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Conserved domains on  [gi|489785904|ref|WP_003689795|]
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lactoylglutathione lyase [Neisseria gonorrhoeae]

Protein Classification

VOC family protein( domain architecture ID 50733)

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

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
VOC super family cl14632
vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate (VOC) superfamily is composed ...
 2-126 2.76e-74

vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate (VOC) superfamily is composed of structurally related proteins with paired beta.alpha.beta.beta.beta motifs that provide a metal coordination environment with two or three open or readily accessible coordination sites to promote direct electrophilic participation of the metal ion in catalysis. VOC is found in a variety of structurally related metalloproteins, including the type I extradiol dioxygenases, glyoxalase I and a group of antibiotic resistance proteins. A bound metal ion is required for protein activities for the members of this superfamily. A variety of metal ions have been found in the catalytic centers of these proteins including Fe(II), Mn(II), Zn(II), Ni(II) and Mg(II). Type I extradiol dioxygenases catalyze the incorporation of both atoms of molecular oxygen into aromatic substrates, which results in the cleavage of aromatic rings. They are key enzymes in the degradation of aromatic compounds. Type I extradiol dioxygenases include class I and class II enzymes. Class I and II enzymes show sequence similarity; the two-domain class II enzymes evolved from a class I enzyme through gene duplication. Glyoxylase I catalyzes the glutathione-dependent inactivation of toxic methylglyoxal, requiring zinc or nickel ions for activity. The antibiotic resistance proteins in this family use a variety of mechanisms to block the function of antibiotics. Bleomycin resistance protein (BLMA) sequesters bleomycin's activity by directly binding to it. Whereas, three types of fosfomycin resistance proteins employ different mechanisms to render fosfomycin inactive by modifying the fosfomycin molecule. Although the proteins in this superfamily are functionally distinct, their structures are similar. The difference among the three dimensional structures of the three types of proteins in this superfamily is interesting from an evolutionary perspective. Both glyoxalase I and BLMA show domain swapping between subunits. However, there is no domain swapping for type 1 extradiol dioxygenases.


The actual alignment was detected with superfamily member TIGR00068:

Pssm-ID: 472697  Cd Length: 150  Bit Score: 217.75  E-value: 2.76e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489785904    2 GNLEKSLDSYQNVLGMKLLRRKDYPEGRFTLAFVGYGDETDSTVLELTHNWDTERYDLGDAYGHIAVEVDDAYEACERVK 81
Cdd:TIGR00068  26 GDLDKSLDFYTEVLGMKLLRKRDFPEMKFSLAFLGYGDETSAAVIELTHNWGTEKYDLGNGFGHIAIGVDDVYKACERVR 105

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 489785904   82 RQGGNVVREAGLMKHGTTVIAFVEDPDGCKIEFVQKKSGDDSVAY 126
Cdd:TIGR00068 106 ALGGNVVREPGPVKGGTTVIAFVEDPDGYKIELIQRKSTKDGLGN 150
 
Name Accession Description Interval E-value
glyox_I TIGR00068
lactoylglutathione lyase; Lactoylglutathione lyase is also known as aldoketomutase and ...
 2-126 2.76e-74

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: 217.75  E-value: 2.76e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489785904    2 GNLEKSLDSYQNVLGMKLLRRKDYPEGRFTLAFVGYGDETDSTVLELTHNWDTERYDLGDAYGHIAVEVDDAYEACERVK 81
Cdd:TIGR00068  26 GDLDKSLDFYTEVLGMKLLRKRDFPEMKFSLAFLGYGDETSAAVIELTHNWGTEKYDLGNGFGHIAIGVDDVYKACERVR 105

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 489785904   82 RQGGNVVREAGLMKHGTTVIAFVEDPDGCKIEFVQKKSGDDSVAY 126
Cdd:TIGR00068 106 ALGGNVVREPGPVKGGTTVIAFVEDPDGYKIELIQRKSTKDGLGN 150
GlxI_Ni cd16358
Glyoxalase I that uses Ni(++) as cofactor; This family includes Escherichia coil and other ...
 2-115 1.25e-69

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: 204.94  E-value: 1.25e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489785904   2 GNLEKSLDSYQNVLGMKLLRRKDYPEGRFTLAFVGYGDETDSTVLELTHNWDTERYDLGDAYGHIAVEVDDAYEACERVK 81
Cdd:cd16358    9 GDLDRSIKFYTEVLGMKLLRKRDYPEGKYTLAFVGYGDEDENTVLELTYNWGVDKYDLGTAYGHIAIGVEDVYETCERIR 88

                         90       100       110
                 ....*....|....*....|....*....|....
gi 489785904  82 RQGGNVVREAGLMKHGTTVIAFVEDPDGCKIEFV 115
Cdd:cd16358   89 KKGGKVTREPGPMKGGTTVIAFVEDPDGYKIELI 122
PRK10291 PRK10291
glyoxalase I; Provisional
 1-118 1.89e-49

glyoxalase I; Provisional


Pssm-ID: 182358  Cd Length: 129  Bit Score: 154.03  E-value: 1.89e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489785904   1 MGNLEKSLDSYQNVLGMKLLRRKDYPEGRFTLAFVGYGDETDSTVLELTHNWDTERYDLGDAYGHIAVEVDDAYEACERV 80
Cdd:PRK10291   4 VGDLQRSIDFYTNVLGMKLLRTSENPEYKYSLAFVGYGPETEEAVIELTYNWGVDKYELGTAYGHIALSVDNAAEACEKI 83

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 489785904  81 KRQGGNVVREAGLMKHGTTVIAFVEDPDGCKIEFVQKK 118
Cdd:PRK10291  84 RQNGGNVTREAGPVKGGTTVIAFVEDPDGYKIELIEEK 121
GloA COG0346
Catechol 2,3-dioxygenase or related enzyme, vicinal oxygen chelate (VOC) family [Secondary ...
 3-120 1.72e-32

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: 110.85  E-value: 1.72e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489785904   3 NLEKSLDSYQNVLGMKLLRRKDYPEGRFTLAFVGYGDETdstVLELTHNWDTERYDLGDAYGHIAVEVDDAYEACERVKR 82
Cdd:COG0346   12 DLEASLAFYTDVLGLELVKRTDFGDGGFGHAFLRLGDGT---ELELFEAPGAAPAPGGGGLHHLAFRVDDLDAAYARLRA 88

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 489785904  83 QGGNVVREAGLMKHGTTViAFVEDPDGCKIEFVQKKSG 120
Cdd:COG0346   89 AGVEIEGEPRDRAYGYRS-AYFRDPDGNLIELVEPPPG 125
Glyoxalase pfam00903
Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;
2-114 4.60e-21

Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;


Pssm-ID: 395724 [Multi-domain]  Cd Length: 121  Bit Score: 81.73  E-value: 4.60e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489785904    2 GNLEKSLDSYQNVLGMKLLRRKDYPEGRFTLAFVGYGDETdstVLELTHNWDTERYDLG---DAYGHIAVEVDDAYEACE 78
Cdd:pfam00903  10 GDLEKSLDFYTDVLGFKLVEETDAGEEGGLRSAFFLAGGR---VLELLLNETPPPAAAGfggHHIAFIAFSVDDVDAAYD 86

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 489785904   79 RVKRQGGNVVREAGLMKHGTTVIaFVEDPDGCKIEF 114
Cdd:pfam00903  87 RLKAAGVEIVREPGRHGWGGRYS-YFRDPDGNLIEL 121
 
Name Accession Description Interval E-value
glyox_I TIGR00068
lactoylglutathione lyase; Lactoylglutathione lyase is also known as aldoketomutase and ...
 2-126 2.76e-74

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: 217.75  E-value: 2.76e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489785904    2 GNLEKSLDSYQNVLGMKLLRRKDYPEGRFTLAFVGYGDETDSTVLELTHNWDTERYDLGDAYGHIAVEVDDAYEACERVK 81
Cdd:TIGR00068  26 GDLDKSLDFYTEVLGMKLLRKRDFPEMKFSLAFLGYGDETSAAVIELTHNWGTEKYDLGNGFGHIAIGVDDVYKACERVR 105

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 489785904   82 RQGGNVVREAGLMKHGTTVIAFVEDPDGCKIEFVQKKSGDDSVAY 126
Cdd:TIGR00068 106 ALGGNVVREPGPVKGGTTVIAFVEDPDGYKIELIQRKSTKDGLGN 150
GlxI_Ni cd16358
Glyoxalase I that uses Ni(++) as cofactor; This family includes Escherichia coil and other ...
 2-115 1.25e-69

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: 204.94  E-value: 1.25e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489785904   2 GNLEKSLDSYQNVLGMKLLRRKDYPEGRFTLAFVGYGDETDSTVLELTHNWDTERYDLGDAYGHIAVEVDDAYEACERVK 81
Cdd:cd16358    9 GDLDRSIKFYTEVLGMKLLRKRDYPEGKYTLAFVGYGDEDENTVLELTYNWGVDKYDLGTAYGHIAIGVEDVYETCERIR 88

                         90       100       110
                 ....*....|....*....|....*....|....
gi 489785904  82 RQGGNVVREAGLMKHGTTVIAFVEDPDGCKIEFV 115
Cdd:cd16358   89 KKGGKVTREPGPMKGGTTVIAFVEDPDGYKIELI 122
PRK10291 PRK10291
glyoxalase I; Provisional
 1-118 1.89e-49

glyoxalase I; Provisional


Pssm-ID: 182358  Cd Length: 129  Bit Score: 154.03  E-value: 1.89e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489785904   1 MGNLEKSLDSYQNVLGMKLLRRKDYPEGRFTLAFVGYGDETDSTVLELTHNWDTERYDLGDAYGHIAVEVDDAYEACERV 80
Cdd:PRK10291   4 VGDLQRSIDFYTNVLGMKLLRTSENPEYKYSLAFVGYGPETEEAVIELTYNWGVDKYELGTAYGHIALSVDNAAEACEKI 83

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 489785904  81 KRQGGNVVREAGLMKHGTTVIAFVEDPDGCKIEFVQKK 118
Cdd:PRK10291  84 RQNGGNVTREAGPVKGGTTVIAFVEDPDGYKIELIEEK 121
PLN02300 PLN02300
lactoylglutathione lyase
 2-118 3.62e-41

lactoylglutathione lyase


Pssm-ID: 215169 [Multi-domain]  Cd Length: 286  Bit Score: 137.99  E-value: 3.62e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489785904   2 GNLEKSLDSYQNVLGMKLLRRKDYPEGRFTLAFVGYGDETDSTVLELTHNWDTERYDLGDAYGHIAVEVDDAYEACERVK 81
Cdd:PLN02300  33 GDLDRTIKFYTECLGMKLLRKRDIPEEKYTNAFLGYGPEDSNFVVELTYNYGVDKYDIGTGFGHFGIAVEDVAKTVELVK 112

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 489785904  82 RQGGNVVREAGLMKHGTTVIAFVEDPDGCKIEFVQKK 118
Cdd:PLN02300 113 AKGGKVTREPGPVKGGKSVIAFVKDPDGYKFELIQRG 149
GlxI_Zn cd07233
Glyoxalase I that uses Zn(++) as cofactor; This family includes eukaryotic glyoxalase I that ...
 3-115 3.38e-39

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: 128.60  E-value: 3.38e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489785904   3 NLEKSLDSYQNVLGMKLLRRKDYPEGRFTLAFVGYGDETDS-------------TVLELTHNWDTER-----YDLGDA-- 62
Cdd:cd07233   10 DPKKSLKFYTEVLGMKLLRKKDFPEMKFSLYFLGYEDPKDIpkdprtawvfsreGTLELTHNWGTENdedpvYHNGNSdp 89

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 489785904  63 --YGHIAVEVDDAYEACERVKRQGGNVVR--EAGLMKHgttvIAFVEDPDGCKIEFV 115
Cdd:cd07233   90 rgFGHIGIAVDDVYAACERFEELGVKFKKkpDDGKMKG----IAFIKDPDGYWIEIL 142
PLN02300 PLN02300
lactoylglutathione lyase
 2-115 4.51e-33

lactoylglutathione lyase


Pssm-ID: 215169 [Multi-domain]  Cd Length: 286  Bit Score: 116.80  E-value: 4.51e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489785904   2 GNLEKSLDSYQNVLGMKLLRRKDYPEGRFTLAFVGYGDETDSTVLELTHNWDTERYDLGDAYGHIAVEVDDAYEACERVK 81
Cdd:PLN02300 163 GDLDRSIKFYEKAFGMKLLRKRDNPEYKYTIAMMGYGPEDKTTVLELTYNYGVTEYTKGNAYAQIAIGTDDVYKTAEAIK 242

                         90       100       110
                 ....*....|....*....|....*....|....
gi 489785904  82 RQGGNVVREAGLMKHGTTVIAFVEDPDGCKIEFV 115
Cdd:PLN02300 243 LVGGKITREPGPLPGINTKITACLDPDGWKTVFV 276
GloA COG0346
Catechol 2,3-dioxygenase or related enzyme, vicinal oxygen chelate (VOC) family [Secondary ...
 3-120 1.72e-32

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: 110.85  E-value: 1.72e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489785904   3 NLEKSLDSYQNVLGMKLLRRKDYPEGRFTLAFVGYGDETdstVLELTHNWDTERYDLGDAYGHIAVEVDDAYEACERVKR 82
Cdd:COG0346   12 DLEASLAFYTDVLGLELVKRTDFGDGGFGHAFLRLGDGT---ELELFEAPGAAPAPGGGGLHHLAFRVDDLDAAYARLRA 88

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 489785904  83 QGGNVVREAGLMKHGTTViAFVEDPDGCKIEFVQKKSG 120
Cdd:COG0346   89 AGVEIEGEPRDRAYGYRS-AYFRDPDGNLIELVEPPPG 125
PLN02367 PLN02367
lactoylglutathione lyase
 7-127 4.99e-30

lactoylglutathione lyase


Pssm-ID: 177995  Cd Length: 233  Bit Score: 107.78  E-value: 4.99e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489785904   7 SLDSYQNVLGMKLLRRKDYPEGRFTLAFVGY-------GDETDSTV--------LELTHNWDTER------YDLGDA--- 62
Cdd:PLN02367  89 SLDFYSRVLGMSLLKRLDFPEMKFSLYFMGYedtasapTDPTERTVwtfgqkatIELTHNWGTESdpdfkgYHNGNSepr 168

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489785904  63 -YGHIAVEVDDAYEACERVKRQGGNVVR--EAGLMKHgttvIAFVEDPDGCKIE-FVQKKSGDDSVAYA 127
Cdd:PLN02367 169 gFGHIGITVDDVYKACERFEELGVEFVKkpNDGKMKG----IAFIKDPDGYWIEiFDLKTIGTTTVNAA 233
PLN03042 PLN03042
Lactoylglutathione lyase; Provisional
 6-113 6.27e-30

Lactoylglutathione lyase; Provisional


Pssm-ID: 215548  Cd Length: 185  Bit Score: 106.06  E-value: 6.27e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489785904   6 KSLDSYQNVLGMKLLRRKDYPEGRFTLAFVGY-------GDETDSTV--------LELTHNWDTER------YDLGDA-- 62
Cdd:PLN03042  40 ASLDFYSRVLGMSLLKRLDFPEMKFSLYFLGYedsetapTDPPERTVwtfgrkatIELTHNWGTESdpefkgYHNGNSdp 119

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 489785904  63 --YGHIAVEVDDAYEACERVKRQGGNVVR--EAGLMKHgttvIAFVEDPDGCKIE 113
Cdd:PLN03042 120 rgFGHIGITVDDVYKACERFEKLGVEFVKkpDDGKMKG----LAFIKDPDGYWIE 170
Glyoxalase pfam00903
Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;
2-114 4.60e-21

Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;


Pssm-ID: 395724 [Multi-domain]  Cd Length: 121  Bit Score: 81.73  E-value: 4.60e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489785904    2 GNLEKSLDSYQNVLGMKLLRRKDYPEGRFTLAFVGYGDETdstVLELTHNWDTERYDLG---DAYGHIAVEVDDAYEACE 78
Cdd:pfam00903  10 GDLEKSLDFYTDVLGFKLVEETDAGEEGGLRSAFFLAGGR---VLELLLNETPPPAAAGfggHHIAFIAFSVDDVDAAYD 86

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 489785904   79 RVKRQGGNVVREAGLMKHGTTVIaFVEDPDGCKIEF 114
Cdd:pfam00903  87 RLKAAGVEIVREPGRHGWGGRYS-YFRDPDGNLIEL 121
VOC cd06587
vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate (VOC) superfamily is composed ...
 2-114 8.12e-15

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: 65.24  E-value: 8.12e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489785904   2 GNLEKSLDSYQNVLGMKLLRRKDYPEgrftLAFVGYGDETdstVLELTHnWDTERYDLGDAYGHIAVEVDDAYEACERVK 81
Cdd:cd06587    7 PDLDASVAFYEEVLGFEVVSRNEGGG----FAFLRLGPGL---RLALLE-GPEPERPGGGGLFHLAFEVDDVDEVDERLR 78

                         90       100       110
                 ....*....|....*....|....*....|....
gi 489785904  82 RQGGNVVREAGLM-KHGTTVIAFVEDPDGCKIEF 114
Cdd:cd06587   79 EAGAEGELVAPPVdDPWGGRSFYFRDPDGNLIEF 112
GLOD4_N cd08358
N-terminal domain of human glyoxalase domain-containing protein 4 and similar proteins; ...
 2-79 2.54e-13

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: 62.00  E-value: 2.54e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489785904   2 GNLEKSLDSYQNVLGMKLLRRKDYPEG-----------RFTLAFVGYGDETDSTVLELTHNWDTERYDLGDAYGHIAVEV 70
Cdd:cd08358   11 GDRNKTIKFYREILGMKVLRHEEFEEGckaacngpydgKWSKTMVGYGPEDDHFVVELTYNYGIGDYELGNDFLGITIHS 90


                 ....*....
gi 489785904  71 DDAYEACER 79
Cdd:cd08358   91 KQAVSRAKK 99
MMCE cd07249
Methylmalonyl-CoA epimerase (MMCE); MMCE, also called methylmalonyl-CoA racemase (EC 5.1.99.1) ...
 3-116 7.65e-11

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: 55.27  E-value: 7.65e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489785904   3 NLEKSLDSYQNVLGMKLLRRKDYPEGRFTLAFVGYGDetdsTVLELTH--NWDTERYDLGDAYG----HIAVEVDDAYEA 76
Cdd:cd07249   10 DLDEALKFYEDVLGVKVSEPEELEEQGVRVAFLELGN----TQIELLEplGEDSPIAKFLDKKGgglhHIAFEVDDIDAA 85

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 489785904  77 CERVKRQGGNVVREA-GLMKHGTTViAFVEDPDGCK--IEFVQ 116
Cdd:cd07249   86 VEELKAQGVRLLSEGpRIGAHGKRV-AFLHPKDTGGvlIELVE 127
VOC COG3324
Lactoylglutathione lyase-related enzyme, vicinal oxygen chelate (VOC) family [General function ...
 3-119 3.26e-09

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


Pssm-ID: 442553 [Multi-domain]  Cd Length: 119  Bit Score: 50.79  E-value: 3.26e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489785904   3 NLEKSLDSYQNVLGMKLLRRKDyPEGRFTLAFVGYGDetdstVLELTHNWDTErydlGDAYGHIAVEVDDAYEACERVKR 82
Cdd:COG3324   14 DLERAKAFYEEVFGWTFEDDAG-PGGDYAEFDTDGGQ-----VGGLMPGAEEP----GGPGWLLYFAVDDLDAAVARVEA 83

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 489785904  83 QGGNVVRE-AGLMKHGTtvIAFVEDPDGCKIEFVQKKS 119
Cdd:COG3324   84 AGGTVLRPpTDIPPWGR--FAVFRDPEGNRFGLWQPAA 119
PhnB COG2764
Zn-dependent glyoxalase, PhnB family [Energy production and conversion];
3-116 2.54e-08

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


Pssm-ID: 442048 [Multi-domain]  Cd Length: 118  Bit Score: 48.70  E-value: 2.54e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489785904   3 NLEKSLDSYQNVLGMKLLRRKDYPEGRFTLAFVGYGDetdsTVLELTHNWDTERYDLGDAYgHIAVEVDDAYEACERVKR 82
Cdd:COG2764   10 DAEEALEFYEDVFGFEVVFRMTDPDGKIMHAELRIGG----SVLMLSDAPPDSPAAEGNGV-SLSLYVDDVDALFARLVA 84

                         90       100       110
                 ....*....|....*....|....*....|....
gi 489785904  83 QGGNVVREAGLMKHGTTViAFVEDPDGCKIEFVQ 116
Cdd:COG2764   85 AGATVVMPLQDTFWGDRF-GMVRDPFGVLWMINT 117
CatE COG2514
Catechol-2,3-dioxygenase [Secondary metabolites biosynthesis, transport and catabolism];
3-125 5.68e-08

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


Pssm-ID: 442004 [Multi-domain]  Cd Length: 141  Bit Score: 48.03  E-value: 5.68e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489785904   3 NLEKSLDSYQNVLGMKLLRRKDypeGRFTLAFVGygdetDSTVLELTHNWDTERYDLGDAYGHIAVEVDDAYE---ACER 79
Cdd:COG2514   13 DLERSAAFYTDVLGLEVVEREG---GRVYLRADG-----GEHLLVLEEAPGAPPRPGAAGLDHVAFRVPSRADldaALAR 84

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 489785904  80 VKRQGgnvVREAGLMKHGTTVIAFVEDPDGCKIEFVQKKSGDDSVA 125
Cdd:COG2514   85 LAAAG---VPVEGAVDHGVGESLYFRDPDGNLIELYTDRPRFEHVG 127
GLOD4_C cd16357
C-terminal domain of human glyoxalase domain-containing protein 4 and similar proteins; ...
 3-114 2.64e-06

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: 43.31  E-value: 2.64e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489785904   3 NLEKSLDSYQNVLGMKLLRRkdyPEGRFTLafvGYGDetDSTVLELThnwDT-ERYDLGDAYGHIAVEVDDAYEAC--ER 79
Cdd:cd16357    8 DLEKSIDYWSDLLGMKVFEK---SEKSALL---GYGE--DQAKLELV---DIpEPVDHGTAFGRIAFSCPADELPPieEK 76

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 489785904  80 VKRQGGNVVREagLMKHGTTVIAFVE-----DPDGCKIEF 114
Cdd:cd16357   77 VKAAGQTILTP--LVSLDTPGKATVQvvilaDPDGHEICF 114
Glyoxalase_4 pfam13669
Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;
3-88 4.72e-06

Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;


Pssm-ID: 463951 [Multi-domain]  Cd Length: 109  Bit Score: 42.27  E-value: 4.72e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489785904    3 NLEKSLDSYQNVLGMKLLRRKDYPEGRFTLAFVGYGDEtdSTVLELTHNWDTERY--DLGDAYGHIAVEVDDAYEACERV 80
Cdd:pfam13669   9 DLDRALALWGALLGLGPEGDYRSEPQNVDLAFALLGDG--PVEVELIQPLDGDSPlaRHGPGLHHLAYWVDDLDAAVARL 86


                  ....*...
gi 489785904   81 KRQGGNVV 88
Cdd:pfam13669  87 LDQGYRVA 94
metmalonyl_epim TIGR03081
methylmalonyl-CoA epimerase; Members of this protein family are the enzyme methylmalonyl-CoA ...
 3-116 2.40e-05

methylmalonyl-CoA epimerase; Members of this protein family are the enzyme methylmalonyl-CoA epimerase (EC 5.1.99.1), also called methylmalonyl-CoA racemase. This enzyme converts (2R)-methylmalonyl-CoA to (2S)-methylmalonyl-CoA, which is then a substrate for methylmalonyl-CoA mutase (TIGR00642). It is known in bacteria, archaea, and as a mitochondrial protein in animals. It is closely related to lactoylglutathione lyase (TIGR00068), which is also called glyoxylase I, and is also a homodimer.


Pssm-ID: 213772 [Multi-domain]  Cd Length: 128  Bit Score: 40.77  E-value: 2.40e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489785904    3 NLEKSLDSYQNVLGMKLLRRKDYPEGRFTLAFVGYGDetdsTVLELTHNWDTE----RY--DLGDAYGHIAVEVDDAYEA 76
Cdd:TIGR03081  11 DLEEAAKFYEDVLGAQVSEIEELPEQGVKVVFIALGN----TKVELLEPLGEDspiaKFleKNGGGIHHIAIEVDDIEAA 86

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 489785904   77 CERVKRQGGNVVREAGLMKHGTTVIAFV--EDPDGCKIEFVQ 116
Cdd:TIGR03081  87 LETLKEKGVRLIDEEPRIGAHGKPVAFLhpKSTGGVLIELEQ 128
PRK04101 PRK04101
metallothiol transferase FosB;
3-114 5.94e-05

metallothiol transferase FosB;


Pssm-ID: 179740  Cd Length: 139  Bit Score: 39.93  E-value: 5.94e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489785904   3 NLEKSLDSYQNVLGMKLLRRkdypeGRFTLAFvgygdETDSTVLELTHNWDTERYDLGDAYGHIA--VEVDDAYEACERV 80
Cdd:PRK04101  14 NLEKSIEFYEKVLGAKLLVK-----GRKTAYF-----DLNGLWIALNEEKDIPRNEIHQSYTHIAfsIEEEDFDHWYQRL 83

                         90       100       110
                 ....*....|....*....|....*....|....
gi 489785904  81 KRQGGNVVREAGLMKHGTTVIAFVeDPDGCKIEF 114
Cdd:PRK04101  84 KENDVNILPGRERDERDKKSIYFT-DPDGHKFEF 116
VOC_like cd07245
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 3-114 7.59e-05

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


Pssm-ID: 319909 [Multi-domain]  Cd Length: 117  Bit Score: 39.22  E-value: 7.59e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489785904   3 NLEKSLDSYQNVLGMKLLRRKdyPEGRFTLAFVGYGDETDSTVLELTHNWDTERYDLGDAYGHIAVEVDDAYEACERVKR 82
Cdd:cd07245   10 DLERARRFYTDVLGLEEVPRP--PFLKFGGAWLYLGGGQQIHLVVEQNPSELPRPEHPGRDRHPSFSVPDLDALKQRLKE 87

                         90       100       110
                 ....*....|....*....|....*....|...
gi 489785904  83 QGGNVVREAGLmkhGTTVIA-FVEDPDGCKIEF 114
Cdd:cd07245   88 AGIPYTESTSP---GGGVTQlFFRDPDGNRLEF 117
FosA cd07244
fosfomycin resistant protein subfamily FosA; This subfamily family contains FosA, a fosfomycin ...
 3-113 1.10e-04

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: 38.80  E-value: 1.10e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489785904   3 NLEKSLDSYQNVLGMKLLRRkdYPEGrftlAFVGYGDetdstvLELTHNWDTERYDLGDaYGHIA--VEVDDAYEACERV 80
Cdd:cd07244   11 DLERSLAFYVDLLGFKPHVR--WDKG----AYLTAGD------LWLCLSLDPAAEPSPD-YTHIAftVSEEDFEELSERL 77

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 489785904  81 KRQGgnvvreAGLMKHGTTVIA--FVEDPDGCKIE 113
Cdd:cd07244   78 RAAG------VKIWQENSSEGDslYFLDPDGHKLE 106
FosB cd08363
fosfomycin resistant protein subfamily FosB; This subfamily family contains FosB, a fosfomycin ...
 3-114 5.63e-04

fosfomycin resistant protein subfamily FosB; This subfamily family contains FosB, a fosfomycin resistant protein. FosB is a Mg(2+)-dependent L-cysteine thiol transferase. Fosfomycin inhibits the enzyme UDP-nacetylglucosamine-3-enolpyruvyltransferase (MurA), which catalyzes the first committed step in bacterial cell wall biosynthesis. FosB catalyzes the Mg(II) dependent addition of L-cysteine to the epoxide ring of fosfomycin, (1R,2S)-epoxypropylphosphonic acid, rendering it inactive. FosB is evolutionarily related to glyoxalase I and type I extradiol dioxygenases.


Pssm-ID: 319951 [Multi-domain]  Cd Length: 131  Bit Score: 37.33  E-value: 5.63e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489785904   3 NLEKSLDSYQNVLGMKLLrrkdyPEGRFTLAFvgygdETDSTVLELTHNWDTERYDLGDAYGHIAVEVD----DAYEacE 78
Cdd:cd08363   10 NLNKSIAFYKDVLDAKLL-----VLGEKTAYF-----DLNGLWLALNVQEDIPRNEISHSYTHIAFSIDeedlDAFK--E 77

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 489785904  79 RVKRQGGNVVREAGLMKHGTTVIAFvEDPDGCKIEF 114
Cdd:cd08363   78 RLKDNGVNILEGRKRDILEGQSIYF-TDPDGHLFEL 112
VOC_BsCatE_like_N cd07255
N-terminal of Bacillus subtilis CatE like protein; Uncharacterized subfamily of VOC ...
 3-114 2.13e-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: 35.37  E-value: 2.13e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489785904   3 NLEKSLDSYQNVLGMKLLRRKDypeGRFTLAFVGYGDEtdstvLELTHNWDTERYDLGdAYG--HIAVEVDDAYE---AC 77
Cdd:cd07255   12 DLERQSAFYQNVIGLSVLKQNA---SRAYLGVDGKQVL-----LVLEAIPDAVLAPRS-TTGlyHFAILLPDRKAlgrAL 82

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 489785904  78 ERVKRQGgnvvREAGLMKHGTTVIAFVEDPDGCKIEF 114
Cdd:cd07255   83 AHLAEHG----PLIGAADHGVSEAIYLSDPEGNGIEI 115
HppD COG3185
4-hydroxyphenylpyruvate dioxygenase and related hemolysins [Amino acid transport and ...
 60-122 2.49e-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: 36.41  E-value: 2.49e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489785904  60 GDAYGHIAVEVDDAYEACERVKRQGGNVVREAGlmkHGTTVIAFVEDPDGCKIEFVQKKSGDD 122
Cdd:COG3185   65 GPGVCAIAFRVDDAAAAYERALALGAEPFEGPG---PGELRIPAIRGIGGSLHYFVDRYGYGG 124
 
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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