3B59


Conserved Protein Domain Family
BphC5-RrK37_N_like

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cd08362: BphC5-RrK37_N_like 
Click on image for an interactive view with Cn3D
N-terminal, non-catalytic, domain of BphC5 (2,3-dihydroxybiphenyl 1,2-dioxygenase) from Rhodococcus rhodochrous K37, and similar proteins
2,3-dihydroxybiphenyl 1,2-dioxygenase (BphC) catalyzes the extradiol ring cleavage reaction of 2,3-dihydroxybiphenyl, the third step in the polychlorinated biphenyls (PCBs) degradation pathway (bph pathway). The enzyme contains a N-terminal and a C-terminal domain of similar structure fold, resulting from an ancient gene duplication. BphC belongs to the type I extradiol dioxygenase family, which requires a metal in the active site for its catalytic activity. Polychlorinated biphenyl degrading bacteria demonstrate multiplicity of BphCs. Bacterium Rhodococcus rhodochrous K37 has eight genes encoding BphC enzymes. This family includes the N-terminal domain of BphC5-RrK37. The crystal structure of the protein from Novosphingobium aromaticivorans has a Mn(II)in the active site, although most proteins of type I extradiol dioxygenases are activated by Fe(II).
Statistics
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PSSM-Id: 319950
View PSSM: cd08362
Aligned: 21 rows
Threshold Bit Score: 145.47
Threshold Setting Gi: 930004355
Created: 18-Mar-2009
Updated: 18-Aug-2016
Structure
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Program:
Drawing:
Aligned Rows:
 
putative
Conserved site includes 2 residues -Click on image for an interactive view with Cn3D
Feature 1:putative oligomer interface [polypeptide binding site]
Evidence:
  • Structure:3B59_ A/B/C/D/E; oligomer interface of BphC5 from Novosphingobium aromaticivorans, defined by 4A distance.
    View structure with Cn3D

Sequence Alignment
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Format: Row Display: Color Bits: Type Selection:
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
Feature 1                   #          #                                                         
3B59_A         6 VTEIRYVGYGVKDFDAEKAFYADvWGLEPVGEDaNNAWFKAQGadEHHVVQLRRADenRIDVIALAADSrsDVDALRASV 85
gi 42475484    8 LRRLRSVELRTHAAADSAEFYSEvWGLSVVESGrEGAWLRGTGd-QHHALQLTQADrnGLGRISFAVSTpaEVDDAARRV 86
gi 21388675   11 LRSLRSVALGVPDPVSARDFYHEvWGLSTVDEDyDRYWLRATGs-EHHVLRLGTSKtnRLERVAFAVATrrEIDEAAKRL 89
gi 750081054  16 PRSLRSVALLVPDPKASIDFYTEsWGLSAVDRGdDVAWLRGTGe-EHHILQIGHHEqnALGRIVLALGTrrEVDDAARAL 94
gi 378785697   9 ITHLRYVGIAAPDFERATEFYRTaWGLEQVAEDgGIAFFGSPAapENYLLRVRKDSakRMDVVAFGVRQasDVDALAERL 88
gi 733425813   9 LRALRHVGLRTSAFDESVAFYAGpWGLEIVERTdDAVYLRAAGp-EHHVLALYRSAsnALDHVAFAVPTpaEVDAAAAWV 87
gi 317395576   7 ITHLRHISLITPVLEEQAEFYEKiWGLDKVSEDgDSVYFRGAGs-ENHILNLKRGEkaGLHHIAFGMVDknAVDRAAEIL 85
gi 947460996   6 AGQLRSIAIGVTDLDAAERFYNDtWRLETVAKTeDAVYLRGAGp-FHHILALHRSVrpDVRHVTFSVATraDLDAIAART 84
gi 944095007   2 VTHVRHVGLGVPDLGKAQEFYEKrWQLELVRTEdDRLYLGAGCp-ESHVLRLRSAAepRVDLISLAASSprEVDEVAERV 80
gi 943645256   2 ITHVRSVALGVPDIGAAREFFEKhWQLDLVATDsDRVFLGAGCq-ESHVLRLRATAepRVDLLCLAAATvaDVDEIAERV 80
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
Feature 1                                                  
3B59_A        86 EAAGCKVASEPavl-atPGGGYGFRFFSPDGLLFEVSSDVAK 126
gi 42475484   87 AERGILVVQGPgpv-ddAGGGYGLRIVDPEGRIIELIADTLA 127
gi 21388675   90 DALGVPMLRSPgpi-ddAGGGYGLSLVDPEGRCIELSTDTFA 130
gi 750081054  95 ESLGVPIVHEPgpl-ddAAGGYGVQFVDPEGRLIELSVERFA 135
gi 378785697  89 GQAGVRIDREPgkl-dtPGGGHGFRFWDLDGRLIEISSDVAE 129
gi 733425813  88 EAEGTTILEKPgpl-drPGAGYGFRCLDPENRVLEISAENHA 128
gi 317395576  86 ASKGIPVISPPgyl-deEGKGYGLRFADPENRCIELSAWVEM 126
gi 947460996  85 PAAGGRLLSEPaav-dePGGGTAVTIADPQGRILRFVHGDER 125
gi 944095007  81 ARHPQGRLLREpgerqdLGGGYAVWFLDCDGRTVEVSAEVTG 122
gi 943645256  81 AAHPLGRLVSPpatcgdVGGGYRFRFLDCEGRTVEVSSRVAV 122

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