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Conserved domains on  [gi|1540066944|emb|VEH35781|]
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Predicted enzyme related to lactoylglutathione lyase [Cellulomonas fimi]

Protein Classification

VOC family protein( domain architecture ID 16058428)

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
Glyoxalase_6 pfam18029
Glyoxalase-like domain; This entry comprises a diverse set of domains related to the ...
 8-116 7.44e-25

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: 90.52  E-value: 7.44e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540066944   8 SFVIDCPEPLTLARFYGTLLGWEVSGDEGWAD------IREGETQCISFQRVEPYTPprwpgqdVPQQMHLDVMVQDLDA 81
Cdd:pfam18029   1 AVVLDCADPAALAAFWSAALGWEVVPDDTALPdpdgggPIGGGGPRLLFQRVPEPKP-------GKNRVHLDLAVDDLEA 73

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1540066944  82 AEPEVLALGATKAEHQ--PGETFRVFLDPAGHPFCLC 116
Cdd:pfam18029  74 AVARLVALGATVLDDGddPDGGRWVLADPEGNEFCLV 110
 
Name Accession Description Interval E-value
Glyoxalase_6 pfam18029
Glyoxalase-like domain; This entry comprises a diverse set of domains related to the ...
 8-116 7.44e-25

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: 90.52  E-value: 7.44e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540066944   8 SFVIDCPEPLTLARFYGTLLGWEVSGDEGWAD------IREGETQCISFQRVEPYTPprwpgqdVPQQMHLDVMVQDLDA 81
Cdd:pfam18029   1 AVVLDCADPAALAAFWSAALGWEVVPDDTALPdpdgggPIGGGGPRLLFQRVPEPKP-------GKNRVHLDLAVDDLEA 73

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1540066944  82 AEPEVLALGATKAEHQ--PGETFRVFLDPAGHPFCLC 116
Cdd:pfam18029  74 AVARLVALGATVLDDGddPDGGRWVLADPEGNEFCLV 110
VOC COG3324
Lactoylglutathione lyase-related enzyme, vicinal oxygen chelate (VOC) family [General function ...
 9-116 6.25e-12

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


Pssm-ID: 442553 [Multi-domain]  Cd Length: 119  Bit Score: 57.72  E-value: 6.25e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540066944   9 FVIDCPEPLTLARFYGTLLGWEVSGDEG----WADIREGETQCISFqrvepYTPPRWPGQDVPqqmHLDVMVQDLDAAEP 84
Cdd:COG3324     8 VELPVDDLERAKAFYEEVFGWTFEDDAGpggdYAEFDTDGGQVGGL-----MPGAEEPGGPGW---LLYFAVDDLDAAVA 79

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1540066944  85 EVLALGAT----KAEHQPGETFRVFLDPAGHPFCLC 116
Cdd:COG3324    80 RVEAAGGTvlrpPTDIPPWGRFAVFRDPEGNRFGLW 115
VOC cd06587
vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate (VOC) superfamily is composed ...
 8-115 6.18e-07

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: 44.44  E-value: 6.18e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540066944   8 SFVIDCPEPLTLARFYGTLLGWEVSGD---EGWADIREGETQCISFQRVEPYTPPRWPGQDvpqqmHLDVMVQDLDAAEP 84
Cdd:cd06587     1 HVALRVPDLDASVAFYEEVLGFEVVSRnegGGFAFLRLGPGLRLALLEGPEPERPGGGGLF-----HLAFEVDDVDEVDE 75

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1540066944  85 EVLALGATKAEHQPGETFR------VFLDPAGHPFCL 115
Cdd:cd06587    76 RLREAGAEGELVAPPVDDPwggrsfYFRDPDGNLIEF 112
 
Name Accession Description Interval E-value
Glyoxalase_6 pfam18029
Glyoxalase-like domain; This entry comprises a diverse set of domains related to the ...
 8-116 7.44e-25

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: 90.52  E-value: 7.44e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540066944   8 SFVIDCPEPLTLARFYGTLLGWEVSGDEGWAD------IREGETQCISFQRVEPYTPprwpgqdVPQQMHLDVMVQDLDA 81
Cdd:pfam18029   1 AVVLDCADPAALAAFWSAALGWEVVPDDTALPdpdgggPIGGGGPRLLFQRVPEPKP-------GKNRVHLDLAVDDLEA 73

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1540066944  82 AEPEVLALGATKAEHQ--PGETFRVFLDPAGHPFCLC 116
Cdd:pfam18029  74 AVARLVALGATVLDDGddPDGGRWVLADPEGNEFCLV 110
VOC COG3324
Lactoylglutathione lyase-related enzyme, vicinal oxygen chelate (VOC) family [General function ...
 9-116 6.25e-12

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


Pssm-ID: 442553 [Multi-domain]  Cd Length: 119  Bit Score: 57.72  E-value: 6.25e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540066944   9 FVIDCPEPLTLARFYGTLLGWEVSGDEG----WADIREGETQCISFqrvepYTPPRWPGQDVPqqmHLDVMVQDLDAAEP 84
Cdd:COG3324     8 VELPVDDLERAKAFYEEVFGWTFEDDAGpggdYAEFDTDGGQVGGL-----MPGAEEPGGPGW---LLYFAVDDLDAAVA 79

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1540066944  85 EVLALGAT----KAEHQPGETFRVFLDPAGHPFCLC 116
Cdd:COG3324    80 RVEAAGGTvlrpPTDIPPWGRFAVFRDPEGNRFGLW 115
VOC cd06587
vicinal oxygen chelate (VOC) family; The vicinal oxygen chelate (VOC) superfamily is composed ...
 8-115 6.18e-07

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: 44.44  E-value: 6.18e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540066944   8 SFVIDCPEPLTLARFYGTLLGWEVSGD---EGWADIREGETQCISFQRVEPYTPPRWPGQDvpqqmHLDVMVQDLDAAEP 84
Cdd:cd06587     1 HVALRVPDLDASVAFYEEVLGFEVVSRnegGGFAFLRLGPGLRLALLEGPEPERPGGGGLF-----HLAFEVDDVDEVDE 75

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1540066944  85 EVLALGATKAEHQPGETFR------VFLDPAGHPFCL 115
Cdd:cd06587    76 RLREAGAEGELVAPPVDDPwggrsfYFRDPDGNLIEF 112
GloA COG0346
Catechol 2,3-dioxygenase or related enzyme, vicinal oxygen chelate (VOC) family [Secondary ...
 20-116 3.49e-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: 42.67  E-value: 3.49e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540066944  20 ARFYGTLLGWEV-------SGDEGWADIREGETQCISFQrvepYTPPRWPGQDVPQQMHLDVMVQDLDAAEPEVLALGAT 92
Cdd:COG0346    17 LAFYTDVLGLELvkrtdfgDGGFGHAFLRLGDGTELELF----EAPGAAPAPGGGGLHHLAFRVDDLDAAYARLRAAGVE 92

                          90       100
                  ....*....|....*....|....*...
gi 1540066944  93 ----KAEHQPGETFRVFLDPAGHPFCLC 116
Cdd:COG0346    93 iegePRDRAYGYRSAYFRDPDGNLIELV 120
SgaA_N_like cd07247
N-terminal domain of Streptomyces griseus SgaA and similar domains; SgaA suppresses the growth ...
 20-115 3.14e-05

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


Pssm-ID: 319911 [Multi-domain]  Cd Length: 114  Bit Score: 39.94  E-value: 3.14e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540066944  20 ARFYGTLLGWEV----SGDEGWADIREGETQCISFQRVEPYTPPrwpgqdVPQQMHLDVMVQDLDAAEPEVLALGATKAE 95
Cdd:cd07247    15 KAFYGAVFGWTFedegDGGGDYALFTAGGGAVGGLMRAPEEVAG------APPGWLIYFAVDDLDAALARVEAAGGKVVV 88

                          90       100
                  ....*....|....*....|....
gi 1540066944  96 ---HQPGETFR-VFLDPAGHPFCL 115
Cdd:cd07247    89 pptDIPGGGRFaVFADPEGNRFGL 112
 
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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