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Conserved domains on  [gi|446823847|ref|WP_000901103|]
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MULTISPECIES: VOC family protein [Escherichia]

Protein Classification

VOC family protein( domain architecture ID 10793579)

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
PRK11478 PRK11478
VOC family protein;
1-129 1.07e-102

VOC family protein;


:

Pssm-ID: 183156 [Multi-domain]  Cd Length: 129  Bit Score: 288.72  E-value: 1.07e-102
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446823847   1 MLGLKQVHHIAIIATDYAVSKAFYCDILGFTLQSEVYREERDSWKGDLALNGQYVIELFSFPFPPERPSRPEACGLRHLA 80
Cdd:PRK11478   1 MLGLKQVHHIAIIATDYAVSKAFYCDILGFTLQSEVYREARDSWKGDLALNGQYVIELFSFPFPPERPSRPEACGLRHLA 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 446823847  81 FSVDDIDAAVAHLESHNVKCEAIRVDPYTQKRFTFFNDPDGLPLELYEQ 129
Cdd:PRK11478  81 FSVDDIDAAVAHLESHNVKCEAIRVDPYTQKRFTFFNDPDGLPLELYEQ 129
 
Name Accession Description Interval E-value
PRK11478 PRK11478
VOC family protein;
1-129 1.07e-102

VOC family protein;


Pssm-ID: 183156 [Multi-domain]  Cd Length: 129  Bit Score: 288.72  E-value: 1.07e-102
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446823847   1 MLGLKQVHHIAIIATDYAVSKAFYCDILGFTLQSEVYREERDSWKGDLALNGQYVIELFSFPFPPERPSRPEACGLRHLA 80
Cdd:PRK11478   1 MLGLKQVHHIAIIATDYAVSKAFYCDILGFTLQSEVYREARDSWKGDLALNGQYVIELFSFPFPPERPSRPEACGLRHLA 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 446823847  81 FSVDDIDAAVAHLESHNVKCEAIRVDPYTQKRFTFFNDPDGLPLELYEQ 129
Cdd:PRK11478  81 FSVDDIDAAVAHLESHNVKCEAIRVDPYTQKRFTFFNDPDGLPLELYEQ 129
VOC_Bs_YwkD_like cd08352
vicinal oxygen chelate (VOC) family protein Bacillus subtilis YwkD and similar proteins; ...
 5-128 3.48e-77

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: 223.96  E-value: 3.48e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446823847   5 KQVHHIAIIATDYAVSKAFYCDILGFTLQSEVYREERDSWKGDLALnGQYVIELFSFPFPPERPSRPEACGLRHLAFSVD 84
Cdd:cd08352    1 KKIHHIAIICSDYEKSKDFYVDKLGFEIIREHYRPERNDIKLDLAL-GGYQLELFIKPDAPARPSYPEALGLRHLAFKVE 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 446823847  85 DIDAAVAHLESHNVKCEAIRVDPYTQKRFTFFNDPDGLPLELYE 128
Cdd:cd08352   80 DVEATVAELKSLGIETEPIRVDDFTGKKFTFFFDPDGLPLELYE 123
GloA COG0346
Catechol 2,3-dioxygenase or related enzyme, vicinal oxygen chelate (VOC) family [Secondary ...
 7-128 2.76e-34

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: 115.47  E-value: 2.76e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446823847   7 VHHIAIIATDYAVSKAFYCDILGFTLQSEVYREERDSWKGDLALNGQYVIELFSFPfppERPSRPEACGLRHLAFSVDDI 86
Cdd:COG0346    3 LHHVTLRVSDLEASLAFYTDVLGLELVKRTDFGDGGFGHAFLRLGDGTELELFEAP---GAAPAPGGGGLHHLAFRVDDL 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 446823847  87 DAAVAHLESHNVKCEAIRVDPYTQKRFTFFNDPDGLPLELYE 128
Cdd:COG0346   80 DAAYARLRAAGVEIEGEPRDRAYGYRSAYFRDPDGNLIELVE 121
Glyoxalase pfam00903
Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;
6-126 8.66e-33

Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;


Pssm-ID: 395724 [Multi-domain]  Cd Length: 121  Bit Score: 111.39  E-value: 8.66e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446823847    6 QVHHIAIIATDYAVSKAFYCDILGFTLQSEVYREERDSWKGDLALNGQYVIELFSFPFPPERPSRPEACGLRHLAFSVDD 85
Cdd:pfam00903   1 RIDHVALRVGDLEKSLDFYTDVLGFKLVEETDAGEEGGLRSAFFLAGGRVLELLLNETPPPAAAGFGGHHIAFIAFSVDD 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 446823847   86 IDAAVAHLESHNVKCEAIRVDPYTQKRFTFFNDPDGLPLEL 126
Cdd:pfam00903  81 VDAAYDRLKAAGVEIVREPGRHGWGGRYSYFRDPDGNLIEL 121
metmalonyl_epim TIGR03081
methylmalonyl-CoA epimerase; Members of this protein family are the enzyme methylmalonyl-CoA ...
 7-100 8.21e-04

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: 36.92  E-value: 8.21e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446823847    7 VHHIAIIATDYAVSKAFYCDILGFTLQSEVYREERDSWKGDLALnGQYVIELFSfPFPPERP------SRPEacGLRHLA 80
Cdd:TIGR03081   2 IDHVGIAVPDLEEAAKFYEDVLGAQVSEIEELPEQGVKVVFIAL-GNTKVELLE-PLGEDSPiakfleKNGG--GIHHIA 77

                          90       100
                  ....*....|....*....|
gi 446823847   81 FSVDDIDAAVAHLESHNVKC 100
Cdd:TIGR03081  78 IEVDDIEAALETLKEKGVRL 97
 
Name Accession Description Interval E-value
PRK11478 PRK11478
VOC family protein;
1-129 1.07e-102

VOC family protein;


Pssm-ID: 183156 [Multi-domain]  Cd Length: 129  Bit Score: 288.72  E-value: 1.07e-102
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446823847   1 MLGLKQVHHIAIIATDYAVSKAFYCDILGFTLQSEVYREERDSWKGDLALNGQYVIELFSFPFPPERPSRPEACGLRHLA 80
Cdd:PRK11478   1 MLGLKQVHHIAIIATDYAVSKAFYCDILGFTLQSEVYREARDSWKGDLALNGQYVIELFSFPFPPERPSRPEACGLRHLA 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 446823847  81 FSVDDIDAAVAHLESHNVKCEAIRVDPYTQKRFTFFNDPDGLPLELYEQ 129
Cdd:PRK11478  81 FSVDDIDAAVAHLESHNVKCEAIRVDPYTQKRFTFFNDPDGLPLELYEQ 129
VOC_Bs_YwkD_like cd08352
vicinal oxygen chelate (VOC) family protein Bacillus subtilis YwkD and similar proteins; ...
 5-128 3.48e-77

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: 223.96  E-value: 3.48e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446823847   5 KQVHHIAIIATDYAVSKAFYCDILGFTLQSEVYREERDSWKGDLALnGQYVIELFSFPFPPERPSRPEACGLRHLAFSVD 84
Cdd:cd08352    1 KKIHHIAIICSDYEKSKDFYVDKLGFEIIREHYRPERNDIKLDLAL-GGYQLELFIKPDAPARPSYPEALGLRHLAFKVE 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 446823847  85 DIDAAVAHLESHNVKCEAIRVDPYTQKRFTFFNDPDGLPLELYE 128
Cdd:cd08352   80 DVEATVAELKSLGIETEPIRVDDFTGKKFTFFFDPDGLPLELYE 123
GloA COG0346
Catechol 2,3-dioxygenase or related enzyme, vicinal oxygen chelate (VOC) family [Secondary ...
 7-128 2.76e-34

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: 115.47  E-value: 2.76e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446823847   7 VHHIAIIATDYAVSKAFYCDILGFTLQSEVYREERDSWKGDLALNGQYVIELFSFPfppERPSRPEACGLRHLAFSVDDI 86
Cdd:COG0346    3 LHHVTLRVSDLEASLAFYTDVLGLELVKRTDFGDGGFGHAFLRLGDGTELELFEAP---GAAPAPGGGGLHHLAFRVDDL 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 446823847  87 DAAVAHLESHNVKCEAIRVDPYTQKRFTFFNDPDGLPLELYE 128
Cdd:COG0346   80 DAAYARLRAAGVEIEGEPRDRAYGYRSAYFRDPDGNLIELVE 121
Glyoxalase pfam00903
Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;
6-126 8.66e-33

Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;


Pssm-ID: 395724 [Multi-domain]  Cd Length: 121  Bit Score: 111.39  E-value: 8.66e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446823847    6 QVHHIAIIATDYAVSKAFYCDILGFTLQSEVYREERDSWKGDLALNGQYVIELFSFPFPPERPSRPEACGLRHLAFSVDD 85
Cdd:pfam00903   1 RIDHVALRVGDLEKSLDFYTDVLGFKLVEETDAGEEGGLRSAFFLAGGRVLELLLNETPPPAAAGFGGHHIAFIAFSVDD 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 446823847   86 IDAAVAHLESHNVKCEAIRVDPYTQKRFTFFNDPDGLPLEL 126
Cdd:pfam00903  81 VDAAYDRLKAAGVEIVREPGRHGWGGRYSYFRDPDGNLIEL 121
CatE COG2514
Catechol-2,3-dioxygenase [Secondary metabolites biosynthesis, transport and catabolism];
4-127 1.17e-19

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


Pssm-ID: 442004 [Multi-domain]  Cd Length: 141  Bit Score: 78.46  E-value: 1.17e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446823847   4 LKQVHHIAIIATDYAVSKAFYCDILGFTlqsEVYREERDSWkgdLALNGQY-VIELFSfpfPPERPSRPEACGLRHLAFS 82
Cdd:COG2514    1 ITRLGHVTLRVRDLERSAAFYTDVLGLE---VVEREGGRVY---LRADGGEhLLVLEE---APGAPPRPGAAGLDHVAFR 71

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 446823847  83 VD---DIDAAVAHLESHNVKCEAIrVDPYTQKRFtFFNDPDGLPLELY 127
Cdd:COG2514   72 VPsraDLDAALARLAAAGVPVEGA-VDHGVGESL-YFRDPDGNLIELY 117
VOC_like cd07245
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 7-126 3.24e-17

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: 71.58  E-value: 3.24e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446823847   7 VHHIAIIATDYAVSKAFYCDILGFTlqsEVYREERDSWKGD-LALNGQYVIELfSFPFPPERPSRPEACG-LRHLAFSVD 84
Cdd:cd07245    1 LDHVALACPDLERARRFYTDVLGLE---EVPRPPFLKFGGAwLYLGGGQQIHL-VVEQNPSELPRPEHPGrDRHPSFSVP 76

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 446823847  85 DIDAAVAHLESHNVKC-EAIRVDPYtQKRFtFFNDPDGLPLEL 126
Cdd:cd07245   77 DLDALKQRLKEAGIPYtESTSPGGG-VTQL-FFRDPDGNRLEF 117
VOC cd06587
vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate (VOC) superfamily is composed ...
 9-126 2.39e-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: 69.48  E-value: 2.39e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446823847   9 HIAIIATDYAVSKAFYCDILGFTLqseVYREERDSWKGdLALNGQYVIELFSFPFPPERPSRpeacGLRHLAFSVDDIDA 88
Cdd:cd06587    1 HVALRVPDLDASVAFYEEVLGFEV---VSRNEGGGFAF-LRLGPGLRLALLEGPEPERPGGG----GLFHLAFEVDDVDE 72

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 446823847  89 AVAHLESHNVKCE---AIRVDPYTQKRFTFFnDPDGLPLEL 126
Cdd:cd06587   73 VDERLREAGAEGElvaPPVDDPWGGRSFYFR-DPDGNLIEF 112
VOC COG3324
Lactoylglutathione lyase-related enzyme, vicinal oxygen chelate (VOC) family [General function ...
 7-128 2.36e-15

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


Pssm-ID: 442553 [Multi-domain]  Cd Length: 119  Bit Score: 66.97  E-value: 2.36e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446823847   7 VHHIAIIATDYAVSKAFYCDILGFTLqsevyrEERDSWKGD---LALNGQYVIELFSFPFPPERPSrpeacglRHLAFSV 83
Cdd:COG3324    5 IVWVELPVDDLERAKAFYEEVFGWTF------EDDAGPGGDyaeFDTDGGQVGGLMPGAEEPGGPG-------WLLYFAV 71

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 446823847  84 DDIDAAVAHLESHNVKceaIRVDPYTQK---RFTFFNDPDGLPLELYE 128
Cdd:COG3324   72 DDLDAAVARVEAAGGT---VLRPPTDIPpwgRFAVFRDPEGNRFGLWQ 116
VOC_ShValD_like cd16361
vicinal oxygen chelate (VOC) family protein similar to Streptomyces hygroscopicus ValD protein; ...
 7-127 1.08e-14

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: 65.82  E-value: 1.08e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446823847   7 VHHIAIIATDYAVSKAFYCDILGFTLqseVYR----EERDSWKGDLALNGQYV-----------------IELFSFPFPP 65
Cdd:cd16361    2 VNHVGITVPDLDAAVEFYTDVLGAEV---VYRstplAEGDRGGGEMRAAGFVPgfarariamlrlgpgpgIELFEYKGPE 78

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446823847  66 ERPSRPEAC--GLRHLAFSVDDIDAAVAHLESHNVKC-----EAIRVDPYTQKRFTFFNDPDGLPLELY 127
Cdd:cd16361   79 QRAPVPRNSdvGIFHFALQVDDVEAAAERLAAAGGKVlmgprEIPDGGPGKGNRMVYLRDPWGTLIELV 147
VOC_like cd08353
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 4-129 2.83e-14

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: 64.52  E-value: 2.83e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446823847   4 LKQVHHIAIIATDYAVSKAFYCDiLGFTLqsevyrEERDSWKGDLA-----LNGQYV-------------IELFSFPFPP 65
Cdd:cd08353    1 IKRMDHVGIVVEDLDAAIAFFTE-LGLEL------EGRMTVEGEWAdrvvgLDGVRVeiamlrtpdghgrLELSKFLTPA 73

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446823847  66 ----ERPSRPEACGLRHLAFSVDDIDAAVAHLESHNvkCEAIR--VDPYTQKRFTFFNDPDGLPLELYEQ 129
Cdd:cd08353   74 aipgHRPAPANALGLRHVAFAVDDIDAVVARLRKHG--AELVGevVQYEDSYRLCYVRGPEGIIVELAEE 141
Glyoxalase_4 pfam13669
Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;
8-100 2.11e-12

Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;


Pssm-ID: 463951 [Multi-domain]  Cd Length: 109  Bit Score: 58.83  E-value: 2.11e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446823847    8 HHIAIIATDYAVSKAFYCDILGFTlQSEVYREERDSWKGDLALNGQ--YVIELFSfPFPPERPSRPEACGLRHLAFSVDD 85
Cdd:pfam13669   1 HHVGIAVPDLDRALALWGALLGLG-PEGDYRSEPQNVDLAFALLGDgpVEVELIQ-PLDGDSPLARHGPGLHHLAYWVDD 78

                          90
                  ....*....|....*
gi 446823847   86 IDAAVAHLESHNVKC 100
Cdd:pfam13669  79 LDAAVARLLDQGYRV 93
VOC_like cd07264
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 9-128 1.61e-08

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: 49.25  E-value: 1.61e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446823847   9 HIAIIATDYAVSKAFYCDILGFTLQSEVyreerDSWKGDLALNGQYVIELFSFPfPPERPSRPEACG-LRHLAFSVDDID 87
Cdd:cd07264    3 YIVLYVDDFAASLRFYRDVLGLPPRFLH-----EEGEYAEFDTGETKLALFSRK-EMARSGGPDRRGsAFELGFEVDDVE 76

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 446823847  88 AAVAHLESHNVK-CEAIRVDPYTQKRFtFFNDPDGLPLELYE 128
Cdd:cd07264   77 ATVEELVERGAEfVREPANKPWGQTVA-YVRDPDGNLIEICE 117
MMCE cd07249
Methylmalonyl-CoA epimerase (MMCE); MMCE, also called methylmalonyl-CoA racemase (EC 5.1.99.1) ...
 7-128 4.77e-08

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: 47.96  E-value: 4.77e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446823847   7 VHHIAIIATDYAVSKAFYCDILGFtlqSEVYREERDSWKGDLAL--NGQYVIEL---FSFPFPPERPSRPEACGLRHLAF 81
Cdd:cd07249    1 LDHIGIAVPDLDEALKFYEDVLGV---KVSEPEELEEQGVRVAFleLGNTQIELlepLGEDSPIAKFLDKKGGGLHHIAF 77

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 446823847  82 SVDDIDAAVAHLESHNVKC-EAIRVDPYTQKRFTFFNDPD--GLPLELYE 128
Cdd:cd07249   78 EVDDIDAAVEELKAQGVRLlSEGPRIGAHGKRVAFLHPKDtgGVLIELVE 127
VOC_BsCatE_like_N cd07255
N-terminal of Bacillus subtilis CatE like protein; Uncharacterized subfamily of VOC ...
 7-127 1.96e-07

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: 46.54  E-value: 1.96e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446823847   7 VHHIAIIATDYAVSKAFYCDILGFTLQsevyreERDSWKGDLALNGQYV-IELFSFPFPPERPsrPEACGLRHLAFSVDD 85
Cdd:cd07255    3 IGRVTLKVADLERQSAFYQNVIGLSVL------KQNASRAYLGVDGKQVlLVLEAIPDAVLAP--RSTTGLYHFAILLPD 74

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 446823847  86 ---IDAAVAHLESHNVK--------CEAIrvdpytqkrftFFNDPDGLPLELY 127
Cdd:cd07255   75 rkaLGRALAHLAEHGPLigaadhgvSEAI-----------YLSDPEGNGIEIY 116
VOC_like cd07263
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 9-121 2.16e-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: 319924 [Multi-domain]  Cd Length: 120  Bit Score: 46.14  E-value: 2.16e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446823847   9 HIAIIATDYAVSKAFYCDILGFTLQSEVYrEERDSWKgDLALNGQYVIELFSFP--FPPERPSRPEACG-LRHLAFSVDD 85
Cdd:cd07263    1 QVMLYVDDQDKALDFYVEKLGFEVVEDVP-MGGMRWV-TVAPPGSPGTSLLLEPkaHPAQMPQSPEAAGgTPGILLATDD 78

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 446823847  86 IDAAVAHLESHNVKCEAIRVDPYTQkRFTFFNDPDG 121
Cdd:cd07263   79 IDATYERLTAAGVTFVQEPTQMGGG-RVANFRDPDG 113
BphC5-RrK37_N_like cd08362
N-terminal, non-catalytic, domain of BphC5 (2,3-dihydroxybiphenyl 1,2-dioxygenase) from ...
 4-126 5.01e-07

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: 45.32  E-value: 5.01e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446823847   4 LKQVHHIAIIATDYAVSKAFYCDILGFTlqsEVYREERDSWkgdLALNGQ--YVIELfsfpfppeRPSrpEACGLRHLAF 81
Cdd:cd08362    1 VTHLRYVALGVPDLAAEREFYTEVWGLE---EVAEDDDVVY---LRAEGSehHVLRL--------RQS--DENRLDLIAF 64

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 446823847  82 SVD---DIDAAVAHLESHNVKC--EAIRVD-PYTQKRFTFFnDPDGLPLEL 126
Cdd:cd08362   65 AAAtraDVDALAARLAAAGVRIlsEPGPLDdPGGGYGFRFF-DPDGRTIEV 114
BLMA_like cd08349
Bleomycin binding protein (BLMA) and similar proteins; BLMA also called Bleomycin resistance ...
 16-121 5.35e-07

Bleomycin binding protein (BLMA) and similar proteins; BLMA also called Bleomycin resistance protein, confers Bm resistance by directly binding to Bm. Bm is a glycopeptide antibiotic produced naturally by actinomycetes. It is a potent anti-cancer drug, which acts as a strong DNA-cutting agent, thereby causing cell death. BLMA is produced by actinomycetes to protect themselves against their own lethal compound. BLMA has two identically-folded subdomains, with the same alpha/beta fold; these two halves have no sequence similarity. BLMAs are dimers and each dimer binds to two Bm molecules at the Bm-binding pockets formed at the dimer interface; two Bm molecules are bound per dimer. BLMA belongs to a conserved domain superfamily that is found in a variety of structurally related metalloproteins, including the bleomycin resistance protein, glyoxalase I, and type I ring-cleaving dioxygenases. As for the larger superfamily, this family contains members with or without domain swapping.


Pssm-ID: 319937 [Multi-domain]  Cd Length: 114  Bit Score: 44.91  E-value: 5.35e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446823847  16 DYAVSKAFYCDILGFTLqseVYREERDSWkGDLALNGqyvIELFSFPFPPERPSRPE-ACGLRhlafsVDDIDAAVAHLE 94
Cdd:cd08349    8 DIDKTLAFYVDVLGFEV---DYERPPPGY-AILSRGG---VELHLFEHPGLDPAGSGvAAYIR-----VEDIDALHAELK 75

                         90       100       110
                 ....*....|....*....|....*....|...
gi 446823847  95 SHNVKCEAI-RVD-----PYTQKRFTfFNDPDG 121
Cdd:cd08349   76 AAGLPLFGIpRITpiedkPWGMREFA-VVDPDG 107
VOC_like cd08357
uncharacterized subfamily of vicinal oxygen chelate (VOC) familyprotein, glyoxalase I, and ...
 8-125 8.96e-07

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: 44.68  E-value: 8.96e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446823847   8 HHIAIIATDYAVSKAFYCDILGFtlqsevyREERDSWKG-DLALNGQYVIELFSFPFPPE--RPSRPEACGLRH--LAFS 82
Cdd:cd08357    1 FHLAIPVRDLEAARDFYGDVLGC-------PEGRSSETWiDFNFFGHQVVAHLVPNYASTstNAVDGHSVPVPHfgLALT 73

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 446823847  83 VDDIDAAVAHLESHNVKCEairVDPYT--------QKRFtFFNDPDGLPLE 125
Cdd:cd08357   74 VDDFDALAERLKAAGVKFY---IEPYVrfegepgeQWTM-FLLDPSGNALE 120
HPCD_N_class_II cd07266
N-terminal domain of 3,4-dihydroxyphenylacetate 2,3-dioxygenase (HPCD); This subfamily ...
 9-127 3.73e-06

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: 42.78  E-value: 3.73e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446823847   9 HIAIIATDYAVSKAFYCDILGFTLQSE----VY---REERDSWKgdlalngqyvIELFSFPFPperpsrpeacGLRHLAF 81
Cdd:cd07266    7 HAELVVTDLAASREFYVDTLGLHVTDEddnaIYlrgVEEFIHHT----------LVLRKAPEA----------AVGHLGF 66

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 446823847  82 SV---DDIDAAVAHLESHNVKCEaiRVDPYTQKRFTFFNDPDGLPLELY 127
Cdd:cd07266   67 RVrdeADLDKAAAFYKELGLPTE--WREEPGQGRTLRVEDPFGFPIEFY 113
PhnB COG2764
Zn-dependent glyoxalase, PhnB family [Energy production and conversion];
12-128 4.56e-06

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


Pssm-ID: 442048 [Multi-domain]  Cd Length: 118  Bit Score: 42.54  E-value: 4.56e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446823847  12 IIATDYAVSKAFYCDILGFTLQSEVYREERDSWKGDLALNGQyVIELFSfpFPPERPSRPEACGlrHLAFSVDDIDAAVA 91
Cdd:COG2764    6 LVVDDAEEALEFYEDVFGFEVVFRMTDPDGKIMHAELRIGGS-VLMLSD--APPDSPAAEGNGV--SLSLYVDDVDALFA 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 446823847  92 HLESHNVKceaIRVDPYTQ---KRFTFFNDPDGLPLELYE 128
Cdd:COG2764   81 RLVAAGAT---VVMPLQDTfwgDRFGMVRDPFGVLWMINT 117
Glyoxalase_3 pfam13468
Glyoxalase-like domain; This domain is related to the Glyoxalase domain pfam00903.
 7-107 8.92e-06

Glyoxalase-like domain; This domain is related to the Glyoxalase domain pfam00903.


Pssm-ID: 433233  Cd Length: 175  Bit Score: 42.71  E-value: 8.92e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446823847    7 VHHIAIIATDYAVSKAFYCDILGFTLQSEVYREERDSWKGDLALNGQYvIELFSFPfpPERPSRPE-----------ACG 75
Cdd:pfam13468   1 LDHVVLAVPDLDEAAARFARALGFTVTPGGRHPGMGTANALIMFGDGY-LELLAVD--PEAPAPPRgrwfgldrladGEG 77

                          90       100       110
                  ....*....|....*....|....*....|..
gi 446823847   76 LRHLAFSVDDIDAAVAHLESHNVKcEAIRVDP 107
Cdd:pfam13468  78 LLGWALRTDDIDAVAARLRAAGVE-PGRRVRP 108
Fosfomycin_RP cd08345
Fosfomycin resistant protein; This family contains three types of fosfomycin resistant protein. ...
 9-127 1.37e-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: 41.39  E-value: 1.37e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446823847   9 HIAIIATDYAVSKAFYCDILGFtlqsevyREERDSWKGDLALNGQYVIELFSFPFPPERPSRPEACGLRHLAFSVDDIDA 88
Cdd:cd08345    1 HITLIVRDLEKSTAFLQDIFGA-------REVYSSGDKTFSLSKEKFFLLGGLWIALMEGESLQERSYTHIAFQIQSEDF 73

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 446823847  89 AV--AHLESHNVKCEAIRVDPYTQKRFTFFNDPDGLPLELY 127
Cdd:cd08345   74 DRyaERLGALGVEMRPPRPRVEGEGRSIYFYDPDNHLFELH 114
GlxI_Zn cd07233
Glyoxalase I that uses Zn(++) as cofactor; This family includes eukaryotic glyoxalase I that ...
 16-126 1.46e-05

Glyoxalase I that uses Zn(++) as cofactor; This family includes eukaryotic glyoxalase I that prefers the divalent cation zinc 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.


Pssm-ID: 319900 [Multi-domain]  Cd Length: 142  Bit Score: 41.54  E-value: 1.46e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446823847  16 DYAVSKAFYCDILGFTLqseVYREERDSWKGDLALNG-QYVIELFSFPFPPERPSRP----------------------- 71
Cdd:cd07233   10 DPKKSLKFYTEVLGMKL---LRKKDFPEMKFSLYFLGyEDPKDIPKDPRTAWVFSREgtlelthnwgtendedpvyhngn 86

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 446823847  72 -EACGLRHLAFSVDDIDAAVAHLESHNVKCeAIRVDPYTQKRFTFFNDPDGLPLEL 126
Cdd:cd07233   87 sDPRGFGHIGIAVDDVYAACERFEELGVKF-KKKPDDGKMKGIAFIKDPDGYWIEI 141
SgaA_N_like cd07247
N-terminal domain of Streptomyces griseus SgaA and similar domains; SgaA suppresses the growth ...
 12-121 2.23e-05

N-terminal domain of Streptomyces griseus SgaA and similar domains; SgaA suppresses the growth disturbances caused by high osmolarity and a high concentration of A-factor, a microbial hormone, during the early growth phase in Streptomyces griseus. A-factor (2-isocapryloyl-3R-hydroxymethyl-gamma-butyrolactone) controls morphological differentiation and secondary metabolism in Streptomyces griseus. It is a chemical signaling molecule that at a very low concentration acts as a switch for yellow pigment production, aerial mycelium formation, streptomycin production, and streptomycin resistance. The structure and amino acid sequence of SgaA are closely related to a group of antibiotics resistance proteins, including bleomycin resistance protein, mitomycin resistance protein, and fosfomycin resistance proteins. SgaA might also function as a streptomycin resistance protein.


Pssm-ID: 319911 [Multi-domain]  Cd Length: 114  Bit Score: 40.71  E-value: 2.23e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446823847  12 IIATDYAVSKAFYCDILGFTLQSEVYREERDSW--KGDLALNGQYVIElfsfPFPPERPSRPeacglrHLAFSVDDIDAA 89
Cdd:cd07247    6 LPTTDLERAKAFYGAVFGWTFEDEGDGGGDYALftAGGGAVGGLMRAP----EEVAGAPPGW------LIYFAVDDLDAA 75

                         90       100       110
                 ....*....|....*....|....*....|..
gi 446823847  90 VAHLESHNVKCEAIRVDPYTQKRFTFFNDPDG 121
Cdd:cd07247   76 LARVEAAGGKVVVPPTDIPGGGRFAVFADPEG 107
Glyoxalase_6 pfam18029
Glyoxalase-like domain; This entry comprises a diverse set of domains related to the ...
 9-126 7.21e-05

Glyoxalase-like domain; This entry comprises a diverse set of domains related to the Glyoxalase domain. The exact specificity of these proteins is uncertain.


Pssm-ID: 436220  Cd Length: 110  Bit Score: 39.29  E-value: 7.21e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446823847    9 HIAIIATDYAVSKAFYCDILGFTLQSEVYREERDSWKGDLALNGQYVieLFsfpfppERPSRPEACGLR-HLAFSVDDID 87
Cdd:pfam18029   1 AVVLDCADPAALAAFWSAALGWEVVPDDTALPDPDGGGPIGGGGPRL--LF------QRVPEPKPGKNRvHLDLAVDDLE 72

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 446823847   88 AAVAHLeshnVKCEAIRVD---PYTQKRFTFFnDPDGLPLEL 126
Cdd:pfam18029  73 AAVARL----VALGATVLDdgdDPDGGRWVLA-DPEGNEFCL 109
VOC_CChe_VCA0619_like cd08356
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; uncharacterized subfamily of ...
 14-121 1.58e-04

uncharacterized subfamily of vicinal oxygen chelate (VOC) family; uncharacterized subfamily of vicinal oxygen chelate (VOC) family contains Vibrio cholerae VCA0619 and similar proteins. The 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: 319944  Cd Length: 113  Bit Score: 38.44  E-value: 1.58e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446823847  14 ATDYAVSKAFYCDiLGFTLQSEvyreerdswKGDLAL--NGQYVIELFSFPfpperpsRPEACGLRHLAFSVDDIDAAVA 91
Cdd:cd08356    9 AKDFELSKAFYQA-LGFELASE---------EGGVAYfrLGDCSFLLQDFY-------EKEHAENFMMHLLVEDVDAWHQ 71

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 446823847  92 HLESHN------VKCEAIRVDPYTQKRFTFFnDPDG 121
Cdd:cd08356   72 HVKTLGlaerygVKVTDPTDQPWGMRDFVLT-DPSG 106
ED_TypeI_classII_N cd16360
N-terminal domain of type I, class II extradiol dioxygenases; This family contains the ...
 9-127 1.70e-04

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: 38.45  E-value: 1.70e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446823847   9 HIAIIATDYAVSKAFYCDILGftLQsEVYREerdswKGDLALNGQ----YVIELFSFPFPperpsrpeacGLRHLAFSV- 83
Cdd:cd16360    1 YAELGVPDLEKALEFYTDVLG--LQ-VAKRD-----GNSVYLRGYedehHSLVLYEAPEA----------GLKHFAFEVa 62

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 446823847  84 --DDIDAAVAHLESHNVKCEAIR-VDPYTQKRFTFFNDPDGLPLELY 127
Cdd:cd16360   63 seEDLERAAASLTALGCDVTWGPdGEVPGGGKGFRFQDPSGHLLELF 109
HppD COG3185
4-hydroxyphenylpyruvate dioxygenase and related hemolysins [Amino acid transport and ...
 3-99 3.91e-04

4-hydroxyphenylpyruvate dioxygenase and related hemolysins [Amino acid transport and metabolism, General function prediction only];


Pssm-ID: 442418 [Multi-domain]  Cd Length: 333  Bit Score: 38.72  E-value: 3.91e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446823847   3 GLKQVHHIAII--ATDYAVSKAFYCDILGFTLQSEVYREERD---------SWKGD--LALNGqyvielfsfpfpPERPS 69
Cdd:COG3185  143 GLTRIDHIGIAvpRGDLDEWVLFYEDVLGFEEIREEDIEDPYqgvrsavlqSPDGKvrIPLNE------------PTSPD 210

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 446823847  70 RPEA--------CGLRHLAFSVDDIDAAVAHLESHNVK 99
Cdd:COG3185  211 SQIAeflekyrgEGIQHIAFATDDIEATVAALRARGVR 248
GLOD5 cd07253
Human glyoxalase domain-containing protein 5 and similar proteins; Uncharacterized subfamily ...
 4-98 5.95e-04

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: 37.21  E-value: 5.95e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446823847   4 LKQVHHIAIIATDYAVSKAFYCDILGFTLQSevYREERDSwkgdLALNGQYvIELFSF--PFPPeRPSRPEAcGLRHLAF 81
Cdd:cd07253    1 IKRLDHLVLTVKDIERTIDFYTKVLGMTVVT--FKEGRKA----LRFGNQK-INLHQKgkEFEP-KASAPTP-GSADLCF 71

                         90
                 ....*....|....*...
gi 446823847  82 SVD-DIDAAVAHLESHNV 98
Cdd:cd07253   72 ITEtPIDEVLEHLEACGV 89
metmalonyl_epim TIGR03081
methylmalonyl-CoA epimerase; Members of this protein family are the enzyme methylmalonyl-CoA ...
 7-100 8.21e-04

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: 36.92  E-value: 8.21e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446823847    7 VHHIAIIATDYAVSKAFYCDILGFTLQSEVYREERDSWKGDLALnGQYVIELFSfPFPPERP------SRPEacGLRHLA 80
Cdd:TIGR03081   2 IDHVGIAVPDLEEAAKFYEDVLGAQVSEIEELPEQGVKVVFIAL-GNTKVELLE-PLGEDSPiakfleKNGG--GIHHIA 77

                          90       100
                  ....*....|....*....|
gi 446823847   81 FSVDDIDAAVAHLESHNVKC 100
Cdd:TIGR03081  78 IEVDDIEAALETLKEKGVRL 97
VOC_like cd09011
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 12-128 1.77e-03

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: 319953  Cd Length: 122  Bit Score: 35.91  E-value: 1.77e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446823847  12 IIATDYAVSKAFYCDILGftLQSEVYREERDSWKGDLALNgqyviELFSFPFPPERPSRPEACGLRH--LAFSVDDIDAA 89
Cdd:cd09011    8 LVVKDIEKSKKFYEDVLG--QKILLDFGENVVFEGGFALQ-----EKKSWLETIIISDLSIKQQSNNfeLYFEVDDFDAF 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 446823847  90 VAHLESH-NVK-CEAIRVDPYTQKRFTFFnDPDGLPLELYE 128
Cdd:cd09011   81 FEKLNPHkDIEfIHPILEHPWGQRVFRFY-DPDGHIIEIGE 120
ED_TypeI_classII_C cd08343
C-terminal domain of type I, class II extradiol dioxygenases, catalytic domain; This family ...
 9-127 2.15e-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: 35.76  E-value: 2.15e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446823847   9 HIAIIATDYAVSKAFYCDILGFTLQSEVYREERD--SW-KGDlalNGQYVIELFSFPFPPErpsrpeacGLRHLAFSVDD 85
Cdd:cd08343    2 HVVLCSPDVEASRDFYTDVLGFRVSDRIVDPGVDggAFlHCD---RGTDHHTVALAGGPHP--------GLHHVAFEVHD 70

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 446823847  86 IDA---AVAHLESHNVKCEA-IRVDPYTQKRFTFFNDPDGLPLELY 127
Cdd:cd08343   71 LDDvgrGHDRLREKGYKIEWgPGRHGLGSQVFDYWFDPSGNRVEYY 116
FosA cd07244
fosfomycin resistant protein subfamily FosA; This subfamily family contains FosA, a fosfomycin ...
 9-126 3.59e-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: 34.95  E-value: 3.59e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446823847   9 HIAIIATDYAVSKAFYCDILGFTL----QSEVYREERDSWkgdLALNgqyvielfsfpfpPERPSRPEACgLRHLAFSVD 84
Cdd:cd07244    4 HITLAVSDLERSLAFYVDLLGFKPhvrwDKGAYLTAGDLW---LCLS-------------LDPAAEPSPD-YTHIAFTVS 66

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 446823847  85 --DIDAAVAHLESHNVKCeairvdpyTQKRFT-----FFNDPDGLPLEL 126
Cdd:cd07244   67 eeDFEELSERLRAAGVKI--------WQENSSegdslYFLDPDGHKLEL 107
PRK04101 PRK04101
metallothiol transferase FosB;
78-127 4.08e-03

metallothiol transferase FosB;


Pssm-ID: 179740  Cd Length: 139  Bit Score: 34.92  E-value: 4.08e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 446823847  78 HLAFSVD--DIDAAVAHLESHNVKCEAIRVDPYTQKRFTFFNDPDGLPLELY 127
Cdd:PRK04101  66 HIAFSIEeeDFDHWYQRLKENDVNILPGRERDERDKKSIYFTDPDGHKFEFH 117
 
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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