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Conserved domains on  [gi|447165255|ref|WP_001242511|]
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MULTISPECIES: lactoylglutathione lyase [Acinetobacter]

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 ...
 2-125 1.11e-81

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: 236.63  E-value: 1.11e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447165255    2 RMLHTMLRVGNLEQSLKFYTEVLGMKLLRKRDYEEGRFTLAFVGYGDEENNTVLELTHNWDTSSYDLGNGYGHIAIGVED 81
Cdd:TIGR00068  17 RLLHTMLRVGDLDKSLDFYTEVLGMKLLRKRDFPEMKFSLAFLGYGDETSAAVIELTHNWGTEKYDLGNGFGHIAIGVDD 96

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 447165255   82 AYKACEEIKARGGKVVREAGPMKGGVTVIAFVEDPDGYKVELIQ 125
Cdd:TIGR00068  97 VYKACERVRALGGNVVREPGPVKGGTTVIAFVEDPDGYKIELIQ 140
 
Name Accession Description Interval E-value
glyox_I TIGR00068
lactoylglutathione lyase; Lactoylglutathione lyase is also known as aldoketomutase and ...
 2-125 1.11e-81

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: 236.63  E-value: 1.11e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447165255    2 RMLHTMLRVGNLEQSLKFYTEVLGMKLLRKRDYEEGRFTLAFVGYGDEENNTVLELTHNWDTSSYDLGNGYGHIAIGVED 81
Cdd:TIGR00068  17 RLLHTMLRVGDLDKSLDFYTEVLGMKLLRKRDFPEMKFSLAFLGYGDETSAAVIELTHNWGTEKYDLGNGFGHIAIGVDD 96

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 447165255   82 AYKACEEIKARGGKVVREAGPMKGGVTVIAFVEDPDGYKVELIQ 125
Cdd:TIGR00068  97 VYKACERVRALGGNVVREPGPVKGGTTVIAFVEDPDGYKIELIQ 140
GlxI_Ni cd16358
Glyoxalase I that uses Ni(++) as cofactor; This family includes Escherichia coil and other ...
 3-124 5.24e-80

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: 231.13  E-value: 5.24e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447165255   3 MLHTMLRVGNLEQSLKFYTEVLGMKLLRKRDYEEGRFTLAFVGYGDEENNTVLELTHNWDTSSYDLGNGYGHIAIGVEDA 82
Cdd:cd16358    1 MLHTMLRVGDLDRSIKFYTEVLGMKLLRKRDYPEGKYTLAFVGYGDEDENTVLELTYNWGVDKYDLGTAYGHIAIGVEDV 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 447165255  83 YKACEEIKARGGKVVREAGPMKGGVTVIAFVEDPDGYKVELI 124
Cdd:cd16358   81 YETCERIRKKGGKVTREPGPMKGGTTVIAFVEDPDGYKIELI 122
PLN02300 PLN02300
lactoylglutathione lyase
 2-126 9.64e-62

lactoylglutathione lyase


Pssm-ID: 215169 [Multi-domain]  Cd Length: 286  Bit Score: 190.76  E-value: 9.64e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447165255   2 RMLHTMLRVGNLEQSLKFYTEVLGMKLLRKRDYEEGRFTLAFVGYGDEENNTVLELTHNWDTSSYDLGNGYGHIAIGVED 81
Cdd:PLN02300  24 RMLHVVYRVGDLDRTIKFYTECLGMKLLRKRDIPEEKYTNAFLGYGPEDSNFVVELTYNYGVDKYDIGTGFGHFGIAVED 103

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 447165255  82 AYKACEEIKARGGKVVREAGPMKGGVTVIAFVEDPDGYKVELIQQ 126
Cdd:PLN02300 104 VAKTVELVKAKGGKVTREPGPVKGGKSVIAFVKDPDGYKFELIQR 148
GloA COG0346
Catechol 2,3-dioxygenase or related enzyme, vicinal oxygen chelate (VOC) family [Secondary ...
 1-129 5.41e-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: 135.12  E-value: 5.41e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447165255   1 MRMLHTMLRVGNLEQSLKFYTEVLGMKLLRKRDYEEGRFTLAFVGYGDeenNTVLELTHNWDTSSYDLGNGYGHIAIGVE 80
Cdd:COG0346    1 MGLHHVTLRVSDLEASLAFYTDVLGLELVKRTDFGDGGFGHAFLRLGD---GTELELFEAPGAAPAPGGGGLHHLAFRVD 77

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 447165255  81 DAYKACEEIKARGGKVVREAGPMKGGVTViAFVEDPDGYKVELIQQDAN 129
Cdd:COG0346   78 DLDAAYARLRAAGVEIEGEPRDRAYGYRS-AYFRDPDGNLIELVEPPPG 125
Glyoxalase pfam00903
Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;
2-123 1.01e-30

Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;


Pssm-ID: 395724 [Multi-domain]  Cd Length: 121  Bit Score: 106.38  E-value: 1.01e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447165255    2 RMLHTMLRVGNLEQSLKFYTEVLGMKLLRKRDYEEGRFTLAFVGYGDEennTVLELTHNWDTSSYDLG---NGYGHIAIG 78
Cdd:pfam00903   1 RIDHVALRVGDLEKSLDFYTDVLGFKLVEETDAGEEGGLRSAFFLAGG---RVLELLLNETPPPAAAGfggHHIAFIAFS 77

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 447165255   79 VEDAYKACEEIKARGGKVVREAGPMKGGVTVIaFVEDPDGYKVEL 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 ...
 2-125 1.11e-81

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: 236.63  E-value: 1.11e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447165255    2 RMLHTMLRVGNLEQSLKFYTEVLGMKLLRKRDYEEGRFTLAFVGYGDEENNTVLELTHNWDTSSYDLGNGYGHIAIGVED 81
Cdd:TIGR00068  17 RLLHTMLRVGDLDKSLDFYTEVLGMKLLRKRDFPEMKFSLAFLGYGDETSAAVIELTHNWGTEKYDLGNGFGHIAIGVDD 96

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 447165255   82 AYKACEEIKARGGKVVREAGPMKGGVTVIAFVEDPDGYKVELIQ 125
Cdd:TIGR00068  97 VYKACERVRALGGNVVREPGPVKGGTTVIAFVEDPDGYKIELIQ 140
GlxI_Ni cd16358
Glyoxalase I that uses Ni(++) as cofactor; This family includes Escherichia coil and other ...
 3-124 5.24e-80

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: 231.13  E-value: 5.24e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447165255   3 MLHTMLRVGNLEQSLKFYTEVLGMKLLRKRDYEEGRFTLAFVGYGDEENNTVLELTHNWDTSSYDLGNGYGHIAIGVEDA 82
Cdd:cd16358    1 MLHTMLRVGDLDRSIKFYTEVLGMKLLRKRDYPEGKYTLAFVGYGDEDENTVLELTYNWGVDKYDLGTAYGHIAIGVEDV 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 447165255  83 YKACEEIKARGGKVVREAGPMKGGVTVIAFVEDPDGYKVELI 124
Cdd:cd16358   81 YETCERIRKKGGKVTREPGPMKGGTTVIAFVEDPDGYKIELI 122
PLN02300 PLN02300
lactoylglutathione lyase
 2-126 9.64e-62

lactoylglutathione lyase


Pssm-ID: 215169 [Multi-domain]  Cd Length: 286  Bit Score: 190.76  E-value: 9.64e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447165255   2 RMLHTMLRVGNLEQSLKFYTEVLGMKLLRKRDYEEGRFTLAFVGYGDEENNTVLELTHNWDTSSYDLGNGYGHIAIGVED 81
Cdd:PLN02300  24 RMLHVVYRVGDLDRTIKFYTECLGMKLLRKRDIPEEKYTNAFLGYGPEDSNFVVELTYNYGVDKYDIGTGFGHFGIAVED 103

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 447165255  82 AYKACEEIKARGGKVVREAGPMKGGVTVIAFVEDPDGYKVELIQQ 126
Cdd:PLN02300 104 VAKTVELVKAKGGKVTREPGPVKGGKSVIAFVKDPDGYKFELIQR 148
PRK10291 PRK10291
glyoxalase I; Provisional
 7-131 1.60e-50

glyoxalase I; Provisional


Pssm-ID: 182358  Cd Length: 129  Bit Score: 157.11  E-value: 1.60e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447165255   7 MLRVGNLEQSLKFYTEVLGMKLLRKRDYEEGRFTLAFVGYGDEENNTVLELTHNWDTSSYDLGNGYGHIAIGVEDAYKAC 86
Cdd:PRK10291   1 MLRVGDLQRSIDFYTNVLGMKLLRTSENPEYKYSLAFVGYGPETEEAVIELTYNWGVDKYELGTAYGHIALSVDNAAEAC 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 447165255  87 EEIKARGGKVVREAGPMKGGVTVIAFVEDPDGYKVELIQQDANAR 131
Cdd:PRK10291  81 EKIRQNGGNVTREAGPVKGGTTVIAFVEDPDGYKIELIEEKDAGR 125
GlxI_Zn cd07233
Glyoxalase I that uses Zn(++) as cofactor; This family includes eukaryotic glyoxalase I that ...
 3-124 5.02e-48

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: 150.94  E-value: 5.02e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447165255   3 MLHTMLRVGNLEQSLKFYTEVLGMKLLRKRDYEEGRFTLAFVGYGDEEN-------------NTVLELTHNW-----DTS 64
Cdd:cd07233    1 FNHTMLRVKDPKKSLKFYTEVLGMKLLRKKDFPEMKFSLYFLGYEDPKDipkdprtawvfsrEGTLELTHNWgtendEDP 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 447165255  65 SYDLGN----GYGHIAIGVEDAYKACEEIKARGGKVVR--EAGPMKGgvtvIAFVEDPDGYKVELI 124
Cdd:cd07233   81 VYHNGNsdprGFGHIGIAVDDVYAACERFEELGVKFKKkpDDGKMKG----IAFIKDPDGYWIEIL 142
PLN02300 PLN02300
lactoylglutathione lyase
 7-124 2.66e-43

lactoylglutathione lyase


Pssm-ID: 215169 [Multi-domain]  Cd Length: 286  Bit Score: 143.38  E-value: 2.66e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447165255   7 MLRVGNLEQSLKFYTEVLGMKLLRKRDYEEGRFTLAFVGYGDEENNTVLELTHNWDTSSYDLGNGYGHIAIGVEDAYKAC 86
Cdd:PLN02300 159 MLRVGDLDRSIKFYEKAFGMKLLRKRDNPEYKYTIAMMGYGPEDKTTVLELTYNYGVTEYTKGNAYAQIAIGTDDVYKTA 238

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 447165255  87 EEIKARGGKVVREAGPMKGGVTVIAFVEDPDGYKVELI 124
Cdd:PLN02300 239 EAIKLVGGKITREPGPLPGINTKITACLDPDGWKTVFV 276
GloA COG0346
Catechol 2,3-dioxygenase or related enzyme, vicinal oxygen chelate (VOC) family [Secondary ...
 1-129 5.41e-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: 135.12  E-value: 5.41e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447165255   1 MRMLHTMLRVGNLEQSLKFYTEVLGMKLLRKRDYEEGRFTLAFVGYGDeenNTVLELTHNWDTSSYDLGNGYGHIAIGVE 80
Cdd:COG0346    1 MGLHHVTLRVSDLEASLAFYTDVLGLELVKRTDFGDGGFGHAFLRLGD---GTELELFEAPGAAPAPGGGGLHHLAFRVD 77

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 447165255  81 DAYKACEEIKARGGKVVREAGPMKGGVTViAFVEDPDGYKVELIQQDAN 129
Cdd:COG0346   78 DLDAAYARLRAAGVEIEGEPRDRAYGYRS-AYFRDPDGNLIELVEPPPG 125
PLN03042 PLN03042
Lactoylglutathione lyase; Provisional
 3-127 6.51e-35

Lactoylglutathione lyase; Provisional


Pssm-ID: 215548  Cd Length: 185  Bit Score: 119.15  E-value: 6.51e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447165255   3 MLHTMLRVGNLEQSLKFYTEVLGMKLLRKRDYEEGRFTLAFVGYGDEEN-------NTV--------LELTHNWDTSS-- 65
Cdd:PLN03042  28 MQQTMFRIKDPKASLDFYSRVLGMSLLKRLDFPEMKFSLYFLGYEDSETaptdppeRTVwtfgrkatIELTHNWGTESdp 107

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 447165255  66 ----YDLGN----GYGHIAIGVEDAYKACEEIKARGGKVVR--EAGPMKGgvtvIAFVEDPDGYKVELIQQD 127
Cdd:PLN03042 108 efkgYHNGNsdprGFGHIGITVDDVYKACERFEKLGVEFVKkpDDGKMKG----LAFIKDPDGYWIEIFDLK 175
PLN02367 PLN02367
lactoylglutathione lyase
 3-123 5.51e-34

lactoylglutathione lyase


Pssm-ID: 177995  Cd Length: 233  Bit Score: 118.18  E-value: 5.51e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447165255   3 MLHTMLRVGNLEQSLKFYTEVLGMKLLRKRDYEEGRFTLAFVGY-------GDEENNTV--------LELTHNWDTSS-- 65
Cdd:PLN02367  76 MQQTMYRIKDPKASLDFYSRVLGMSLLKRLDFPEMKFSLYFMGYedtasapTDPTERTVwtfgqkatIELTHNWGTESdp 155

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 447165255  66 ----YDLGN----GYGHIAIGVEDAYKACEEIKARGGKVVR--EAGPMKGgvtvIAFVEDPDGYKVEL 123
Cdd:PLN02367 156 dfkgYHNGNseprGFGHIGITVDDVYKACERFEELGVEFVKkpNDGKMKG----IAFIKDPDGYWIEI 219
Glyoxalase pfam00903
Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;
2-123 1.01e-30

Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;


Pssm-ID: 395724 [Multi-domain]  Cd Length: 121  Bit Score: 106.38  E-value: 1.01e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447165255    2 RMLHTMLRVGNLEQSLKFYTEVLGMKLLRKRDYEEGRFTLAFVGYGDEennTVLELTHNWDTSSYDLG---NGYGHIAIG 78
Cdd:pfam00903   1 RIDHVALRVGDLEKSLDFYTDVLGFKLVEETDAGEEGGLRSAFFLAGG---RVLELLLNETPPPAAAGfggHHIAFIAFS 77

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 447165255   79 VEDAYKACEEIKARGGKVVREAGPMKGGVTVIaFVEDPDGYKVEL 123
Cdd:pfam00903  78 VDDVDAAYDRLKAAGVEIVREPGRHGWGGRYS-YFRDPDGNLIEL 121
GLOD4_N cd08358
N-terminal domain of human glyoxalase domain-containing protein 4 and similar proteins; ...
 2-126 4.06e-26

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: 94.74  E-value: 4.06e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447165255   2 RMLHTMLRVGNLEQSLKFYTEVLGMKLLRKRDYEEG-----------RFTLAFVGYGDEENNTVLELTHNWDTSSYDLGN 70
Cdd:cd08358    2 RALHFVFKVGDRNKTIKFYREILGMKVLRHEEFEEGckaacngpydgKWSKTMVGYGPEDDHFVVELTYNYGIGDYELGN 81

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 447165255  71 GYGHIAIGVEDAYKACEEIKArggkvvreagPMKGGVTVIAFVEDPDGYKVELIQQ 126
Cdd:cd08358   82 DFLGITIHSKQAVSRAKKHNW----------PVTQVGDGVYEVKAPGGYKFYLIDK 127
VOC cd06587
vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate (VOC) superfamily is composed ...
 5-123 1.17e-20

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


Pssm-ID: 319898 [Multi-domain]  Cd Length: 112  Bit Score: 80.65  E-value: 1.17e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447165255   5 HTMLRVGNLEQSLKFYTEVLGMKLLRKRDyeegRFTLAFVGYGDeenNTVLELTHnWDTSSYDLGNGYGHIAIGVEDAYK 84
Cdd:cd06587    1 HVALRVPDLDASVAFYEEVLGFEVVSRNE----GGGFAFLRLGP---GLRLALLE-GPEPERPGGGGLFHLAFEVDDVDE 72

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 447165255  85 ACEEIKARGGKVVREAGPM-KGGVTVIAFVEDPDGYKVEL 123
Cdd:cd06587   73 VDERLREAGAEGELVAPPVdDPWGGRSFYFRDPDGNLIEF 112
VOC COG3324
Lactoylglutathione lyase-related enzyme, vicinal oxygen chelate (VOC) family [General function ...
 1-128 4.02e-16

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


Pssm-ID: 442553 [Multi-domain]  Cd Length: 119  Bit Score: 68.89  E-value: 4.02e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447165255   1 MRMLHTMLRVGNLEQSLKFYTEVLGMKLLRKRDyEEGRFTLAFVGYGDeenntVLELTHNWDTSsydlGNGYGHIAIGVE 80
Cdd:COG3324    3 GTIVWVELPVDDLERAKAFYEEVFGWTFEDDAG-PGGDYAEFDTDGGQ-----VGGLMPGAEEP----GGPGWLLYFAVD 72

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 447165255  81 DAYKACEEIKARGGKVVREAGPMKGGVTvIAFVEDPDGYKVELIQQDA 128
Cdd:COG3324   73 DLDAAVARVEAAGGTVLRPPTDIPPWGR-FAVFRDPEGNRFGLWQPAA 119
CatE COG2514
Catechol-2,3-dioxygenase [Secondary metabolites biosynthesis, transport and catabolism];
1-124 2.31e-15

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


Pssm-ID: 442004 [Multi-domain]  Cd Length: 141  Bit Score: 67.68  E-value: 2.31e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447165255   1 MRMLHTMLRVGNLEQSLKFYTEVLGMKLLRKrdyEEGRFTLAFVGygdeeNNTVLELTHNWDTSSYDLGNGYGHIAIGVE 80
Cdd:COG2514    2 TRLGHVTLRVRDLERSAAFYTDVLGLEVVER---EGGRVYLRADG-----GEHLLVLEEAPGAPPRPGAAGLDHVAFRVP 73

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 447165255  81 DAY---KACEEIKARGgkvVREAGPMKGGVTVIAFVEDPDGYKVELI 124
Cdd:COG2514   74 SRAdldAALARLAAAG---VPVEGAVDHGVGESLYFRDPDGNLIELY 117
VOC_like cd07264
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 3-123 2.12e-13

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


Pssm-ID: 319925 [Multi-domain]  Cd Length: 118  Bit Score: 61.96  E-value: 2.12e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447165255   3 MLHTMLRVGNLEQSLKFYTEVLGmkLLRKRDYEEGRFTLAFVGygdeenNTVLEL----THNWDTSSyDLGNGYGHIAIG 78
Cdd:cd07264    1 IAYIVLYVDDFAASLRFYRDVLG--LPPRFLHEEGEYAEFDTG------ETKLALfsrkEMARSGGP-DRRGSAFELGFE 71

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 447165255  79 VEDAYKACEEIKARGGKVVREAGPMKGGVTViAFVEDPDGYKVEL 123
Cdd:cd07264   72 VDDVEATVEELVERGAEFVREPANKPWGQTV-AYVRDPDGNLIEI 115
PhnB COG2764
Zn-dependent glyoxalase, PhnB family [Energy production and conversion];
4-125 1.94e-12

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


Pssm-ID: 442048 [Multi-domain]  Cd Length: 118  Bit Score: 59.48  E-value: 1.94e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447165255   4 LHTMLRVGNLEQSLKFYTEVLGMKLLRKRDYEEGRFTLAFVGYGDeennTVLELTHNWDTSSYDLGNGYgHIAIGVEDAY 83
Cdd:COG2764    2 VTPYLVVDDAEEALEFYEDVFGFEVVFRMTDPDGKIMHAELRIGG----SVLMLSDAPPDSPAAEGNGV-SLSLYVDDVD 76

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 447165255  84 KACEEIKARGGKVVREAGPMKGGVTViAFVEDPDGYKVELIQ 125
Cdd:COG2764   77 ALFARLVAAGATVVMPLQDTFWGDRF-GMVRDPFGVLWMINT 117
GLOD4_C cd16357
C-terminal domain of human glyoxalase domain-containing protein 4 and similar proteins; ...
 7-119 7.47e-12

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: 57.95  E-value: 7.47e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447165255   7 MLRVGNLEQSLKFYTEVLGMKLLRKrdyEEGRFTLafvGYGDEEnnTVLELThnwDT-SSYDLGNGYGHIAIGVEDAYKA 85
Cdd:cd16357    3 SLAVSDLEKSIDYWSDLLGMKVFEK---SEKSALL---GYGEDQ--AKLELV---DIpEPVDHGTAFGRIAFSCPADELP 71

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 447165255  86 C--EEIKARGGKVVREA----GPMKGGVTVIaFVEDPDGY 119
Cdd:cd16357   72 PieEKVKAAGQTILTPLvsldTPGKATVQVV-ILADPDGH 110
VOC_like cd07245
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 5-123 1.92e-10

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


Pssm-ID: 319909 [Multi-domain]  Cd Length: 117  Bit Score: 54.25  E-value: 1.92e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447165255   5 HTMLRVGNLEQSLKFYTEVLGMKLLRKRdyEEGRFTLAFVGYGDEENNTVLELTHNWDTSSYDLGNGYGHIAIGVEDAYK 84
Cdd:cd07245    3 HVALACPDLERARRFYTDVLGLEEVPRP--PFLKFGGAWLYLGGGQQIHLVVEQNPSELPRPEHPGRDRHPSFSVPDLDA 80

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 447165255  85 ACEEIKARGGKVVREAGPmKGGVTVIaFVEDPDGYKVEL 123
Cdd:cd07245   81 LKQRLKEAGIPYTESTSP-GGGVTQL-FFRDPDGNRLEF 117
VOC_like cd07263
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 5-125 1.05e-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: 319924 [Multi-domain]  Cd Length: 120  Bit Score: 52.30  E-value: 1.05e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447165255   5 HTMLRVGNLEQSLKFYTEVLGMKLLRKRDYEEGRFtLAFVGYGDEENNTVLELThNWD---TSSYDLGNGYGHIAIGVED 81
Cdd:cd07263    1 QVMLYVDDQDKALDFYVEKLGFEVVEDVPMGGMRW-VTVAPPGSPGTSLLLEPK-AHPaqmPQSPEAAGGTPGILLATDD 78

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 447165255  82 AYKACEEIKARGGKVVREAGPMkGGVTVIAFvEDPDGYKVELIQ 125
Cdd:cd07263   79 IDATYERLTAAGVTFVQEPTQM-GGGRVANF-RDPDGNLFALME 120
MMCE cd07249
Methylmalonyl-CoA epimerase (MMCE); MMCE, also called methylmalonyl-CoA racemase (EC 5.1.99.1) ...
 10-125 3.43e-09

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: 51.04  E-value: 3.43e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447165255  10 VGNLEQSLKFYTEVLGMKLLRKRDYEEGRFTLAFVGYGdeenNTVLELTH--NwDTSSYDL-----GNGYGHIAIGVEDA 82
Cdd:cd07249    8 VPDLDEALKFYEDVLGVKVSEPEELEEQGVRVAFLELG----NTQIELLEplG-EDSPIAKfldkkGGGLHHIAFEVDDI 82

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 447165255  83 YKACEEIKARGGKVVREA-GPMKGGVTViAFVEDPDGYKV--ELIQ 125
Cdd:cd07249   83 DAAVEELKAQGVRLLSEGpRIGAHGKRV-AFLHPKDTGGVliELVE 127
Glyoxalase_4 pfam13669
Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;
10-106 7.84e-09

Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;


Pssm-ID: 463951 [Multi-domain]  Cd Length: 109  Bit Score: 49.97  E-value: 7.84e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447165255   10 VGNLEQSLKFYTEVLGMKLLRKRDYEEGRFTLAFVGYGDEenNTVLELTHNWDTSSYDLGNGYG--HIAIGVEDAYKACE 87
Cdd:pfam13669   7 VPDLDRALALWGALLGLGPEGDYRSEPQNVDLAFALLGDG--PVEVELIQPLDGDSPLARHGPGlhHLAYWVDDLDAAVA 84

                          90
                  ....*....|....*....
gi 447165255   88 EIKARGGKVVrEAGPMKGG 106
Cdd:pfam13669  85 RLLDQGYRVA-PKGPRAGA 102
SgaA_N_like cd07247
N-terminal domain of Streptomyces griseus SgaA and similar domains; SgaA suppresses the growth ...
 10-125 4.64e-07

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: 45.33  E-value: 4.64e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447165255  10 VGNLEQSLKFYTEVLGmklLRKRDYEEGRFTLAFVGYGDEENNTVLELTHNWDTSsydlgNGYGHIAIGVEDAYKACEEI 89
Cdd:cd07247    8 TTDLERAKAFYGAVFG---WTFEDEGDGGGDYALFTAGGGAVGGLMRAPEEVAGA-----PPGWLIYFAVDDLDAALARV 79

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 447165255  90 KARGGKVVReaGPMK-GGVTVIAFVEDPDGYKVELIQ 125
Cdd:cd07247   80 EAAGGKVVV--PPTDiPGGGRFAVFADPEGNRFGLWS 114
VOC_like cd07251
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 8-119 4.76e-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: 319914 [Multi-domain]  Cd Length: 120  Bit Score: 45.36  E-value: 4.76e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447165255   8 LRVGNLEQSLKFYTEvLGMKllRKRDYEEGrftlaFVGYgdEENNTVLELTHN----WDTSSYDLGNGYGHIAIG----- 78
Cdd:cd07251    4 LGVRDLERSARFYEA-LGWK--PNLDPNDG-----VVFF--QLGGTVLALYPRdalaEDAGVSVTGAGFSGVTLAhnvrs 73

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 447165255  79 VEDAYKACEEIKARGGKVVREAGPMKGGVtVIAFVEDPDGY 119
Cdd:cd07251   74 REEVDQLLAKAVAAGGKILKPPQEVFWGG-YSGYFADPDGH 113
FosA cd07244
fosfomycin resistant protein subfamily FosA; This subfamily family contains FosA, a fosfomycin ...
 5-123 8.67e-07

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


Pssm-ID: 319908 [Multi-domain]  Cd Length: 121  Bit Score: 44.58  E-value: 8.67e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447165255   5 HTMLRVGNLEQSLKFYTEVLGMKLLRKrdYEEGrftlAFVGYGDeenntvLELTHNWDTSSYDLgNGYGHIAIGV--EDA 82
Cdd:cd07244    4 HITLAVSDLERSLAFYVDLLGFKPHVR--WDKG----AYLTAGD------LWLCLSLDPAAEPS-PDYTHIAFTVseEDF 70

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 447165255  83 YKACEEIKARGGKVVREAgpMKGGVTViaFVEDPDGYKVEL 123
Cdd:cd07244   71 EELSERLRAAGVKIWQEN--SSEGDSL--YFLDPDGHKLEL 107
VOC_like cd07262
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 5-122 9.10e-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: 44.53  E-value: 9.10e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447165255   5 HTMLRVGNLEQSLKFYT---EVLGmkllrkrdYEEGRFTLAFVGYGDEENNTVlelthnWDTSSYD-----LGNGyGHIA 76
Cdd:cd07262    3 HVTIGVNDLERSRAFYDaalAPLG--------YKRGFEDGGRVGYGLEGGPDF------WVTEPFDgepatAGNG-THVA 67

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 447165255  77 I------GVEDAYKACeeIKArGGKVVREAG--PMKGGVTVIAFVEDPDGYKVE 122
Cdd:cd07262   68 FaapsraAVDAFHAAA--LAA-GGTDNGAPGlrPHYHPGYYAAYVRDPDGNKIE 118
HPPD_N_like cd08342
N-terminal domain of 4-hydroxyphenylpyruvate dioxygenase (HPPD) and hydroxymandelate Synthase ...
 10-114 1.78e-06

N-terminal domain of 4-hydroxyphenylpyruvate dioxygenase (HPPD) and hydroxymandelate Synthase (HmaS); HppD and HmaS are non-heme iron-dependent dioxygenases, which modify a common substrate, 4-hydroxyphenylpyruvate (HPP), but yield different products. HPPD catalyzes the second reaction in tyrosine catabolism, the conversion of HPP to homogentisate (2,5-dihydroxyphenylacetic acid, HG). HmaS converts HPP to 4-hydroxymandelate, a committed step in the formation of hydroxyphenylglycerine, a structural component of nonproteinogenic macrocyclic peptide antibiotics, such as vancomycin. If the emphasis is on catalytic chemistry, HPPD and HmaS are classified as members of a large family of alpha-keto acid dependent mononuclear non-heme iron oxygenases most of which require Fe(II), molecular oxygen, and an alpha-keto acid (typically alpha-ketoglutarate) to either oxygenate or oxidize a third substrate. Both enzymes are exceptions in that they require two, instead of three, substrates, do not use alpha-ketoglutarate, and incorporate both atoms of dioxygen into the aromatic product. Both HPPD and HmaS exhibit duplicate beta barrel topology in their N- and C-terminal domains which share sequence similarity, suggestive of a gene duplication. Each protein has only one catalytic site located in at the C-terminal domain. This HPPD_N_like domain represents the N-terminal domain.


Pssm-ID: 319930  Cd Length: 141  Bit Score: 44.12  E-value: 1.78e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447165255  10 VGNLEQSLKFYTEVLGMKLLRKRDYEEGRFTLAFVGYGDeeNNTVLelthnwdTSSYDLGNGYG-----H------IAIG 78
Cdd:cd08342    8 VGNAKQAASYYSTGLGFEPVAYHGLETREKASHVLRQGD--IRFVF-------TSPLSSDAPAAdflakHgdgvkdVAFR 78

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 447165255  79 VEDAYKACEEIKARGGKVVREAGPMK--GGVTVIAFVE 114
Cdd:cd08342   79 VEDADAAYERAVARGAKPVAEPVELSdeGGEVVIAAIQ 116
VOC_BsYqjT cd07242
vicinal oxygen chelate (VOC) family protein similar to Bacillus subtilis YqjT; The vicinal ...
 5-124 1.96e-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: 44.02  E-value: 1.96e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447165255   5 HTMLRVGNLEQSLKFYTEVLGMKLlrkRDYEEGRFTLAFvgYGDEENNTVLELTHNWDTSSYDLGN-GYGHIAIGVEDAY 83
Cdd:cd07242    4 HVELAVSDLHRSFKWFEWILGLGW---KEYDTWSFGPSW--KLSGGSLLVVQQTDEFATPEFDRARvGLNHLAFHAESRE 78

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 447165255  84 K---ACEEIKARGGKVV-REAGPMKGGVT-VIAFVEDPDGYKVELI 124
Cdd:cd07242   79 AvdeLTEKLAKIGGVRTyGDRHPFAGGPPhYAAFCEDPDGIKLELV 124
VOC_ShValD_like cd16361
vicinal oxygen chelate (VOC) family protein similar to Streptomyces hygroscopicus ValD protein; ...
 5-125 1.97e-06

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: 44.24  E-value: 1.97e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447165255   5 HTMLRVGNLEQSLKFYTEVLGMKLL-RKRDYEE-----------------GRFTLAFVGYGdeeNNTVLEL--------- 57
Cdd:cd16361    4 HVGITVPDLDAAVEFYTDVLGAEVVyRSTPLAEgdrgggemraagfvpgfARARIAMLRLG---PGPGIELfeykgpeqr 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 447165255  58 ---THNWDTssydlgnGYGHIAIGVEDAYKACEEIKARGGKVV------REAGPMKGGVTViaFVEDPDGYKVELIQ 125
Cdd:cd16361   81 apvPRNSDV-------GIFHFALQVDDVEAAAERLAAAGGKVLmgpreiPDGGPGKGNRMV--YLRDPWGTLIELVS 148
BphC2-C3-RGP6_C_like cd08348
The single-domain 2,3-dihydroxybiphenyl 1,2-dioxygenases; This subfamily contains Rhodococcus ...
 2-123 3.26e-06

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: 43.66  E-value: 3.26e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447165255   2 RMLHTMLRV--GNLEQSLKFYTEVLGMKLLRKRDYeegrftLAFVGYGDEENNTVL-----ELTHNWDTSSydlGNGYGH 74
Cdd:cd08348    1 KLAHFVLRTnpEKFEAMVQWYLDILGARIVARNAK------GCFLSFDEEHHRIAIfgapgGAQPPDKRPT---RVGLAH 71

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 447165255  75 IAI---GVEDAYKACEEIKARGgkvVREAGPMKGGVTVIAFVEDPDGYKVEL 123
Cdd:cd08348   72 IAFtyaSLDDLARNYAQLKERG---IKPVWPVNHGVTTSIYYRDPDGNMLEM 120
GLOD5 cd07253
Human glyoxalase domain-containing protein 5 and similar proteins; Uncharacterized subfamily ...
 2-123 4.82e-06

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: 42.60  E-value: 4.82e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447165255   2 RMLHTMLRVGNLEQSLKFYTEVLGMKLLRkrdYEEGRFTLAFvgyGDEENNtVLELTHNWDTSSYDLGNGYGHIAIGVED 81
Cdd:cd07253    3 RLDHLVLTVKDIERTIDFYTKVLGMTVVT---FKEGRKALRF---GNQKIN-LHQKGKEFEPKASAPTPGSADLCFITET 75

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 447165255  82 AYKAC-EEIKARGgkVVREAGPMK--GGVTVIA--FVEDPDGYKVEL 123
Cdd:cd07253   76 PIDEVlEHLEACG--VTIEEGPVKrtGALGPILsiYFRDPDGNLIEL 120
ED_TypeI_classII_N cd16360
N-terminal domain of type I, class II extradiol dioxygenases; This family contains the ...
 5-124 1.12e-05

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: 41.53  E-value: 1.12e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447165255   5 HTMLRVGNLEQSLKFYTEVLGMKLLrkrdYEEGRfTLAFVGYGDEENNTVLeltHNWDtssydlGNGYGHIAIGV---ED 81
Cdd:cd16360    1 YAELGVPDLEKALEFYTDVLGLQVA----KRDGN-SVYLRGYEDEHHSLVL---YEAP------EAGLKHFAFEVaseED 66

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 447165255  82 AYKACEEIKARGGKVVREAGPMKGGVTVIAFVEDPDGYKVELI 124
Cdd:cd16360   67 LERAAASLTALGCDVTWGPDGEVPGGGKGFRFQDPSGHLLELF 109
COG3607 COG3607
Lactoylglutathione lyase-related enzyme, vicinal oxygen chelate (VOC) family [General function ...
 1-125 8.26e-05

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


Pssm-ID: 442825  Cd Length: 126  Bit Score: 39.43  E-value: 8.26e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447165255   1 MRMLHTMLRVGNLEQSLKFYTEvLGMKLLRKRDYEEgrftLAFVGYGDeenNTVLEL-THN---WDTSSyDLGNGYGH-- 74
Cdd:COG3607    2 PRIIFVNLPVADLERSRAFYEA-LGFTFNPQFSDEG----AACFVLGE---GIVLMLlPREkfaTFTGK-PIADATGFte 72

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 447165255  75 --IAIGVE-----DAykACEEIKARGGKVVREAGPMKGGVTviAFVEDPDGYKVELIQ 125
Cdd:COG3607   73 vlLALNVEsreevDA--LVAKALAAGGTVLKPPQDVGGMYS--GYFADPDGHLWEVAW 126
BphC-JF8_N_like cd09013
N-terminal, non-catalytic, domain of BphC_JF8, (2,3-dihydroxybiphenyl 1,2-dioxygenase) from ...
 5-123 1.06e-04

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


Pssm-ID: 319955  Cd Length: 121  Bit Score: 39.25  E-value: 1.06e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447165255   5 HTMLRVGNLEQSLKFYTEVLGMkllrkrdYEEGRF--TLAFVGYGDEENNTvLELTHNWDTssydlgnGYGHIAIGV--- 79
Cdd:cd09013    9 HVELLTPKPEESLWFFTDVLGL-------EETHREgqSVYLRAWGDWEHHT-LKLTESPEA-------GLGHIAWRAssp 73

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 447165255  80 EDAYKACEEIKARGGKVVREAGPMKGGVTvIAFvEDPDGYKVEL 123
Cdd:cd09013   74 EALERRVAALEASGVGIGWIDGDLGQGPA-YRF-QSPDGHPMEI 115
VOC_like cd08354
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 3-123 1.44e-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: 319942  Cd Length: 122  Bit Score: 38.89  E-value: 1.44e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447165255   3 MLHTMLRVGNLEQSLKFYTEVLGMKLLRKrdyeEGRftLAFVGYGdeenNTVLEL---------THNWDTSSYDlGNGYG 73
Cdd:cd08354    1 ILETCLYADDLDAAEAFYEDVLGLKPMLR----SGR--HAFFRLG----PQVLLVfdpgatskdVRTGEVPGHG-ASGHG 69

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 447165255  74 HIAIGVEDAYKACEE--IKARGGKVVREAGPMKGGVTViaFVEDPDGYKVEL 123
Cdd:cd08354   70 HFAFAVPTEELAAWEarLEAKGVPIESYTQWPEGGKSL--YFRDPAGNLVEL 119
FosB cd08363
fosfomycin resistant protein subfamily FosB; This subfamily family contains FosB, a fosfomycin ...
 5-123 3.05e-04

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


Pssm-ID: 319951 [Multi-domain]  Cd Length: 131  Bit Score: 38.10  E-value: 3.05e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447165255   5 HTMLRVGNLEQSLKFYTEVLGMKLL---RKRDYeegrFTLafvgygdeeNNTVLELTHNWDTSSYDLGNGYGHIAIGV-E 80
Cdd:cd08363    3 HITFSVSNLNKSIAFYKDVLDAKLLvlgEKTAY----FDL---------NGLWLALNVQEDIPRNEISHSYTHIAFSIdE 69

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 447165255  81 DAYKACEEIKARGGKVVREAGPMKGGVTVIAFVEDPDGYKVEL 123
Cdd:cd08363   70 EDLDAFKERLKDNGVNILEGRKRDILEGQSIYFTDPDGHLFEL 112
BLMA_like cd08349
Bleomycin binding protein (BLMA) and similar proteins; BLMA also called Bleomycin resistance ...
 8-121 4.30e-04

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: 37.21  E-value: 4.30e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447165255   8 LRVGNLEQSLKFYTEVLGMKLlrkrDYEEGRFTLAFVGYGDeenntvLELtHNWDTSSYDLGNGYGHIAIGVEDAYKACE 87
Cdd:cd08349    4 LPVRDIDKTLAFYVDVLGFEV----DYERPPPGYAILSRGG------VEL-HLFEHPGLDPAGSGVAAYIRVEDIDALHA 72

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 447165255  88 EIKARG-----GKVVREAGPMKGGVTVIAfVEDPDGYKV 121
Cdd:cd08349   73 ELKAAGlplfgIPRITPIEDKPWGMREFA-VVDPDGNLL 110
2_3_CTD_N cd07265
N-terminal domain of catechol 2,3-dioxygenase; This subfamily contains the N-terminal, ...
 1-123 4.57e-04

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


Pssm-ID: 319926  Cd Length: 122  Bit Score: 37.33  E-value: 4.57e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447165255   1 MRMLHTMLRVGNLEQSLKFYTEVLGMKllrkrdyEEGRftlafvgygDEENNTVLELTHNWDTSSYDLGN----GYGHIA 76
Cdd:cd07265    3 LRPGHVQLRVLDLEEAIKHYREVLGLV-------ETGR---------DDQGRVYLKAWDEYDHHSIILREadtaGLDFMG 66

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 447165255  77 IGVEDAY---KACEEIKARGGKVVR-EAGPMKGGVTVIAFvEDPDGYKVEL 123
Cdd:cd07265   67 FKVLDDAdleQLEARLQAYGVTVTRiPAGELPGVGRRVRF-QLPSGHTMEL 116
VOC_Bs_YwkD_like cd08352
vicinal oxygen chelate (VOC) family protein Bacillus subtilis YwkD and similar proteins; ...
 12-123 9.44e-04

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: 36.75  E-value: 9.44e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447165255  12 NLEQSLKFYTEVLGMKLLRkRDYEEGR----FTLAFVGYgdeenntVLELTHNWDT---SSYDLGNGYGHIAIGVEDAYK 84
Cdd:cd08352   12 DYEKSKDFYVDKLGFEIIR-EHYRPERndikLDLALGGY-------QLELFIKPDAparPSYPEALGLRHLAFKVEDVEA 83

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 447165255  85 ACEEIKARGGKV--VRE----AGPMkggvtviAFVEDPDGYKVEL 123
Cdd:cd08352   84 TVAELKSLGIETepIRVddftGKKF-------TFFFDPDGLPLEL 121
BphC5-RrK37_N_like cd08362
N-terminal, non-catalytic, domain of BphC5 (2,3-dihydroxybiphenyl 1,2-dioxygenase) from ...
 8-128 2.66e-03

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: 35.30  E-value: 2.66e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447165255   8 LRVGNLEQSLKFYTEVLGMKLLRKrdyEEGRFTLAfvGYGDEenNTVLELTHnwdtssyDLGNGYGHIAIGVEDAY---K 84
Cdd:cd08362    9 LGVPDLAAEREFYTEVWGLEEVAE---DDDVVYLR--AEGSE--HHVLRLRQ-------SDENRLDLIAFAAATRAdvdA 74

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 447165255  85 ACEEIKARGGKVVREAGPMK--GGVTVIAFVeDPDGYKVELIQQDA 128
Cdd:cd08362   75 LAARLAAAGVRILSEPGPLDdpGGGYGFRFF-DPDGRTIEVSADVA 119
VOC_BsCatE_like_N cd07255
N-terminal of Bacillus subtilis CatE like protein; Uncharacterized subfamily of VOC ...
 1-123 4.71e-03

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: 34.59  E-value: 4.71e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447165255   1 MRMLHTMLRVGNLEQSLKFYTEVLGMKLLRKrdyEEGRFTLafvgyGDEENNTVLELTHNWDTSSYDLGN-GYGHIAIGV 79
Cdd:cd07255    1 TRIGRVTLKVADLERQSAFYQNVIGLSVLKQ---NASRAYL-----GVDGKQVLLVLEAIPDAVLAPRSTtGLYHFAILL 72

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 447165255  80 EDAYKAceeikARGGKVVREAGPMKG----GVTVIAFVEDPDGYKVEL 123
Cdd:cd07255   73 PDRKAL-----GRALAHLAEHGPLIGaadhGVSEAIYLSDPEGNGIEI 115
VOC_like cd09011
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 1-123 4.94e-03

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


Pssm-ID: 319953  Cd Length: 122  Bit Score: 34.75  E-value: 4.94e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447165255   1 MRMLHTMLRVGNLEQSLKFYTEVLGMKLLrkrdYEEGRFTLAFVGYGDEENNTVLELTHNWDTSSYDLGNGYgHIAIGVE 80
Cdd:cd09011    1 MKFVNPLLVVKDIEKSKKFYEDVLGQKIL----LDFGENVVFEGGFALQEKKSWLETIIISDLSIKQQSNNF-ELYFEVD 75

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 447165255  81 DAYKACEEIKARGG-KVVREAGPMKGGVTVIAFVeDPDGYKVEL 123
Cdd:cd09011   76 DFDAFFEKLNPHKDiEFIHPILEHPWGQRVFRFY-DPDGHIIEI 118
PRK04101 PRK04101
metallothiol transferase FosB;
5-123 6.75e-03

metallothiol transferase FosB;


Pssm-ID: 179740  Cd Length: 139  Bit Score: 34.54  E-value: 6.75e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447165255   5 HTMLRVGNLEQSLKFYTEVLGMKLLRKrdyeeGRFTLAFvgygdEENNTVLELTHNWDTSSYDLGNGYGHIAIGVEDayK 84
Cdd:PRK04101   7 HICFSVSNLEKSIEFYEKVLGAKLLVK-----GRKTAYF-----DLNGLWIALNEEKDIPRNEIHQSYTHIAFSIEE--E 74

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 447165255  85 ACEEIKAR--GGKVV------REAGPMKGgvtvIAFVeDPDGYKVEL 123
Cdd:PRK04101  75 DFDHWYQRlkENDVNilpgreRDERDKKS----IYFT-DPDGHKFEF 116
 
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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