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Conserved domains on  [gi|15600304|ref|NP_253798|]
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lactoylglutathione lyase [Pseudomonas aeruginosa PAO1]

Protein Classification

lactoylglutathione lyase( domain architecture ID 10163464)

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
GlxI_Zn cd07233
Glyoxalase I that uses Zn(++) as cofactor; This family includes eukaryotic glyoxalase I that ...
 24-165 3.71e-85

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: 246.85  E-value: 3.71e-85
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600304  24 FNHTMLRVKDPKRSLDFYSRVLGMRLLRRLDFEEGRFSLYFLAMTRGEEVPDavDERQRYTFGRQSVLELTHNWGSESDD 103
Cdd:cd07233   1 FNHTMLRVKDPKKSLKFYTEVLGMKLLRKKDFPEMKFSLYFLGYEDPKDIPK--DPRTAWVFSREGTLELTHNWGTENDE 78

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15600304 104 SQ-YHNGNQDPRGFGHICFSVPDLVAACERFETLGVNFVKPLDRG-MKNVAFISDPDGYWVEIV 165
Cdd:cd07233  79 DPvYHNGNSDPRGFGHIGIAVDDVYAACERFEELGVKFKKKPDDGkMKGIAFIKDPDGYWIEIL 142
 
Name Accession Description Interval E-value
GlxI_Zn cd07233
Glyoxalase I that uses Zn(++) as cofactor; This family includes eukaryotic glyoxalase I that ...
 24-165 3.71e-85

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: 246.85  E-value: 3.71e-85
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600304  24 FNHTMLRVKDPKRSLDFYSRVLGMRLLRRLDFEEGRFSLYFLAMTRGEEVPDavDERQRYTFGRQSVLELTHNWGSESDD 103
Cdd:cd07233   1 FNHTMLRVKDPKKSLKFYTEVLGMKLLRKKDFPEMKFSLYFLGYEDPKDIPK--DPRTAWVFSREGTLELTHNWGTENDE 78

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15600304 104 SQ-YHNGNQDPRGFGHICFSVPDLVAACERFETLGVNFVKPLDRG-MKNVAFISDPDGYWVEIV 165
Cdd:cd07233  79 DPvYHNGNSDPRGFGHIGIAVDDVYAACERFEELGVKFKKKPDDGkMKGIAFIKDPDGYWIEIL 142
PLN03042 PLN03042
Lactoylglutathione lyase; Provisional
 9-167 1.35e-83

Lactoylglutathione lyase; Provisional


Pssm-ID: 215548  Cd Length: 185  Bit Score: 244.34  E-value: 1.35e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600304    9 PGICMEPDAITQEYVFNHTMLRVKDPKRSLDFYSRVLGMRLLRRLDFEEGRFSLYFLAMTRGEEVPDAVDERQRYTFGRQ 88
Cdd:PLN03042  13 PGLCGNPDEATKGYIMQQTMFRIKDPKASLDFYSRVLGMSLLKRLDFPEMKFSLYFLGYEDSETAPTDPPERTVWTFGRK 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600304   89 SVLELTHNWGSESDDS--QYHNGNQDPRGFGHICFSVPDLVAACERFETLGVNFVK-PLDRGMKNVAFISDPDGYWVEIV 165
Cdd:PLN03042  93 ATIELTHNWGTESDPEfkGYHNGNSDPRGFGHIGITVDDVYKACERFEKLGVEFVKkPDDGKMKGLAFIKDPDGYWIEIF 172


                 ..
gi 15600304  166 QA 167
Cdd:PLN03042 173 DL 174
glyox_I TIGR00068
lactoylglutathione lyase; Lactoylglutathione lyase is also known as aldoketomutase and ...
 10-176 5.57e-61

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: 185.78  E-value: 5.57e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600304    10 GICMEPDAITQEYVFNHTMLRVKDPKRSLDFYSRVLGMRLLRRLDFEEGRFSLYFLAMTRGEEvpdavderqrytfgrQS 89
Cdd:TIGR00068   4 SGDLVADPKTKKRRLLHTMLRVGDLDKSLDFYTEVLGMKLLRKRDFPEMKFSLAFLGYGDETS---------------AA 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600304    90 VLELTHNWGSESddsqYHNGNqdprGFGHICFSVPDLVAACERFETLGVNFVK---PLDRGMKNVAFISDPDGYWVEIVQ 166
Cdd:TIGR00068  69 VIELTHNWGTEK----YDLGN----GFGHIAIGVDDVYKACERVRALGGNVVRepgPVKGGTTVIAFVEDPDGYKIELIQ 140

                         170
                  ....*....|
gi 15600304   167 aslNGEMGRG 176
Cdd:TIGR00068 141 ---RKSTKDG 147
GloA COG0346
Catechol 2,3-dioxygenase or related enzyme, vicinal oxygen chelate (VOC) family [Secondary ...
 24-166 1.89e-34

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: 117.79  E-value: 1.89e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600304  24 FNHTMLRVKDPKRSLDFYSRVLGMRLLRRLDFEEGRFSLYFLamtrgeevpdavderqryTFGRQSVLELTHNWGSESDD 103
Cdd:COG0346   3 LHHVTLRVSDLEASLAFYTDVLGLELVKRTDFGDGGFGHAFL------------------RLGDGTELELFEAPGAAPAP 64

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15600304 104 SqyhngnqdPRGFGHICFSVPDLVAACERFETLGVNFVK-PLDRGM-KNVAFISDPDGYWVEIVQ 166
Cdd:COG0346  65 G--------GGGLHHLAFRVDDLDAAYARLRAAGVEIEGePRDRAYgYRSAYFRDPDGNLIELVE 121
Glyoxalase pfam00903
Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;
24-164 2.35e-27

Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;


Pssm-ID: 395724 [Multi-domain]  Cd Length: 121  Bit Score: 99.44  E-value: 2.35e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600304    24 FNHTMLRVKDPKRSLDFYSRVLGMRLLRRLDFEEGRfslyflamtrgeevpdavDERQRYTFGRQSVLELTHNWGSESDD 103
Cdd:pfam00903   2 IDHVALRVGDLEKSLDFYTDVLGFKLVEETDAGEEG------------------GLRSAFFLAGGRVLELLLNETPPPAA 63

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15600304   104 SQYHngnqdPRGFGHICFSVPDLVAACERFETLGVNFVKPLDRGM--KNVAFISDPDGYWVEI 164
Cdd:pfam00903  64 AGFG-----GHHIAFIAFSVDDVDAAYDRLKAAGVEIVREPGRHGwgGRYSYFRDPDGNLIEL 121
 
Name Accession Description Interval E-value
GlxI_Zn cd07233
Glyoxalase I that uses Zn(++) as cofactor; This family includes eukaryotic glyoxalase I that ...
 24-165 3.71e-85

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: 246.85  E-value: 3.71e-85
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600304  24 FNHTMLRVKDPKRSLDFYSRVLGMRLLRRLDFEEGRFSLYFLAMTRGEEVPDavDERQRYTFGRQSVLELTHNWGSESDD 103
Cdd:cd07233   1 FNHTMLRVKDPKKSLKFYTEVLGMKLLRKKDFPEMKFSLYFLGYEDPKDIPK--DPRTAWVFSREGTLELTHNWGTENDE 78

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15600304 104 SQ-YHNGNQDPRGFGHICFSVPDLVAACERFETLGVNFVKPLDRG-MKNVAFISDPDGYWVEIV 165
Cdd:cd07233  79 DPvYHNGNSDPRGFGHIGIAVDDVYAACERFEELGVKFKKKPDDGkMKGIAFIKDPDGYWIEIL 142
PLN03042 PLN03042
Lactoylglutathione lyase; Provisional
 9-167 1.35e-83

Lactoylglutathione lyase; Provisional


Pssm-ID: 215548  Cd Length: 185  Bit Score: 244.34  E-value: 1.35e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600304    9 PGICMEPDAITQEYVFNHTMLRVKDPKRSLDFYSRVLGMRLLRRLDFEEGRFSLYFLAMTRGEEVPDAVDERQRYTFGRQ 88
Cdd:PLN03042  13 PGLCGNPDEATKGYIMQQTMFRIKDPKASLDFYSRVLGMSLLKRLDFPEMKFSLYFLGYEDSETAPTDPPERTVWTFGRK 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600304   89 SVLELTHNWGSESDDS--QYHNGNQDPRGFGHICFSVPDLVAACERFETLGVNFVK-PLDRGMKNVAFISDPDGYWVEIV 165
Cdd:PLN03042  93 ATIELTHNWGTESDPEfkGYHNGNSDPRGFGHIGITVDDVYKACERFEKLGVEFVKkPDDGKMKGLAFIKDPDGYWIEIF 172


                 ..
gi 15600304  166 QA 167
Cdd:PLN03042 173 DL 174
PLN02367 PLN02367
lactoylglutathione lyase
 9-164 1.87e-73

lactoylglutathione lyase


Pssm-ID: 177995  Cd Length: 233  Bit Score: 220.64  E-value: 1.87e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600304    9 PGICMEPDAITQEYVFNHTMLRVKDPKRSLDFYSRVLGMRLLRRLDFEEGRFSLYFLAMTRGEEVPDAVDERQRYTFGRQ 88
Cdd:PLN02367  61 PGLSTSPDEATKGYIMQQTMYRIKDPKASLDFYSRVLGMSLLKRLDFPEMKFSLYFMGYEDTASAPTDPTERTVWTFGQK 140

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15600304   89 SVLELTHNWGSESDD--SQYHNGNQDPRGFGHICFSVPDLVAACERFETLGVNFV-KPLDRGMKNVAFISDPDGYWVEI 164
Cdd:PLN02367 141 ATIELTHNWGTESDPdfKGYHNGNSEPRGFGHIGITVDDVYKACERFEELGVEFVkKPNDGKMKGIAFIKDPDGYWIEI 219
glyox_I TIGR00068
lactoylglutathione lyase; Lactoylglutathione lyase is also known as aldoketomutase and ...
 10-176 5.57e-61

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: 185.78  E-value: 5.57e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600304    10 GICMEPDAITQEYVFNHTMLRVKDPKRSLDFYSRVLGMRLLRRLDFEEGRFSLYFLAMTRGEEvpdavderqrytfgrQS 89
Cdd:TIGR00068   4 SGDLVADPKTKKRRLLHTMLRVGDLDKSLDFYTEVLGMKLLRKRDFPEMKFSLAFLGYGDETS---------------AA 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600304    90 VLELTHNWGSESddsqYHNGNqdprGFGHICFSVPDLVAACERFETLGVNFVK---PLDRGMKNVAFISDPDGYWVEIVQ 166
Cdd:TIGR00068  69 VIELTHNWGTEK----YDLGN----GFGHIAIGVDDVYKACERVRALGGNVVRepgPVKGGTTVIAFVEDPDGYKIELIQ 140

                         170
                  ....*....|
gi 15600304   167 aslNGEMGRG 176
Cdd:TIGR00068 141 ---RKSTKDG 147
GloA COG0346
Catechol 2,3-dioxygenase or related enzyme, vicinal oxygen chelate (VOC) family [Secondary ...
 24-166 1.89e-34

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: 117.79  E-value: 1.89e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600304  24 FNHTMLRVKDPKRSLDFYSRVLGMRLLRRLDFEEGRFSLYFLamtrgeevpdavderqryTFGRQSVLELTHNWGSESDD 103
Cdd:COG0346   3 LHHVTLRVSDLEASLAFYTDVLGLELVKRTDFGDGGFGHAFL------------------RLGDGTELELFEAPGAAPAP 64

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15600304 104 SqyhngnqdPRGFGHICFSVPDLVAACERFETLGVNFVK-PLDRGM-KNVAFISDPDGYWVEIVQ 166
Cdd:COG0346  65 G--------GGGLHHLAFRVDDLDAAYARLRAAGVEIEGePRDRAYgYRSAYFRDPDGNLIELVE 121
GlxI_Ni cd16358
Glyoxalase I that uses Ni(++) as cofactor; This family includes Escherichia coil and other ...
 26-165 2.17e-34

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: 117.50  E-value: 2.17e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600304  26 HTMLRVKDPKRSLDFYSRVLGMRLLRRLDFEEGRFSLYFLAMTrgeevpdavDERQrytfgrQSVLELTHNWGSESddsq 105
Cdd:cd16358   3 HTMLRVGDLDRSIKFYTEVLGMKLLRKRDYPEGKYTLAFVGYG---------DEDE------NTVLELTYNWGVDK---- 63

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15600304 106 YHNGNqdprGFGHICFSVPDLVAACERFETLGVNFVK---PLDRGMKNVAFISDPDGYWVEIV 165
Cdd:cd16358  64 YDLGT----AYGHIAIGVEDVYETCERIRKKGGKVTRepgPMKGGTTVIAFVEDPDGYKIELI 122
Glyoxalase pfam00903
Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;
24-164 2.35e-27

Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;


Pssm-ID: 395724 [Multi-domain]  Cd Length: 121  Bit Score: 99.44  E-value: 2.35e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600304    24 FNHTMLRVKDPKRSLDFYSRVLGMRLLRRLDFEEGRfslyflamtrgeevpdavDERQRYTFGRQSVLELTHNWGSESDD 103
Cdd:pfam00903   2 IDHVALRVGDLEKSLDFYTDVLGFKLVEETDAGEEG------------------GLRSAFFLAGGRVLELLLNETPPPAA 63

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15600304   104 SQYHngnqdPRGFGHICFSVPDLVAACERFETLGVNFVKPLDRGM--KNVAFISDPDGYWVEI 164
Cdd:pfam00903  64 AGFG-----GHHIAFIAFSVDDVDAAYDRLKAAGVEIVREPGRHGwgGRYSYFRDPDGNLIEL 121
PRK10291 PRK10291
glyoxalase I; Provisional
 28-176 1.76e-23

glyoxalase I; Provisional


Pssm-ID: 182358  Cd Length: 129  Bit Score: 89.70  E-value: 1.76e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600304   28 MLRVKDPKRSLDFYSRVLGMRLLRRLDFEEGRFSLYFLAMtrGEEVPDAvderqrytfgrqsVLELTHNWGSESddsqYH 107
Cdd:PRK10291   1 MLRVGDLQRSIDFYTNVLGMKLLRTSENPEYKYSLAFVGY--GPETEEA-------------VIELTYNWGVDK----YE 61

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15600304  108 NGNqdprGFGHICFSVPDLVAACERFETLGVNFVK---PLDRGMKNVAFISDPDGYWVEIVQASlngEMGRG 176
Cdd:PRK10291  62 LGT----AYGHIALSVDNAAEACEKIRQNGGNVTReagPVKGGTTVIAFVEDPDGYKIELIEEK---DAGRG 126
PLN02300 PLN02300
lactoylglutathione lyase
 26-166 5.36e-18

lactoylglutathione lyase


Pssm-ID: 215169 [Multi-domain]  Cd Length: 286  Bit Score: 79.05  E-value: 5.36e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600304   26 HTMLRVKDPKRSLDFYSRVLGMRLLRRLDFEEGRFSLYFLAmtrgeevpdavderqrytFGRQS---VLELTHNWGSESd 102
Cdd:PLN02300  27 HVVYRVGDLDRTIKFYTECLGMKLLRKRDIPEEKYTNAFLG------------------YGPEDsnfVVELTYNYGVDK- 87

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15600304  103 dsqYHNGNqdprGFGHICFSVPDLVAACERFETLGVNFVK---PLDRGMKNVAFISDPDGYWVEIVQ 166
Cdd:PLN02300  88 ---YDIGT----GFGHFGIAVEDVAKTVELVKAKGGKVTRepgPVKGGKSVIAFVKDPDGYKFELIQ 147
CatE COG2514
Catechol-2,3-dioxygenase [Secondary metabolites biosynthesis, transport and catabolism];
24-165 3.10e-14

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


Pssm-ID: 442004 [Multi-domain]  Cd Length: 141  Bit Score: 66.13  E-value: 3.10e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600304  24 FNHTMLRVKDPKRSLDFYSRVLGMRLLRRldfEEGRFSLyflamtrgeevpdavderqrYTFGRQSVLELThnwgsESDD 103
Cdd:COG2514   4 LGHVTLRVRDLERSAAFYTDVLGLEVVER---EGGRVYL--------------------RADGGEHLLVLE-----EAPG 55

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15600304 104 SQYHNGnqdPRGFGHICFSVP---DLVAACERFETLGVNFVKPLDRGMKNVAFISDPDGYWVEIV 165
Cdd:COG2514  56 APPRPG---AAGLDHVAFRVPsraDLDAALARLAAAGVPVEGAVDHGVGESLYFRDPDGNLIELY 117
VOC cd06587
vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate (VOC) superfamily is composed ...
 26-164 5.20e-14

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: 64.85  E-value: 5.20e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600304  26 HTMLRVKDPKRSLDFYSRVLGMRLLRRLDFEEGRFslyflamtrgeevpdavderqrYTFGRQSVLELTHNWGSESDdsq 105
Cdd:cd06587   1 HVALRVPDLDASVAFYEEVLGFEVVSRNEGGGFAF----------------------LRLGPGLRLALLEGPEPERP--- 55

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15600304 106 yhngnqDPRGFGHICFSVPDLVAACERFETLGVNFVK----PLDRGMKNVAFISDPDGYWVEI 164
Cdd:cd06587  56 ------GGGGLFHLAFEVDDVDEVDERLREAGAEGELvappVDDPWGGRSFYFRDPDGNLIEF 112
VOC_like cd07264
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 26-167 2.65e-12

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: 60.42  E-value: 2.65e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600304  26 HTMLRVKDPKRSLDFYSRVLGmrLLRRLDFEEGRFSLYFLAmtrgeevpdavderqrytfgrQSVLELThnwgsESDDSQ 105
Cdd:cd07264   3 YIVLYVDDFAASLRFYRDVLG--LPPRFLHEEGEYAEFDTG---------------------ETKLALF-----SRKEMA 54

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15600304 106 YHNGNQDPRGFGHICFSVPDLVAACERFETLGVNFVKPLDR---GMKnVAFISDPDGYWVEIVQA 167
Cdd:cd07264  55 RSGGPDRRGSAFELGFEVDDVEATVEELVERGAEFVREPANkpwGQT-VAYVRDPDGNLIEICEP 118
VOC COG3324
Lactoylglutathione lyase-related enzyme, vicinal oxygen chelate (VOC) family [General function ...
 24-168 9.21e-12

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


Pssm-ID: 442553 [Multi-domain]  Cd Length: 119  Bit Score: 58.88  E-value: 9.21e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600304  24 FNHTMLRVKDPKRSLDFYSRVLGMRLLRRLDFEEGrfslyFLAMTRGEEVPDAVderqrytfgrqsvlelthnwgsesdd 103
Cdd:COG3324   5 IVWVELPVDDLERAKAFYEEVFGWTFEDDAGPGGD-----YAEFDTDGGQVGGL-------------------------- 53

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15600304 104 sqyHNGNQDPRGFG-HICFSVPDLVAACERFETLGVNFVKPLDRGMKN--VAFISDPDGYWVEIVQAS 168
Cdd:COG3324  54 ---MPGAEEPGGPGwLLYFAVDDLDAAVARVEAAGGTVLRPPTDIPPWgrFAVFRDPEGNRFGLWQPA 118
PLN02300 PLN02300
lactoylglutathione lyase
 28-160 1.00e-09

lactoylglutathione lyase


Pssm-ID: 215169 [Multi-domain]  Cd Length: 286  Bit Score: 55.94  E-value: 1.00e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600304   28 MLRVKDPKRSLDFYSRVLGMRLLRRLDFEEGRFSLYFlaMTRGEEvpdavderqrytfGRQSVLELTHNWGSesddSQYH 107
Cdd:PLN02300 159 MLRVGDLDRSIKFYEKAFGMKLLRKRDNPEYKYTIAM--MGYGPE-------------DKTTVLELTYNYGV----TEYT 219

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 15600304  108 NGNqdprGFGHICFSVPDLVAACERFETLGVNFVK---PLDrGM--KNVAFIsDPDGY 160
Cdd:PLN02300 220 KGN----AYAQIAIGTDDVYKTAEAIKLVGGKITRepgPLP-GIntKITACL-DPDGW 271
VOC_like cd07245
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 24-164 2.03e-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: 319909 [Multi-domain]  Cd Length: 117  Bit Score: 47.31  E-value: 2.03e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600304  24 FNHTMLRVKDPKRSLDFYSRVLGmrllrrldFEEGrfslyflamtrgeEVPDAvDERQRYTF--GRQSVLELthnwGSES 101
Cdd:cd07245   1 LDHVALACPDLERARRFYTDVLG--------LEEV-------------PRPPF-LKFGGAWLylGGGQQIHL----VVEQ 54

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15600304 102 DDSQYHNGNQDPRGfGHICFSVPDLVAACERFETLGVNFVKPLDRGMKNVA-FISDPDGYWVEI 164
Cdd:cd07245  55 NPSELPRPEHPGRD-RHPSFSVPDLDALKQRLKEAGIPYTESTSPGGGVTQlFFRDPDGNRLEF 117
GLOD5 cd07253
Human glyoxalase domain-containing protein 5 and similar proteins; Uncharacterized subfamily ...
 26-164 2.19e-06

Human glyoxalase domain-containing protein 5 and similar proteins; Uncharacterized subfamily of VOC family contains human glyoxalase domain-containing protein 5 and similar proteins. The vicinal oxygen chelate (VOC) superfamily is composed of structurally related proteins with paired beta.alpha.beta.beta.beta motifs that provide a metal coordination environment with two or three open or readily accessible coordination sites to promote direct electrophilic participation of the metal ion in catalysis. VOC domain is found in a variety of structurally related metalloproteins, including the bleomycin resistance protein, glyoxalase I, and type I ring-cleaving dioxygenases. A bound metal ion is required for protein activities for the members of this superfamily. A variety of metal ions have been found in the catalytic centers of these proteins including Fe(II), Mn(II), Zn(II), Ni(II) and Mg(II). The protein superfamily contains members with or without domain swapping. The proteins of this family share three conserved metal binding amino acids with the type I extradiol dioxygenases, which shows no domain swapping.


Pssm-ID: 319916 [Multi-domain]  Cd Length: 123  Bit Score: 44.52  E-value: 2.19e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600304  26 HTMLRVKDPKRSLDFYSRVLGMRLLRrldFEEGRFSLyflamtrgeevpdavderqryTFGRQSV--LELTHNWGSESDD 103
Cdd:cd07253   6 HLVLTVKDIERTIDFYTKVLGMTVVT---FKEGRKAL---------------------RFGNQKInlHQKGKEFEPKASA 61

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15600304 104 SQyhngnqdpRGFGHICFSV-PDLVAACERFETLGVNFVK-PLDR----GMKNVAFISDPDGYWVEI 164
Cdd:cd07253  62 PT--------PGSADLCFITeTPIDEVLEHLEACGVTIEEgPVKRtgalGPILSIYFRDPDGNLIEL 120
Glyoxalase_4 pfam13669
Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;
31-141 5.56e-06

Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;


Pssm-ID: 463951 [Multi-domain]  Cd Length: 109  Bit Score: 43.42  E-value: 5.56e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600304    31 VKDPKRSLDFYSRVLGMRLLRRLDFEEGRFSLYFLamtrgeevpdavderqrYTFGRQSVLELTHNWGsesDDSQYHNGn 110
Cdd:pfam13669   7 VPDLDRALALWGALLGLGPEGDYRSEPQNVDLAFA-----------------LLGDGPVEVELIQPLD---GDSPLARH- 65

                          90       100       110
                  ....*....|....*....|....*....|.
gi 15600304   111 qdPRGFGHICFSVPDLVAACERFETLGVNFV 141
Cdd:pfam13669  66 --GPGLHHLAYWVDDLDAAVARLLDQGYRVA 94
VOC_like cd07263
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 26-166 1.01e-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: 319924 [Multi-domain]  Cd Length: 120  Bit Score: 42.67  E-value: 1.01e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600304  26 HTMLRVKDPKRSLDFYSRVLGMRLLRRLDFEEGRFslYFLAMTRGEEVpdavderqrytfgrQSVLElthnwgsesDDSQ 105
Cdd:cd07263   1 QVMLYVDDQDKALDFYVEKLGFEVVEDVPMGGMRW--VTVAPPGSPGT--------------SLLLE---------PKAH 55

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15600304 106 YHNGNQDPR---GFGHICFSVPDLVAACERFETLGVNFVK-PLDRGMKNVAFISDPDGYWVEIVQ 166
Cdd:cd07263  56 PAQMPQSPEaagGTPGILLATDDIDATYERLTAAGVTFVQePTQMGGGRVANFRDPDGNLFALME 120
GLOD4_N cd08358
N-terminal domain of human glyoxalase domain-containing protein 4 and similar proteins; ...
 26-160 3.60e-05

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


Pssm-ID: 319946  Cd Length: 127  Bit Score: 41.58  E-value: 3.60e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600304  26 HTMLRVKDPKRSLDFYSRVLGMRLLRRLDFEEGrfslyFLAMTRGeevpdAVDERQRYT---FGRQS---VLELTHNWGS 99
Cdd:cd08358   5 HFVFKVGDRNKTIKFYREILGMKVLRHEEFEEG-----CKAACNG-----PYDGKWSKTmvgYGPEDdhfVVELTYNYGI 74

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15600304 100 esddSQYHNGNQdprgFGHICFSVPDLVAACERFETlgvnfvkPLDRGMKNVAFISDPDGY 160
Cdd:cd08358  75 ----GDYELGND----FLGITIHSKQAVSRAKKHNW-------PVTQVGDGVYEVKAPGGY 120
MMCE cd07249
Methylmalonyl-CoA epimerase (MMCE); MMCE, also called methylmalonyl-CoA racemase (EC 5.1.99.1) ...
 31-166 3.93e-05

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: 41.41  E-value: 3.93e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600304  31 VKDPKRSLDFYSRVLGMRLLRRLDFEEGRFSLYFLAMTRGEevpdavderqrytfgrqsvLELTHNWGsesDDSQYHNGN 110
Cdd:cd07249   8 VPDLDEALKFYEDVLGVKVSEPEELEEQGVRVAFLELGNTQ-------------------IELLEPLG---EDSPIAKFL 65

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15600304 111 QDPR-GFGHICFSVPDLVAACERFETLGVNFV----KPLDRGMKnVAFISDPD--GYWVEIVQ 166
Cdd:cd07249  66 DKKGgGLHHIAFEVDDIDAAVEELKAQGVRLLsegpRIGAHGKR-VAFLHPKDtgGVLIELVE 127
FosA cd07244
fosfomycin resistant protein subfamily FosA; This subfamily family contains FosA, a fosfomycin ...
 24-54 5.44e-05

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


Pssm-ID: 319908 [Multi-domain]  Cd Length: 121  Bit Score: 40.73  E-value: 5.44e-05
                        10        20        30
                ....*....|....*....|....*....|.
gi 15600304  24 FNHTMLRVKDPKRSLDFYSRVLGMRLLRRLD 54
Cdd:cd07244   2 INHITLAVSDLERSLAFYVDLLGFKPHVRWD 32
PhnB COG2764
Zn-dependent glyoxalase, PhnB family [Energy production and conversion];
29-167 8.85e-05

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


Pssm-ID: 442048 [Multi-domain]  Cd Length: 118  Bit Score: 40.22  E-value: 8.85e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600304  29 LRVKDPKRSLDFYSRVLGMRLLRRLDFEEGRfsLYFLAMTRGEevpdavderqrytfgrqSVLELthnwGSESDDSQYHN 108
Cdd:COG2764   6 LVVDDAEEALEFYEDVFGFEVVFRMTDPDGK--IMHAELRIGG-----------------SVLML----SDAPPDSPAAE 62

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15600304 109 GNQdprgfGHICFSVPDLVAACERFETLGVNFVKPL------DRgmknVAFISDPDGYWVEIVQA 167
Cdd:COG2764  63 GNG-----VSLSLYVDDVDALFARLVAAGATVVMPLqdtfwgDR----FGMVRDPFGVLWMINTP 118
VOC_Bs_YwkD_like cd08352
vicinal oxygen chelate (VOC) family protein Bacillus subtilis YwkD and similar proteins; ...
 24-164 1.80e-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: 39.45  E-value: 1.80e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600304  24 FNHTMLRVKDPKRSLDFYSRVLGMRLLRRLDFEEGRFSLYFLAMTRGE-EV---PDAVDerqrytfgRQSVLELThnwgs 99
Cdd:cd08352   3 IHHIAIICSDYEKSKDFYVDKLGFEIIREHYRPERNDIKLDLALGGYQlELfikPDAPA--------RPSYPEAL----- 69

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15600304 100 esddsqyhngnqdprGFGHICFSVPDLVAACERFETLGVNfVKPL--DR--GmKNVAFISDPDGYWVEI 164
Cdd:cd08352  70 ---------------GLRHLAFKVEDVEATVAELKSLGIE-TEPIrvDDftG-KKFTFFFDPDGLPLEL 121
HppD COG3185
4-hydroxyphenylpyruvate dioxygenase and related hemolysins [Amino acid transport and ...
 38-160 1.09e-03

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: 38.33  E-value: 1.09e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600304  38 LDFYSRVLGMRLLRRLDFEEGRFSLYFLAMTrgeeVPDavderqrytfgRQSVLELthNwGSESDDSQ------YHNGNq 111
Cdd:COG3185 163 VLFYEDVLGFEEIREEDIEDPYQGVRSAVLQ----SPD-----------GKVRIPL--N-EPTSPDSQiaefleKYRGE- 223

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
gi 15600304 112 dprGFGHICFSVPDLVAACERFETLGvnfvkpldrgmknVAFISDPDGY 160
Cdd:COG3185 224 ---GIQHIAFATDDIEATVAALRARG-------------VRFLDIPDNY 256
VOC_ShValD_like cd16361
vicinal oxygen chelate (VOC) family protein similar to Streptomyces hygroscopicus ValD protein; ...
 24-166 1.46e-03

vicinal oxygen chelate (VOC) family protein similar to Streptomyces hygroscopicus ValD protein; This subfamily of vicinal oxygen chelate (VOC) family protein includes Streptomyces hygroscopicus ValD protein and similar proteins. ValD protein functions in validamycin biosynthetic pathway. 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: 319968  Cd Length: 150  Bit Score: 37.31  E-value: 1.46e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600304  24 FNHTMLRVKDPKRSLDFYSRVLGMRLLRRL-DFEEGRfslyflaMTRGEEVPDAVDERqrYTFGRQSVLELTHNWGSESd 102
Cdd:cd16361   2 VNHVGITVPDLDAAVEFYTDVLGAEVVYRStPLAEGD-------RGGGEMRAAGFVPG--FARARIAMLRLGPGPGIEL- 71

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15600304 103 dSQYHNGNQDP-------RGFGHICFSVPDLVAACERFETLG--------VNFVKPLDRGMKNVaFISDPDGYWVEIVQ 166
Cdd:cd16361  72 -FEYKGPEQRApvprnsdVGIFHFALQVDDVEAAAERLAAAGgkvlmgprEIPDGGPGKGNRMV-YLRDPWGTLIELVS 148
VOC_BsCatE_like_N cd07255
N-terminal of Bacillus subtilis CatE like protein; Uncharacterized subfamily of VOC ...
 25-164 1.51e-03

N-terminal of Bacillus subtilis CatE like protein; Uncharacterized subfamily of VOC superfamily contains Bacillus subtilis CatE and similar proteins. CatE is proposed to function as Catechol-2,3-dioxygenase. VOC is composed of structurally related proteins with paired beta.alpha.beta.beta.beta motifs that provide a metal coordination environment with two or three open or readily accessible coordination sites to promote direct electrophilic participation of the metal ion in catalysis. VOC domain is found in a variety of structurally related metalloproteins, including the bleomycin resistance protein, glyoxalase I, and type I ring-cleaving dioxygenases. A bound metal ion is required for protein activities for the members of this superfamily. A variety of metal ions have been found in the catalytic centers of these proteins including Fe(II), Mn(II), Zn(II), Ni(II) and Mg(II). The protein superfamily contains members with or without domain swapping. The proteins of this family share three conserved metal binding amino acids with the type I extradiol dioxygenases, which shows no domain swapping.


Pssm-ID: 319918  Cd Length: 124  Bit Score: 36.91  E-value: 1.51e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600304  25 NHTMLRVKDPKRSLDFYSRVLGMRLLRR------LDFEEGRFSLyflamtRGEEVPDAVDERQRYTfgrqsvlelthnwg 98
Cdd:cd07255   4 GRVTLKVADLERQSAFYQNVIGLSVLKQnasrayLGVDGKQVLL------VLEAIPDAVLAPRSTT-------------- 63

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15600304  99 sesddsqyhngnqdprGFGHICFSVPD---LVAACERFETLGVnFVKPLDRGMKNVAFISDPDGYWVEI 164
Cdd:cd07255  64 ----------------GLYHFAILLPDrkaLGRALAHLAEHGP-LIGAADHGVSEAIYLSDPEGNGIEI 115
GLOD4_C cd16357
C-terminal domain of human glyoxalase domain-containing protein 4 and similar proteins; ...
 28-164 2.94e-03

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


Pssm-ID: 319964  Cd Length: 114  Bit Score: 35.99  E-value: 2.94e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600304  28 MLRVKDPKRSLDFYSRVLGMRLLRRldfEEGRFSLYFlamtrGEEvpdavderqrytfgrQSVLELThnwgsESDDSQYH 107
Cdd:cd16357   3 SLAVSDLEKSIDYWSDLLGMKVFEK---SEKSALLGY-----GED---------------QAKLELV-----DIPEPVDH 54

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15600304 108 NgnqdpRGFGHICFSVP--------DLVAACErfETLGVNFVKpLDRGMK---NVAFISDPDGYwvEI 164
Cdd:cd16357  55 G-----TAFGRIAFSCPadelppieEKVKAAG--QTILTPLVS-LDTPGKatvQVVILADPDGH--EI 112
PcpA_N_like cd08346
N-terminal domain of Sphingobium chlorophenolicum 2,6-dichloro-p-hydroquinone 1,2-dioxygenase ...
 24-64 7.22e-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: 34.96  E-value: 7.22e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|...
gi 15600304  24 FNHTMLRVKDPKRSLDFYSRVLGMRLLRRLDFEEGR--FSLYF 64
Cdd:cd08346   2 IHHITAITGDAQENVDFYVKVLGLRLVKKTVNQDDPpmYHLYY 44
 
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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