQIRQAGGKV------TREAGPVKGGNTIiaFVEDPDGYKIELI 124
Cdd:cd16361   84 prnSDVGIF--HFALQVDDVEAAAERLAAAGGKVlmgpreIPDGGPGKGNRMV--YLRDPWGTLIELV 147
VOC_BsYqjT cd07242
vicinal oxygen chelate (VOC) family protein similar to Bacillus subtilis YqjT; The vicinal ...
 5-124 1.37e-06

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: 44.40  E-value: 1.37e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488139740   5 HTMLRVGDLQRSIDFYTKVLGMRLlrtsenTEY-KYSLAFVGYSDESKGSVIELTYNWGVDQYD-MGTAFGHLALGVDDV 82
Cdd:cd07242    4 HVELAVSDLHRSFKWFEWILGLGW------KEYdTWSFGPSWKLSGGSLLVVQQTDEFATPEFDrARVGLNHLAFHAESR 77

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 488139740  83 AATcDQIRQ----AGGKVT-REAGPVKGG-NTIIAFVEDPDGYKIELI 124
Cdd:cd07242   78 EAV-DELTEklakIGGVRTyGDRHPFAGGpPHYAAFCEDPDGIKLELV 124
metmalonyl_epim TIGR03081
methylmalonyl-CoA epimerase; Members of this protein family are the enzyme methylmalonyl-CoA ...
 2-125 1.25e-05

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


Pssm-ID: 213772 [Multi-domain]  Cd Length: 128  Bit Score: 41.93  E-value: 1.25e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488139740    2 RLLHTMLRVGDLQRSIDFYTKVLGMRLLRTSENTEYKYSLAFVGySDESKGSVIE-LTYNWGVDQYDMGTAFG--HLALG 78
Cdd:TIGR03081   1 RIDHVGIAVPDLEEAAKFYEDVLGAQVSEIEELPEQGVKVVFIA-LGNTKVELLEpLGEDSPIAKFLEKNGGGihHIAIE 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 488139740   79 VDDVAATCDQIRQAGGKVTREAGPVKGGNTIIAFV--EDPDGYKIELIE 125
Cdd:TIGR03081  80 VDDIEAALETLKEKGVRLIDEEPRIGAHGKPVAFLhpKSTGGVLIELEQ 128
Fosfomycin_RP cd08345
Fosfomycin resistant protein; This family contains three types of fosfomycin resistant protein. ...
 5-123 3.74e-05

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


Pssm-ID: 319933  Cd Length: 118  Bit Score: 40.23  E-value: 3.74e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488139740   5 HTMLRVGDLQRSIDFYTKVLGMRLLRTSENTEYKYS-LAF-------VGYSDESKgsVIELTYNwgvdqydmgtafgHLA 76
Cdd:cd08345    1 HITLIVRDLEKSTAFLQDIFGAREVYSSGDKTFSLSkEKFfllgglwIALMEGES--LQERSYT-------------HIA 65

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 488139740  77 LGVD--DVAATCDQIRQAGGKVTREAGPVKGGNTIIAFVeDPDGYKIEL 123
Cdd:cd08345   66 FQIQseDFDRYAERLGALGVEMRPPRPRVEGEGRSIYFY-DPDNHLFEL 113
VOC_BsCatE_like_N cd07255
N-terminal of Bacillus subtilis CatE like protein; Uncharacterized subfamily of VOC ...
 1-123 5.33e-05

N-terminal of Bacillus subtilis CatE like protein; Uncharacterized subfamily of VOC superfamily contains Bacillus subtilis CatE and similar proteins. CatE is proposed to function as Catechol-2,3-dioxygenase. VOC is composed of structurally related proteins with paired beta.alpha.beta.beta.beta motifs that provide a metal coordination environment with two or three open or readily accessible coordination sites to promote direct electrophilic participation of the metal ion in catalysis. VOC domain is found in a variety of structurally related metalloproteins, including the bleomycin resistance protein, glyoxalase I, and type I ring-cleaving dioxygenases. A bound metal ion is required for protein activities for the members of this superfamily. A variety of metal ions have been found in the catalytic centers of these proteins including Fe(II), Mn(II), Zn(II), Ni(II) and Mg(II). The protein superfamily contains members with or without domain swapping. The proteins of this family share three conserved metal binding amino acids with the type I extradiol dioxygenases, which shows no domain swapping.


Pssm-ID: 319918  Cd Length: 124  Bit Score: 39.99  E-value: 5.33e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488139740   1 MRLLHTMLRVGDLQRSIDFYTKVLGMRLLRTSENTEYkysLAFVGYSDEskgsvIELTYNWGVDQYDMGTAfG--HLALG 78
Cdd:cd07255    1 TRIGRVTLKVADLERQSAFYQNVIGLSVLKQNASRAY---LGVDGKQVL-----LVLEAIPDAVLAPRSTT-GlyHFAIL 71

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 488139740  79 VDDVAATCDQIRQAGgkvtrEAGPVKGG------NTIIAfvEDPDGYKIEL 123
Cdd:cd07255   72 LPDRKALGRALAHLA-----EHGPLIGAadhgvsEAIYL--SDPEGNGIEI 115
BphC5-RrK37_N_like cd08362
N-terminal, non-catalytic, domain of BphC5 (2,3-dihydroxybiphenyl 1,2-dioxygenase) from ...
 2-124 6.06e-05

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: 39.93  E-value: 6.06e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488139740   2 RLLHTMLRVGDLQRSIDFYTKVLGMRLLRTSENTEYkyslaFVGYSDESkgSVIELTYNwgvDQYDMgtafGHLALGVD- 80
Cdd:cd08362    3 HLRYVALGVPDLAAEREFYTEVWGLEEVAEDDDVVY-----LRAEGSEH--HVLRLRQS---DENRL----DLIAFAAAt 68

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 488139740  81 --DVAATCDQIRQAGGKVTREAGPVK--GGNTIIAFVeDPDGYKIELI 124
Cdd:cd08362   69 raDVDALAARLAAAGVRILSEPGPLDdpGGGYGFRFF-DPDGRTIEVS 115
HPCD_C_class_II cd07256
C-terminal domain of 3,4-dihydroxyphenylacetate 2,3-dioxygenase (HPCD); This subfamily ...
 1-123 1.05e-04

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


Pssm-ID: 319919  Cd Length: 160  Bit Score: 39.79  E-value: 1.05e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488139740   1 MRLLHTMLRVGDLQRSIDFYTKvLGMRLLRTSENTEYKYSLAFVgysdESKGSVIELTYNWGVdqydmGTAFGHLALGVD 80
Cdd:cd07256    2 LRIDHFNQRVPDVDAGLRYYED-LGFRVSEYTEDDDGETWAAWM----HRKGGVHDTALTNGN-----GPRLHHVAFWVP 71

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 488139740  81 D---VAATCDQIRQAGGKVTREAGPVKGG--NTIIAFVEDPDGYKIEL 123
Cdd:cd07256   72 EphnIIQTCDLMAAARYSDRIERGPGRHGvsNAFFLYILDPDGHRIEI 119
MhqB_like_C cd08360
C-terminal domain of Burkholderia sp. NF100 MhqB and similar proteins; This subfamily contains ...
 2-118 5.25e-04

C-terminal domain of Burkholderia sp. NF100 MhqB and similar proteins; This subfamily contains the C-terminal, catalytic, domain of Burkholderia sp. NF100 MhqB and similar proteins. MhqB is a type I extradiol dioxygenase involved in the catabolism of methylhydroquinone, an intermediate in the degradation of fenitrothion. The purified enzyme has shown extradiol ring cleavage activity toward 3-methylcatechol. Fe2+ was suggested as a cofactor, the same as most other enzymes in the family. Burkholderia sp. NF100 MhqB is encoded on the plasmid pNF1. The type I family of extradiol dioxygenases contains two structurally homologous barrel-shaped domains at the N- and C-terminal. The active-site metal is located in the C-terminal barrel and plays an essential role in the catalytic mechanism.


Pssm-ID: 319948  Cd Length: 134  Bit Score: 37.49  E-value: 5.25e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488139740   2 RLLHTMLRVGDLQRSIDFYTKVLGMRLlrtsenteykyslafvgySDESKGSVIELTYNWGVDQYDMG------TAFGHL 75
Cdd:cd08360    3 RLGHVLLFSPDVDRSVDFYRDLLGLKV------------------SDRSFDIIAFMRGAAGSDHHLIAfakssaTGLHHM 64

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 488139740  76 ALGVDDVaatcDQIRQaGGKVTREAGPVKG--------GNTIIAFVEDPDG 118
Cdd:cd08360   65 SWDVSDV----NEIGI-GASQLLRAGYKDGwglgrhvlGSNYFHYVRDPWG 110
PRK04101 PRK04101
metallothiol transferase FosB;
5-37 7.58e-04

metallothiol transferase FosB;


Pssm-ID: 179740  Cd Length: 139  Bit Score: 37.23  E-value: 7.58e-04
                         10        20        30
                 ....*....|....*....|....*....|...
gi 488139740   5 HTMLRVGDLQRSIDFYTKVLGMRLLRTSENTEY 37
Cdd:PRK04101   7 HICFSVSNLEKSIEFYEKVLGAKLLVKGRKTAY 39
BphC2-C3-RGP6_C_like cd08348
The single-domain 2,3-dihydroxybiphenyl 1,2-dioxygenases; This subfamily contains Rhodococcus ...
 2-123 1.31e-03

The single-domain 2,3-dihydroxybiphenyl 1,2-dioxygenases; This subfamily contains Rhodococcus globerulus P6 BphC2-RGP6 and BphC3-RGP6, and similar proteins. BphC catalyzes the extradiol ring cleavage reaction of 2,3-dihydroxybiphenyl, yielding 2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoic acid. This is the third step in the polychlorinated biphenyls (PCBs) degradation pathway (bph pathway). This subfamily of BphCs belongs to the type I extradiol dioxygenase family, which require a metal in the active site in its catalytic mechanism. Most type I extradiol dioxygenases are activated by Fe(II). Polychlorinated biphenyl degrading bacteria demonstrate a multiplicity of BphCs. For example, three types of BphC enzymes have been found in Rhodococcus globerulus (BphC1-RGP6 - BphC3-RGP6), all three enzymes are type I extradiol dioxygenases. BphC2-RGP6 and BphC3-RGP6 are one-domain dioxygenases, which form hexamers. BphC1-RGP6 has an internal duplication, it is a two-domain dioxygenase which forms octamers, its two domains do not belong to this subfamily.


Pssm-ID: 319936  Cd Length: 137  Bit Score: 36.34  E-value: 1.31e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488139740   2 RLLHTMLRVGD--LQRSIDFYTKVLGMRLlrTSENTeykySLAFVGYSDESKGSVIELTYNWGVDQYDMGTA--FGHLAL 77
Cdd:cd08348    1 KLAHFVLRTNPekFEAMVQWYLDILGARI--VARNA----KGCFLSFDEEHHRIAIFGAPGGAQPPDKRPTRvgLAHIAF 74

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 488139740  78 ---GVDDVAATCDQIRQAGGKVtreAGPVKGGNTIIAFVEDPDGYKIEL 123
Cdd:cd08348   75 tyaSLDDLARNYAQLKERGIKP---VWPVNHGVTTSIYYRDPDGNMLEM 120
PcpA_N_like cd08346
N-terminal domain of Sphingobium chlorophenolicum 2,6-dichloro-p-hydroquinone 1,2-dioxygenase ...
 5-34 1.68e-03

N-terminal domain of Sphingobium chlorophenolicum 2,6-dichloro-p-hydroquinone 1,2-dioxygenase (PcpA), and similar proteins; The N-terminal domain of Sphingobium chlorophenolicum (formerly Sphingomonas chlorophenolica) 2,6-dichloro-p-hydroquinone1,2-dioxygenase (PcpA), and similar proteins. PcpA is a key enzyme in the pentachlorophenol (PCP) degradation pathway, catalyzing the conversion of 2,6-dichloro-p-hydroquinone to 2-chloromaleylacetate. This domain belongs to a conserved domain superfamily that is found in a variety of structurally related metalloproteins, including the bleomycin resistance protein, glyoxalase I, and type I ring-cleaving dioxygenases.


Pssm-ID: 319934  Cd Length: 124  Bit Score: 36.11  E-value: 1.68e-03
                         10        20        30
                 ....*....|....*....|....*....|
gi 488139740   5 HTMLRVGDLQRSIDFYTKVLGMRLLRTSEN 34
Cdd:cd08346    4 HITAITGDAQENVDFYVKVLGLRLVKKTVN 33
HPCD_N_class_II cd07266
N-terminal domain of 3,4-dihydroxyphenylacetate 2,3-dioxygenase (HPCD); This subfamily ...
 1-123 4.59e-03

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


Pssm-ID: 319927  Cd Length: 118  Bit Score: 34.69  E-value: 4.59e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488139740   1 MRLLHTMLRVGDLQRSIDFYTKVLGMRLLRTSENTEYKYSLafvgysDESKGSVIELTYNwgvdqydMGTAFGHLALGV- 79
Cdd:cd07266    3 IRLAHAELVVTDLAASREFYVDTLGLHVTDEDDNAIYLRGV------EEFIHHTLVLRKA-------PEAAVGHLGFRVr 69

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 488139740  80 --DDVAATCDQIRQAGGKVTREAGPVKGgntIIAFVEDPDGYKIEL 123
Cdd:cd07266   70 deADLDKAAAFYKELGLPTEWREEPGQG---RTLRVEDPFGFPIEF 112
2_3_CTD_N cd07265
N-terminal domain of catechol 2,3-dioxygenase; This subfamily contains the N-terminal, ...
 1-55 4.60e-03

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


Pssm-ID: 319926  Cd Length: 122  Bit Score: 34.63  E-value: 4.60e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 488139740   1 MRLLHTMLRVGDLQRSIDFYTKVLGMR-LLRTSENTEYkyslaFVGYSDESKGSVI 55
Cdd:cd07265    3 LRPGHVQLRVLDLEEAIKHYREVLGLVeTGRDDQGRVY-----LKAWDEYDHHSII 53
 
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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