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Conserved domains on  [gi|499513149|ref|WP_011199789|]
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MULTISPECIES: VOC family protein [Basfia]

Protein Classification

VOC family protein( domain architecture ID 10170093)

vicinal oxygen chelate (VOC) family protein similar to Escherichia coli YaeR protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
VOC_Bs_YwkD_like cd08352
vicinal oxygen chelate (VOC) family protein Bacillus subtilis YwkD and similar proteins; ...
 6-129 3.39e-70

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.


:

Pssm-ID: 319940 [Multi-domain]  Cd Length: 123  Bit Score: 206.63  E-value: 3.39e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499513149   6 TGFHHIAIIVSDYEKSKYFYTQILGAEVIEETYRASRHSYKLDLKFaDGSQIELFSFPSSPSRLTMPEACGLRHLAFKVK 85
Cdd:cd08352    1 KKIHHIAIICSDYEKSKDFYVDKLGFEIIREHYRPERNDIKLDLAL-GGYQLELFIKPDAPARPSYPEALGLRHLAFKVE 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 499513149  86 DIEEAVQYLKTQQIECEDIRIDELTGKKFTFFKDPDNLPLELYE 129
Cdd:cd08352   80 DVEATVAELKSLGIETEPIRVDDFTGKKFTFFFDPDGLPLELYE 123
 
Name Accession Description Interval E-value
VOC_Bs_YwkD_like cd08352
vicinal oxygen chelate (VOC) family protein Bacillus subtilis YwkD and similar proteins; ...
 6-129 3.39e-70

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.


Pssm-ID: 319940 [Multi-domain]  Cd Length: 123  Bit Score: 206.63  E-value: 3.39e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499513149   6 TGFHHIAIIVSDYEKSKYFYTQILGAEVIEETYRASRHSYKLDLKFaDGSQIELFSFPSSPSRLTMPEACGLRHLAFKVK 85
Cdd:cd08352    1 KKIHHIAIICSDYEKSKDFYVDKLGFEIIREHYRPERNDIKLDLAL-GGYQLELFIKPDAPARPSYPEALGLRHLAFKVE 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 499513149  86 DIEEAVQYLKTQQIECEDIRIDELTGKKFTFFKDPDNLPLELYE 129
Cdd:cd08352   80 DVEATVAELKSLGIETEPIRVDDFTGKKFTFFFDPDGLPLELYE 123
PRK11478 PRK11478
VOC family protein;
9-129 2.89e-55

VOC family protein;


Pssm-ID: 183156 [Multi-domain]  Cd Length: 129  Bit Score: 168.92  E-value: 2.89e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499513149   9 HHIAIIVSDYEKSKYFYTQILGAEVIEETYRASRHSYKLDLKFADGSQIELFSFPSSPSRLTMPEACGLRHLAFKVKDIE 88
Cdd:PRK11478   8 HHIAIIATDYAVSKAFYCDILGFTLQSEVYREARDSWKGDLALNGQYVIELFSFPFPPERPSRPEACGLRHLAFSVDDID 87

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 499513149  89 EAVQYLKTQQIECEDIRIDELTGKKFTFFKDPDNLPLELYE 129
Cdd:PRK11478  88 AAVAHLESHNVKCEAIRVDPYTQKRFTFFNDPDGLPLELYE 128
GloA COG0346
Catechol 2,3-dioxygenase or related enzyme, vicinal oxygen chelate (VOC) family [Secondary ...
 6-129 3.79e-38

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


Pssm-ID: 440115 [Multi-domain]  Cd Length: 125  Bit Score: 125.49  E-value: 3.79e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499513149   6 TGFHHIAIIVSDYEKSKYFYTQILGAEVIEETYRASRHSYKLDLKFADGSQIELFSFPSSPSrltMPEACGLRHLAFKVK 85
Cdd:COG0346    1 MGLHHVTLRVSDLEASLAFYTDVLGLELVKRTDFGDGGFGHAFLRLGDGTELELFEAPGAAP---APGGGGLHHLAFRVD 77

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 499513149  86 DIEEAVQYLKTQQIECEDIRIDELTGKKFTFFKDPDNLPLELYE 129
Cdd:COG0346   78 DLDAAYARLRAAGVEIEGEPRDRAYGYRSAYFRDPDGNLIELVE 121
Glyoxalase pfam00903
Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;
7-127 1.18e-25

Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;


Pssm-ID: 395724 [Multi-domain]  Cd Length: 121  Bit Score: 93.67  E-value: 1.18e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499513149    7 GFHHIAIIVSDYEKSKYFYTQILGAEVIEETYRASRHSYKLDLKFADGSQIELFSFPSSPSRLTMPEACGLRHLAFKVKD 86
Cdd:pfam00903   1 RIDHVALRVGDLEKSLDFYTDVLGFKLVEETDAGEEGGLRSAFFLAGGRVLELLLNETPPPAAAGFGGHHIAFIAFSVDD 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 499513149   87 IEEAVQYLKTQQIECEDIRIDELTGKKFTFFKDPDNLPLEL 127
Cdd:pfam00903  81 VDAAYDRLKAAGVEIVREPGRHGWGGRYSYFRDPDGNLIEL 121
metmalonyl_epim TIGR03081
methylmalonyl-CoA epimerase; Members of this protein family are the enzyme methylmalonyl-CoA ...
 8-129 1.64e-07

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.


Pssm-ID: 213772 [Multi-domain]  Cd Length: 128  Bit Score: 46.93  E-value: 1.64e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499513149    8 FHHIAIIVSDYEKSKYFYTQILGAEViEETYRASRHSYKLDLKFADGSQIELF---SFPSSPSRLTMPEACGLRHLAFKV 84
Cdd:TIGR03081   2 IDHVGIAVPDLEEAAKFYEDVLGAQV-SEIEELPEQGVKVVFIALGNTKVELLeplGEDSPIAKFLEKNGGGIHHIAIEV 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 499513149   85 KDIEEAVQYLKTQQIECedirIDELT-----GKKFTFF--KDPDNLPLELYE 129
Cdd:TIGR03081  81 DDIEAALETLKEKGVRL----IDEEPrigahGKPVAFLhpKSTGGVLIELEQ 128
 
Name Accession Description Interval E-value
VOC_Bs_YwkD_like cd08352
vicinal oxygen chelate (VOC) family protein Bacillus subtilis YwkD and similar proteins; ...
 6-129 3.39e-70

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.


Pssm-ID: 319940 [Multi-domain]  Cd Length: 123  Bit Score: 206.63  E-value: 3.39e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499513149   6 TGFHHIAIIVSDYEKSKYFYTQILGAEVIEETYRASRHSYKLDLKFaDGSQIELFSFPSSPSRLTMPEACGLRHLAFKVK 85
Cdd:cd08352    1 KKIHHIAIICSDYEKSKDFYVDKLGFEIIREHYRPERNDIKLDLAL-GGYQLELFIKPDAPARPSYPEALGLRHLAFKVE 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 499513149  86 DIEEAVQYLKTQQIECEDIRIDELTGKKFTFFKDPDNLPLELYE 129
Cdd:cd08352   80 DVEATVAELKSLGIETEPIRVDDFTGKKFTFFFDPDGLPLELYE 123
PRK11478 PRK11478
VOC family protein;
9-129 2.89e-55

VOC family protein;


Pssm-ID: 183156 [Multi-domain]  Cd Length: 129  Bit Score: 168.92  E-value: 2.89e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499513149   9 HHIAIIVSDYEKSKYFYTQILGAEVIEETYRASRHSYKLDLKFADGSQIELFSFPSSPSRLTMPEACGLRHLAFKVKDIE 88
Cdd:PRK11478   8 HHIAIIATDYAVSKAFYCDILGFTLQSEVYREARDSWKGDLALNGQYVIELFSFPFPPERPSRPEACGLRHLAFSVDDID 87

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 499513149  89 EAVQYLKTQQIECEDIRIDELTGKKFTFFKDPDNLPLELYE 129
Cdd:PRK11478  88 AAVAHLESHNVKCEAIRVDPYTQKRFTFFNDPDGLPLELYE 128
GloA COG0346
Catechol 2,3-dioxygenase or related enzyme, vicinal oxygen chelate (VOC) family [Secondary ...
 6-129 3.79e-38

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


Pssm-ID: 440115 [Multi-domain]  Cd Length: 125  Bit Score: 125.49  E-value: 3.79e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499513149   6 TGFHHIAIIVSDYEKSKYFYTQILGAEVIEETYRASRHSYKLDLKFADGSQIELFSFPSSPSrltMPEACGLRHLAFKVK 85
Cdd:COG0346    1 MGLHHVTLRVSDLEASLAFYTDVLGLELVKRTDFGDGGFGHAFLRLGDGTELELFEAPGAAP---APGGGGLHHLAFRVD 77

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 499513149  86 DIEEAVQYLKTQQIECEDIRIDELTGKKFTFFKDPDNLPLELYE 129
Cdd:COG0346   78 DLDAAYARLRAAGVEIEGEPRDRAYGYRSAYFRDPDGNLIELVE 121
Glyoxalase pfam00903
Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;
7-127 1.18e-25

Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;


Pssm-ID: 395724 [Multi-domain]  Cd Length: 121  Bit Score: 93.67  E-value: 1.18e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499513149    7 GFHHIAIIVSDYEKSKYFYTQILGAEVIEETYRASRHSYKLDLKFADGSQIELFSFPSSPSRLTMPEACGLRHLAFKVKD 86
Cdd:pfam00903   1 RIDHVALRVGDLEKSLDFYTDVLGFKLVEETDAGEEGGLRSAFFLAGGRVLELLLNETPPPAAAGFGGHHIAFIAFSVDD 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 499513149   87 IEEAVQYLKTQQIECEDIRIDELTGKKFTFFKDPDNLPLEL 127
Cdd:pfam00903  81 VDAAYDRLKAAGVEIVREPGRHGWGGRYSYFRDPDGNLIEL 121
CatE COG2514
Catechol-2,3-dioxygenase [Secondary metabolites biosynthesis, transport and catabolism];
6-128 9.10e-19

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


Pssm-ID: 442004 [Multi-domain]  Cd Length: 141  Bit Score: 76.54  E-value: 9.10e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499513149   6 TGFHHIAIIVSDYEKSKYFYTQILGAEVIEETyrASRHSYKLDlkfADGSQIELFSFPSSPSRltmPEACGLRHLAFKV- 84
Cdd:COG2514    2 TRLGHVTLRVRDLERSAAFYTDVLGLEVVERE--GGRVYLRAD---GGEHLLVLEEAPGAPPR---PGAAGLDHVAFRVp 73

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 499513149  85 --KDIEEAVQYLKTQQIECEDIrIDELTGKKFtFFKDPDNLPLELY 128
Cdd:COG2514   74 srADLDAALARLAAAGVPVEGA-VDHGVGESL-YFRDPDGNLIELY 117
VOC cd06587
vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate (VOC) superfamily is composed ...
 10-127 4.87e-16

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.


Pssm-ID: 319898 [Multi-domain]  Cd Length: 112  Bit Score: 68.71  E-value: 4.87e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499513149  10 HIAIIVSDYEKSKYFYTQILGAEVIEETYRASRHsyklDLKFADGSQIELFSFPSSPSrltmPEACGLRHLAFKVKDIEE 89
Cdd:cd06587    1 HVALRVPDLDASVAFYEEVLGFEVVSRNEGGGFA----FLRLGPGLRLALLEGPEPER----PGGGGLFHLAFEVDDVDE 72

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 499513149  90 AVQYLKTQQIECEDIRIDELT--GKKFTFFKDPDNLPLEL 127
Cdd:cd06587   73 VDERLREAGAEGELVAPPVDDpwGGRSFYFRDPDGNLIEF 112
VOC_ShValD_like cd16361
vicinal oxygen chelate (VOC) family protein similar to Streptomyces hygroscopicus ValD protein; ...
 7-128 2.76e-15

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.


Pssm-ID: 319968  Cd Length: 150  Bit Score: 67.74  E-value: 2.76e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499513149   7 GFHHIAIIVSDYEKSKYFYTQILGAEVIeetYR----------ASRHSYKLD-----------LKFADGSQIELFSFPSS 65
Cdd:cd16361    1 GVNHVGITVPDLDAAVEFYTDVLGAEVV---YRstplaegdrgGGEMRAAGFvpgfarariamLRLGPGPGIELFEYKGP 77

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499513149  66 PSRLTMPEAC--GLRHLAFKVKDIEEAVQYLKTQ------QIEcEDIRIDELTGKKFTFFKDPDNLPLELY 128
Cdd:cd16361   78 EQRAPVPRNSdvGIFHFALQVDDVEAAAERLAAAggkvlmGPR-EIPDGGPGKGNRMVYLRDPWGTLIELV 147
VOC_like cd07245
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 8-127 5.35e-15

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.


Pssm-ID: 319909 [Multi-domain]  Cd Length: 117  Bit Score: 66.19  E-value: 5.35e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499513149   8 FHHIAIIVSDYEKSKYFYTQILGAEVIEetyraSRHSYKLD---LKFADGSQIELfSFPSSPSRLTMPEACG-LRHLAFK 83
Cdd:cd07245    1 LDHVALACPDLERARRFYTDVLGLEEVP-----RPPFLKFGgawLYLGGGQQIHL-VVEQNPSELPRPEHPGrDRHPSFS 74

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 499513149  84 VKDIEEAVQYLKTQQIECEDiRIDELTGKKFTFFKDPDNLPLEL 127
Cdd:cd07245   75 VPDLDALKQRLKEAGIPYTE-STSPGGGVTQLFFRDPDGNRLEF 117
MMCE cd07249
Methylmalonyl-CoA epimerase (MMCE); MMCE, also called methylmalonyl-CoA racemase (EC 5.1.99.1) ...
 9-117 7.58e-13

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.


Pssm-ID: 319912 [Multi-domain]  Cd Length: 127  Bit Score: 60.67  E-value: 7.58e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499513149   9 HHIAIIVSDYEKSKYFYTQILGAEVIEETYRASrHSYKLDLKFADGSQIEL---FSFPSSPSRLTMPEACGLRHLAFKVK 85
Cdd:cd07249    2 DHIGIAVPDLDEALKFYEDVLGVKVSEPEELEE-QGVRVAFLELGNTQIELlepLGEDSPIAKFLDKKGGGLHHIAFEVD 80

                         90       100       110
                 ....*....|....*....|....*....|...
gi 499513149  86 DIEEAVQYLKTQQIEC-EDIRIDELTGKKFTFF 117
Cdd:cd07249   81 DIDAAVEELKAQGVRLlSEGPRIGAHGKRVAFL 113
VOC_like cd08353
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 8-100 3.78e-09

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.


Pssm-ID: 319941  Cd Length: 142  Bit Score: 51.42  E-value: 3.78e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499513149   8 FHHIAIIVSDYEKSKYFYTQiLGAEVIEETYRASR---HSYKLD--------LKFADG-SQIELFSF----PSSPSRLTM 71
Cdd:cd08353    4 MDHVGIVVEDLDAAIAFFTE-LGLELEGRMTVEGEwadRVVGLDgvrveiamLRTPDGhGRLELSKFltpaAIPGHRPAP 82

                         90       100
                 ....*....|....*....|....*....
gi 499513149  72 PEACGLRHLAFKVKDIEEAVQYLKTQQIE 100
Cdd:cd08353   83 ANALGLRHVAFAVDDIDAVVARLRKHGAE 111
VOC COG3324
Lactoylglutathione lyase-related enzyme, vicinal oxygen chelate (VOC) family [General function ...
 6-129 2.44e-08

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


Pssm-ID: 442553 [Multi-domain]  Cd Length: 119  Bit Score: 48.86  E-value: 2.44e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499513149   6 TGFHHIAIIVSDYEKSKYFYTQILGAEVIEETYRASRHSYkldLKFADGSQIELFSFPSSPSRltmpeacGLRHLAFKVK 85
Cdd:COG3324    3 GTIVWVELPVDDLERAKAFYEEVFGWTFEDDAGPGGDYAE---FDTDGGQVGGLMPGAEEPGG-------PGWLLYFAVD 72

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 499513149  86 DIEEAVQYLKTQQIECEDIRIDELTGKKFTFFKDPDNLPLELYE 129
Cdd:COG3324   73 DLDAAVARVEAAGGTVLRPPTDIPPWGRFAVFRDPEGNRFGLWQ 116
Glyoxalase_4 pfam13669
Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;
9-95 5.42e-08

Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;


Pssm-ID: 463951 [Multi-domain]  Cd Length: 109  Bit Score: 47.66  E-value: 5.42e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499513149    9 HHIAIIVSDYEKSKYFYTQILGAEViEETYRASRHSYKLD-LKFADGS-QIELFSfPSSPSrlTMPEAC--GLRHLAFKV 84
Cdd:pfam13669   1 HHVGIAVPDLDRALALWGALLGLGP-EGDYRSEPQNVDLAfALLGDGPvEVELIQ-PLDGD--SPLARHgpGLHHLAYWV 76

                          90
                  ....*....|.
gi 499513149   85 KDIEEAVQYLK 95
Cdd:pfam13669  77 DDLDAAVARLL 87
metmalonyl_epim TIGR03081
methylmalonyl-CoA epimerase; Members of this protein family are the enzyme methylmalonyl-CoA ...
 8-129 1.64e-07

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.


Pssm-ID: 213772 [Multi-domain]  Cd Length: 128  Bit Score: 46.93  E-value: 1.64e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499513149    8 FHHIAIIVSDYEKSKYFYTQILGAEViEETYRASRHSYKLDLKFADGSQIELF---SFPSSPSRLTMPEACGLRHLAFKV 84
Cdd:TIGR03081   2 IDHVGIAVPDLEEAAKFYEDVLGAQV-SEIEELPEQGVKVVFIALGNTKVELLeplGEDSPIAKFLEKNGGGIHHIAIEV 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 499513149   85 KDIEEAVQYLKTQQIECedirIDELT-----GKKFTFF--KDPDNLPLELYE 129
Cdd:TIGR03081  81 DDIEAALETLKEKGVRL----IDEEPrigahGKPVAFLhpKSTGGVLIELEQ 128
HPCD_N_class_II cd07266
N-terminal domain of 3,4-dihydroxyphenylacetate 2,3-dioxygenase (HPCD); This subfamily ...
 10-128 1.67e-07

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.


Pssm-ID: 319927  Cd Length: 118  Bit Score: 46.63  E-value: 1.67e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499513149  10 HIAIIVSDYEKSKYFYTQILGAEVIEEtyrasrhsykldlkfaDGSQIELFS---FPSSPSRLTMPEACGLRHLAFKV-- 84
Cdd:cd07266    7 HAELVVTDLAASREFYVDTLGLHVTDE----------------DDNAIYLRGveeFIHHTLVLRKAPEAAVGHLGFRVrd 70

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 499513149  85 -KDIEEAVQYLKTQQIECEdiRIDELTGKKFTFFKDPDNLPLELY 128
Cdd:cd07266   71 eADLDKAAAFYKELGLPTE--WREEPGQGRTLRVEDPFGFPIEFY 113
VOC_BsYqjT cd07242
vicinal oxygen chelate (VOC) family protein similar to Bacillus subtilis YqjT; The vicinal ...
 7-127 8.76e-07

vicinal oxygen chelate (VOC) family protein similar to Bacillus subtilis YqjT; 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.


Pssm-ID: 319906  Cd Length: 126  Bit Score: 44.79  E-value: 8.76e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499513149   7 GFHHIAIIVSDYEKSKYFYTQILGAEVIEETYRASRHSYKLDlkfaDGSQIELFSFPsspsRLTMPE----ACGLRHLAF 82
Cdd:cd07242    1 GVSHVELAVSDLHRSFKWFEWILGLGWKEYDTWSFGPSWKLS----GGSLLVVQQTD----EFATPEfdraRVGLNHLAF 72

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 499513149  83 KVKDIEEaVQYLKTQQIECEDIRI-------DELTGKKFTFFKDPDNLPLEL 127
Cdd:cd07242   73 HAESREA-VDELTEKLAKIGGVRTygdrhpfAGGPPHYAAFCEDPDGIKLEL 123
VOC_like cd07264
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 10-129 9.85e-07

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.


Pssm-ID: 319925 [Multi-domain]  Cd Length: 118  Bit Score: 44.63  E-value: 9.85e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499513149  10 HIAIIVSDYEKSKYFYTQILGAEVieETYRASRHSYKLDLkfaDGSQIELFSFPSsPSRLTMPEACG-LRHLAFKVKDIE 88
Cdd:cd07264    3 YIVLYVDDFAASLRFYRDVLGLPP--RFLHEEGEYAEFDT---GETKLALFSRKE-MARSGGPDRRGsAFELGFEVDDVE 76

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 499513149  89 EAVQYLKTQQIECEDIRIDELTGKKFTFFKDPDNLPLELYE 129
Cdd:cd07264   77 ATVEELVERGAEFVREPANKPWGQTVAYVRDPDGNLIEICE 117
ED_TypeI_classII_N cd16360
N-terminal domain of type I, class II extradiol dioxygenases; This family contains the ...
 10-128 2.13e-06

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.


Pssm-ID: 319967  Cd Length: 111  Bit Score: 43.46  E-value: 2.13e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499513149  10 HIAIIVSDYEKSKYFYTQILGaevIEETYRasrhsykldlkfaDGSQIELFSFPSSPSRLTMPEAC--GLRHLAFKVKDi 87
Cdd:cd16360    1 YAELGVPDLEKALEFYTDVLG---LQVAKR-------------DGNSVYLRGYEDEHHSLVLYEAPeaGLKHFAFEVAS- 63

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 499513149  88 EEAVQYLKT--QQIECEDIRI--DELTGKKFTF-FKDPDNLPLELY 128
Cdd:cd16360   64 EEDLERAAAslTALGCDVTWGpdGEVPGGGKGFrFQDPSGHLLELF 109
BphC-JF8_N_like cd09013
N-terminal, non-catalytic, domain of BphC_JF8, (2,3-dihydroxybiphenyl 1,2-dioxygenase) from ...
 8-128 5.93e-06

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.


Pssm-ID: 319955  Cd Length: 121  Bit Score: 42.72  E-value: 5.93e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499513149   8 FHHIAIIVSDYEKSKYFYTQILGaevIEETYRASRHSYkldLK-FADGSQIELfsfpsspsRLTMPEACGLRHLAFKVK- 85
Cdd:cd09013    7 LAHVELLTPKPEESLWFFTDVLG---LEETHREGQSVY---LRaWGDWEHHTL--------KLTESPEAGLGHIAWRASs 72

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 499513149  86 --DIEEAVQYLKTQQIECEDIRIDELTGKKFTfFKDPDNLPLELY 128
Cdd:cd09013   73 peALERRVAALEASGVGIGWIDGDLGQGPAYR-FQSPDGHPMEIY 116
VOC_BsYyaH cd07241
vicinal oxygen chelate (VOC) family protein similar to Bacillus subtilis YyaH; The vicinal ...
 9-97 6.07e-06

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.


Pssm-ID: 319905  Cd Length: 125  Bit Score: 42.78  E-value: 6.07e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499513149   9 HHIAIIVSDYEKSKYFYTQILGAEV--IEETYRASRHSYKldLKFADGSQIELFSFPSSPSRLTMPEACGLRHLAFKV-- 84
Cdd:cd07241    3 EHVALWTNDLERMKDFYVKYFGAESndIYHNKKKGFRSYF--LTFDSGARLELMSRPDVTDPDKEVERTGLAHIAFSVgs 80

                         90
                 ....*....|....
gi 499513149  85 -KDIEEAVQYLKTQ 97
Cdd:cd07241   81 kEAVDELTERLRAD 94
VOC_like cd07263
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 10-122 1.05e-05

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


Pssm-ID: 319924 [Multi-domain]  Cd Length: 120  Bit Score: 41.90  E-value: 1.05e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499513149  10 HIAIIVSDYEKSKYFYTQILGAEVIEETYRASRHSYKLDLKFADGSQIELF--SFPSSPSRlTMPEACGLRHLAFKVKDI 87
Cdd:cd07263    1 QVMLYVDDQDKALDFYVEKLGFEVVEDVPMGGMRWVTVAPPGSPGTSLLLEpkAHPAQMPQ-SPEAAGGTPGILLATDDI 79

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 499513149  88 EEAVQYLKTQQIECEDIrIDELTGKKFTFFKDPDN 122
Cdd:cd07263   80 DATYERLTAAGVTFVQE-PTQMGGGRVANFRDPDG 113
Fosfomycin_RP cd08345
Fosfomycin resistant protein; This family contains three types of fosfomycin resistant protein. ...
 10-128 2.03e-05

Fosfomycin resistant protein; This family contains three types of fosfomycin resistant protein. Fosfomycin inhibits the enzyme UDP-N-acetylglucosamine-3-enolpyruvyltransferase (MurA), which catalyzes the first committed step in bacterial cell wall biosynthesis. The three types of fosfomycin resistance proteins, employ different mechanisms to render fosfomycin [(1R,2S)-epoxypropylphosphonic acid] inactive. FosB catalyzes the addition of L-cysteine to the epoxide ring of fosfomycin. FosX catalyzes the addition of a water molecule to the C1 position of the antibiotic with inversion of configuration at C1. FosA catalyzes the addition of glutathione to the antibiotic fosfomycin, making it inactive. Catalytic activities of both FosX and FosA are Mn(II)-dependent, but FosB is activated by Mg(II). Fosfomycin resistant proteins are evolutionarily related to glyoxalase I and type I extradiol dioxygenases.


Pssm-ID: 319933  Cd Length: 118  Bit Score: 41.00  E-value: 2.03e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499513149  10 HIAIIVSDYEKSKYFYTQILGAeviEETYRASRHSYKLD-LKFAD--GSQIELFSFPSSPSRltmpeacGLRHLAFKVKD 86
Cdd:cd08345    1 HITLIVRDLEKSTAFLQDIFGA---REVYSSGDKTFSLSkEKFFLlgGLWIALMEGESLQER-------SYTHIAFQIQS 70

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 499513149  87 iEEAVQYlkTQQIECEDIRI------DELTGKKFtFFKDPDNLPLELY 128
Cdd:cd08345   71 -EDFDRY--AERLGALGVEMrpprprVEGEGRSI-YFYDPDNHLFELH 114
GLOD5 cd07253
Human glyoxalase domain-containing protein 5 and similar proteins; Uncharacterized subfamily ...
 10-123 5.46e-05

Human glyoxalase domain-containing protein 5 and similar proteins; Uncharacterized subfamily of VOC family contains human glyoxalase domain-containing protein 5 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.


Pssm-ID: 319916 [Multi-domain]  Cd Length: 123  Bit Score: 39.90  E-value: 5.46e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499513149  10 HIAIIVSDYEKSKYFYTQILGAEVIeeTYRASRHSykldLKFadGSQI--------ELFSFPSSPSRltmpeacGLRHLA 81
Cdd:cd07253    6 HLVLTVKDIERTIDFYTKVLGMTVV--TFKEGRKA----LRF--GNQKinlhqkgkEFEPKASAPTP-------GSADLC 70

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 499513149  82 FKV-KDIEEAVQYLKTQQIECEDiRIDELTGKKFT----FFKDPD-NL 123
Cdd:cd07253   71 FITeTPIDEVLEHLEACGVTIEE-GPVKRTGALGPilsiYFRDPDgNL 117
BphC5-RrK37_N_like cd08362
N-terminal, non-catalytic, domain of BphC5 (2,3-dihydroxybiphenyl 1,2-dioxygenase) from ...
 6-62 6.44e-05

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).


Pssm-ID: 319950 [Multi-domain]  Cd Length: 120  Bit Score: 39.93  E-value: 6.44e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499513149   6 TGFHHIAIIVSDYEKSKYFYTQILGAEVIEETYRAS------RHSYKLDLKFADGSQIELFSF 62
Cdd:cd08362    2 THLRYVALGVPDLAAEREFYTEVWGLEEVAEDDDVVylraegSEHHVLRLRQSDENRLDLIAF 64
VOC_BsCatE_like_N cd07255
N-terminal of Bacillus subtilis CatE like protein; Uncharacterized subfamily of VOC ...
 6-89 7.13e-04

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.


Pssm-ID: 319918  Cd Length: 124  Bit Score: 36.91  E-value: 7.13e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499513149   6 TGFHHIAIIVSDYEKSKYFYTQILGAEVIEETyrASRhsykldLKFADGSQIELFSFPSSPS-RLTMPEACGLRHLAFKV 84
Cdd:cd07255    1 TRIGRVTLKVADLERQSAFYQNVIGLSVLKQN--ASR------AYLGVDGKQVLLVLEAIPDaVLAPRSTTGLYHFAILL 72


                 ....*
gi 499513149  85 KDIEE 89
Cdd:cd07255   73 PDRKA 77
FosX cd08364
fosfomycin resistant protein subfamily FosX; This subfamily family contains FosX, a fosfomycin ...
 5-128 8.56e-04

fosfomycin resistant protein subfamily FosX; This subfamily family contains FosX, a fosfomycin resistant protein. FosX is a Mn(II)-dependent fosfomycin-specific epoxide hydrolase. Fosfomycin inhibits the enzyme UDP-Nacetylglucosamine-3-enolpyruvyltransferase (MurA), which catalyzes the first committed step in bacterial cell wall biosynthesis. FosX catalyzes the addition of a water molecule to the C1 position of the antibiotic with inversion of the configuration at C1 in the presence of Mn(II). The hydrated fosfomycin loses the inhibition activity. FosX is evolutionarily related to glyoxalase I and type I extradiol dioxygenases.


Pssm-ID: 319952  Cd Length: 130  Bit Score: 36.87  E-value: 8.56e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499513149   5 FTGFHHIAIIVSDYEKSKYFYTQILGAEVI----EETYRASRHSYkldlkFADGSQ-IELFSFPSSPSRltmpeacGLRH 79
Cdd:cd08364    1 IEGISHITFIVKDLDRTAAFLTEIFGAEEVydsgAETFSLSPEKF-----FLIGGLwIAIMEGEPLLER-------SYNH 68

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 499513149  80 LAFKVK--DIEEAVQYLKTQQIECEDIRiDELTGKKFT-FFKDPDNLPLELY 128
Cdd:cd08364   69 IAFKVSegDLDEYRARIKKLGLEIRPPR-SRVQGEGRSlYFYDFDNHLFELH 119
BphC1-RGP6_C_like cd07237
C-terminal domain of 2,3-dihydroxybiphenyl 1,2-dioxygenase; This subfamily contains the ...
 7-89 1.33e-03

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.


Pssm-ID: 319902  Cd Length: 153  Bit Score: 36.48  E-value: 1.33e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499513149   7 GFHHIAIIVSDYEKSKYFYTQILGAevieetyrasRHSYKLDLKFADGSQIELFSFPSSPSRLT-----MPEACGLRHLA 81
Cdd:cd07237    9 GLGHVVLIVPDVDEALAFYTDVLGF----------RLSDEIRIPLPPGVTARLHFLHCNGRHHSlafgaGPGPKRLHHLM 78


                 ....*...
gi 499513149  82 FKVKDIEE 89
Cdd:cd07237   79 LEVTSLDD 86
VOC_like cd08357
uncharacterized subfamily of vicinal oxygen chelate (VOC) familyprotein, glyoxalase I, and ...
 9-126 1.65e-03

uncharacterized subfamily of vicinal oxygen chelate (VOC) familyprotein, glyoxalase I, and type I ring-cleaving dioxygenases; 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.


Pssm-ID: 319945 [Multi-domain]  Cd Length: 124  Bit Score: 36.21  E-value: 1.65e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499513149   9 HHIAIIVSDYEKSKYFYTQILGAevieetyRASRHSYK-LDLKFAdGSQI---ELFSFPSSPSRLTMPEACGLRH--LAF 82
Cdd:cd08357    1 FHLAIPVRDLEAARDFYGDVLGC-------PEGRSSETwIDFNFF-GHQVvahLVPNYASTSTNAVDGHSVPVPHfgLAL 72

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 499513149  83 KVKDIEEAVQYLKTQQIECE---DIRIDELTGKKFT-FFKDPDNLPLE 126
Cdd:cd08357   73 TVDDFDALAERLKAAGVKFYiepYVRFEGEPGEQWTmFLLDPSGNALE 120
FosA cd07244
fosfomycin resistant protein subfamily FosA; This subfamily family contains FosA, a fosfomycin ...
 7-30 8.32e-03

fosfomycin resistant protein subfamily FosA; This subfamily family contains FosA, a fosfomycin resistant protein. FosA is a Mn(II) and K(+)-dependent glutathione transferase. Fosfomycin inhibits the enzyme UDP-N-acetylglucosamine-3-enolpyruvyltransferase (MurA), which catalyzes the first committed step in bacterial cell wall biosynthesis. FosA, catalyzes the addition of glutathione to the antibiotic fosfomycin, (1R,2S)-epoxypropylphosphonic acid, making it inactive. FosA is a Mn(II) dependent enzyme. It is evolutionarily related to glyoxalase I and type I extradiol dioxygenases.


Pssm-ID: 319908 [Multi-domain]  Cd Length: 121  Bit Score: 34.18  E-value: 8.32e-03
                         10        20
                 ....*....|....*....|....
gi 499513149   7 GFHHIAIIVSDYEKSKYFYTQILG 30
Cdd:cd07244    1 GINHITLAVSDLERSLAFYVDLLG 24
ED_TypeI_classII_C cd08343
C-terminal domain of type I, class II extradiol dioxygenases, catalytic domain; This family ...
 10-128 9.66e-03

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.


Pssm-ID: 319931  Cd Length: 132  Bit Score: 33.83  E-value: 9.66e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499513149  10 HIAIIVSDYEKSKYFYTQILGAEVIEETY----------RASRHSYKLDLKFADGSqielfsfpsspsrltmpeACGLRH 79
Cdd:cd08343    2 HVVLCSPDVEASRDFYTDVLGFRVSDRIVdpgvdggaflHCDRGTDHHTVALAGGP------------------HPGLHH 63

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 499513149  80 LAFKVKDIEE---AVQYLKTQqieceDIRID------ELTGKKFTFFKDPDNLPLELY 128
Cdd:cd08343   64 VAFEVHDLDDvgrGHDRLREK-----GYKIEwgpgrhGLGSQVFDYWFDPSGNRVEYY 116
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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