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Conserved domains on  [gi|447068012|ref|WP_001145268|]
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MULTISPECIES: VOC family protein [Bacillus]

Protein Classification

VOC family protein( domain architecture ID 10001243)

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

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

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
GloA COG0346
Catechol 2,3-dioxygenase or related enzyme, vicinal oxygen chelate (VOC) family [Secondary ...
4-127 7.79e-32

Catechol 2,3-dioxygenase or related enzyme, vicinal oxygen chelate (VOC) family [Secondary metabolites biosynthesis, transport and catabolism];


:

Pssm-ID: 440115 [Multi-domain]  Cd Length: 125  Bit Score: 109.31  E-value: 7.79e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447068012   4 RRIEHVGLMVANLEASISFYEEVVGLQLLKRMGHPNPDLKLAFLGVEEskETILELIEGYN-SSLPAEGKVHHICFKVDS 82
Cdd:COG0346    1 MGLHHVTLRVSDLEASLAFYTDVLGLELVKRTDFGDGGFGHAFLRLGD--GTELELFEAPGaAPAPGGGGLHHLAFRVDD 78
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 447068012  83 LEDEIERIQKHGVTFLlgEEIETLPDGTRYIFFAGPDGEWIEFFE 127
Cdd:COG0346   79 LDAAYARLRAAGVEIE--GEPRDRAYGYRSAYFRDPDGNLIELVE 121
 
Name Accession Description Interval E-value
GloA COG0346
Catechol 2,3-dioxygenase or related enzyme, vicinal oxygen chelate (VOC) family [Secondary ...
4-127 7.79e-32

Catechol 2,3-dioxygenase or related enzyme, vicinal oxygen chelate (VOC) family [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 440115 [Multi-domain]  Cd Length: 125  Bit Score: 109.31  E-value: 7.79e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447068012   4 RRIEHVGLMVANLEASISFYEEVVGLQLLKRMGHPNPDLKLAFLGVEEskETILELIEGYN-SSLPAEGKVHHICFKVDS 82
Cdd:COG0346    1 MGLHHVTLRVSDLEASLAFYTDVLGLELVKRTDFGDGGFGHAFLRLGD--GTELELFEAPGaAPAPGGGGLHHLAFRVDD 78
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 447068012  83 LEDEIERIQKHGVTFLlgEEIETLPDGTRYIFFAGPDGEWIEFFE 127
Cdd:COG0346   79 LDAAYARLRAAGVEIE--GEPRDRAYGYRSAYFRDPDGNLIELVE 121
VOC cd06587
vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate (VOC) superfamily is composed ...
8-125 2.67e-25

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: 92.20  E-value: 2.67e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447068012   8 HVGLMVANLEASISFYEEVVGLQLLKRMGHPnpdlKLAFLGVEEskETILELIEGYNSSLPAEGKVHHICFKVDSLEDEI 87
Cdd:cd06587    1 HVALRVPDLDASVAFYEEVLGFEVVSRNEGG----GFAFLRLGP--GLRLALLEGPEPERPGGGGLFHLAFEVDDVDEVD 74
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 447068012  88 ERIQKHGVTFLLGEEIETLPDGTRYIFFAGPDGEWIEF 125
Cdd:cd06587   75 ERLREAGAEGELVAPPVDDPWGGRSFYFRDPDGNLIEF 112
Glyoxalase pfam00903
Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;
5-125 1.89e-19

Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;


Pssm-ID: 395724 [Multi-domain]  Cd Length: 121  Bit Score: 77.49  E-value: 1.89e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447068012    5 RIEHVGLMVANLEASISFYEEVVGLQLLKRMGHPN-PDLKLAFLGVEeskETILELIEGYNSSLPAEGK----VHHICFK 79
Cdd:pfam00903   1 RIDHVALRVGDLEKSLDFYTDVLGFKLVEETDAGEeGGLRSAFFLAG---GRVLELLLNETPPPAAAGFgghhIAFIAFS 77
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 447068012   80 VDSLEDEIERIQKHGVTFLlgEEIETLPDGTRYIFFAGPDGEWIEF 125
Cdd:pfam00903  78 VDDVDAAYDRLKAAGVEIV--REPGRHGWGGRYSYFRDPDGNLIEL 121
glyox_I TIGR00068
lactoylglutathione lyase; Lactoylglutathione lyase is also known as aldoketomutase and ...
4-128 6.71e-18

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: 74.46  E-value: 6.71e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447068012    4 RRIEHVGLMVANLEASISFYEEVVGLQLLKRMGHPNPDLKLAFLGVE-ESKETILELIEGYNSSLPAEGKVH-HICFKVD 81
Cdd:TIGR00068  16 RRLLHTMLRVGDLDKSLDFYTEVLGMKLLRKRDFPEMKFSLAFLGYGdETSAAVIELTHNWGTEKYDLGNGFgHIAIGVD 95
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 447068012   82 SLEDEIERIQKHGVTFLlgEEIETLPDGTRYI-FFAGPDGEWIEFFET 128
Cdd:TIGR00068  96 DVYKACERVRALGGNVV--REPGPVKGGTTVIaFVEDPDGYKIELIQR 141
PRK10291 PRK10291
glyoxalase I; Provisional
11-129 2.36e-09

glyoxalase I; Provisional


Pssm-ID: 182358  Cd Length: 129  Bit Score: 51.56  E-value: 2.36e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447068012  11 LMVANLEASISFYEEVVGLQLLKRMGHPNPDLKLAFLGV-EESKETILELIEGYNSSLPAEGKVH-HICFKVDSLEDEIE 88
Cdd:PRK10291   2 LRVGDLQRSIDFYTNVLGMKLLRTSENPEYKYSLAFVGYgPETEEAVIELTYNWGVDKYELGTAYgHIALSVDNAAEACE 81
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 447068012  89 RIQKHGVTflLGEEIETLPDGTRYI-FFAGPDGEWIEFFETE 129
Cdd:PRK10291  82 KIRQNGGN--VTREAGPVKGGTTVIaFVEDPDGYKIELIEEK 121
 
Name Accession Description Interval E-value
GloA COG0346
Catechol 2,3-dioxygenase or related enzyme, vicinal oxygen chelate (VOC) family [Secondary ...
4-127 7.79e-32

Catechol 2,3-dioxygenase or related enzyme, vicinal oxygen chelate (VOC) family [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 440115 [Multi-domain]  Cd Length: 125  Bit Score: 109.31  E-value: 7.79e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447068012   4 RRIEHVGLMVANLEASISFYEEVVGLQLLKRMGHPNPDLKLAFLGVEEskETILELIEGYN-SSLPAEGKVHHICFKVDS 82
Cdd:COG0346    1 MGLHHVTLRVSDLEASLAFYTDVLGLELVKRTDFGDGGFGHAFLRLGD--GTELELFEAPGaAPAPGGGGLHHLAFRVDD 78
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 447068012  83 LEDEIERIQKHGVTFLlgEEIETLPDGTRYIFFAGPDGEWIEFFE 127
Cdd:COG0346   79 LDAAYARLRAAGVEIE--GEPRDRAYGYRSAYFRDPDGNLIELVE 121
VOC cd06587
vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate (VOC) superfamily is composed ...
8-125 2.67e-25

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: 92.20  E-value: 2.67e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447068012   8 HVGLMVANLEASISFYEEVVGLQLLKRMGHPnpdlKLAFLGVEEskETILELIEGYNSSLPAEGKVHHICFKVDSLEDEI 87
Cdd:cd06587    1 HVALRVPDLDASVAFYEEVLGFEVVSRNEGG----GFAFLRLGP--GLRLALLEGPEPERPGGGGLFHLAFEVDDVDEVD 74
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 447068012  88 ERIQKHGVTFLLGEEIETLPDGTRYIFFAGPDGEWIEF 125
Cdd:cd06587   75 ERLREAGAEGELVAPPVDDPWGGRSFYFRDPDGNLIEF 112
Glyoxalase pfam00903
Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;
5-125 1.89e-19

Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;


Pssm-ID: 395724 [Multi-domain]  Cd Length: 121  Bit Score: 77.49  E-value: 1.89e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447068012    5 RIEHVGLMVANLEASISFYEEVVGLQLLKRMGHPN-PDLKLAFLGVEeskETILELIEGYNSSLPAEGK----VHHICFK 79
Cdd:pfam00903   1 RIDHVALRVGDLEKSLDFYTDVLGFKLVEETDAGEeGGLRSAFFLAG---GRVLELLLNETPPPAAAGFgghhIAFIAFS 77
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 447068012   80 VDSLEDEIERIQKHGVTFLlgEEIETLPDGTRYIFFAGPDGEWIEF 125
Cdd:pfam00903  78 VDDVDAAYDRLKAAGVEIV--REPGRHGWGGRYSYFRDPDGNLIEL 121
glyox_I TIGR00068
lactoylglutathione lyase; Lactoylglutathione lyase is also known as aldoketomutase and ...
4-128 6.71e-18

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: 74.46  E-value: 6.71e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447068012    4 RRIEHVGLMVANLEASISFYEEVVGLQLLKRMGHPNPDLKLAFLGVE-ESKETILELIEGYNSSLPAEGKVH-HICFKVD 81
Cdd:TIGR00068  16 RRLLHTMLRVGDLDKSLDFYTEVLGMKLLRKRDFPEMKFSLAFLGYGdETSAAVIELTHNWGTEKYDLGNGFgHIAIGVD 95
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 447068012   82 SLEDEIERIQKHGVTFLlgEEIETLPDGTRYI-FFAGPDGEWIEFFET 128
Cdd:TIGR00068  96 DVYKACERVRALGGNVV--REPGPVKGGTTVIaFVEDPDGYKIELIQR 141
CatE COG2514
Catechol-2,3-dioxygenase [Secondary metabolites biosynthesis, transport and catabolism];
3-126 2.62e-17

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


Pssm-ID: 442004 [Multi-domain]  Cd Length: 141  Bit Score: 72.68  E-value: 2.62e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447068012   3 VRRIEHVGLMVANLEASISFYEEVVGLQLLKRMGHpnpdlkLAFLGVEESkETILELIEGYN-SSLPAEGKVHHICFKVD 81
Cdd:COG2514    1 ITRLGHVTLRVRDLERSAAFYTDVLGLEVVEREGG------RVYLRADGG-EHLLVLEEAPGaPPRPGAAGLDHVAFRVP 73
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 447068012  82 S---LEDEIERIQKHGVTFLLGEEietlPDGTRYIFFAGPDGEWIEFF 126
Cdd:COG2514   74 SradLDAALARLAAAGVPVEGAVD----HGVGESLYFRDPDGNLIELY 117
MMCE cd07249
Methylmalonyl-CoA epimerase (MMCE); MMCE, also called methylmalonyl-CoA racemase (EC 5.1.99.1) ...
6-115 7.50e-17

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: 71.07  E-value: 7.50e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447068012   6 IEHVGLMVANLEASISFYEEVVGLQLLKRMGHPNPDLKLAFLGVEESKetiLELIE--GYNSSL------PAEGkVHHIC 77
Cdd:cd07249    1 LDHIGIAVPDLDEALKFYEDVLGVKVSEPEELEEQGVRVAFLELGNTQ---IELLEplGEDSPIakfldkKGGG-LHHIA 76
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 447068012  78 FKVDSLEDEIERIQKHGVTfLLGEEIETLPDGTRYIFF 115
Cdd:cd07249   77 FEVDDIDAAVEELKAQGVR-LLSEGPRIGAHGKRVAFL 113
GlxI_Ni cd16358
Glyoxalase I that uses Ni(++) as cofactor; This family includes Escherichia coil and other ...
8-125 3.20e-15

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: 66.65  E-value: 3.20e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447068012   8 HVGLMVANLEASISFYEEVVGLQLLKRMGHPNPDLKLAFLGV-EESKETILELIEGYNSSLPAEGKVH-HICFKVDSLED 85
Cdd:cd16358    3 HTMLRVGDLDRSIKFYTEVLGMKLLRKRDYPEGKYTLAFVGYgDEDENTVLELTYNWGVDKYDLGTAYgHIAIGVEDVYE 82
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 447068012  86 EIERIQKHGVTFLlgEEIETLPDGTRYI-FFAGPDGEWIEF 125
Cdd:cd16358   83 TCERIRKKGGKVT--REPGPMKGGTTVIaFVEDPDGYKIEL 121
VOC_like cd07245
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
6-125 8.15e-15

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: 65.42  E-value: 8.15e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447068012   6 IEHVGLMVANLEASISFYEEVVGLQLLKRmgHPNPDLKLAFLGVEEskETILELIEGYNSSLPAE----GKVHHICFKVD 81
Cdd:cd07245    1 LDHVALACPDLERARRFYTDVLGLEEVPR--PPFLKFGGAWLYLGG--GQQIHLVVEQNPSELPRpehpGRDRHPSFSVP 76
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 447068012  82 SLEDEIERIQKHGVTFllgEEIETLPDGTRYIFFAGPDGEWIEF 125
Cdd:cd07245   77 DLDALKQRLKEAGIPY---TESTSPGGGVTQLFFRDPDGNRLEF 117
VOC COG3324
Lactoylglutathione lyase-related enzyme, vicinal oxygen chelate (VOC) family [General function ...
2-127 1.09e-14

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


Pssm-ID: 442553 [Multi-domain]  Cd Length: 119  Bit Score: 65.04  E-value: 1.09e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447068012   2 PVRRIEHVGLMVANLEASISFYEEVVGLQLLKRMGHPNPdlklaFLGVEESKETILELIEGynSSLPAEGKVHhICFKVD 81
Cdd:COG3324    1 MPGTIVWVELPVDDLERAKAFYEEVFGWTFEDDAGPGGD-----YAEFDTDGGQVGGLMPG--AEEPGGPGWL-LYFAVD 72
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 447068012  82 SLEDEIERIQKHGVTFLlgEEIETLPDGTRYIFFAGPDGEWIEFFE 127
Cdd:COG3324   73 DLDAAVARVEAAGGTVL--RPPTDIPPWGRFAVFRDPEGNRFGLWQ 116
GlxI_Zn cd07233
Glyoxalase I that uses Zn(++) as cofactor; This family includes eukaryotic glyoxalase I that ...
8-126 1.34e-14

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: 65.43  E-value: 1.34e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447068012   8 HVGLMVANLEASISFYEEVVGLQLLKRMGHPNPDLKLAFLGVEE--------------SKETILELIEGYNSSLPAEGKV 73
Cdd:cd07233    3 HTMLRVKDPKKSLKFYTEVLGMKLLRKKDFPEMKFSLYFLGYEDpkdipkdprtawvfSREGTLELTHNWGTENDEDPVY 82
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 447068012  74 H----------HICFKVDSLEDEIERIQKHGVTFllgeeIETLPDGT-RYIFFA-GPDGEWIEFF 126
Cdd:cd07233   83 HngnsdprgfgHIGIAVDDVYAACERFEELGVKF-----KKKPDDGKmKGIAFIkDPDGYWIEIL 142
metmalonyl_epim TIGR03081
methylmalonyl-CoA epimerase; Members of this protein family are the enzyme methylmalonyl-CoA ...
5-102 8.92e-12

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


Pssm-ID: 213772 [Multi-domain]  Cd Length: 128  Bit Score: 57.72  E-value: 8.92e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447068012    5 RIEHVGLMVANLEASISFYEEVVGLQLLKRMGHPNPDLKLAFLGVEESKetiLELIEGYNSSLPA-------EGKVHHIC 77
Cdd:TIGR03081   1 RIDHVGIAVPDLEEAAKFYEDVLGAQVSEIEELPEQGVKVVFIALGNTK---VELLEPLGEDSPIakfleknGGGIHHIA 77
                          90       100
                  ....*....|....*....|....*
gi 447068012   78 FKVDSLEDEIERIQKHGVTfLLGEE 102
Cdd:TIGR03081  78 IEVDDIEAALETLKEKGVR-LIDEE 101
VOC_ShValD_like cd16361
vicinal oxygen chelate (VOC) family protein similar to Streptomyces hygroscopicus ValD protein; ...
5-125 9.27e-11

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: 55.80  E-value: 9.27e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447068012   5 RIEHVGLMVANLEASISFYEEVVGLQLLKRM------------------GHPNPDLKLAFLGVEESkeTILELIEGYNSS 66
Cdd:cd16361    1 GVNHVGITVPDLDAAVEFYTDVLGAEVVYRStplaegdrgggemraagfVPGFARARIAMLRLGPG--PGIELFEYKGPE 78
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 447068012  67 LPAEGK------VHHICFKVDSLEDEIERIQKHGVTFLLG-EEIETLPD--GTRYIFFAGPDGEWIEF 125
Cdd:cd16361   79 QRAPVPrnsdvgIFHFALQVDDVEAAAERLAAAGGKVLMGpREIPDGGPgkGNRMVYLRDPWGTLIEL 146
Glyoxalase_4 pfam13669
Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;
8-114 2.25e-10

Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;


Pssm-ID: 463951 [Multi-domain]  Cd Length: 109  Bit Score: 53.82  E-value: 2.25e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447068012    8 HVGLMVANLEASISFYEEVVGLQLL--KRMGHPNPDLKLAFLGVEESKetiLELIE--GYNSSL-PAEGKVHHICFKVDS 82
Cdd:pfam13669   2 HVGIAVPDLDRALALWGALLGLGPEgdYRSEPQNVDLAFALLGDGPVE---VELIQplDGDSPLaRHGPGLHHLAYWVDD 78
                          90       100       110
                  ....*....|....*....|....*....|..
gi 447068012   83 LEDEIERIQKHGVTFlLGEEIETLPDGTRYIF 114
Cdd:pfam13669  79 LDAAVARLLDQGYRV-APKGPRAGAAGRRVAF 109
HppD COG3185
4-hydroxyphenylpyruvate dioxygenase and related hemolysins [Amino acid transport and ...
1-98 3.24e-10

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: 56.05  E-value: 3.24e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447068012   1 MPVRRIEHVGLMVA--NLEASISFYEEVVGLQLLKR--------------MGHPNPDLKLAFLGVEESKETILELIEGYN 64
Cdd:COG3185  142 AGLTRIDHIGIAVPrgDLDEWVLFYEDVLGFEEIREediedpyqgvrsavLQSPDGKVRIPLNEPTSPDSQIAEFLEKYR 221
                         90       100       110
                 ....*....|....*....|....*....|....
gi 447068012  65 sslpAEGkVHHICFKVDSLEDEIERIQKHGVTFL 98
Cdd:COG3185  222 ----GEG-IQHIAFATDDIEATVAALRARGVRFL 250
VOC_Bs_YwkD_like cd08352
vicinal oxygen chelate (VOC) family protein Bacillus subtilis YwkD and similar proteins; ...
4-127 7.04e-10

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: 52.93  E-value: 7.04e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447068012   4 RRIEHVGLMVANLEASISFYEEVVGLQLLKRMGHPNPD---LKLAFLGVEesketiLELIEGYN-----SSLPAEGkVHH 75
Cdd:cd08352    1 KKIHHIAIICSDYEKSKDFYVDKLGFEIIREHYRPERNdikLDLALGGYQ------LELFIKPDaparpSYPEALG-LRH 73
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 447068012  76 ICFKVDSLEDEIERIQKHGVTFllgEEIETLP-DGTRYIFFAGPDGEWIEFFE 127
Cdd:cd08352   74 LAFKVEDVEATVAELKSLGIET---EPIRVDDfTGKKFTFFFDPDGLPLELYE 123
PRK10291 PRK10291
glyoxalase I; Provisional
11-129 2.36e-09

glyoxalase I; Provisional


Pssm-ID: 182358  Cd Length: 129  Bit Score: 51.56  E-value: 2.36e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447068012  11 LMVANLEASISFYEEVVGLQLLKRMGHPNPDLKLAFLGV-EESKETILELIEGYNSSLPAEGKVH-HICFKVDSLEDEIE 88
Cdd:PRK10291   2 LRVGDLQRSIDFYTNVLGMKLLRTSENPEYKYSLAFVGYgPETEEAVIELTYNWGVDKYELGTAYgHIALSVDNAAEACE 81
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 447068012  89 RIQKHGVTflLGEEIETLPDGTRYI-FFAGPDGEWIEFFETE 129
Cdd:PRK10291  82 KIRQNGGN--VTREAGPVKGGTTVIaFVEDPDGYKIELIEEK 121
BphC5-RrK37_N_like cd08362
N-terminal, non-catalytic, domain of BphC5 (2,3-dihydroxybiphenyl 1,2-dioxygenase) from ...
3-125 2.92e-09

N-terminal, non-catalytic, domain of BphC5 (2,3-dihydroxybiphenyl 1,2-dioxygenase) from Rhodococcus rhodochrous K37, and similar proteins; 2,3-dihydroxybiphenyl 1,2-dioxygenase (BphC) catalyzes the extradiol ring cleavage reaction of 2,3-dihydroxybiphenyl, the third step in the polychlorinated biphenyls (PCBs) degradation pathway (bph pathway). The enzyme contains a N-terminal and a C-terminal domain of similar structure fold, resulting from an ancient gene duplication. BphC belongs to the type I extradiol dioxygenase family, which requires a metal in the active site for its catalytic activity. Polychlorinated biphenyl degrading bacteria demonstrate multiplicity of BphCs. Bacterium Rhodococcus rhodochrous K37 has eight genes encoding BphC enzymes. This family includes the N-terminal domain of BphC5-RrK37. The crystal structure of the protein from Novosphingobium aromaticivorans has a Mn(II)in the active site, although most proteins of type I extradiol dioxygenases are activated by Fe(II).


Pssm-ID: 319950 [Multi-domain]  Cd Length: 120  Bit Score: 51.10  E-value: 2.92e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447068012   3 VRRIEHVGLMVANLEASISFYEEVVGLQLLkrmghpNPDLKLAFLGVEESKETILELIEGynsslpAEGKVHHICFKVDS 82
Cdd:cd08362    1 VTHLRYVALGVPDLAAEREFYTEVWGLEEV------AEDDDVVYLRAEGSEHHVLRLRQS------DENRLDLIAFAAAT 68
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 447068012  83 ---LEDEIERIQKHGVTFLLGE-EIETLPDGTRYIFFaGPDGEWIEF 125
Cdd:cd08362   69 radVDALAARLAAAGVRILSEPgPLDDPGGGYGFRFF-DPDGRTIEV 114
PLN03042 PLN03042
Lactoylglutathione lyase; Provisional
18-130 6.34e-09

Lactoylglutathione lyase; Provisional


Pssm-ID: 215548  Cd Length: 185  Bit Score: 51.36  E-value: 6.34e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447068012  18 ASISFYEEVVGLQLLKRMGHPNPDLKLAFLGVEESKE----------------TILELIEGYNS-SLPAEGKVH------ 74
Cdd:PLN03042  40 ASLDFYSRVLGMSLLKRLDFPEMKFSLYFLGYEDSETaptdppertvwtfgrkATIELTHNWGTeSDPEFKGYHngnsdp 119
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 447068012  75 ----HICFKVDSLEDEIERIQKHGVTFllgeeiETLPDGTRY---IFFAGPDGEWIEFFETER 130
Cdd:PLN03042 120 rgfgHIGITVDDVYKACERFEKLGVEF------VKKPDDGKMkglAFIKDPDGYWIEIFDLKR 176
PLN02367 PLN02367
lactoylglutathione lyase
17-130 6.61e-09

lactoylglutathione lyase


Pssm-ID: 177995  Cd Length: 233  Bit Score: 51.92  E-value: 6.61e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447068012  17 EASISFYEEVVGLQLLKRMGHPNPDLKLAFLGVEE----------------SKETILEL-----------IEGYNSSLPA 69
Cdd:PLN02367  87 KASLDFYSRVLGMSLLKRLDFPEMKFSLYFMGYEDtasaptdptertvwtfGQKATIELthnwgtesdpdFKGYHNGNSE 166
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 447068012  70 EGKVHHICFKVDSLEDEIERIQKHGVTFLLGEEietlpDGTR--YIFFAGPDGEWIEFFETER 130
Cdd:PLN02367 167 PRGFGHIGITVDDVYKACERFEELGVEFVKKPN-----DGKMkgIAFIKDPDGYWIEIFDLKT 224
VOC_like cd08353
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
3-127 1.32e-08

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: 319941  Cd Length: 142  Bit Score: 49.88  E-value: 1.32e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447068012   3 VRRIEHVGLMVANLEASISFYEEvVGLQLLKRM-----------GHPNPDLKLAFLGVEESkETILEL--------IEGY 63
Cdd:cd08353    1 IKRMDHVGIVVEDLDAAIAFFTE-LGLELEGRMtvegewadrvvGLDGVRVEIAMLRTPDG-HGRLELskfltpaaIPGH 78
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 447068012  64 NSSLPAEGKVHHICFKVDSLEDEIERIQKHGVTfLLGeEIETLPDGTRYIFFAGPDGEWIEFFE 127
Cdd:cd08353   79 RPAPANALGLRHVAFAVDDIDAVVARLRKHGAE-LVG-EVVQYEDSYRLCYVRGPEGIIVELAE 140
VOC_like cd07264
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
6-128 1.78e-08

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


Pssm-ID: 319925 [Multi-domain]  Cd Length: 118  Bit Score: 48.87  E-value: 1.78e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447068012   6 IEHVGLMVANLEASISFYEEVvgLQLLKRMGHPNP--------DLKLAFLGVEESKETILELIEGYNSSlpaegkvhhIC 77
Cdd:cd07264    1 IAYIVLYVDDFAASLRFYRDV--LGLPPRFLHEEGeyaefdtgETKLALFSRKEMARSGGPDRRGSAFE---------LG 69
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 447068012  78 FKVDSLEDEIERIQKHGVTFLlgEEIETLPDGTRYIFFAGPDGEWIEFFET 128
Cdd:cd07264   70 FEVDDVEATVEELVERGAEFV--REPANKPWGQTVAYVRDPDGNLIEICEP 118
VOC_BsCatE_like_N cd07255
N-terminal of Bacillus subtilis CatE like protein; Uncharacterized subfamily of VOC ...
5-126 1.14e-07

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: 46.92  E-value: 1.14e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447068012   5 RIEHVGLMVANLEASISFYEEVVGLQLLKRMGhpnpdlKLAFLGVEESKETI-LELIEGYNSSLPAEGKVHHICFKVDSL 83
Cdd:cd07255    2 RIGRVTLKVADLERQSAFYQNVIGLSVLKQNA------SRAYLGVDGKQVLLvLEAIPDAVLAPRSTTGLYHFAILLPDR 75
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 447068012  84 EDeIERIQKHgvtfLLGEEIETLPDGTRY---IFFAGPDGEWIEFF 126
Cdd:cd07255   76 KA-LGRALAH----LAEHGPLIGAADHGVseaIYLSDPEGNGIEIY 116
PRK11478 PRK11478
VOC family protein;
3-127 1.57e-07

VOC family protein;


Pssm-ID: 183156 [Multi-domain]  Cd Length: 129  Bit Score: 46.81  E-value: 1.57e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447068012   3 VRRIEHVGLMVANLEASISFYEEVVGLQLLKRMGHPNPDL---KLAFLGveeskETILELIE----GYNSSLPAEGKVHH 75
Cdd:PRK11478   4 LKQVHHIAIIATDYAVSKAFYCDILGFTLQSEVYREARDSwkgDLALNG-----QYVIELFSfpfpPERPSRPEACGLRH 78
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 447068012  76 ICFKVDSLEDEIERIQKHGVTFllgEEIETLP-DGTRYIFFAGPDGEWIEFFE 127
Cdd:PRK11478  79 LAFSVDDIDAAVAHLESHNVKC---EAIRVDPyTQKRFTFFNDPDGLPLELYE 128
GLOD5 cd07253
Human glyoxalase domain-containing protein 5 and similar proteins; Uncharacterized subfamily ...
3-124 2.78e-07

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: 46.07  E-value: 2.78e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447068012   3 VRRIEHVGLMVANLEASISFYEEVVGLQlLKRMGHPNPdlKLAFlgveesKETILELIE-GYN----SSLPAEGkVHHIC 77
Cdd:cd07253    1 IKRLDHLVLTVKDIERTIDFYTKVLGMT-VVTFKEGRK--ALRF------GNQKINLHQkGKEfepkASAPTPG-SADLC 70
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 447068012  78 FKVDSLEDE-IERIQKHGVTFLLGEEIETLPDGTRY-IFFAGPDGEWIE 124
Cdd:cd07253   71 FITETPIDEvLEHLEACGVTIEEGPVKRTGALGPILsIYFRDPDGNLIE 119
BphC-JF8_C_like cd09014
C-terminal, catalytic domain of BphC_JF8, (2,3-dihydroxybiphenyl 1,2-dioxygenase); 2, ...
1-130 4.57e-07

C-terminal, catalytic domain of BphC_JF8, (2,3-dihydroxybiphenyl 1,2-dioxygenase); 2,3-dihydroxybiphenyl 1,2-dioxygenase (BphC) catalyzes the extradiol ring cleavage reaction of 2,3-dihydroxybiphenyl, a key step in the polychlorinated biphenyls (PCBs) degradation pathway (bph pathway). BphC belongs to the type I extradiol dioxygenase family, which requires a metal ion in the active site in its catalytic mechanism. Polychlorinated biphenyl degrading bacteria demonstrate a multiplicity of BphCs. This subfamily of BphC is represented by the enzyme purified from the thermophilic biphenyl and naphthalene degrader, Bacillus sp. JF8. The members in this family of BphC enzymes may use either Mn(II) or Fe(II) as cofactors. The enzyme purified from Bacillus sp. JF8 is Mn(II)-dependent, however, the enzyme from Rhodococcus jostii RHAI has Fe(II) bound to it. BphC_JF8 is thermostable and its optimum activity is at 85 degrees C. The enzymes in this family have an internal duplication. This family represents the C-terminal repeat.


Pssm-ID: 319956  Cd Length: 167  Bit Score: 46.22  E-value: 4.57e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447068012   1 MPVRRIEHVGLMVANLEASISFYEEVVGLQLLKRMGHPNPDLKLAFLGVEESKETILELIEGynssLPAEGKVHHICFKV 80
Cdd:cd09014    2 IPVRRIDHLNLLASDVTANRQFMSDTLGFRLREQIRDNNGGEAGAWMSVSSLVHDVAVMRDG----KGEPGRLHHLAYWY 77
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 447068012  81 DSLED-----EIERIQ---------KHGVT--FLL------GEEIETLPDGTRYIFfaGPDGEWIEFFETER 130
Cdd:cd09014   78 GTPEDllraaDIFREHgiqieagpgKHGISqaFFLyvyepgGNRVELFGGAGYLIF--DPDWEPVEWTEEDL 147
VOC_like cd08354
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
10-125 9.87e-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: 319942  Cd Length: 122  Bit Score: 44.66  E-value: 9.87e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447068012  10 GLMVANLEASISFYEEVVGLQLLKRMGHP-----NPDLKLAFLGVEESKETILELIEGYNSSLPAegkvhHICFKVDSLE 84
Cdd:cd08354    5 CLYADDLDAAEAFYEDVLGLKPMLRSGRHaffrlGPQVLLVFDPGATSKDVRTGEVPGHGASGHG-----HFAFAVPTEE 79
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 447068012  85 -DEIE-RIQKHGVTFllgEEIETLPDGTRYIFFAGPDGEWIEF 125
Cdd:cd08354   80 lAAWEaRLEAKGVPI---ESYTQWPEGGKSLYFRDPAGNLVEL 119
Fosfomycin_RP cd08345
Fosfomycin resistant protein; This family contains three types of fosfomycin resistant protein. ...
8-125 1.48e-06

Fosfomycin resistant protein; This family contains three types of fosfomycin resistant protein. Fosfomycin inhibits the enzyme UDP-N-acetylglucosamine-3-enolpyruvyltransferase (MurA), which catalyzes the first committed step in bacterial cell wall biosynthesis. The three types of fosfomycin resistance proteins, employ different mechanisms to render fosfomycin [(1R,2S)-epoxypropylphosphonic acid] inactive. FosB catalyzes the addition of L-cysteine to the epoxide ring of fosfomycin. FosX catalyzes the addition of a water molecule to the C1 position of the antibiotic with inversion of configuration at C1. FosA catalyzes the addition of glutathione to the antibiotic fosfomycin, making it inactive. Catalytic activities of both FosX and FosA are Mn(II)-dependent, but FosB is activated by Mg(II). Fosfomycin resistant proteins are evolutionarily related to glyoxalase I and type I extradiol dioxygenases.


Pssm-ID: 319933  Cd Length: 118  Bit Score: 44.09  E-value: 1.48e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447068012   8 HVGLMVANLEASISFYEEVVGLQLLKRMGHPNPDL-KLAFLgveESKETILELIEGYNsslPAEGKVHHICFKVDS--LE 84
Cdd:cd08345    1 HITLIVRDLEKSTAFLQDIFGAREVYSSGDKTFSLsKEKFF---LLGGLWIALMEGES---LQERSYTHIAFQIQSedFD 74
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 447068012  85 DEIERIQKHGVTFLLGEEiETLPDGtRYIFFAGPDGEWIEF 125
Cdd:cd08345   75 RYAERLGALGVEMRPPRP-RVEGEG-RSIYFYDPDNHLFEL 113
ED_TypeI_classII_C cd08343
C-terminal domain of type I, class II extradiol dioxygenases, catalytic domain; This family ...
8-126 2.78e-06

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: 43.46  E-value: 2.78e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447068012   8 HVGLMVANLEASISFYEEVVGLQLLKRMGHPNPDLkLAFL-GVEESKETILELIEGynsslpAEGKVHHICFKVDSLEDE 86
Cdd:cd08343    2 HVVLCSPDVEASRDFYTDVLGFRVSDRIVDPGVDG-GAFLhCDRGTDHHTVALAGG------PHPGLHHVAFEVHDLDDV 74
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 447068012  87 IERIQKHGVtflLGEEIET-----LPDGTRYIFFAGPDGEWIEFF 126
Cdd:cd08343   75 GRGHDRLRE---KGYKIEWgpgrhGLGSQVFDYWFDPSGNRVEYY 116
PLN02300 PLN02300
lactoylglutathione lyase
9-63 3.82e-06

lactoylglutathione lyase


Pssm-ID: 215169 [Multi-domain]  Cd Length: 286  Bit Score: 44.39  E-value: 3.82e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 447068012   9 VGLMVANLEASISFYEEVVGLQLLKRMGHPNPDLKLAFLGV-EESKETILELIEGY 63
Cdd:PLN02300 158 VMLRVGDLDRSIKFYEKAFGMKLLRKRDNPEYKYTIAMMGYgPEDKTTVLELTYNY 213
VOC_like cd07254
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
8-128 3.92e-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: 319917 [Multi-domain]  Cd Length: 120  Bit Score: 42.83  E-value: 3.92e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447068012   8 HVGLMVANLEASISFYEEVVGLQLLKRMGH------PNPDLKLAFLGVEEsketileliegynsslPAEGKVHHICFKVD 81
Cdd:cd07254    4 HLSLNVTDLERSIRFYSDLFGAEPAKRKADyakfmlEDPPLNLALLVNDR----------------KEPYGLNHLGIQVD 67
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 447068012  82 SLE---DEIERIQKHGVTFLlgEEIETLPDGTRY--IFFAGPDGEWIEFFET 128
Cdd:cd07254   68 SKEevaALKARAEAAGLPVR--KEPRTTCCYAVQdkFWLTDPDGNAWEFYAT 117
ED_TypeI_classII_N cd16360
N-terminal domain of type I, class II extradiol dioxygenases; This family contains the ...
8-126 1.31e-05

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: 41.15  E-value: 1.31e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447068012   8 HVGLMVANLEASISFYEEVVGLQLLKRmghpnpDLKLAFLGVEESKETILELIEGYNSSLpaegkvHHICFKVDSlEDEI 87
Cdd:cd16360    1 YAELGVPDLEKALEFYTDVLGLQVAKR------DGNSVYLRGYEDEHHSLVLYEAPEAGL------KHFAFEVAS-EEDL 67
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 447068012  88 ERIQKH----GVTFLLGEEIETLPDGTRYIFFAgPDGEWIEFF 126
Cdd:cd16360   68 ERAAASltalGCDVTWGPDGEVPGGGKGFRFQD-PSGHLLELF 109
PRK04101 PRK04101
metallothiol transferase FosB;
6-125 3.16e-05

metallothiol transferase FosB;


Pssm-ID: 179740  Cd Length: 139  Bit Score: 40.70  E-value: 3.16e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447068012   6 IEHVGLMVANLEASISFYEEVVGLQLLKRmGHpnpdlKLAF-------LGVEESKEtIL--ELIEGYNsslpaegkvhHI 76
Cdd:PRK04101   5 INHICFSVSNLEKSIEFYEKVLGAKLLVK-GR-----KTAYfdlnglwIALNEEKD-IPrnEIHQSYT----------HI 67
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 447068012  77 CFKVD--SLEDEIERIQKHGVTFLLGEEiETLPDGtRYIFFAGPDGEWIEF 125
Cdd:PRK04101  68 AFSIEeeDFDHWYQRLKENDVNILPGRE-RDERDK-KSIYFTDPDGHKFEF 116
VOC_like cd09011
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
11-128 5.08e-05

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


Pssm-ID: 319953  Cd Length: 122  Bit Score: 40.15  E-value: 5.08e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447068012  11 LMVANLEASISFYEEVVGLQLLKRMGHpNPDLKLAFlGVEESKeTILELIEGYNSSLPAEGKVHHICFKVDSLEDEIERI 90
Cdd:cd09011    8 LVVKDIEKSKKFYEDVLGQKILLDFGE-NVVFEGGF-ALQEKK-SWLETIIISDLSIKQQSNNFELYFEVDDFDAFFEKL 84
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 447068012  91 QKHGVTFLLgEEIETLPDGTRYIFFAGPDGEWIEFFET 128
Cdd:cd09011   85 NPHKDIEFI-HPILEHPWGQRVFRFYDPDGHIIEIGES 121
Glyoxalase_3 pfam13468
Glyoxalase-like domain; This domain is related to the Glyoxalase domain pfam00903.
6-122 6.65e-05

Glyoxalase-like domain; This domain is related to the Glyoxalase domain pfam00903.


Pssm-ID: 433233  Cd Length: 175  Bit Score: 40.40  E-value: 6.65e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447068012    6 IEHVGLMVANLEASISFYEEVVGLQLLKRMGHPN----------PDLKLAFLGVEESKETILELIEGYNSSLPAEGKVHH 75
Cdd:pfam13468   1 LDHVVLAVPDLDEAAARFARALGFTVTPGGRHPGmgtanalimfGDGYLELLAVDPEAPAPPRGRWFGLDRLADGEGLLG 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 447068012   76 ICFKVDSLEDEIERIQKHGVTFllGEEIEtlPDGT----RYIFFAGPDGEW 122
Cdd:pfam13468  81 WALRTDDIDAVAARLRAAGVEP--GRRVR--PDGGdlrwRLLFLADGALPA 127
PLN02300 PLN02300
lactoylglutathione lyase
4-63 7.77e-05

lactoylglutathione lyase


Pssm-ID: 215169 [Multi-domain]  Cd Length: 286  Bit Score: 40.53  E-value: 7.77e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 447068012   4 RRIEHVGLMVANLEASISFYEEVVGLQLLKRMGHPNPDLKLAFLGV-EESKETILELIEGY 63
Cdd:PLN02300  23 RRMLHVVYRVGDLDRTIKFYTECLGMKLLRKRDIPEEKYTNAFLGYgPEDSNFVVELTYNY 83
2_3_CTD_N cd07265
N-terminal domain of catechol 2,3-dioxygenase; This subfamily contains the N-terminal, ...
3-126 2.02e-04

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: 38.48  E-value: 2.02e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447068012   3 VRRIEHVGLMVANLEASISFYEEVVGLQLLKRMGHPNPDLKlaflGVEESKETILELIEGYNSSLpaegkvHHICFKV-- 80
Cdd:cd07265    2 VLRPGHVQLRVLDLEEAIKHYREVLGLVETGRDDQGRVYLK----AWDEYDHHSIILREADTAGL------DFMGFKVld 71
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 447068012  81 -DSLEDEIERIQKHGVTfllgeeIETLPDGT-----RYIFFAGPDGEWIEFF 126
Cdd:cd07265   72 dADLEQLEARLQAYGVT------VTRIPAGElpgvgRRVRFQLPSGHTMELY 117
BphC5-RK37_C_like cd07239
C-terminal, catalytic domain of BphC5 (2,3-dihydroxybiphenyl 1,2-dioxygenase); 2, ...
1-125 2.23e-04

C-terminal, catalytic domain of BphC5 (2,3-dihydroxybiphenyl 1,2-dioxygenase); 2,3-dihydroxybiphenyl 1,2-dioxygenase (BphC) catalyzes the extradiol ring cleavage reaction of 2,3-dihydroxybiphenyl, the third step in the polychlorinated biphenyls (PCBs) degradation pathway (bph pathway). The enzyme contains a N-terminal and a C-terminal domain of similar structure fold, resulting from an ancient gene duplication. BphC belongs to the type I extradiol dioxygenase family, which requires a metal in the active site for its catalytic activity. Polychlorinated biphenyl degrading bacteria demonstrate multiplicity of BphCs. Bacterium Rhodococcus rhodochrous K37 has eight genes encoding BphC enzymes. This family includes the C-terminal domain of BphC5-RrK37. The crystal structure of the protein from Novosphingobium aromaticivorans has a Mn(II)in the active site, although most proteins of type I extradiol dioxygenases are activated by Fe(II).


Pssm-ID: 319904  Cd Length: 143  Bit Score: 38.72  E-value: 2.23e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447068012   1 MPVRrIEHVGLMVANLEASISFYEEVVGLQLLKRMGHpnpdlKLAFLGVEESKETIlELIEGYNSSLpaegkvHHICFKV 80
Cdd:cd07239    1 VPVK-LSHVVLNSPDLDKTVAFYEDVLGFRVSDWLGD-----VMHFLRCNSQHHSI-AIARGPHTSL------NHVAYEM 67
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 447068012  81 DSLEDE---IERIQKHGVTFLLGEEIETLPDGTrYIFFAGPDGEWIEF 125
Cdd:cd07239   68 RSVDEYmrgSGRLIRSGARKIWGPGRHMAGDNT-FSYFLDPHGNVVEY 114
BphC1-RGP6_C_like cd07237
C-terminal domain of 2,3-dihydroxybiphenyl 1,2-dioxygenase; This subfamily contains the ...
8-95 3.03e-04

C-terminal domain of 2,3-dihydroxybiphenyl 1,2-dioxygenase; This subfamily contains the C-terminal, catalytic, domain of BphC1-RGP6 and similar proteins. BphC catalyzes the extradiol ring cleavage reaction of 2,3-dihydroxybiphenyl, 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. 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. BphC1-RGP6 has an internal duplication, it is a two-domain dioxygenase which forms octamers, and has Fe(II) at the catalytic site. Its C-terminal repeat is represented in this subfamily. BphC2-RGP6 and BphC3-RGP6 are one-domain dioxygenases, they belong to a different subfamily of the ED_TypeI_classII_C (C-terminal domain of type I, class II extradiol dioxygenases) family.


Pssm-ID: 319902  Cd Length: 153  Bit Score: 38.41  E-value: 3.03e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447068012   8 HVGLMVANLEASISFYEEVVGLQL---LKRMGHPNPDLKLAFLGVEESKETiLELIEGynsslPAEGKVHHICFKVDSLE 84
Cdd:cd07237   12 HVVLIVPDVDEALAFYTDVLGFRLsdeIRIPLPPGVTARLHFLHCNGRHHS-LAFGAG-----PGPKRLHHLMLEVTSLD 85
                         90
                 ....*....|....
gi 447068012  85 D---EIERIQKHGV 95
Cdd:cd07237   86 DvgrAYDRVRKRGI 99
PcpA_N_like cd08346
N-terminal domain of Sphingobium chlorophenolicum 2,6-dichloro-p-hydroquinone 1,2-dioxygenase ...
6-120 3.29e-04

N-terminal domain of Sphingobium chlorophenolicum 2,6-dichloro-p-hydroquinone 1,2-dioxygenase (PcpA), and similar proteins; The N-terminal domain of Sphingobium chlorophenolicum (formerly Sphingomonas chlorophenolica) 2,6-dichloro-p-hydroquinone1,2-dioxygenase (PcpA), and similar proteins. PcpA is a key enzyme in the pentachlorophenol (PCP) degradation pathway, catalyzing the conversion of 2,6-dichloro-p-hydroquinone to 2-chloromaleylacetate. This domain belongs to a conserved domain superfamily that is found in a variety of structurally related metalloproteins, including the bleomycin resistance protein, glyoxalase I, and type I ring-cleaving dioxygenases.


Pssm-ID: 319934  Cd Length: 124  Bit Score: 37.65  E-value: 3.29e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447068012   6 IEHVGLMVANLEASISFYEEVVGLQLLKR-MGHPNPDLKLAFLGVEE-SKETILEL--IEGYNSSLPAEGKVHHICFKV- 80
Cdd:cd08346    2 IHHITAITGDAQENVDFYVKVLGLRLVKKtVNQDDPPMYHLYYGDELgSPGTLLTFfpWPLGGPGRRGTGQISRIGLRVp 81
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 447068012  81 -DSLEDEIERIQKHGVTFllgEEIETlPDGTRYIFFAGPDG 120
Cdd:cd08346   82 kGSLSFWAERLEKFGVPH---SEVVT-RFGEKYLRFEDPDG 118
ChaP_like cd08351
ChaP, an enzyme involved in the biosynthesis of the antitumor agent chartreusin (cha), and ...
17-126 5.02e-04

ChaP, an enzyme involved in the biosynthesis of the antitumor agent chartreusin (cha), and similar proteins; ChaP is an enzyme involved in the biosynthesis of the potent antitumor agent chartreusin (cha). Cha is an aromatic polyketide glycoside produced by Streptomyces chartreusis. ChaP may play a role as a meta-cleavage dioxygenase in the oxidative rearrangement of the anthracyclic polyketide. ChaP belongs to a conserved domain superfamily that is found in a variety of structurally related metalloproteins, including the bleomycin resistance protein, glyoxalase I, and type I ring-cleaving dioxygenases.


Pssm-ID: 319939  Cd Length: 118  Bit Score: 37.10  E-value: 5.02e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447068012  17 EASISFYEEVVGLQLLKRMGHpnpdlklaFLGVEESKETILELIEgynsslpAEGKV--HHICFKVDSLE-DEI-ERIQK 92
Cdd:cd08351   14 EASARFLAEILGLPAPPPWGP--------FAPVRLNNGLTLDFAD-------PRGEIapQHYAFLVSDDEfDAIlARIRA 78
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 447068012  93 HGVTF------LLGEEIETLpDGTRYIFFAGPDGEWIEFF 126
Cdd:cd08351   79 RGLEYwadpqhREPGEINHN-DGGRGVYFRDPDGHLLEIL 117
VOC_like cd08359
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
9-124 8.68e-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: 319947 [Multi-domain]  Cd Length: 119  Bit Score: 36.61  E-value: 8.68e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447068012   9 VGLMVANLEASISFYEEVVGLQLLKRMGHpnpdlkLAFLGVEESKETILELIEGYNSSLPAEGKVHH----ICFKVDSLE 84
Cdd:cd08359    5 PVIVTEDVAATAAFYVKHFGFRVIFDSDW------YVSLRRAERHGFELAIMDGQHGAVPAASQTQSsgliINFEVDDAD 78
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 447068012  85 DEIERIQKHGVTFLlgEEIETLPDGTRYIFFAGPDGEWIE 124
Cdd:cd08359   79 AEYERLTQAGLEFL--EPPRDEPWGQRRFIVRDPNGVLID 116
PcpA_C_like cd08347
C-terminal domain of Sphingobium chlorophenolicum 2,6-dichloro-p-hydroquinone 1,2-dioxygenase ...
9-94 8.83e-04

C-terminal domain of Sphingobium chlorophenolicum 2,6-dichloro-p-hydroquinone 1,2-dioxygenase (PcpA), and similar proteins; The C-terminal domain of Sphingobium chlorophenolicum (formerly Sphingomonas chlorophenolica) 2,6-dichloro-p-hydroquinone 1,2-dioxygenase (PcpA), and similar proteins. PcpA is a key enzyme in the pentachlorophenol (PCP) degradation pathway, catalyzing the conversion of 2,6-dichloro-p-hydroquinone to 2-chloromaleylacetate. This domain belongs to a conserved domain superfamily that is found in a variety of structurally related metalloproteins, including the bleomycin resistance protein, glyoxalase I, and type I ring-cleaving dioxygenases.


Pssm-ID: 319935  Cd Length: 157  Bit Score: 36.84  E-value: 8.83e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447068012   9 VGLMVANLEASISFYEEVVGLqllKRMGHPNPDLKLAFLGVEESKETILELIEGYNSSLPAEGKVHHICFKVDSLEDE-- 86
Cdd:cd08347    5 VTLTVREPEETDAFLTNVFGF---TEVGEEGDLVRLFAGGNGSGGVVDVLDDPDLPSAQQGYGTVHHVAFRVADDEEQaa 81

                 ....*....
gi 447068012  87 -IERIQKHG 94
Cdd:cd08347   82 wKERLEELG 90
FosA cd07244
fosfomycin resistant protein subfamily FosA; This subfamily family contains FosA, a fosfomycin ...
6-34 1.02e-03

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: 36.49  E-value: 1.02e-03
                         10        20
                 ....*....|....*....|....*....
gi 447068012   6 IEHVGLMVANLEASISFYEEVVGLQLLKR 34
Cdd:cd07244    2 INHITLAVSDLERSLAFYVDLLGFKPHVR 30
VOC_BsYyaH cd07241
vicinal oxygen chelate (VOC) family protein similar to Bacillus subtilis YyaH; The vicinal ...
5-124 1.56e-03

vicinal oxygen chelate (VOC) family protein similar to Bacillus subtilis YyaH; 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: 319905  Cd Length: 125  Bit Score: 35.85  E-value: 1.56e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447068012   5 RIEHVGLMVANLEASISFYEEVVGLQLLKRMGHPNPDLKLAFLGVEESKEtiLELIEGYN-SSLPAEGKVH---HICFKV 80
Cdd:cd07241    1 KIEHVALWTNDLERMKDFYVKYFGAESNDIYHNKKKGFRSYFLTFDSGAR--LELMSRPDvTDPDKEVERTglaHIAFSV 78
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 447068012  81 DSLE--DEI-ERIQKHGvtFLLGEEIETLPDGTRYIFFAGPDGEWIE 124
Cdd:cd07241   79 GSKEavDELtERLRADG--YAVVGGPRTTGDGYYESVILDPEGNRIE 123
2_3_CTD_C cd07243
C-terminal domain of catechol 2,3-dioxygenase; This subfamily contains the C-terminal, ...
5-117 2.76e-03

C-terminal domain of catechol 2,3-dioxygenase; This subfamily contains the C-terminal, 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 C-terminal domain.


Pssm-ID: 319907  Cd Length: 144  Bit Score: 35.46  E-value: 2.76e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447068012   5 RIEHVGLMVANLEASISFYEEVVGLQLLKRMGHPNPDLKLAFLGVEESKETILELIEGynsslPAEGKVHHICFKVDSLE 84
Cdd:cd07243    6 RLDHCLLYGERIAETTRFFTDVLGFYLTERVLDPDGGTRVGIFLSCSNKAHDIAFVGY-----PEDGKLHHTSFFLESWE 80
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 447068012  85 D-------------EIE-RIQKHGVTflLGEEIETL-PDGTRYIFFAG 117
Cdd:cd07243   81 DvlkagdiiskndvSIDiGPTRHGIT--RGQTIYFFdPSGNRNETFAG 126
HPCD_N_class_II cd07266
N-terminal domain of 3,4-dihydroxyphenylacetate 2,3-dioxygenase (HPCD); This subfamily ...
5-130 3.65e-03

N-terminal domain of 3,4-dihydroxyphenylacetate 2,3-dioxygenase (HPCD); This subfamily contains the N-terminal, non-catalytic, domain of HPCD. HPCD catalyses the second step in the degradation of 4-hydroxyphenylacetate to succinate and pyruvate. The aromatic ring of 4-hydroxyphenylacetate is opened by this dioxygenase to yield the 3,4-diol product, 2-hydroxy-5-carboxymethylmuconate semialdehyde. HPCD is a homotetramer and each monomer contains two structurally homologous barrel-shaped domains at the N- and C-terminus. The active-site metal is located in the C-terminal barrel and plays an essential role in the catalytic mechanism. Most extradiol dioxygenases contain Fe(II) in their active site, but HPCD can be activated by either Mn(II) or Fe(II). These enzymes belong to the type I class II family of extradiol dioxygenases. The class III 3,4-dihydroxyphenylacetate 2,3-dioxygenases belong to a different superfamily.


Pssm-ID: 319927  Cd Length: 118  Bit Score: 34.69  E-value: 3.65e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447068012   5 RIEHVGLMVANLEASISFYEEVVGLQLLkrmghpNPDLKLAFL-GVEESKETILELIEGynsslpAEGKVHHICFKVDSL 83
Cdd:cd07266    4 RLAHAELVVTDLAASREFYVDTLGLHVT------DEDDNAIYLrGVEEFIHHTLVLRKA------PEAAVGHLGFRVRDE 71
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 447068012  84 EDeIERIQKHGVTFLLGEEIETLPDGTRYIFFAGPDGEWIEFF-ETER 130
Cdd:cd07266   72 AD-LDKAAAFYKELGLPTEWREEPGQGRTLRVEDPFGFPIEFYlEMDH 118
PpCmtC_C cd07258
C-terminal domain of 2,3-dihydroxy-p-cumate-3,4-dioxygenase (PpCmtC); This subfamily contains ...
8-125 5.24e-03

C-terminal domain of 2,3-dihydroxy-p-cumate-3,4-dioxygenase (PpCmtC); This subfamily contains the C-terminal, catalytic, domain of PpCmtC. 2,3-dihydroxy-p-cumate-3,4-dioxygenase (CmtC of Pseudomonas putida F1) is a dioxygenase involved in the eight-step catabolism pathway of p-cymene. CmtC acts upon the reaction intermediate 2,3-dihydroxy-p-cumate, yielding 2-hydroxy-3-carboxy-6-oxo-7-methylocta-2,4-dienoate. The CmtC belongs to the type I family of extradiol dioxygenases. Fe2+ was suggested as a cofactor, same as for other enzymes in the family. The type I family of extradiol dioxygenases contains two structurally homologous barrel-shaped domains at the N- and C-terminal. The active-site metal is located in the C-terminal barrel and plays an essential role in the catalytic mechanism.


Pssm-ID: 319921  Cd Length: 138  Bit Score: 34.87  E-value: 5.24e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447068012   8 HVGLMVANLEASISFYEEVVGLQLLKRMGhpnpdlKLAFLGVEESKETIleliegynSSLPAEGK-VHHICFKVDSLEDE 86
Cdd:cd07258    2 HVGLNSTNPERDEDFWTDVCNARVSDRIG------DIFLMRVNAIHHTF--------ALGPASSSgIQHINHQVTSIDDV 67
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 447068012  87 IE---RIQKHGVTFLLGEEIETlPDGTRYIFFAGPDGEWIEF 125
Cdd:cd07258   68 LRsyyRLKEHDVPIVFGPGRHP-TSGARFLYFKGPDGMTFEY 108
MhqB_like_C cd08360
C-terminal domain of Burkholderia sp. NF100 MhqB and similar proteins; This subfamily contains ...
4-89 5.69e-03

C-terminal domain of Burkholderia sp. NF100 MhqB and similar proteins; This subfamily contains the C-terminal, catalytic, domain of Burkholderia sp. NF100 MhqB and similar proteins. MhqB is a type I extradiol dioxygenase involved in the catabolism of methylhydroquinone, an intermediate in the degradation of fenitrothion. The purified enzyme has shown extradiol ring cleavage activity toward 3-methylcatechol. Fe2+ was suggested as a cofactor, the same as most other enzymes in the family. Burkholderia sp. NF100 MhqB is encoded on the plasmid pNF1. The type I family of extradiol dioxygenases contains two structurally homologous barrel-shaped domains at the N- and C-terminal. The active-site metal is located in the C-terminal barrel and plays an essential role in the catalytic mechanism.


Pssm-ID: 319948  Cd Length: 134  Bit Score: 34.41  E-value: 5.69e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447068012   4 RRIEHVGLMVANLEASISFYEEVVGLQLLKRMGHpnpdlKLAFL-GVEESKETILELIegyNSSLPAegkVHHICFKVDS 82
Cdd:cd08360    2 RRLGHVLLFSPDVDRSVDFYRDLLGLKVSDRSFD-----IIAFMrGAAGSDHHLIAFA---KSSATG---LHHMSWDVSD 70

                 ....*..
gi 447068012  83 LeDEIER 89
Cdd:cd08360   71 V-NEIGI 76
Glyoxalase_2 pfam12681
Glyoxalase-like domain; This domain is related to the Glyoxalase domain pfam00903.
11-128 7.39e-03

Glyoxalase-like domain; This domain is related to the Glyoxalase domain pfam00903.


Pssm-ID: 403776  Cd Length: 118  Bit Score: 33.92  E-value: 7.39e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447068012   11 LMVANLEASISFYEEVVGLQLLKRMGHpnpdlKLAFLGVEESKETILELIeGYNSSLPAEGKVHHICFKVDSLEDEIERI 90
Cdd:pfam12681   6 LVVKDINISRKFYEDVLDQKIKLDFGE-----NVSFEGGFAIQSDFKELI-GIDLSIAEQSNNFELYFEVADVDAFLQKI 79
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 447068012   91 QKHGVTFLLgEEIETLPDGTRYIFFAGPDGEWIEFFET 128
Cdd:pfam12681  80 KEIGNIEYL-HELKEQPWGQRVFRFYDPDGHIIEIGES 116
 
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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