ArsI/CadI family heavy metal resistance metalloenzyme; This family belong to the broader VOC (Vicinal Oxygen Chelate) domain family (see PF00903), which includes glyoxalase I, fosfomycin resistance proteins FosA and FosB, and dioxygenases such as 4-hydroxyphenylpyruvate dioxygenase. Members of this specific family include none of those, but instead include CadI from Mycobacterium tuberculosis and ArsI from Bacillus sp. MD1. They have an invariant CC motif at about position 95, and have poorly conserved C-terminal extension regions that nearly always contain at least one addition CC motif, often several. ArsI has been characterized as an organoarsenical lyase.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504131995   3 RIQLALNVDDLDAAIVFYSKLFNTAPAKRKPGYANFAVVEPPVKLVLIESPGQGGTINHLGVEVESSDKVHAEIARLSEA 82
Cdd:NF041414   1 RVQLALNVDDLDASVAFYSKLFGVEPAKRKPGYANFAIAEPPLKLVLLENPGAGGTLNHLGVEVESSEEVHAAIARLEEA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504131995  83 GLFTQEEINTTCCFATQDKVWVSGPANEQWEVYTVLADSETFGSSPKLLErntidadsdadaGAVCCAGSTAgdpessAA 162
Cdd:NF041414  81 GLFTFEEIDTTCCYATQDKVWVTDPDGERWEVYTVLADSETFGTSPALAA------------GAACCATAAA------SS 142

                 ..
gi 504131995 163 CC 164
Cdd:NF041414 143 CC 144

ArsI/CadI family heavy metal resistance metalloenzyme; This family belong to the broader VOC (Vicinal Oxygen Chelate) domain family (see PF00903), which includes glyoxalase I, fosfomycin resistance proteins FosA and FosB, and dioxygenases such as 4-hydroxyphenylpyruvate dioxygenase. Members of this specific family include none of those, but instead include CadI from Mycobacterium tuberculosis and ArsI from Bacillus sp. MD1. They have an invariant CC motif at about position 95, and have poorly conserved C-terminal extension regions that nearly always contain at least one addition CC motif, often several. ArsI has been characterized as an organoarsenical lyase.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504131995   3 RIQLALNVDDLDAAIVFYSKLFNTAPAKRKPGYANFAVVEPPVKLVLIESPGQGGTINHLGVEVESSDKVHAEIARLSEA 82
Cdd:NF041414   1 RVQLALNVDDLDASVAFYSKLFGVEPAKRKPGYANFAIAEPPLKLVLLENPGAGGTLNHLGVEVESSEEVHAAIARLEEA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504131995  83 GLFTQEEINTTCCFATQDKVWVSGPANEQWEVYTVLADSETFGSSPKLLErntidadsdadaGAVCCAGSTAgdpessAA 162
Cdd:NF041414  81 GLFTFEEIDTTCCYATQDKVWVTDPDGERWEVYTVLADSETFGTSPALAA------------GAACCATAAA------SS 142

                 ..
gi 504131995 163 CC 164
Cdd:NF041414 143 CC 144

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

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504131995   6 LALNVDDLDAAIVFYSKLFNTAPAKRKPGYANFAVVEPPVKLVLIESPG-----QGGTINHLGVEVESSDKVHAEIARLS 80
Cdd:COG2514    7 VTLRVRDLERSAAFYTDVLGLEVVEREGGRVYLRADGGEHLLVLEEAPGapprpGAAGLDHVAFRVPSRADLDAALARLA 86

                 ....
gi 504131995  81 EAGL 84
Cdd:COG2514   87 AAGV 90

ArsI/CadI family heavy metal resistance metalloenzyme; This family belong to the broader VOC (Vicinal Oxygen Chelate) domain family (see PF00903), which includes glyoxalase I, fosfomycin resistance proteins FosA and FosB, and dioxygenases such as 4-hydroxyphenylpyruvate dioxygenase. Members of this specific family include none of those, but instead include CadI from Mycobacterium tuberculosis and ArsI from Bacillus sp. MD1. They have an invariant CC motif at about position 95, and have poorly conserved C-terminal extension regions that nearly always contain at least one addition CC motif, often several. ArsI has been characterized as an organoarsenical lyase.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504131995   3 RIQLALNVDDLDAAIVFYSKLFNTAPAKRKPGYANFAVVEPPVKLVLIESPGQGGTINHLGVEVESSDKVHAEIARLSEA 82
Cdd:NF041414   1 RVQLALNVDDLDASVAFYSKLFGVEPAKRKPGYANFAIAEPPLKLVLLENPGAGGTLNHLGVEVESSEEVHAAIARLEEA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504131995  83 GLFTQEEINTTCCFATQDKVWVSGPANEQWEVYTVLADSETFGSSPKLLErntidadsdadaGAVCCAGSTAgdpessAA 162
Cdd:NF041414  81 GLFTFEEIDTTCCYATQDKVWVTDPDGERWEVYTVLADSETFGTSPALAA------------GAACCATAAA------SS 142

                 ..
gi 504131995 163 CC 164
Cdd:NF041414 143 CC 144

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

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504131995   6 LALNVDDLDAAIVFYSKLFNTAPAKRKPGYANFAVVEPPVKLVLIESPG-----QGGTINHLGVEVESSDKVHAEIARLS 80
Cdd:COG2514    7 VTLRVRDLERSAAFYTDVLGLEVVEREGGRVYLRADGGEHLLVLEEAPGapprpGAAGLDHVAFRVPSRADLDAALARLA 86

                 ....
gi 504131995  81 EAGL 84
Cdd:COG2514   87 AAGV 90

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 504131995   6 LALNVDDLDAAIVFYSKLFNTAPAKR-KPGYANFAVVEPPVKLVLIESPGQ----GGTINHLGVEVESSDKVHAEIARLS 80
Cdd:cd06587    2 VALRVPDLDASVAFYEEVLGFEVVSRnEGGGFAFLRLGPGLRLALLEGPEPerpgGGGLFHLAFEVDDVDEVDERLREAG 81

                         90       100       110
                 ....*....|....*....|....*....|....
gi 504131995  81 EAGLFTQEEINTtccFATQDKVWVSGPANEQWEV 114
Cdd:cd06587   82 AEGELVAPPVDD---PWGGRSFYFRDPDGNLIEF 112

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 504131995   6 LALNVDDLDAAIVFYSKLFNTAPAKRKP---GYANFAVVE--PPVKLVLIESPG-----QGGTINHLGVEVESsdkVHAE 75
Cdd:COG0346    6 VTLRVSDLEASLAFYTDVLGLELVKRTDfgdGGFGHAFLRlgDGTELELFEAPGaapapGGGGLHHLAFRVDD---LDAA 82

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 504131995  76 IARLSEAGLFTQEEINTTccFATQDKVWVSGPANEQWEVYTVLAD 120
Cdd:COG0346   83 YARLRAAGVEIEGEPRDR--AYGYRSAYFRDPDGNLIELVEPPPG 125

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 504131995   6 LALNVDDLDAAIVFYSKLFNTAPAKRKPGYANFAVVEP-PVKLVLIESPGQGgtINHLGVEVESSDKVHAEIARLSEAGL 84
Cdd:cd16360    2 AELGVPDLEKALEFYTDVLGLQVAKRDGNSVYLRGYEDeHHSLVLYEAPEAG--LKHFAFEVASEEDLERAAASLTALGC 79

                 ....*
gi 504131995  85 FTQEE 89
Cdd:cd16360   80 DVTWG 84

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 504131995   5 QLALNVDDLDAAIVFYSKLFNTAPAKRKPGYA---NFAVVEPP-VKLVLIESPGQ-----------GGTINHLGVEVess 69
Cdd:cd07249    3 HIGIAVPDLDEALKFYEDVLGVKVSEPEELEEqgvRVAFLELGnTQIELLEPLGEdspiakfldkkGGGLHHIAFEV--- 79

                         90
                 ....*....|....*
gi 504131995  70 DKVHAEIARLSEAGL 84
Cdd:cd07249   80 DDIDAAVEELKAQGV 94