methylmalonyl-CoA epimerase, mitochondrial isoform 1 precursor [Mus musculus]
methylmalonyl-CoA epimerase( domain architecture ID 10798993)
methylmalonyl-CoA epimerase is a vicinal oxygen chelate (VOC) family protein that catalyzes the interconversion of (2R)-methylmalonyl-CoA and (2S)-methylmalonyl-CoA
List of domain hits
Name | Accession | Description | Interval | E-value | |||
metmalonyl_epim | TIGR03081 | methylmalonyl-CoA epimerase; Members of this protein family are the enzyme methylmalonyl-CoA ... |
49-177 | 1.96e-75 | |||
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: 221.81 E-value: 1.96e-75
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Name | Accession | Description | Interval | E-value | |||
metmalonyl_epim | TIGR03081 | methylmalonyl-CoA epimerase; Members of this protein family are the enzyme methylmalonyl-CoA ... |
49-177 | 1.96e-75 | |||
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: 221.81 E-value: 1.96e-75
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MMCE | cd07249 | Methylmalonyl-CoA epimerase (MMCE); MMCE, also called methylmalonyl-CoA racemase (EC 5.1.99.1) ... |
50-177 | 2.48e-65 | |||
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: 196.26 E-value: 2.48e-65
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HppD | COG3185 | 4-hydroxyphenylpyruvate dioxygenase and related hemolysins [Amino acid transport and ... |
46-175 | 1.91e-33 | |||
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: 120.77 E-value: 1.91e-33
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Glyoxalase_4 | pfam13669 | Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily; |
51-162 | 4.54e-21 | |||
Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily; Pssm-ID: 463951 [Multi-domain] Cd Length: 109 Bit Score: 83.10 E-value: 4.54e-21
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PRK04101 | PRK04101 | metallothiol transferase FosB; |
46-74 | 4.30e-03 | |||
metallothiol transferase FosB; Pssm-ID: 179740 Cd Length: 139 Bit Score: 35.69 E-value: 4.30e-03
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Name | Accession | Description | Interval | E-value | |||
metmalonyl_epim | TIGR03081 | methylmalonyl-CoA epimerase; Members of this protein family are the enzyme methylmalonyl-CoA ... |
49-177 | 1.96e-75 | |||
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: 221.81 E-value: 1.96e-75
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MMCE | cd07249 | Methylmalonyl-CoA epimerase (MMCE); MMCE, also called methylmalonyl-CoA racemase (EC 5.1.99.1) ... |
50-177 | 2.48e-65 | |||
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: 196.26 E-value: 2.48e-65
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HppD | COG3185 | 4-hydroxyphenylpyruvate dioxygenase and related hemolysins [Amino acid transport and ... |
46-175 | 1.91e-33 | |||
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: 120.77 E-value: 1.91e-33
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GloA | COG0346 | Catechol 2,3-dioxygenase or related enzyme, vicinal oxygen chelate (VOC) family [Secondary ... |
49-175 | 1.04e-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: 97.76 E-value: 1.04e-26
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Glyoxalase_4 | pfam13669 | Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily; |
51-162 | 4.54e-21 | |||
Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily; Pssm-ID: 463951 [Multi-domain] Cd Length: 109 Bit Score: 83.10 E-value: 4.54e-21
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Glyoxalase | pfam00903 | Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily; |
49-175 | 1.17e-18 | |||
Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily; Pssm-ID: 395724 [Multi-domain] Cd Length: 121 Bit Score: 77.10 E-value: 1.17e-18
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VOC | cd06587 | vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate (VOC) superfamily is composed ... |
52-175 | 2.67e-13 | |||
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: 62.93 E-value: 2.67e-13
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VOC_like | cd07245 | uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ... |
50-175 | 9.89e-11 | |||
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: 56.17 E-value: 9.89e-11
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VOC | COG3324 | Lactoylglutathione lyase-related enzyme, vicinal oxygen chelate (VOC) family [General function ... |
48-175 | 1.90e-09 | |||
Lactoylglutathione lyase-related enzyme, vicinal oxygen chelate (VOC) family [General function prediction only]; Pssm-ID: 442553 [Multi-domain] Cd Length: 119 Bit Score: 52.72 E-value: 1.90e-09
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CatE | COG2514 | Catechol-2,3-dioxygenase [Secondary metabolites biosynthesis, transport and catabolism]; |
49-134 | 2.77e-09 | |||
Catechol-2,3-dioxygenase [Secondary metabolites biosynthesis, transport and catabolism]; Pssm-ID: 442004 [Multi-domain] Cd Length: 141 Bit Score: 53.04 E-value: 2.77e-09
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VOC_ShValD_like | cd16361 | vicinal oxygen chelate (VOC) family protein similar to Streptomyces hygroscopicus ValD protein; ... |
49-136 | 1.66e-08 | |||
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: 51.18 E-value: 1.66e-08
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GlxI_Ni | cd16358 | Glyoxalase I that uses Ni(++) as cofactor; This family includes Escherichia coil and other ... |
52-175 | 1.19e-07 | |||
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: 48.16 E-value: 1.19e-07
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ED_TypeI_classII_C | cd08343 | C-terminal domain of type I, class II extradiol dioxygenases, catalytic domain; This family ... |
52-175 | 1.23e-07 | |||
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: 48.08 E-value: 1.23e-07
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VOC_Bs_YwkD_like | cd08352 | vicinal oxygen chelate (VOC) family protein Bacillus subtilis YwkD and similar proteins; ... |
49-145 | 1.30e-07 | |||
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: 47.92 E-value: 1.30e-07
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GLOD5 | cd07253 | Human glyoxalase domain-containing protein 5 and similar proteins; Uncharacterized subfamily ... |
49-176 | 1.91e-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: 47.61 E-value: 1.91e-07
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VOC_like | cd07264 | uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ... |
52-178 | 2.06e-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: 319925 [Multi-domain] Cd Length: 118 Bit Score: 44.63 E-value: 2.06e-06
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Glyoxalase_3 | pfam13468 | Glyoxalase-like domain; This domain is related to the Glyoxalase domain pfam00903. |
50-141 | 3.99e-06 | |||
Glyoxalase-like domain; This domain is related to the Glyoxalase domain pfam00903. Pssm-ID: 433233 Cd Length: 175 Bit Score: 45.02 E-value: 3.99e-06
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VOC_like | cd08353 | uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ... |
49-142 | 5.30e-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: 319941 Cd Length: 142 Bit Score: 44.10 E-value: 5.30e-06
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MhqB_like_C | cd08360 | C-terminal domain of Burkholderia sp. NF100 MhqB and similar proteins; This subfamily contains ... |
49-132 | 1.58e-05 | |||
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: 42.50 E-value: 1.58e-05
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BphC1-RGP6_C_like | cd07237 | C-terminal domain of 2,3-dihydroxybiphenyl 1,2-dioxygenase; This subfamily contains the ... |
50-132 | 2.59e-05 | |||
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: 42.26 E-value: 2.59e-05
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HPPD_C_like | cd07250 | C-terminal domain of 4-hydroxyphenylpyruvate dioxygenase (HppD) and hydroxymandelate synthase ... |
47-141 | 4.69e-05 | |||
C-terminal domain of 4-hydroxyphenylpyruvate dioxygenase (HppD) and hydroxymandelate synthase (HmaS); HppD and HmaS are non-heme iron-dependent dioxygenases, which modify a common substrate, 4-hydroxyphenylpyruvate (HPP), but yield different products. HPPD catalyzes the second reaction in tyrosine catabolism, the conversion of 4-hydroxyphenylpyruvate to homogentisate (2,5-dihydroxyphenylacetic acid, HG). HmaS converts HPP to 4-hydroxymandelate, a committed step in the formation of hydroxyphenylglycerine, a structural component of nonproteinogenic macrocyclic peptide antibiotics, such as vancomycin. If the emphasis is on catalytic chemistry, HPPD and HmaS are classified as members of a large family of alpha-keto acid dependent mononuclear non-heme iron oxygenases most of which require Fe(II), molecular oxygen, and an alpha-keto acid (typically alpha-ketoglutarate) to either oxygenate or oxidize a third substrate. Both enzymes are exceptions in that they require two, instead of three, substrates, do not use alpha-ketoglutarate, and incorporate both atoms of dioxygen into the aromatic product. Both HPPD and HmaS exhibit duplicate beta barrel topology in their N- and C-terminal domains which share sequence similarity, suggestive of a gene duplication. Each protein has only one catalytic site located in at the C-terminal domain. This HPPD_C_like domain represents the C-terminal domain. Pssm-ID: 319913 Cd Length: 194 Bit Score: 42.16 E-value: 4.69e-05
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PhnB | COG2764 | Zn-dependent glyoxalase, PhnB family [Energy production and conversion]; |
55-135 | 6.01e-05 | |||
Zn-dependent glyoxalase, PhnB family [Energy production and conversion]; Pssm-ID: 442048 [Multi-domain] Cd Length: 118 Bit Score: 40.61 E-value: 6.01e-05
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VOC_like | cd08354 | uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ... |
54-175 | 2.03e-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: 319942 Cd Length: 122 Bit Score: 39.27 E-value: 2.03e-04
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VOC_like | cd07263 | uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ... |
52-142 | 3.16e-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: 319924 [Multi-domain] Cd Length: 120 Bit Score: 38.82 E-value: 3.16e-04
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GlxI_Zn | cd07233 | Glyoxalase I that uses Zn(++) as cofactor; This family includes eukaryotic glyoxalase I that ... |
50-135 | 3.84e-04 | |||
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: 38.85 E-value: 3.84e-04
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VOC_like | cd07246 | uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ... |
55-136 | 4.31e-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: 319910 [Multi-domain] Cd Length: 124 Bit Score: 38.43 E-value: 4.31e-04
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FosA | cd07244 | fosfomycin resistant protein subfamily FosA; This subfamily family contains FosA, a fosfomycin ... |
50-72 | 5.29e-04 | |||
fosfomycin resistant protein subfamily FosA; This subfamily family contains FosA, a fosfomycin resistant protein. FosA is a Mn(II) and K(+)-dependent glutathione transferase. Fosfomycin inhibits the enzyme UDP-N-acetylglucosamine-3-enolpyruvyltransferase (MurA), which catalyzes the first committed step in bacterial cell wall biosynthesis. FosA, catalyzes the addition of glutathione to the antibiotic fosfomycin, (1R,2S)-epoxypropylphosphonic acid, making it inactive. FosA is a Mn(II) dependent enzyme. It is evolutionarily related to glyoxalase I and type I extradiol dioxygenases. Pssm-ID: 319908 [Multi-domain] Cd Length: 121 Bit Score: 38.03 E-value: 5.29e-04
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ED_TypeI_classII_N | cd16360 | N-terminal domain of type I, class II extradiol dioxygenases; This family contains the ... |
52-76 | 8.19e-04 | |||
N-terminal domain of type I, class II extradiol dioxygenases; This family contains the N-terminal non-catalytic domain of type I, class II extradiol dioxygenases. Dioxygenases catalyze the incorporation of both atoms of molecular oxygen into substrates using a variety of reaction mechanisms, resulting in the cleavage of aromatic rings. Two major groups of dioxygenases have been identified according to the cleavage site; extradiol enzymes cleave the aromatic ring between a hydroxylated carbon and an adjacent non-hydroxylated carbon, whereas intradiol enzymes cleave the aromatic ring between two hydroxyl groups. Extradiol dioxygenases are classified into type I and type II enzymes. Type I extradiol dioxygenases include class I and class II enzymes. These two classes of enzymes show sequence similarity; the two-domain class II enzymes evolved from a class I enzyme through gene duplication. The extradiol dioxygenases represented in this family are type I, class II enzymes, and are composed of the N- and C-terminal domains of similar structure fold, resulting from an ancient gene duplication. The active site is located in a funnel-shaped space of the C-terminal domain. A catalytically essential metal, Fe(II) or Mn(II), presents in all the enzymes in this family. Pssm-ID: 319967 Cd Length: 111 Bit Score: 37.30 E-value: 8.19e-04
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THT_oxygenase_C | cd07257 | The C-terminal domain of 2,4,5-trihydroxytoluene (THT) oxygenase; This subfamily contains the ... |
49-137 | 9.14e-04 | |||
The C-terminal domain of 2,4,5-trihydroxytoluene (THT) oxygenase; This subfamily contains the C-terminal, catalytic, domain of THT oxygenase. THT oxygenase is an extradiol dioxygenase in the 2,4-dinitrotoluene (DNT) degradation pathway. It catalyzes the conversion of 2,4,5-trihydroxytoluene to an unstable ring fission product, 2,4-dihydroxy-5-methyl-6-oxo-2,4-hexadienoic acid. The native protein was determined to be a dimer by gel filtration. The enzyme belongs to the type I family of extradiol dioxygenases which contains two structurally homologous barrel-shaped domains at the N- and C-terminus of each monomer. The active-site metal is located in the C-terminal barrel. Fe(II) is required for its catalytic activity. Pssm-ID: 319920 Cd Length: 152 Bit Score: 37.70 E-value: 9.14e-04
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HPCD_N_class_II | cd07266 | N-terminal domain of 3,4-dihydroxyphenylacetate 2,3-dioxygenase (HPCD); This subfamily ... |
49-77 | 1.23e-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: 37.00 E-value: 1.23e-03
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PRK04101 | PRK04101 | metallothiol transferase FosB; |
46-74 | 4.30e-03 | |||
metallothiol transferase FosB; Pssm-ID: 179740 Cd Length: 139 Bit Score: 35.69 E-value: 4.30e-03
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VOC_like | cd07254 | uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ... |
52-142 | 4.39e-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: 319917 [Multi-domain] Cd Length: 120 Bit Score: 35.52 E-value: 4.39e-03
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PLN02300 | PLN02300 | lactoylglutathione lyase |
49-142 | 5.44e-03 | |||
lactoylglutathione lyase Pssm-ID: 215169 [Multi-domain] Cd Length: 286 Bit Score: 36.30 E-value: 5.44e-03
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COG3565 | COG3565 | Predicted dioxygenase of extradiol dioxygenase family [General function prediction only]; |
52-74 | 5.44e-03 | |||
Predicted dioxygenase of extradiol dioxygenase family [General function prediction only]; Pssm-ID: 442786 Cd Length: 139 Bit Score: 35.54 E-value: 5.44e-03
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FosB | cd08363 | fosfomycin resistant protein subfamily FosB; This subfamily family contains FosB, a fosfomycin ... |
50-73 | 5.52e-03 | |||
fosfomycin resistant protein subfamily FosB; This subfamily family contains FosB, a fosfomycin resistant protein. FosB is a Mg(2+)-dependent L-cysteine thiol transferase. Fosfomycin inhibits the enzyme UDP-nacetylglucosamine-3-enolpyruvyltransferase (MurA), which catalyzes the first committed step in bacterial cell wall biosynthesis. FosB catalyzes the Mg(II) dependent addition of L-cysteine to the epoxide ring of fosfomycin, (1R,2S)-epoxypropylphosphonic acid, rendering it inactive. FosB is evolutionarily related to glyoxalase I and type I extradiol dioxygenases. Pssm-ID: 319951 [Multi-domain] Cd Length: 131 Bit Score: 35.40 E-value: 5.52e-03
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VOC_BsCatE_like_N | cd07255 | N-terminal of Bacillus subtilis CatE like protein; Uncharacterized subfamily of VOC ... |
49-77 | 6.32e-03 | |||
N-terminal of Bacillus subtilis CatE like protein; Uncharacterized subfamily of VOC superfamily contains Bacillus subtilis CatE and similar proteins. CatE is proposed to function as Catechol-2,3-dioxygenase. VOC is composed of structurally related proteins with paired beta.alpha.beta.beta.beta motifs that provide a metal coordination environment with two or three open or readily accessible coordination sites to promote direct electrophilic participation of the metal ion in catalysis. VOC domain is found in a variety of structurally related metalloproteins, including the bleomycin resistance protein, glyoxalase I, and type I ring-cleaving dioxygenases. A bound metal ion is required for protein activities for the members of this superfamily. A variety of metal ions have been found in the catalytic centers of these proteins including Fe(II), Mn(II), Zn(II), Ni(II) and Mg(II). The protein superfamily contains members with or without domain swapping. The proteins of this family share three conserved metal binding amino acids with the type I extradiol dioxygenases, which shows no domain swapping. Pssm-ID: 319918 Cd Length: 124 Bit Score: 34.98 E-value: 6.32e-03
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PRK10291 | PRK10291 | glyoxalase I; Provisional |
57-135 | 7.83e-03 | |||
glyoxalase I; Provisional Pssm-ID: 182358 Cd Length: 129 Bit Score: 35.00 E-value: 7.83e-03
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HPPD_N_like | cd08342 | N-terminal domain of 4-hydroxyphenylpyruvate dioxygenase (HPPD) and hydroxymandelate Synthase ... |
52-149 | 7.97e-03 | |||
N-terminal domain of 4-hydroxyphenylpyruvate dioxygenase (HPPD) and hydroxymandelate Synthase (HmaS); HppD and HmaS are non-heme iron-dependent dioxygenases, which modify a common substrate, 4-hydroxyphenylpyruvate (HPP), but yield different products. HPPD catalyzes the second reaction in tyrosine catabolism, the conversion of HPP to homogentisate (2,5-dihydroxyphenylacetic acid, HG). HmaS converts HPP to 4-hydroxymandelate, a committed step in the formation of hydroxyphenylglycerine, a structural component of nonproteinogenic macrocyclic peptide antibiotics, such as vancomycin. If the emphasis is on catalytic chemistry, HPPD and HmaS are classified as members of a large family of alpha-keto acid dependent mononuclear non-heme iron oxygenases most of which require Fe(II), molecular oxygen, and an alpha-keto acid (typically alpha-ketoglutarate) to either oxygenate or oxidize a third substrate. Both enzymes are exceptions in that they require two, instead of three, substrates, do not use alpha-ketoglutarate, and incorporate both atoms of dioxygen into the aromatic product. Both HPPD and HmaS exhibit duplicate beta barrel topology in their N- and C-terminal domains which share sequence similarity, suggestive of a gene duplication. Each protein has only one catalytic site located in at the C-terminal domain. This HPPD_N_like domain represents the N-terminal domain. Pssm-ID: 319930 Cd Length: 141 Bit Score: 34.88 E-value: 7.97e-03
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