2KF2,2REZ


Conserved Protein Domain Family
TcmN_ARO-CYC_like

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cd08860: TcmN_ARO-CYC_like 
Click on image for an interactive view with Cn3D
N-terminal aromatase/cyclase domain of the multifunctional protein tetracenomycin (TcmN) and related domains
This family includes the N-terminal aromatase/cyclase (ARO/CYC) domain of Streptomyces glaucescens TcmN, and related domains. It belongs to the SRPBCC (START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC) domain superfamily of proteins that bind hydrophobic ligands. SRPBCC domains have a deep hydrophobic ligand-binding pocket. ARO/CYC domains participate in the diversification of aromatic polyketides by promoting polyketide cyclization. They occur in two architectural forms, monodomain and didomain. Monodomain aromatase/cyclases have a single ARO/CYC domain. For some, such as TcmN, this single domain is linked to a second domain of unrelated function. TcmN is a multifunctional cyclase-dehydratase-O-methyl transferase. Its N-terminal ARO/CYC domain participates in polyketide binding and catalysis; it promotes C9-C14 first-ring (and C7-C16 second-ring) cyclizations. Its C-terminal domain has O-methyltransferase activity. Didomain aromatase/cyclases contain two ARO/CYC domains, and they biosynthesize C7-C12 first ring cyclized polyketides. These latter domains belong to a different subfamily in the SRPBCC superfamily.
Statistics
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PSSM-Id: 176869
View PSSM: cd08860
Aligned: 7 rows
Threshold Bit Score: 216.963
Threshold Setting Gi: 45259320
Created: 5-Mar-2010
Updated: 2-Oct-2020
Structure
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Program:
Drawing:
Aligned Rows:
 
Conserved site includes 6 residues -Click on image for an interactive view with Cn3D
Feature 1:active site [active site]
Evidence:
  • Comment:based on substrate docking simulations and mutagenesis of tetracenomycin ARO/CYC

Sequence Alignment
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Format: Row Display: Color Bits: Type Selection:
Feature 1                                     #                                # #            
2KF2_A      3 GHTDNEITIAAPMELVWTMTNDIEKWPGLFsEYASVEVLGRDddKVTFRLTMHPDa-dGKVWSWVSERVADPv-tRTVRA 80  Streptomyces coeli...
2REZ_A      6 ARTDNSIVVNAPFELVWDVTNDIEAWPELFsEYAEAEILRQDgdGFDFRLKTRPDa-nGRVWEWVSHRVPDKg-sRTVRA 83  Streptomyces glauc...
CAM58801    3 GRTDNSVVIDAPVQLVWDMTNDVSQWAVLFeEYAESEVLAVDgdTVRFRLTTQPDe-dGKQWSWVSERTRDLe-nRTVTA 80  Streptomyces sp. A...
YP_714580   3 GHTDNSILIDADIDTVWTITNDLPTWPDLFtEYASVDIIESNgnTFKFRLTMHPDe-nGTAWSWVSERTLDPv-nRQVRA 80  Frankia alni ACN14a
ABX71144    3 SSTDNSVHIAAPLDVVWRLTNDVRTWPDLFtEYASVEVLHEDgpTVRFRLTMVPDd-dGTVWSWVSERTTDVa-aHSVRA 80  Streptomyces sangl...
CAM34342    3 GHTDNSTVIDAPLDLVWDMTNDVASWPDLFsEYAEATVLERDgnRIVFRLAMHPDa-gGTVWSWVSERILDPv-aRTVHA 80  Streptomyces tendae
CAE51178    2 PRIENSIVIGADPRLVFDVTNDIARWSEIFdEYSHAKVLSEE--RDGRWTEIVFEltnEEGAGWRSWRILDHrelVAVAE 79  Streptomyces resis...
Feature 1      #                         # #                                      
2KF2_A     81 QRVEtGPFQYMNIVWEYAETAeGTVMRWTQDFAMKPDAPVddawMTDNINRNSRTQMALIRDRIEQAA 148 Streptomyces coelicolor A3(2)
2REZ_A     84 HRVEtGPFAYMNLHWTYRAVAgGTEMRWVQEFDMKPGAPFdnahMTAHLNTTTRANMERIKKIIEDRH 151 Streptomyces glaucescens
CAM58801   81 RRLDnGLFEYMNIRWEYTEGPdGVRMRWIQEFSMKPSAPVddsgAEDHLNRQTVKEMARIKKLIEEAA 148 Streptomyces sp. A2991200
YP_714580  81 YRVEtGPFEYMHIHWTYTPEGtGTRMRWVQDFHMRPAAPLndeqMTARINTNTAREMAVIRDKVERAA 148 Frankia alni ACN14a
ABX71144   81 HRIEtGPFVYMRIRWSYEPDGeGTKMRWRQEFEAKPDAPFddeaITKRINENTRIQMDVIKKKVEAAA 148 Streptomyces sanglieri
CAM34342   81 RRVEtGNFKYMWLFWEYTTEDdGVRLRWVQDFELKPGLPMddaaMTDRLNANSVAQLELIKEKIEAVA 148 Streptomyces tendae
CAE51178   80 RRDPlYPFAYMHLRWSYQEVPeGTLMTWIQDFELDDRFEVplatVLERMNTHTRHNQAGIKQKIESGA 147 Streptomyces resistomycificus

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