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        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446940401   5 KVHHVAIICSNYEVSKDFYTIILGFKVINEVYRKERDSYKLDLCVGEeYQIELFSFPSPPERPSFPEAAGLRHLAFAVIN 84
Cdd:cd08352    2 KIHHIAIICSDYEKSKDFYVDKLGFEIIREHYRPERNDIKLDLALGG-YQLELFIKPDAPARPSYPEALGLRHLAFKVED 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 446940401  85 IEEAVTHLNQCGVETESIRIDEITGKKFVFFQDPDGLPLELYE 127
Cdd:cd08352   81 VEATVAELKSLGIETEPIRVDDFTGKKFTFFFDPDGLPLELYE 123

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        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446940401   5 KVHHVAIICSNYEVSKDFYTIILGFKVINEVYRKERDSYKLDLCVGEeYQIELFSFPSPPERPSFPEAAGLRHLAFAVIN 84
Cdd:cd08352    2 KIHHIAIICSDYEKSKDFYVDKLGFEIIREHYRPERNDIKLDLALGG-YQLELFIKPDAPARPSYPEALGLRHLAFKVED 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 446940401  85 IEEAVTHLNQCGVETESIRIDEITGKKFVFFQDPDGLPLELYE 127
Cdd:cd08352   81 VEATVAELKSLGIETEPIRVDDFTGKKFTFFFDPDGLPLELYE 123

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 446940401   5 KVHHVAIICSNYEVSKDFYTIILGFKVINEVYRKERDSYKLDLCVGEEYQIELFSFPsppERPSFPEAAGLRHLAFAVIN 84
Cdd:COG0346    2 GLHHVTLRVSDLEASLAFYTDVLGLELVKRTDFGDGGFGHAFLRLGDGTELELFEAP---GAAPAPGGGGLHHLAFRVDD 78

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 446940401  85 IEEAVTHLNQCGVETESIRIDEITGKKFVFFQDPDGLPLELYE 127
Cdd:COG0346   79 LDAAYARLRAAGVEIEGEPRDRAYGYRSAYFRDPDGNLIELVE 121

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 446940401    5 KVHHVAIICSNYEVSKDFYTIILGFKVINEVYRKERDSYKLDLCVGEEYqIELFSfPSPPERP--SFPE--AAGLRHLAF 80
Cdd:TIGR03081   1 RIDHVGIAVPDLEEAAKFYEDVLGAQVSEIEELPEQGVKVVFIALGNTK-VELLE-PLGEDSPiaKFLEknGGGIHHIAI 78

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 446940401   81 AVINIEEAVTHLNQCGVEtesiRIDEIT-----GKKFVFF--QDPDGLPLELYE 127
Cdd:TIGR03081  79 EVDDIEAALETLKEKGVR----LIDEEPrigahGKPVAFLhpKSTGGVLIELEQ 128

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        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446940401   5 KVHHVAIICSNYEVSKDFYTIILGFKVINEVYRKERDSYKLDLCVGEeYQIELFSFPSPPERPSFPEAAGLRHLAFAVIN 84
Cdd:cd08352    2 KIHHIAIICSDYEKSKDFYVDKLGFEIIREHYRPERNDIKLDLALGG-YQLELFIKPDAPARPSYPEALGLRHLAFKVED 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 446940401  85 IEEAVTHLNQCGVETESIRIDEITGKKFVFFQDPDGLPLELYE 127
Cdd:cd08352   81 VEATVAELKSLGIETEPIRVDDFTGKKFTFFFDPDGLPLELYE 123

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 446940401   5 KVHHVAIICSNYEVSKDFYTIILGFKVINEVYRKERDSYKLDLCVGEEYQIELFSFPsppERPSFPEAAGLRHLAFAVIN 84
Cdd:COG0346    2 GLHHVTLRVSDLEASLAFYTDVLGLELVKRTDFGDGGFGHAFLRLGDGTELELFEAP---GAAPAPGGGGLHHLAFRVDD 78

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 446940401  85 IEEAVTHLNQCGVETESIRIDEITGKKFVFFQDPDGLPLELYE 127
Cdd:COG0346   79 LDAAYARLRAAGVEIEGEPRDRAYGYRSAYFRDPDGNLIELVE 121

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

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446940401   5 KVHHVAIICSNYEVSKDFYTIILGFKVInevyRKERDSYKLdLCVGEEYQIELFSFPSPPERpsfPEAAGLRHLAFAVIN 84
Cdd:COG2514    3 RLGHVTLRVRDLERSAAFYTDVLGLEVV----EREGGRVYL-RADGGEHLLVLEEAPGAPPR---PGAAGLDHVAFRVPS 74

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 446940401  85 IEE---AVTHLNQCGVETESIRidEITGKKFVFFQDPDGLPLELY 126
Cdd:COG2514   75 RADldaALARLAAAGVPVEGAV--DHGVGESLYFRDPDGNLIELY 117

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 446940401   8 HVAIICSNYEVSKDFYTIILGFKVineVYRKERDSYKLDLCvGEEYQIELFSFPSPPERPsfpeAAGLRHLAFAVINIEE 87
Cdd:cd06587    1 HVALRVPDLDASVAFYEEVLGFEV---VSRNEGGGFAFLRL-GPGLRLALLEGPEPERPG----GGGLFHLAFEVDDVDE 72

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 446940401  88 AVTHLNQCGVETESIRIDEIT--GKKFVFFQDPDGLPLEL 125
Cdd:cd06587   73 VDERLREAGAEGELVAPPVDDpwGGRSFYFRDPDGNLIEF 112

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

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446940401   5 KVHHVAIICSNYEVSKDFYTIILGFKVinEVYRKERDSYkLDLCVGEEYQIELFSFPSPPERPSFpeaaglrHLAFAVIN 84
Cdd:COG3324    4 TIVWVELPVDDLERAKAFYEEVFGWTF--EDDAGPGGDY-AEFDTDGGQVGGLMPGAEEPGGPGW-------LLYFAVDD 73

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 446940401  85 IEEAVTHLNQCGVETESIRIDEITGKKFVFFQDPDGLPLELYE 127
Cdd:COG3324   74 LDAAVARVEAAGGTVLRPPTDIPPWGRFAVFRDPEGNRFGLWQ 116

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 446940401   6 VHHVAIICSNYEVSKDFYTIILGFKVineVYRKERDSYKLDLCVGE--EYQIEL---FSFPSPPERpsFPEA--AGLRHL 78
Cdd:cd07249    1 LDHIGIAVPDLDEALKFYEDVLGVKV---SEPEELEEQGVRVAFLElgNTQIELlepLGEDSPIAK--FLDKkgGGLHHI 75

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 446940401  79 AFAVINIEEAVTHLNQCGVET-ESIRIDEITGKKFVFFQDPD--GLPLELYE 127
Cdd:cd07249   76 AFEVDDIDAAVEELKAQGVRLlSEGPRIGAHGKRVAFLHPKDtgGVLIELVE 127

Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446940401    7 HHVAIICSNYEVSKDFYTIILGFKVInEVYRKERDSYKLDLCV--GEEYQIELFsfpSPPERPSFPEAA--GLRHLAFAV 82
Cdd:pfam13669   1 HHVGIAVPDLDRALALWGALLGLGPE-GDYRSEPQNVDLAFALlgDGPVEVELI---QPLDGDSPLARHgpGLHHLAYWV 76

                          90
                  ....*....|....*.
gi 446940401   83 INIEEAVTHLNQCGVE 98
Cdd:pfam13669  77 DDLDAAVARLLDQGYR 92

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        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446940401   8 HVAIICSNYEVSKDFYTIILGFKVI----NEVYRKERDSYKLDLCVGEeyqielfsfpsPPErpsfpeaAGLRHLAFAVI 83
Cdd:cd16360    1 YAELGVPDLEKALEFYTDVLGLQVAkrdgNSVYLRGYEDEHHSLVLYE-----------APE-------AGLKHFAFEVA 62

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 446940401  84 N---IEEAVTHLNQCGVETESIRIDEITG-KKFVFFQDPDGLPLELY 126
Cdd:cd16360   63 SeedLERAAASLTALGCDVTWGPDGEVPGgGKGFRFQDPSGHLLELF 109

N-terminal, non-catalytic, domain of BphC_JF8, (2,3-dihydroxybiphenyl 1,2-dioxygenase) from Bacillus sp. JF8, and similar proteins; 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 N-terminal repeat.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446940401   3 ICKVHHVAIICSNYEVSKDFYTIILGFkvinEVYRKERDSYKLDlCVGEEYQIELFSFPSPperpsfpeAAGLRHLAFAV 82
Cdd:cd09013    4 LAQLAHVELLTPKPEESLWFFTDVLGL----EETHREGQSVYLR-AWGDWEHHTLKLTESP--------EAGLGHIAWRA 70

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 446940401  83 IN---IEEAVTHLNQCGVETESIRIDEITGKKFVfFQDPDGLPLELY 126
Cdd:cd09013   71 SSpeaLERRVAALEASGVGIGWIDGDLGQGPAYR-FQSPDGHPMEIY 116

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        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446940401   6 VHHVAIICSNYEVSKDFYTIILGFKVInevyrkERDSYKLDLCV-GEEYQIELFSFPSPPERPsfPEAAGLRHLAFAVIN 84
Cdd:cd07255    3 IGRVTLKVADLERQSAFYQNVIGLSVL------KQNASRAYLGVdGKQVLLVLEAIPDAVLAP--RSTTGLYHFAILLPD 74

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 446940401  85 IEE---AVTHLNQCGVETESirIDEITGKKFvFFQDPDGLPLELY 126
Cdd:cd07255   75 RKAlgrALAHLAEHGPLIGA--ADHGVSEAI-YLSDPEGNGIEIY 116

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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446940401   5 KVHHVAIICSNYEVSKDFYTIILGFKViNEVYRKERDSYK-LDLCVGEEYQIELFSFPSPPERPSFPEAAGLRHLAFAVi 83
Cdd:cd07241    1 KIEHVALWTNDLERMKDFYVKYFGAES-NDIYHNKKKGFRsYFLTFDSGARLELMSRPDVTDPDKEVERTGLAHIAFSV- 78

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 446940401  84 NIEEAVTHLNQCGVETESIRIDE--ITGKKFV--FFQDPDGLPLEL 125
Cdd:cd07241   79 GSKEAVDELTERLRADGYAVVGGprTTGDGYYesVILDPEGNRIEI 124

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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446940401   8 HVAIICSNYEVSKDFYTIILGFKVINEVYRKERDSYKLDLCVGEEYQIELFSFPSPPerpsfpeaAGLRHLAFAVINIEE 87
Cdd:cd08343    2 HVVLCSPDVEASRDFYTDVLGFRVSDRIVDPGVDGGAFLHCDRGTDHHTVALAGGPH--------PGLHHVAFEVHDLDD 73

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 446940401  88 ---AVTHLNQCGVETES-----IrideITGKKFVFFQDPDGLPLELY 126
Cdd:cd08343   74 vgrGHDRLREKGYKIEWgpgrhG----LGSQVFDYWFDPSGNRVEYY 116

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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446940401   7 HHVAIICSNYEVSKDFYTIILGFK-VINEVYRKERDSYKLdlCVGEEYQ---IELFSFPSPPERPSFPEAAGLRHLAFAV 82
Cdd:cd08346    3 HHITAITGDAQENVDFYVKVLGLRlVKKTVNQDDPPMYHL--YYGDELGspgTLLTFFPWPLGGPGRRGTGQISRIGLRV 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 446940401  83 I--NIEEAVTHLNQCGVETESIRidEITGKKFVFFQDPDGLPLEL 125
Cdd:cd08346   81 PkgSLSFWAERLEKFGVPHSEVV--TRFGEKYLRFEDPDGTRLFL 123

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
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 446940401  72 AAGLRHLAFAVINIEEAV--THLNQCGVETESiRIDEITGKKFVFFQDPDGLPLEL 125
Cdd:cd08354   65 ASGHGHFAFAVPTEELAAweARLEAKGVPIES-YTQWPEGGKSLYFRDPAGNLVEL 119

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).

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446940401   6 VHHVAIICSNYEVSKDFYTIILGFKVINEvyrkERDSYKLDLCVGEEYQIELfsfpsppeRPSfpEAAGLRHLAFAVIN- 84
Cdd:cd08362    4 LRYVALGVPDLAAEREFYTEVWGLEEVAE----DDDVVYLRAEGSEHHVLRL--------RQS--DENRLDLIAFAAATr 69

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 446940401  85 --IEEAVTHLNQ--CGVETESIRIDEIT-GKKFVFFqDPDGLPLEL 125
Cdd:cd08362   70 adVDALAARLAAagVRILSEPGPLDDPGgGYGFRFF-DPDGRTIEV 114

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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446940401   8 HVAIICSNYEVSKDFYTIILGFKVI-----NEVYRKERDSYkldlcvgEEYQIELfsfpsppeRPSfpEAAGLRHLAFAV 82
Cdd:cd07265    7 HVQLRVLDLEEAIKHYREVLGLVETgrddqGRVYLKAWDEY-------DHHSIIL--------REA--DTAGLDFMGFKV 69

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 446940401  83 INIE--EAVTH-LNQCGVETESIRIDEI--TGKKfVFFQDPDGLPLELY 126
Cdd:cd07265   70 LDDAdlEQLEArLQAYGVTVTRIPAGELpgVGRR-VRFQLPSGHTMELY 117