1DBF,1COM,1UFY,1XHO


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: 2-Oct-2020
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:
Feature 1            #                                                  #  #  #          ##  ##  
1DBF_A         3 IRGIRGATTVERdTEEEILQKTKQLLEKIIEENHTKp-eDVVQMLLSATPDLHAVFPAKAVRELSgwqyVPVTCMQEMDV 81  Bacillus subtilis
1COM_A         3 IRGIRGATTVERdTEEEILQKTKQLLEKIIEENHTKp-eDVVQMLLSATPDLHAVFPAKAVRELSgwqyVPVTCMQEMDV 81  Bacillus subtilis
NP_781943      1 MYAIRGAISIDEnSVEEIRGKTLELFESILKENKINk-eDIVSILFSCTKDIDKAYPGKFLREKYdlnkVGIMHFNEMIV 79  Clostridium tet...
ACA55459       1 MQSIRGAITIEKnEVKYIEEASIKLFSEILARNNLSi-eDIVSIFISCTNDIDKDYPGKYIRENFnlknIAIMHFNEMYV 79  Clostridium bot...
YP_001513104   3 IIGIRGAITVNEnSTVAIDAASYEMMKKIIELNSIVe-dDVISITFTMTKDLNQRYPSAIVREKLnwknTPILNFEEKDI 81  Alkaliphilus or...
YP_001567321   7 IVGIRGATSLNEdHPIELTENVIELWNEIMNKNDIS---RIISVIFSVTPDIKSLNPATILREKLdlnnVPFMSLEEASF 83  Petrotoga mobil...
AAD33790       2 IRGIRGAITVERnEAGEIIAATETLLREMVRANDVAa-hDVSFVLISVTDDITAAFPAQALRRLDgwtyVPVMCTREIPV 80  Geobacillus ste...
YP_175390      2 IRGVRGATTVTKnEAQEIEQATETLVREMVSQNALQp-eQIAQVIVTATNDIDATFPAKAVRHLQgwqyVPVMCAQEIPV 80  Bacillus clausi...
ZP_01861756    3 IRGVRGAITISSdSEKEIISSTELLLLEMINKNGIEp-eQVASVFISATADIHTAFPARALRKIKnwkyVPVLSMQEMEV 81  Bacillus sp. SG-1
CAC97270       1 MRAIRGATTIESnTPEEIYTATKELFEEILTQNGITdseSLTSVIITVTEDIFAAFPAKAVRETHgfeyVPVMGMQEIPV 80  Listeria innocua
Feature 1           #    ##                  #      #    
1DBF_A        82 TGGLKKCIRVMMTVQTdvp--qdqIRHVYLEKAVVLRPDL 119 Bacillus subtilis
1COM_A        82 TGGLKKCIRVMMTVQTdvp--qdqIRHVYLEKAVVLRPDL 119 Bacillus subtilis
NP_781943     80 ENSLNLCIRILILLNGhn----lnIKYVYLGKAKKLRDDL 115 Clostridium tetani E88
ACA55459      80 EGSMPLCIRILILIDKknknieenIEYVYLGRAKTLRKDL 119 Clostridium botulinum A3 str. Loch Maree
YP_001513104  82 IHSLEKCIRVLIYAYSdka--kkdVAHVYLKEAEKLRPDL 119 Alkaliphilus oremlandii OhILAs
YP_001567321  84 NDSRKKIIRVLIICESs------tQNFVYLHEAKNLRTKK 117 Petrotoga mobilis SJ95
AAD33790      81 PGSLPRCIRVMMTVETdkr--qdeICHVYLKDAAMLRPDL 118 Geobacillus stearothermophilus
YP_175390     81 KGSLPLCIRVMMTVNTslk--qeeIKHVFLEGAIVLRPDL 118 Bacillus clausii KSM-K16
ZP_01861756   82 KDSLNKCIRIMIHWNTekk--qedIRHVYLRKAHTLRPDL 119 Bacillus sp. SG-1
CAC97270      81 PNSLPMCIRFMVFTDLhkp--ltaINHVYLHGAKVLRPDL 118 Listeria innocua

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