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Conserved domains on  [gi|2205678935|ref|WP_240801190|]
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lactoylglutathione lyase [Vogesella mureinivorans]

Protein Classification

lactoylglutathione lyase( domain architecture ID 10794439)

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

EC:  4.4.1.5
Gene Ontology:  GO:0004462|GO:0046872
PubMed:  14641060

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
glyox_I TIGR00068
lactoylglutathione lyase; Lactoylglutathione lyase is also known as aldoketomutase and ...
 2-128 1.27e-83

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: 241.25  E-value: 1.27e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205678935   2 RLLHTMIRVGQLDRSIAFYTDVLGMTLLRRHDYPEGRFTLAFVGYGDEDSNSVIELTHNWDTDSYELGNAFGHLAVEVAD 81
Cdd:TIGR00068  17 RLLHTMLRVGDLDKSLDFYTEVLGMKLLRKRDFPEMKFSLAFLGYGDETSAAVIELTHNWGTEKYDLGNGFGHIAIGVDD 96

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 2205678935  82 AYATCDAVRAKGGKVVREAGPMKHGTTVIAFVEDPDGYKIEFIQKGT 128
Cdd:TIGR00068  97 VYKACERVRALGGNVVREPGPVKGGTTVIAFVEDPDGYKIELIQRKS 143
 
Name Accession Description Interval E-value
glyox_I TIGR00068
lactoylglutathione lyase; Lactoylglutathione lyase is also known as aldoketomutase and ...
 2-128 1.27e-83

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: 241.25  E-value: 1.27e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205678935   2 RLLHTMIRVGQLDRSIAFYTDVLGMTLLRRHDYPEGRFTLAFVGYGDEDSNSVIELTHNWDTDSYELGNAFGHLAVEVAD 81
Cdd:TIGR00068  17 RLLHTMLRVGDLDKSLDFYTEVLGMKLLRKRDFPEMKFSLAFLGYGDETSAAVIELTHNWGTEKYDLGNGFGHIAIGVDD 96

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 2205678935  82 AYATCDAVRAKGGKVVREAGPMKHGTTVIAFVEDPDGYKIEFIQKGT 128
Cdd:TIGR00068  97 VYKACERVRALGGNVVREPGPVKGGTTVIAFVEDPDGYKIELIQRKS 143
GlxI_Ni cd16358
Glyoxalase I that uses Ni(++) as cofactor; This family includes Escherichia coil and other ...
 3-124 1.47e-78

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: 227.28  E-value: 1.47e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205678935   3 LLHTMIRVGQLDRSIAFYTDVLGMTLLRRHDYPEGRFTLAFVGYGDEDSNSVIELTHNWDTDSYELGNAFGHLAVEVADA 82
Cdd:cd16358     1 MLHTMLRVGDLDRSIKFYTEVLGMKLLRKRDYPEGKYTLAFVGYGDEDENTVLELTYNWGVDKYDLGTAYGHIAIGVEDV 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 2205678935  83 YATCDAVRAKGGKVVREAGPMKHGTTVIAFVEDPDGYKIEFI 124
Cdd:cd16358    81 YETCERIRKKGGKVTREPGPMKGGTTVIAFVEDPDGYKIELI 122
PLN02300 PLN02300
lactoylglutathione lyase
 2-127 5.48e-59

lactoylglutathione lyase


Pssm-ID: 215169 [Multi-domain]  Cd Length: 286  Bit Score: 183.44  E-value: 5.48e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205678935   2 RLLHTMIRVGQLDRSIAFYTDVLGMTLLRRHDYPEGRFTLAFVGYGDEDSNSVIELTHNWDTDSYELGNAFGHLAVEVAD 81
Cdd:PLN02300   24 RMLHVVYRVGDLDRTIKFYTECLGMKLLRKRDIPEEKYTNAFLGYGPEDSNFVVELTYNYGVDKYDIGTGFGHFGIAVED 103

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 2205678935  82 AYATCDAVRAKGGKVVREAGPMKHGTTVIAFVEDPDGYKIEFIQKG 127
Cdd:PLN02300  104 VAKTVELVKAKGGKVTREPGPVKGGKSVIAFVKDPDGYKFELIQRG 149
GloA COG0346
Catechol 2,3-dioxygenase or related enzyme, vicinal oxygen chelate (VOC) family [Secondary ...
 1-127 4.57e-41

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: 132.42  E-value: 4.57e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205678935   1 MRLLHTMIRVGQLDRSIAFYTDVLGMTLLRRHDYPEGRFTLAFVGYGDedsNSVIELTHNWDTDSYELGNAFGHLAVEVA 80
Cdd:COG0346     1 MGLHHVTLRVSDLEASLAFYTDVLGLELVKRTDFGDGGFGHAFLRLGD---GTELELFEAPGAAPAPGGGGLHHLAFRVD 77

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 2205678935  81 DAYATCDAVRAKGGKVVREAGPMKHGTTViAFVEDPDGYKIEFIQKG 127
Cdd:COG0346    78 DLDAAYARLRAAGVEIEGEPRDRAYGYRS-AYFRDPDGNLIELVEPP 123
Glyoxalase pfam00903
Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;
2-123 8.15e-29

Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;


Pssm-ID: 395724 [Multi-domain]  Cd Length: 121  Bit Score: 101.37  E-value: 8.15e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205678935   2 RLLHTMIRVGQLDRSIAFYTDVLGMTLLRRHDYPEGRFTLAFVGYGDEDsnsVIELTHNWDTDSYELGNA---FGHLAVE 78
Cdd:pfam00903   1 RIDHVALRVGDLEKSLDFYTDVLGFKLVEETDAGEEGGLRSAFFLAGGR---VLELLLNETPPPAAAGFGghhIAFIAFS 77

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 2205678935  79 VADAYATCDAVRAKGGKVVREAGPMKHGTTVIaFVEDPDGYKIEF 123
Cdd:pfam00903  78 VDDVDAAYDRLKAAGVEIVREPGRHGWGGRYS-YFRDPDGNLIEL 121
 
Name Accession Description Interval E-value
glyox_I TIGR00068
lactoylglutathione lyase; Lactoylglutathione lyase is also known as aldoketomutase and ...
 2-128 1.27e-83

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: 241.25  E-value: 1.27e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205678935   2 RLLHTMIRVGQLDRSIAFYTDVLGMTLLRRHDYPEGRFTLAFVGYGDEDSNSVIELTHNWDTDSYELGNAFGHLAVEVAD 81
Cdd:TIGR00068  17 RLLHTMLRVGDLDKSLDFYTEVLGMKLLRKRDFPEMKFSLAFLGYGDETSAAVIELTHNWGTEKYDLGNGFGHIAIGVDD 96

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 2205678935  82 AYATCDAVRAKGGKVVREAGPMKHGTTVIAFVEDPDGYKIEFIQKGT 128
Cdd:TIGR00068  97 VYKACERVRALGGNVVREPGPVKGGTTVIAFVEDPDGYKIELIQRKS 143
GlxI_Ni cd16358
Glyoxalase I that uses Ni(++) as cofactor; This family includes Escherichia coil and other ...
 3-124 1.47e-78

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: 227.28  E-value: 1.47e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205678935   3 LLHTMIRVGQLDRSIAFYTDVLGMTLLRRHDYPEGRFTLAFVGYGDEDSNSVIELTHNWDTDSYELGNAFGHLAVEVADA 82
Cdd:cd16358     1 MLHTMLRVGDLDRSIKFYTEVLGMKLLRKRDYPEGKYTLAFVGYGDEDENTVLELTYNWGVDKYDLGTAYGHIAIGVEDV 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 2205678935  83 YATCDAVRAKGGKVVREAGPMKHGTTVIAFVEDPDGYKIEFI 124
Cdd:cd16358    81 YETCERIRKKGGKVTREPGPMKGGTTVIAFVEDPDGYKIELI 122
PLN02300 PLN02300
lactoylglutathione lyase
 2-127 5.48e-59

lactoylglutathione lyase


Pssm-ID: 215169 [Multi-domain]  Cd Length: 286  Bit Score: 183.44  E-value: 5.48e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205678935   2 RLLHTMIRVGQLDRSIAFYTDVLGMTLLRRHDYPEGRFTLAFVGYGDEDSNSVIELTHNWDTDSYELGNAFGHLAVEVAD 81
Cdd:PLN02300   24 RMLHVVYRVGDLDRTIKFYTECLGMKLLRKRDIPEEKYTNAFLGYGPEDSNFVVELTYNYGVDKYDIGTGFGHFGIAVED 103

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 2205678935  82 AYATCDAVRAKGGKVVREAGPMKHGTTVIAFVEDPDGYKIEFIQKG 127
Cdd:PLN02300  104 VAKTVELVKAKGGKVTREPGPVKGGKSVIAFVKDPDGYKFELIQRG 149
PRK10291 PRK10291
glyoxalase I; Provisional
 7-125 6.87e-52

glyoxalase I; Provisional


Pssm-ID: 182358  Cd Length: 129  Bit Score: 160.19  E-value: 6.87e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205678935   7 MIRVGQLDRSIAFYTDVLGMTLLRRHDYPEGRFTLAFVGYGDEDSNSVIELTHNWDTDSYELGNAFGHLAVEVADAYATC 86
Cdd:PRK10291    1 MLRVGDLQRSIDFYTNVLGMKLLRTSENPEYKYSLAFVGYGPETEEAVIELTYNWGVDKYELGTAYGHIALSVDNAAEAC 80

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 2205678935  87 DAVRAKGGKVVREAGPMKHGTTVIAFVEDPDGYKIEFIQ 125
Cdd:PRK10291   81 EKIRQNGGNVTREAGPVKGGTTVIAFVEDPDGYKIELIE 119
GloA COG0346
Catechol 2,3-dioxygenase or related enzyme, vicinal oxygen chelate (VOC) family [Secondary ...
 1-127 4.57e-41

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: 132.42  E-value: 4.57e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205678935   1 MRLLHTMIRVGQLDRSIAFYTDVLGMTLLRRHDYPEGRFTLAFVGYGDedsNSVIELTHNWDTDSYELGNAFGHLAVEVA 80
Cdd:COG0346     1 MGLHHVTLRVSDLEASLAFYTDVLGLELVKRTDFGDGGFGHAFLRLGD---GTELELFEAPGAAPAPGGGGLHHLAFRVD 77

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 2205678935  81 DAYATCDAVRAKGGKVVREAGPMKHGTTViAFVEDPDGYKIEFIQKG 127
Cdd:COG0346    78 DLDAAYARLRAAGVEIEGEPRDRAYGYRS-AYFRDPDGNLIELVEPP 123
GlxI_Zn cd07233
Glyoxalase I that uses Zn(++) as cofactor; This family includes eukaryotic glyoxalase I that ...
 3-124 9.21e-41

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: 132.45  E-value: 9.21e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205678935   3 LLHTMIRVGQLDRSIAFYTDVLGMTLLRRHDYPEGRFTLAFVGYGDEDS-------------NSVIELTHNWDTDS---- 65
Cdd:cd07233     1 FNHTMLRVKDPKKSLKFYTEVLGMKLLRKKDFPEMKFSLYFLGYEDPKDipkdprtawvfsrEGTLELTHNWGTENdedp 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2205678935  66 -YELGNA----FGHLAVEVADAYATCDAVRAKGGKVVR--EAGPMKHgttvIAFVEDPDGYKIEFI 124
Cdd:cd07233    81 vYHNGNSdprgFGHIGIAVDDVYAACERFEELGVKFKKkpDDGKMKG----IAFIKDPDGYWIEIL 142
PLN02300 PLN02300
lactoylglutathione lyase
 2-124 7.70e-40

lactoylglutathione lyase


Pssm-ID: 215169 [Multi-domain]  Cd Length: 286  Bit Score: 134.52  E-value: 7.70e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205678935   2 RLLHTMIRVGQLDRSIAFYTDVLGMTLLRRHDYPEGRFTLAFVGYGDEDSNSVIELTHNWDTDSYELGNAFGHLAVEVAD 81
Cdd:PLN02300  154 PLCQVMLRVGDLDRSIKFYEKAFGMKLLRKRDNPEYKYTIAMMGYGPEDKTTVLELTYNYGVTEYTKGNAYAQIAIGTDD 233

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 2205678935  82 AYATCDAVRAKGGKVVREAGPMKHGTTVIAFVEDPDGYKIEFI 124
Cdd:PLN02300  234 VYKTAEAIKLVGGKITREPGPLPGINTKITACLDPDGWKTVFV 276
PLN03042 PLN03042
Lactoylglutathione lyase; Provisional
 6-128 4.63e-30

Lactoylglutathione lyase; Provisional


Pssm-ID: 215548  Cd Length: 185  Bit Score: 106.44  E-value: 4.63e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205678935   6 TMIRVGQLDRSIAFYTDVLGMTLLRRHDYPEGRFTLAFVGYgdEDSNSV-----------------IELTHNWDTDS--- 65
Cdd:PLN03042   31 TMFRIKDPKASLDFYSRVLGMSLLKRLDFPEMKFSLYFLGY--EDSETAptdppertvwtfgrkatIELTHNWGTESdpe 108

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2205678935  66 ---YELGNA----FGHLAVEVADAYATCDAVRAKGGKVVR--EAGPMKHgttvIAFVEDPDGYKIEFIQKGT 128
Cdd:PLN03042  109 fkgYHNGNSdprgFGHIGITVDDVYKACERFEKLGVEFVKkpDDGKMKG----LAFIKDPDGYWIEIFDLKR 176
PLN02367 PLN02367
lactoylglutathione lyase
 5-122 5.77e-29

lactoylglutathione lyase


Pssm-ID: 177995  Cd Length: 233  Bit Score: 105.08  E-value: 5.77e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205678935   5 HTMIRVGQLDRSIAFYTDVLGMTLLRRHDYPEGRFTLAFVGYGDEDS---------------NSVIELTHNWDTDS---- 65
Cdd:PLN02367   78 QTMYRIKDPKASLDFYSRVLGMSLLKRLDFPEMKFSLYFMGYEDTASaptdptertvwtfgqKATIELTHNWGTESdpdf 157

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2205678935  66 --YELGNA----FGHLAVEVADAYATCDAVRAKGGKVVR--EAGPMKHgttvIAFVEDPDGYKIE 122
Cdd:PLN02367  158 kgYHNGNSeprgFGHIGITVDDVYKACERFEELGVEFVKkpNDGKMKG----IAFIKDPDGYWIE 218
Glyoxalase pfam00903
Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;
2-123 8.15e-29

Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;


Pssm-ID: 395724 [Multi-domain]  Cd Length: 121  Bit Score: 101.37  E-value: 8.15e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205678935   2 RLLHTMIRVGQLDRSIAFYTDVLGMTLLRRHDYPEGRFTLAFVGYGDEDsnsVIELTHNWDTDSYELGNA---FGHLAVE 78
Cdd:pfam00903   1 RIDHVALRVGDLEKSLDFYTDVLGFKLVEETDAGEEGGLRSAFFLAGGR---VLELLLNETPPPAAAGFGghhIAFIAFS 77

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 2205678935  79 VADAYATCDAVRAKGGKVVREAGPMKHGTTVIaFVEDPDGYKIEF 123
Cdd:pfam00903  78 VDDVDAAYDRLKAAGVEIVREPGRHGWGGRYS-YFRDPDGNLIEL 121
GLOD4_N cd08358
N-terminal domain of human glyoxalase domain-containing protein 4 and similar proteins; ...
 2-126 2.09e-22

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: 85.11  E-value: 2.09e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205678935   2 RLLHTMIRVGQLDRSIAFYTDVLGMTLLRRHDYPEG-----------RFTLAFVGYGDEDSNSVIELTHNWDTDSYELGN 70
Cdd:cd08358     2 RALHFVFKVGDRNKTIKFYREILGMKVLRHEEFEEGckaacngpydgKWSKTMVGYGPEDDHFVVELTYNYGIGDYELGN 81

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2205678935  71 AFGHLAVEVADAYAtcdavRAKggkvvREAGPMKHGTTVIAFVEDPDGYKIEFIQK 126
Cdd:cd08358    82 DFLGITIHSKQAVS-----RAK-----KHNWPVTQVGDGVYEVKAPGGYKFYLIDK 127
VOC cd06587
vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate (VOC) superfamily is composed ...
 5-123 5.45e-18

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: 73.33  E-value: 5.45e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205678935   5 HTMIRVGQLDRSIAFYTDVLGMTLLRRHDYPEgrftLAFVGYGDedsNSVIELTHnWDTDSYELGNAFGHLAVEVADAYA 84
Cdd:cd06587     1 HVALRVPDLDASVAFYEEVLGFEVVSRNEGGG----FAFLRLGP---GLRLALLE-GPEPERPGGGGLFHLAFEVDDVDE 72

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 2205678935  85 TCDAVRAKGGKVVREAGPM-KHGTTVIAFVEDPDGYKIEF 123
Cdd:cd06587    73 VDERLREAGAEGELVAPPVdDPWGGRSFYFRDPDGNLIEF 112
VOC COG3324
Lactoylglutathione lyase-related enzyme, vicinal oxygen chelate (VOC) family [General function ...
 1-125 1.35e-15

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


Pssm-ID: 442553 [Multi-domain]  Cd Length: 119  Bit Score: 67.35  E-value: 1.35e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205678935   1 MRLLHTMIRVGQLDRSIAFYTDVLGMTLLRRHDyPEGRFTLAFVGYGDedsnsVIELTHNWDTDsyelGNAFGHLAVEVA 80
Cdd:COG3324     3 GTIVWVELPVDDLERAKAFYEEVFGWTFEDDAG-PGGDYAEFDTDGGQ-----VGGLMPGAEEP----GGPGWLLYFAVD 72

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 2205678935  81 DAYATCDAVRAKGGKVVREagPMKHGTT-VIAFVEDPDGYKIEFIQ 125
Cdd:COG3324    73 DLDAAVARVEAAGGTVLRP--PTDIPPWgRFAVFRDPEGNRFGLWQ 116
PhnB COG2764
Zn-dependent glyoxalase, PhnB family [Energy production and conversion];
4-125 9.21e-15

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


Pssm-ID: 442048 [Multi-domain]  Cd Length: 118  Bit Score: 65.26  E-value: 9.21e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205678935   4 LHTMIRVGQLDRSIAFYTDVLGMTLLRRHDYPEGRFTLAFVGYGDedsnSVIELTHNWDTDSYELGNAFgHLAVEVADAY 83
Cdd:COG2764     2 VTPYLVVDDAEEALEFYEDVFGFEVVFRMTDPDGKIMHAELRIGG----SVLMLSDAPPDSPAAEGNGV-SLSLYVDDVD 76

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 2205678935  84 ATCDAVRAKGGKVVREAGPMKHGTTViAFVEDPDGYKIEFIQ 125
Cdd:COG2764    77 ALFARLVAAGATVVMPLQDTFWGDRF-GMVRDPFGVLWMINT 117
CatE COG2514
Catechol-2,3-dioxygenase [Secondary metabolites biosynthesis, transport and catabolism];
1-124 1.98e-13

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


Pssm-ID: 442004 [Multi-domain]  Cd Length: 141  Bit Score: 62.28  E-value: 1.98e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205678935   1 MRLLHTMIRVGQLDRSIAFYTDVLGMTLLRRHDypeGRFTLAFVGygdedSNSVIELTHNWDTDSYELGNAFGHLAVEV- 79
Cdd:COG2514     2 TRLGHVTLRVRDLERSAAFYTDVLGLEVVEREG---GRVYLRADG-----GEHLLVLEEAPGAPPRPGAAGLDHVAFRVp 73

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 2205678935  80 --ADAYATCDAVRAKGgkvVREAGPMKHGTTVIAFVEDPDGYKIEFI 124
Cdd:COG2514    74 srADLDAALARLAAAG---VPVEGAVDHGVGESLYFRDPDGNLIELY 117
VOC_like cd07264
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 3-123 3.86e-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: 58.50  E-value: 3.86e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205678935   3 LLHTMIRVGQLDRSIAFYTDVLGmtLLRRHDYPEGRFTLAFVGygdedsNSVIEL----THNWDTDSyELGNAFGHLAVE 78
Cdd:cd07264     1 IAYIVLYVDDFAASLRFYRDVLG--LPPRFLHEEGEYAEFDTG------ETKLALfsrkEMARSGGP-DRRGSAFELGFE 71

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 2205678935  79 VADAYATCDAVRAKGGKVVREAGPMKHGTTViAFVEDPDGYKIEF 123
Cdd:cd07264    72 VDDVEATVEELVERGAEFVREPANKPWGQTV-AYVRDPDGNLIEI 115
Glyoxalase_4 pfam13669
Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;
13-97 7.52e-10

Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;


Pssm-ID: 463951 [Multi-domain]  Cd Length: 109  Bit Score: 52.28  E-value: 7.52e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205678935  13 LDRSIAFYTDVLGMTLLRRHDYPEGRFTLAFVGYGdeDSNSVIELTHNWDTDSY--ELGNAFGHLAVEVADAYATCDAVR 90
Cdd:pfam13669  10 LDRALALWGALLGLGPEGDYRSEPQNVDLAFALLG--DGPVEVELIQPLDGDSPlaRHGPGLHHLAYWVDDLDAAVARLL 87


                  ....*..
gi 2205678935  91 AKGGKVV 97
Cdd:pfam13669  88 DQGYRVA 94
VOC_like cd07262
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 3-124 9.83e-09

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: 319923 [Multi-domain]  Cd Length: 121  Bit Score: 49.92  E-value: 9.83e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205678935   3 LLHTMIRVGQLDRSIAFYTDVLGmTLlrrhDYPEGRFTLAFVGYGDEDSNSVIeLTHNWDTDSYELGNAFgHLAVeVADA 82
Cdd:cd07262     1 ISHVTIGVNDLERSRAFYDAALA-PL----GYKRGFEDGGRVGYGLEGGPDFW-VTEPFDGEPATAGNGT-HVAF-AAPS 72

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 2205678935  83 YATCDAVRAK----GGKVVREAG--PMKHGTTVIAFVEDPDGYKIEFI 124
Cdd:cd07262    73 RAAVDAFHAAalaaGGTDNGAPGlrPHYHPGYYAAYVRDPDGNKIEAV 120
MMCE cd07249
Methylmalonyl-CoA epimerase (MMCE); MMCE, also called methylmalonyl-CoA racemase (EC 5.1.99.1) ...
 5-125 3.00e-08

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: 48.73  E-value: 3.00e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205678935   5 HTMIRVGQLDRSIAFYTDVLGMTLLRRHDYPEGRFTLAFVGYGdedsNSVIELTHNWDTDS------YELGNAFGHLAVE 78
Cdd:cd07249     3 HIGIAVPDLDEALKFYEDVLGVKVSEPEELEEQGVRVAFLELG----NTQIELLEPLGEDSpiakflDKKGGGLHHIAFE 78

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 2205678935  79 VADAYATCDAVRAKGGKVVREA-GPMKHGTTViAFVEDPDGYK--IEFIQ 125
Cdd:cd07249    79 VDDIDAAVEELKAQGVRLLSEGpRIGAHGKRV-AFLHPKDTGGvlIELVE 127
GLOD4_C cd16357
C-terminal domain of human glyoxalase domain-containing protein 4 and similar proteins; ...
 7-123 2.35e-07

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: 46.01  E-value: 2.35e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205678935   7 MIRVGQLDRSIAFYTDVLGMTLLRRhdyPEGRFTLafvGYGDEDSNsvIELThnwDT-DSYELGNAFGHLAVEVADAYAT 85
Cdd:cd16357     3 SLAVSDLEKSIDYWSDLLGMKVFEK---SEKSALL---GYGEDQAK--LELV---DIpEPVDHGTAFGRIAFSCPADELP 71

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 2205678935  86 C--DAVRAKGGKVVREA----GPMKHGTTVIaFVEDPDGYKIEF 123
Cdd:cd16357    72 PieEKVKAAGQTILTPLvsldTPGKATVQVV-ILADPDGHEICF 114
SgaA_N_like cd07247
N-terminal domain of Streptomyces griseus SgaA and similar domains; SgaA suppresses the growth ...
 13-121 2.71e-07

N-terminal domain of Streptomyces griseus SgaA and similar domains; SgaA suppresses the growth disturbances caused by high osmolarity and a high concentration of A-factor, a microbial hormone, during the early growth phase in Streptomyces griseus. A-factor (2-isocapryloyl-3R-hydroxymethyl-gamma-butyrolactone) controls morphological differentiation and secondary metabolism in Streptomyces griseus. It is a chemical signaling molecule that at a very low concentration acts as a switch for yellow pigment production, aerial mycelium formation, streptomycin production, and streptomycin resistance. The structure and amino acid sequence of SgaA are closely related to a group of antibiotics resistance proteins, including bleomycin resistance protein, mitomycin resistance protein, and fosfomycin resistance proteins. SgaA might also function as a streptomycin resistance protein.


Pssm-ID: 319911 [Multi-domain]  Cd Length: 114  Bit Score: 45.72  E-value: 2.71e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205678935  13 LDRSIAFYTDVLGMTLlrrHDYPEGRFTLAFVGYGDEDSNSVIELThnwdtdsYELGNAFGHLAV--EVADAYATCDAVR 90
Cdd:cd07247    11 LERAKAFYGAVFGWTF---EDEGDGGGDYALFTAGGGAVGGLMRAP-------EEVAGAPPGWLIyfAVDDLDAALARVE 80

                          90       100       110
                  ....*....|....*....|....*....|..
gi 2205678935  91 AKGGKVVReaGPMK-HGTTVIAFVEDPDGYKI 121
Cdd:cd07247    81 AAGGKVVV--PPTDiPGGGRFAVFADPEGNRF 110
VOC_like cd07263
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 5-118 5.49e-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: 319924 [Multi-domain]  Cd Length: 120  Bit Score: 44.98  E-value: 5.49e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205678935   5 HTMIRVGQLDRSIAFYTDVLGMTLLRRHDYPEGRF-TLAfvgygDEDSNSVIELTHN--WDTDSYELGNAFGHLA---VE 78
Cdd:cd07263     1 QVMLYVDDQDKALDFYVEKLGFEVVEDVPMGGMRWvTVA-----PPGSPGTSLLLEPkaHPAQMPQSPEAAGGTPgilLA 75

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 2205678935  79 VADAYATCDAVRAKGGKVVREagPMKHGTTVIAFVEDPDG 118
Cdd:cd07263    76 TDDIDATYERLTAAGVTFVQE--PTQMGGGRVANFRDPDG 113
FosA cd07244
fosfomycin resistant protein subfamily FosA; This subfamily family contains FosA, a fosfomycin ...
 5-122 2.97e-06

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: 43.04  E-value: 2.97e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205678935   5 HTMIRVGQLDRSIAFYTDVLGMTLLRRhdYPEGrftlAFVGYG--------DEDSNSVIELTHnwdtdsyelgNAFGhla 76
Cdd:cd07244     4 HITLAVSDLERSLAFYVDLLGFKPHVR--WDKG----AYLTAGdlwlclslDPAAEPSPDYTH----------IAFT--- 64

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 2205678935  77 VEVADAYATCDAVRAKGGKVVREAgpMKHGTTViaFVEDPDGYKIE 122
Cdd:cd07244    65 VSEEDFEELSERLRAAGVKIWQEN--SSEGDSL--YFLDPDGHKLE 106
VOC_like cd07245
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 3-123 4.38e-06

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


Pssm-ID: 319909 [Multi-domain]  Cd Length: 117  Bit Score: 42.69  E-value: 4.38e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205678935   3 LLHTMIRVGQLDRSIAFYTDVLGMTLLRRHdyPEGRFTLAFVGYGDEDSNSVIELTHNWDTDSYELGNAFGHLAVEVADA 82
Cdd:cd07245     1 LDHVALACPDLERARRFYTDVLGLEEVPRP--PFLKFGGAWLYLGGGQQIHLVVEQNPSELPRPEHPGRDRHPSFSVPDL 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 2205678935  83 YATCDAVRAKGGKVVREAGPmkhGTTVIA-FVEDPDGYKIEF 123
Cdd:cd07245    79 DALKQRLKEAGIPYTESTSP---GGGVTQlFFRDPDGNRLEF 117
GLOD5 cd07253
Human glyoxalase domain-containing protein 5 and similar proteins; Uncharacterized subfamily ...
 2-122 1.98e-05

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: 41.06  E-value: 1.98e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205678935   2 RLLHTMIRVGQLDRSIAFYTDVLGMTLLRrhdYPEGRFTLAFvgygdedSNSVIELthnWDTDsYELGNAFGHLAVEVAD 81
Cdd:cd07253     3 RLDHLVLTVKDIERTIDFYTKVLGMTVVT---FKEGRKALRF-------GNQKINL---HQKG-KEFEPKASAPTPGSAD 68

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2205678935  82 ayaTC-------DAVRA--KGGKVVREAGPMK----HGTTVIAFVEDPDGYKIE 122
Cdd:cd07253    69 ---LCfitetpiDEVLEhlEACGVTIEEGPVKrtgaLGPILSIYFRDPDGNLIE 119
COG3607 COG3607
Lactoylglutathione lyase-related enzyme, vicinal oxygen chelate (VOC) family [General function ...
 13-125 2.47e-05

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


Pssm-ID: 442825  Cd Length: 126  Bit Score: 40.97  E-value: 2.47e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205678935  13 LDRSIAFYTDvLGMTLLRRHDYPEgrftLAFVGYGDedsNSVIELthnWDTDSY------ELGNAFGHLAVEVA------ 80
Cdd:COG3607    14 LERSRAFYEA-LGFTFNPQFSDEG----AACFVLGE---GIVLML---LPREKFatftgkPIADATGFTEVLLAlnvesr 82

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 2205678935  81 -DAYATCDAVRAKGGKVVREagPMKHGTTVIAFVEDPDGYKIEFIQ 125
Cdd:COG3607    83 eEVDALVAKALAAGGTVLKP--PQDVGGMYSGYFADPDGHLWEVAW 126
VOC_Bs_YwkD_like cd08352
vicinal oxygen chelate (VOC) family protein Bacillus subtilis YwkD and similar proteins; ...
 5-123 1.33e-04

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


Pssm-ID: 319940 [Multi-domain]  Cd Length: 123  Bit Score: 38.68  E-value: 1.33e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205678935   5 HTMIRVGQLDRSIAFYTDVLGMTLLRRHDYPEG---RFTLAFVGYgdedsnsVIELTHNWDT---DSYELGNAFGHLAVE 78
Cdd:cd08352     5 HIAIICSDYEKSKDFYVDKLGFEIIREHYRPERndiKLDLALGGY-------QLELFIKPDAparPSYPEALGLRHLAFK 77

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2205678935  79 VADAYATCDAVRAKGGKV--VRE----AGPMkhgttviAFVEDPDGYKIEF 123
Cdd:cd08352    78 VEDVEATVAELKSLGIETepIRVddftGKKF-------TFFFDPDGLPLEL 121
ED_TypeI_classII_N cd16360
N-terminal domain of type I, class II extradiol dioxygenases; This family contains the ...
 5-124 3.22e-04

N-terminal domain of type I, class II extradiol dioxygenases; This family contains the N-terminal non-catalytic domain of type I, class II extradiol dioxygenases. Dioxygenases catalyze the incorporation of both atoms of molecular oxygen into substrates using a variety of reaction mechanisms, resulting in the cleavage of aromatic rings. Two major groups of dioxygenases have been identified according to the cleavage site; extradiol enzymes cleave the aromatic ring between a hydroxylated carbon and an adjacent non-hydroxylated carbon, whereas intradiol enzymes cleave the aromatic ring between two hydroxyl groups. Extradiol dioxygenases are classified into type I and type II enzymes. Type I extradiol dioxygenases include class I and class II enzymes. These two classes of enzymes show sequence similarity; the two-domain class II enzymes evolved from a class I enzyme through gene duplication. The extradiol dioxygenases represented in this family are type I, class II enzymes, and are composed of the N- and C-terminal domains of similar structure fold, resulting from an ancient gene duplication. The active site is located in a funnel-shaped space of the C-terminal domain. A catalytically essential metal, Fe(II) or Mn(II), presents in all the enzymes in this family.


Pssm-ID: 319967  Cd Length: 111  Bit Score: 37.68  E-value: 3.22e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205678935   5 HTMIRVGQLDRSIAFYTDVLGMTLLRRhdypEGRfTLAFVGYGDEDSNSVIeltHNWDtdsyelGNAFGHLAVEVADAya 84
Cdd:cd16360     1 YAELGVPDLEKALEFYTDVLGLQVAKR----DGN-SVYLRGYEDEHHSLVL---YEAP------EAGLKHFAFEVASE-- 64

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 2205678935  85 tcDAVR-------AKGGKVVREAGPMKHGTTVIAFVEDPDGYKIEFI 124
Cdd:cd16360    65 --EDLEraaasltALGCDVTWGPDGEVPGGGKGFRFQDPSGHLLELF 109
VOC_BsCatE_like_N cd07255
N-terminal of Bacillus subtilis CatE like protein; Uncharacterized subfamily of VOC ...
 1-123 7.04e-04

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: 7.04e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205678935   1 MRLLHTMIRVGQLDRSIAFYTDVLGMTLLRRHDypeGRFTLAFVGYGDEdsnsvIELTHNWDtDSYELGNAFG--HLAVE 78
Cdd:cd07255     1 TRIGRVTLKVADLERQSAFYQNVIGLSVLKQNA---SRAYLGVDGKQVL-----LVLEAIPD-AVLAPRSTTGlyHFAIL 71

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 2205678935  79 VADAYATCDAVR--AKGGKVVreaGPMKHGTTVIAFVEDPDGYKIEF 123
Cdd:cd07255    72 LPDRKALGRALAhlAEHGPLI---GAADHGVSEAIYLSDPEGNGIEI 115
BphC2-C3-RGP6_C_like cd08348
The single-domain 2,3-dihydroxybiphenyl 1,2-dioxygenases; This subfamily contains Rhodococcus ...
 2-122 8.81e-04

The single-domain 2,3-dihydroxybiphenyl 1,2-dioxygenases; This subfamily contains Rhodococcus globerulus P6 BphC2-RGP6 and BphC3-RGP6, and similar proteins. BphC catalyzes the extradiol ring cleavage reaction of 2,3-dihydroxybiphenyl, yielding 2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoic acid. This is the third step in the polychlorinated biphenyls (PCBs) degradation pathway (bph pathway). This subfamily of BphCs belongs to the type I extradiol dioxygenase family, which require a metal in the active site in its catalytic mechanism. Most type I extradiol dioxygenases are activated by Fe(II). Polychlorinated biphenyl degrading bacteria demonstrate a multiplicity of BphCs. For example, three types of BphC enzymes have been found in Rhodococcus globerulus (BphC1-RGP6 - BphC3-RGP6), all three enzymes are type I extradiol dioxygenases. BphC2-RGP6 and BphC3-RGP6 are one-domain dioxygenases, which form hexamers. BphC1-RGP6 has an internal duplication, it is a two-domain dioxygenase which forms octamers, its two domains do not belong to this subfamily.


Pssm-ID: 319936  Cd Length: 137  Bit Score: 36.73  E-value: 8.81e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205678935   2 RLLHTMIRVGQ--LDRSIAFYTDVLGMTLLRRHDYpegrftLAFVGYGDEDSNSVI--ELTHNWDTDSYELGNAFGHLAV 77
Cdd:cd08348     1 KLAHFVLRTNPekFEAMVQWYLDILGARIVARNAK------GCFLSFDEEHHRIAIfgAPGGAQPPDKRPTRVGLAHIAF 74

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2205678935  78 ------EVADAYAtcdAVRAKGgkvVREAGPMKHGTTVIAFVEDPDGYKIE 122
Cdd:cd08348    75 tyasldDLARNYA---QLKERG---IKPVWPVNHGVTTSIYYRDPDGNMLE 119
VOC_like cd07251
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 10-123 1.38e-03

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: 319914 [Multi-domain]  Cd Length: 120  Bit Score: 36.12  E-value: 1.38e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205678935  10 VGQLDRSIAFYTDvLGMTLLRRHD-----YPEGRFTLAF---------VGYGDEDSN-SVIELTHNWDTdsyelgnafgh 74
Cdd:cd07251     6 VRDLERSARFYEA-LGWKPNLDPNdgvvfFQLGGTVLALyprdalaedAGVSVTGAGfSGVTLAHNVRS----------- 73

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 2205678935  75 lAVEVADAYATcdaVRAKGGKVVREAGPMKHGtTVIAFVEDPDGYKIEF 123
Cdd:cd07251    74 -REEVDQLLAK---AVAAGGKILKPPQEVFWG-GYSGYFADPDGHIWEV 117
VOC_like cd07238
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 8-118 3.25e-03

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: 319903  Cd Length: 112  Bit Score: 34.76  E-value: 3.25e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205678935   8 IRVGQLDRSIAFYTDVLGMTLLRRHDYpegrfTLAFVGYGDEDSNsvIELTHNWDTdsyelGNAFGHLAVEVADAYATCD 87
Cdd:cd07238     6 IATADPERAAAFYGDHLGLPLVMDHGW-----IVTFASPGNAHAQ--ISLAREGGS-----GTVVPDLSIEVDDVDAVHA 73

                          90       100       110
                  ....*....|....*....|....*....|..
gi 2205678935  88 AVRAKGGKVVReaGPMKHGTTVIA-FVEDPDG 118
Cdd:cd07238    74 RVVAAGLRIEY--GPTTEAWGVRRfFVRDPFG 103
BLMA_like cd08349
Bleomycin binding protein (BLMA) and similar proteins; BLMA also called Bleomycin resistance ...
 9-125 3.89e-03

Bleomycin binding protein (BLMA) and similar proteins; BLMA also called Bleomycin resistance protein, confers Bm resistance by directly binding to Bm. Bm is a glycopeptide antibiotic produced naturally by actinomycetes. It is a potent anti-cancer drug, which acts as a strong DNA-cutting agent, thereby causing cell death. BLMA is produced by actinomycetes to protect themselves against their own lethal compound. BLMA has two identically-folded subdomains, with the same alpha/beta fold; these two halves have no sequence similarity. BLMAs are dimers and each dimer binds to two Bm molecules at the Bm-binding pockets formed at the dimer interface; two Bm molecules are bound per dimer. BLMA 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. As for the larger superfamily, this family contains members with or without domain swapping.


Pssm-ID: 319937 [Multi-domain]  Cd Length: 114  Bit Score: 34.51  E-value: 3.89e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205678935   9 RVGQLDRSIAFYTDVLGMTLLRRHDYPEgrftLAFVGYGDedsnsvIELtHNWDTDSYELGNAFGHLAVEVADAYATCDA 88
Cdd:cd08349     5 PVRDIDKTLAFYVDVLGFEVDYERPPPG----YAILSRGG------VEL-HLFEHPGLDPAGSGVAAYIRVEDIDALHAE 73

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 2205678935  89 VRAKG-----GKVVREAGPMKHGTTVIAfVEDPDGYKIEFIQ 125
Cdd:cd08349    74 LKAAGlplfgIPRITPIEDKPWGMREFA-VVDPDGNLLRFGQ 114
VOC_BsYqjT cd07242
vicinal oxygen chelate (VOC) family protein similar to Bacillus subtilis YqjT; The vicinal ...
 5-122 4.13e-03

vicinal oxygen chelate (VOC) family protein similar to Bacillus subtilis YqjT; 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: 319906  Cd Length: 126  Bit Score: 34.77  E-value: 4.13e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205678935   5 HTMIRVGQLDRSIAFYTDVLGMtllrrhDYPEGRFTLAFVGYGDEDSNSVIELTHNWD-TDSY-ELGNAFGHLAVEVADA 82
Cdd:cd07242     4 HVELAVSDLHRSFKWFEWILGL------GWKEYDTWSFGPSWKLSGGSLLVVQQTDEFaTPEFdRARVGLNHLAFHAESR 77

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 2205678935  83 YATCDA---VRAKGGKVV-REAGPMKHGTT-VIAFVEDPDGYKIE 122
Cdd:cd07242    78 EAVDELtekLAKIGGVRTyGDRHPFAGGPPhYAAFCEDPDGIKLE 122
2_3_CTD_N cd07265
N-terminal domain of catechol 2,3-dioxygenase; This subfamily contains the N-terminal, ...
 1-55 7.49e-03

N-terminal domain of catechol 2,3-dioxygenase; This subfamily contains the N-terminal, non-catalytic, domain of catechol 2,3-dioxygenase. Catechol 2,3-dioxygenase (2,3-CTD, catechol:oxygen 2,3-oxidoreductase) catalyzes an extradiol cleavage of catechol to form 2-hydroxymuconate semialdehyde with the insertion of two atoms of oxygen. The enzyme is a homotetramer and contains catalytically essential Fe(II) . The reaction proceeds by an ordered bi-unit mechanism. First, catechol binds to the enzyme, this is then followed by the binding of dioxygen to form a tertiary complex, and then the aromatic ring is cleaved to produce 2-hydroxymuconate semialdehyde. Catechol 2,3-dioxygenase belongs to the type I extradiol dioxygenase family. The subunit comprises the N- and C-terminal domains of similar structure fold, resulting from an ancient gene duplication. The active site is located in a funnel-shaped space of the C-terminal domain. This subfamily represents the N-terminal domain.


Pssm-ID: 319926  Cd Length: 122  Bit Score: 33.86  E-value: 7.49e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2205678935   1 MRLLHTMIRVGQLDRSIAFYTDVLGMTLLRRHDypEGRftLAFVGYGDEDSNSVI 55
Cdd:cd07265     3 LRPGHVQLRVLDLEEAIKHYREVLGLVETGRDD--QGR--VYLKAWDEYDHHSII 53
VOC_ShValD_like cd16361
vicinal oxygen chelate (VOC) family protein similar to Streptomyces hygroscopicus ValD protein; ...
 5-125 7.51e-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: 34.23  E-value: 7.51e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205678935   5 HTMIRVGQLDRSIAFYTDVLGMTLLRRHDYPE------------------GRFTLAFVGYGDEDSnsvIEL--THNWDTD 64
Cdd:cd16361     4 HVGITVPDLDAAVEFYTDVLGAEVVYRSTPLAegdrgggemraagfvpgfARARIAMLRLGPGPG---IELfeYKGPEQR 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2205678935  65 SYELGNA-FG--HLAVEVADAYATCDAVRAKGGKVV-----REAGPMKHGTTVIaFVEDPDGYKIEFIQ 125
Cdd:cd16361    81 APVPRNSdVGifHFALQVDDVEAAAERLAAAGGKVLmgpreIPDGGPGKGNRMV-YLRDPWGTLIELVS 148
 
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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