1B65,1VZ8


Conserved Protein Domain Family
DmpA_OAT
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cd00123: DmpA_OAT 
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DmpA/OAT superfamily; composed of L-aminopeptidase D-amidase/D-esterase (DmpA), ornithine acetyltransferase (OAT) and similar proteins. DmpA is an aminopeptidase that releases N-terminal D and L amino acids from peptide substrates. This group represents one of the rare aminopeptidases that are not metalloenzymes. DmpA shows similarity in catalytic mechanism to N-terminal nucleophile (Ntn) hydrolases, which are enzymes that catalyze the cleavage of amide bonds through the nucleophilic attack of the side chain of an N-terminal serine, threonine, or cysteine. OAT catalyzes the first and fifth steps in arginine biosynthesis, coupling acetylation of glutamate with deacetylation of N-acetylornithine, which allows recycling of the acetyl group in the arginine biosynthetic pathway. The superfamily also contains an enzyme, endo-type 6-aminohexanoate-oligomer hydrolase, that have been shown to be involved in nylon degradation. Proteins in this superfamily undergo autocatalytic cleavage of an inactive precursor at the site immediately upstream to the catalytic nucleophile.
Links
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Statistics
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PSSM-Id: 238070
Aligned: 3 rows
Threshold Bit Score: 230.359
Created: 4-Sep-2001
Updated: 2-Oct-2020
Structure
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Program:
Drawing:
Aligned Rows:
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active sitecleavage site
Conserved site includes 8 residues -Click on image for an interactive view with Cn3D
Feature 1:active site pocket [active site]
Evidence:
  • Structure:1B65; Ochrobactrum anthropi DmpA's active site pocket is formed by residues from two subunits.
  • Structure:1VZ8_AB: Streptomyces clavuligerus OAT's active site pocket is formed by residues from two subunits; a sulfate molecule is in the pocket.
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Sequence Alignment
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Format: Row Display: Color Bits: Type Selection: 
Feature 1                                                                                     
1B65_A     32 VDGVGVGFQTiieneprpgrkrparsGVTAILPhmqsetpvpVYAGVHRfngngemt---gthwiedgGYFLgPVVITnt 108 Ochrobactrum anthropi
1VZ8_A      9 PRGFVVHTAPvglad-------dgrdDFTVLASta------pATVSAVFtrsrfagpsvvlcreavadGQAR-GVVVLar 74  Streptomyces clavu...
BAA01528   55 FPGVSIGAAHyee----------gptGATVIHIpa------gARTAVDArggav---------glsggYDFNhAICLAgg 109 Flavobacterium sp.

Feature 1                                                ###                                  
1B65_A    109 h--------giGMAHHATVRWMVDryastyqtddflwimPVVAETYdgalndingfpvtEADVRKAldnvasgpvqegnc 180 Ochrobactrum anthropi
1VZ8_A     75 nanvatglegeENAREVREAVARAlglp--------egeXLIASTGvigrqy--pxesiREHLKTLewpageggfdr--- 141 Streptomyces clavu...
BAA01528  110 a-------gygLEAGAGVSDALLErlehrtg--faelqlVSSAVIYdfsars-tavypdKALGRAAlefavpgefpqgra 179 Flavobacterium sp.

Feature 1                                              # #                                    
1B65_A    181 ------gggtgmitygfkggTGTASRVVefggrsFTIGALVQANhgqrdwltiagvpvg----------------qhmrd 238 Ochrobactrum anthropi
1VZ8_A    142 ---------aaraixttdtrPKEVRVSVg----gATLVGIAKGVgxle-------------------------------- 176 Streptomyces clavu...
BAA01528  180 gagmsasagkvdwdrteitgQGAAFRRLg----dVRILAVVVPNpvgvivdragtvvrgnydaqtgvrrhpvfdyqeafa 255 Flavobacterium sp.

Feature 1                #                                       ##                           
1B65_A    239 gtpqsqlqerGSIIVVLATDLPLMPHQLKRLAR-RASIGIgrngt-pggnnSGDIFIAFSTanqrpmqhrsapfldvemv 316 Ochrobactrum anthropi
1VZ8_A    177 -------pdxATLLTFFATDARLDPAEQDRLFRrVXDRTFnavsi-dtdtsTSDTAVLFANglag--------------- 233 Streptomyces clavu...
BAA01528  256 eqvppvteagNTTISAIVTNVRMSPVELNQFAK-QVHSSMhrgiqpfhtdmDGDTLFAVTTdeidlpttpg----ssrgr 330 Flavobacterium sp.

Feature 1                             
1B65_A    317 ndepLDTVYLAAVDSVEEAVVNAM 340 Ochrobactrum anthropi
1VZ8_A    234 -evdAGEFEEALHTAALALVKDIA 256 Streptomyces clavuligerus
BAA01528  331 lsvnATALGAIASEVMWDAVLEAG 354 Flavobacterium sp.

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