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Conserved domains on  [gi|165932331|ref|NP_079650|]
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lactoylglutathione lyase [Mus musculus]

Protein Classification

lactoylglutathione lyase( domain architecture ID 10791519)

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PLN03042 PLN03042
Lactoylglutathione lyase; Provisional
 20-184 3.13e-108

Lactoylglutathione lyase; Provisional


:

Pssm-ID: 215548  Cd Length: 185  Bit Score: 307.13  E-value: 3.13e-108
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165932331  20 CSDPDPSTKDFLLQQTMLRIKDPKKSLDFYTRVLGLTLLQKLDFPAMKFSLYFLAYEDKNDIPKDKSEKTAWTFSRKATL 99
Cdd:PLN03042  16 CGNPDEATKGYIMQQTMFRIKDPKASLDFYSRVLGMSLLKRLDFPEMKFSLYFLGYEDSETAPTDPPERTVWTFGRKATI 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165932331 100 ELTHNWGTEDD-ETQSYHNGNSDPRGFGHIGIAVPDVYSACKRFEELGVKFVKKPDDGKMKGLAFIQDPDGYWIEILNPN 178
Cdd:PLN03042  96 ELTHNWGTESDpEFKGYHNGNSDPRGFGHIGITVDDVYKACERFEKLGVEFVKKPDDGKMKGLAFIKDPDGYWIEIFDLK 175


                 ....*.
gi 165932331 179 KIATII 184
Cdd:PLN03042 176 RIGGIT 181
 
Name Accession Description Interval E-value
PLN03042 PLN03042
Lactoylglutathione lyase; Provisional
 20-184 3.13e-108

Lactoylglutathione lyase; Provisional


Pssm-ID: 215548  Cd Length: 185  Bit Score: 307.13  E-value: 3.13e-108
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165932331  20 CSDPDPSTKDFLLQQTMLRIKDPKKSLDFYTRVLGLTLLQKLDFPAMKFSLYFLAYEDKNDIPKDKSEKTAWTFSRKATL 99
Cdd:PLN03042  16 CGNPDEATKGYIMQQTMFRIKDPKASLDFYSRVLGMSLLKRLDFPEMKFSLYFLGYEDSETAPTDPPERTVWTFGRKATI 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165932331 100 ELTHNWGTEDD-ETQSYHNGNSDPRGFGHIGIAVPDVYSACKRFEELGVKFVKKPDDGKMKGLAFIQDPDGYWIEILNPN 178
Cdd:PLN03042  96 ELTHNWGTESDpEFKGYHNGNSDPRGFGHIGITVDDVYKACERFEKLGVEFVKKPDDGKMKGLAFIKDPDGYWIEIFDLK 175


                 ....*.
gi 165932331 179 KIATII 184
Cdd:PLN03042 176 RIGGIT 181
GlxI_Zn cd07233
Glyoxalase I that uses Zn(++) as cofactor; This family includes eukaryotic glyoxalase I that ...
 32-175 2.59e-102

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: 290.38  E-value: 2.59e-102
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165932331  32 LQQTMLRIKDPKKSLDFYTRVLGLTLLQKLDFPAMKFSLYFLAYEDKNDIPKDksEKTAWTFSRKATLELTHNWGTEDDE 111
Cdd:cd07233    1 FNHTMLRVKDPKKSLKFYTEVLGMKLLRKKDFPEMKFSLYFLGYEDPKDIPKD--PRTAWVFSREGTLELTHNWGTENDE 78

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 165932331 112 TQSYHNGNSDPRGFGHIGIAVPDVYSACKRFEELGVKFVKKPDDGKMKGLAFIQDPDGYWIEIL 175
Cdd:cd07233   79 DPVYHNGNSDPRGFGHIGIAVDDVYAACERFEELGVKFKKKPDDGKMKGIAFIKDPDGYWIEIL 142
glyox_I TIGR00068
lactoylglutathione lyase; Lactoylglutathione lyase is also known as aldoketomutase and ...
 16-182 1.49e-77

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: 228.15  E-value: 1.49e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165932331   16 AFSCCSDPDPSTKDFLLQQTMLRIKDPKKSLDFYTRVLGLTLLQKLDFPAMKFSLYFLAYEDKNDIpkdksektawtfsr 95
Cdd:TIGR00068   2 AESGDLVADPKTKKRRLLHTMLRVGDLDKSLDFYTEVLGMKLLRKRDFPEMKFSLAFLGYGDETSA-------------- 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165932331   96 kATLELTHNWGTEddetqSYHNGNsdprGFGHIGIAVPDVYSACKRFEELGVKFVKK--PDDGKMKGLAFIQDPDGYWIE 173
Cdd:TIGR00068  68 -AVIELTHNWGTE-----KYDLGN----GFGHIAIGVDDVYKACERVRALGGNVVREpgPVKGGTTVIAFVEDPDGYKIE 137


                  ....*....
gi 165932331  174 ILNPNKIAT 182
Cdd:TIGR00068 138 LIQRKSTKD 146
GloA COG0346
Catechol 2,3-dioxygenase or related enzyme, vicinal oxygen chelate (VOC) family [Secondary ...
 35-177 5.44e-31

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: 108.93  E-value: 5.44e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165932331  35 TMLRIKDPKKSLDFYTRVLGLTLLQKLDFPAMKFSLYFLAYEDkndipkdksektawtfsrKATLELTHNWGTEDDETqs 114
Cdd:COG0346    6 VTLRVSDLEASLAFYTDVLGLELVKRTDFGDGGFGHAFLRLGD------------------GTELELFEAPGAAPAPG-- 65

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 165932331 115 yhngnsdPRGFGHIGIAVPDVYSACKRFEELGVKFVKKPDDGKM-KGLAFIQDPDGYWIEILNP 177
Cdd:COG0346   66 -------GGGLHHLAFRVDDLDAAYARLRAAGVEIEGEPRDRAYgYRSAYFRDPDGNLIELVEP 122
Glyoxalase pfam00903
Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;
32-174 1.01e-26

Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;


Pssm-ID: 395724 [Multi-domain]  Cd Length: 121  Bit Score: 97.90  E-value: 1.01e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165932331   32 LQQTMLRIKDPKKSLDFYTRVLGLTLLqkldfpamkfslyflayeDKNDIPKDKSEKTAWTFSRKATLELTHNWGTEDDE 111
Cdd:pfam00903   2 IDHVALRVGDLEKSLDFYTDVLGFKLV------------------EETDAGEEGGLRSAFFLAGGRVLELLLNETPPPAA 63

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 165932331  112 TQSYHngnsdpRGFGHIGIAVPDVYSACKRFEELGVKFVKKPDDGKMKGLAF-IQDPDGYWIEI 174
Cdd:pfam00903  64 AGFGG------HHIAFIAFSVDDVDAAYDRLKAAGVEIVREPGRHGWGGRYSyFRDPDGNLIEL 121
 
Name Accession Description Interval E-value
PLN03042 PLN03042
Lactoylglutathione lyase; Provisional
 20-184 3.13e-108

Lactoylglutathione lyase; Provisional


Pssm-ID: 215548  Cd Length: 185  Bit Score: 307.13  E-value: 3.13e-108
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165932331  20 CSDPDPSTKDFLLQQTMLRIKDPKKSLDFYTRVLGLTLLQKLDFPAMKFSLYFLAYEDKNDIPKDKSEKTAWTFSRKATL 99
Cdd:PLN03042  16 CGNPDEATKGYIMQQTMFRIKDPKASLDFYSRVLGMSLLKRLDFPEMKFSLYFLGYEDSETAPTDPPERTVWTFGRKATI 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165932331 100 ELTHNWGTEDD-ETQSYHNGNSDPRGFGHIGIAVPDVYSACKRFEELGVKFVKKPDDGKMKGLAFIQDPDGYWIEILNPN 178
Cdd:PLN03042  96 ELTHNWGTESDpEFKGYHNGNSDPRGFGHIGITVDDVYKACERFEKLGVEFVKKPDDGKMKGLAFIKDPDGYWIEIFDLK 175


                 ....*.
gi 165932331 179 KIATII 184
Cdd:PLN03042 176 RIGGIT 181
GlxI_Zn cd07233
Glyoxalase I that uses Zn(++) as cofactor; This family includes eukaryotic glyoxalase I that ...
 32-175 2.59e-102

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: 290.38  E-value: 2.59e-102
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165932331  32 LQQTMLRIKDPKKSLDFYTRVLGLTLLQKLDFPAMKFSLYFLAYEDKNDIPKDksEKTAWTFSRKATLELTHNWGTEDDE 111
Cdd:cd07233    1 FNHTMLRVKDPKKSLKFYTEVLGMKLLRKKDFPEMKFSLYFLGYEDPKDIPKD--PRTAWVFSREGTLELTHNWGTENDE 78

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 165932331 112 TQSYHNGNSDPRGFGHIGIAVPDVYSACKRFEELGVKFVKKPDDGKMKGLAFIQDPDGYWIEIL 175
Cdd:cd07233   79 DPVYHNGNSDPRGFGHIGIAVDDVYAACERFEELGVKFKKKPDDGKMKGIAFIKDPDGYWIEIL 142
PLN02367 PLN02367
lactoylglutathione lyase
 21-183 4.65e-96

lactoylglutathione lyase


Pssm-ID: 177995  Cd Length: 233  Bit Score: 278.04  E-value: 4.65e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165932331  21 SDPDPSTKDFLLQQTMLRIKDPKKSLDFYTRVLGLTLLQKLDFPAMKFSLYFLAYEDKNDIPKDKSEKTAWTFSRKATLE 100
Cdd:PLN02367  65 TSPDEATKGYIMQQTMYRIKDPKASLDFYSRVLGMSLLKRLDFPEMKFSLYFMGYEDTASAPTDPTERTVWTFGQKATIE 144

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165932331 101 LTHNWGTEDD-ETQSYHNGNSDPRGFGHIGIAVPDVYSACKRFEELGVKFVKKPDDGKMKGLAFIQDPDGYWIEILNPNK 179
Cdd:PLN02367 145 LTHNWGTESDpDFKGYHNGNSEPRGFGHIGITVDDVYKACERFEELGVEFVKKPNDGKMKGIAFIKDPDGYWIEIFDLKT 224


                 ....
gi 165932331 180 IATI 183
Cdd:PLN02367 225 IGTT 228
glyox_I TIGR00068
lactoylglutathione lyase; Lactoylglutathione lyase is also known as aldoketomutase and ...
 16-182 1.49e-77

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: 228.15  E-value: 1.49e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165932331   16 AFSCCSDPDPSTKDFLLQQTMLRIKDPKKSLDFYTRVLGLTLLQKLDFPAMKFSLYFLAYEDKNDIpkdksektawtfsr 95
Cdd:TIGR00068   2 AESGDLVADPKTKKRRLLHTMLRVGDLDKSLDFYTEVLGMKLLRKRDFPEMKFSLAFLGYGDETSA-------------- 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165932331   96 kATLELTHNWGTEddetqSYHNGNsdprGFGHIGIAVPDVYSACKRFEELGVKFVKK--PDDGKMKGLAFIQDPDGYWIE 173
Cdd:TIGR00068  68 -AVIELTHNWGTE-----KYDLGN----GFGHIAIGVDDVYKACERVRALGGNVVREpgPVKGGTTVIAFVEDPDGYKIE 137


                  ....*....
gi 165932331  174 ILNPNKIAT 182
Cdd:TIGR00068 138 LIQRKSTKD 146
GlxI_Ni cd16358
Glyoxalase I that uses Ni(++) as cofactor; This family includes Escherichia coil and other ...
 32-175 7.93e-38

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: 126.36  E-value: 7.93e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165932331  32 LQQTMLRIKDPKKSLDFYTRVLGLTLLQKLDFPAMKFSLYFLAYEDKNDipkdksektawtfsrKATLELTHNWGTEdde 111
Cdd:cd16358    1 MLHTMLRVGDLDRSIKFYTEVLGMKLLRKRDYPEGKYTLAFVGYGDEDE---------------NTVLELTYNWGVD--- 62

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 165932331 112 tqSYHNGNsdprGFGHIGIAVPDVYSACKRFEELGVKFVKKPddGKMKG----LAFIQDPDGYWIEIL 175
Cdd:cd16358   63 --KYDLGT----AYGHIAIGVEDVYETCERIRKKGGKVTREP--GPMKGgttvIAFVEDPDGYKIELI 122
GloA COG0346
Catechol 2,3-dioxygenase or related enzyme, vicinal oxygen chelate (VOC) family [Secondary ...
 35-177 5.44e-31

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: 108.93  E-value: 5.44e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165932331  35 TMLRIKDPKKSLDFYTRVLGLTLLQKLDFPAMKFSLYFLAYEDkndipkdksektawtfsrKATLELTHNWGTEDDETqs 114
Cdd:COG0346    6 VTLRVSDLEASLAFYTDVLGLELVKRTDFGDGGFGHAFLRLGD------------------GTELELFEAPGAAPAPG-- 65

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 165932331 115 yhngnsdPRGFGHIGIAVPDVYSACKRFEELGVKFVKKPDDGKM-KGLAFIQDPDGYWIEILNP 177
Cdd:COG0346   66 -------GGGLHHLAFRVDDLDAAYARLRAAGVEIEGEPRDRAYgYRSAYFRDPDGNLIELVEP 122
Glyoxalase pfam00903
Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;
32-174 1.01e-26

Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;


Pssm-ID: 395724 [Multi-domain]  Cd Length: 121  Bit Score: 97.90  E-value: 1.01e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165932331   32 LQQTMLRIKDPKKSLDFYTRVLGLTLLqkldfpamkfslyflayeDKNDIPKDKSEKTAWTFSRKATLELTHNWGTEDDE 111
Cdd:pfam00903   2 IDHVALRVGDLEKSLDFYTDVLGFKLV------------------EETDAGEEGGLRSAFFLAGGRVLELLLNETPPPAA 63

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 165932331  112 TQSYHngnsdpRGFGHIGIAVPDVYSACKRFEELGVKFVKKPDDGKMKGLAF-IQDPDGYWIEI 174
Cdd:pfam00903  64 AGFGG------HHIAFIAFSVDDVDAAYDRLKAAGVEIVREPGRHGWGGRYSyFRDPDGNLIEL 121
PRK10291 PRK10291
glyoxalase I; Provisional
 36-175 1.85e-22

glyoxalase I; Provisional


Pssm-ID: 182358  Cd Length: 129  Bit Score: 87.39  E-value: 1.85e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165932331  36 MLRIKDPKKSLDFYTRVLGLTLLQKLDFPAMKFSLYFLAYEDKndipkdksektawtfSRKATLELTHNWGTEddetqSY 115
Cdd:PRK10291   1 MLRVGDLQRSIDFYTNVLGMKLLRTSENPEYKYSLAFVGYGPE---------------TEEAVIELTYNWGVD-----KY 60

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 165932331 116 HNGNSdprgFGHIGIAVPDVYSACKRFEELGVKFVKK--PDDGKMKGLAFIQDPDGYWIEIL 175
Cdd:PRK10291  61 ELGTA----YGHIALSVDNAAEACEKIRQNGGNVTREagPVKGGTTVIAFVEDPDGYKIELI 118
PLN02300 PLN02300
lactoylglutathione lyase
 38-175 5.65e-20

lactoylglutathione lyase


Pssm-ID: 215169 [Multi-domain]  Cd Length: 286  Bit Score: 84.45  E-value: 5.65e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165932331  38 RIKDPKKSLDFYTRVLGLTLLQKLDFPAMKFSLYFLAY--EDKNdipkdksektawtfsrkATLELTHNWGTEddetqSY 115
Cdd:PLN02300  31 RVGDLDRTIKFYTECLGMKLLRKRDIPEEKYTNAFLGYgpEDSN-----------------FVVELTYNYGVD-----KY 88

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 165932331 116 HNGNsdprGFGHIGIAVPDVYSACKRFEELGVKFVKKPddGKMKG----LAFIQDPDGYWIEIL 175
Cdd:PLN02300  89 DIGT----GFGHFGIAVEDVAKTVELVKAKGGKVTREP--GPVKGgksvIAFVKDPDGYKFELI 146
PLN02300 PLN02300
lactoylglutathione lyase
 3-170 1.27e-13

lactoylglutathione lyase


Pssm-ID: 215169 [Multi-domain]  Cd Length: 286  Bit Score: 67.11  E-value: 1.27e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165932331   3 EPQPASSGltdETAFSCCSDPDPSTKDFL--------LQQTMLRIKDPKKSLDFYTRVLGLTLLQKLDFPAMKFSLYFLA 74
Cdd:PLN02300 121 EPGPVKGG---KSVIAFVKDPDGYKFELIqrgptpepLCQVMLRVGDLDRSIKFYEKAFGMKLLRKRDNPEYKYTIAMMG 197

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165932331  75 Y--EDKNdipkdksektawtfsrkATLELTHNWGTEDdetqsYHNGNsdprGFGHIGIAVPDVYSACKRFEELGVKFVKK 152
Cdd:PLN02300 198 YgpEDKT-----------------TVLELTYNYGVTE-----YTKGN----AYAQIAIGTDDVYKTAEAIKLVGGKITRE 251

                        170       180
                 ....*....|....*....|...
gi 165932331 153 PddGKMKGL-----AFIqDPDGY 170
Cdd:PLN02300 252 P--GPLPGIntkitACL-DPDGW 271
VOC cd06587
vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate (VOC) superfamily is composed ...
 35-174 2.77e-13

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: 62.93  E-value: 2.77e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165932331  35 TMLRIKDPKKSLDFYTRVLGLTLLQKLDfpamKFSLYFLAYEDkndipkdksektawtfsrKATLELTHNWGTEDDEtqs 114
Cdd:cd06587    2 VALRVPDLDASVAFYEEVLGFEVVSRNE----GGGFAFLRLGP------------------GLRLALLEGPEPERPG--- 56

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 165932331 115 yhngnsdPRGFGHIGIAVPDVYSACKRFEELGVKFVKK---PDDGKMKGLAFIQDPDGYWIEI 174
Cdd:cd06587   57 -------GGGLFHLAFEVDDVDEVDERLREAGAEGELVappVDDPWGGRSFYFRDPDGNLIEF 112
VOC COG3324
Lactoylglutathione lyase-related enzyme, vicinal oxygen chelate (VOC) family [General function ...
 37-177 2.23e-09

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


Pssm-ID: 442553 [Multi-domain]  Cd Length: 119  Bit Score: 52.72  E-value: 2.23e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165932331  37 LRIKDPKKSLDFYTRVLGLTLLQKLDFPAmkfslyflayedkndipkdksekTAWTFSrkatlelthnwgTEDDETQSYH 116
Cdd:COG3324   10 LPVDDLERAKAFYEEVFGWTFEDDAGPGG-----------------------DYAEFD------------TDGGQVGGLM 54

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 165932331 117 NGNSDPRGFG-HIGIAVPDVYSACKRFEELGVKFVKKPDDGKMKG-LAFIQDPDGYWIEILNP 177
Cdd:COG3324   55 PGAEEPGGPGwLLYFAVDDLDAAVARVEAAGGTVLRPPTDIPPWGrFAVFRDPEGNRFGLWQP 117
VOC_like cd07264
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 32-177 7.78e-08

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


Pssm-ID: 319925 [Multi-domain]  Cd Length: 118  Bit Score: 48.48  E-value: 7.78e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165932331  32 LQQTMLRIKDPKKSLDFYTRVLGLTllqkldfpamkfslyflayedkndiPKDKSEKTAWT--FSRKATLELTHNwGTED 109
Cdd:cd07264    1 IAYIVLYVDDFAASLRFYRDVLGLP-------------------------PRFLHEEGEYAefDTGETKLALFSR-KEMA 54

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165932331 110 DETqsyhnGNSDPRGFGHIGIAVPDVYSACKRFEELGVKFVKKPDDgKMKGL--AFIQDPDGYWIEILNP 177
Cdd:cd07264   55 RSG-----GPDRRGSAFELGFEVDDVEATVEELVERGAEFVREPAN-KPWGQtvAYVRDPDGNLIEICEP 118
CatE COG2514
Catechol-2,3-dioxygenase [Secondary metabolites biosynthesis, transport and catabolism];
37-174 1.78e-07

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


Pssm-ID: 442004 [Multi-domain]  Cd Length: 141  Bit Score: 48.03  E-value: 1.78e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165932331  37 LRIKDPKKSLDFYTRVLGLTLLQKLDfpamkfSLYFLAyedkndipkdksektawTFSRKATLELThnwgtEDDETQSYH 116
Cdd:COG2514    9 LRVRDLERSAAFYTDVLGLEVVEREG------GRVYLR-----------------ADGGEHLLVLE-----EAPGAPPRP 60

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 165932331 117 NGNsdprGFGHIGIAVP---DVYSACKRFEELGVKFVKKPDDGKMKGLAFiQDPDGYWIEI 174
Cdd:COG2514   61 GAA----GLDHVAFRVPsraDLDAALARLAAAGVPVEGAVDHGVGESLYF-RDPDGNLIEL 116
VOC_like cd07245
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 37-174 1.38e-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: 319909 [Multi-domain]  Cd Length: 117  Bit Score: 45.39  E-value: 1.38e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165932331  37 LRIKDPKKSLDFYTRVLGLTLLQKLDFpaMKFSLYFLAYEDKNDIpkdksektawtfsrkatleltH----NWGTEDdeT 112
Cdd:cd07245    6 LACPDLERARRFYTDVLGLEEVPRPPF--LKFGGAWLYLGGGQQI---------------------HlvveQNPSEL--P 60

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 165932331 113 QSYHNGNSDprgfgHIGIAVPDVYSACKRFEELGVKFVKK-PDDGKMKGLaFIQDPDGYWIEI 174
Cdd:cd07245   61 RPEHPGRDR-----HPSFSVPDLDALKQRLKEAGIPYTEStSPGGGVTQL-FFRDPDGNRLEF 117
GloA COG0346
Catechol 2,3-dioxygenase or related enzyme, vicinal oxygen chelate (VOC) family [Secondary ...
 123-175 2.38e-04

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: 39.21  E-value: 2.38e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 165932331 123 RGFGHIGIAVPDvYSACKRF--EELGVKFVKKPDDGKMK-GLAFIQDPDGYWIEIL 175
Cdd:COG0346    1 MGLHHVTLRVSD-LEASLAFytDVLGLELVKRTDFGDGGfGHAFLRLGDGTELELF 55
MMCE cd07249
Methylmalonyl-CoA epimerase (MMCE); MMCE, also called methylmalonyl-CoA racemase (EC 5.1.99.1) ...
 127-177 2.88e-03

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: 36.01  E-value: 2.88e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 165932331 127 HIGIAVPDVYSACKRFEE-LGVKFV--KKPDDGKMKgLAFIqDPDGYWIEILNP 177
Cdd:cd07249    3 HIGIAVPDLDEALKFYEDvLGVKVSepEELEEQGVR-VAFL-ELGNTQIELLEP 54
 
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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