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Conserved domains on  [gi|2214681167|ref|NP_001390445|]
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lactoylglutathione lyase [Oryza sativa Japonica Group]

Protein Classification

lactoylglutathione lyase( domain architecture ID 11476608)

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PLN02300 PLN02300
lactoylglutathione lyase
 6-291 0e+00

lactoylglutathione lyase


:

Pssm-ID: 215169 [Multi-domain]  Cd Length: 286  Bit Score: 547.84  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214681167   6 EAEKSPEVVLEWPKKDKKRLLHAVYRVGDLDRTIKCYTECFGMKLLRKRDVPEEKYTNAFLGFGPEDTNFALELTYNYGV 85
Cdd:PLN02300    6 STAAEAEDLLEWPKKDKRRMLHVVYRVGDLDRTIKFYTECLGMKLLRKRDIPEEKYTNAFLGYGPEDSNFVVELTYNYGV 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214681167  86 DKYDIGAGFGHFAIATEDVYKLAEKIKSSCCcKITREPGPVKGGSTVIAFAQDPDGYMFELIQRGPTPEPLCQVMLRVGD 165
Cdd:PLN02300   86 DKYDIGTGFGHFGIAVEDVAKTVELVKAKGG-KVTREPGPVKGGKSVIAFVKDPDGYKFELIQRGPTPEPLCQVMLRVGD 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214681167 166 LDRSIKFYEKALGMKLLRKKDVPDYKYTIAMLGYADEDKTTVIELTYNYGVTEYTKGNAYAQVAIGTEDVYKSAEAVELV 245
Cdd:PLN02300  165 LDRSIKFYEKAFGMKLLRKRDNPEYKYTIAMMGYGPEDKTTVLELTYNYGVTEYTKGNAYAQIAIGTDDVYKTAEAIKLV 244

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 2214681167 246 tkelGGKILRQPGPLPGLNTKIASFLDPDGWKVVLVDNADFLKELQ 291
Cdd:PLN02300  245 ----GGKITREPGPLPGINTKITACLDPDGWKTVFVDNIDFLKELE 286
 
Name Accession Description Interval E-value
PLN02300 PLN02300
lactoylglutathione lyase
 6-291 0e+00

lactoylglutathione lyase


Pssm-ID: 215169 [Multi-domain]  Cd Length: 286  Bit Score: 547.84  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214681167   6 EAEKSPEVVLEWPKKDKKRLLHAVYRVGDLDRTIKCYTECFGMKLLRKRDVPEEKYTNAFLGFGPEDTNFALELTYNYGV 85
Cdd:PLN02300    6 STAAEAEDLLEWPKKDKRRMLHVVYRVGDLDRTIKFYTECLGMKLLRKRDIPEEKYTNAFLGYGPEDSNFVVELTYNYGV 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214681167  86 DKYDIGAGFGHFAIATEDVYKLAEKIKSSCCcKITREPGPVKGGSTVIAFAQDPDGYMFELIQRGPTPEPLCQVMLRVGD 165
Cdd:PLN02300   86 DKYDIGTGFGHFGIAVEDVAKTVELVKAKGG-KVTREPGPVKGGKSVIAFVKDPDGYKFELIQRGPTPEPLCQVMLRVGD 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214681167 166 LDRSIKFYEKALGMKLLRKKDVPDYKYTIAMLGYADEDKTTVIELTYNYGVTEYTKGNAYAQVAIGTEDVYKSAEAVELV 245
Cdd:PLN02300  165 LDRSIKFYEKAFGMKLLRKRDNPEYKYTIAMMGYGPEDKTTVLELTYNYGVTEYTKGNAYAQIAIGTDDVYKTAEAIKLV 244

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 2214681167 246 tkelGGKILRQPGPLPGLNTKIASFLDPDGWKVVLVDNADFLKELQ 291
Cdd:PLN02300  245 ----GGKITREPGPLPGINTKITACLDPDGWKTVFVDNIDFLKELE 286
glyox_I TIGR00068
lactoylglutathione lyase; Lactoylglutathione lyase is also known as aldoketomutase and ...
 15-158 1.44e-78

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: 235.09  E-value: 1.44e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214681167  15 LEWPKKDKKRLLHAVYRVGDLDRTIKCYTECFGMKLLRKRDVPEEKYTNAFLGFGPEDTNFALELTYNYGVDKYDIGAGF 94
Cdd:TIGR00068   8 VADPKTKKRRLLHTMLRVGDLDKSLDFYTEVLGMKLLRKRDFPEMKFSLAFLGYGDETSAAVIELTHNWGTEKYDLGNGF 87

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2214681167  95 GHFAIATEDVYKLAEKIKSScCCKITREPGPVKGGSTVIAFAQDPDGYMFELIQRGPTPEPLCQ 158
Cdd:TIGR00068  88 GHIAIGVDDVYKACERVRAL-GGNVVREPGPVKGGTTVIAFVEDPDGYKIELIQRKSTKDGLGN 150
GlxI_Ni cd16358
Glyoxalase I that uses Ni(++) as cofactor; This family includes Escherichia coil and other ...
 25-147 2.83e-71

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: 215.34  E-value: 2.83e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214681167  25 LLHAVYRVGDLDRTIKCYTECFGMKLLRKRDVPEEKYTNAFLGFGPEDTNFALELTYNYGVDKYDIGAGFGHFAIATEDV 104
Cdd:cd16358     1 MLHTMLRVGDLDRSIKFYTEVLGMKLLRKRDYPEGKYTLAFVGYGDEDENTVLELTYNWGVDKYDLGTAYGHIAIGVEDV 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 2214681167 105 YKLAEKIKSScCCKITREPGPVKGGSTVIAFAQDPDGYMFELI 147
Cdd:cd16358    81 YETCERIRKK-GGKVTREPGPMKGGTTVIAFVEDPDGYKIELI 122
GloA COG0346
Catechol 2,3-dioxygenase or related enzyme, vicinal oxygen chelate (VOC) family [Secondary ...
 23-151 2.40e-26

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: 100.07  E-value: 2.40e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214681167  23 KRLLHAVYRVGDLDRTIKCYTECFGMKLLRKRDVPEEKYTNAFLGFGpedTNFALELTYNYGVDKYDIGAGFGHFAIATE 102
Cdd:COG0346     1 MGLHHVTLRVSDLEASLAFYTDVLGLELVKRTDFGDGGFGHAFLRLG---DGTELELFEAPGAAPAPGGGGLHHLAFRVD 77

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 2214681167 103 DVYKLAEKIKsSCCCKITREPGPVKGGSTVIAFaQDPDGYMFELIQRGP 151
Cdd:COG0346    78 DLDAAYARLR-AAGVEIEGEPRDRAYGYRSAYF-RDPDGNLIELVEPPP 124
Glyoxalase pfam00903
Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;
24-146 1.21e-25

Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;


Pssm-ID: 395724 [Multi-domain]  Cd Length: 121  Bit Score: 98.29  E-value: 1.21e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214681167  24 RLLHAVYRVGDLDRTIKCYTECFGMKLLRKRDVPEEkYTNAFLGFGPEDTnfALELTYNYGVDKYDIG---AGFGHFAIA 100
Cdd:pfam00903   1 RIDHVALRVGDLEKSLDFYTDVLGFKLVEETDAGEE-GGLRSAFFLAGGR--VLELLLNETPPPAAAGfggHHIAFIAFS 77

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 2214681167 101 TEDVYKLAEKIKSScCCKITREPGPVKGGSTVIAFaQDPDGYMFEL 146
Cdd:pfam00903  78 VDDVDAAYDRLKAA-GVEIVREPGRHGWGGRYSYF-RDPDGNLIEL 121
 
Name Accession Description Interval E-value
PLN02300 PLN02300
lactoylglutathione lyase
 6-291 0e+00

lactoylglutathione lyase


Pssm-ID: 215169 [Multi-domain]  Cd Length: 286  Bit Score: 547.84  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214681167   6 EAEKSPEVVLEWPKKDKKRLLHAVYRVGDLDRTIKCYTECFGMKLLRKRDVPEEKYTNAFLGFGPEDTNFALELTYNYGV 85
Cdd:PLN02300    6 STAAEAEDLLEWPKKDKRRMLHVVYRVGDLDRTIKFYTECLGMKLLRKRDIPEEKYTNAFLGYGPEDSNFVVELTYNYGV 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214681167  86 DKYDIGAGFGHFAIATEDVYKLAEKIKSSCCcKITREPGPVKGGSTVIAFAQDPDGYMFELIQRGPTPEPLCQVMLRVGD 165
Cdd:PLN02300   86 DKYDIGTGFGHFGIAVEDVAKTVELVKAKGG-KVTREPGPVKGGKSVIAFVKDPDGYKFELIQRGPTPEPLCQVMLRVGD 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214681167 166 LDRSIKFYEKALGMKLLRKKDVPDYKYTIAMLGYADEDKTTVIELTYNYGVTEYTKGNAYAQVAIGTEDVYKSAEAVELV 245
Cdd:PLN02300  165 LDRSIKFYEKAFGMKLLRKRDNPEYKYTIAMMGYGPEDKTTVLELTYNYGVTEYTKGNAYAQIAIGTDDVYKTAEAIKLV 244

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 2214681167 246 tkelGGKILRQPGPLPGLNTKIASFLDPDGWKVVLVDNADFLKELQ 291
Cdd:PLN02300  245 ----GGKITREPGPLPGINTKITACLDPDGWKTVFVDNIDFLKELE 286
glyox_I TIGR00068
lactoylglutathione lyase; Lactoylglutathione lyase is also known as aldoketomutase and ...
 15-158 1.44e-78

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: 235.09  E-value: 1.44e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214681167  15 LEWPKKDKKRLLHAVYRVGDLDRTIKCYTECFGMKLLRKRDVPEEKYTNAFLGFGPEDTNFALELTYNYGVDKYDIGAGF 94
Cdd:TIGR00068   8 VADPKTKKRRLLHTMLRVGDLDKSLDFYTEVLGMKLLRKRDFPEMKFSLAFLGYGDETSAAVIELTHNWGTEKYDLGNGF 87

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2214681167  95 GHFAIATEDVYKLAEKIKSScCCKITREPGPVKGGSTVIAFAQDPDGYMFELIQRGPTPEPLCQ 158
Cdd:TIGR00068  88 GHIAIGVDDVYKACERVRAL-GGNVVREPGPVKGGTTVIAFVEDPDGYKIELIQRKSTKDGLGN 150
GlxI_Ni cd16358
Glyoxalase I that uses Ni(++) as cofactor; This family includes Escherichia coil and other ...
 25-147 2.83e-71

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: 215.34  E-value: 2.83e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214681167  25 LLHAVYRVGDLDRTIKCYTECFGMKLLRKRDVPEEKYTNAFLGFGPEDTNFALELTYNYGVDKYDIGAGFGHFAIATEDV 104
Cdd:cd16358     1 MLHTMLRVGDLDRSIKFYTEVLGMKLLRKRDYPEGKYTLAFVGYGDEDENTVLELTYNWGVDKYDLGTAYGHIAIGVEDV 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 2214681167 105 YKLAEKIKSScCCKITREPGPVKGGSTVIAFAQDPDGYMFELI 147
Cdd:cd16358    81 YETCERIRKK-GGKVTREPGPMKGGTTVIAFVEDPDGYKIELI 122
GlxI_Ni cd16358
Glyoxalase I that uses Ni(++) as cofactor; This family includes Escherichia coil and other ...
 156-281 3.34e-66

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: 202.63  E-value: 3.34e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214681167 156 LCQVMLRVGDLDRSIKFYEKALGMKLLRKKDVPDYKYTIAMLGYADEDKTTVIELTYNYGVTEYTKGNAYAQVAIGTEDV 235
Cdd:cd16358     1 MLHTMLRVGDLDRSIKFYTEVLGMKLLRKRDYPEGKYTLAFVGYGDEDENTVLELTYNWGVDKYDLGTAYGHIAIGVEDV 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 2214681167 236 YKSAEAVelvtKELGGKILRQPGPLPGLNTKIASFLDPDGWKVVLV 281
Cdd:cd16358    81 YETCERI----RKKGGKVTREPGPMKGGTTVIAFVEDPDGYKIELI 122
glyox_I TIGR00068
lactoylglutathione lyase; Lactoylglutathione lyase is also known as aldoketomutase and ...
 156-283 2.34e-51

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: 165.75  E-value: 2.34e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214681167 156 LCQVMLRVGDLDRSIKFYEKALGMKLLRKKDVPDYKYTIAMLGYADEDKTTVIELTYNYGVTEYTKGNAYAQVAIGTEDV 235
Cdd:TIGR00068  18 LLHTMLRVGDLDKSLDFYTEVLGMKLLRKRDFPEMKFSLAFLGYGDETSAAVIELTHNWGTEKYDLGNGFGHIAIGVDDV 97

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 2214681167 236 YKSAEAVelvtKELGGKILRQPGPLPGLNTKIASFLDPDGWKVVLVDN 283
Cdd:TIGR00068  98 YKACERV----RALGGNVVREPGPVKGGTTVIAFVEDPDGYKIELIQR 141
PRK10291 PRK10291
glyoxalase I; Provisional
 31-148 4.95e-39

glyoxalase I; Provisional


Pssm-ID: 182358  Cd Length: 129  Bit Score: 133.22  E-value: 4.95e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214681167  31 RVGDLDRTIKCYTECFGMKLLRKRDVPEEKYTNAFLGFGPEDTNFALELTYNYGVDKYDIGAGFGHFAIATEDVYKLAEK 110
Cdd:PRK10291    3 RVGDLQRSIDFYTNVLGMKLLRTSENPEYKYSLAFVGYGPETEEAVIELTYNWGVDKYELGTAYGHIALSVDNAAEACEK 82

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 2214681167 111 IKSScCCKITREPGPVKGGSTVIAFAQDPDGYMFELIQ 148
Cdd:PRK10291   83 IRQN-GGNVTREAGPVKGGTTVIAFVEDPDGYKIELIE 119
PRK10291 PRK10291
glyoxalase I; Provisional
 160-285 4.74e-34

glyoxalase I; Provisional


Pssm-ID: 182358  Cd Length: 129  Bit Score: 120.51  E-value: 4.74e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214681167 160 MLRVGDLDRSIKFYEKALGMKLLRKKDVPDYKYTIAMLGYADEDKTTVIELTYNYGVTEYTKGNAYAQVAIGTEDvykSA 239
Cdd:PRK10291    1 MLRVGDLQRSIDFYTNVLGMKLLRTSENPEYKYSLAFVGYGPETEEAVIELTYNWGVDKYELGTAYGHIALSVDN---AA 77

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 2214681167 240 EAVELVtKELGGKILRQPGPLPGLNTKIASFLDPDGWKVVLVDNAD 285
Cdd:PRK10291   78 EACEKI-RQNGGNVTREAGPVKGGTTVIAFVEDPDGYKIELIEEKD 122
GlxI_Zn cd07233
Glyoxalase I that uses Zn(++) as cofactor; This family includes eukaryotic glyoxalase I that ...
 25-147 4.62e-27

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: 102.79  E-value: 4.62e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214681167  25 LLHAVYRVGDLDRTIKCYTECFGMKLLRKRDVPEEKYTNAFLGFGPEDTNFA-------------LELTYNYGVD----- 86
Cdd:cd07233     1 FNHTMLRVKDPKKSLKFYTEVLGMKLLRKKDFPEMKFSLYFLGYEDPKDIPKdprtawvfsregtLELTHNWGTEndedp 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2214681167  87 KYDIG----AGFGHFAIATEDVYKLAEKIKS-SCCCKITREPGPVKGgstvIAFAQDPDGYMFELI 147
Cdd:cd07233    81 VYHNGnsdpRGFGHIGIAVDDVYAACERFEElGVKFKKKPDDGKMKG----IAFIKDPDGYWIEIL 142
GloA COG0346
Catechol 2,3-dioxygenase or related enzyme, vicinal oxygen chelate (VOC) family [Secondary ...
 23-151 2.40e-26

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: 100.07  E-value: 2.40e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214681167  23 KRLLHAVYRVGDLDRTIKCYTECFGMKLLRKRDVPEEKYTNAFLGFGpedTNFALELTYNYGVDKYDIGAGFGHFAIATE 102
Cdd:COG0346     1 MGLHHVTLRVSDLEASLAFYTDVLGLELVKRTDFGDGGFGHAFLRLG---DGTELELFEAPGAAPAPGGGGLHHLAFRVD 77

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 2214681167 103 DVYKLAEKIKsSCCCKITREPGPVKGGSTVIAFaQDPDGYMFELIQRGP 151
Cdd:COG0346    78 DLDAAYARLR-AAGVEIEGEPRDRAYGYRSAYF-RDPDGNLIELVEPPP 124
Glyoxalase pfam00903
Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;
24-146 1.21e-25

Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;


Pssm-ID: 395724 [Multi-domain]  Cd Length: 121  Bit Score: 98.29  E-value: 1.21e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214681167  24 RLLHAVYRVGDLDRTIKCYTECFGMKLLRKRDVPEEkYTNAFLGFGPEDTnfALELTYNYGVDKYDIG---AGFGHFAIA 100
Cdd:pfam00903   1 RIDHVALRVGDLEKSLDFYTDVLGFKLVEETDAGEE-GGLRSAFFLAGGR--VLELLLNETPPPAAAGfggHHIAFIAFS 77

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 2214681167 101 TEDVYKLAEKIKSScCCKITREPGPVKGGSTVIAFaQDPDGYMFEL 146
Cdd:pfam00903  78 VDDVDAAYDRLKAA-GVEIVREPGRHGWGGRYSYF-RDPDGNLIEL 121
GloA COG0346
Catechol 2,3-dioxygenase or related enzyme, vicinal oxygen chelate (VOC) family [Secondary ...
 159-285 1.07e-24

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: 95.83  E-value: 1.07e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214681167 159 VMLRVGDLDRSIKFYEKALGMKLLRKKDVPDYKYTIAMLGYADEdktTVIELTYNYGVTEYTKGNAYAQVAIGTEDVYKS 238
Cdd:COG0346     6 VTLRVSDLEASLAFYTDVLGLELVKRTDFGDGGFGHAFLRLGDG---TELELFEAPGAAPAPGGGGLHHLAFRVDDLDAA 82

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 2214681167 239 AEAVelvtKELGGKILRQPGPLPGlNTKIASFLDPDGWKVVLVDNAD 285
Cdd:COG0346    83 YARL----RAAGVEIEGEPRDRAY-GYRSAYFRDPDGNLIELVEPPP 124
GLOD4_N cd08358
N-terminal domain of human glyoxalase domain-containing protein 4 and similar proteins; ...
 23-149 9.87e-23

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: 90.89  E-value: 9.87e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214681167  23 KRLLHAVYRVGDLDRTIKCYTECFGMKLLRKRDVPE-----------EKYTNAFLGFGPEDTNFALELTYNYGVDKYDIG 91
Cdd:cd08358     1 RRALHFVFKVGDRNKTIKFYREILGMKVLRHEEFEEgckaacngpydGKWSKTMVGYGPEDDHFVVELTYNYGIGDYELG 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2214681167  92 AGFGHFAIATEDVYKLAEKIKSsccckitrepgPVKGGSTVIAFAQDPDGYMFELIQR 149
Cdd:cd08358    81 NDFLGITIHSKQAVSRAKKHNW-----------PVTQVGDGVYEVKAPGGYKFYLIDK 127
GlxI_Zn cd07233
Glyoxalase I that uses Zn(++) as cofactor; This family includes eukaryotic glyoxalase I that ...
 158-276 9.02e-22

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: 88.54  E-value: 9.02e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214681167 158 QVMLRVGDLDRSIKFYEKALGMKLLRKKDVPDYKYTIAMLGYADEDKT-------------TVIELTYNYGvTE------ 218
Cdd:cd07233     3 HTMLRVKDPKKSLKFYTEVLGMKLLRKKDFPEMKFSLYFLGYEDPKDIpkdprtawvfsreGTLELTHNWG-TEndedpv 81

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2214681167 219 YTKGNAYAQ----VAIGTEDVYKSAEAVElvtkELGGKIlrQPGPLPGLNTKIASFLDPDGW 276
Cdd:cd07233    82 YHNGNSDPRgfghIGIAVDDVYAACERFE----ELGVKF--KKKPDDGKMKGIAFIKDPDGY 137
Glyoxalase pfam00903
Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;
158-280 2.31e-18

Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;


Pssm-ID: 395724 [Multi-domain]  Cd Length: 121  Bit Score: 79.03  E-value: 2.31e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214681167 158 QVMLRVGDLDRSIKFYEKALGMKLLRKKDVPDYKYTIAMLGYADEdktTVIELTYNYGVTEYTKGNA---YAQVAIGTED 234
Cdd:pfam00903   4 HVALRVGDLEKSLDFYTDVLGFKLVEETDAGEEGGLRSAFFLAGG---RVLELLLNETPPPAAAGFGghhIAFIAFSVDD 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 2214681167 235 VYKSAEAVelvtKELGGKILRQPGPLPGlNTKIASFLDPDGWKVVL 280
Cdd:pfam00903  81 VDAAYDRL----KAAGVEIVREPGRHGW-GGRYSYFRDPDGNLIEL 121
GLOD4_N cd08358
N-terminal domain of human glyoxalase domain-containing protein 4 and similar proteins; ...
 161-282 7.79e-17

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: 75.09  E-value: 7.79e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214681167 161 LRVGDLDRSIKFYEKALGMKLLRKKDVP-----------DYKYTIAMLGYADEDKTTVIELTYNYGVTEYTKGNAYAQVA 229
Cdd:cd08358     8 FKVGDRNKTIKFYREILGMKVLRHEEFEegckaacngpyDGKWSKTMVGYGPEDDHFVVELTYNYGIGDYELGNDFLGIT 87

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2214681167 230 IGTEDVYKSAEAVELVTKELGGKILRqpgplpglnTKiasflDPDGWKVVLVD 282
Cdd:cd08358    88 IHSKQAVSRAKKHNWPVTQVGDGVYE---------VK-----APGGYKFYLID 126
PLN03042 PLN03042
Lactoylglutathione lyase; Provisional
 158-282 1.58e-16

Lactoylglutathione lyase; Provisional


Pssm-ID: 215548  Cd Length: 185  Bit Score: 75.63  E-value: 1.58e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214681167 158 QVMLRVGDLDRSIKFYEKALGMKLLRKKDVPDYKYTIAMLGYadEDKTTV-----------------IELTYNYGvTE-- 218
Cdd:PLN03042   30 QTMFRIKDPKASLDFYSRVLGMSLLKRLDFPEMKFSLYFLGY--EDSETAptdppertvwtfgrkatIELTHNWG-TEsd 106

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2214681167 219 -----YTKGNA----YAQVAIGTEDVYKSAEAVElvtkELGGKILRQP--GPLPGLntkiASFLDPDGWKVVLVD 282
Cdd:PLN03042  107 pefkgYHNGNSdprgFGHIGITVDDVYKACERFE----KLGVEFVKKPddGKMKGL----AFIKDPDGYWIEIFD 173
PLN02367 PLN02367
lactoylglutathione lyase
 158-282 7.26e-16

lactoylglutathione lyase


Pssm-ID: 177995  Cd Length: 233  Bit Score: 75.04  E-value: 7.26e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214681167 158 QVMLRVGDLDRSIKFYEKALGMKLLRKKDVPDYKYTIAMLGY-------ADEDKTTV--------IELTYNYGvTE---- 218
Cdd:PLN02367   78 QTMYRIKDPKASLDFYSRVLGMSLLKRLDFPEMKFSLYFMGYedtasapTDPTERTVwtfgqkatIELTHNWG-TEsdpd 156

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2214681167 219 ---YTKGNA----YAQVAIGTEDVYKSAEAVElvtkELGGKILRQP--GPLPGlntkIASFLDPDGWKVVLVD 282
Cdd:PLN02367  157 fkgYHNGNSeprgFGHIGITVDDVYKACERFE----ELGVEFVKKPndGKMKG----IAFIKDPDGYWIEIFD 221
PLN02367 PLN02367
lactoylglutathione lyase
 29-146 8.43e-16

lactoylglutathione lyase


Pssm-ID: 177995  Cd Length: 233  Bit Score: 75.04  E-value: 8.43e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214681167  29 VYRVGDLDRTIKCYTECFGMKLLRKRDVPEEKYTNAFLGFgpEDTNFA-----------------LELTYNYGVDK---- 87
Cdd:PLN02367   80 MYRIKDPKASLDFYSRVLGMSLLKRLDFPEMKFSLYFMGY--EDTASAptdptertvwtfgqkatIELTHNWGTESdpdf 157

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2214681167  88 --YDIG----AGFGHFAIATEDVYKLAEKIKsSCCCKITREP--GPVKGgstvIAFAQDPDGYMFEL 146
Cdd:PLN02367  158 kgYHNGnsepRGFGHIGITVDDVYKACERFE-ELGVEFVKKPndGKMKG----IAFIKDPDGYWIEI 219
PLN03042 PLN03042
Lactoylglutathione lyase; Provisional
 1-147 3.65e-15

Lactoylglutathione lyase; Provisional


Pssm-ID: 215548  Cd Length: 185  Bit Score: 72.16  E-value: 3.65e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214681167   1 MASGSEAEKSPEVVLEWPKKDKKRLLH-AVYRVGDLDRTIKCYTECFGMKLLRKRDVPEEKYTNAFLGF---------GP 70
Cdd:PLN03042    3 SASKESAANNPGLCGNPDEATKGYIMQqTMFRIKDPKASLDFYSRVLGMSLLKRLDFPEMKFSLYFLGYedsetaptdPP 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214681167  71 EDTNF------ALELTYNYGVDK------YDIG----AGFGHFAIATEDVYKLAEKIKsscccKITRE--PGPVKGGSTV 132
Cdd:PLN03042   83 ERTVWtfgrkaTIELTHNWGTESdpefkgYHNGnsdpRGFGHIGITVDDVYKACERFE-----KLGVEfvKKPDDGKMKG 157

                         170
                  ....*....|....*
gi 2214681167 133 IAFAQDPDGYMFELI 147
Cdd:PLN03042  158 LAFIKDPDGYWIEIF 172
VOC cd06587
vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate (VOC) superfamily is composed ...
 27-146 1.15e-14

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


Pssm-ID: 319898 [Multi-domain]  Cd Length: 112  Bit Score: 68.71  E-value: 1.15e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214681167  27 HAVYRVGDLDRTIKCYTECFGMKLLRKRDVPEEkytnAFLGFGPEDTnfaLELTYNYGVDKyDIGAGFGHFAIATEDVYK 106
Cdd:cd06587     1 HVALRVPDLDASVAFYEEVLGFEVVSRNEGGGF----AFLRLGPGLR---LALLEGPEPER-PGGGGLFHLAFEVDDVDE 72

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 2214681167 107 LAEKIKSSCCCKITREPGPVKGGSTVIAFAQDPDGYMFEL 146
Cdd:cd06587    73 VDERLREAGAEGELVAPPVDDPWGGRSFYFRDPDGNLIEF 112
VOC cd06587
vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate (VOC) superfamily is composed ...
 159-280 1.84e-14

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


Pssm-ID: 319898 [Multi-domain]  Cd Length: 112  Bit Score: 68.32  E-value: 1.84e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214681167 159 VMLRVGDLDRSIKFYEKALGMKLLRKKDVPDYkytiAMLGYADEdktTVIELTYNYGVtEYTKGNAYAQVAIGTEDVyks 238
Cdd:cd06587     2 VALRVPDLDASVAFYEEVLGFEVVSRNEGGGF----AFLRLGPG---LRLALLEGPEP-ERPGGGGLFHLAFEVDDV--- 70

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 2214681167 239 AEAVELVTKELGGKILRQPGPLPGLNTKIASFLDPDGWKVVL 280
Cdd:cd06587    71 DEVDERLREAGAEGELVAPPVDDPWGGRSFYFRDPDGNLIEF 112
VOC COG3324
Lactoylglutathione lyase-related enzyme, vicinal oxygen chelate (VOC) family [General function ...
 153-275 2.74e-10

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


Pssm-ID: 442553 [Multi-domain]  Cd Length: 119  Bit Score: 56.95  E-value: 2.74e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214681167 153 PEPLCQVMLRVGDLDRSIKFYEKALGMKLLRKKDvPDYKYTIamlgyADEDKTTVIELtynyGVTEYTKGNAYAQVAIGT 232
Cdd:COG3324     2 PGTIVWVELPVDDLERAKAFYEEVFGWTFEDDAG-PGGDYAE-----FDTDGGQVGGL----MPGAEEPGGPGWLLYFAV 71

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 2214681167 233 EDVyksAEAVELVtKELGGKILRQPGPLPGLNtKIASFLDPDG 275
Cdd:COG3324    72 DDL---DAAVARV-EAAGGTVLRPPTDIPPWG-RFAVFRDPEG 109
CatE COG2514
Catechol-2,3-dioxygenase [Secondary metabolites biosynthesis, transport and catabolism];
24-181 2.85e-10

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


Pssm-ID: 442004 [Multi-domain]  Cd Length: 141  Bit Score: 57.28  E-value: 2.85e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214681167  24 RLLHAVYRVGDLDRTIKCYTECFGMKLLRKRDvpeekyTNAFLGFGPEDTNfaLELTYNYGVDKYDIGAGFGHFAIAT-- 101
Cdd:COG2514     3 RLGHVTLRVRDLERSAAFYTDVLGLEVVEREG------GRVYLRADGGEHL--LVLEEAPGAPPRPGAAGLDHVAFRVps 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214681167 102 -EDVYKLAEKIKSSCCckitREPGPV-KGGSTVIAFaQDPDGYMFELIQRGPTPEPlcqvmlrVGDLDRsikfyeKALGM 179
Cdd:COG2514    75 rADLDAALARLAAAGV----PVEGAVdHGVGESLYF-RDPDGNLIELYTDRPRFEH-------VGDLET------DVLGF 136


                  ..
gi 2214681167 180 KL 181
Cdd:COG2514   137 RL 138
MMCE cd07249
Methylmalonyl-CoA epimerase (MMCE); MMCE, also called methylmalonyl-CoA racemase (EC 5.1.99.1) ...
 156-281 1.23e-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: 52.19  E-value: 1.23e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214681167 156 LCQVMLRVGDLDRSIKFYEKALGMKLLRKKDVPDYKYTIAMLGYADedktTVIEL------TYNYGVTEYTKGNAYAQVA 229
Cdd:cd07249     1 LDHIGIAVPDLDEALKFYEDVLGVKVSEPEELEEQGVRVAFLELGN----TQIELleplgeDSPIAKFLDKKGGGLHHIA 76

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2214681167 230 IGTEDVYKSAEAVelvtKELGGKILrQPGPLPG-LNTKIAsFLDPDGWKVVLV 281
Cdd:cd07249    77 FEVDDIDAAVEEL----KAQGVRLL-SEGPRIGaHGKRVA-FLHPKDTGGVLI 123
ED_TypeI_classII_N cd16360
N-terminal domain of type I, class II extradiol dioxygenases; This family contains the ...
 27-147 2.26e-07

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: 48.47  E-value: 2.26e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214681167  27 HAVYRVGDLDRTIKCYTECFGMKLLRkrdvpEEKYTNAFLGFGPEdtnfalelTYNYGVDKYDiGAGFGHFAIAT---ED 103
Cdd:cd16360     1 YAELGVPDLEKALEFYTDVLGLQVAK-----RDGNSVYLRGYEDE--------HHSLVLYEAP-EAGLKHFAFEVaseED 66

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 2214681167 104 VYKLAEKIKSScCCKITREPGP-VKGGSTVIAFaQDPDGYMFELI 147
Cdd:cd16360    67 LERAAASLTAL-GCDVTWGPDGeVPGGGKGFRF-QDPSGHLLELF 109
SgaA_N_like cd07247
N-terminal domain of Streptomyces griseus SgaA and similar domains; SgaA suppresses the growth ...
 163-275 4.52e-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: 47.64  E-value: 4.52e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214681167 163 VGDLDRSIKFYEKALGmklLRKKDVPDYKYTIAMLGYADEDKTTVIELTYnygvtEYTKGNAYAQVAIGTEDVYKSAEAV 242
Cdd:cd07247     8 TTDLERAKAFYGAVFG---WTFEDEGDGGGDYALFTAGGGAVGGLMRAPE-----EVAGAPPGWLIYFAVDDLDAALARV 79

                          90       100       110
                  ....*....|....*....|....*....|...
gi 2214681167 243 ElvtkELGGKILRQPGPLPGLnTKIASFLDPDG 275
Cdd:cd07247    80 E----AAGGKVVVPPTDIPGG-GRFAVFADPEG 107
VOC_like cd07262
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 159-278 2.09e-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: 319923 [Multi-domain]  Cd Length: 121  Bit Score: 46.07  E-value: 2.09e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214681167 159 VMLRVGDLDRSIKFYEKA---LGMKLLRKKDvpdykytiAMLGYADEDKTTVIeLTYNYGVTEYTKGNAyAQVAIgtedV 235
Cdd:cd07262     4 VTIGVNDLERSRAFYDAAlapLGYKRGFEDG--------GRVGYGLEGGPDFW-VTEPFDGEPATAGNG-THVAF----A 69

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2214681167 236 YKSAEAVE------LvtkELGGKILRQPGPLP--GLNTKIASFLDPDGWKV 278
Cdd:cd07262    70 APSRAAVDafhaaaL---AAGGTDNGAPGLRPhyHPGYYAAYVRDPDGNKI 117
CatE COG2514
Catechol-2,3-dioxygenase [Secondary metabolites biosynthesis, transport and catabolism];
159-275 2.42e-06

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


Pssm-ID: 442004 [Multi-domain]  Cd Length: 141  Bit Score: 46.10  E-value: 2.42e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214681167 159 VMLRVGDLDRSIKFYEKALGMKLLRKKDvpdykyTIAMLGyADEDkTTVIELTYNYGVTEYTKGNAYAQVAIGTEDvyks 238
Cdd:COG2514     7 VTLRVRDLERSAAFYTDVLGLEVVEREG------GRVYLR-ADGG-EHLLVLEEAPGAPPRPGAAGLDHVAFRVPS---- 74

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 2214681167 239 AEAVELVTKELGGKILRQPGPLPGLNTKIASFLDPDG 275
Cdd:COG2514    75 RADLDAALARLAAAGVPVEGAVDHGVGESLYFRDPDG 111
VOC COG3324
Lactoylglutathione lyase-related enzyme, vicinal oxygen chelate (VOC) family [General function ...
 24-151 3.50e-06

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


Pssm-ID: 442553 [Multi-domain]  Cd Length: 119  Bit Score: 45.40  E-value: 3.50e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214681167  24 RLLHAVYRVGDLDRTIKCYTECFGMKLLRKRDVPEEkYTNAFLGFGpedTNFALeltynyGVDKYDIGAGFGHFAIATED 103
Cdd:COG3324     4 TIVWVELPVDDLERAKAFYEEVFGWTFEDDAGPGGD-YAEFDTDGG---QVGGL------MPGAEEPGGPGWLLYFAVDD 73

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 2214681167 104 VYKLAEKIKSSCCcKITREPGPVKGGSTvIAFAQDPDGYMFELIQRGP 151
Cdd:COG3324    74 LDAAVARVEAAGG-TVLRPPTDIPPWGR-FAVFRDPEGNRFGLWQPAA 119
GLOD4_C cd16357
C-terminal domain of human glyoxalase domain-containing protein 4 and similar proteins; ...
 158-203 3.22e-05

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: 42.16  E-value: 3.22e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 2214681167 158 QVMLRVGDLDRSIKFYEKALGMKLLRKKDvpdykyTIAMLGYADED 203
Cdd:cd16357     1 KVSLAVSDLEKSIDYWSDLLGMKVFEKSE------KSALLGYGEDQ 40
VOC_like cd07264
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 158-275 1.23e-04

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


Pssm-ID: 319925 [Multi-domain]  Cd Length: 118  Bit Score: 40.78  E-value: 1.23e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214681167 158 QVMLRVGDLDRSIKFYEKALGmkLLRKKDVPDYKY--------TIAMLGYADEDKTTVIELtynygvteytkGNAYAQVA 229
Cdd:cd07264     3 YIVLYVDDFAASLRFYRDVLG--LPPRFLHEEGEYaefdtgetKLALFSRKEMARSGGPDR-----------RGSAFELG 69

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 2214681167 230 IGTEDVYKSAEAVelvtKELGGKILRQPGPLP-GLntKIASFLDPDG 275
Cdd:cd07264    70 FEVDDVEATVEEL----VERGAEFVREPANKPwGQ--TVAYVRDPDG 110
HppD COG3185
4-hydroxyphenylpyruvate dioxygenase and related hemolysins [Amino acid transport and ...
 91-282 7.89e-04

4-hydroxyphenylpyruvate dioxygenase and related hemolysins [Amino acid transport and metabolism, General function prediction only];


Pssm-ID: 442418 [Multi-domain]  Cd Length: 333  Bit Score: 40.26  E-value: 7.89e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214681167  91 GAGFGHFAIATEDV---YKLAEKIKssccCKITREPGP-------VKG-GSTVIAFAQDPDG---YM--FELIQRGPTPE 154
Cdd:COG3185    65 GPGVCAIAFRVDDAaaaYERALALG----AEPFEGPGPgelripaIRGiGGSLHYFVDRYGYggiYDpdFEPLPGDAAPA 140

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214681167 155 P--------LCQVMlRVGDLDRSIKFYEKALGMKLLRKKDVPDyKYT---IAMLgyADEDKTTVIELtyNYGVT------ 217
Cdd:COG3185   141 GagltridhIGIAV-PRGDLDEWVLFYEDVLGFEEIREEDIED-PYQgvrSAVL--QSPDGKVRIPL--NEPTSpdsqia 214

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2214681167 218 ---EYTKGNAYAQVAIGTEDVYKSAEAVelvtKELGGKILRQPGP--------LPGLNTKIAsFLDPdgwKVVLVD 282
Cdd:COG3185   215 eflEKYRGEGIQHIAFATDDIEATVAAL----RARGVRFLDIPDNyyddleprVGAHGEDVA-FLHP---KGILVD 282
GLOD5 cd07253
Human glyoxalase domain-containing protein 5 and similar proteins; Uncharacterized subfamily ...
 23-146 9.90e-04

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: 38.36  E-value: 9.90e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214681167  23 KRLLHAVYRVGDLDRTIKCYTECFGMKLLRKRdvpEEKYTnafLGFGPEDTNFaLELTYNYGVDKYDIGAGFGHFAIATE 102
Cdd:cd07253     2 KRLDHLVLTVKDIERTIDFYTKVLGMTVVTFK---EGRKA---LRFGNQKINL-HQKGKEFEPKASAPTPGSADLCFITE 74

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 2214681167 103 -DVYKLAEKIKSsccCKITREPGPVK-----GGSTVIAFaQDPDGYMFEL 146
Cdd:cd07253    75 tPIDEVLEHLEA---CGVTIEEGPVKrtgalGPILSIYF-RDPDGNLIEL 120
MMCE cd07249
Methylmalonyl-CoA epimerase (MMCE); MMCE, also called methylmalonyl-CoA racemase (EC 5.1.99.1) ...
 32-148 1.82e-03

Methylmalonyl-CoA epimerase (MMCE); MMCE, also called methylmalonyl-CoA racemase (EC 5.1.99.1) interconverts (2R)-methylmalonyl-CoA and (2S)-methylmalonyl-CoA. MMCE has been found in bacteria, archaea, and in animals. In eukaryotes, MMCE is an essential enzyme in a pathway that converts propionyl-CoA to succinyl-CoA, and is important in the breakdown of odd-chain length fatty acids, branched-chain amino acids, and other metabolites. In bacteria, MMCE participates in the reverse pathway for propionate fermentation, glyoxylate regeneration, and the biosynthesis of polyketide antibiotics. MMCE is closely related to glyoxalase I and type I extradiol dioxygenases.


Pssm-ID: 319912 [Multi-domain]  Cd Length: 127  Bit Score: 37.56  E-value: 1.82e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214681167  32 VGDLDRTIKCYTECFGMKLLRKRDVPEEKYTNAFLGFGP----------EDTNFALELTYNygvdkydiGAGFGHFAIAT 101
Cdd:cd07249     8 VPDLDEALKFYEDVLGVKVSEPEELEEQGVRVAFLELGNtqielleplgEDSPIAKFLDKK--------GGGLHHIAFEV 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 2214681167 102 EDVYKLAEKIKSSCCCKITREPGPVKGGSTViAF--AQDPDGYMFELIQ 148
Cdd:cd07249    80 DDIDAAVEELKAQGVRLLSEGPRIGAHGKRV-AFlhPKDTGGVLIELVE 127
PhnB COG2764
Zn-dependent glyoxalase, PhnB family [Energy production and conversion];
161-275 2.06e-03

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


Pssm-ID: 442048 [Multi-domain]  Cd Length: 118  Bit Score: 37.14  E-value: 2.06e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214681167 161 LRVGDLDRSIKFYEKALGMKLLRKKDVPDYKYTIAMLGYADedktTVIELTYNYGVTEYTKGNAYAqVAIGTEDVYKSAE 240
Cdd:COG2764     6 LVVDDAEEALEFYEDVFGFEVVFRMTDPDGKIMHAELRIGG----SVLMLSDAPPDSPAAEGNGVS-LSLYVDDVDALFA 80

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 2214681167 241 AVelvtKELGGKILRQPGPLP-GlnTKIASFLDPDG 275
Cdd:COG2764    81 RL----VAAGATVVMPLQDTFwG--DRFGMVRDPFG 110
VOC_like cd07251
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 32-146 4.96e-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: 4.96e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214681167  32 VGDLDRTIKCYTEcFGMKLLRKRDVPEEKY-TNAF-LGFGPEDtNFALELtynyGVDkyDIGAGFGHFAIA-----TEDV 104
Cdd:cd07251     6 VRDLERSARFYEA-LGWKPNLDPNDGVVFFqLGGTvLALYPRD-ALAEDA----GVS--VTGAGFSGVTLAhnvrsREEV 77

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 2214681167 105 YKLAEKIKSSCCcKITREPGPVKGGStVIAFAQDPDGYMFEL 146
Cdd:cd07251    78 DQLLAKAVAAGG-KILKPPQEVFWGG-YSGYFADPDGHIWEV 117
ED_TypeI_classII_C cd08343
C-terminal domain of type I, class II extradiol dioxygenases, catalytic domain; This family ...
 27-155 8.04e-03

C-terminal domain of type I, class II extradiol dioxygenases, catalytic domain; This family contains the C-terminal, 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: 319931  Cd Length: 132  Bit Score: 35.76  E-value: 8.04e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214681167  27 HAVYRVGDLDRTIKCYTECFGMKLlrkRDVpeekytnaflgFGPEDTNFALELTYNYGVDKYDI------GAGFGHFAIA 100
Cdd:cd08343     2 HVVLCSPDVEASRDFYTDVLGFRV---SDR-----------IVDPGVDGGAFLHCDRGTDHHTValaggpHPGLHHVAFE 67

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2214681167 101 TEDV-------YKLAEKiksscccKITREPGPVK--GGSTVIAFAQDPDGYMFELIQRGPTPEP 155
Cdd:cd08343    68 VHDLddvgrghDRLREK-------GYKIEWGPGRhgLGSQVFDYWFDPSGNRVEYYTDGDLVDD 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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