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 58037329  50 LNHVAVAVPDLEKASSFYRDVLGAQVSEVVPLPEHGVSVVFVNLGNTKMELLHPLGSDSPITGFLqKNKAGGMHHVCIEV 129
Cdd:cd07249   1 LDHIGIAVPDLDEALKFYEDVLGVKVSEPEELEEQGVRVAFLELGNTQIELLEPLGEDSPIAKFL-DKKGGGLHHIAFEV 79

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
gi 58037329 130 DNISAAVMDLKKKKIRSLSDEAKIGAHGKPVIFLHPKDCGGVLVELEQ 177
Cdd:cd07249  80 DDIDAAVEELKAQGVRLLSEGPRIGAHGKRVAFLHPKDTGGVLIELVE 127

Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037329    51 NHVAVAVPDLEKASSFYRDVLGAQVSEVVPLPEHGVSVVFVNLGNTKM--ELLHPLGSDSPItgflqKNKAGGMHHVCIE 128
Cdd:pfam13669   1 HHVGIAVPDLDRALALWGALLGLGPEGDYRSEPQNVDLAFALLGDGPVevELIQPLDGDSPL-----ARHGPGLHHLAYW 75

                          90       100       110
                  ....*....|....*....|....*....|....
gi 58037329   129 VDNISAAVMDLKKKKIRSLSDEAKIGAHGKPVIF 162
Cdd:pfam13669  76 VDDLDAAVARLLDQGYRVAPKGPRAGAAGRRVAF 109

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 58037329  50 LNHVAVAVPDLEKASSFYRDVLGAQVSEVVPLPEHGVSVVFVNLGNTKMELLHPLGSDSPITGFLqKNKAGGMHHVCIEV 129
Cdd:cd07249   1 LDHIGIAVPDLDEALKFYEDVLGVKVSEPEELEEQGVRVAFLELGNTQIELLEPLGEDSPIAKFL-DKKGGGLHHIAFEV 79

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
gi 58037329 130 DNISAAVMDLKKKKIRSLSDEAKIGAHGKPVIFLHPKDCGGVLVELEQ 177
Cdd:cd07249  80 DDIDAAVEELKAQGVRLLSEGPRIGAHGKRVAFLHPKDTGGVLIELVE 127

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 58037329  49 RLNHVAVAVPDLEKASSFYRDVLGAQVSEVVPLPEHGVSVVFVNLGN-TKMELLHPLGsDSPITGflqknkAGGMHHVCI 127
Cdd:COG0346   2 GLHHVTLRVSDLEASLAFYTDVLGLELVKRTDFGDGGFGHAFLRLGDgTELELFEAPG-AAPAPG------GGGLHHLAF 74

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
gi 58037329 128 EVDNISAAVMDLKKKKIRsLSDEAKIGAHGKPVIFLhpKDCGGVLVEL 175
Cdd:COG0346  75 RVDDLDAAYARLRAAGVE-IEGEPRDRAYGYRSAYF--RDPDGNLIEL 119

Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037329    49 RLNHVAVAVPDLEKASSFYRDVLGAQVSEVVPLPEH-GVSVVFVNLGNTKMELLHPLGSDSPITGFlqknKAGGMHHVCI 127
Cdd:pfam00903   1 RIDHVALRVGDLEKSLDFYTDVLGFKLVEETDAGEEgGLRSAFFLAGGRVLELLLNETPPPAAAGF----GGHHIAFIAF 76

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 58037329   128 EVDNISAAVMDLKKKKIRslsDEAKIGAHGKPVIFLHPKDCGGVLVEL 175
Cdd:pfam00903  77 SVDDVDAAYDRLKAAGVE---IVREPGRHGWGGRYSYFRDPDGNLIEL 121

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 58037329  50 LNHVAVAVPDLEKASSFYRDVLGAqvsEVVPLPEHGV-SVVFVNLGNTKMelLHpLGSDSPITGFLQKNKAGGMHHVCIE 128
Cdd:cd07245   1 LDHVALACPDLERARRFYTDVLGL---EEVPRPPFLKfGGAWLYLGGGQQ--IH-LVVEQNPSELPRPEHPGRDRHPSFS 74

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 58037329 129 VDNISAAVMDLKKKKI---RSLSDEAKIGAhgkpvIFLHpkDCGGVLVEL 175
Cdd:cd07245  75 VPDLDALKQRLKEAGIpytESTSPGGGVTQ-----LFFR--DPDGNRLEF 117

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

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037329  49 RLNHVAVAVPDLEKASSFYRDVLGAQVSEvvplpEHGVSVVF-VNLGNTKMELLHPlgsdspiTGFLQKNKAGGMHHVCI 127
Cdd:COG2514   3 RLGHVTLRVRDLERSAAFYTDVLGLEVVE-----REGGRVYLrADGGEHLLVLEEA-------PGAPPRPGAAGLDHVAF 70

                ....*..
gi 58037329 128 EVDNISA 134
Cdd:COG2514  71 RVPSRAD 77

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.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037329  52 HVAVAVPDLEKASSFYRDVLGAQVSEVVPLPEHGVSVVFVNLG----NTKMELLHPLGSDSpitgflqKNKAGGMHHVCI 127
Cdd:cd16358   3 HTMLRVGDLDRSIKFYTEVLGMKLLRKRDYPEGKYTLAFVGYGdedeNTVLELTYNWGVDK-------YDLGTAYGHIAI 75

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
gi 58037329 128 EVDNISAAVMDLKKKKIRsLSDEAKIGAHGKPVI-FLHPKDcgGVLVEL 175
Cdd:cd16358  76 GVEDVYETCERIRKKGGK-VTREPGPMKGGTTVIaFVEDPD--GYKIEL 121

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 58037329  49 RLNHVAVAVPDLEKASSFYRDVLGAQVSEVVPLPEHGVSVVFVNLGNTKMELlhplgsdspitgFLQKN--------KAG 120
Cdd:cd08352   2 KIHHIAIICSDYEKSKDFYVDKLGFEIIREHYRPERNDIKLDLALGGYQLEL------------FIKPDaparpsypEAL 69

                        90       100
                ....*....|....*....|....*
gi 58037329 121 GMHHVCIEVDNISAAVMDLKKKKIR 145
Cdd:cd08352  70 GLRHLAFKVEDVEATVAELKSLGIE 94

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 58037329  52 HVAVAVPDLEKASSFYRDVLGAQVSEVVPLPEHGVsvvfVNLGNTKMELL------HPLGSDSPITGFLqknkaggmhhV 125
Cdd:cd07264   3 YIVLYVDDFAASLRFYRDVLGLPPRFLHEEGEYAE----FDTGETKLALFsrkemaRSGGPDRRGSAFE----------L 68

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|...
gi 58037329 126 CIEVDNISAAVMDLKKKKIRSLSDEAKIgAHGKPVIFLhpKDCGGVLVELEQA 178
Cdd:cd07264  69 GFEVDDVEATVEELVERGAEFVREPANK-PWGQTVAYV--RDPDGNLIEICEP 118

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 58037329  49 RLNHVAVAVPDLEKASSFYRD----------VLGAQVSEVVPLPEHGVSVVFVNL--GNTKMEL---LHPlgsdSPITGF 113
Cdd:cd08353   3 RMDHVGIVVEDLDAAIAFFTElglelegrmtVEGEWADRVVGLDGVRVEIAMLRTpdGHGRLELskfLTP----AAIPGH 78

                        90       100       110
                ....*....|....*....|....*....|
gi 58037329 114 LQ-KNKAGGMHHVCIEVDNISAAVMDLKKK 142
Cdd:cd08353  79 RPaPANALGLRHVAFAVDDIDAVVARLRKH 108

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.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037329  50 LNHVAVAVPDLEKASSFYRDVLGAQVSEVV---PLPEHGVSVVF--VN-------LGNTKMellhplgsdspitgflqkn 117
Cdd:cd07237  10 LGHVVLIVPDVDEALAFYTDVLGFRLSDEIripLPPGVTARLHFlhCNgrhhslaFGAGPG------------------- 70

                        90
                ....*....|....*
gi 58037329 118 kAGGMHHVCIEVDNI 132
Cdd:cd07237  71 -PKRLHHLMLEVTSL 84

Zn-dependent glyoxalase, PhnB family [Energy production and conversion];

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037329  55 VAVPDLEKASSFYRDVLGAQVSEVVPLPEHGVSVVFVNLGNTKMELLHPLGsDSPITgflqknkAGGMHHVCIEVDNISA 134
Cdd:COG2764   6 LVVDDAEEALEFYEDVFGFEVVFRMTDPDGKIMHAELRIGGSVLMLSDAPP-DSPAA-------EGNGVSLSLYVDDVDA 77

                .
gi 58037329 135 A 135
Cdd:COG2764  78 L 78

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 58037329  52 HVAVAVPDLEKASSFYRDVLGAQVSEVVPLPEHGVSVVFVNLGNTKMELLHPLGSDSPITGflQKNKAGGMHHVCIEVDN 131
Cdd:cd07263   1 QVMLYVDDQDKALDFYVEKLGFEVVEDVPMGGMRWVTVAPPGSPGTSLLLEPKAHPAQMPQ--SPEAAGGTPGILLATDD 78

                        90
                ....*....|.
gi 58037329 132 ISAAVMDLKKK 142
Cdd:cd07263  79 IDATYERLTAA 89

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 58037329  55 VAVPDLEKASSFYRDVLGAQVSEVVPLPEHGVSVVFVNLGNTKMELLHPlgsdSPITGFLQKNKAGGMH-HVCIEVDNIS 133
Cdd:cd07246   7 LVVEDAAAAIAFYKKAFGAEELGRTTQEDGRVGHAELRIGGTVVMVADE----NPERGALSPTKLGGTPvIFHLYVEDVD 82

                ...
gi 58037329 134 AAV 136
Cdd:cd07246  83 ATF 85

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 58037329  52 HVAVAVPDLEKASSFYRDVLGAQVS 76
Cdd:cd16360   1 YAELGVPDLEKALEFYTDVLGLQVA 25

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
                ....*....|....*....|....*....
gi 58037329  49 RLNHVAVAVPDLEKASSFYRDVLGAQVSE 77
Cdd:cd07266   4 RLAHAELVVTDLAASREFYVDTLGLHVTD 32

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 58037329  52 HVAVAVPDLEKASSFYRDVLGAQVSEVVP------LPEHGVSVVFVNLGNTkmellhplgsdspitgflqknKAGGMHHV 125
Cdd:cd07254   4 HLSLNVTDLERSIRFYSDLFGAEPAKRKAdyakfmLEDPPLNLALLVNDRK---------------------EPYGLNHL 62

                        90
                ....*....|....*..
gi 58037329 126 CIEVDNiSAAVMDLKKK 142
Cdd:cd07254  63 GIQVDS-KEEVAALKAR 78

Predicted dioxygenase of extradiol dioxygenase family [General function prediction only];

                        10        20
                ....*....|....*....|...
gi 58037329  52 HVAVAVPDLEKASSFYRDVLGAQ 74
Cdd:COG3565   7 HLAFPVTDLDAARRFYGDVLGCE 29

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 58037329  49 RLNHVAVAVPDLEKASSFYRDVLGAQVSE 77
Cdd:cd07255   2 RIGRVTLKVADLERQSAFYQNVIGLSVLK 30

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.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037329  52 HVAVAVPDLEKASSFYRDVLGAQVSEVVPLPEHGVSVVFVNLGNTKMELLHPLGSDSPITGFLQKnkaggmhH------V 125
Cdd:cd08342   3 HVEFYVGNAKQAASYYSTGLGFEPVAYHGLETREKASHVLRQGDIRFVFTSPLSSDAPAADFLAK-------HgdgvkdV 75

                        90       100
                ....*....|....*....|....
gi 58037329 126 CIEVDNISAAVMDLKKKKIRSLSD 149
Cdd:cd08342  76 AFRVEDADAAYERAVARGAKPVAE 99