NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|79317307|ref|NP_001030996|]
View 

lactoylglutathione lyase family protein / glyoxalase I family protein [Arabidopsis thaliana]

Protein Classification

lactoylglutathione lyase( domain architecture ID 11476702)

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

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
PLN02367 PLN02367
lactoylglutathione lyase
 12-235 5.92e-168

lactoylglutathione lyase


:

Pssm-ID: 177995  Cd Length: 233  Bit Score: 462.16  E-value: 5.92e-168
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79317307   12 RISPLIRFVKPYSTGFSFITCACNSTRRPKRFDQLCVFSMASEARESPANNPGLSTNRDEATKGYIMQQTMFRIKDPKAS 91
Cdd:PLN02367  10 RLSPLILIVKPYSSGSSFITCFCNSTRKPKRFDRLRVFSMASEPKESPANNPGLSTSPDEATKGYIMQQTMYRIKDPKAS 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79317307   92 LDFYSRVLGMSLLKRLDFSEMKFSLYFLGYEDTTTAPTDPTERTVWTFGQPATIELTHNWGTESDPEFKGYHNGNSEPRG 171
Cdd:PLN02367  90 LDFYSRVLGMSLLKRLDFPEMKFSLYFMGYEDTASAPTDPTERTVWTFGQKATIELTHNWGTESDPDFKGYHNGNSEPRG 169

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 79317307  172 FGHIGVTVDDVHKACERFEELGVEFAKKPNDGKMKNIAFIKDPDGYWIEIFDLKTIGTTTVNAA 235
Cdd:PLN02367 170 FGHIGITVDDVYKACERFEELGVEFVKKPNDGKMKGIAFIKDPDGYWIEIFDLKTIGTTTVNAA 233
 
Name Accession Description Interval E-value
PLN02367 PLN02367
lactoylglutathione lyase
 12-235 5.92e-168

lactoylglutathione lyase


Pssm-ID: 177995  Cd Length: 233  Bit Score: 462.16  E-value: 5.92e-168
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79317307   12 RISPLIRFVKPYSTGFSFITCACNSTRRPKRFDQLCVFSMASEARESPANNPGLSTNRDEATKGYIMQQTMFRIKDPKAS 91
Cdd:PLN02367  10 RLSPLILIVKPYSSGSSFITCFCNSTRKPKRFDRLRVFSMASEPKESPANNPGLSTSPDEATKGYIMQQTMYRIKDPKAS 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79317307   92 LDFYSRVLGMSLLKRLDFSEMKFSLYFLGYEDTTTAPTDPTERTVWTFGQPATIELTHNWGTESDPEFKGYHNGNSEPRG 171
Cdd:PLN02367  90 LDFYSRVLGMSLLKRLDFPEMKFSLYFMGYEDTASAPTDPTERTVWTFGQKATIELTHNWGTESDPDFKGYHNGNSEPRG 169

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 79317307  172 FGHIGVTVDDVHKACERFEELGVEFAKKPNDGKMKNIAFIKDPDGYWIEIFDLKTIGTTTVNAA 235
Cdd:PLN02367 170 FGHIGITVDDVYKACERFEELGVEFVKKPNDGKMKGIAFIKDPDGYWIEIFDLKTIGTTTVNAA 233
GlxI_Zn cd07233
Glyoxalase I that uses Zn(++) as cofactor; This family includes eukaryotic glyoxalase I that ...
 78-222 3.10e-93

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: 269.58  E-value: 3.10e-93
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79317307  78 MQQTMFRIKDPKASLDFYSRVLGMSLLKRLDFSEMKFSLYFLGYEDTTTAPTDptERTVWTFGQPATIELTHNWGTESDP 157
Cdd:cd07233   1 FNHTMLRVKDPKKSLKFYTEVLGMKLLRKKDFPEMKFSLYFLGYEDPKDIPKD--PRTAWVFSREGTLELTHNWGTENDE 78

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 79317307 158 EFKgYHNGNSEPRGFGHIGVTVDDVHKACERFEELGVEFAKKPNDGKMKNIAFIKDPDGYWIEIF 222
Cdd:cd07233  79 DPV-YHNGNSDPRGFGHIGIAVDDVYAACERFEELGVKFKKKPDDGKMKGIAFIKDPDGYWIEIL 142
glyox_I TIGR00068
lactoylglutathione lyase; Lactoylglutathione lyase is also known as aldoketomutase and ...
 64-233 9.93e-76

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: 225.84  E-value: 9.93e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79317307    64 GLSTNRDEATKGYIMQQTMFRIKDPKASLDFYSRVLGMSLLKRLDFSEMKFSLYFLGYEDTTtaptdptertvwtfgQPA 143
Cdd:TIGR00068   4 SGDLVADPKTKKRRLLHTMLRVGDLDKSLDFYTEVLGMKLLRKRDFPEMKFSLAFLGYGDET---------------SAA 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79317307   144 TIELTHNWGTESdpefkgYHNGNseprGFGHIGVTVDDVHKACERFEELGVEFAKKPN--DGKMKNIAFIKDPDGYWIEI 221
Cdd:TIGR00068  69 VIELTHNWGTEK------YDLGN----GFGHIAIGVDDVYKACERVRALGGNVVREPGpvKGGTTVIAFVEDPDGYKIEL 138

                         170
                  ....*....|..
gi 79317307   222 FDLKTIGTTTVN 233
Cdd:TIGR00068 139 IQRKSTKDGLGN 150
GloA COG0346
Catechol 2,3-dioxygenase or related enzyme, vicinal oxygen chelate (VOC) family [Secondary ...
 81-222 1.22e-30

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: 109.70  E-value: 1.22e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79317307  81 TMFRIKDPKASLDFYSRVLGMSLLKRLDFSEMKFSLYFLgyedtttaptdptertvwTFGQPATIELTHNWGTESDPefk 160
Cdd:COG0346   6 VTLRVSDLEASLAFYTDVLGLELVKRTDFGDGGFGHAFL------------------RLGDGTELELFEAPGAAPAP--- 64

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 79317307 161 gyhngnsEPRGFGHIGVTVDDVHKACERFEELGVEFAKKPNDGKM-KNIAFIKDPDGYWIEIF 222
Cdd:COG0346  65 -------GGGGLHHLAFRVDDLDAAYARLRAAGVEIEGEPRDRAYgYRSAYFRDPDGNLIELV 120
Glyoxalase pfam00903
Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;
80-221 6.22e-26

Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;


Pssm-ID: 395724 [Multi-domain]  Cd Length: 121  Bit Score: 97.52  E-value: 6.22e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79317307    80 QTMFRIKDPKASLDFYSRVLGMSLLKRLDFSEMkfslyflgyedtttaptdPTERTVWTFGQPATIELTHNWGTESDPEF 159
Cdd:pfam00903   4 HVALRVGDLEKSLDFYTDVLGFKLVEETDAGEE------------------GGLRSAFFLAGGRVLELLLNETPPPAAAG 65

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 79317307   160 KGYHngnseprGFGHIGVTVDDVHKACERFEELGVEFAKKPNDGKMKNIAF-IKDPDGYWIEI 221
Cdd:pfam00903  66 FGGH-------HIAFIAFSVDDVDAAYDRLKAAGVEIVREPGRHGWGGRYSyFRDPDGNLIEL 121
 
Name Accession Description Interval E-value
PLN02367 PLN02367
lactoylglutathione lyase
 12-235 5.92e-168

lactoylglutathione lyase


Pssm-ID: 177995  Cd Length: 233  Bit Score: 462.16  E-value: 5.92e-168
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79317307   12 RISPLIRFVKPYSTGFSFITCACNSTRRPKRFDQLCVFSMASEARESPANNPGLSTNRDEATKGYIMQQTMFRIKDPKAS 91
Cdd:PLN02367  10 RLSPLILIVKPYSSGSSFITCFCNSTRKPKRFDRLRVFSMASEPKESPANNPGLSTSPDEATKGYIMQQTMYRIKDPKAS 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79317307   92 LDFYSRVLGMSLLKRLDFSEMKFSLYFLGYEDTTTAPTDPTERTVWTFGQPATIELTHNWGTESDPEFKGYHNGNSEPRG 171
Cdd:PLN02367  90 LDFYSRVLGMSLLKRLDFPEMKFSLYFMGYEDTASAPTDPTERTVWTFGQKATIELTHNWGTESDPDFKGYHNGNSEPRG 169

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 79317307  172 FGHIGVTVDDVHKACERFEELGVEFAKKPNDGKMKNIAFIKDPDGYWIEIFDLKTIGTTTVNAA 235
Cdd:PLN02367 170 FGHIGITVDDVYKACERFEELGVEFVKKPNDGKMKGIAFIKDPDGYWIEIFDLKTIGTTTVNAA 233
PLN03042 PLN03042
Lactoylglutathione lyase; Provisional
 51-235 8.41e-131

Lactoylglutathione lyase; Provisional


Pssm-ID: 215548  Cd Length: 185  Bit Score: 366.45  E-value: 8.41e-131
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79317307   51 MASEARESPANNPGLSTNRDEATKGYIMQQTMFRIKDPKASLDFYSRVLGMSLLKRLDFSEMKFSLYFLGYEDTTTAPTD 130
Cdd:PLN03042   1 MASASKESAANNPGLCGNPDEATKGYIMQQTMFRIKDPKASLDFYSRVLGMSLLKRLDFPEMKFSLYFLGYEDSETAPTD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79317307  131 PTERTVWTFGQPATIELTHNWGTESDPEFKGYHNGNSEPRGFGHIGVTVDDVHKACERFEELGVEFAKKPNDGKMKNIAF 210
Cdd:PLN03042  81 PPERTVWTFGRKATIELTHNWGTESDPEFKGYHNGNSDPRGFGHIGITVDDVYKACERFEKLGVEFVKKPDDGKMKGLAF 160

                        170       180
                 ....*....|....*....|....*
gi 79317307  211 IKDPDGYWIEIFDLKTIGTTTVNAA 235
Cdd:PLN03042 161 IKDPDGYWIEIFDLKRIGGITAGAA 185
GlxI_Zn cd07233
Glyoxalase I that uses Zn(++) as cofactor; This family includes eukaryotic glyoxalase I that ...
 78-222 3.10e-93

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: 269.58  E-value: 3.10e-93
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79317307  78 MQQTMFRIKDPKASLDFYSRVLGMSLLKRLDFSEMKFSLYFLGYEDTTTAPTDptERTVWTFGQPATIELTHNWGTESDP 157
Cdd:cd07233   1 FNHTMLRVKDPKKSLKFYTEVLGMKLLRKKDFPEMKFSLYFLGYEDPKDIPKD--PRTAWVFSREGTLELTHNWGTENDE 78

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 79317307 158 EFKgYHNGNSEPRGFGHIGVTVDDVHKACERFEELGVEFAKKPNDGKMKNIAFIKDPDGYWIEIF 222
Cdd:cd07233  79 DPV-YHNGNSDPRGFGHIGIAVDDVYAACERFEELGVKFKKKPDDGKMKGIAFIKDPDGYWIEIL 142
glyox_I TIGR00068
lactoylglutathione lyase; Lactoylglutathione lyase is also known as aldoketomutase and ...
 64-233 9.93e-76

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: 225.84  E-value: 9.93e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79317307    64 GLSTNRDEATKGYIMQQTMFRIKDPKASLDFYSRVLGMSLLKRLDFSEMKFSLYFLGYEDTTtaptdptertvwtfgQPA 143
Cdd:TIGR00068   4 SGDLVADPKTKKRRLLHTMLRVGDLDKSLDFYTEVLGMKLLRKRDFPEMKFSLAFLGYGDET---------------SAA 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79317307   144 TIELTHNWGTESdpefkgYHNGNseprGFGHIGVTVDDVHKACERFEELGVEFAKKPN--DGKMKNIAFIKDPDGYWIEI 221
Cdd:TIGR00068  69 VIELTHNWGTEK------YDLGN----GFGHIAIGVDDVYKACERVRALGGNVVREPGpvKGGTTVIAFVEDPDGYKIEL 138

                         170
                  ....*....|..
gi 79317307   222 FDLKTIGTTTVN 233
Cdd:TIGR00068 139 IQRKSTKDGLGN 150
GlxI_Ni cd16358
Glyoxalase I that uses Ni(++) as cofactor; This family includes Escherichia coil and other ...
 78-221 8.46e-35

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: 120.58  E-value: 8.46e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79317307  78 MQQTMFRIKDPKASLDFYSRVLGMSLLKRLDFSEMKFSLYFLGYedtttaptdPTERTvwtfgqPATIELTHNWGTESdp 157
Cdd:cd16358   1 MLHTMLRVGDLDRSIKFYTEVLGMKLLRKRDYPEGKYTLAFVGY---------GDEDE------NTVLELTYNWGVDK-- 63

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 79317307 158 efkgYHNGNseprGFGHIGVTVDDVHKACERFEELGVEFAKKPndGKMKN----IAFIKDPDGYWIEI 221
Cdd:cd16358  64 ----YDLGT----AYGHIAIGVEDVYETCERIRKKGGKVTREP--GPMKGgttvIAFVEDPDGYKIEL 121
GloA COG0346
Catechol 2,3-dioxygenase or related enzyme, vicinal oxygen chelate (VOC) family [Secondary ...
 81-222 1.22e-30

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: 109.70  E-value: 1.22e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79317307  81 TMFRIKDPKASLDFYSRVLGMSLLKRLDFSEMKFSLYFLgyedtttaptdptertvwTFGQPATIELTHNWGTESDPefk 160
Cdd:COG0346   6 VTLRVSDLEASLAFYTDVLGLELVKRTDFGDGGFGHAFL------------------RLGDGTELELFEAPGAAPAP--- 64

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 79317307 161 gyhngnsEPRGFGHIGVTVDDVHKACERFEELGVEFAKKPNDGKM-KNIAFIKDPDGYWIEIF 222
Cdd:COG0346  65 -------GGGGLHHLAFRVDDLDAAYARLRAAGVEIEGEPRDRAYgYRSAYFRDPDGNLIELV 120
Glyoxalase pfam00903
Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;
80-221 6.22e-26

Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;


Pssm-ID: 395724 [Multi-domain]  Cd Length: 121  Bit Score: 97.52  E-value: 6.22e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79317307    80 QTMFRIKDPKASLDFYSRVLGMSLLKRLDFSEMkfslyflgyedtttaptdPTERTVWTFGQPATIELTHNWGTESDPEF 159
Cdd:pfam00903   4 HVALRVGDLEKSLDFYTDVLGFKLVEETDAGEE------------------GGLRSAFFLAGGRVLELLLNETPPPAAAG 65

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 79317307   160 KGYHngnseprGFGHIGVTVDDVHKACERFEELGVEFAKKPNDGKMKNIAF-IKDPDGYWIEI 221
Cdd:pfam00903  66 FGGH-------HIAFIAFSVDDVDAAYDRLKAAGVEIVREPGRHGWGGRYSyFRDPDGNLIEL 121
PRK10291 PRK10291
glyoxalase I; Provisional
 82-228 1.92e-23

glyoxalase I; Provisional


Pssm-ID: 182358  Cd Length: 129  Bit Score: 91.62  E-value: 1.92e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79317307   82 MFRIKDPKASLDFYSRVLGMSLLKRLDFSEMKFSLYFLGYEDTTtaptdptertvwtfgQPATIELTHNWGTESdpefkg 161
Cdd:PRK10291   1 MLRVGDLQRSIDFYTNVLGMKLLRTSENPEYKYSLAFVGYGPET---------------EEAVIELTYNWGVDK------ 59

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 79317307  162 YHNGNSeprgFGHIGVTVDDVHKACERFEELGVEFAKK--PNDGKMKNIAFIKDPDGYWIEIFDLKTIG 228
Cdd:PRK10291  60 YELGTA----YGHIALSVDNAAEACEKIRQNGGNVTREagPVKGGTTVIAFVEDPDGYKIELIEEKDAG 124
PLN02300 PLN02300
lactoylglutathione lyase
 78-221 8.55e-19

lactoylglutathione lyase


Pssm-ID: 215169 [Multi-domain]  Cd Length: 286  Bit Score: 82.91  E-value: 8.55e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79317307   78 MQQTMFRIKDPKASLDFYSRVLGMSLLKRLDFSEMKFSLYFLGYedtttaptdPTERTVWtfgqpaTIELTHNWGTESdp 157
Cdd:PLN02300  25 MLHVVYRVGDLDRTIKFYTECLGMKLLRKRDIPEEKYTNAFLGY---------GPEDSNF------VVELTYNYGVDK-- 87

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 79317307  158 efkgYHNGNseprGFGHIGVTVDDVHKACERFEELGVEFAKKPN--DGKMKNIAFIKDPDGYWIEI 221
Cdd:PLN02300  88 ----YDIGT----GFGHFGIAVEDVAKTVELVKAKGGKVTREPGpvKGGKSVIAFVKDPDGYKFEL 145
PLN02300 PLN02300
lactoylglutathione lyase
 80-222 2.66e-12

lactoylglutathione lyase


Pssm-ID: 215169 [Multi-domain]  Cd Length: 286  Bit Score: 64.80  E-value: 2.66e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79317307   80 QTMFRIKDPKASLDFYSRVLGMSLLKRLDFSEMKFSLYFLGYedtttapTDPTERTVwtfgqpatIELTHNWG-TEsdpe 158
Cdd:PLN02300 157 QVMLRVGDLDRSIKFYEKAFGMKLLRKRDNPEYKYTIAMMGY-------GPEDKTTV--------LELTYNYGvTE---- 217

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 79317307  159 fkgYHNGNseprGFGHIGVTVDDVHKACERFEELGVEFAKKPN--DGKMKNIAFIKDPDGyWIEIF 222
Cdd:PLN02300 218 ---YTKGN----AYAQIAIGTDDVYKTAEAIKLVGGKITREPGplPGINTKITACLDPDG-WKTVF 275
VOC cd06587
vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate (VOC) superfamily is composed ...
 81-221 1.66e-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: 59.46  E-value: 1.66e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79317307  81 TMFRIKDPKASLDFYSRVLGMSLLKRLDfsemkfslyflgyedtttaptdPTERTVWTFGQPATIELTHNWGTESDPefk 160
Cdd:cd06587   2 VALRVPDLDASVAFYEEVLGFEVVSRNE----------------------GGGFAFLRLGPGLRLALLEGPEPERPG--- 56

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 79317307 161 gyhngnsePRGFGHIGVTVDDVHKACERFEELGVEF---AKKPNDGKMKNIAFIKDPDGYWIEI 221
Cdd:cd06587  57 --------GGGLFHLAFEVDDVDEVDERLREAGAEGelvAPPVDDPWGGRSFYFRDPDGNLIEF 112
VOC COG3324
Lactoylglutathione lyase-related enzyme, vicinal oxygen chelate (VOC) family [General function ...
 86-222 4.95e-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: 4.95e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79317307  86 KDPKASLDFYSRVLGMSLLKRLDFSEmkfslyflGYedtttaptdpterTVWTFGQPATIELthnwgtesdpefkgyHNG 165
Cdd:COG3324  13 DDLERAKAFYEEVFGWTFEDDAGPGG--------DY-------------AEFDTDGGQVGGL---------------MPG 56

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 79317307 166 NSEPRGFG-HIGVTVDDVHKACERFEELGVEFAKKPND----GKMkniAFIKDPDGYWIEIF 222
Cdd:COG3324  57 AEEPGGPGwLLYFAVDDLDAAVARVEAAGGTVLRPPTDippwGRF---AVFRDPEGNRFGLW 115
VOC_like cd07264
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 80-222 1.36e-07

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


Pssm-ID: 319925 [Multi-domain]  Cd Length: 118  Bit Score: 48.87  E-value: 1.36e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79317307  80 QTMFRIKDPKASLDFYSRVLGmslLKR-----------LDFSEMKFSLYflgyedtttaptdptertvwTFGQPATIElt 148
Cdd:cd07264   3 YIVLYVDDFAASLRFYRDVLG---LPPrflheegeyaeFDTGETKLALF--------------------SRKEMARSG-- 57

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 79317307 149 hnwgtesdpefkgyhnGNSEPRGFGHIGVTVDDVHKACERFEELGVEFAKKP--NDGKMKnIAFIKDPDGYWIEIF 222
Cdd:cd07264  58 ----------------GPDRRGSAFELGFEVDDVEATVEELVERGAEFVREPanKPWGQT-VAYVRDPDGNLIEIC 116
CatE COG2514
Catechol-2,3-dioxygenase [Secondary metabolites biosynthesis, transport and catabolism];
83-222 4.92e-07

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


Pssm-ID: 442004 [Multi-domain]  Cd Length: 141  Bit Score: 47.65  E-value: 4.92e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79317307  83 FRIKDPKASLDFYSRVLGMSLLKRLDfsemkfSLYFLGyedtttaptdptertvwTFGQPATIELTHNWGTESDPEFKGY 162
Cdd:COG2514   9 LRVRDLERSAAFYTDVLGLEVVEREG------GRVYLR-----------------ADGGEHLLVLEEAPGAPPRPGAAGL 65

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 79317307 163 HngnseprgfgHIGVTVD---DVHKACERFEELGVEFAKKPNDGKMKNIAFiKDPDGYWIEIF 222
Cdd:COG2514  66 D----------HVAFRVPsraDLDAALARLAAAGVPVEGAVDHGVGESLYF-RDPDGNLIELY 117
Glyoxalase_4 pfam13669
Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;
86-200 3.24e-06

Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;


Pssm-ID: 463951 [Multi-domain]  Cd Length: 109  Bit Score: 44.58  E-value: 3.24e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79317307    86 KDPKASLDFYSRVLGMSLLKRLDFSEMKFSLYFLGyedtttaptdptertvwTFGQPATIELTHNWGTESDPEFKGYhng 165
Cdd:pfam13669   8 PDLDRALALWGALLGLGPEGDYRSEPQNVDLAFAL-----------------LGDGPVEVELIQPLDGDSPLARHGP--- 67

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 79317307   166 nseprGFGHIGVTVDDVHKACERFEELGVEFAKKP 200
Cdd:pfam13669  68 -----GLHHLAYWVDDLDAAVARLLDQGYRVAPKG 97
GloA COG0346
Catechol 2,3-dioxygenase or related enzyme, vicinal oxygen chelate (VOC) family [Secondary ...
 170-223 1.78e-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: 39.98  E-value: 1.78e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 79317307 170 RGFGHIGVTVDDVHKACERFEE-LGVEFAKKPNDGKMK-NIAFIKDPDGYWIEIFD 223
Cdd:COG0346   1 MGLHHVTLRVSDLEASLAFYTDvLGLELVKRTDFGDGGfGHAFLRLGDGTELELFE 56
HppD COG3185
4-hydroxyphenylpyruvate dioxygenase and related hemolysins [Amino acid transport and ...
 174-229 6.01e-04

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: 40.26  E-value: 6.01e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 79317307 174 HIGVTVDDVHKACERFEELGVEF------------AKKPNDGKM------KNIAFIKDPDGYWIEIFDLKTIGT 229
Cdd:COG3185 227 HIAFATDDIEATVAALRARGVRFldipdnyyddlePRVGAHGEDvaflhpKGILVDRDTGGVLLQIFTKPVGGT 300
VOC_Bs_YwkD_like cd08352
vicinal oxygen chelate (VOC) family protein Bacillus subtilis YwkD and similar proteins; ...
 87-221 6.81e-04

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


Pssm-ID: 319940 [Multi-domain]  Cd Length: 123  Bit Score: 38.29  E-value: 6.81e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79317307  87 DPKASLDFYSRVLGMSLL---KRLDFSEMKFSLYFLGYEdtttaptdptertVWTFGQPATIElthnwgTESDPEfkgyh 163
Cdd:cd08352  12 DYEKSKDFYVDKLGFEIIrehYRPERNDIKLDLALGGYQ-------------LELFIKPDAPA------RPSYPE----- 67

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 79317307 164 ngnsePRGFGHIGVTVDDVHKACERFEELGVE---FAKKPNDGkmKNIAFIKDPDGYWIEI 221
Cdd:cd08352  68 -----ALGLRHLAFKVEDVEATVAELKSLGIEtepIRVDDFTG--KKFTFFFDPDGLPLEL 121
VOC_like cd07263
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 80-219 7.97e-04

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


Pssm-ID: 319924 [Multi-domain]  Cd Length: 120  Bit Score: 38.05  E-value: 7.97e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79317307  80 QTMFRIKDPKASLDFYSRVLGMSLLKRLDFSEMKFSlyflgyedtttaptdpterTVWTFGQPATIELTHNWGTESDPEF 159
Cdd:cd07263   1 QVMLYVDDQDKALDFYVEKLGFEVVEDVPMGGMRWV-------------------TVAPPGSPGTSLLLEPKAHPAQMPQ 61

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 79317307 160 KGYHNGnseprGFGHIGVTVDDVHKACERFEELGVEFAKKPNDGKMKNIAFIKDPDG-YWI 219
Cdd:cd07263  62 SPEAAG-----GTPGILLATDDIDATYERLTAAGVTFVQEPTQMGGGRVANFRDPDGnLFA 117
MMCE cd07249
Methylmalonyl-CoA epimerase (MMCE); MMCE, also called methylmalonyl-CoA racemase (EC 5.1.99.1) ...
 86-221 4.62e-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: 4.62e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79317307  86 KDPKASLDFYSRVLGMSLLKRLDFSEMKFSLYFLGYEdtttaptdptertvwtfgqPATIELTHNWGTESDPEFKGYHNG 165
Cdd:cd07249   9 PDLDEALKFYEDVLGVKVSEPEELEEQGVRVAFLELG-------------------NTQIELLEPLGEDSPIAKFLDKKG 69

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 79317307 166 NseprGFGHIGVTVDDVHKACERFEELGVEFAKKPN----DGkmKNIAFI--KDPDGYWIEI 221
Cdd:cd07249  70 G----GLHHIAFEVDDIDAAVEELKAQGVRLLSEGPrigaHG--KRVAFLhpKDTGGVLIEL 125
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH