Conserved Protein Domain Family
AroH

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cd02185: AroH 
Click on image for an interactive view with Cn3D
Chorismate mutase (AroH) is one of at least five chorismate-utilizing enzymes present in microorganisms that catalyze the rearrangement of chorismate to prephenic acid, the first committed step in the biosynthesis of aromatic amino acids. In prokaryotes, chorismate mutase may be fused to prephenate dehydratase, prephenate dehydrogenase, or 3-deoxy-D-arabino-heptulosonat-7-phosphate (DAHP) as part of a bifunctional enzyme. The AroH domain forms a homotrimer with three-fold symmetry.
Links
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Statistics
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PSSM-Id: 100026
View PSSM: cd02185
Aligned: 47 rows
Threshold Bit Score: 137.67
Threshold Setting Gi: 160901740
Created: 31-Jul-2008
Updated: 17-Jan-2013
Structure
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Program:
Drawing:
Aligned Rows:
 
active sitehomotrimer
Conserved site includes 13 residues -Click on image for an interactive view with Cn3D
Feature 1:active site [active site]
Evidence:
  • Structure:1COM; Bacillus subtilis chorismate mutase with bound prephenate
    View structure with Cn3D
  • Comment:enzyme forms a trimer with three active sites, each within the interaction surface between two subunits
  • Citation:PMID 8046752

Sequence Alignment
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Format: Row Display: Color Bits: Type Selection:
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
Feature 1            #                                                  #  #  #          ##  ##  
1DBF_A         3 IRGIRGATTVERdTEEEILQKTKQLLEKIIEENHTKp-eDVVQMLLSATPDLHAVFPAKAVRELSgwqyVPVTCMQEMDV 81
1COM_A         3 IRGIRGATTVERdTEEEILQKTKQLLEKIIEENHTKp-eDVVQMLLSATPDLHAVFPAKAVRELSgwqyVPVTCMQEMDV 81
gi 28210999    1 MYAIRGAISIDEnSVEEIRGKTLELFESILKENKINk-eDIVSILFSCTKDIDKAYPGKFLREKYdlnkVGIMHFNEMIV 79
gi 169407048   1 MQSIRGAITIEKnEVKYIEEASIKLFSEILARNNLSi-eDIVSIFISCTNDIDKDYPGKYIRENFnlknIAIMHFNEMYV 79
gi 158320597   3 IIGIRGAITVNEnSTVAIDAASYEMMKKIIELNSIVe-dDVISITFTMTKDLNQRYPSAIVREKLnwknTPILNFEEKDI 81
gi 160901740   7 IVGIRGATSLNEdHPIELTENVIELWNEIMNKNDIS---RIISVIFSVTPDIKSLNPATILREKLdlnnVPFMSLEEASF 83
gi 4928945     2 IRGIRGAITVERnEAGEIIAATETLLREMVRANDVAa-hDVSFVLISVTDDITAAFPAQALRRLDgwtyVPVMCTREIPV 80
gi 56963659    2 IRGVRGATTVTKnEAQEIEQATETLVREMVSQNALQp-eQIAQVIVTATNDIDATFPAKAVRHLQgwqyVPVMCAQEIPV 80
gi 149183316   3 IRGVRGAITISSdSEKEIISSTELLLLEMINKNGIEp-eQVASVFISATADIHTAFPARALRKIKnwkyVPVLSMQEMEV 81
gi 16414541    1 MRAIRGATTIESnTPEEIYTATKELFEEILTQNGITdseSLTSVIITVTEDIFAAFPAKAVRETHgfeyVPVMGMQEIPV 80
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
Feature 1           #    ##                  #      #    
1DBF_A        82 TGGLKKCIRVMMTVQTdvp--qdqIRHVYLEKAVVLRPDL 119
1COM_A        82 TGGLKKCIRVMMTVQTdvp--qdqIRHVYLEKAVVLRPDL 119
gi 28210999   80 ENSLNLCIRILILLNGhn----lnIKYVYLGKAKKLRDDL 115
gi 169407048  80 EGSMPLCIRILILIDKknknieenIEYVYLGRAKTLRKDL 119
gi 158320597  82 IHSLEKCIRVLIYAYSdka--kkdVAHVYLKEAEKLRPDL 119
gi 160901740  84 NDSRKKIIRVLIICESs------tQNFVYLHEAKNLRTKK 117
gi 4928945    81 PGSLPRCIRVMMTVETdkr--qdeICHVYLKDAAMLRPDL 118
gi 56963659   81 KGSLPLCIRVMMTVNTslk--qeeIKHVFLEGAIVLRPDL 118
gi 149183316  82 KDSLNKCIRIMIHWNTekk--qedIRHVYLRKAHTLRPDL 119
gi 16414541   81 PNSLPMCIRFMVFTDLhkp--ltaINHVYLHGAKVLRPDL 118

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