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Conserved domains on  [gi|512673084|ref|WP_016473197|]
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MULTISPECIES: VOC family protein [Streptomyces]

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 ...
18-194 3.64e-12

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 pfam13468:

Pssm-ID: 472697  Cd Length: 175  Bit Score: 63.12  E-value: 3.64e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512673084   18 HVLVRVHDLHRAVQDF-RAAGFDVAYATAPERKALHAHVWFPQGPVIELLTTPPGARwmRLPVDLRFGRGAGDrmvrwar 96
Cdd:pfam13468   3 HVVLAVPDLDEAAARFaRALGFTVTPGGRHPGMGTANALIMFGDGYLELLAVDPEAP--APPRGRWFGLDRLA------- 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512673084   97 QDEGFCDLALlvEHAELAGVTRRLADDGVPCGRavhwtRRRPDGGETRFAFSYPRAGRLPF-LVTPYD---PPQHPSGVR 172
Cdd:pfam13468  74 DGEGLLGWAL--RTDDIDAVAARLRAAGVEPGR-----RVRPDGGDLRWRLLFLADGALPAgGLLPFLiqwGTSHPALTR 146
                         170       180
                  ....*....|....*....|..
gi 512673084  173 HPNGARALTRIVLGVHPDDLPA 194
Cdd:pfam13468 147 HPNGATGLASLVIAVPDPDATA 168
 
Name Accession Description Interval E-value
Glyoxalase_3 pfam13468
Glyoxalase-like domain; This domain is related to the Glyoxalase domain pfam00903.
18-194 3.64e-12

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


Pssm-ID: 433233  Cd Length: 175  Bit Score: 63.12  E-value: 3.64e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512673084   18 HVLVRVHDLHRAVQDF-RAAGFDVAYATAPERKALHAHVWFPQGPVIELLTTPPGARwmRLPVDLRFGRGAGDrmvrwar 96
Cdd:pfam13468   3 HVVLAVPDLDEAAARFaRALGFTVTPGGRHPGMGTANALIMFGDGYLELLAVDPEAP--APPRGRWFGLDRLA------- 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512673084   97 QDEGFCDLALlvEHAELAGVTRRLADDGVPCGRavhwtRRRPDGGETRFAFSYPRAGRLPF-LVTPYD---PPQHPSGVR 172
Cdd:pfam13468  74 DGEGLLGWAL--RTDDIDAVAARLRAAGVEPGR-----RVRPDGGDLRWRLLFLADGALPAgGLLPFLiqwGTSHPALTR 146
                         170       180
                  ....*....|....*....|..
gi 512673084  173 HPNGARALTRIVLGVHPDDLPA 194
Cdd:pfam13468 147 HPNGATGLASLVIAVPDPDATA 168
 
Name Accession Description Interval E-value
Glyoxalase_3 pfam13468
Glyoxalase-like domain; This domain is related to the Glyoxalase domain pfam00903.
18-194 3.64e-12

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


Pssm-ID: 433233  Cd Length: 175  Bit Score: 63.12  E-value: 3.64e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512673084   18 HVLVRVHDLHRAVQDF-RAAGFDVAYATAPERKALHAHVWFPQGPVIELLTTPPGARwmRLPVDLRFGRGAGDrmvrwar 96
Cdd:pfam13468   3 HVVLAVPDLDEAAARFaRALGFTVTPGGRHPGMGTANALIMFGDGYLELLAVDPEAP--APPRGRWFGLDRLA------- 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512673084   97 QDEGFCDLALlvEHAELAGVTRRLADDGVPCGRavhwtRRRPDGGETRFAFSYPRAGRLPF-LVTPYD---PPQHPSGVR 172
Cdd:pfam13468  74 DGEGLLGWAL--RTDDIDAVAARLRAAGVEPGR-----RVRPDGGDLRWRLLFLADGALPAgGLLPFLiqwGTSHPALTR 146
                         170       180
                  ....*....|....*....|..
gi 512673084  173 HPNGARALTRIVLGVHPDDLPA 194
Cdd:pfam13468 147 HPNGATGLASLVIAVPDPDATA 168
 
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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