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Conserved domains on  [gi|1418734434|gb|RAY99890|]
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glyoxalase [Enterobacter asburiae]

Protein Classification

VOC family protein( domain architecture ID 50733)

vicinal oxygen chelate (VOC) family protein uses a metal center to coordinate a substrate, intermediate, or transition state through vicinal oxygen atoms

CATH:  3.10.180.10
Gene Ontology:  GO:0046872|GO:0003824
PubMed:  21820381|11076500

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
VOC super family cl14632
vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate (VOC) superfamily is composed ...
22-137 7.46e-06

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.


The actual alignment was detected with superfamily member cd07264:

Pssm-ID: 472697 [Multi-domain]  Cd Length: 118  Bit Score: 42.32  E-value: 7.46e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418734434  22 DTESSSAFYVQTLGLPLKPMEGNTDYLLTEEDQLEgvkhFAVWPLAQAAASCFGEEkwpvehPIPQGWVEYEVQDLDSAT 101
Cdd:cd07264    10 DFAASLRFYRDVLGLPPRFLHEEGEYAEFDTGETK----LALFSRKEMARSGGPDR------RGSAFELGFEVDDVEATV 79
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1418734434 102 RVLSEKGYRLLVANRLEPWGQTVTRLLSPEGLLTGL 137
Cdd:cd07264    80 EELVERGAEFVREPANKPWGQTVAYVRDPDGNLIEI 115
 
Name Accession Description Interval E-value
VOC_like cd07264
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
22-137 7.46e-06

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: 42.32  E-value: 7.46e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418734434  22 DTESSSAFYVQTLGLPLKPMEGNTDYLLTEEDQLEgvkhFAVWPLAQAAASCFGEEkwpvehPIPQGWVEYEVQDLDSAT 101
Cdd:cd07264    10 DFAASLRFYRDVLGLPPRFLHEEGEYAEFDTGETK----LALFSRKEMARSGGPDR------RGSAFELGFEVDDVEATV 79
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1418734434 102 RVLSEKGYRLLVANRLEPWGQTVTRLLSPEGLLTGL 137
Cdd:cd07264    80 EELVERGAEFVREPANKPWGQTVAYVRDPDGNLIEI 115
GloA COG0346
Catechol 2,3-dioxygenase or related enzyme, vicinal oxygen chelate (VOC) family [Secondary ...
19-134 9.10e-06

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: 42.29  E-value: 9.10e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418734434  19 ISRDTESSSAFYVQTLGLPLkpmegntdylLTEEDQLEGVKHFAVWPLAQAAASCFGEEKWPVEHPIPQGWVE--YEVQD 96
Cdd:COG0346     9 RVSDLEASLAFYTDVLGLEL----------VKRTDFGDGGFGHAFLRLGDGTELELFEAPGAAPAPGGGGLHHlaFRVDD 78
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1418734434  97 LDSATRVLSEKGYRLLVANRLEPWGQTVTRLLSPEGLL 134
Cdd:COG0346    79 LDAAYARLRAAGVEIEGEPRDRAYGYRSAYFRDPDGNL 116
Glyoxalase pfam00903
Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;
21-134 3.12e-04

Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;


Pssm-ID: 395724 [Multi-domain]  Cd Length: 121  Bit Score: 38.20  E-value: 3.12e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418734434  21 RDTESSSAFYVQTLGLplkpmegntdYLLTEEDQLEGVKHFAVWPLAQAAASCFGEEkWPVEHPIPQ------GWVEYEV 94
Cdd:pfam00903  10 GDLEKSLDFYTDVLGF----------KLVEETDAGEEGGLRSAFFLAGGRVLELLLN-ETPPPAAAGfgghhiAFIAFSV 78
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1418734434  95 QDLDSATRVLSEKGYRLLVANRLEPWGQTVTRLLSPEGLL 134
Cdd:pfam00903  79 DDVDAAYDRLKAAGVEIVREPGRHGWGGRYSYFRDPDGNL 118
 
Name Accession Description Interval E-value
VOC_like cd07264
uncharacterized subfamily of vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate ...
22-137 7.46e-06

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: 42.32  E-value: 7.46e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418734434  22 DTESSSAFYVQTLGLPLKPMEGNTDYLLTEEDQLEgvkhFAVWPLAQAAASCFGEEkwpvehPIPQGWVEYEVQDLDSAT 101
Cdd:cd07264    10 DFAASLRFYRDVLGLPPRFLHEEGEYAEFDTGETK----LALFSRKEMARSGGPDR------RGSAFELGFEVDDVEATV 79
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1418734434 102 RVLSEKGYRLLVANRLEPWGQTVTRLLSPEGLLTGL 137
Cdd:cd07264    80 EELVERGAEFVREPANKPWGQTVAYVRDPDGNLIEI 115
GloA COG0346
Catechol 2,3-dioxygenase or related enzyme, vicinal oxygen chelate (VOC) family [Secondary ...
19-134 9.10e-06

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: 42.29  E-value: 9.10e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418734434  19 ISRDTESSSAFYVQTLGLPLkpmegntdylLTEEDQLEGVKHFAVWPLAQAAASCFGEEKWPVEHPIPQGWVE--YEVQD 96
Cdd:COG0346     9 RVSDLEASLAFYTDVLGLEL----------VKRTDFGDGGFGHAFLRLGDGTELELFEAPGAAPAPGGGGLHHlaFRVDD 78
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1418734434  97 LDSATRVLSEKGYRLLVANRLEPWGQTVTRLLSPEGLL 134
Cdd:COG0346    79 LDAAYARLRAAGVEIEGEPRDRAYGYRSAYFRDPDGNL 116
Glyoxalase pfam00903
Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;
21-134 3.12e-04

Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily;


Pssm-ID: 395724 [Multi-domain]  Cd Length: 121  Bit Score: 38.20  E-value: 3.12e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418734434  21 RDTESSSAFYVQTLGLplkpmegntdYLLTEEDQLEGVKHFAVWPLAQAAASCFGEEkWPVEHPIPQ------GWVEYEV 94
Cdd:pfam00903  10 GDLEKSLDFYTDVLGF----------KLVEETDAGEEGGLRSAFFLAGGRVLELLLN-ETPPPAAAGfgghhiAFIAFSV 78
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1418734434  95 QDLDSATRVLSEKGYRLLVANRLEPWGQTVTRLLSPEGLL 134
Cdd:pfam00903  79 DDVDAAYDRLKAAGVEIVREPGRHGWGGRYSYFRDPDGNL 118
 
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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