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Conserved domains on  [gi|119393695|gb|ABL74382|]
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putative glyoxalase/bleomycin resistance protein [Actinomyces sp. Lu 9419]

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; ...
 11-156 2.53e-68

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: 204.87  E-value: 2.53e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119393695  11 AVHHVAYTVPDLDQAVEFFTEVIGAELAYTLVQDAAGDW----MTRKLDVDATATARIAMLRLGPVTNLELFEYAAPDQR 86
Cdd:cd16361    1 GVNHVGITVPDLDAAVEFYTDVLGAEVVYRSTPLAEGDRgggeMRAAGFVPGFARARIAMLRLGPGPGIELFEYKGPEQR 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119393695  87 RQLPRNSDWGGHHLAIHVADVDAAAEYLRAQPGVRVLGDPETITDGPIAGDRWVYFATPWGMQLELINLP 156
Cdd:cd16361   81 APVPRNSDVGIFHFALQVDDVEAAAERLAAAGGKVLMGPREIPDGGPGKGNRMVYLRDPWGTLIELVSHP 150
 
Name Accession Description Interval E-value
VOC_ShValD_like cd16361
vicinal oxygen chelate (VOC) family protein similar to Streptomyces hygroscopicus ValD protein; ...
 11-156 2.53e-68

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: 204.87  E-value: 2.53e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119393695  11 AVHHVAYTVPDLDQAVEFFTEVIGAELAYTLVQDAAGDW----MTRKLDVDATATARIAMLRLGPVTNLELFEYAAPDQR 86
Cdd:cd16361    1 GVNHVGITVPDLDAAVEFYTDVLGAEVVYRSTPLAEGDRgggeMRAAGFVPGFARARIAMLRLGPGPGIELFEYKGPEQR 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119393695  87 RQLPRNSDWGGHHLAIHVADVDAAAEYLRAQPGVRVLGDPETITDGPIAGDRWVYFATPWGMQLELINLP 156
Cdd:cd16361   81 APVPRNSDVGIFHFALQVDDVEAAAERLAAAGGKVLMGPREIPDGGPGKGNRMVYLRDPWGTLIELVSHP 150
GloA COG0346
Catechol 2,3-dioxygenase or related enzyme, vicinal oxygen chelate (VOC) family [Secondary ...
 12-158 1.31e-24

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: 92.75  E-value: 1.31e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119393695  12 VHHVAYTVPDLDQAVEFFTEVIGAELAYTLVQDAAGdwmtrkldvdatatARIAMLRLGPVTNLELFEYAAPDqrrqlPR 91
Cdd:COG0346    3 LHHVTLRVSDLEASLAFYTDVLGLELVKRTDFGDGG--------------FGHAFLRLGDGTELELFEAPGAA-----PA 63

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 119393695  92 NSDWGGHHLAIHVADVDAAAEYLRAQpGVRVLGDPETITDGPiagdRWVYFATPWGMQLELINLPAG 158
Cdd:COG0346   64 PGGGGLHHLAFRVDDLDAAYARLRAA-GVEIEGEPRDRAYGY----RSAYFRDPDGNLIELVEPPPG 125
Glyoxalase pfam00903
Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;
12-152 5.49e-13

Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;


Pssm-ID: 395724 [Multi-domain]  Cd Length: 121  Bit Score: 62.47  E-value: 5.49e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119393695   12 VHHVAYTVPDLDQAVEFFTEVIGAELAYTLVQDAAGDWMTRKLDVDATAtariamlrlgpvtnLELFEYAAPDQRRQLpr 91
Cdd:pfam00903   2 IDHVALRVGDLEKSLDFYTDVLGFKLVEETDAGEEGGLRSAFFLAGGRV--------------LELLLNETPPPAAAG-- 65

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 119393695   92 nsdWGGHHLAIH---VADVDAAAEYLRAQpGVRVLGDPETITDgpiaGDRWVYFATPWGMQLEL 152
Cdd:pfam00903  66 ---FGGHHIAFIafsVDDVDAAYDRLKAA-GVEIVREPGRHGW----GGRYSYFRDPDGNLIEL 121
PRK11478 PRK11478
VOC family protein;
8-152 6.20e-09

VOC family protein;


Pssm-ID: 183156 [Multi-domain]  Cd Length: 129  Bit Score: 51.82  E-value: 6.20e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119393695   8 GAVAVHHVAYTVPDLDQAVEFFTEVIGAELAYTLVQDAAGDWmtrKLDvdatatariamLRLGPVTNLELFEYAAPDQRR 87
Cdd:PRK11478   3 GLKQVHHIAIIATDYAVSKAFYCDILGFTLQSEVYREARDSW---KGD-----------LALNGQYVIELFSFPFPPERP 68

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 119393695  88 QLPRNSdwGGHHLAIHVADVDAAAEYLRAQpGVRVlgdpETITDGPIAGDRWVYFATPWGMQLEL 152
Cdd:PRK11478  69 SRPEAC--GLRHLAFSVDDIDAAVAHLESH-NVKC----EAIRVDPYTQKRFTFFNDPDGLPLEL 126
metmalonyl_epim TIGR03081
methylmalonyl-CoA epimerase; Members of this protein family are the enzyme methylmalonyl-CoA ...
 12-125 9.84e-09

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: 51.17  E-value: 9.84e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119393695   12 VHHVAYTVPDLDQAVEFFTEVIGAELAYTLVQDAAGdwmtrkldvdatatARIAMLRLGPvTNLELFEYAAPDQ--RRQL 89
Cdd:TIGR03081   2 IDHVGIAVPDLEEAAKFYEDVLGAQVSEIEELPEQG--------------VKVVFIALGN-TKVELLEPLGEDSpiAKFL 66

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 119393695   90 PRNSDwGGHHLAIHVADVDAAAEYLRAQpGVRVLGD 125
Cdd:TIGR03081  67 EKNGG-GIHHIAIEVDDIEAALETLKEK-GVRLIDE 100
 
Name Accession Description Interval E-value
VOC_ShValD_like cd16361
vicinal oxygen chelate (VOC) family protein similar to Streptomyces hygroscopicus ValD protein; ...
 11-156 2.53e-68

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: 204.87  E-value: 2.53e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119393695  11 AVHHVAYTVPDLDQAVEFFTEVIGAELAYTLVQDAAGDW----MTRKLDVDATATARIAMLRLGPVTNLELFEYAAPDQR 86
Cdd:cd16361    1 GVNHVGITVPDLDAAVEFYTDVLGAEVVYRSTPLAEGDRgggeMRAAGFVPGFARARIAMLRLGPGPGIELFEYKGPEQR 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119393695  87 RQLPRNSDWGGHHLAIHVADVDAAAEYLRAQPGVRVLGDPETITDGPIAGDRWVYFATPWGMQLELINLP 156
Cdd:cd16361   81 APVPRNSDVGIFHFALQVDDVEAAAERLAAAGGKVLMGPREIPDGGPGKGNRMVYLRDPWGTLIELVSHP 150
GloA COG0346
Catechol 2,3-dioxygenase or related enzyme, vicinal oxygen chelate (VOC) family [Secondary ...
 12-158 1.31e-24

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: 92.75  E-value: 1.31e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119393695  12 VHHVAYTVPDLDQAVEFFTEVIGAELAYTLVQDAAGdwmtrkldvdatatARIAMLRLGPVTNLELFEYAAPDqrrqlPR 91
Cdd:COG0346    3 LHHVTLRVSDLEASLAFYTDVLGLELVKRTDFGDGG--------------FGHAFLRLGDGTELELFEAPGAA-----PA 63

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 119393695  92 NSDWGGHHLAIHVADVDAAAEYLRAQpGVRVLGDPETITDGPiagdRWVYFATPWGMQLELINLPAG 158
Cdd:COG0346   64 PGGGGLHHLAFRVDDLDAAYARLRAA-GVEIEGEPRDRAYGY----RSAYFRDPDGNLIELVEPPPG 125
VOC cd06587
vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate (VOC) superfamily is composed ...
 14-152 1.42e-14

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: 66.39  E-value: 1.42e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119393695  14 HVAYTVPDLDQAVEFFTEVIGAELAYTLVQDaagdwmtrkldvdatataRIAMLRLGPVTNLELFEYAAPdqrrqlPRNS 93
Cdd:cd06587    1 HVALRVPDLDASVAFYEEVLGFEVVSRNEGG------------------GFAFLRLGPGLRLALLEGPEP------ERPG 56

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 119393695  94 DWGGHHLAIHVADVDAAAEYLRAQpGVRVLGDPETITDGPiaGDRWVYFATPWGMQLEL 152
Cdd:cd06587   57 GGGLFHLAFEVDDVDEVDERLREA-GAEGELVAPPVDDPW--GGRSFYFRDPDGNLIEF 112
MMCE cd07249
Methylmalonyl-CoA epimerase (MMCE); MMCE, also called methylmalonyl-CoA racemase (EC 5.1.99.1) ...
 12-152 9.07e-14

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: 64.52  E-value: 9.07e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119393695  12 VHHVAYTVPDLDQAVEFFTEVIGAELAYTLVQDAAGdwmtrkldvdatatARIAMLRLGPvTNLELFEYAAPD-QRRQLP 90
Cdd:cd07249    1 LDHIGIAVPDLDEALKFYEDVLGVKVSEPEELEEQG--------------VRVAFLELGN-TQIELLEPLGEDsPIAKFL 65

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 119393695  91 RNSDWGGHHLAIHVADVDAAAEYLRAQpGVRVLGDPETItdgPIAGDRWVYFATPW--GMQLEL 152
Cdd:cd07249   66 DKKGGGLHHIAFEVDDIDAAVEELKAQ-GVRLLSEGPRI---GAHGKRVAFLHPKDtgGVLIEL 125
VOC_Bs_YwkD_like cd08352
vicinal oxygen chelate (VOC) family protein Bacillus subtilis YwkD and similar proteins; ...
 11-152 1.70e-13

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: 63.72  E-value: 1.70e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119393695  11 AVHHVAYTVPDLDQAVEFFTEVIGAELAYTLVQDAAGDWmtrKLDvdatatariamLRLGPVTnLELFEYAAPDQRrqLP 90
Cdd:cd08352    2 KIHHIAIICSDYEKSKDFYVDKLGFEIIREHYRPERNDI---KLD-----------LALGGYQ-LELFIKPDAPAR--PS 64

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 119393695  91 RNSDWGGHHLAIHVADVDAAAEYLRAQpGVRVlgdpETITDGPIAGDRWVYFATPWGMQLEL 152
Cdd:cd08352   65 YPEALGLRHLAFKVEDVEATVAELKSL-GIET----EPIRVDDFTGKKFTFFFDPDGLPLEL 121
Glyoxalase pfam00903
Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;
12-152 5.49e-13

Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;


Pssm-ID: 395724 [Multi-domain]  Cd Length: 121  Bit Score: 62.47  E-value: 5.49e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119393695   12 VHHVAYTVPDLDQAVEFFTEVIGAELAYTLVQDAAGDWMTRKLDVDATAtariamlrlgpvtnLELFEYAAPDQRRQLpr 91
Cdd:pfam00903   2 IDHVALRVGDLEKSLDFYTDVLGFKLVEETDAGEEGGLRSAFFLAGGRV--------------LELLLNETPPPAAAG-- 65

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 119393695   92 nsdWGGHHLAIH---VADVDAAAEYLRAQpGVRVLGDPETITDgpiaGDRWVYFATPWGMQLEL 152
Cdd:pfam00903  66 ---FGGHHIAFIafsVDDVDAAYDRLKAA-GVEIVREPGRHGW----GGRYSYFRDPDGNLIEL 121
Glyoxalase_4 pfam13669
Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;
13-142 1.26e-10

Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;


Pssm-ID: 463951 [Multi-domain]  Cd Length: 109  Bit Score: 55.75  E-value: 1.26e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119393695   13 HHVAYTVPDLDQAVEFFTEVIGAELAYTLVQDAAGdwmtrkldvdatATARIAMLRLGPVTnLELfeyAAPDQRRQLPRN 92
Cdd:pfam13669   1 HHVGIAVPDLDRALALWGALLGLGPEGDYRSEPQN------------VDLAFALLGDGPVE-VEL---IQPLDGDSPLAR 64

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 119393695   93 SDWGGHHLAIHVADVDAAAEYLRAQpGVRVLGDPetitDGPIAGDRWVYF 142
Cdd:pfam13669  65 HGPGLHHLAYWVDDLDAAVARLLDQ-GYRVAPKG----PRAGAAGRRVAF 109
VOC COG3324
Lactoylglutathione lyase-related enzyme, vicinal oxygen chelate (VOC) family [General function ...
 9-153 1.43e-09

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


Pssm-ID: 442553 [Multi-domain]  Cd Length: 119  Bit Score: 53.10  E-value: 1.43e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119393695   9 AVAVHHVAYTVPDLDQAVEFFTEVIGAElaytlvqdaagdwmtrkLDVDATATARIAMLRLGPVTNLELFeyaapdQRRQ 88
Cdd:COG3324    2 PGTIVWVELPVDDLERAKAFYEEVFGWT-----------------FEDDAGPGGDYAEFDTDGGQVGGLM------PGAE 58

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 119393695  89 LPRNSDWgghHLAIHVADVDAAAEYLRAQpGVRVLGDPETITDgpiaGDRWVYFATPWGMQLELI 153
Cdd:COG3324   59 EPGGPGW---LLYFAVDDLDAAVARVEAA-GGTVLRPPTDIPP----WGRFAVFRDPEGNRFGLW 115
VOC_like cd08353
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 13-125 4.81e-09

uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate (VOC) superfamily is composed of structurally related proteins with paired beta.alpha.beta.beta.beta motifs that provide a metal coordination environment with two or three open or readily accessible coordination sites to promote direct electrophilic participation of the metal ion in catalysis. VOC domain is found in a variety of structurally related metalloproteins, including the bleomycin resistance protein, glyoxalase I, and type I ring-cleaving dioxygenases. A bound metal ion is required for protein activities for the members of this superfamily. A variety of metal ions have been found in the catalytic centers of these proteins including Fe(II), Mn(II), Zn(II), Ni(II) and Mg(II). The protein superfamily contains members with or without domain swapping. The proteins of this family share three conserved metal binding amino acids with the type I extradiol dioxygenases, which shows no domain swapping.


Pssm-ID: 319941  Cd Length: 142  Bit Score: 52.19  E-value: 4.81e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119393695  13 HHVAYTVPDLDQAVEFFTEvIGAEL-AYTLVQdaaGDWMTRKLDVDAtATARIAMLRL-GPVTNLELFEYAAPDQR---R 87
Cdd:cd08353    5 DHVGIVVEDLDAAIAFFTE-LGLELeGRMTVE---GEWADRVVGLDG-VRVEIAMLRTpDGHGRLELSKFLTPAAIpghR 79

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 119393695  88 QLPRNSdWGGHHLAIHVADVDAAAEYLRAQpGVRVLGD 125
Cdd:cd08353   80 PAPANA-LGLRHVAFAVDDIDAVVARLRKH-GAELVGE 115
PRK11478 PRK11478
VOC family protein;
8-152 6.20e-09

VOC family protein;


Pssm-ID: 183156 [Multi-domain]  Cd Length: 129  Bit Score: 51.82  E-value: 6.20e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119393695   8 GAVAVHHVAYTVPDLDQAVEFFTEVIGAELAYTLVQDAAGDWmtrKLDvdatatariamLRLGPVTNLELFEYAAPDQRR 87
Cdd:PRK11478   3 GLKQVHHIAIIATDYAVSKAFYCDILGFTLQSEVYREARDSW---KGD-----------LALNGQYVIELFSFPFPPERP 68

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 119393695  88 QLPRNSdwGGHHLAIHVADVDAAAEYLRAQpGVRVlgdpETITDGPIAGDRWVYFATPWGMQLEL 152
Cdd:PRK11478  69 SRPEAC--GLRHLAFSVDDIDAAVAHLESH-NVKC----EAIRVDPYTQKRFTFFNDPDGLPLEL 126
metmalonyl_epim TIGR03081
methylmalonyl-CoA epimerase; Members of this protein family are the enzyme methylmalonyl-CoA ...
 12-125 9.84e-09

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: 51.17  E-value: 9.84e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119393695   12 VHHVAYTVPDLDQAVEFFTEVIGAELAYTLVQDAAGdwmtrkldvdatatARIAMLRLGPvTNLELFEYAAPDQ--RRQL 89
Cdd:TIGR03081   2 IDHVGIAVPDLEEAAKFYEDVLGAQVSEIEELPEQG--------------VKVVFIALGN-TKVELLEPLGEDSpiAKFL 66

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 119393695   90 PRNSDwGGHHLAIHVADVDAAAEYLRAQpGVRVLGD 125
Cdd:TIGR03081  67 EKNGG-GIHHIAIEVDDIEAALETLKEK-GVRLIDE 100
CatE COG2514
Catechol-2,3-dioxygenase [Secondary metabolites biosynthesis, transport and catabolism];
11-153 1.36e-08

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


Pssm-ID: 442004 [Multi-domain]  Cd Length: 141  Bit Score: 51.11  E-value: 1.36e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119393695  11 AVHHVAYTVPDLDQAVEFFTEVIGAELAYtlvqdaagdwmtrkldvdatATARIAMLRL-GPVTNLELFEyaAPDQRrql 89
Cdd:COG2514    3 RLGHVTLRVRDLERSAAFYTDVLGLEVVE--------------------REGGRVYLRAdGGEHLLVLEE--APGAP--- 57

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 119393695  90 PRNSDWGGHHLAIHV---ADVDAAAEYLRAQpGVRVLGdpetitdgpiAGDRWV----YFATPWGMQLELI 153
Cdd:COG2514   58 PRPGAAGLDHVAFRVpsrADLDAALARLAAA-GVPVEG----------AVDHGVgeslYFRDPDGNLIELY 117
VOC_like cd07245
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
 12-152 1.93e-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: 319909 [Multi-domain]  Cd Length: 117  Bit Score: 50.39  E-value: 1.93e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119393695  12 VHHVAYTVPDLDQAVEFFTEVIGAElaytlvqdaagdwmtrKLDVDATATARIAMLRLGPVTNLELFEYAAPDqrrQLPR 91
Cdd:cd07245    1 LDHVALACPDLERARRFYTDVLGLE----------------EVPRPPFLKFGGAWLYLGGGQQIHLVVEQNPS---ELPR 61

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 119393695  92 NSDWG-GHHLAIHVADVDAAAEYLRAQpGVrvlgdpETITDGPIAGDRW-VYFATPWGMQLEL 152
Cdd:cd07245   62 PEHPGrDRHPSFSVPDLDALKQRLKEA-GI------PYTESTSPGGGVTqLFFRDPDGNRLEF 117
HppD COG3185
4-hydroxyphenylpyruvate dioxygenase and related hemolysins [Amino acid transport and ...
 7-131 4.38e-06

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: 45.65  E-value: 4.38e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119393695   7 PGAVAVHHVAYTVP--DLDQAVEFFTEVIGAELaytlvqdaagdwmTRKLDVDATATA-RIAMLRL--GPVTnLELFEYA 81
Cdd:COG3185  142 AGLTRIDHIGIAVPrgDLDEWVLFYEDVLGFEE-------------IREEDIEDPYQGvRSAVLQSpdGKVR-IPLNEPT 207

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 119393695  82 APD-Q-RRQLPRNSDWGGHHLAIHVADVDAAAEYLRAQpGVRVLGDPETITD 131
Cdd:COG3185  208 SPDsQiAEFLEKYRGEGIQHIAFATDDIEATVAALRAR-GVRFLDIPDNYYD 258
GloA COG0346
Catechol 2,3-dioxygenase or related enzyme, vicinal oxygen chelate (VOC) family [Secondary ...
 98-168 1.18e-03

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: 37.28  E-value: 1.18e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 119393695  98 HHLAIHVADVDAAAEYLRAQPGVRVLGDpetiTDGPIAGDRWVYFATPWGMQLELINLPAGAPFEQQTEVR 168
Cdd:COG0346    4 HHVTLRVSDLEASLAFYTDVLGLELVKR----TDFGDGGFGHAFLRLGDGTELELFEAPGAAPAPGGGGLH 70
ED_TypeI_classII_N cd16360
N-terminal domain of type I, class II extradiol dioxygenases; This family contains the ...
 14-153 1.25e-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: 36.91  E-value: 1.25e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119393695  14 HVAYTVPDLDQAVEFFTEVIGAELAYtlvQDAAGDWMtrKLDVDATATARIamlRLGPVTNLELFEYAAPDQrrqlprns 93
Cdd:cd16360    1 YAELGVPDLEKALEFYTDVLGLQVAK---RDGNSVYL--RGYEDEHHSLVL---YEAPEAGLKHFAFEVASE-------- 64

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 119393695  94 dwgghhlaihvADVDAAAEYLRAQpGVRVLGDPETITDGpiaGDRWVYFATPWGMQLELI 153
Cdd:cd16360   65 -----------EDLERAAASLTAL-GCDVTWGPDGEVPG---GGKGFRFQDPSGHLLELF 109
VOC_BsYyaH cd07241
vicinal oxygen chelate (VOC) family protein similar to Bacillus subtilis YyaH; The vicinal ...
 12-132 1.40e-03

vicinal oxygen chelate (VOC) family protein similar to Bacillus subtilis YyaH; The vicinal oxygen chelate (VOC) superfamily is composed of structurally related proteins with paired beta.alpha.beta.beta.beta motifs that provide a metal coordination environment with two or three open or readily accessible coordination sites to promote direct electrophilic participation of the metal ion in catalysis. VOC domain is found in a variety of structurally related metalloproteins, including the bleomycin resistance protein, glyoxalase I, and type I ring-cleaving dioxygenases. A bound metal ion is required for protein activities for the members of this superfamily. A variety of metal ions have been found in the catalytic centers of these proteins including Fe(II), Mn(II), Zn(II), Ni(II) and Mg(II). The protein superfamily contains members with or without domain swapping. The proteins of this family share three conserved metal binding amino acids with the type I extradiol dioxygenases, which shows no domain swapping.


Pssm-ID: 319905  Cd Length: 125  Bit Score: 37.00  E-value: 1.40e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119393695  12 VHHVAYTVPDLDQAVEFFTEVIGAElAYTLVQDAAGDWMTRKLDVDatATARIAMLRLGPVTNLElfeyaaPDQRRQlpr 91
Cdd:cd07241    2 IEHVALWTNDLERMKDFYVKYFGAE-SNDIYHNKKKGFRSYFLTFD--SGARLELMSRPDVTDPD------KEVERT--- 69

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 119393695  92 nsdwGGHHLAIHVAD---VDAAAEYLRAQpGVRVLGDPETITDG 132
Cdd:cd07241   70 ----GLAHIAFSVGSkeaVDELTERLRAD-GYAVVGGPRTTGDG 108
BphC5-RrK37_N_like cd08362
N-terminal, non-catalytic, domain of BphC5 (2,3-dihydroxybiphenyl 1,2-dioxygenase) from ...
 12-153 1.53e-03

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: 36.84  E-value: 1.53e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119393695  12 VHHVAYTVPDLDQAVEFFTEVIGAELAYTlVQDAAgdWMtrkldvdaTATAR---IAMLRLGPVTNLELFEYAAPDqrrq 88
Cdd:cd08362    4 LRYVALGVPDLAAEREFYTEVWGLEEVAE-DDDVV--YL--------RAEGSehhVLRLRQSDENRLDLIAFAAAT---- 68

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 119393695  89 lprnsdwgghhlaihVADVDAAAEYLRAQpGVRVLGDPETItDGPIAGDRwVYFATPWGMQLELI 153
Cdd:cd08362   69 ---------------RADVDALAARLAAA-GVRILSEPGPL-DDPGGGYG-FRFFDPDGRTIEVS 115
ED_TypeI_classII_C cd08343
C-terminal domain of type I, class II extradiol dioxygenases, catalytic domain; This family ...
 14-152 3.74e-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: 3.74e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119393695  14 HVAYTVPDLDQAVEFFTEVIGAELAYTLVQ--DAAGDWMTRKLDVDAtatARIAMLRlGPVTNLelfeyaapdqrrqlpr 91
Cdd:cd08343    2 HVVLCSPDVEASRDFYTDVLGFRVSDRIVDpgVDGGAFLHCDRGTDH---HTVALAG-GPHPGL---------------- 61

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 119393695  92 nsdwggHHLAIHVADVDA---AAEYLRAQ-------PGVRVLGDpeTITDgpiagdrwvYFATPWGMQLEL 152
Cdd:cd08343   62 ------HHVAFEVHDLDDvgrGHDRLREKgykiewgPGRHGLGS--QVFD---------YWFDPSGNRVEY 115
 
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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