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Conserved domains on  [gi|1688832407|gb|TOP19702|]
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VOC family protein [Vibrio parahaemolyticus]

Protein Classification

VOC family protein( domain architecture ID 11611485)

vicinal oxygen chelate (VOC) family protein uses a metal center to coordinate a substrate, intermediate, or transition state through vicinal oxygen atoms; similar to Actinomyces sp. 2-epi-5-epi-valiolone epimerase, which catalyzes the epimerization of 2-epi-5-epi-valiolone to 5-epi-valiolone

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
VOC_ShValD_like cd16361
vicinal oxygen chelate (VOC) family protein similar to Streptomyces hygroscopicus ValD protein; ...
 2-151 3.44e-73

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: 216.04  E-value: 3.44e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1688832407   2 KMNHVGIMVGDMDKAVEFYTQALGLKVVMGNTKVVEEREtAIGRMCIAVFGEGFKGFNIAHLVTSDGIGLELFEMKERQA 81
Cdd:cd16361     1 GVNHVGITVPDLDAAVEFYTDVLGAEVVYRSTPLAEGDR-GGGEMRAAGFVPGFARARIAMLRLGPGPGIELFEYKGPEQ 79

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1688832407  82 RHEVD-FSRIGIFHFCLQTDDFEGAIKRTEAFGGKVRMDIMRYHPEDDNKPAKMVYLEDPFGNLFELYSHT 151
Cdd:cd16361    80 RAPVPrNSDVGIFHFALQVDDVEAAAERLAAAGGKVLMGPREIPDGGPGKGNRMVYLRDPWGTLIELVSHP 150
 
Name Accession Description Interval E-value
VOC_ShValD_like cd16361
vicinal oxygen chelate (VOC) family protein similar to Streptomyces hygroscopicus ValD protein; ...
 2-151 3.44e-73

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: 216.04  E-value: 3.44e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1688832407   2 KMNHVGIMVGDMDKAVEFYTQALGLKVVMGNTKVVEEREtAIGRMCIAVFGEGFKGFNIAHLVTSDGIGLELFEMKERQA 81
Cdd:cd16361     1 GVNHVGITVPDLDAAVEFYTDVLGAEVVYRSTPLAEGDR-GGGEMRAAGFVPGFARARIAMLRLGPGPGIELFEYKGPEQ 79

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1688832407  82 RHEVD-FSRIGIFHFCLQTDDFEGAIKRTEAFGGKVRMDIMRYHPEDDNKPAKMVYLEDPFGNLFELYSHT 151
Cdd:cd16361    80 RAPVPrNSDVGIFHFALQVDDVEAAAERLAAAGGKVLMGPREIPDGGPGKGNRMVYLRDPWGTLIELVSHP 150
glyox_marine TIGR03645
lactoylglutathione lyase family protein; Members of this protein family share homology with ...
 4-158 2.78e-59

lactoylglutathione lyase family protein; Members of this protein family share homology with lactoylglutathione lyase (glyoxalase I) and are found mainly in marine members of the gammaproteobacteria, including CPS_0532 from Colwellia psychrerythraea 34H. This family excludes a well-separated, more narrowly distributed paralogous family, exemplified by CPS_3492 from C. psychrerythraea. The function is of this protein family is unknown.


Pssm-ID: 132684  Cd Length: 162  Bit Score: 181.52  E-value: 2.78e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1688832407   4 NHVGIMVGDMDKAVEFYTQALGLKVVMGNTKVVEErETAIGRMCIAVFGEGFKGFNIAHLVTSDGIGLELFEMKERQA-R 82
Cdd:TIGR03645   6 SHIGISVPDLDAAVKFYTEVLGWYLIMPPTEIVED-DSAIGEMCTDVFGEGWGSFKIAHLSTGDRIGVELFEFKNQENpE 84

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1688832407  83 HEVDFSRIGIFHFCLQTDDFEGAIKRTEAFGGKVRMDIMR-YHPEDdnKPAKMVYLEDPFGNLFELYSHTYEETYAS 158
Cdd:TIGR03645  85 DNFEYWKTGVFHFCVQDPDVEGLAERIVAAGGKKRMPVPRyYYPGE--KPYRMIYMEDPFGNILEIYSHSYELTYSA 159
GloA COG0346
Catechol 2,3-dioxygenase or related enzyme, vicinal oxygen chelate (VOC) family [Secondary ...
 1-151 1.89e-22

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: 86.58  E-value: 1.89e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1688832407   1 MKMNHVGIMVGDMDKAVEFYTQALGLkvvmgntKVVEEREtaigrmciavFGEGfkGFNIAHLVTSDGIGLELFEMKERQ 80
Cdd:COG0346     1 MGLHHVTLRVSDLEASLAFYTDVLGL-------ELVKRTD----------FGDG--GFGHAFLRLGDGTELELFEAPGAA 61

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1688832407  81 ARHEvdfsRIGIFHFCLQTDDFEGAIKRTEAFGGKVRMDimryhPEDDNKPAKMVYLEDPFGNLFELYSHT 151
Cdd:COG0346    62 PAPG----GGGLHHLAFRVDDLDAAYARLRAAGVEIEGE-----PRDRAYGYRSAYFRDPDGNLIELVEPP 123
Glyoxalase pfam00903
Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;
2-147 2.24e-16

Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;


Pssm-ID: 395724 [Multi-domain]  Cd Length: 121  Bit Score: 70.55  E-value: 2.24e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1688832407   2 KMNHVGIMVGDMDKAVEFYTQALGLKVvmgntkVVEERETAIGRMCIAVFGEGfkgfniahlvtsdGIGLELFEMkERQA 81
Cdd:pfam00903   1 RIDHVALRVGDLEKSLDFYTDVLGFKL------VEETDAGEEGGLRSAFFLAG-------------GRVLELLLN-ETPP 60

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1688832407  82 RHEVDFSRIGIFHFCLQTDDFEGAIKRTEAFGGKVRMDIMRyHPEDdnkpAKMVYLEDPFGNLFEL 147
Cdd:pfam00903  61 PAAAGFGGHHIAFIAFSVDDVDAAYDRLKAAGVEIVREPGR-HGWG----GRYSYFRDPDGNLIEL 121
PLN02300 PLN02300
lactoylglutathione lyase
 2-147 2.14e-04

lactoylglutathione lyase


Pssm-ID: 215169 [Multi-domain]  Cd Length: 286  Bit Score: 40.15  E-value: 2.14e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1688832407   2 KMNHVGIMVGDMDKAVEFYTQALGLKvVMGNTKVVEERETAigrmciAVFGEGFKGFNIAHLVTSDgIGLELFEMKErqa 81
Cdd:PLN02300   24 RMLHVVYRVGDLDRTIKFYTECLGMK-LLRKRDIPEEKYTN------AFLGYGPEDSNFVVELTYN-YGVDKYDIGT--- 92

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1688832407  82 rhevdfsriGIFHFCLQTDDFEGAIKRTEAFGGKVRMDIMryhPEDDNKpAKMVYLEDPFGNLFEL 147
Cdd:PLN02300   93 ---------GFGHFGIAVEDVAKTVELVKAKGGKVTREPG---PVKGGK-SVIAFVKDPDGYKFEL 145
 
Name Accession Description Interval E-value
VOC_ShValD_like cd16361
vicinal oxygen chelate (VOC) family protein similar to Streptomyces hygroscopicus ValD protein; ...
 2-151 3.44e-73

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: 216.04  E-value: 3.44e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1688832407   2 KMNHVGIMVGDMDKAVEFYTQALGLKVVMGNTKVVEEREtAIGRMCIAVFGEGFKGFNIAHLVTSDGIGLELFEMKERQA 81
Cdd:cd16361     1 GVNHVGITVPDLDAAVEFYTDVLGAEVVYRSTPLAEGDR-GGGEMRAAGFVPGFARARIAMLRLGPGPGIELFEYKGPEQ 79

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1688832407  82 RHEVD-FSRIGIFHFCLQTDDFEGAIKRTEAFGGKVRMDIMRYHPEDDNKPAKMVYLEDPFGNLFELYSHT 151
Cdd:cd16361    80 RAPVPrNSDVGIFHFALQVDDVEAAAERLAAAGGKVLMGPREIPDGGPGKGNRMVYLRDPWGTLIELVSHP 150
glyox_marine TIGR03645
lactoylglutathione lyase family protein; Members of this protein family share homology with ...
 4-158 2.78e-59

lactoylglutathione lyase family protein; Members of this protein family share homology with lactoylglutathione lyase (glyoxalase I) and are found mainly in marine members of the gammaproteobacteria, including CPS_0532 from Colwellia psychrerythraea 34H. This family excludes a well-separated, more narrowly distributed paralogous family, exemplified by CPS_3492 from C. psychrerythraea. The function is of this protein family is unknown.


Pssm-ID: 132684  Cd Length: 162  Bit Score: 181.52  E-value: 2.78e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1688832407   4 NHVGIMVGDMDKAVEFYTQALGLKVVMGNTKVVEErETAIGRMCIAVFGEGFKGFNIAHLVTSDGIGLELFEMKERQA-R 82
Cdd:TIGR03645   6 SHIGISVPDLDAAVKFYTEVLGWYLIMPPTEIVED-DSAIGEMCTDVFGEGWGSFKIAHLSTGDRIGVELFEFKNQENpE 84

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1688832407  83 HEVDFSRIGIFHFCLQTDDFEGAIKRTEAFGGKVRMDIMR-YHPEDdnKPAKMVYLEDPFGNLFELYSHTYEETYAS 158
Cdd:TIGR03645  85 DNFEYWKTGVFHFCVQDPDVEGLAERIVAAGGKKRMPVPRyYYPGE--KPYRMIYMEDPFGNILEIYSHSYELTYSA 159
GloA COG0346
Catechol 2,3-dioxygenase or related enzyme, vicinal oxygen chelate (VOC) family [Secondary ...
 1-151 1.89e-22

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: 86.58  E-value: 1.89e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1688832407   1 MKMNHVGIMVGDMDKAVEFYTQALGLkvvmgntKVVEEREtaigrmciavFGEGfkGFNIAHLVTSDGIGLELFEMKERQ 80
Cdd:COG0346     1 MGLHHVTLRVSDLEASLAFYTDVLGL-------ELVKRTD----------FGDG--GFGHAFLRLGDGTELELFEAPGAA 61

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1688832407  81 ARHEvdfsRIGIFHFCLQTDDFEGAIKRTEAFGGKVRMDimryhPEDDNKPAKMVYLEDPFGNLFELYSHT 151
Cdd:COG0346    62 PAPG----GGGLHHLAFRVDDLDAAYARLRAAGVEIEGE-----PRDRAYGYRSAYFRDPDGNLIELVEPP 123
VOC cd06587
vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate (VOC) superfamily is composed ...
 5-147 6.00e-17

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: 71.79  E-value: 6.00e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1688832407   5 HVGIMVGDMDKAVEFYTQALGLKVVmgntkvveeretaigrmciavfgEGFKGFNIAHLVTSDGIGLELFEMKERQARHe 84
Cdd:cd06587     1 HVALRVPDLDASVAFYEEVLGFEVV-----------------------SRNEGGGFAFLRLGPGLRLALLEGPEPERPG- 56

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1688832407  85 vdfsRIGIFHFCLQTDDFEGAIKRTEAFGGKVRmdiMRYHPEDDNKPAKMVYLEDPFGNLFEL 147
Cdd:cd06587    57 ----GGGLFHLAFEVDDVDEVDERLREAGAEGE---LVAPPVDDPWGGRSFYFRDPDGNLIEF 112
Glyoxalase pfam00903
Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;
2-147 2.24e-16

Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;


Pssm-ID: 395724 [Multi-domain]  Cd Length: 121  Bit Score: 70.55  E-value: 2.24e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1688832407   2 KMNHVGIMVGDMDKAVEFYTQALGLKVvmgntkVVEERETAIGRMCIAVFGEGfkgfniahlvtsdGIGLELFEMkERQA 81
Cdd:pfam00903   1 RIDHVALRVGDLEKSLDFYTDVLGFKL------VEETDAGEEGGLRSAFFLAG-------------GRVLELLLN-ETPP 60

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1688832407  82 RHEVDFSRIGIFHFCLQTDDFEGAIKRTEAFGGKVRMDIMRyHPEDdnkpAKMVYLEDPFGNLFEL 147
Cdd:pfam00903  61 PAAAGFGGHHIAFIAFSVDDVDAAYDRLKAAGVEIVREPGR-HGWG----GRYSYFRDPDGNLIEL 121
VOC COG3324
Lactoylglutathione lyase-related enzyme, vicinal oxygen chelate (VOC) family [General function ...
 1-150 3.13e-16

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


Pssm-ID: 442553 [Multi-domain]  Cd Length: 119  Bit Score: 70.05  E-value: 3.13e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1688832407   1 MKMNHVGIMVGDMDKAVEFYTQALGLKvvmgntkvVEERETAIGRMciavfgegfkgfniAHLVTSDGIGLELFEMKERQ 80
Cdd:COG3324     3 GTIVWVELPVDDLERAKAFYEEVFGWT--------FEDDAGPGGDY--------------AEFDTDGGQVGGLMPGAEEP 60

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1688832407  81 ARhevdfsriGIFHFCLQTDDFEGAIKRTEAFGGKVRMDimryhPEDDNKPAKMVYLEDPFGNLFELYSH 150
Cdd:COG3324    61 GG--------PGWLLYFAVDDLDAAVARVEAAGGTVLRP-----PTDIPPWGRFAVFRDPEGNRFGLWQP 117
CatE COG2514
Catechol-2,3-dioxygenase [Secondary metabolites biosynthesis, transport and catabolism];
1-161 2.06e-15

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


Pssm-ID: 442004 [Multi-domain]  Cd Length: 141  Bit Score: 68.83  E-value: 2.06e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1688832407   1 MKMNHVGIMVGDMDKAVEFYTQALGLkvvmgntKVVEERETAigrmciAVFGegfkgfniahlVTSDGIGLELFEMKERQ 80
Cdd:COG2514     2 TRLGHVTLRVRDLERSAAFYTDVLGL-------EVVEREGGR------VYLR-----------ADGGEHLLVLEEAPGAP 57

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1688832407  81 ARHEvdfsRIGIFHFCLQTD---DFEGAIKRTEAFGgkvrmdiMRYHPEDDNKPAKMVYLEDPFGNLFELYSHTYEETYA 157
Cdd:COG2514    58 PRPG----AAGLDHVAFRVPsraDLDAALARLAAAG-------VPVEGAVDHGVGESLYFRDPDGNLIELYTDRPRFEHV 126


                  ....
gi 1688832407 158 SEYE 161
Cdd:COG2514   127 GDLE 130
VOC_like cd07264
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 5-150 3.62e-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: 319925 [Multi-domain]  Cd Length: 118  Bit Score: 51.56  E-value: 3.62e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1688832407   5 HVGIMVGDMDKAVEFYTQALGLKVvmgntkvveERETAIGRmciavfgegfkgfniAHLVTSDGIGLELFEMKErQARHE 84
Cdd:cd07264     3 YIVLYVDDFAASLRFYRDVLGLPP---------RFLHEEGE---------------YAEFDTGETKLALFSRKE-MARSG 57

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1688832407  85 VDFSRIGIFHFCLQTDDFEGAIKRTEAFGGKVRMdimryhpEDDNKP--AKMVYLEDPFGNLFELYSH 150
Cdd:cd07264    58 GPDRRGSAFELGFEVDDVEATVEELVERGAEFVR-------EPANKPwgQTVAYVRDPDGNLIEICEP 118
VOC_like cd07245
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 4-147 2.60e-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: 319909 [Multi-domain]  Cd Length: 117  Bit Score: 46.54  E-value: 2.60e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1688832407   4 NHVGIMVGDMDKAVEFYTQALGLKVVmgntkvveERETAiGRMCIAVFGEGfkGFNIAHLVtsDGIGLELFEMKERQARH 83
Cdd:cd07245     2 DHVALACPDLERARRFYTDVLGLEEV--------PRPPF-LKFGGAWLYLG--GGQQIHLV--VEQNPSELPRPEHPGRD 68

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1688832407  84 EvdfsrigifHFCLQTDDFEGAIKRTEAFGGKVRMDImryhpEDDNKPAKmVYLEDPFGNLFEL 147
Cdd:cd07245    69 R---------HPSFSVPDLDALKQRLKEAGIPYTEST-----SPGGGVTQ-LFFRDPDGNRLEF 117
Glyoxalase_3 pfam13468
Glyoxalase-like domain; This domain is related to the Glyoxalase domain pfam00903.
 5-119 3.82e-07

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


Pssm-ID: 433233  Cd Length: 175  Bit Score: 47.33  E-value: 3.82e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1688832407   5 HVGIMVGDMDKAVEFYTQALGLKVVMGNtkvveeRETAIG-RMCIAVFGEGFkgfniahlvtsdgigLEL--FEMKERQA 81
Cdd:pfam13468   3 HVVLAVPDLDEAAARFARALGFTVTPGG------RHPGMGtANALIMFGDGY---------------LELlaVDPEAPAP 61

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1688832407  82 RHEVDFSR------IGIFHFCLQTDDFEGAIKRTEA----FGGKVRMD 119
Cdd:pfam13468  62 PRGRWFGLdrladgEGLLGWALRTDDIDAVAARLRAagvePGRRVRPD 109
VOC_like cd08353
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 2-147 7.42e-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: 319941  Cd Length: 142  Bit Score: 46.03  E-value: 7.42e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1688832407   2 KMNHVGIMVGDMDKAVEFYTqALGLkVVMGNTKVveERETAiGRmciaVFGEGFKGFNIAHLVTSDGIG-LELFEMKERQ 80
Cdd:cd08353     3 RMDHVGIVVEDLDAAIAFFT-ELGL-ELEGRMTV--EGEWA-DR----VVGLDGVRVEIAMLRTPDGHGrLELSKFLTPA 73

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1688832407  81 ARHEVDFS---RIGIFHFCLQTDDFEGAIKRTEAFGGKVRMDIMRYhpEDDnkpAKMVYLEDPFGNLFEL 147
Cdd:cd08353    74 AIPGHRPApanALGLRHVAFAVDDIDAVVARLRKHGAELVGEVVQY--EDS---YRLCYVRGPEGIIVEL 138
MMCE cd07249
Methylmalonyl-CoA epimerase (MMCE); MMCE, also called methylmalonyl-CoA racemase (EC 5.1.99.1) ...
 4-147 1.52e-06

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: 44.87  E-value: 1.52e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1688832407   4 NHVGIMVGDMDKAVEFYTQALGLKVVmgNTKVVEERETAIgrmciavfgegfkgfniaHLVTSDGIGLELFE-------- 75
Cdd:cd07249     2 DHIGIAVPDLDEALKFYEDVLGVKVS--EPEELEEQGVRV------------------AFLELGNTQIELLEplgedspi 61

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1688832407  76 MKERQARHEvdfsriGIFHFCLQTDDFEGAIKRTEAFGGKVRMDIMRyhPEDDNKPAKMVYLEDPFGNLFEL 147
Cdd:cd07249    62 AKFLDKKGG------GLHHIAFEVDDIDAAVEELKAQGVRLLSEGPR--IGAHGKRVAFLHPKDTGGVLIEL 125
Glyoxalase_4 pfam13669
Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;
4-116 4.21e-06

Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;


Pssm-ID: 463951 [Multi-domain]  Cd Length: 109  Bit Score: 43.42  E-value: 4.21e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1688832407   4 NHVGIMVGDMDKAVEFYTQALGLKVvmgnTKVVEERETAIgRMCIAVFGEGFkgfniahlvtsdgIGLELFEMKERQARH 83
Cdd:pfam13669   1 HHVGIAVPDLDRALALWGALLGLGP----EGDYRSEPQNV-DLAFALLGDGP-------------VEVELIQPLDGDSPL 62

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1688832407  84 evDFSRIGIFHFCLQTDDFEGAIKRTEAFGGKV 116
Cdd:pfam13669  63 --ARHGPGLHHLAYWVDDLDAAVARLLDQGYRV 93
SgaA_N_like cd07247
N-terminal domain of Streptomyces griseus SgaA and similar domains; SgaA suppresses the growth ...
 4-149 6.02e-06

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: 43.02  E-value: 6.02e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1688832407   4 NHVGIMVGDMDKAVEFYTQALGLKVvmgntkvvEERETAIGRMCIAVFGEGFKGfniahlvtsdGIGlelfemkERQARH 83
Cdd:cd07247     2 VWFELPTTDLERAKAFYGAVFGWTF--------EDEGDGGGDYALFTAGGGAVG----------GLM-------RAPEEV 56

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1688832407  84 EVDFSRIGIFhfcLQTDDFEGAIKRTEAFGGKVRMDimryhPEDDNKPAKMVYLEDPFGNLFELYS 149
Cdd:cd07247    57 AGAPPGWLIY---FAVDDLDAALARVEAAGGKVVVP-----PTDIPGGGRFAVFADPEGNRFGLWS 114
PhnB COG2764
Zn-dependent glyoxalase, PhnB family [Energy production and conversion];
8-150 9.51e-06

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


Pssm-ID: 442048 [Multi-domain]  Cd Length: 118  Bit Score: 42.54  E-value: 9.51e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1688832407   8 IMVGDMDKAVEFYTQALGLKVVMgntkVVEERETAIGrmciavFGEgfkgfniahlVTSDGIGLELFEmkerqARHEVDF 87
Cdd:COG2764     6 LVVDDAEEALEFYEDVFGFEVVF----RMTDPDGKIM------HAE----------LRIGGSVLMLSD-----APPDSPA 60

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1688832407  88 SRIGIFHFCLQTDDFEGAIKRTEAFGGKVRMDimryhpeddnkPAKMVY------LEDPFGNLFELYSH 150
Cdd:COG2764    61 AEGNGVSLSLYVDDVDALFARLVAAGATVVMP-----------LQDTFWgdrfgmVRDPFGVLWMINTP 118
GLOD5 cd07253
Human glyoxalase domain-containing protein 5 and similar proteins; Uncharacterized subfamily ...
 2-147 1.19e-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: 39.52  E-value: 1.19e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1688832407   2 KMNHVGIMVGDMDKAVEFYTQALGLKVVMgntkvveeretaigrmciavFGEGFKGFNIAHLVtsdgIGLELFEMK-ERQ 80
Cdd:cd07253     3 RLDHLVLTVKDIERTIDFYTKVLGMTVVT--------------------FKEGRKALRFGNQK----INLHQKGKEfEPK 58

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1688832407  81 ARHEVDfsriGIFHFCLQTDDF----------------EGAIKRTEAFGgkvrmdimryhpeddnkPAKMVYLEDPFGNL 144
Cdd:cd07253    59 ASAPTP----GSADLCFITETPidevlehleacgvtieEGPVKRTGALG-----------------PILSIYFRDPDGNL 117


                  ...
gi 1688832407 145 FEL 147
Cdd:cd07253   118 IEL 120
PLN02300 PLN02300
lactoylglutathione lyase
 2-147 2.14e-04

lactoylglutathione lyase


Pssm-ID: 215169 [Multi-domain]  Cd Length: 286  Bit Score: 40.15  E-value: 2.14e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1688832407   2 KMNHVGIMVGDMDKAVEFYTQALGLKvVMGNTKVVEERETAigrmciAVFGEGFKGFNIAHLVTSDgIGLELFEMKErqa 81
Cdd:PLN02300   24 RMLHVVYRVGDLDRTIKFYTECLGMK-LLRKRDIPEEKYTN------AFLGYGPEDSNFVVELTYN-YGVDKYDIGT--- 92

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1688832407  82 rhevdfsriGIFHFCLQTDDFEGAIKRTEAFGGKVRMDIMryhPEDDNKpAKMVYLEDPFGNLFEL 147
Cdd:PLN02300   93 ---------GFGHFGIAVEDVAKTVELVKAKGGKVTREPG---PVKGGK-SVIAFVKDPDGYKFEL 145
GlxI_Ni cd16358
Glyoxalase I that uses Ni(++) as cofactor; This family includes Escherichia coil and other ...
 3-147 7.69e-04

Glyoxalase I that uses Ni(++) as cofactor; This family includes Escherichia coil and other prokaryotic glyoxalase I that uses nickel as cofactor. Glyoxalase I (also known as lactoylglutathione lyase; EC 4.4.1.5) is part of the glyoxalase system, a two-step system for detoxifying methylglyoxal, a side product of glycolysis. This system is responsible for the conversion of reactive, acyclic alpha-oxoaldehydes into the corresponding alpha-hydroxyacids and involves 2 enzymes, glyoxalase I and II. Glyoxalase I catalyses an intramolecular redox reaction of the hemithioacetal (formed from methylglyoxal and glutathione) to form the thioester, S-D-lactoylglutathione. This reaction involves the transfer of two hydrogen atoms from C1 to C2 of the methylglyoxal, and proceeds via an ene-diol intermediate. Glyoxalase I has a requirement for bound metal ions for catalysis. Eukaryotic glyoxalase I prefers the divalent cation zinc as cofactor, whereas Escherichia coil and other prokaryotic glyoxalase I uses nickel. However, eukaryotic Trypanosomatid parasites also use nickel as a cofactor, which could possibly be explained by acquiring their GLOI gene by horizontal gene transfer. Human glyoxalase I is a two-domain enzyme and it has the structure of a domain-swapped dimer with two active sites located at the dimer interface. In yeast, in various plants, insects and Plasmodia, glyoxalase I is four-domain, possibly the result of a further gene duplication and an additional gene fusing event.


Pssm-ID: 319965 [Multi-domain]  Cd Length: 122  Bit Score: 37.38  E-value: 7.69e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1688832407   3 MNHVGIMVGDMDKAVEFYTQALGLkvvmgntKVVEERETAIGRMCIAVFGEGFKGFNIAHLVTSDgIGLELFEMKErqar 82
Cdd:cd16358     1 MLHTMLRVGDLDRSIKFYTEVLGM-------KLLRKRDYPEGKYTLAFVGYGDEDENTVLELTYN-WGVDKYDLGT---- 68

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1688832407  83 hevdfsriGIFHFCLQTDDFEGAIKRTEAFGGKvrmdIMRYHPEDDNKPAKMVYLEDPFGNLFEL 147
Cdd:cd16358    69 --------AYGHIAIGVEDVYETCERIRKKGGK----VTREPGPMKGGTTVIAFVEDPDGYKIEL 121
Glyoxalase_6 pfam18029
Glyoxalase-like domain; This entry comprises a diverse set of domains related to the ...
 12-147 8.02e-04

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: 36.97  E-value: 8.02e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1688832407  12 DMDKAVEFYTQALGLKVVMGNTKVVEEREtaigrmciavfgegfkgfniAHLVTSDGIGLELFEMKERQARHevdfSRIg 91
Cdd:pfam18029   8 DPAALAAFWSAALGWEVVPDDTALPDPDG--------------------GGPIGGGGPRLLFQRVPEPKPGK----NRV- 62

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1688832407  92 ifHFCLQTDDFEGAIKRTEAFGGKVrmdiMRYHPEDDNKPAkmvYLEDPFGNLFEL 147
Cdd:pfam18029  63 --HLDLAVDDLEAAVARLVALGATV----LDDGDDPDGGRW---VLADPEGNEFCL 109
GlxI_Zn cd07233
Glyoxalase I that uses Zn(++) as cofactor; This family includes eukaryotic glyoxalase I that ...
 3-147 8.03e-04

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: 37.69  E-value: 8.03e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1688832407   3 MNHVGIMVGDMDKAVEFYTQALGLKVVmgNTKVVEEretaigrmciAVFGEGFKGFNIAHLVTSDGIGLELF-------- 74
Cdd:cd07233     1 FNHTMLRVKDPKKSLKFYTEVLGMKLL--RKKDFPE----------MKFSLYFLGYEDPKDIPKDPRTAWVFsregtlel 68

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1688832407  75 ------EMKERQARHEVDFSRIGIFHFCLQTDDFEGAIKRTEAFGGKVRmdimryHPEDDNKPAKMVYLEDPFGNLFEL 147
Cdd:cd07233    69 thnwgtENDEDPVYHNGNSDPRGFGHIGIAVDDVYAACERFEELGVKFK------KKPDDGKMKGIAFIKDPDGYWIEI 141
FosA cd07244
fosfomycin resistant protein subfamily FosA; This subfamily family contains FosA, a fosfomycin ...
 4-29 1.56e-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: 36.49  E-value: 1.56e-03
                          10        20
                  ....*....|....*....|....*.
gi 1688832407   4 NHVGIMVGDMDKAVEFYTQALGLKVV 29
Cdd:cd07244     3 NHITLAVSDLERSLAFYVDLLGFKPH 28
2_3_CTD_N cd07265
N-terminal domain of catechol 2,3-dioxygenase; This subfamily contains the N-terminal, ...
 1-148 3.00e-03

N-terminal domain of catechol 2,3-dioxygenase; This subfamily contains the N-terminal, non-catalytic, domain of catechol 2,3-dioxygenase. Catechol 2,3-dioxygenase (2,3-CTD, catechol:oxygen 2,3-oxidoreductase) catalyzes an extradiol cleavage of catechol to form 2-hydroxymuconate semialdehyde with the insertion of two atoms of oxygen. The enzyme is a homotetramer and contains catalytically essential Fe(II) . The reaction proceeds by an ordered bi-unit mechanism. First, catechol binds to the enzyme, this is then followed by the binding of dioxygen to form a tertiary complex, and then the aromatic ring is cleaved to produce 2-hydroxymuconate semialdehyde. Catechol 2,3-dioxygenase belongs to the type I extradiol dioxygenase family. The subunit comprises the N- and C-terminal domains of similar structure fold, resulting from an ancient gene duplication. The active site is located in a funnel-shaped space of the C-terminal domain. This subfamily represents the N-terminal domain.


Pssm-ID: 319926  Cd Length: 122  Bit Score: 35.79  E-value: 3.00e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1688832407   1 MKMNHVGIMVGDMDKAVEFYTQALGLKVVMgntkvveerETAIGRMCIAVFGEgFKGFNIAhLVTSDGIGLELFEMKerq 80
Cdd:cd07265     3 LRPGHVQLRVLDLEEAIKHYREVLGLVETG---------RDDQGRVYLKAWDE-YDHHSII-LREADTAGLDFMGFK--- 68

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1688832407  81 arhevdfsrigifhfCLQTDDFEGAIKRTEAFGGKVRMdimryHPE-DDNKPAKMVYLEDPFGNLFELY 148
Cdd:cd07265    69 ---------------VLDDADLEQLEARLQAYGVTVTR-----IPAgELPGVGRRVRFQLPSGHTMELY 117
VOC_like cd07262
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 4-49 3.03e-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: 319923 [Multi-domain]  Cd Length: 121  Bit Score: 35.67  E-value: 3.03e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1688832407   4 NHVGIMVGDMDKAVEFYTQA---LGLKVVMGNTKVVEERETAIGRMCIA 49
Cdd:cd07262     2 SHVTIGVNDLERSRAFYDAAlapLGYKRGFEDGGRVGYGLEGGPDFWVT 50
VOC_Bs_YwkD_like cd08352
vicinal oxygen chelate (VOC) family protein Bacillus subtilis YwkD and similar proteins; ...
 1-148 3.83e-03

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: 35.60  E-value: 3.83e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1688832407   1 MKMNHVGIMVGDMDKAVEFYTQALGLKVVMGNTKvvEERETAIgrmciavfgegfkgFNIAhlvtSDGIGLELFEMKERQ 80
Cdd:cd08352     1 KKIHHIAIICSDYEKSKDFYVDKLGFEIIREHYR--PERNDIK--------------LDLA----LGGYQLELFIKPDAP 60

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1688832407  81 ARHevdfSR---IGIFHFCLQTDDFEGAIKRTEAFGgkVRMDIMRYhpeDDNKPAKMVYLEDPFGNLFELY 148
Cdd:cd08352    61 ARP----SYpeaLGLRHLAFKVEDVEATVAELKSLG--IETEPIRV---DDFTGKKFTFFFDPDGLPLELY 122
ED_TypeI_classII_N cd16360
N-terminal domain of type I, class II extradiol dioxygenases; This family contains the ...
 5-149 6.98e-03

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: 34.60  E-value: 6.98e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1688832407   5 HVGIMVGDMDKAVEFYTQALGLKVVMGNTKVVEeretaigrmciavfgegFKGFNIAHlvtsdgiglelFEMKERQArhe 84
Cdd:cd16360     1 YAELGVPDLEKALEFYTDVLGLQVAKRDGNSVY-----------------LRGYEDEH-----------HSLVLYEA--- 49

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1688832407  85 vdfSRIGIFHFCLQTDDfEGAIKRTEAFGGKVRMDIMRYHPEDDNKPAKMVYLEDPFGNLFELYS 149
Cdd:cd16360    50 ---PEAGLKHFAFEVAS-EEDLERAAASLTALGCDVTWGPDGEVPGGGKGFRFQDPSGHLLELFV 110
 
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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