1B4U,2PW6,3BCZ,1BOU


Conserved Protein Domain Family
Extradiol_Dioxygenase_3B_like

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cd07320: Extradiol_Dioxygenase_3B_like 
Click on image for an interactive view with Cn3D
Subunit B of Class III Extradiol ring-cleavage 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 of the aromatic ring. Intradiol enzymes cleave the aromatic ring between two hydroxyl groups, whereas extradiol enzymes cleave the aromatic ring between a hydroxylated carbon and an adjacent non-hydroxylated carbon. Extradiol dioxygenases can be further divided into three classes. Class I and II enzymes are evolutionary related and show sequence similarity, with the two-domain class II enzymes evolving from the class I enzyme through gene duplication. Class III enzymes are different in sequence and structure and usually have two subunits, designated A and B. This model represents the catalytic subunit B of extradiol dioxygenase class III enzymes. Enzymes belonging to this family include Protocatechuate 4,5-dioxygenase (LigAB), 2'-aminobiphenyl-2,3-diol 1,2-dioxygenase (CarB), 4,5-DOPA Dioxygenase, 2,3-dihydroxyphenylpropionate 1,2-dioxygenase, and 3,4-dihydroxyphenylacetate (homoprotocatechuate) 2,3-dioxygenase (HPCD). There are also some family members that do not show the typical dioxygenase activity.
Statistics
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PSSM-Id: 153371
View PSSM: cd07320
Aligned: 7 rows
Threshold Bit Score: 234.695
Threshold Setting Gi: 161172364
Created: 6-Jan-2010
Updated: 2-Oct-2020
Structure
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Program:
Drawing:
Aligned Rows:
 
metal bindingactive site
Conserved site includes 2 residues -Click on image for an interactive view with Cn3D
Feature 1:metal binding site [ion binding site]
Evidence:
  • Structure:1BOU_B, Sphingomonas paucimobilis LigAB coordinates Fe(II).
    View structure with Cn3D
  • Structure:2PW6_A; Escherichia coli Uncharacterized Protein Jw3007 coordinates Zn.
    View structure with Cn3D
  • Comment:Some members may not have a conserved metal binding site.

Sequence Alignment
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Format: Row Display: Color Bits: Type Selection:
Feature 1              #                                                                         
1B4U_B         6 TGITSSHIPalgaaiqtgtsdndywgpvfkgyqpirdwikqpgnmpDVVILVYNdhasafdmniiptFAIGCAETfkpad 85  Sphingomonas pa...
2PW6_A        16 PALFLGHGSpxnvlednlytr-------------swqklgxtlprpQAIVVVSAhwf-------trgTGVTAXETpptih 75  Escherichia coli
3BCZ_A        39 RAIIAPHAGytycgscaah-----------------aykqvdpsitRRIFILGPshhv-----plsrCALSSVDIyrt-- 94  human
1BOU_B         6 TGITSSHIPalgaaiqtgtsdndywgpvfkgyqpirdwikqpgnmpDVVILVYNdhasafdmniiptFAIGCAETfkpad 85  Sphingomonas pa...
BAG80151       6 LAAKITHVPsmylselpgknhgcrqg---aidghkeiskrcremgvDTIIVFDThwlv------nsaYHINCADHfegvy 76  Escherichia col...
Q8R8N9         8 HPPIIVHEVgrgeerkiqktids----------lenisqeikqkrpDTVIVITPhgyv-----fkdaVSITTLPSlegdl 72  Thermoanaerobac...
YP_002577874   4 LAAIVPHGDeilipedeesarlhn--------amielgerikekkvDEYIFVSPhhl-------riqTHMAIMLTeyleg 68  Aciduliprofundu...
Feature 1                                                                                        
1B4U_B        86 eg-----wgprpvPDVKGHPDLAWHIAQSlildefDMTImnqm---------dvdHGCTVPLSMIFgepe--ewpCKVIP 149 Sphingomonas pa...
2PW6_A        76 dfggfpqalydthYPAPGSPALAQRLVELla--piPVTLdkea--------wgfdHGSWGVLIKXYpd-----adIPXVQ 140 Escherichia coli
3BCZ_A        95 -----------plYDLRIDQKIYGELWKTg-----XFERxslqt-------dedeHSIEXHLPYTAkaxeshkdeFTIIP 151 human
1BOU_B        86 eg-----wgprpvPDVKGHPDLAWHIAQSlildefDMTImnqm---------dvdHGCTVPLSMIFgepe--ewpCKVIP 149 Sphingomonas pa...
BAG80151      77 tsnelphfirdmtYNYEGNPELGQLIADEalk-lgVRAKahnip------slkleYGTLVPMRYMNed-----khFKVVS 144 Escherichia col...
Q8R8N9        73 sq----fgarevkFKFENDLDLAREIMEEtkkrniPIAEvseelikkyvlpkkldHGTIVPLYFVTkhy----pdFKLIH 144 Thermoanaerobac...
YP_002577874  69 swk---yknlrfrRKIKCNKDLAWEIYEKtrk-slPVVGvnf----------galEGELSKICLDWgt------lIPLYF 128 Aciduliprofundu...
Feature 1                                                                                        
1B4U_B       150 FPVNvvtyp----ppsgKRCFALGDSIRaavesfpedlNVHVWGTGGMSHqlqgp----------ragliNKEFDLNFID 215 Sphingomonas pa...
2PW6_A       141 LSIDssk--------paAWHFEXGRKLAalr-----deGIXLVASGNVVHnlrtvkwh----gdsspypwATSFNEYVKA 203 Escherichia coli
3BCZ_A       152 VLVGal---------seSKEQEFGKLFSkyl----adpSNLFVVSSDFCHwgqrfrysyydesqgeiyrsIEHLDKXGXS 218 human
1BOU_B       150 FPVNvvtyp----ppsgKRCFALGDSIRaavesfpedlNVHVWGTGGMSHqlqgp----------ragliNKEFDLNFID 215 Sphingomonas pa...
BAG80151     145 ISAFctv-------hdfADSRKLGEAILkaie--qydgTVAVLASGSLSHrfiddqraee-gmnsytrefDRQMDERVVK 214 Escherichia col...
Q8R8N9       145 MSYGfl---------pfEKLYEFGVAIKdain--ksdrRVVFIASGDLSHkltpnsp-------ngytpkGEVFDKTLLQ 206 Thermoanaerobac...
YP_002577874 129 LPKRkmvlmtpareipyESLIDFGKIVGeivm--nskkRIGVIISADHAHahrkdgp-------ygyhpdADYYDKYIME 199 Aciduliprofundu...
Feature 1                                      #                                                 
1B4U_B       216 KLisdpeelskmph----iqylresgsegvELVMWLIMRGALPekvr------dlyTFYHIpa-------sNTALGAMIL 278 Sphingomonas pa...
2PW6_A       204 NLtwqgpveqhplvnyldheggtlsnptpeHYLPLLYVLGAWDgqep------itiPVEGIex-------gSLSXLSVQI 270 Escherichia coli
3BCZ_A       219 IIeqldpvsfsn--------ylkkyhnticGRHPIGVLLNAITelqkngxnxsfsfLNYAQssqcrnwqdsSVSYAAGAL 290 human
1BOU_B       216 KLisdpeelskmph----iqylresgsegvELVMWLIMRGALPekvr------dlyTFYHIpa-------sNTALGAMIL 278 Sphingomonas pa...
BAG80151     215 LWregqfkefcnml-----peyadycygegNMHDTVMLLGMLGwdkyd---gkvefITELFps-------sGTGQVNAVF 279 Escherichia col...
Q8R8N9       207 LLsemkveevirm------dkdlieeaaecGFRSVCVMLGVLDgyevn----akvlSHEGPf---------GVGYGVAKF 267 Thermoanaerobac...
YP_002577874 200 NLenldmllklk--------ektienakpdSFWQLLILNGILKgnpl-----klkkKVYGLp--------tYFGMAVAWY 258 Aciduliprofundu...

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