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Conserved domains on  [gi|517918368|ref|WP_019088576|]
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VOC family protein [Acetobacter ascendens]

Protein Classification

VOC family protein( domain architecture ID 50733)

vicinal oxygen chelate (VOC) family protein uses a metal center to coordinate a substrate, intermediate, or transition state through vicinal oxygen atoms

CATH:  3.10.180.10
Gene Ontology:  GO:0046872|GO:0003824
PubMed:  21820381|11076500

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
VOC super family cl14632
vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate (VOC) superfamily is composed ...
 4-133 1.04e-28

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


The actual alignment was detected with superfamily member TIGR00068:

Pssm-ID: 472697  Cd Length: 150  Bit Score: 102.19  E-value: 1.04e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517918368    4 MIHSMLRVLDEARSTHFYADTLGIKPVGRFEF--ESFTLVYLA--NDEQTFELELTINHGrTESYDLGEGYGHLAVSVAD 79
Cdd:TIGR00068  18 LLHTMLRVGDLDKSLDFYTEVLGMKLLRKRDFpeMKFSLAFLGygDETSAAVIELTHNWG-TEKYDLGNGFGHIAIGVDD 96

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 517918368   80 VQAEHARMEAAGHPVT----PVKtleNKGQVVGqffFLTDPDGYKIEVLQRGAPGRFL 133
Cdd:TIGR00068  97 VYKACERVRALGGNVVrepgPVK---GGTTVIA---FVEDPDGYKIELIQRKSTKDGL 148
 
Name Accession Description Interval E-value
glyox_I TIGR00068
lactoylglutathione lyase; Lactoylglutathione lyase is also known as aldoketomutase and ...
 4-133 1.04e-28

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: 102.19  E-value: 1.04e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517918368    4 MIHSMLRVLDEARSTHFYADTLGIKPVGRFEF--ESFTLVYLA--NDEQTFELELTINHGrTESYDLGEGYGHLAVSVAD 79
Cdd:TIGR00068  18 LLHTMLRVGDLDKSLDFYTEVLGMKLLRKRDFpeMKFSLAFLGygDETSAAVIELTHNWG-TEKYDLGNGFGHIAIGVDD 96

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 517918368   80 VQAEHARMEAAGHPVT----PVKtleNKGQVVGqffFLTDPDGYKIEVLQRGAPGRFL 133
Cdd:TIGR00068  97 VYKACERVRALGGNVVrepgPVK---GGTTVIA---FVEDPDGYKIELIQRKSTKDGL 148
GlxI_Ni cd16358
Glyoxalase I that uses Ni(++) as cofactor; This family includes Escherichia coil and other ...
 4-124 8.80e-26

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: 94.00  E-value: 8.80e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517918368   4 MIHSMLRVLDEARSTHFYADTLGIKPVGRFEF--ESFTLVYL--ANDEQTFELELTINHGrTESYDLGEGYGHLAVSVAD 79
Cdd:cd16358    1 MLHTMLRVGDLDRSIKFYTEVLGMKLLRKRDYpeGKYTLAFVgyGDEDENTVLELTYNWG-VDKYDLGTAYGHIAIGVED 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 517918368  80 VQAEHARMEAAGHPVTPVKTLENKGQVVgqFFFLTDPDGYKIEVL 124
Cdd:cd16358   80 VYETCERIRKKGGKVTREPGPMKGGTTV--IAFVEDPDGYKIELI 122
GloA COG0346
Catechol 2,3-dioxygenase or related enzyme, vicinal oxygen chelate (VOC) family [Secondary ...
 3-129 1.39e-25

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: 93.52  E-value: 1.39e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517918368   3 KMIHSMLRVLDEARSTHFYADTLGIKPVGRFEFE--SFTLVYLANDEQTfELELTINHGrTESYDLGEGYGHLAVSVADV 80
Cdd:COG0346    2 GLHHVTLRVSDLEASLAFYTDVLGLELVKRTDFGdgGFGHAFLRLGDGT-ELELFEAPG-AAPAPGGGGLHHLAFRVDDL 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 517918368  81 QAEHARMEAAGHPVTPVKTLENKGQvvgQFFFLTDPDGYKIEVLQRGAP 129
Cdd:COG0346   80 DAAYARLRAAGVEIEGEPRDRAYGY---RSAYFRDPDGNLIELVEPPPG 125
PLN02300 PLN02300
lactoylglutathione lyase
 3-128 5.04e-19

lactoylglutathione lyase


Pssm-ID: 215169 [Multi-domain]  Cd Length: 286  Bit Score: 80.21  E-value: 5.04e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517918368   3 KMIHSMLRVLDEARSTHFYADTLGIKPVGRFEF--ESFTLVYLA--NDEQTFELELTINHGrTESYDLGEGYGHLAVSVA 78
Cdd:PLN02300  24 RMLHVVYRVGDLDRTIKFYTECLGMKLLRKRDIpeEKYTNAFLGygPEDSNFVVELTYNYG-VDKYDIGTGFGHFGIAVE 102

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 517918368  79 DVQAEHARMEAAGHPVTPVKTLENKGQVVgqFFFLTDPDGYKIEVLQRGA 128
Cdd:PLN02300 103 DVAKTVELVKAKGGKVTREPGPVKGGKSV--IAFVKDPDGYKFELIQRGP 150
Glyoxalase pfam00903
Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;
3-123 2.87e-11

Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;


Pssm-ID: 395724 [Multi-domain]  Cd Length: 121  Bit Score: 56.69  E-value: 2.87e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517918368    3 KMIHSMLRVLDEARSTHFYADTLGIKPVGRF---EFESFTLVYLANDEQTFELELTINHGRTESYDLGEGYGHLAVSVAD 79
Cdd:pfam00903   1 RIDHVALRVGDLEKSLDFYTDVLGFKLVEETdagEEGGLRSAFFLAGGRVLELLLNETPPPAAAGFGGHHIAFIAFSVDD 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 517918368   80 VQAEHARMEAAGhpVTPVKTLENKGQVVGQFFFlTDPDGYKIEV 123
Cdd:pfam00903  81 VDAAYDRLKAAG--VEIVREPGRHGWGGRYSYF-RDPDGNLIEL 121
 
Name Accession Description Interval E-value
glyox_I TIGR00068
lactoylglutathione lyase; Lactoylglutathione lyase is also known as aldoketomutase and ...
 4-133 1.04e-28

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: 102.19  E-value: 1.04e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517918368    4 MIHSMLRVLDEARSTHFYADTLGIKPVGRFEF--ESFTLVYLA--NDEQTFELELTINHGrTESYDLGEGYGHLAVSVAD 79
Cdd:TIGR00068  18 LLHTMLRVGDLDKSLDFYTEVLGMKLLRKRDFpeMKFSLAFLGygDETSAAVIELTHNWG-TEKYDLGNGFGHIAIGVDD 96

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 517918368   80 VQAEHARMEAAGHPVT----PVKtleNKGQVVGqffFLTDPDGYKIEVLQRGAPGRFL 133
Cdd:TIGR00068  97 VYKACERVRALGGNVVrepgPVK---GGTTVIA---FVEDPDGYKIELIQRKSTKDGL 148
GlxI_Ni cd16358
Glyoxalase I that uses Ni(++) as cofactor; This family includes Escherichia coil and other ...
 4-124 8.80e-26

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: 94.00  E-value: 8.80e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517918368   4 MIHSMLRVLDEARSTHFYADTLGIKPVGRFEF--ESFTLVYL--ANDEQTFELELTINHGrTESYDLGEGYGHLAVSVAD 79
Cdd:cd16358    1 MLHTMLRVGDLDRSIKFYTEVLGMKLLRKRDYpeGKYTLAFVgyGDEDENTVLELTYNWG-VDKYDLGTAYGHIAIGVED 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 517918368  80 VQAEHARMEAAGHPVTPVKTLENKGQVVgqFFFLTDPDGYKIEVL 124
Cdd:cd16358   80 VYETCERIRKKGGKVTREPGPMKGGTTV--IAFVEDPDGYKIELI 122
GloA COG0346
Catechol 2,3-dioxygenase or related enzyme, vicinal oxygen chelate (VOC) family [Secondary ...
 3-129 1.39e-25

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: 93.52  E-value: 1.39e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517918368   3 KMIHSMLRVLDEARSTHFYADTLGIKPVGRFEFE--SFTLVYLANDEQTfELELTINHGrTESYDLGEGYGHLAVSVADV 80
Cdd:COG0346    2 GLHHVTLRVSDLEASLAFYTDVLGLELVKRTDFGdgGFGHAFLRLGDGT-ELELFEAPG-AAPAPGGGGLHHLAFRVDDL 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 517918368  81 QAEHARMEAAGHPVTPVKTLENKGQvvgQFFFLTDPDGYKIEVLQRGAP 129
Cdd:COG0346   80 DAAYARLRAAGVEIEGEPRDRAYGY---RSAYFRDPDGNLIELVEPPPG 125
GlxI_Zn cd07233
Glyoxalase I that uses Zn(++) as cofactor; This family includes eukaryotic glyoxalase I that ...
 6-124 7.31e-23

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: 87.00  E-value: 7.31e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517918368   6 HSMLRVLDEARSTHFYADTLGIKPVGRFEFES--FTLVYLA--------NDEQTFE-------LELTINHG----RTESY 64
Cdd:cd07233    3 HTMLRVKDPKKSLKFYTEVLGMKLLRKKDFPEmkFSLYFLGyedpkdipKDPRTAWvfsregtLELTHNWGtendEDPVY 82

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 517918368  65 DLG----EGYGHLAVSVADVQAEHARMEAAGhpvTPVKTLENKGQVVGqFFFLTDPDGYKIEVL 124
Cdd:cd07233   83 HNGnsdpRGFGHIGIAVDDVYAACERFEELG---VKFKKKPDDGKMKG-IAFIKDPDGYWIEIL 142
PLN02300 PLN02300
lactoylglutathione lyase
 3-128 5.04e-19

lactoylglutathione lyase


Pssm-ID: 215169 [Multi-domain]  Cd Length: 286  Bit Score: 80.21  E-value: 5.04e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517918368   3 KMIHSMLRVLDEARSTHFYADTLGIKPVGRFEF--ESFTLVYLA--NDEQTFELELTINHGrTESYDLGEGYGHLAVSVA 78
Cdd:PLN02300  24 RMLHVVYRVGDLDRTIKFYTECLGMKLLRKRDIpeEKYTNAFLGygPEDSNFVVELTYNYG-VDKYDIGTGFGHFGIAVE 102

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 517918368  79 DVQAEHARMEAAGHPVTPVKTLENKGQVVgqFFFLTDPDGYKIEVLQRGA 128
Cdd:PLN02300 103 DVAKTVELVKAKGGKVTREPGPVKGGKSV--IAFVKDPDGYKFELIQRGP 150
VOC cd06587
vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate (VOC) superfamily is composed ...
 6-123 1.09e-15

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: 67.94  E-value: 1.09e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517918368   6 HSMLRVLDEARSTHFYADTLGIKPVGRFEFESFTLVYLANDeqtfeLELTINHGRTESYDLGEGYGHLAVSVADVQAEHA 85
Cdd:cd06587    1 HVALRVPDLDASVAFYEEVLGFEVVSRNEGGGFAFLRLGPG-----LRLALLEGPEPERPGGGGLFHLAFEVDDVDEVDE 75

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 517918368  86 RMEAAGHPVTPVKTLENKGQVVGQFFFlTDPDGYKIEV 123
Cdd:cd06587   76 RLREAGAEGELVAPPVDDPWGGRSFYF-RDPDGNLIEF 112
PRK10291 PRK10291
glyoxalase I; Provisional
 8-133 8.58e-15

glyoxalase I; Provisional


Pssm-ID: 182358  Cd Length: 129  Bit Score: 65.81  E-value: 8.58e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517918368   8 MLRVLDEARSTHFYADTLGIKPVGRFEFESF--TLVYLANDEQTFE--LELTINHGrTESYDLGEGYGHLAVSVADVQAE 83
Cdd:PRK10291   1 MLRVGDLQRSIDFYTNVLGMKLLRTSENPEYkySLAFVGYGPETEEavIELTYNWG-VDKYELGTAYGHIALSVDNAAEA 79

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 517918368  84 HARMEAAGHPVTPVKTLENKGQVVgqFFFLTDPDGYKIEVLQRGAPGRFL 133
Cdd:PRK10291  80 CEKIRQNGGNVTREAGPVKGGTTV--IAFVEDPDGYKIELIEEKDAGRGL 127
PLN03042 PLN03042
Lactoylglutathione lyase; Provisional
 4-132 1.36e-13

Lactoylglutathione lyase; Provisional


Pssm-ID: 215548  Cd Length: 185  Bit Score: 64.07  E-value: 1.36e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517918368   4 MIHSMLRVLDEARSTHFYADTLGIKPVGRFEFES--FTLVYLANDEQ-------------TFE----LELTINHGrTES- 63
Cdd:PLN03042  28 MQQTMFRIKDPKASLDFYSRVLGMSLLKRLDFPEmkFSLYFLGYEDSetaptdppertvwTFGrkatIELTHNWG-TESd 106

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 517918368  64 -----YDLG----EGYGHLAVSVADVQAEHARMEAAGhpVTPVKTlENKGQVVGqFFFLTDPDGYKIEVLQRGAPGRF 132
Cdd:PLN03042 107 pefkgYHNGnsdpRGFGHIGITVDDVYKACERFEKLG--VEFVKK-PDDGKMKG-LAFIKDPDGYWIEIFDLKRIGGI 180
CatE COG2514
Catechol-2,3-dioxygenase [Secondary metabolites biosynthesis, transport and catabolism];
2-123 1.16e-11

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


Pssm-ID: 442004 [Multi-domain]  Cd Length: 141  Bit Score: 58.05  E-value: 1.16e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517918368   2 AKMIHSMLRVLDEARSTHFYADTLGIKPVGRFEfesfTLVYLANDEQTFELELTinHGRTESYDLGE-GYGHLAVSV--- 77
Cdd:COG2514    2 TRLGHVTLRVRDLERSAAFYTDVLGLEVVEREG----GRVYLRADGGEHLLVLE--EAPGAPPRPGAaGLDHVAFRVpsr 75

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 517918368  78 ADVQAEHARMEAAGHPVTPVKTLEnkgqvVGQFFFLTDPDGYKIEV 123
Cdd:COG2514   76 ADLDAALARLAAAGVPVEGAVDHG-----VGESLYFRDPDGNLIEL 116
VOC COG3324
Lactoylglutathione lyase-related enzyme, vicinal oxygen chelate (VOC) family [General function ...
 1-128 1.35e-11

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


Pssm-ID: 442553 [Multi-domain]  Cd Length: 119  Bit Score: 57.34  E-value: 1.35e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517918368   1 MAKMIHSMLRVLDEARSTHFYADTLGIKPVGRFEFESFTLVYLANDEQTFELEltinhgrTESYDLGEGYGHLAVSVADV 80
Cdd:COG3324    2 PGTIVWVELPVDDLERAKAFYEEVFGWTFEDDAGPGGDYAEFDTDGGQVGGLM-------PGAEEPGGPGWLLYFAVDDL 74

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 517918368  81 QAEHARMEAAGHPVTPVKTLENKGqvvGQFFFLTDPDGYKIEVLQRGA 128
Cdd:COG3324   75 DAAVARVEAAGGTVLRPPTDIPPW---GRFAVFRDPEGNRFGLWQPAA 119
Glyoxalase pfam00903
Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;
3-123 2.87e-11

Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;


Pssm-ID: 395724 [Multi-domain]  Cd Length: 121  Bit Score: 56.69  E-value: 2.87e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517918368    3 KMIHSMLRVLDEARSTHFYADTLGIKPVGRF---EFESFTLVYLANDEQTFELELTINHGRTESYDLGEGYGHLAVSVAD 79
Cdd:pfam00903   1 RIDHVALRVGDLEKSLDFYTDVLGFKLVEETdagEEGGLRSAFFLAGGRVLELLLNETPPPAAAGFGGHHIAFIAFSVDD 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 517918368   80 VQAEHARMEAAGhpVTPVKTLENKGQVVGQFFFlTDPDGYKIEV 123
Cdd:pfam00903  81 VDAAYDRLKAAG--VEIVREPGRHGWGGRYSYF-RDPDGNLIEL 121
GLOD4_C cd16357
C-terminal domain of human glyoxalase domain-containing protein 4 and similar proteins; ...
 8-121 3.33e-11

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: 56.03  E-value: 3.33e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517918368   8 MLRVLDEARSTHFYADTLGIKPVGRFEfESFTLVYlanDEQTFELELtinHGRTESYDLGEGYGHLAVSV-ADVQAEH-A 85
Cdd:cd16357    3 SLAVSDLEKSIDYWSDLLGMKVFEKSE-KSALLGY---GEDQAKLEL---VDIPEPVDHGTAFGRIAFSCpADELPPIeE 75

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 517918368  86 RMEAAGHPV-TPVKTLENKG----QVVgqffFLTDPDGYKI 121
Cdd:cd16357   76 KVKAAGQTIlTPLVSLDTPGkatvQVV----ILADPDGHEI 112
VOC_Bs_YwkD_like cd08352
vicinal oxygen chelate (VOC) family protein Bacillus subtilis YwkD and similar proteins; ...
 13-123 2.18e-10

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: 54.09  E-value: 2.18e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517918368  13 DEARSTHFYADTLG---IKPVGRFEFESFTLvYLANDEQTFELELTINHGRTESYDLGEGYGHLAVSVADVQAEHARMEA 89
Cdd:cd08352   12 DYEKSKDFYVDKLGfeiIREHYRPERNDIKL-DLALGGYQLELFIKPDAPARPSYPEALGLRHLAFKVEDVEATVAELKS 90

                         90       100       110
                 ....*....|....*....|....*....|....
gi 517918368  90 AGHPVTPVKTLENKGQvvgQFFFLTDPDGYKIEV 123
Cdd:cd08352   91 LGIETEPIRVDDFTGK---KFTFFFDPDGLPLEL 121
PLN02300 PLN02300
lactoylglutathione lyase
 8-120 3.92e-10

lactoylglutathione lyase


Pssm-ID: 215169 [Multi-domain]  Cd Length: 286  Bit Score: 55.94  E-value: 3.92e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517918368   8 MLRVLDEARSTHFYADTLGIKPVGRFEFES--FTLVYL--ANDEQTFELELTINHGRTEsYDLGEGYGHLAVSVADV--Q 81
Cdd:PLN02300 159 MLRVGDLDRSIKFYEKAFGMKLLRKRDNPEykYTIAMMgyGPEDKTTVLELTYNYGVTE-YTKGNAYAQIAIGTDDVykT 237

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 517918368  82 AEHARMEAAghpvtpvKTLENKGQVVG---QFFFLTDPDGYK 120
Cdd:PLN02300 238 AEAIKLVGG-------KITREPGPLPGintKITACLDPDGWK 272
PLN02367 PLN02367
lactoylglutathione lyase
 4-124 1.16e-09

lactoylglutathione lyase


Pssm-ID: 177995  Cd Length: 233  Bit Score: 54.23  E-value: 1.16e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517918368   4 MIHSMLRVLDEARSTHFYADTLGIKPVGRFEFES--FTLVYLANDE-----------------QTFELELTINHGrTES- 63
Cdd:PLN02367  76 MQQTMYRIKDPKASLDFYSRVLGMSLLKRLDFPEmkFSLYFMGYEDtasaptdptertvwtfgQKATIELTHNWG-TESd 154

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517918368  64 -----YDLG----EGYGHLAVSVADVQAEHARMEAAGhpVTPVKTlENKGQVVGqFFFLTDPDGYKIEVL 124
Cdd:PLN02367 155 pdfkgYHNGnsepRGFGHIGITVDDVYKACERFEELG--VEFVKK-PNDGKMKG-IAFIKDPDGYWIEIF 220
VOC_like cd07245
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 6-123 1.25e-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: 319909 [Multi-domain]  Cd Length: 117  Bit Score: 51.93  E-value: 1.25e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517918368   6 HSMLRVLDEARSTHFYADTLGIKPVGRFEFESFTLVYLANDEQtFELELTINHGRTESYDLGEGY--GHLAVSVADVQAE 83
Cdd:cd07245    3 HVALACPDLERARRFYTDVLGLEEVPRPPFLKFGGAWLYLGGG-QQIHLVVEQNPSELPRPEHPGrdRHPSFSVPDLDAL 81

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 517918368  84 HARMEAAGHPVTPVKTLENKgqvVGQFFFlTDPDGYKIEV 123
Cdd:cd07245   82 KQRLKEAGIPYTESTSPGGG---VTQLFF-RDPDGNRLEF 117
VOC_like cd07254
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 3-126 3.64e-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: 319917 [Multi-domain]  Cd Length: 120  Bit Score: 48.23  E-value: 3.64e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517918368   3 KMIHSMLRVLDEARSTHFYADTLGIKPVGRF-EFESFTLvylandeQTFELELTIN-HGRTESYdlgeGYGHLAVSVAD- 79
Cdd:cd07254    1 KRFHLSLNVTDLERSIRFYSDLFGAEPAKRKaDYAKFML-------EDPPLNLALLvNDRKEPY----GLNHLGIQVDSk 69

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 517918368  80 --VQAEHARMEAAGHPVtpvktLENKGQV----VGQFFFLTDPDGYKIEVLQR 126
Cdd:cd07254   70 eeVAALKARAEAAGLPV-----RKEPRTTccyaVQDKFWLTDPDGNAWEFYAT 117
BLMA_like cd08349
Bleomycin binding protein (BLMA) and similar proteins; BLMA also called Bleomycin resistance ...
 9-121 8.16e-08

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: 47.22  E-value: 8.16e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517918368   9 LRVLDEARSTHFYADTLGIKPVGRFEFESFtlVYLANDEQTFELEltinhgRTESYDLGEGYGHLAVSVADVQAEHARME 88
Cdd:cd08349    4 LPVRDIDKTLAFYVDVLGFEVDYERPPPGY--AILSRGGVELHLF------EHPGLDPAGSGVAAYIRVEDIDALHAELK 75

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 517918368  89 AAG--HPVTPVKTlENKGQVVGQF-FFLTDPDGYKI 121
Cdd:cd08349   76 AAGlpLFGIPRIT-PIEDKPWGMReFAVVDPDGNLL 110
Glyoxalase_4 pfam13669
Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;
11-96 4.32e-07

Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;


Pssm-ID: 463951 [Multi-domain]  Cd Length: 109  Bit Score: 45.35  E-value: 4.32e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517918368   11 VLDEARSTHFYADTLGIKPVGRFEFES--FTLVYLANDEQTFELELTINHGRTESYDL-GEGYGHLAVSVADVQAEHARM 87
Cdd:pfam13669   7 VPDLDRALALWGALLGLGPEGDYRSEPqnVDLAFALLGDGPVEVELIQPLDGDSPLARhGPGLHHLAYWVDDLDAAVARL 86


                  ....*....
gi 517918368   88 EAAGHPVTP 96
Cdd:pfam13669  87 LDQGYRVAP 95
FosA cd07244
fosfomycin resistant protein subfamily FosA; This subfamily family contains FosA, a fosfomycin ...
 6-123 1.22e-06

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


Pssm-ID: 319908 [Multi-domain]  Cd Length: 121  Bit Score: 44.20  E-value: 1.22e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517918368   6 HSMLRVLDEARSTHFYADTLGIKPVGRFEfesfTLVYLANDEQTFELELTINHGRTESYdlgegyGHLAVSVADVQAEHA 85
Cdd:cd07244    4 HITLAVSDLERSLAFYVDLLGFKPHVRWD----KGAYLTAGDLWLCLSLDPAAEPSPDY------THIAFTVSEEDFEEL 73

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 517918368  86 --RMEAAGhpVTPVKtlENKGQvvGQFFFLTDPDGYKIEV 123
Cdd:cd07244   74 seRLRAAG--VKIWQ--ENSSE--GDSLYFLDPDGHKLEL 107
ED_TypeI_classII_N cd16360
N-terminal domain of type I, class II extradiol dioxygenases; This family contains the ...
 6-124 3.29e-06

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: 43.07  E-value: 3.29e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517918368   6 HSMLRVLDEARSTHFYADTLGIKPVGR---------FEFESFTLVYLANDEQtfeleltinhgrtesydlgeGYGHLAVS 76
Cdd:cd16360    1 YAELGVPDLEKALEFYTDVLGLQVAKRdgnsvylrgYEDEHHSLVLYEAPEA--------------------GLKHFAFE 60

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 517918368  77 VA---DVQAEHARMEAAGHPVTPVKTLENKGQvvGQFFFLTDPDGYKIEVL 124
Cdd:cd16360   61 VAseeDLERAAASLTALGCDVTWGPDGEVPGG--GKGFRFQDPSGHLLELF 109
GLOD4_N cd08358
N-terminal domain of human glyoxalase domain-containing protein 4 and similar proteins; ...
 5-126 9.74e-06

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: 41.97  E-value: 9.74e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517918368   5 IHSMLRVLDEARSTHFYADTLGIKPVGRFEFE---------------SFTLVYLANDEQTFELELTINHGrTESYDLGEG 69
Cdd:cd08358    4 LHFVFKVGDRNKTIKFYREILGMKVLRHEEFEegckaacngpydgkwSKTMVGYGPEDDHFVVELTYNYG-IGDYELGND 82

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 517918368  70 YGHLAVSVADVQAEHARMEaagHPVTpvktlenkgQVVGQFFFLTDPDGYKIEVLQR 126
Cdd:cd08358   83 FLGITIHSKQAVSRAKKHN---WPVT---------QVGDGVYEVKAPGGYKFYLIDK 127
PRK11478 PRK11478
VOC family protein;
6-126 1.73e-05

VOC family protein;


Pssm-ID: 183156 [Multi-domain]  Cd Length: 129  Bit Score: 41.42  E-value: 1.73e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517918368   6 HSMLRVLDEARSTHFYADTLG---IKPVGRFEFESFTLVYLANDEQTFELELTINHGRTESYDLGEGYGHLAVSVADVQA 82
Cdd:PRK11478   9 HIAIIATDYAVSKAFYCDILGftlQSEVYREARDSWKGDLALNGQYVIELFSFPFPPERPSRPEACGLRHLAFSVDDIDA 88

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 517918368  83 EHARMEAAGHPVTPVKTLENKGQvvgQFFFLTDPDGYKIEVLQR 126
Cdd:PRK11478  89 AVAHLESHNVKCEAIRVDPYTQK---RFTFFNDPDGLPLELYEQ 129
VOC_like cd08354
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 4-123 2.83e-05

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


Pssm-ID: 319942  Cd Length: 122  Bit Score: 40.81  E-value: 2.83e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517918368   4 MIHSMLRVLDEARSTHFYADTLGIKPVGRfefeSFTLVYLANDEQT---FELELTINHGRTESY--DLGEGYGHLAVSVA 78
Cdd:cd08354    1 ILETCLYADDLDAAEAFYEDVLGLKPMLR----SGRHAFFRLGPQVllvFDPGATSKDVRTGEVpgHGASGHGHFAFAVP 76

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 517918368  79 D--VQAEHARMEAAGHPVTPVKTLENKGQVVgqffFLTDPDGYKIEV 123
Cdd:cd08354   77 TeeLAAWEARLEAKGVPIESYTQWPEGGKSL----YFRDPAGNLVEL 119
COG3607 COG3607
Lactoylglutathione lyase-related enzyme, vicinal oxygen chelate (VOC) family [General function ...
 1-125 9.25e-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: 9.25e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517918368   1 MAKMIHSMLRVLDEARSTHFYADtLGIKPVGRFEFESFTLVYLAN-------DEQTFE--LELTINHGRTESydlGEGYG 71
Cdd:COG3607    1 MPRIIFVNLPVADLERSRAFYEA-LGFTFNPQFSDEGAACFVLGEgivlmllPREKFAtfTGKPIADATGFT---EVLLA 76

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 517918368  72 HLAVSVADVQAEHARMEAAGHPVTpvktleNKGQVVG---QFFFlTDPDGYKIEVLQ 125
Cdd:COG3607   77 LNVESREEVDALVAKALAAGGTVL------KPPQDVGgmySGYF-ADPDGHLWEVAW 126
PhnB COG2764
Zn-dependent glyoxalase, PhnB family [Energy production and conversion];
5-126 1.08e-04

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


Pssm-ID: 442048 [Multi-domain]  Cd Length: 118  Bit Score: 39.07  E-value: 1.08e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517918368   5 IHSMLRVLDEARSTHFYADTLGIKPVGRFEFEsftlvylanDEQTFELELTINHGR------TESYDLGEGYG-HLAVSV 77
Cdd:COG2764    2 VTPYLVVDDAEEALEFYEDVFGFEVVFRMTDP---------DGKIMHAELRIGGSVlmlsdaPPDSPAAEGNGvSLSLYV 72

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 517918368  78 ADVQAEHARMEAAGhpVTPVKTLENK--GQVVGQFfflTDPDGYKIEVLQR 126
Cdd:COG2764   73 DDVDALFARLVAAG--ATVVMPLQDTfwGDRFGMV---RDPFGVLWMINTP 118
VOC_like cd07238
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 13-124 1.18e-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: 319903  Cd Length: 112  Bit Score: 39.00  E-value: 1.18e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517918368  13 DEARSTHFYADTLGIKPVGRfefESFTLVYLANDEQTFELELtINHGRTesydlGEGYGHLAVSVADVQAEHARMEAAGH 92
Cdd:cd07238   10 DPERAAAFYGDHLGLPLVMD---HGWIVTFASPGNAHAQISL-AREGGS-----GTVVPDLSIEVDDVDAVHARVVAAGL 80

                         90       100       110
                 ....*....|....*....|....*....|..
gi 517918368  93 PVTPVKTLENKGQvvgQFFFLTDPDGYKIEVL 124
Cdd:cd07238   81 RIEYGPTTEAWGV---RRFFVRDPFGRLINIL 109
VOC_like cd07263
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 8-125 1.71e-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: 319924 [Multi-domain]  Cd Length: 120  Bit Score: 38.43  E-value: 1.71e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517918368   8 MLRVLDEARSTHFYADTLGIKPVGRFEFESFTLVYLA---NDEQTFELE-LTINHGRTESYDLGEGYGHLAVSVADVQAE 83
Cdd:cd07263    3 MLYVDDQDKALDFYVEKLGFEVVEDVPMGGMRWVTVAppgSPGTSLLLEpKAHPAQMPQSPEAAGGTPGILLATDDIDAT 82

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 517918368  84 HARMEAAGHPVTPvktlENKGQVVGQFFFLTDPDGYKIEVLQ 125
Cdd:cd07263   83 YERLTAAGVTFVQ----EPTQMGGGRVANFRDPDGNLFALME 120
EhpR_like cd07261
phenazine resistance protein, EhpR; Phenazine resistance protein (EhpR) in Enterobacter ...
 8-123 2.28e-04

phenazine resistance protein, EhpR; Phenazine resistance protein (EhpR) in Enterobacter agglomerans confers resistance by binding D-alanyl-griseoluteic acid and acting as a chaperone involved in exporting the antibiotic rather than by altering it chemically. EhpR is evolutionarily related to glyoxalase I and type I extradiol dioxygenases.


Pssm-ID: 319922  Cd Length: 114  Bit Score: 38.15  E-value: 2.28e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517918368   8 MLRVLDEARSTHFYADTLGIKPVgrFEFESFTLVYLANDeqtFELELTINHGRTESYDLGEGYGHLAVSVA---DVQAEH 84
Cdd:cd07261    3 ILYVDNPERSTEFYRFLLGKEPV--ESSPTFASFVLSGG---AKLGLWSSEEVEPKVAVTGGGAELSFMVPsgeQVDEVY 77

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 517918368  85 ARMEAAGHPVT--PVKTlenkgqVVGQFFFLTDPDGYKIEV 123
Cdd:cd07261   78 AEWKAMGIPIIqePTTM------DFGYTFVATDPDGHRLRV 112
VOC_BsCatE_like_N cd07255
N-terminal of Bacillus subtilis CatE like protein; Uncharacterized subfamily of VOC ...
 6-123 1.04e-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: 36.52  E-value: 1.04e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517918368   6 HSMLRVLDEARSTHFYADTLGIKPVGRfefeSFTLVYLANDEQTFELELTINHGRTESYDLGEGYGHLAVSVADVQA--- 82
Cdd:cd07255    5 RVTLKVADLERQSAFYQNVIGLSVLKQ----NASRAYLGVDGKQVLLVLEAIPDAVLAPRSTTGLYHFAILLPDRKAlgr 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 517918368  83 ------EHARMEAAG-HPVTpvktlenkgqvvgQFFFLTDPDGYKIEV 123
Cdd:cd07255   81 alahlaEHGPLIGAAdHGVS-------------EAIYLSDPEGNGIEI 115
BphC2-C3-RGP6_C_like cd08348
The single-domain 2,3-dihydroxybiphenyl 1,2-dioxygenases; This subfamily contains Rhodococcus ...
 3-123 9.16e-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: 34.03  E-value: 9.16e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517918368   3 KMIHSMLRVLDEA--RSTHFYADTLGIKPVGRFEFESFtlvyLANDEQTFELEL-TINHGRTESYDL--GEGYGHLAV-- 75
Cdd:cd08348    1 KLAHFVLRTNPEKfeAMVQWYLDILGARIVARNAKGCF----LSFDEEHHRIAIfGAPGGAQPPDKRptRVGLAHIAFty 76

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 517918368  76 -SVADVQAEHARMEAAG-HPVTPVktleNKGQVVGQFFFltDPDGYKIEV 123
Cdd:cd08348   77 aSLDDLARNYAQLKERGiKPVWPV----NHGVTTSIYYR--DPDGNMLEM 120
 
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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