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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530368214   47 RLNHVAIAVPDLEKAAAFYKNILGAQ-----------------------------------------------------V 73
Cdd:TIGR03081   1 RIDHVGIAVPDLEEAAKFYEDVLGAQvseieelpeqgvkvvfialgntkvelleplgedspiakflekngggihhiaieV 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 530368214   74 DNINAAVMDLKKKKIRSLSEEVKIGAHGKPVIFLHPKDCGGVLVELEQ 121
Cdd:TIGR03081  81 DDIEAALETLKEKGVRLIDEEPRIGAHGKPVAFLHPKSTGGVLIELEQ 128

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530368214   47 RLNHVAIAVPDLEKAAAFYKNILGAQ-----------------------------------------------------V 73
Cdd:TIGR03081   1 RIDHVGIAVPDLEEAAKFYEDVLGAQvseieelpeqgvkvvfialgntkvelleplgedspiakflekngggihhiaieV 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 530368214   74 DNINAAVMDLKKKKIRSLSEEVKIGAHGKPVIFLHPKDCGGVLVELEQ 121
Cdd:TIGR03081  81 DDIEAALETLKEKGVRLIDEEPRIGAHGKPVAFLHPKSTGGVLIELEQ 128

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

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530368214  47 RLNHVAIAVPDLEKAAAFYKNILGAQ------------------------------------------------VDNINA 78
Cdd:COG0346    2 GLHHVTLRVSDLEASLAFYTDVLGLElvkrtdfgdggfghaflrlgdgtelelfeapgaapapgggglhhlafrVDDLDA 81

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 530368214  79 AVMDLKKKKIRsLSEEVKIGAHGKPVIFLhpKDCGGVLVEL 119
Cdd:COG0346   82 AYARLRAAGVE-IEGEPRDRAYGYRSAYF--RDPDGNLIEL 119

metallothiol transferase FosB;

                         10        20
                 ....*....|....*....|....*
gi 530368214  48 LNHVAIAVPDLEKAAAFYKNILGAQ 72
Cdd:PRK04101   5 INHICFSVSNLEKSIEFYEKVLGAK 29

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530368214   47 RLNHVAIAVPDLEKAAAFYKNILGAQ-----------------------------------------------------V 73
Cdd:TIGR03081   1 RIDHVGIAVPDLEEAAKFYEDVLGAQvseieelpeqgvkvvfialgntkvelleplgedspiakflekngggihhiaieV 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 530368214   74 DNINAAVMDLKKKKIRSLSEEVKIGAHGKPVIFLHPKDCGGVLVELEQ 121
Cdd:TIGR03081  81 DDIEAALETLKEKGVRLIDEEPRIGAHGKPVAFLHPKSTGGVLIELEQ 128

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

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530368214  47 RLNHVAIAVPDLEKAAAFYKNILGAQ------------------------------------------------VDNINA 78
Cdd:COG0346    2 GLHHVTLRVSDLEASLAFYTDVLGLElvkrtdfgdggfghaflrlgdgtelelfeapgaapapgggglhhlafrVDDLDA 81

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 530368214  79 AVMDLKKKKIRsLSEEVKIGAHGKPVIFLhpKDCGGVLVEL 119
Cdd:COG0346   82 AYARLRAAGVE-IEGEPRDRAYGYRSAYF--RDPDGNLIEL 119

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.

                         10        20
                 ....*....|....*....|...
gi 530368214  48 LNHVAIAVPDLEKAAAFYKNILG 70
Cdd:cd07245    1 LDHVALACPDLERARRFYTDVLG 23

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

                         10        20
                 ....*....|....*....|....*..
gi 530368214  47 RLNHVAIAVPDLEKAAAFYKNILGAQV 73
Cdd:COG2514    3 RLGHVTLRVRDLERSAAFYTDVLGLEV 29

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.

                         10        20
                 ....*....|....*....|....*..
gi 530368214  47 RLNHVAIAVPDLEKAAAFYKNILGAQV 73
Cdd:cd16361    1 GVNHVGITVPDLDAAVEFYTDVLGAEV 27

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

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530368214  46 GRLNHVAIAVPDLEKAAAFYKNILGAQVD-----NINAAVMDLKKKKIRSLSEEVKIGAHGKPVIFLHPKDCGGVLVELE 120
Cdd:COG3324    3 GTIVWVELPVDDLERAKAFYEEVFGWTFEddagpGGDYAEFDTDGGQVGGLMPGAEEPGGPGWLLYFAVDDLDAAVARVE 82

                 ..
gi 530368214 121 QA 122
Cdd:COG3324   83 AA 84

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.

                         10        20
                 ....*....|....*....|....*..
gi 530368214  47 RLNHVAIAVPDLEKAAAFYKNILGAQV 73
Cdd:cd08352    2 KIHHIAIICSDYEKSKDFYVDKLGFEI 28

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.

                         10        20        30
                 ....*....|....*....|....*....|
gi 530368214  44 NLGRLNHVAIAVPDLEKAAAFYKNILGAQV 73
Cdd:cd07266    1 DIIRLAHAELVVTDLAASREFYVDTLGLHV 30

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.

                         10        20
                 ....*....|....*....|....*..
gi 530368214  47 RLNHVAIAVPDLEKAAAFYKNILGAQV 73
Cdd:cd07255    2 RIGRVTLKVADLERQSAFYQNVIGLSV 28

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.

                         10        20
                 ....*....|....*....|....
gi 530368214  50 HVAIAVPDLEKAAAFYKNILGAQV 73
Cdd:cd16360    1 YAELGVPDLEKALEFYTDVLGLQV 24