Conserved Protein Domain Family
GATase1_CPSase

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cd01744: GATase1_CPSase 
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Small chain of the glutamine-dependent form of carbamoyl phosphate synthase, CPSase II
This group of sequences represents the small chain of the glutamine-dependent form of carbamoyl phosphate synthase, CPSase II. CPSase II catalyzes the production of carbomyl phosphate (CP) from bicarbonate, glutamine and two molecules of MgATP. The reaction is believed to proceed by a series of four biochemical reactions involving a minimum of three discrete highly reactive intermediates. The synthesis of CP is critical for the initiation of two separate biosynthetic pathways. In one CP is coupled to aspartate, its carbon and nitrogen nuclei ultimately incorporated into the aromatic moieties of pyrimidine nucleotides. In the second pathway CP is condensed with ornithine at the start of the urea cycle and is utilized for the detoxification of ammonia and biosynthesis of arginine. CPSases may be encoded by one or by several genes, depending on the species. The E.coli enzyme is a heterodimer consisting of two polypeptide chains referred to as the small and large subunit. Ammonia an intermediate during the biosynthesis of carbomyl phosphate produced by the hydrolysis of glutamine in the small subunit of the enzyme is delivered via a molecular tunnel between the remotely located carboxyphosphate active site in the large subunit. CPSase IIs belong to the triad family of amidotransferases having a conserved Cys-His-Glu catalytic triad in the glutaminase active site. This group also contains the sequence from the mammalian urea cycle form which has lost the active site Cys, resulting in an ammonia-dependent form, CPSase I.
Statistics
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PSSM-Id: 153215
View PSSM: cd01744
Aligned: 78 rows
Threshold Bit Score: 204.652
Threshold Setting Gi: 42519110
Created: 27-Aug-2004
Updated: 17-Jan-2013
Structure
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Program:
Drawing:
Aligned Rows:
 
catalytic sitesubunit
Conserved site includes 3 residues -Click on image for an interactive view with Cn3D
Feature 1:catalytic site [active site]
Evidence:
  • Comment:Conserved trio of residues critical for the catalytic hydrolysis of glutamine and the production of ammonia.
  • Citation:PMID 9174345

Sequence Alignment
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Format: Row Display: Color Bits: Type Selection:
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
Feature 1                                                                                     # 
1JDB_C      194 VVAYDFGAKRNILRMLVDRGCRLTIVPaqtsaedvlkmnPDGIFLSNGPGDPapcdyAITAIQKFLETd---IPVFGICL 270
gi 62516049 170 IAIIDLGLKHSMLRELSLRQVNANVLPynatvrdiktlrPDGIIISNGPSQAk---eVLPYLRQILDEylgkLPILGVGL 246
gi 23023550 170 IVVIDFGLKHGILRMLGDYDANVSVLPyttsvdevltldPDGIILSTGPGDPrslpeSVLTLIRVLQTk---APLLGIGL 246
gi 28378457 171 VVVIDFGLKHGILRELSKRACNVTVLPytatteeilnldPDGVILSTGPGKPqdlpvSVTEMIKNIQNr---VPLFAIGL 247
gi 29337201 167 VAILNFGEKAAITAELQARGADVVVLPptaslkavaayhPDGILLSNGPGDPtdyhtYLATIRQLAQR----YPLAGICL 242
gi 42519110 170 VAVIDLGLKHSLLRSLSLREINSVVLPynasiydiinlrADAIVISNGPSGVeevapFLKPVFDKFYGk---LPILGIGL 246
gi 51892341 172 VVAVDFGAKENILRELTARGCDVTVVPatasaeevlslrPEGVVLTNGPGAPtdvpeAVEMVRGLLSQg--dLPIFGICL 249
gi 71541214 174 IVLLDLGTKKGVIDSLVRRDCEVIAVPantgareilrlhPDGILVSDGPGDPgaigyAIDTCRELLGK----VALLGVGL 249
gi 78042709 175 VVLVDYGAKNSILQSLLKRGAEVFVVPplmpaeqilalaPQGVVLSNGPGDPadlqeSIFIIRQLIGK----LPILGICL 250
gi 77406384 173 IVVLDFGLKHSILRELSKRQCDVTVIPyntslegiknlyPEGIILSNGPGNPeklqeILNTIKELQKS----VPMLGIGL 248
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
Feature 1                                                                                       
1JDB_C      271 GHQLLALASGAKTVKMKFGHHGGNHPVkdvekNVVMITAQNHGFAVdeatlpa-nlrvthkSLFDGTLQGIHRTDKPAFS 349
gi 62516049 247 GFLAISAYLDLSLVDLPQYQNGTNFPVirqssGQIWQTAMNIGQLVlpddtav-tfneeyfDLHNELLAGFSNDKLQLLA 325
gi 23023550 247 GHELFALANDATLVALPSEHHGMNHPIqeiisRQIFYAMQGQGYAVdeelldhkklfvtyrDLVDGAVQGLRHRDYPAFS 326
gi 28378457 248 GHELFAMANGAQIMKLSPEHHGANHPIrevitNQIIYAAQGQGFAVdadtvdrnklittfvDLIDGTIQGLRLRDFPAFS 327
gi 29337201 243 GHQLIALAYGAQTYQLSFGHHGLNHPVqacadGRIIMTSQNHDYAVdpasikgtplivthtELNDGSIEGLRLPHQAVMS 322
gi 42519110 247 GFLAISNYLDLELLDLIPAYNGSNFPVieqtnNRIWQTAMNIDQLVvpdslsl-nlsrkyfDLRSELLAGYSIKKDKVLA 325
gi 51892341 250 GHQIAALALGATTYKLPYGHRGANHPVkelatGRIHITSQNHGYAVaaeslpp-evevthvSLHDGTVEGLAHRRLPLFT 328
gi 71541214 250 GHQILALAMGASILRLPYGHRGSNHPVknlenNRVYITTQNHGFSLeesslsgtgievtmrSLNDGSIEGIRHREMPVFS 329
gi 78042709 251 GHQLLALAHGAQTYKLKFGHRGSNHPVietesKRVFITSHNHGFAVreesligtgleiwfrNLNDNTIEGLRSRYSKILS 330
gi 77406384 249 GHQLIAMANGAEIMRLPVAKKGTNYPMrdiatGRLETVSQFNHFTVnrlnlph-dllvtheGLNDQEIVALRHRSFPVMS 327
                       170       180
                ....*....|....*....|..
Feature 1          # #                
1JDB_C      350 FQGHPEAsPGPHDAAPLFDHFI 371
gi 62516049 326 VAFNPEGaPGTEDAQVIFDDFL 347
gi 23023550 327 VQFFPDAaPGPYEATAVFADFF 348
gi 28378457 328 VQFFPDGaPGPTETRDIFDEFV 349
gi 29337201 323 VQFHPEAhPGPQEAGQFFDDFL 344
gi 42519110 326 TAFNPEGsPGNFDAASIYDQFL 347
gi 51892341 329 VQYHPEAcPGPRENRYLFDRFL 350
gi 71541214 330 LQFDPEGyPGYSETGFFYDDFI 351
gi 78042709 331 VQFHPEAaPGPNDADFIFDLFL 352
gi 77406384 328 VQFYPEAaPGPHDVTYFFDEFL 349

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