2C45,1PQH


Conserved Protein Domain Family
Asp_decarbox

?
cd06919: Asp_decarbox 
Click on image for an interactive view with Cn3D
Aspartate alpha-decarboxylase or L-aspartate 1-decarboxylase, a pyruvoyl group-dependent decarboxylase in beta-alanine production
Decarboxylation of aspartate is the major route of beta-alanine production in bacteria, and is catalyzed by the enzyme L-aspartate decarboxylase (ADC), EC:4.1.1.11 which requires a pyruvoyl group for its activity. The pyruvoyl cofactor is covalently bound to the enzyme. The protein is synthesized as a proenzyme and cleaved via self-processing at Gly23-Ser24 to yield an alpha chain (C-terminal fragment) and beta chain (N-terminal fragment), and the pyruvoyl group. Beta-alanine is required for the biosynthesis of pantothenate, in which the enzyme plays a critical regulatory role. The active site of the tetrameric enzyme is located at the interface of two subunits, with a Lysine and a Histidine from the beta chain of one subunit forming the active site with residues from the alpha chain of the adjacent subunit. This alignment model spans the precursor (or both beta and alpha chains) of aspartate decarboxylase.
Statistics
?
PSSM-Id: 132994
View PSSM: cd06919
Aligned: 58 rows
Threshold Bit Score: 149.194
Threshold Setting Gi: 119872877
Created: 8-Jan-2008
Updated: 17-Jan-2013
Structure
?
Program:
Drawing:
Aligned Rows:
 
active sitetetramerization
Conserved site includes 5 residues -Click on image for an interactive view with Cn3D
Feature 1:active site [active site]
Evidence:
  • Comment:Gly23-Ser24 form the cofactor pyruvoyl by intramolecular non-hydrolytic serinolysis
  • Comment:Structures demonstrating the active configuration with the covalently bound cofactor are not included in this alignment model, as they are proteolytically cleaved and split into two smaller chains, represented by the stretches in this alignment which are N- and C-terminal to Gly23-Ser24
  • Structure:1PQH: A Ser24Thr mutant of aspartate 1-decarboxylase from Escherichia coli binds malonic acid, indicating the location of the substrate in the native active enzyme
    View structure with Cn3D
  • Citation:PMID 9546220

Sequence Alignment
?
Format: Row Display: Color Bits: Type Selection:
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
Feature 1               # #            ##                                #                       
2C45_A         2 LRTMLKSKIHRATVTCADLHYVGSVTIDADLMDAADLLegEQVTIVDIdnGARLVTYAITGErgSGVIGINGAAAHLVHp 81
1PQH_A        19 IRTMLQGKLHRVKVTHADLHYEGTCAIDQDFLDAAGILenEAIDIWNVtnGKRFSTYAIAAErgSRIISVNGAAAHXASv 98
gi 110668287   2 RRWLLKSKLHRARVTGTEKDYEGSISIDAALLSEADIAvgEQVQVVNVtnGERFETYTIEGE--SRQMELNGAAARLAEt 79
gi 118340533   2 QRIMLKSKLHRARVTATEIDYEGSIAIDEDLLDRVGIMplEQVHIFNInsGARFITYVINAErgSGIFSINGAAARLTQi 81
gi 167730032   2 LRQILLAKLHRATVTECDLNYNGSIKIDEELLEKSGMRefERVDVFDItnGNRFSTYIIVGErgSGVIGINGAAARLVQv 81
gi 153891149  14 HRTFLKTKLHRATLTAADPDYEGSISIDRALCRAAGMLeyEQVDVLDInnGARFTTYVIYGE--PGQVQVNGAAARLVRp 91
gi 170079124   3 QIKLMHAKLHHLRVTQAELDYVGSITIDQALIEKVGILplEEVNIWNVenGNRLTTYVLPGErdSGVVCLNGAAAHLCSp 82
gi 13474851    1 MRKLVAGKLHGIHVTEANLNYHGSITLDPDHCEAAGILpmEFVEIWNKnsGARISTYVILGErgSRCCILNGAAARTCQp 80
gi 2498747     3 SIRLMHAKLHRVCVTEANVNYVGSITIDPVMLERVGLLplEEVDIINLsnGNRFSTYVLPGQahSKEICPNGGAALLCQp 82
gi 10954747   26 VEKYVGAKLHGLRVTDAKLNYHGSITIDADFCREVGLKplEYVEIWNKmsGARISTYVLYGDpgSRCCILNGAAARTCQq 105
                         90       100       110
                 ....*....|....*....|....*....|...
Feature 1                                         
2C45_A        82 GDLVILIAYATmdda--rartYQPRIVFVDAYN 112
1PQH_A        99 GDIVIIASFVTmpde--eartWRPNVAYFEGDN 129
gi 110668287  80 GDVIIVISYGLyvk----deqPEPTVLLLDEEN 108
gi 118340533  82 NDRIIVAAYGMintd---qekHNAQVTLLDESN 111
gi 167730032  82 GDKVIVMNYGImdet--eienHKPCIILLNDNN 112
gi 153891149  92 GDLVIVLAYCRldek--evpaHKPRVVLMGPGN 122
gi 170079124  83 GDRLIVAAYELrdrrdvlaqgHTAKVILADEQN 115
gi 13474851   81 DDPIIVCNSIYldea--hitsLKPRIVTFDQDN 111
gi 2498747    83 GDRLIIFAYELcdrrevlqkgHQAKVLVTNESN 115
gi 10954747  106 GDEIIIASSVFcevd--diikLKPRVLVFGEKN 136

| Disclaimer | Privacy statement | Accessibility |
NCBI Home NCBI Search NCBI SiteMap