1KMY,2ZI8,2WL9,3VB0,2EHZ,2EI2,1EIQ,1KWB,2WL3


Conserved Protein Domain Family
BphC1-RGP6_C_like

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cd07237: BphC1-RGP6_C_like 
Click on image for an interactive view with Cn3D
C-terminal domain of 2,3-dihydroxybiphenyl 1,2-dioxygenase
This subfamily contains the C-terminal, catalytic, domain of BphC1-RGP6 and similar proteins. BphC catalyzes the extradiol ring cleavage reaction of 2,3-dihydroxybiphenyl, the third step in the polychlorinated biphenyls (PCBs) degradation pathway (bph pathway). This subfamily of BphCs belongs to the type I extradiol dioxygenase family, which require a metal in the active site in its catalytic mechanism. Polychlorinated biphenyl degrading bacteria demonstrate a multiplicity of BphCs. For example, three types of BphC enzymes have been found in Rhodococcus globerulus (BphC1-RGP6 - BphC3-RGP6), all three enzymes are type I extradiol dioxygenases. BphC1-RGP6 has an internal duplication, it is a two-domain dioxygenase which forms octamers, and has Fe(II) at the catalytic site. Its C-terminal repeat is represented in this subfamily. BphC2-RGP6 and BphC3-RGP6 are one-domain dioxygenases, they belong to a different subfamily of the ED_TypeI_classII_C (C-terminal domain of type I, class II extradiol dioxygenases) family.
Statistics
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PSSM-Id: 319902
View PSSM: cd07237
Aligned: 32 rows
Threshold Bit Score: 180.547
Threshold Setting Gi: 4455074
Created: 18-Mar-2009
Updated: 18-Aug-2016
Structure
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Program:
Drawing:
Aligned Rows:
 
Fe binding siteactive site
Conserved site includes 3 residues -Click on image for an interactive view with Cn3D
Feature 1: Fe binding site [ion binding site], 3 residue positions
Conserved feature residue pattern:H H EClick to see conserved feature residue pattern help
Evidence:
  • Comment:Fe(II) binding site
  • Structure:1KMY_A; Fe(II) binding site of 2,3-dihydroxybiphenyl 1,2-dioxygenase from Burkholderia cepacia, by 3.5A distance.
    View structure with Cn3D
  • Citation:PMID 9857017

Sequence Alignment
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Format: Row Display: Color Bits: Type Selection:
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
Feature 1                  #                                                                    
1KMY_A      134 SGFLTGEQGLGHFVRCVPD---SDKALAFYTDvLGFQLSDVIdmkmg-pdvtvPAYFLHCNERHHTLAIAAFPl------ 203
3VB0_A      136 GEEANGIFGLGHLVVIVAD---RAKTQSFFTDvLGFGLSDRVtwp------eaDIFFLHCNQRHHTVALSAPAlgl---k 203
gi 3913216  135 VDFVTEDQGFGHIVVMVDD---YDETMRFYREvLGLQTSDLVkvgag--gvqtRMAFMRCNPRQHSLAFWAGDs------ 203
gi 3243172  136 VTFITGQQGFGHIVLSTDD---YEGQVKFYHEtLGFLISDYNdlllp-grppaHITFFHVNGRHHSLALGNMPl------ 205
gi 33330425 137 PGFITGEMGMGHLAITSRK---PEQMRRFWQEvFDARHSDHIveria--gvtlDIDFFRVNPRHHSIAIAVVKdmpmdpi 211
gi 15384206 140 GRFSTGDQGLGHIGHIILRqenPQKAYEFYARvLGMRGSVEYhipiphigitaKPIFLHSNDRDHSVAFLGGPa------ 213
gi 3337417  141 GKFLTGDQGLGHCIVRQND---VEAARKFYSL-LGFRGDVEYrlplp-ngmtaELTFMHCNARDHSIAFGAMPa------ 209
2EHZ_A      141 GKFVTGDQGLGHCIVRQTD---VAEAHKFYSL-LGFRGDVEYriplp-ngmtaELSFMHCNARDHSIAFGAMPa------ 209
gi 127815   141 GKFVTGDQGLGHCIVRQTD---VAAAHKFYSL-LGFRGDVEYriplp-ngmtaELSFMHCNARDHSIAFGAMPa------ 209
2EI2_A      141 GKFVTGDQGLGHCIVRQTD---VAEAHKFYSL-LGFRGDVEYriplp-ngmtaELSFMHCNARDHSIAFGAMPa------ 209
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
Feature 1            #                                                  #                       
1KMY_A      204 pKRIHHFMLEVASLDDVGFAFDRVDADG-LITSTLGRHTNDHMVSFYASTPSGVEVEYGWSARtvd--rswVVVRHDSPS 280
3VB0_A      204 pGMVHHLMLEAKSKEQVDRAFAAVKRLGyDVLMTIGQHSNDKVYSFYMMAPAGFAVELGFGGQvigdleswHVGFYDAPS 283
gi 3913216  204 tTRLNHFMLQTQTLDQTGMTLDRCFHGG-IPATNLGRHVNDYAVSFYITTPSGFMIEYGWGVRevv--sdyPVDKYRSVS 280
gi 3243172  206 pKRFNHFMLEASSLDDVGFALDRAKNAGaHILMDLGRHSNDKVISFYVMTPSGWAVEFGWGSLivdd-eiwHVTHHPEPS 284
gi 33330425 212 rTRIQHMNLLTTSVSGLTDAFLRCRKLGfEMAHEIGEHPNDREQSFYVMTPSGFEMELGWNALe------vDEETWRTTS 285
gi 15384206 214 aKRINHLMIEVDNIDDVGYTHDIVRKRQiPVAVQLGKHSNDQMVSFYSANPSNWLFEYGALGRra-----tYQSEYYVSD 288
gi 3337417  210 aKRLNHLMIEYTHIEDLGCTHQLFTKEKiDIALQLGIHSNDKALTFYGATPSGWLIEPGWRGApa-----iAESEYYVGD 284
2EHZ_A      210 aKRLNHLMLEYTHMEDLGYTHQQFVKNEiDIALQLGIHANDKALTFYGATPSGWLIEPGWRGAta-----iDEAEYYVGD 284
gi 127815   210 aKRLNHLMLEYTHMEDLGYTHQQFVKNEiDIALQLGIHANDKALTFYGATPSGWLIEPGWRGAta-----iDEAEYYVGD 284
2EI2_A      210 aKRLNHLMLEYTHMEDLGYTHQQFVKNEiDIALQLGIHANDKALTFYGATPSGWLIEPGWRGAta-----iDEAEYYVGD 284

                ....*
Feature 1            
1KMY_A      281 MWGHK 285
3VB0_A      284 IWGHE 288
gi 3913216  281 IWGHR 285
gi 3243172  285 IWGHK 289
gi 33330425 286 YKRHQ 290
gi 15384206 289 IWGHE 293
gi 3337417  285 IFGHT 289
2EHZ_A      285 IFGHG 289
gi 127815   285 IFGHG 289
2EI2_A      285 IFGHG 289

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