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        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583667157   2 SRVQLALNVDDLDESITFYRKLFGVEPAKVKPGYANFAITEPPLKLVLLENPGK-GGSINHLGVEVESSETVHAEIARLT 80
Cdd:cd07254     1 KRFHLSLNVTDLERSIRFYSDLFGAEPAKRKADYAKFMLEDPPLNLALLVNDRKePYGLNHLGIQVDSKEEVAALKARAE 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1583667157  81 GEGLFTDEEIGTTCCFATQDKVWVTGPAGEKWEVYTVLAD 120
Cdd:cd07254    81 AAGLPVRKEPRTTCCYAVQDKFWLTDPDGNAWEFYATLTE 120

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 1583667157   6 LALNVDDLDESITFYRKLFGVEPAKVKP------GYANFAITEPPlKLVLLENPG-----KGGSINHLGVEVESsetVHA 74
Cdd:COG0346     6 VTLRVSDLEASLAFYTDVLGLELVKRTDfgdggfGHAFLRLGDGT-ELELFEAPGaapapGGGGLHHLAFRVDD---LDA 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1583667157  75 EIARLTGEGLFTDEEIGTTccFATQDKVWVTGPAGEKWEVYTVLAD 120
Cdd:COG0346    82 AYARLRAAGVEIEGEPRDR--AYGYRSAYFRDPDGNLIELVEPPPG 125

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        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583667157   2 SRVQLALNVDDLDESITFYRKLFGVEPAKVKPGYANFAITEPPLKLVLLENPGK-GGSINHLGVEVESSETVHAEIARLT 80
Cdd:cd07254     1 KRFHLSLNVTDLERSIRFYSDLFGAEPAKRKADYAKFMLEDPPLNLALLVNDRKePYGLNHLGIQVDSKEEVAALKARAE 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1583667157  81 GEGLFTDEEIGTTCCFATQDKVWVTGPAGEKWEVYTVLAD 120
Cdd:cd07254    81 AAGLPVRKEPRTTCCYAVQDKFWLTDPDGNAWEFYATLTE 120

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 1583667157   6 LALNVDDLDESITFYRKLFGVEPA-KVKPGYANFAITEPPLKLVLLENPG----KGGSINHLGVEVESSETVHAEIARLT 80
Cdd:cd06587     2 VALRVPDLDASVAFYEEVLGFEVVsRNEGGGFAFLRLGPGLRLALLEGPEperpGGGGLFHLAFEVDDVDEVDERLREAG 81

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1583667157  81 GEGLFTDEEIGTtccFATQDKVWVTGPAGEKWEV 114
Cdd:cd06587    82 AEGELVAPPVDD---PWGGRSFYFRDPDGNLIEF 112

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

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583667157   6 LALNVDDLDESITFYRKLFGVEPAKVKPGYANFAITEPPLKLVLLENPG-----KGGSINHLGVEVESSETVHAEIARLT 80
Cdd:COG2514     7 VTLRVRDLERSAAFYTDVLGLEVVEREGGRVYLRADGGEHLLVLEEAPGapprpGAAGLDHVAFRVPSRADLDAALARLA 86

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1583667157  81 GEGLFTDEEIgttcCFATQDKVWVTGPAGEKWEVYT 116
Cdd:COG2514    87 AAGVPVEGAV----DHGVGESLYFRDPDGNLIELYT 118

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        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1583667157   6 LALNVDDLDESITFYRKLFGVEPAKVKPGYANFAITEP-PLKLVLLENPGKGgsINHLGVEVESSETVHAEIARLTGEG 83
Cdd:cd16360     2 AELGVPDLEKALEFYTDVLGLQVAKRDGNSVYLRGYEDeHHSLVLYEAPEAG--LKHFAFEVASEEDLERAAASLTALG 78

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583667157   5 QLALNVDDLDESITFYRKLFGVEPAKVKPGYA---NFAITEPP-LKLVLLE--NPG---------KGGSINHLGVEVESs 69
Cdd:cd07249     3 HIGIAVPDLDEALKFYEDVLGVKVSEPEELEEqgvRVAFLELGnTQIELLEplGEDspiakfldkKGGGLHHIAFEVDD- 81

                          90
                  ....*....|....*
gi 1583667157  70 etVHAEIARLTGEGL 84
Cdd:cd07249    82 --IDAAVEELKAQGV 94

phenazine resistance protein, EhpR; Phenazine resistance protein (EhpR) in Enterobacter agglomerans confers resistance by binding D-alanyl-griseoluteic acid and acting as a chaperone involved in exporting the antibiotic rather than by altering it chemically. EhpR is evolutionarily related to glyoxalase I and type I extradiol dioxygenases.

                          10        20        30
                  ....*....|....*....|....*....|.
gi 1583667157   8 LNVDDLDESITFYRKLFGVEPAKVKPGYANF 38
Cdd:cd07261     4 LYVDNPERSTEFYRFLLGKEPVESSPTFASF 34

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        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1583667157   5 QLALNVDDLDESITFYRKLFGVEPAKVKPGYANFAITEPPLKLVLLENPGKG 56
Cdd:cd07255     5 RVTLKVADLERQSAFYQNVIGLSVLKQNASRAYLGVDGKQVLLVLEAIPDAV 56