3LM4


Conserved Protein Domain Family
BphC-JF8_N_like

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cd09013: BphC-JF8_N_like 
Click on image for an interactive view with Cn3D
N-terminal, non-catalytic, domain of BphC_JF8, (2,3-dihydroxybiphenyl 1,2-dioxygenase) from Bacillus sp. JF8, and similar proteins
2,3-dihydroxybiphenyl 1,2-dioxygenase (BphC) catalyzes the extradiol ring cleavage reaction of 2,3-dihydroxybiphenyl, a key step in the polychlorinated biphenyls (PCBs) degradation pathway (bph pathway). BphC belongs to the type I extradiol dioxygenase family, which requires a metal ion in the active site in its catalytic mechanism. Polychlorinated biphenyl degrading bacteria demonstrate a multiplicity of BphCs. This subfamily of BphC is represented by the enzyme purified from the thermophilic biphenyl and naphthalene degrader, Bacillus sp. JF8. The members in this family of BphC enzymes may use either Mn(II) or Fe(II) as cofactors. The enzyme purified from Bacillus sp. JF8 is Mn(II)-dependent, however, the enzyme from Rhodococcus jostii RHAI has Fe(II) bound to it. BphC_JF8 is thermostable and its optimum activity is at 85 degrees C. The enzymes in this family have an internal duplication. This family represents the N-terminal repeat.
Statistics
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PSSM-Id: 319955
View PSSM: cd09013
Aligned: 10 rows
Threshold Bit Score: 174.845
Threshold Setting Gi: 283946136
Created: 2-Jun-2010
Updated: 18-Aug-2016
Structure
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Program:
Drawing:
Aligned Rows:
 
tetramer
Conserved site includes 12 residues -Click on image for an interactive view with Cn3D
Feature 1:tetramer interface [polypeptide binding site]
Evidence:
  • Structure:3LM4_A/B/C/D; Rhodococcus 2,3-dihydroxy biphenyl dioxygenase tetramer interface, 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        ##  ##                    #                  #  #                   ###         
3LM4_A         6 RFDIAHLARAELFSPKPQETLDFFTKFLGXYVTHregqSVYLRGYEdpYPWSLKITEApeaGXGHAAXRTSSpeALERRA 85
gi 27378930    6 ILDLAHLGHMELLTPKPDESLKFFVDVMGMTISGrkgeSVYLRGWDdyERYSLKLTASktsGMEHMALRARSqqALERRV 85
gi 283818173   5 IWDLAHLGHVELLTPKLDQSTRFFTEIMGMSITAtagdSIYLRAYDdyEHHTLKLTASpqaGMRHFAWRARSpqALQRRV 84
gi 283815759   5 PHYLSQLAHLELFSPNVEQTVAFLTNIVGLDETGrddtSVYLRAWGdyFHHTLKITYRaepGLATLGWRADSeeALAEVV 84
gi 476042     15 VPRVHNLHHVELLTPKPNESLDFFTRVLGLHETHregqSVYLRGSGewGQYSTILTESptaGLGHMGWQVAEpeHVQGWG 94
gi 163846921   5 IFDTHQLAHVEILTPKPDQTLWFFRDLLGMEVTTqqgqSVYLRAYEdwYHHTLKITEArepGLGHVAWRASSpqALERRV 84
gi 55978433    6 IFDVHQLAHVEIYTPNPEGTLWFFRDLLGMEVTKqegqSVYMRAYEdwYHHTLKITEApkpGLGHVAWRTSSpqALERRV 85
gi 400767      9 IFDVAQLAHVELLSPKLEESIVFFTKYLGMEVTAragnSVYLRAYEdfYHNTLKITESaeaGLGHVGWRASSpqALERRV 88
gi 283946136   2 TPRLVKLGHIALSTPDLERSLWFFRDVVGLDEVEradgVVHLRAWGerEHHSLSLRAGe-tGVDHIAWRASApgDVEAFA 80
gi 75397869    2 TAEIAKFGHIALITPNLEKSVWFFRDIVGLEEVDrqgdTIFLRAWGdwEHHTLSLTPGnraRVDHIAWRTKRpeDVETFA 81
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
Feature 1                                               #   #
3LM4_A        86 KSLTDGNVDG-TWSEDQf--GYGKTFEYQSPDGHNLQLLWEAEK 126
gi 27378930   86 AALKGSGFDI-GWIDGDm--GQGPTFRCRDPDGHIVELYYETEW 126
gi 283818173  85 EAIQQTPYAI-GWNEGGl--GHGPAFEFHSPDGHLTEIYFETEK 125
gi 283815759  85 AYLESIGAGI-GWVDADp--GRGRAYRFQSPDGHTHEVFWDVVW 125
gi 476042     95 RRLKDAGVEH-RFEAGGssfAQGDTVSFEGPYGHKMELFYDFER 137
gi 163846921  85 KALEASGFGR-GWLDGDl--GHGPAYQFTTPDGHPMEILWEVDY 125
gi 55978433   86 KALEATGLGK-GWIDGDl--GHGPAYRFTTPDGHPMELLWEVEY 126
gi 400767     89 LELEKSGLGR-GWIDGDi--GHGKAYQFTTPDGHQMEIFFEVEY 129
gi 283946136  81 ARLEAGGVAVeRVPAGTe-aGQGDAIRFSSPGGHPYEIYFDVDR 123
gi 75397869   82 EQLKAKGTEV-QWIEPGeekGQGKAIRFRLPNGYPFEIYYDVEK 124

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