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Conserved domains on  [gi|491376449|ref|WP_005234340|]
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MULTISPECIES: VOC family protein [Enterococcus]

Protein Classification

VOC family protein( domain architecture ID 10001243)

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

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
GloA COG0346
Catechol 2,3-dioxygenase or related enzyme, vicinal oxygen chelate (VOC) family [Secondary ...
 1-121 2.12e-35

Catechol 2,3-dioxygenase or related enzyme, vicinal oxygen chelate (VOC) family [Secondary metabolites biosynthesis, transport and catabolism];


:

Pssm-ID: 440115 [Multi-domain]  Cd Length: 125  Bit Score: 118.17  E-value: 2.12e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491376449   1 MKMAHTCVRVKDLTASLDFYQTAFGFEESRRRDFPEHQFTLVYLTLpGDDYELELTYNYDHPGYELGDGYGHIAISTDDL 80
Cdd:COG0346    1 MGLHHVTLRVSDLEASLAFYTDVLGLELVKRTDFGDGGFGHAFLRL-GDGTELELFEAPGAAPAPGGGGLHHLAFRVDDL 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 491376449  81 EALHEKHQAAGFDVTDLKGLPGTSPSYYFVKDPDGYKIEVI 121
Cdd:COG0346   80 DAAYARLRAAGVEIEGEPRDRAYGYRSAYFRDPDGNLIELV 120
 
Name Accession Description Interval E-value
GloA COG0346
Catechol 2,3-dioxygenase or related enzyme, vicinal oxygen chelate (VOC) family [Secondary ...
 1-121 2.12e-35

Catechol 2,3-dioxygenase or related enzyme, vicinal oxygen chelate (VOC) family [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 440115 [Multi-domain]  Cd Length: 125  Bit Score: 118.17  E-value: 2.12e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491376449   1 MKMAHTCVRVKDLTASLDFYQTAFGFEESRRRDFPEHQFTLVYLTLpGDDYELELTYNYDHPGYELGDGYGHIAISTDDL 80
Cdd:COG0346    1 MGLHHVTLRVSDLEASLAFYTDVLGLELVKRTDFGDGGFGHAFLRL-GDGTELELFEAPGAAPAPGGGGLHHLAFRVDDL 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 491376449  81 EALHEKHQAAGFDVTDLKGLPGTSPSYYFVKDPDGYKIEVI 121
Cdd:COG0346   80 DAAYARLRAAGVEIEGEPRDRAYGYRSAYFRDPDGNLIELV 120
glyox_I TIGR00068
lactoylglutathione lyase; Lactoylglutathione lyase is also known as aldoketomutase and ...
 3-124 4.43e-34

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: 115.67  E-value: 4.43e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491376449    3 MAHTCVRVKDLTASLDFYQTAFGFEESRRRDFPEHQFTLVYLTL-PGDD-YELELTYNYDHPGYELGDGYGHIAISTDDL 80
Cdd:TIGR00068  18 LLHTMLRVGDLDKSLDFYTEVLGMKLLRKRDFPEMKFSLAFLGYgDETSaAVIELTHNWGTEKYDLGNGFGHIAIGVDDV 97

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 491376449   81 EALHEKHQAAGFDVTDLKG-LPGTSPSYYFVKDPDGYKIEVIREK 124
Cdd:TIGR00068  98 YKACERVRALGGNVVREPGpVKGGTTVIAFVEDPDGYKIELIQRK 142
GlxI_Ni cd16358
Glyoxalase I that uses Ni(++) as cofactor; This family includes Escherichia coil and other ...
 3-121 6.97e-33

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: 111.72  E-value: 6.97e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491376449   3 MAHTCVRVKDLTASLDFYQTAFGFEESRRRDFPEHQFTLVYLTLpGDDYE---LELTYNYDHPGYELGDGYGHIAISTDD 79
Cdd:cd16358    1 MLHTMLRVGDLDRSIKFYTEVLGMKLLRKRDYPEGKYTLAFVGY-GDEDEntvLELTYNWGVDKYDLGTAYGHIAIGVED 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 491376449  80 LEALHEKHQAAGFDVTDLKG-LPGTSPSYYFVKDPDGYKIEVI 121
Cdd:cd16358   80 VYETCERIRKKGGKVTREPGpMKGGTTVIAFVEDPDGYKIELI 122
PLN02300 PLN02300
lactoylglutathione lyase
 2-124 7.82e-24

lactoylglutathione lyase


Pssm-ID: 215169 [Multi-domain]  Cd Length: 286  Bit Score: 92.54  E-value: 7.82e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491376449   2 KMAHTCVRVKDLTASLDFYQTAFGFEESRRRDFPEHQFTLVYLTLPGDD--YELELTYNYDHPGYELGDGYGHIAISTDD 79
Cdd:PLN02300  24 RMLHVVYRVGDLDRTIKFYTECLGMKLLRKRDIPEEKYTNAFLGYGPEDsnFVVELTYNYGVDKYDIGTGFGHFGIAVED 103

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 491376449  80 LEALHEKHQAAGFDVTDLKG-LPGTSPSYYFVKDPDGYKIEVIREK 124
Cdd:PLN02300 104 VAKTVELVKAKGGKVTREPGpVKGGKSVIAFVKDPDGYKFELIQRG 149
Glyoxalase pfam00903
Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;
2-120 7.15e-22

Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;


Pssm-ID: 395724 [Multi-domain]  Cd Length: 121  Bit Score: 83.65  E-value: 7.15e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491376449    2 KMAHTCVRVKDLTASLDFYQTAFGFEESRRRDFPEHQfTLVYLTLPGDDYELELTYNYDHPGYELG---DGYGHIAISTD 78
Cdd:pfam00903   1 RIDHVALRVGDLEKSLDFYTDVLGFKLVEETDAGEEG-GLRSAFFLAGGRVLELLLNETPPPAAAGfggHHIAFIAFSVD 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 491376449   79 DLEALHEKHQAAGFDVTDLKGLPGTSPSYYFVKDPDGYKIEV 120
Cdd:pfam00903  80 DVDAAYDRLKAAGVEIVREPGRHGWGGRYSYFRDPDGNLIEL 121
 
Name Accession Description Interval E-value
GloA COG0346
Catechol 2,3-dioxygenase or related enzyme, vicinal oxygen chelate (VOC) family [Secondary ...
 1-121 2.12e-35

Catechol 2,3-dioxygenase or related enzyme, vicinal oxygen chelate (VOC) family [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 440115 [Multi-domain]  Cd Length: 125  Bit Score: 118.17  E-value: 2.12e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491376449   1 MKMAHTCVRVKDLTASLDFYQTAFGFEESRRRDFPEHQFTLVYLTLpGDDYELELTYNYDHPGYELGDGYGHIAISTDDL 80
Cdd:COG0346    1 MGLHHVTLRVSDLEASLAFYTDVLGLELVKRTDFGDGGFGHAFLRL-GDGTELELFEAPGAAPAPGGGGLHHLAFRVDDL 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 491376449  81 EALHEKHQAAGFDVTDLKGLPGTSPSYYFVKDPDGYKIEVI 121
Cdd:COG0346   80 DAAYARLRAAGVEIEGEPRDRAYGYRSAYFRDPDGNLIELV 120
glyox_I TIGR00068
lactoylglutathione lyase; Lactoylglutathione lyase is also known as aldoketomutase and ...
 3-124 4.43e-34

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: 115.67  E-value: 4.43e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491376449    3 MAHTCVRVKDLTASLDFYQTAFGFEESRRRDFPEHQFTLVYLTL-PGDD-YELELTYNYDHPGYELGDGYGHIAISTDDL 80
Cdd:TIGR00068  18 LLHTMLRVGDLDKSLDFYTEVLGMKLLRKRDFPEMKFSLAFLGYgDETSaAVIELTHNWGTEKYDLGNGFGHIAIGVDDV 97

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 491376449   81 EALHEKHQAAGFDVTDLKG-LPGTSPSYYFVKDPDGYKIEVIREK 124
Cdd:TIGR00068  98 YKACERVRALGGNVVREPGpVKGGTTVIAFVEDPDGYKIELIQRK 142
GlxI_Ni cd16358
Glyoxalase I that uses Ni(++) as cofactor; This family includes Escherichia coil and other ...
 3-121 6.97e-33

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: 111.72  E-value: 6.97e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491376449   3 MAHTCVRVKDLTASLDFYQTAFGFEESRRRDFPEHQFTLVYLTLpGDDYE---LELTYNYDHPGYELGDGYGHIAISTDD 79
Cdd:cd16358    1 MLHTMLRVGDLDRSIKFYTEVLGMKLLRKRDYPEGKYTLAFVGY-GDEDEntvLELTYNWGVDKYDLGTAYGHIAIGVED 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 491376449  80 LEALHEKHQAAGFDVTDLKG-LPGTSPSYYFVKDPDGYKIEVI 121
Cdd:cd16358   80 VYETCERIRKKGGKVTREPGpMKGGTTVIAFVEDPDGYKIELI 122
GlxI_Zn cd07233
Glyoxalase I that uses Zn(++) as cofactor; This family includes eukaryotic glyoxalase I that ...
 3-121 9.19e-29

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: 101.63  E-value: 9.19e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491376449   3 MAHTCVRVKDLTASLDFYQTAFGFEESRRRDFPEHQFTLVYL------TLPGDDYE---------LELTYNY-----DHP 62
Cdd:cd07233    1 FNHTMLRVKDPKKSLKFYTEVLGMKLLRKKDFPEMKFSLYFLgyedpkDIPKDPRTawvfsregtLELTHNWgtendEDP 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 491376449  63 GYELGD----GYGHIAISTDDLEALHEKHQAAGFDV----TD--LKGLpgtspsyYFVKDPDGYKIEVI 121
Cdd:cd07233   81 VYHNGNsdprGFGHIGIAVDDVYAACERFEELGVKFkkkpDDgkMKGI-------AFIKDPDGYWIEIL 142
PLN02300 PLN02300
lactoylglutathione lyase
 2-124 7.82e-24

lactoylglutathione lyase


Pssm-ID: 215169 [Multi-domain]  Cd Length: 286  Bit Score: 92.54  E-value: 7.82e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491376449   2 KMAHTCVRVKDLTASLDFYQTAFGFEESRRRDFPEHQFTLVYLTLPGDD--YELELTYNYDHPGYELGDGYGHIAISTDD 79
Cdd:PLN02300  24 RMLHVVYRVGDLDRTIKFYTECLGMKLLRKRDIPEEKYTNAFLGYGPEDsnFVVELTYNYGVDKYDIGTGFGHFGIAVED 103

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 491376449  80 LEALHEKHQAAGFDVTDLKG-LPGTSPSYYFVKDPDGYKIEVIREK 124
Cdd:PLN02300 104 VAKTVELVKAKGGKVTREPGpVKGGKSVIAFVKDPDGYKFELIQRG 149
PLN02300 PLN02300
lactoylglutathione lyase
 9-117 3.78e-22

lactoylglutathione lyase


Pssm-ID: 215169 [Multi-domain]  Cd Length: 286  Bit Score: 87.91  E-value: 3.78e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491376449   9 RVKDLTASLDFYQTAFGFEESRRRDFPEHQFTLVYLTLpGDDYE---LELTYNYDHPGYELGDGYGHIAISTDDLEALHE 85
Cdd:PLN02300 161 RVGDLDRSIKFYEKAFGMKLLRKRDNPEYKYTIAMMGY-GPEDKttvLELTYNYGVTEYTKGNAYAQIAIGTDDVYKTAE 239

                         90       100       110
                 ....*....|....*....|....*....|...
gi 491376449  86 KHQAAGFDVTDLKG-LPGTSPSYYFVKDPDGYK 117
Cdd:PLN02300 240 AIKLVGGKITREPGpLPGINTKITACLDPDGWK 272
Glyoxalase pfam00903
Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;
2-120 7.15e-22

Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;


Pssm-ID: 395724 [Multi-domain]  Cd Length: 121  Bit Score: 83.65  E-value: 7.15e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491376449    2 KMAHTCVRVKDLTASLDFYQTAFGFEESRRRDFPEHQfTLVYLTLPGDDYELELTYNYDHPGYELG---DGYGHIAISTD 78
Cdd:pfam00903   1 RIDHVALRVGDLEKSLDFYTDVLGFKLVEETDAGEEG-GLRSAFFLAGGRVLELLLNETPPPAAAGfggHHIAFIAFSVD 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 491376449   79 DLEALHEKHQAAGFDVTDLKGLPGTSPSYYFVKDPDGYKIEV 120
Cdd:pfam00903  80 DVDAAYDRLKAAGVEIVREPGRHGWGGRYSYFRDPDGNLIEL 121
PRK10291 PRK10291
glyoxalase I; Provisional
 8-124 3.56e-21

glyoxalase I; Provisional


Pssm-ID: 182358  Cd Length: 129  Bit Score: 81.99  E-value: 3.56e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491376449   8 VRVKDLTASLDFYQTAFGFEESRRRDFPEHQFTLVYLTLPGDDYE--LELTYNYDHPGYELGDGYGHIAISTDDLEALHE 85
Cdd:PRK10291   2 LRVGDLQRSIDFYTNVLGMKLLRTSENPEYKYSLAFVGYGPETEEavIELTYNWGVDKYELGTAYGHIALSVDNAAEACE 81

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 491376449  86 KHQAAGFDVTDLKG-LPGTSPSYYFVKDPDGYKIEVIREK 124
Cdd:PRK10291  82 KIRQNGGNVTREAGpVKGGTTVIAFVEDPDGYKIELIEEK 121
CatE COG2514
Catechol-2,3-dioxygenase [Secondary metabolites biosynthesis, transport and catabolism];
1-124 2.44e-20

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


Pssm-ID: 442004 [Multi-domain]  Cd Length: 141  Bit Score: 80.00  E-value: 2.44e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491376449   1 MKMAHTCVRVKDLTASLDFYQTAFGFEESRRRDfpehqfTLVYLTLPGDDYELELTYNYDHPGYELGDGYGHIAI---ST 77
Cdd:COG2514    2 TRLGHVTLRVRDLERSAAFYTDVLGLEVVEREG------GRVYLRADGGEHLLVLEEAPGAPPRPGAAGLDHVAFrvpSR 75

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 491376449  78 DDLEALHEKHQAAGFDVTDlKGLPGTSPSYYFvKDPDGYKIEVIREK 124
Cdd:COG2514   76 ADLDAALARLAAAGVPVEG-AVDHGVGESLYF-RDPDGNLIELYTDR 120
VOC cd06587
vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate (VOC) superfamily is composed ...
 5-120 6.76e-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: 78.34  E-value: 6.76e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491376449   5 HTCVRVKDLTASLDFYQTAFGFEESRRRDFPEHqftlVYLTLpGDDYELELTYNYDHPgYELGDGYGHIAISTDDLEALH 84
Cdd:cd06587    1 HVALRVPDLDASVAFYEEVLGFEVVSRNEGGGF----AFLRL-GPGLRLALLEGPEPE-RPGGGGLFHLAFEVDDVDEVD 74

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 491376449  85 EKHQAAGFDVTDLKGLPGTSPSYY--FVKDPDGYKIEV 120
Cdd:cd06587   75 ERLREAGAEGELVAPPVDDPWGGRsfYFRDPDGNLIEF 112
PLN03042 PLN03042
Lactoylglutathione lyase; Provisional
 3-121 1.11e-19

Lactoylglutathione lyase; Provisional


Pssm-ID: 215548  Cd Length: 185  Bit Score: 79.48  E-value: 1.11e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491376449   3 MAHTCVRVKDLTASLDFYQTAFGFEESRRRDFPEHQFTLVYL------TLPGDDYE-----------LELTYNY------ 59
Cdd:PLN03042  28 MQQTMFRIKDPKASLDFYSRVLGMSLLKRLDFPEMKFSLYFLgyedseTAPTDPPErtvwtfgrkatIELTHNWgtesdp 107

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 491376449  60 DHPGYELGD----GYGHIAISTDDLEALHEKHQAAGF------DVTDLKGLPgtspsyyFVKDPDGYKIEVI 121
Cdd:PLN03042 108 EFKGYHNGNsdprGFGHIGITVDDVYKACERFEKLGVefvkkpDDGKMKGLA-------FIKDPDGYWIEIF 172
PLN02367 PLN02367
lactoylglutathione lyase
 3-120 3.02e-19

lactoylglutathione lyase


Pssm-ID: 177995  Cd Length: 233  Bit Score: 79.66  E-value: 3.02e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491376449   3 MAHTCVRVKDLTASLDFYQTAFGFEESRRRDFPEHQFTLVYL------TLPGDDYE-----------LELTYNY------ 59
Cdd:PLN02367  76 MQQTMYRIKDPKASLDFYSRVLGMSLLKRLDFPEMKFSLYFMgyedtaSAPTDPTErtvwtfgqkatIELTHNWgtesdp 155

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 491376449  60 DHPGYELGD----GYGHIAISTDDLEALHEKHQAAGFDVTDlKGLPGTSPSYYFVKDPDGYKIEV 120
Cdd:PLN02367 156 DFKGYHNGNseprGFGHIGITVDDVYKACERFEELGVEFVK-KPNDGKMKGIAFIKDPDGYWIEI 219
VOC COG3324
Lactoylglutathione lyase-related enzyme, vicinal oxygen chelate (VOC) family [General function ...
 1-124 3.53e-12

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


Pssm-ID: 442553 [Multi-domain]  Cd Length: 119  Bit Score: 58.49  E-value: 3.53e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491376449   1 MKMAHTCVRVKDLTASLDFYQTAFGFEESRRRDFPEHqftlvYLTLPGDDYE-LELTYNYDHPgyelGDGYGHIAISTDD 79
Cdd:COG3324    3 GTIVWVELPVDDLERAKAFYEEVFGWTFEDDAGPGGD-----YAEFDTDGGQvGGLMPGAEEP----GGPGWLLYFAVDD 73

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 491376449  80 LEALHEKHQAAGFDVTDlkglPGTSPSYY----FVKDPDGYKIEVIREK 124
Cdd:COG3324   74 LDAAVARVEAAGGTVLR----PPTDIPPWgrfaVFRDPEGNRFGLWQPA 118
PhnB COG2764
Zn-dependent glyoxalase, PhnB family [Energy production and conversion];
4-120 9.36e-11

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


Pssm-ID: 442048 [Multi-domain]  Cd Length: 118  Bit Score: 54.86  E-value: 9.36e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491376449   4 AHTCVRVKDLTASLDFYQTAFGFEESRRRDFPEHQftLVYLTLPGDDYELELTYNYDHPGYELGDGYgHIAISTDDLEAL 83
Cdd:COG2764    2 VTPYLVVDDAEEALEFYEDVFGFEVVFRMTDPDGK--IMHAELRIGGSVLMLSDAPPDSPAAEGNGV-SLSLYVDDVDAL 78

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 491376449  84 HEKHQAAGFDVT-DLKGLPgTSPSYYFVKDPDGYKIEV 120
Cdd:COG2764   79 FARLVAAGATVVmPLQDTF-WGDRFGMVRDPFGVLWMI 115
VOC_Bs_YwkD_like cd08352
vicinal oxygen chelate (VOC) family protein Bacillus subtilis YwkD and similar proteins; ...
 1-120 2.11e-09

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: 51.39  E-value: 2.11e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491376449   1 MKMAHTCVRVKDLTASLDFYQTAFGFEESRRRDFPEHQFTLvyLTLPGDDYELELTYNYDHP---GYELGDGYGHIAIST 77
Cdd:cd08352    1 KKIHHIAIICSDYEKSKDFYVDKLGFEIIREHYRPERNDIK--LDLALGGYQLELFIKPDAParpSYPEALGLRHLAFKV 78

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 491376449  78 DDLEALHEKHQAAGFDVTDLKGLPGTSPSYYFVKDPDGYKIEV 120
Cdd:cd08352   79 EDVEATVAELKSLGIETEPIRVDDFTGKKFTFFFDPDGLPLEL 121
Glyoxalase_4 pfam13669
Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;
5-96 3.77e-09

Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;


Pssm-ID: 463951 [Multi-domain]  Cd Length: 109  Bit Score: 50.35  E-value: 3.77e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491376449    5 HTCVRVKDLTASLDFYQTAFGFEESRRRDFPEHQFTLVYLTLPGDDYELEL--TYNYDHPGYELGDGYGHIAISTDDLEA 82
Cdd:pfam13669   2 HVGIAVPDLDRALALWGALLGLGPEGDYRSEPQNVDLAFALLGDGPVEVELiqPLDGDSPLARHGPGLHHLAYWVDDLDA 81

                          90
                  ....*....|....
gi 491376449   83 LHEKHQAAGFDVTD 96
Cdd:pfam13669  82 AVARLLDQGYRVAP 95
VOC_like cd07263
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 5-115 5.00e-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: 50.37  E-value: 5.00e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491376449   5 HTCVRVKDLTASLDFYQTAFGFEESRRRDFPEHQFtlvyLTL-PGDDYELELT-YNYDHP-----GYELGDGYGHIAIST 77
Cdd:cd07263    1 QVMLYVDDQDKALDFYVEKLGFEVVEDVPMGGMRW----VTVaPPGSPGTSLLlEPKAHPaqmpqSPEAAGGTPGILLAT 76

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 491376449  78 DDLEALHEKHQAAGFDVTDLKGLPGTSPSYYFvKDPDG 115
Cdd:cd07263   77 DDIDATYERLTAAGVTFVQEPTQMGGGRVANF-RDPDG 113
VOC_like cd07262
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 5-121 5.94e-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: 319923 [Multi-domain]  Cd Length: 121  Bit Score: 50.30  E-value: 5.94e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491376449   5 HTCVRVKDLTASLDFYQTAFG-FEESRRRDFPEHqftlVYLTLPGDDyELELTYNYDHPGYELGDGyGHIAISTDDLEAL 83
Cdd:cd07262    3 HVTIGVNDLERSRAFYDAALApLGYKRGFEDGGR----VGYGLEGGP-DFWVTEPFDGEPATAGNG-THVAFAAPSRAAV 76

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 491376449  84 HEKHQAA----GFDVTDLKGLPGTSPSYY--FVKDPDGYKIEVI 121
Cdd:cd07262   77 DAFHAAAlaagGTDNGAPGLRPHYHPGYYaaYVRDPDGNKIEAV 120
VOC_like cd07245
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 5-120 6.80e-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: 50.01  E-value: 6.80e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491376449   5 HTCVRVKDLTASLDFYQTAFGFEESRRRDFPEhqFTLVYLTLpGDDYELELTY--NYDHPGYELGDGYG-HIAISTDDLE 81
Cdd:cd07245    3 HVALACPDLERARRFYTDVLGLEEVPRPPFLK--FGGAWLYL-GGGQQIHLVVeqNPSELPRPEHPGRDrHPSFSVPDLD 79

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 491376449  82 ALHEKHQAAGFDVTDlKGLPGTSPSYYFVKDPDGYKIEV 120
Cdd:cd07245   80 ALKQRLKEAGIPYTE-STSPGGGVTQLFFRDPDGNRLEF 117
BLMA_like cd08349
Bleomycin binding protein (BLMA) and similar proteins; BLMA also called Bleomycin resistance ...
 9-118 2.95e-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: 47.99  E-value: 2.95e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491376449   9 RVKDLTASLDFYQTAFGFEESRRRDFPEhqftlvYLTLPGDDYELELTYnydHPGYELGDGYGHIAISTDDLEALHEKHQ 88
Cdd:cd08349    5 PVRDIDKTLAFYVDVLGFEVDYERPPPG------YAILSRGGVELHLFE---HPGLDPAGSGVAAYIRVEDIDALHAELK 75

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 491376449  89 AAGFDVTDLKGL--PGTSPSYY--F-VKDPDGYKI 118
Cdd:cd08349   76 AAGLPLFGIPRItpIEDKPWGMreFaVVDPDGNLL 110
MMCE cd07249
Methylmalonyl-CoA epimerase (MMCE); MMCE, also called methylmalonyl-CoA racemase (EC 5.1.99.1) ...
 5-104 6.38e-08

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


Pssm-ID: 319912 [Multi-domain]  Cd Length: 127  Bit Score: 47.57  E-value: 6.38e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491376449   5 HTCVRVKDLTASLDFYQTAFGFEESRRRDFPEHQFTLVYLTLPGDDYELELTYNYDHPGYEL----GDGYGHIAISTDDL 80
Cdd:cd07249    3 HIGIAVPDLDEALKFYEDVLGVKVSEPEELEEQGVRVAFLELGNTQIELLEPLGEDSPIAKFldkkGGGLHHIAFEVDDI 82

                         90       100
                 ....*....|....*....|....
gi 491376449  81 EALHEKHQAAGFDVTDLKGLPGTS 104
Cdd:cd07249   83 DAAVEELKAQGVRLLSEGPRIGAH 106
FosA cd07244
fosfomycin resistant protein subfamily FosA; This subfamily family contains FosA, a fosfomycin ...
 5-120 3.97e-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: 45.35  E-value: 3.97e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491376449   5 HTCVRVKDLTASLDFYQTAFGFEESRRRDfpehqfTLVYLTLPGddyeLELTYNYDHPGYELGDgYGHIA--ISTDDLEA 82
Cdd:cd07244    4 HITLAVSDLERSLAFYVDLLGFKPHVRWD------KGAYLTAGD----LWLCLSLDPAAEPSPD-YTHIAftVSEEDFEE 72

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 491376449  83 LHEKHQAAGfdVTDLKGLPGTSPSYYFVkDPDGYKIEV 120
Cdd:cd07244   73 LSERLRAAG--VKIWQENSSEGDSLYFL-DPDGHKLEL 107
FosB cd08363
fosfomycin resistant protein subfamily FosB; This subfamily family contains FosB, a fosfomycin ...
 5-120 1.13e-06

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: 44.26  E-value: 1.13e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491376449   5 HTCVRVKDLTASLDFYQTAFGfeesrrRDFPEHQFTLVYLTLPGddYELELTYNYDHPGYELGDGYGHIAISTD--DLEA 82
Cdd:cd08363    3 HITFSVSNLNKSIAFYKDVLD------AKLLVLGEKTAYFDLNG--LWLALNVQEDIPRNEISHSYTHIAFSIDeeDLDA 74

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 491376449  83 LHEKHQAAGfdVTDLKGLP---GTSPSYYFvKDPDGYKIEV 120
Cdd:cd08363   75 FKERLKDNG--VNILEGRKrdiLEGQSIYF-TDPDGHLFEL 112
PRK04101 PRK04101
metallothiol transferase FosB;
5-120 1.18e-06

metallothiol transferase FosB;


Pssm-ID: 179740  Cd Length: 139  Bit Score: 44.55  E-value: 1.18e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491376449   5 HTCVRVKDLTASLDFYQTAFGFE---ESRrrdfpehqfTLVYLTLPGddYELELTYNYDHPGYELGDGYGHIA--ISTDD 79
Cdd:PRK04101   7 HICFSVSNLEKSIEFYEKVLGAKllvKGR---------KTAYFDLNG--LWIALNEEKDIPRNEIHQSYTHIAfsIEEED 75

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 491376449  80 LEALHEKHQAAgfDVTDLKGLP---GTSPSYYFVkDPDGYKIEV 120
Cdd:PRK04101  76 FDHWYQRLKEN--DVNILPGRErdeRDKKSIYFT-DPDGHKFEF 116
VOC_like cd07254
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 5-120 7.45e-06

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


Pssm-ID: 319917 [Multi-domain]  Cd Length: 120  Bit Score: 42.06  E-value: 7.45e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491376449   5 HTCVRVKDLTASLDFYQTAFGFEESRRRD------FPEHQFTLVYLTLPGDDyeleltynydhpgyelGDGYGHIAISTD 78
Cdd:cd07254    4 HLSLNVTDLERSIRFYSDLFGAEPAKRKAdyakfmLEDPPLNLALLVNDRKE----------------PYGLNHLGIQVD 67

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 491376449  79 DLEALH-EKHQ--AAGFDVTDlkgLPGTSPSY-----YFVKDPDGYKIEV 120
Cdd:cd07254   68 SKEEVAaLKARaeAAGLPVRK---EPRTTCCYavqdkFWLTDPDGNAWEF 114
HppD COG3185
4-hydroxyphenylpyruvate dioxygenase and related hemolysins [Amino acid transport and ...
 7-124 1.02e-05

4-hydroxyphenylpyruvate dioxygenase and related hemolysins [Amino acid transport and metabolism, General function prediction only];


Pssm-ID: 442418 [Multi-domain]  Cd Length: 333  Bit Score: 42.95  E-value: 1.02e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491376449   7 CVRVKDLTASLDFYQTAFGFEESRRRDFPEHQfTLVY---LTLPGDDYELEL-----------TYNYDHPgyelGDGYGH 72
Cdd:COG3185  153 AVPRGDLDEWVLFYEDVLGFEEIREEDIEDPY-QGVRsavLQSPDGKVRIPLneptspdsqiaEFLEKYR----GEGIQH 227

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 491376449  73 IAISTDDLEALHEKHQAAGFDVTDlkglpgTSPSYYFVKDP----DGYKIEVIREK 124
Cdd:COG3185  228 IAFATDDIEATVAALRARGVRFLD------IPDNYYDDLEPrvgaHGEDVAFLHPK 277
BphC-JF8_N_like cd09013
N-terminal, non-catalytic, domain of BphC_JF8, (2,3-dihydroxybiphenyl 1,2-dioxygenase) from ...
 2-123 1.19e-05

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: 41.57  E-value: 1.19e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491376449   2 KMAHTCVRVKDLTASLDFYQTAFGFEESRRRDfpehqfTLVYLTLPGD--DYELELTYNYDhpgyelgDGYGHIAISTD- 78
Cdd:cd09013    6 QLAHVELLTPKPEESLWFFTDVLGLEETHREG------QSVYLRAWGDweHHTLKLTESPE-------AGLGHIAWRASs 72

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 491376449  79 --DLEALHEKHQAAGFDVTDLKGLPGTSPSYYFvKDPDGYKIEVIRE 123
Cdd:cd09013   73 peALERRVAALEASGVGIGWIDGDLGQGPAYRF-QSPDGHPMEIYWE 118
Fosfomycin_RP cd08345
Fosfomycin resistant protein; This family contains three types of fosfomycin resistant protein. ...
 5-119 1.89e-05

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


Pssm-ID: 319933  Cd Length: 118  Bit Score: 41.00  E-value: 1.89e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491376449   5 HTCVRVKDLTASLDFYQTAFGFEESRRRDfpEHQFTL---VYLTLPGddyeLELTYNYDHPGYElgDGYGHIAISTDDLE 81
Cdd:cd08345    1 HITLIVRDLEKSTAFLQDIFGAREVYSSG--DKTFSLskeKFFLLGG----LWIALMEGESLQE--RSYTHIAFQIQSED 72

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 491376449  82 ALHEKHQAAGFDVTDLKGLP---GTSPSYYFVkDPDGYKIE 119
Cdd:cd08345   73 FDRYAERLGALGVEMRPPRPrveGEGRSIYFY-DPDNHLFE 112
VOC_BsYyaH cd07241
vicinal oxygen chelate (VOC) family protein similar to Bacillus subtilis YyaH; The vicinal ...
 2-120 4.16e-05

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


Pssm-ID: 319905  Cd Length: 125  Bit Score: 40.09  E-value: 4.16e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491376449   2 KMAHTCVRVKDLTASLDFYQTAFGFEESRRRDFPEHQFTLVYLTLpGDDYELEL---TYNYDHPGYELGDGYGHIAISTD 78
Cdd:cd07241    1 KIEHVALWTNDLERMKDFYVKYFGAESNDIYHNKKKGFRSYFLTF-DSGARLELmsrPDVTDPDKEVERTGLAHIAFSVG 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 491376449  79 DLEA---LHEKHQAAGFDVTdlkGLPGTSPSYYF---VKDPDGYKIEV 120
Cdd:cd07241   80 SKEAvdeLTERLRADGYAVV---GGPRTTGDGYYesvILDPEGNRIEI 124
GLOD4_N cd08358
N-terminal domain of human glyoxalase domain-containing protein 4 and similar proteins; ...
 49-123 4.65e-05

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: 40.04  E-value: 4.65e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 491376449  49 DDYELELTYNYDHPGYELGDGYGHIAISTDDLEALHEKHQaagFDVTDlkglpgTSPSYYFVKDPDGYKIEVIRE 123
Cdd:cd08358   62 DHFVVELTYNYGIGDYELGNDFLGITIHSKQAVSRAKKHN---WPVTQ------VGDGVYEVKAPGGYKFYLIDK 127
VOC_like cd08354
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 6-120 1.24e-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: 1.24e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491376449   6 TCVRVKDLTASLDFYQTAFG---FEESRRRDFPEHQFTLVYLTLPGDDYelELTYNYDHPGYElGDGYGHIA--ISTDDL 80
Cdd:cd08354    4 TCLYADDLDAAEAFYEDVLGlkpMLRSGRHAFFRLGPQVLLVFDPGATS--KDVRTGEVPGHG-ASGHGHFAfaVPTEEL 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 491376449  81 EALHEKHQAAGFDVTDLKGLPGTSPSYYFvKDPDGYKIEV 120
Cdd:cd08354   81 AAWEARLEAKGVPIESYTQWPEGGKSLYF-RDPAGNLVEL 119
VOC_like cd07264
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 3-120 2.20e-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: 319925 [Multi-domain]  Cd Length: 118  Bit Score: 38.08  E-value: 2.20e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491376449   3 MAHTCVRVKDLTASLDFYQTAFGFEESRrrdfpeHQFTLVYLTLPGDDYELELTYNYDHPGYELGDGYGH---IAISTDD 79
Cdd:cd07264    1 IAYIVLYVDDFAASLRFYRDVLGLPPRF------LHEEGEYAEFDTGETKLALFSRKEMARSGGPDRRGSafeLGFEVDD 74

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 491376449  80 LEALHEKHQAAGFDVtdlKGLPGTSP---SYYFVKDPDGYKIEV 120
Cdd:cd07264   75 VEATVEELVERGAEF---VREPANKPwgqTVAYVRDPDGNLIEI 115
COG3607 COG3607
Lactoylglutathione lyase-related enzyme, vicinal oxygen chelate (VOC) family [General function ...
 10-120 3.71e-04

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


Pssm-ID: 442825  Cd Length: 126  Bit Score: 37.50  E-value: 3.71e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491376449  10 VKDLTASLDFYqTAFGFEesRRRDFPEHQFTLVYLtlpGDDYELELtynYDHPGY------ELGDGYGH----IAISTD- 78
Cdd:COG3607   11 VADLERSRAFY-EALGFT--FNPQFSDEGAACFVL---GEGIVLML---LPREKFatftgkPIADATGFtevlLALNVEs 81

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 491376449  79 --DLEALHEKHQAAGFDVTdlkGLPGTSPSYY--FVKDPDGYKIEV 120
Cdd:COG3607   82 reEVDALVAKALAAGGTVL---KPPQDVGGMYsgYFADPDGHLWEV 124
GLOD5 cd07253
Human glyoxalase domain-containing protein 5 and similar proteins; Uncharacterized subfamily ...
 2-120 7.15e-04

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: 36.82  E-value: 7.15e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491376449   2 KMAHTCVRVKDLTASLDFYQTAFGFEESR-RRDFPEHQFTLVYLTLPGDDYELELTYNYDHPgyelgdGYGHIAISTDDL 80
Cdd:cd07253    3 RLDHLVLTVKDIERTIDFYTKVLGMTVVTfKEGRKALRFGNQKINLHQKGKEFEPKASAPTP------GSADLCFITETP 76

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 491376449  81 EALHEKHQAAgFDVTDLKGlP-------GTSPSYYFvKDPDGYKIEV 120
Cdd:cd07253   77 IDEVLEHLEA-CGVTIEEG-PvkrtgalGPILSIYF-RDPDGNLIEL 120
GLOD4_C cd16357
C-terminal domain of human glyoxalase domain-containing protein 4 and similar proteins; ...
 7-118 7.66e-04

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


Pssm-ID: 319964  Cd Length: 114  Bit Score: 36.38  E-value: 7.66e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491376449   7 CVRVKDLTASLDFYQTAFGFEESRRRD------FPEHQFTLVYLTLPGDdyeleltynYDHpgyelGDGYGHIAIS--TD 78
Cdd:cd16357    3 SLAVSDLEKSIDYWSDLLGMKVFEKSEksallgYGEDQAKLELVDIPEP---------VDH-----GTAFGRIAFScpAD 68

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 491376449  79 DLEALHEKHQAAGFDV-TDLKGL--PGtspsyyfvK---------DPDGYKI 118
Cdd:cd16357   69 ELPPIEEKVKAAGQTIlTPLVSLdtPG--------KatvqvvilaDPDGHEI 112
Glyoxalase_3 pfam13468
Glyoxalase-like domain; This domain is related to the Glyoxalase domain pfam00903.
 5-94 8.46e-04

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


Pssm-ID: 433233  Cd Length: 175  Bit Score: 36.93  E-value: 8.46e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491376449    5 HTCVRVKDLTASLDFYQTAFGFEESRRRdfpEHQF-----TLVYLtlpGDDY-ELeLTYNYDHPG-----------YELG 67
Cdd:pfam13468   3 HVVLAVPDLDEAAARFARALGFTVTPGG---RHPGmgtanALIMF---GDGYlEL-LAVDPEAPApprgrwfgldrLADG 75

                          90       100
                  ....*....|....*....|....*..
gi 491376449   68 DGYGHIAISTDDLEALHEKHQAAGFDV 94
Cdd:pfam13468  76 EGLLGWALRTDDIDAVAARLRAAGVEP 102
MRD cd07235
Mitomycin C resistance protein (MRD); Mitomycin C (MC) is a naturally occurring antibiotic, ...
 10-120 1.01e-03

Mitomycin C resistance protein (MRD); Mitomycin C (MC) is a naturally occurring antibiotic, and antitumor agent used in the treatment of cancer. Its antitumor activity is exerted primarily through monofunctional and bifunctional alkylation of DNA. MRD binds to MC and functions as a component of the MC exporting system. MC is bound to MRD by a stacking interaction between a His and a Trp. MRD adopts a structural fold similar to bleomycin resistance protein, glyoxalase I, and extradiol dioxygenases; and it has binding sites at an identical location to binding sites in these evolutionarily related enzymes.


Pssm-ID: 319901  Cd Length: 123  Bit Score: 36.32  E-value: 1.01e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491376449  10 VKDLTASLDFYQTaFGFEESRRRDFPEHqftlVYLTLPG------DDYELELTYnydHPGYELGDGYGHIAIS-----TD 78
Cdd:cd07235    8 VEDMAKSLEFYRK-LGFEVPEEADSAPH----TEAALPGgirlalDTEETIRSY---DPGWQAPTGGGRFAIAflcptPA 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 491376449  79 DLEALHEKHQAAGFDVTdLKglPGTSP---SYYFVKDPDGYKIEV 120
Cdd:cd07235   80 EVDAKYAELTGAGYEGH-LK--PWNAPwgqRYAIVKDPDGNVVDL 121
ED_TypeI_classII_N cd16360
N-terminal domain of type I, class II extradiol dioxygenases; This family contains the ...
 5-121 1.66e-03

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: 35.37  E-value: 1.66e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491376449   5 HTCVRVKDLTASLDFYQTAFGFEESRRRDfpehqfTLVYLTLPGDDYELELTYNYDHPGYelgDGYGHIAISTDDLEALH 84
Cdd:cd16360    1 YAELGVPDLEKALEFYTDVLGLQVAKRDG------NSVYLRGYEDEHHSLVLYEAPEAGL---KHFAFEVASEEDLERAA 71

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 491376449  85 EKHQAAGFDVTDLKGLPGTSPSYYF-VKDPDGYKIEVI 121
Cdd:cd16360   72 ASLTALGCDVTWGPDGEVPGGGKGFrFQDPSGHLLELF 109
Glyoxalase_6 pfam18029
Glyoxalase-like domain; This entry comprises a diverse set of domains related to the ...
 5-115 4.67e-03

Glyoxalase-like domain; This entry comprises a diverse set of domains related to the Glyoxalase domain. The exact specificity of these proteins is uncertain.


Pssm-ID: 436220  Cd Length: 110  Bit Score: 34.28  E-value: 4.67e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491376449    5 HTCVRVKDLTASLDFYQTAFGFEESRRRDFPEHQFTLVYLTLPGDDYELELTynydhPGYELGDGYGHIAISTDDLEALH 84
Cdd:pfam18029   1 AVVLDCADPAALAAFWSAALGWEVVPDDTALPDPDGGGPIGGGGPRLLFQRV-----PEPKPGKNRVHLDLAVDDLEAAV 75

                          90       100       110
                  ....*....|....*....|....*....|.
gi 491376449   85 EKHQAAGFDVTDLKGLPGTSPSYYfvKDPDG 115
Cdd:pfam18029  76 ARLVALGATVLDDGDDPDGGRWVL--ADPEG 104
PcpA_C_like cd08347
C-terminal domain of Sphingobium chlorophenolicum 2,6-dichloro-p-hydroquinone 1,2-dioxygenase ...
 8-120 6.50e-03

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


Pssm-ID: 319935  Cd Length: 157  Bit Score: 34.53  E-value: 6.50e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491376449   8 VRVKDLTASLDFYQTAFGFEESRRRDfpehqfTLVYLTLPGDDYELELTYnYDHPGYELG-DGYG---HIAISTDDLE-- 81
Cdd:cd08347    7 LTVREPEETDAFLTNVFGFTEVGEEG------DLVRLFAGGNGSGGVVDV-LDDPDLPSAqQGYGtvhHVAFRVADDEeq 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 491376449  82 -ALHEKHQAAGFDVTDLKGlpgtspSYYF----VKDPDGYKIEV 120
Cdd:cd08347   80 aAWKERLEELGFDNSGIVD------RFYFeslyFREPGGVLFEI 117
BLMT_like cd08350
BLMT, a bleomycin resistance protein encoded on the transposon Tn5, and similar proteins; BLMT ...
 11-123 6.90e-03

BLMT, a bleomycin resistance protein encoded on the transposon Tn5, and similar proteins; BLMT is a bleomycin (Bm) resistance protein, encoded by the ble gene on the transposon Tn5. This protein confers a survival advantage to Escherichia coli host cells. 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. BLMT has strong binding affinity to Bm and it protects against this lethal compound through drug sequestering. BLMT has two identically-folded subdomains, with the same alpha/beta fold; these two halves have no sequence similarity. BLMT is a dimer with two Bm-binding pockets formed at the dimer interface.


Pssm-ID: 319938  Cd Length: 118  Bit Score: 33.79  E-value: 6.90e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491376449  11 KDLTASLDFYQtAFGFEESRRRDfpehqftlVYLTLPGDDYELELtynYDHPGYELGDGYGHIAISTDDLEALHEKHQAA 90
Cdd:cd08350   11 RDFDATAAFYA-RLGFQTVYRDD--------GWMILRRGDLTLEF---FPHPDLDPAASWFSCCLRVDDLDALYAQWSAA 78

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 491376449  91 GFD--------VTDLKGLPGtSPSYYFVKDPDGYKIEVIRE 123
Cdd:cd08350   79 GIPedtrgiprLHPPQTQPW-GIRMFALIDPDGSLLRLIQN 118
 
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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