2ZW6,2ZW5,2ZW4


Conserved Protein Domain Family
BAT

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cd16354: BAT 
Click on image for an interactive view with Cn3D
Bleomycin N-Acetyltransferase and similar proteins
BlmB, encodes a bleomycin N-acetyltransferase, designated BAT, which inactivates Bm using acetyl-coenzyme A (AcCoA). BAT forms a dimer structure via interaction of its C-terminal domains in the monomers. The N-terminal domain of BAT has a tunnel with two entrances: a wide entrance that accommodates the metal-binding domain of Bm and a narrow entrance that accommodates acetyl-CoA (AcCoA). A groove formed on the dimer interface of two BAT C-terminal domains forms the DNA-binding domain of Bm. In a ternary complex of BAT, BmA(2), and CoA, a thiol group of CoA is positioned near the primary amine of Bm at the midpoint of the tunnel and ensures efficient transfer of an acetyl group from AcCoA to the primary amine of Bm. BAT belongs to vicinal oxygen chelate (VOC) superfamily that 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 domain is found in a variety of structurally related metalloproteins, including thiocoraline, bleomycin resistance protein, glyoxalase I, and type I ring-cleaving dioxygenases. 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). The protein superfamily contains members with or without domain swapping. The proteins of this family share three conserved metal binding amino acids with the type I extradiol dioxygenases, which shows no domain swapping.
Statistics
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PSSM-Id: 319961
View PSSM: cd16354
Aligned: 9 rows
Threshold Bit Score: 137.196
Threshold Setting Gi: 506282659
Created: 29-Dec-2015
Updated: 18-Aug-2016
Structure
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Program:
Drawing:
Aligned Rows:
 
homodimer
Conserved site includes 24 residues -Click on image for an interactive view with Cn3D
Feature 1:homodimer interface [polypeptide binding site]
Evidence:
  • Structure:2ZW6: Streptomyces verticillus bleomycin N-acetyltransferase forms a homodimer, contacts at 4A
    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        ####                                    ########  #          #  ########   ##   
2ZW6_A       185 VITELPVRDVAATLRLVEaALGARTAFAIG-DPPEFAEAaLTPWSAGPRFRLAAvpgpgpvEPVRLHLDAAGtaDSLHRR 263
gi 671528201 192 AHPVLPVRDVEATLDLLHaGLGLEPGFRVG-EPARYAAArLGPWSVGPGLRLTLtpggepiAAVTVALDAGVplAGLADR 270
gi 506282659 177 LQPVVQVVDVAATAALLVaVLGARVSFIAG-EPAHVAGIvLGPWSTGPGLRLVRppr-gecAPVELVLDVGPgfVGLRES 254
gi 491222964 182 VEVSLPVSDIRSELALLEsVLRARAGYELG-DPPELAGVvFGAWSVAPALRLVAapp--piTPLVINVDAGTefDAAYRR 258
gi 119433802 177 AEVALPVRDVAATLTLLReALGGRTLFSVG-DPPEVAGVsFGPWSVGPRLQLVStrr-wriARVTLYLDVGVelEALHDR 254
gi 752663145  88 VEATLPVLDVAAELDVLRaVLGARVLYEVG-DPPAMVGVvFGPWSVGPGLRLVVars--piAPITVTVDVGTefDSAHRR 164
2ZW5_A       185 VITELPVRDVAATLRLVEaALGARTAFAIG-DPPEFAEAaLTPWSAGPRFRLAAvpgpgpvEPVRLHLDAAGtaDSLHRR 263
2ZW4_A       185 VITELPVRDVAATLRLVEaALGARTAFAIG-DPPEFAEAaLTPWSAGPRFRLAAvpgpgpvEPVRLHLDAAGtaDSLHRR 263
gi 521056635 177 IRSQVPVRDVMSTADLLVnLLGLQVIYQFGePEVEFARLgLSRWNGGPALDLQRsg---eiAPLTLGVDIGVpvDPVYQA 253
                         90       100       110
                 ....*....|....*....|....*....|....*.
Feature 1                                            
2ZW6_A       264 AVDAGARVDgPPVRRPWGRSEFVITLPEGHELTVSA 299
gi 671528201 271 WTAAGGRTGgPVRRMPWGDHELCCLLPEGHRLLIGG 306
gi 506282659 255 ALASGVAGVePIVDQPWGRREFALRLPEGHRVVLST 290
gi 491222964 259 ALAAGADIAaEPVEQPWGASEFVLRLTDGHQLVVSG 294
gi 119433802 255 AVDAGADVVqRPTEQPWGMRECVVQLPEGHHIVLTA 290
gi 752663145 165 AAASGADIAsAPVEQPWGMREFVLRLSDGHQLVVTG 200
2ZW5_A       264 AVDAGARVDgPPVRRPWGRSEFVITLPEGHELTVSA 299
2ZW4_A       264 AVDAGARVDgPPVRRPWGRSEFVITLPEGHELTVSA 299
gi 521056635 254 VLAAGLAVDaRPADMPWHRREFAFRLPEGHAITVSG 289

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