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Conserved domains on  [gi|639298388|ref|WP_024589304|]
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MULTISPECIES: lactoylglutathione lyase [Pseudoalteromonas]

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 ...
 14-172 2.67e-93

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 PLN03042:

Pssm-ID: 472697  Cd Length: 185  Bit Score: 269.00  E-value: 2.67e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639298388  14 ATQGFVMQQTMLRIKDPKPSLEFYQNVLGMKLLGKYDFPGMKFTLYFLGYEQELPQGDDKT-KAEWVFRRPALIELTHNW 92
Cdd:PLN03042  22 ATKGYIMQQTMFRIKDPKASLDFYSRVLGMSLLKRLDFPEMKFSLYFLGYEDSETAPTDPPeRTVWTFGRKATIELTHNW 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639298388  93 GTESDDSFEGYHSGNQEPKGFGHIGISVPDVYEACERFAKYDVEFVKKPDDGSMKGLAFIKDPDGYWIEILSAEGITEII 172
Cdd:PLN03042 102 GTESDPEFKGYHNGNSDPRGFGHIGITVDDVYKACERFEKLGVEFVKKPDDGKMKGLAFIKDPDGYWIEIFDLKRIGGIT 181
 
Name Accession Description Interval E-value
PLN03042 PLN03042
Lactoylglutathione lyase; Provisional
 14-172 2.67e-93

Lactoylglutathione lyase; Provisional


Pssm-ID: 215548  Cd Length: 185  Bit Score: 269.00  E-value: 2.67e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639298388  14 ATQGFVMQQTMLRIKDPKPSLEFYQNVLGMKLLGKYDFPGMKFTLYFLGYEQELPQGDDKT-KAEWVFRRPALIELTHNW 92
Cdd:PLN03042  22 ATKGYIMQQTMFRIKDPKASLDFYSRVLGMSLLKRLDFPEMKFSLYFLGYEDSETAPTDPPeRTVWTFGRKATIELTHNW 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639298388  93 GTESDDSFEGYHSGNQEPKGFGHIGISVPDVYEACERFAKYDVEFVKKPDDGSMKGLAFIKDPDGYWIEILSAEGITEII 172
Cdd:PLN03042 102 GTESDPEFKGYHNGNSDPRGFGHIGITVDDVYKACERFEKLGVEFVKKPDDGKMKGLAFIKDPDGYWIEIFDLKRIGGIT 181
GlxI_Zn cd07233
Glyoxalase I that uses Zn(++) as cofactor; This family includes eukaryotic glyoxalase I that ...
 20-163 2.11e-87

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: 252.25  E-value: 2.11e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639298388  20 MQQTMLRIKDPKPSLEFYQNVLGMKLLGKYDFPGMKFTLYFLGYEQELPQGDDKTKAeWVFRRPALIELTHNWGTESDDS 99
Cdd:cd07233    1 FNHTMLRVKDPKKSLKFYTEVLGMKLLRKKDFPEMKFSLYFLGYEDPKDIPKDPRTA-WVFSREGTLELTHNWGTENDED 79

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 639298388 100 FEgYHSGNQEPKGFGHIGISVPDVYEACERFAKYDVEFVKKPDDGSMKGLAFIKDPDGYWIEIL 163
Cdd:cd07233   80 PV-YHNGNSDPRGFGHIGIAVDDVYAACERFEELGVKFKKKPDDGKMKGIAFIKDPDGYWIEIL 142
glyox_I TIGR00068
lactoylglutathione lyase; Lactoylglutathione lyase is also known as aldoketomutase and ...
 14-163 3.76e-62

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: 188.86  E-value: 3.76e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639298388   14 ATQGFVMQQTMLRIKDPKPSLEFYQNVLGMKLLGKYDFPGMKFTLYFLGYEqelpqgdDKTKAewvfrrpALIELTHNWG 93
Cdd:TIGR00068  12 KTKKRRLLHTMLRVGDLDKSLDFYTEVLGMKLLRKRDFPEMKFSLAFLGYG-------DETSA-------AVIELTHNWG 77

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 639298388   94 TESddsfegYHSGNqepkGFGHIGISVPDVYEACERFAKYDVEFVKK--PDDGSMKGLAFIKDPDGYWIEIL 163
Cdd:TIGR00068  78 TEK------YDLGN----GFGHIAIGVDDVYKACERVRALGGNVVREpgPVKGGTTVIAFVEDPDGYKIELI 139
GloA COG0346
Catechol 2,3-dioxygenase or related enzyme, vicinal oxygen chelate (VOC) family [Secondary ...
 23-167 3.83e-27

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: 98.91  E-value: 3.83e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639298388  23 TMLRIKDPKPSLEFYQNVLGMKLLGKYDFPGMKFTLYFLGYEQelpqgddktkaewvfrrPALIELTHNWGTESDDsfeg 102
Cdd:COG0346    6 VTLRVSDLEASLAFYTDVLGLELVKRTDFGDGGFGHAFLRLGD-----------------GTELELFEAPGAAPAP---- 64

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 639298388 103 yhsgnqEPKGFGHIGISVPDVYEACERFAKYDVEFVKKPDDG-SMKGLAFIKDPDGYWIEILSAEG 167
Cdd:COG0346   65 ------GGGGLHHLAFRVDDLDAAYARLRAAGVEIEGEPRDRaYGYRSAYFRDPDGNLIELVEPPP 124
Glyoxalase pfam00903
Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;
22-162 3.29e-24

Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;


Pssm-ID: 395724 [Multi-domain]  Cd Length: 121  Bit Score: 91.36  E-value: 3.29e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639298388   22 QTMLRIKDPKPSLEFYQNVLGMKLLGKYDFPGMkftlyflgyeqelpqgdDKTKAEWVFRRPALIELTHNWGTESDDSFE 101
Cdd:pfam00903   4 HVALRVGDLEKSLDFYTDVLGFKLVEETDAGEE-----------------GGLRSAFFLAGGRVLELLLNETPPPAAAGF 66

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 639298388  102 GYHsgnqepkGFGHIGISVPDVYEACERFAKYDVEFVKKPDDGSMKGLAF-IKDPDGYWIEI 162
Cdd:pfam00903  67 GGH-------HIAFIAFSVDDVDAAYDRLKAAGVEIVREPGRHGWGGRYSyFRDPDGNLIEL 121
 
Name Accession Description Interval E-value
PLN03042 PLN03042
Lactoylglutathione lyase; Provisional
 14-172 2.67e-93

Lactoylglutathione lyase; Provisional


Pssm-ID: 215548  Cd Length: 185  Bit Score: 269.00  E-value: 2.67e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639298388  14 ATQGFVMQQTMLRIKDPKPSLEFYQNVLGMKLLGKYDFPGMKFTLYFLGYEQELPQGDDKT-KAEWVFRRPALIELTHNW 92
Cdd:PLN03042  22 ATKGYIMQQTMFRIKDPKASLDFYSRVLGMSLLKRLDFPEMKFSLYFLGYEDSETAPTDPPeRTVWTFGRKATIELTHNW 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639298388  93 GTESDDSFEGYHSGNQEPKGFGHIGISVPDVYEACERFAKYDVEFVKKPDDGSMKGLAFIKDPDGYWIEILSAEGITEII 172
Cdd:PLN03042 102 GTESDPEFKGYHNGNSDPRGFGHIGITVDDVYKACERFEKLGVEFVKKPDDGKMKGLAFIKDPDGYWIEIFDLKRIGGIT 181
GlxI_Zn cd07233
Glyoxalase I that uses Zn(++) as cofactor; This family includes eukaryotic glyoxalase I that ...
 20-163 2.11e-87

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: 252.25  E-value: 2.11e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639298388  20 MQQTMLRIKDPKPSLEFYQNVLGMKLLGKYDFPGMKFTLYFLGYEQELPQGDDKTKAeWVFRRPALIELTHNWGTESDDS 99
Cdd:cd07233    1 FNHTMLRVKDPKKSLKFYTEVLGMKLLRKKDFPEMKFSLYFLGYEDPKDIPKDPRTA-WVFSREGTLELTHNWGTENDED 79

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 639298388 100 FEgYHSGNQEPKGFGHIGISVPDVYEACERFAKYDVEFVKKPDDGSMKGLAFIKDPDGYWIEIL 163
Cdd:cd07233   80 PV-YHNGNSDPRGFGHIGIAVDDVYAACERFEELGVKFKKKPDDGKMKGIAFIKDPDGYWIEIL 142
PLN02367 PLN02367
lactoylglutathione lyase
 12-168 2.60e-87

lactoylglutathione lyase


Pssm-ID: 177995  Cd Length: 233  Bit Score: 255.69  E-value: 2.60e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639298388  12 EQATQGFVMQQTMLRIKDPKPSLEFYQNVLGMKLLGKYDFPGMKFTLYFLGYEQELPQGDDKT-KAEWVFRRPALIELTH 90
Cdd:PLN02367  68 DEATKGYIMQQTMYRIKDPKASLDFYSRVLGMSLLKRLDFPEMKFSLYFMGYEDTASAPTDPTeRTVWTFGQKATIELTH 147

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 639298388  91 NWGTESDDSFEGYHSGNQEPKGFGHIGISVPDVYEACERFAKYDVEFVKKPDDGSMKGLAFIKDPDGYWIEILSAEGI 168
Cdd:PLN02367 148 NWGTESDPDFKGYHNGNSEPRGFGHIGITVDDVYKACERFEELGVEFVKKPNDGKMKGIAFIKDPDGYWIEIFDLKTI 225
glyox_I TIGR00068
lactoylglutathione lyase; Lactoylglutathione lyase is also known as aldoketomutase and ...
 14-163 3.76e-62

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: 188.86  E-value: 3.76e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639298388   14 ATQGFVMQQTMLRIKDPKPSLEFYQNVLGMKLLGKYDFPGMKFTLYFLGYEqelpqgdDKTKAewvfrrpALIELTHNWG 93
Cdd:TIGR00068  12 KTKKRRLLHTMLRVGDLDKSLDFYTEVLGMKLLRKRDFPEMKFSLAFLGYG-------DETSA-------AVIELTHNWG 77

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 639298388   94 TESddsfegYHSGNqepkGFGHIGISVPDVYEACERFAKYDVEFVKK--PDDGSMKGLAFIKDPDGYWIEIL 163
Cdd:TIGR00068  78 TEK------YDLGN----GFGHIAIGVDDVYKACERVRALGGNVVREpgPVKGGTTVIAFVEDPDGYKIELI 139
GlxI_Ni cd16358
Glyoxalase I that uses Ni(++) as cofactor; This family includes Escherichia coil and other ...
 20-163 1.35e-37

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: 125.59  E-value: 1.35e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639298388  20 MQQTMLRIKDPKPSLEFYQNVLGMKLLGKYDFPGMKFTLYFLGYEQElpqgddktkaewvfRRPALIELTHNWGTESdds 99
Cdd:cd16358    1 MLHTMLRVGDLDRSIKFYTEVLGMKLLRKRDYPEGKYTLAFVGYGDE--------------DENTVLELTYNWGVDK--- 63

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 639298388 100 fegYHSGNqepkGFGHIGISVPDVYEACERFAKYDVEFVKKPddGSMKG----LAFIKDPDGYWIEIL 163
Cdd:cd16358   64 ---YDLGT----AYGHIAIGVEDVYETCERIRKKGGKVTREP--GPMKGgttvIAFVEDPDGYKIELI 122
GloA COG0346
Catechol 2,3-dioxygenase or related enzyme, vicinal oxygen chelate (VOC) family [Secondary ...
 23-167 3.83e-27

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: 98.91  E-value: 3.83e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639298388  23 TMLRIKDPKPSLEFYQNVLGMKLLGKYDFPGMKFTLYFLGYEQelpqgddktkaewvfrrPALIELTHNWGTESDDsfeg 102
Cdd:COG0346    6 VTLRVSDLEASLAFYTDVLGLELVKRTDFGDGGFGHAFLRLGD-----------------GTELELFEAPGAAPAP---- 64

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 639298388 103 yhsgnqEPKGFGHIGISVPDVYEACERFAKYDVEFVKKPDDG-SMKGLAFIKDPDGYWIEILSAEG 167
Cdd:COG0346   65 ------GGGGLHHLAFRVDDLDAAYARLRAAGVEIEGEPRDRaYGYRSAYFRDPDGNLIELVEPPP 124
Glyoxalase pfam00903
Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;
22-162 3.29e-24

Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;


Pssm-ID: 395724 [Multi-domain]  Cd Length: 121  Bit Score: 91.36  E-value: 3.29e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639298388   22 QTMLRIKDPKPSLEFYQNVLGMKLLGKYDFPGMkftlyflgyeqelpqgdDKTKAEWVFRRPALIELTHNWGTESDDSFE 101
Cdd:pfam00903   4 HVALRVGDLEKSLDFYTDVLGFKLVEETDAGEE-----------------GGLRSAFFLAGGRVLELLLNETPPPAAAGF 66

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 639298388  102 GYHsgnqepkGFGHIGISVPDVYEACERFAKYDVEFVKKPDDGSMKGLAF-IKDPDGYWIEI 162
Cdd:pfam00903  67 GGH-------HIAFIAFSVDDVDAAYDRLKAAGVEIVREPGRHGWGGRYSyFRDPDGNLIEL 121
PRK10291 PRK10291
glyoxalase I; Provisional
 24-166 2.42e-23

glyoxalase I; Provisional


Pssm-ID: 182358  Cd Length: 129  Bit Score: 89.31  E-value: 2.42e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639298388  24 MLRIKDPKPSLEFYQNVLGMKLLGKYDFPGMKFTLYFLGYEQELPQgddktkaewvfrrpALIELTHNWGTESddsfegY 103
Cdd:PRK10291   1 MLRVGDLQRSIDFYTNVLGMKLLRTSENPEYKYSLAFVGYGPETEE--------------AVIELTYNWGVDK------Y 60

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 639298388 104 HSGNqepkGFGHIGISVPDVYEACERFAKYDVEFVKK--PDDGSMKGLAFIKDPDGYWIEILSAE 166
Cdd:PRK10291  61 ELGT----AYGHIALSVDNAAEACEKIRQNGGNVTREagPVKGGTTVIAFVEDPDGYKIELIEEK 121
PLN02300 PLN02300
lactoylglutathione lyase
 20-170 4.22e-19

lactoylglutathione lyase


Pssm-ID: 215169 [Multi-domain]  Cd Length: 286  Bit Score: 81.75  E-value: 4.22e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639298388  20 MQQTMLRIKDPKPSLEFYQNVLGMKLLGKYDFPGMKFTLYFLGYEQElpqgddktKAEWVfrrpalIELTHNWGTESdds 99
Cdd:PLN02300  25 MLHVVYRVGDLDRTIKFYTECLGMKLLRKRDIPEEKYTNAFLGYGPE--------DSNFV------VELTYNYGVDK--- 87

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 639298388 100 fegYHSGNqepkGFGHIGISVPDVYEACERFAKYDVEFVKKPddGSMKG----LAFIKDPDGYWIEILSAEGITE 170
Cdd:PLN02300  88 ---YDIGT----GFGHFGIAVEDVAKTVELVKAKGGKVTREP--GPVKGgksvIAFVKDPDGYKFELIQRGPTPE 153
PLN02300 PLN02300
lactoylglutathione lyase
 22-158 1.28e-14

lactoylglutathione lyase


Pssm-ID: 215169 [Multi-domain]  Cd Length: 286  Bit Score: 69.81  E-value: 1.28e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639298388  22 QTMLRIKDPKPSLEFYQNVLGMKLLGKYDFPGMKFTLYFLGYEQElpqgdDKTkaewvfrrpALIELTHNWG-TEsddsf 100
Cdd:PLN02300 157 QVMLRVGDLDRSIKFYEKAFGMKLLRKRDNPEYKYTIAMMGYGPE-----DKT---------TVLELTYNYGvTE----- 217

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 639298388 101 egYHSGNqepkGFGHIGISVPDVYEACERFAKYDVEFVKKPddGSMKGL-----AFIkDPDGY 158
Cdd:PLN02300 218 --YTKGN----AYAQIAIGTDDVYKTAEAIKLVGGKITREP--GPLPGIntkitACL-DPDGW 271
VOC cd06587
vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate (VOC) superfamily is composed ...
 23-162 1.32e-11

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: 58.31  E-value: 1.32e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639298388  23 TMLRIKDPKPSLEFYQNVLGMKLLgkYDFPGMKFTLYFLGYEQELpqgddktkaewvfrrpaliELthnwgtesddsFEG 102
Cdd:cd06587    2 VALRVPDLDASVAFYEEVLGFEVV--SRNEGGGFAFLRLGPGLRL-------------------AL-----------LEG 49

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 639298388 103 YHSGNQEPKGFGHIGISVPDVYEACERFAKYDVEFVKK---PDDGSMKGLAFIKDPDGYWIEI 162
Cdd:cd06587   50 PEPERPGGGGLFHLAFEVDDVDEVDERLREAGAEGELVappVDDPWGGRSFYFRDPDGNLIEF 112
CatE COG2514
Catechol-2,3-dioxygenase [Secondary metabolites biosynthesis, transport and catabolism];
25-162 2.71e-07

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


Pssm-ID: 442004 [Multi-domain]  Cd Length: 141  Bit Score: 47.26  E-value: 2.71e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639298388  25 LRIKDPKPSLEFYQNVLGMKLLGKYDfpgmkfTLYFLGYEqelpqGDDktkaewvfrrpALIELTHNwgtesddsfeGYH 104
Cdd:COG2514    9 LRVRDLERSAAFYTDVLGLEVVEREG------GRVYLRAD-----GGE-----------HLLVLEEA----------PGA 56

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 639298388 105 SGNQEPKGFGHIGISVP---DVYEACERFAKYDVEFVKKPDDGSMKGLAFiKDPDGYWIEI 162
Cdd:COG2514   57 PPRPGAAGLDHVAFRVPsraDLDAALARLAAAGVPVEGAVDHGVGESLYF-RDPDGNLIEL 116
VOC COG3324
Lactoylglutathione lyase-related enzyme, vicinal oxygen chelate (VOC) family [General function ...
 25-167 3.82e-06

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


Pssm-ID: 442553 [Multi-domain]  Cd Length: 119  Bit Score: 43.86  E-value: 3.82e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639298388  25 LRIKDPKPSLEFYQNVLGMKLLGKYDFPGmkftlyflGYeqelpqgddktkaeWVFRRPALIELthnwgtesddsfeGYH 104
Cdd:COG3324   10 LPVDDLERAKAFYEEVFGWTFEDDAGPGG--------DY--------------AEFDTDGGQVG-------------GLM 54

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 639298388 105 SGNQEPKGFG-HIGISVPDVYEACERFAKYDVEFVKKPDDGSMKG-LAFIKDPDGYWIEILSAEG 167
Cdd:COG3324   55 PGAEEPGGPGwLLYFAVDDLDAAVARVEAAGGTVLRPPTDIPPWGrFAVFRDPEGNRFGLWQPAA 119
VOC_like cd07245
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 25-162 2.04e-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: 319909 [Multi-domain]  Cd Length: 117  Bit Score: 41.92  E-value: 2.04e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639298388  25 LRIKDPKPSLEFYQNVLGMKLLGKYDFPGMKFTLYFLGYEQELpqgddktkaewvfrrpALIELTHNwgtesDDSFEGYH 104
Cdd:cd07245    6 LACPDLERARRFYTDVLGLEEVPRPPFLKFGGAWLYLGGGQQI----------------HLVVEQNP-----SELPRPEH 64

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 639298388 105 SGNQepkgfGHIGISVPDVYEACERFAKYDVEFVKKPDDGSMKGLAFIKDPDGYWIEI 162
Cdd:cd07245   65 PGRD-----RHPSFSVPDLDALKQRLKEAGIPYTESTSPGGGVTQLFFRDPDGNRLEF 117
VOC_like cd07264
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 22-165 1.92e-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: 39.24  E-value: 1.92e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639298388  22 QTMLRIKDPKPSLEFYQNVLGMKLLGKYDfpgmkftlyflgyeqelpqgdDKTKAEWVFRRPALIELTHNWGTESDdsfe 101
Cdd:cd07264    3 YIVLYVDDFAASLRFYRDVLGLPPRFLHE---------------------EGEYAEFDTGETKLALFSRKEMARSG---- 57

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 639298388 102 gyhsGNQEPKGFGHIGISVPDVYEACERFAKYDVEFVKKPDDgSMKGL--AFIKDPDGYWIEILSA 165
Cdd:cd07264   58 ----GPDRRGSAFELGFEVDDVEATVEELVERGAEFVREPAN-KPWGQtvAYVRDPDGNLIEICEP 118
PcpA_N_like cd08346
N-terminal domain of Sphingobium chlorophenolicum 2,6-dichloro-p-hydroquinone 1,2-dioxygenase ...
 27-157 1.46e-03

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


Pssm-ID: 319934  Cd Length: 124  Bit Score: 36.88  E-value: 1.46e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639298388  27 IKDPKPSLEFYQNVLGMKLLGK---YDFPGMkFTLYFlGYEQELPqGDDKTKAEWVFRRPALielthnwgtesddsfEGY 103
Cdd:cd08346    9 TGDAQENVDFYVKVLGLRLVKKtvnQDDPPM-YHLYY-GDELGSP-GTLLTFFPWPLGGPGR---------------RGT 70

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 639298388 104 HSgnqepkgFGHIGISVP----DVYEacERFAKYDVEFVKKPDDGSMKGLAFiKDPDG 157
Cdd:cd08346   71 GQ-------ISRIGLRVPkgslSFWA--ERLEKFGVPHSEVVTRFGEKYLRF-EDPDG 118
BphC1-RGP6_C_like cd07237
C-terminal domain of 2,3-dihydroxybiphenyl 1,2-dioxygenase; This subfamily contains the ...
 25-62 3.85e-03

C-terminal domain of 2,3-dihydroxybiphenyl 1,2-dioxygenase; This subfamily contains the C-terminal, catalytic, domain of BphC1-RGP6 and similar proteins. BphC catalyzes the extradiol ring cleavage reaction of 2,3-dihydroxybiphenyl, 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. 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. BphC1-RGP6 has an internal duplication, it is a two-domain dioxygenase which forms octamers, and has Fe(II) at the catalytic site. Its C-terminal repeat is represented in this subfamily. BphC2-RGP6 and BphC3-RGP6 are one-domain dioxygenases, they belong to a different subfamily of the ED_TypeI_classII_C (C-terminal domain of type I, class II extradiol dioxygenases) family.


Pssm-ID: 319902  Cd Length: 153  Bit Score: 36.10  E-value: 3.85e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 639298388  25 LRIKDPKPSLEFYQNVLGMKLLGKYDF---PGMKFTLYFLG 62
Cdd:cd07237   15 LIVPDVDEALAFYTDVLGFRLSDEIRIplpPGVTARLHFLH 55
GloA COG0346
Catechol 2,3-dioxygenase or related enzyme, vicinal oxygen chelate (VOC) family [Secondary ...
 111-167 6.13e-03

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: 34.97  E-value: 6.13e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 639298388 111 KGFGHIGISVPDvYEACERFakY-DV---EFVKKPDDGSMK-GLAFIKDPDGYWIEILSAEG 167
Cdd:COG0346    1 MGLHHVTLRVSD-LEASLAF--YtDVlglELVKRTDFGDGGfGHAFLRLGDGTELELFEAPG 59
GLOD4_N cd08358
N-terminal domain of human glyoxalase domain-containing protein 4 and similar proteins; ...
 25-158 8.48e-03

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: 34.65  E-value: 8.48e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639298388  25 LRIKDPKPSLEFYQNVLGMKLL--------------GKYDfpgMKFTLYFLGYEQElpqgDDKtkaewvFrrpaLIELTH 90
Cdd:cd08358    8 FKVGDRNKTIKFYREILGMKVLrheefeegckaacnGPYD---GKWSKTMVGYGPE----DDH------F----VVELTY 70

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 639298388  91 NWGTESddsfegYHSGNQepkgFGHIGISVPDVYEACERfAKYDVEfvKKPDDGSMkglafIKDPDGY 158
Cdd:cd08358   71 NYGIGD------YELGND----FLGITIHSKQAVSRAKK-HNWPVT--QVGDGVYE-----VKAPGGY 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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