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Conserved domains on  [gi|446290599|ref|WP_000368454|]
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MULTISPECIES: succinylglutamate desuccinylase [Salmonella]

Protein Classification

succinylglutamate desuccinylase( domain architecture ID 10012321)

succinylglutamate desuccinylase catalyzes the formation of succinate and L-glutamate from N-succinyl-L-glutamate in the fifth and final reaction of the ammonia-producing arginine catabolic pathway, L-arginine degradation II (AST pathway)

EC:  3.5.1.96
Gene Ontology:  GO:0008270|GO:0016788|GO:0009017|GO:0019545

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK05324 PRK05324
succinylglutamate desuccinylase; Provisional
 1-322 0e+00

succinylglutamate desuccinylase; Provisional


:

Pssm-ID: 235408  Cd Length: 329  Bit Score: 539.00  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446290599   1 MDNFLALTLSGTTPRV-TQGKGAGFRWRWLGHGLLELTPDAPVDRALILSAGIHGNETAPVEMLDKLLSALYSGSLTLTW 79
Cdd:PRK05324   4 MDDFLALTLAGHPPAVtEFGLGNGVRWRWLGEGVLELTPAAPSTKALVLSAGIHGNETAPIELLDQLVRDLLAGELPLRA 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446290599  80 RVLVVLGNPQALAAGIRYCHSDMNRMFGGRWQSFAESDETRRARELELSLETFFSSGQARVRWHLDLHTAIRGSHHLRFG 159
Cdd:PRK05324  84 RLLVILGNPPAMRAGKRYLDEDLNRLFGGRHQQFPGSDEARRAAELEQAVEDFFAAGAERVRWHYDLHTAIRGSKHEQFA 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446290599 160 VLPQRDRPWETDFLAWLGAAGLEALVFHQAPGGTFTHFSSEHFGALSCTLELGKALPFRQNDLTQFNVTSQALSALLSGV 239
Cdd:PRK05324 164 VLPQRGRPWSREQLAWLGAAGIEAVLLHNAPGGTFSHFSSEHFGALACTLELGKVLPFGQNDLSRFAATDQALRALISGE 243

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446290599 240 E-TSTSFSPPLRYRVVSQITRHSDKFALYMDAQTLNFTAFAKGTLLAEEGDKRVTVTHDVEYVLFPNPSVACGLRAGLML 318
Cdd:PRK05324 244 ElPERSADPPRLYRVVRQITKHSDDFELHFADDVENFTAFPKGTLLAEDGDERYVVEHDGERIVFPNPNVAIGLRAGLML 323


                 ....
gi 446290599 319 ERLP 322
Cdd:PRK05324 324 VPTT 327
 
Name Accession Description Interval E-value
PRK05324 PRK05324
succinylglutamate desuccinylase; Provisional
 1-322 0e+00

succinylglutamate desuccinylase; Provisional


Pssm-ID: 235408  Cd Length: 329  Bit Score: 539.00  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446290599   1 MDNFLALTLSGTTPRV-TQGKGAGFRWRWLGHGLLELTPDAPVDRALILSAGIHGNETAPVEMLDKLLSALYSGSLTLTW 79
Cdd:PRK05324   4 MDDFLALTLAGHPPAVtEFGLGNGVRWRWLGEGVLELTPAAPSTKALVLSAGIHGNETAPIELLDQLVRDLLAGELPLRA 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446290599  80 RVLVVLGNPQALAAGIRYCHSDMNRMFGGRWQSFAESDETRRARELELSLETFFSSGQARVRWHLDLHTAIRGSHHLRFG 159
Cdd:PRK05324  84 RLLVILGNPPAMRAGKRYLDEDLNRLFGGRHQQFPGSDEARRAAELEQAVEDFFAAGAERVRWHYDLHTAIRGSKHEQFA 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446290599 160 VLPQRDRPWETDFLAWLGAAGLEALVFHQAPGGTFTHFSSEHFGALSCTLELGKALPFRQNDLTQFNVTSQALSALLSGV 239
Cdd:PRK05324 164 VLPQRGRPWSREQLAWLGAAGIEAVLLHNAPGGTFSHFSSEHFGALACTLELGKVLPFGQNDLSRFAATDQALRALISGE 243

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446290599 240 E-TSTSFSPPLRYRVVSQITRHSDKFALYMDAQTLNFTAFAKGTLLAEEGDKRVTVTHDVEYVLFPNPSVACGLRAGLML 318
Cdd:PRK05324 244 ElPERSADPPRLYRVVRQITKHSDDFELHFADDVENFTAFPKGTLLAEDGDERYVVEHDGERIVFPNPNVAIGLRAGLML 323


                 ....
gi 446290599 319 ERLP 322
Cdd:PRK05324 324 VPTT 327
arg_catab_astE TIGR03242
succinylglutamate desuccinylase; Members of this protein family are succinylglutamate ...
 3-319 1.62e-163

succinylglutamate desuccinylase; Members of this protein family are succinylglutamate desuccinylase, the fifth and final enzyme of the arginine succinyltransferase (AST) pathway for arginine catabolism. This model excludes the related protein aspartoacylase. [Energy metabolism, Amino acids and amines]


Pssm-ID: 132286  Cd Length: 319  Bit Score: 457.98  E-value: 1.62e-163
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446290599    3 NFLALTLSGTTPRVTQGKGAGFRWRWLGHGLLELTPDAPVDRALILSAGIHGNETAPVEMLDKLLSALYSGSLTLTWRVL 82
Cdd:TIGR03242   1 DFLALTLTGKKPHVTQGETNNVRWRWLGEGVLELTPHAPPQKSLVISAGIHGNETAPIEILEQLLGDIAAGKLPLRVRLL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446290599   83 VVLGNPQALAAGIRYCHSDMNRMFGGRWQSFAESDETRRARELELSLETFFS-SGQARVRWHLDLHTAIRGSHHLRFGVL 161
Cdd:TIGR03242  81 VILGNPPAMRTGKRYLHDDLNRMFGGRYQQLAPSFETCRAAELEQCVEDFFSqGGRSVARWHYDLHTAIRGSLHEQFALL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446290599  162 PQRDRPWETDFLAWLGAAGLEALVFHQAPGGTFTHFSSEHFGALSCTLELGKALPFRQNDLTQFNVTSQALSALLSGVET 241
Cdd:TIGR03242 161 PYQGRPWDREFLTWLGAAGLDALVFHTEPGGTFSHFSSEHFGALACTLELGKALPFGQNDLSQFAAITSALRALISDEAI 240

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446290599  242 STSFSPPLR-YRVVSQITRHSDKFALYMDAQTLNFTAFAKGTLLAEEGDKRVTVTHDVEYVLFPNPSVACGLRAGLMLE 319
Cdd:TIGR03242 241 PARRTDPLRlFRVVSSITKHSDSFELHVASDTLNFTPFPKGTLLATDGNERYRVTHEGERILFPNPNVANGLRAGLMLV 319
AstE COG2988
Succinylglutamate desuccinylase [Amino acid transport and metabolism];
27-322 2.00e-153

Succinylglutamate desuccinylase [Amino acid transport and metabolism];


Pssm-ID: 442227  Cd Length: 305  Bit Score: 431.96  E-value: 2.00e-153
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446290599  27 RWLGHGLLELTPDAPVDRALILSAGIHGNETAPVEMLDKLLSALYSGSLTLTWRVLVVLGNPQALAAGIRYCHSDMNRMF 106
Cdd:COG2988    8 RWLDEGVLELTPHAPGIKAVVISGGIHGNETAPIELLDKLLQDLLLGERPLSFRLLLILGNPAAMRAGRRYLDEDLNRLF 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446290599 107 GGRWQSFAESDETRRARELELSLETFFSSGQaRVRWHLDLHTAIRGSHHLRFGVLPQRDRPWETDFLAWLGAAGLEALVF 186
Cdd:COG2988   88 GGRHLQNPESYEAARAKELEQAVGPFFAAGG-RVRLHIDLHTAIRNSGHERFAVYPFRGRPFDLALLAYLAAAGPEAVVL 166

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446290599 187 HQAPGGTFTHFSSEHFGALSCTLELGKALPFRQNDLTQFNVTSQALSALLSGVETS-TSFSPPLRYRVVSQITRHSDKFA 265
Cdd:COG2988  167 HHAPGGTFSHFSAELCGAQAFTLELGKVRPFGQNDLSRFAATEEALRALLSGAELPeHPAQDLDLYRVVQQIIKHGDDFM 246

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 446290599 266 LYMDAQTLNFTAFAKGTLLAEEGDKRVTVTHDVEYVLFPNPSVACGLRAGLMLERLP 322
Cdd:COG2988  247 LHPDLDTLNFTPLPPGTLLAEDGGKEYRVEGDEERIVFPNEAVYYGQRAALLLTPKE 303
M14_ASTE cd03855
Peptidase M14 Succinylglutamate desuccinylase (ASTE) subfamily; Peptidase M14 ...
 3-238 9.76e-125

Peptidase M14 Succinylglutamate desuccinylase (ASTE) subfamily; Peptidase M14 Succinylglutamate desuccinylase (ASTE, also known as N-succinyl-L-glutamate amidohydrolase, N2-succinylglutamate desuccinylase, and SGDS; EC 3.5.1.96) belongs to the Succinylglutamate desuccinylase (ASTE)/aspartoacylase (ASPA) subfamily of the M14 family of metallocarboxypeptidases. This group includes succinylglutamate desuccinylase that catalyzes the fifth and last step in arginine catabolism by the arginine succinyltransferase pathway. It hydrolyzes N-succinyl-L-glutamate to succinate and L-glutamate.


Pssm-ID: 349428  Cd Length: 239  Bit Score: 356.90  E-value: 9.76e-125
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446290599   3 NFLALTLSGTTPRVTQG--KGAGFRWRWLGHGLLELTPDAPVDRALILSAGIHGNETAPVEMLDKLLSALYSGSLTLTWR 80
Cdd:cd03855    1 DFLALTLSGSEPAEGELaaVSNGTRVRWLATGVLELTPAASASKSVVLSAGIHGNETAPIEILDQLINDLIRGELALAHR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446290599  81 VLVVLGNPQALAAGIRYCHSDMNRMFGGRWQSFAESDETRRARELELSLETFFSSGQARVRWHLDLHTAIRGSHHLRFGV 160
Cdd:cd03855   81 LLFIFGNPPAIRQGKRFIEENLNRLFSGRHSKLPPSYETARAAELEQAVADFFAKASGEVRWHLDLHTAIRGSKHEQFAV 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446290599 161 LPQRD-RPWETDFLAWLGAAGLEALVFHQAPGGTFTHFSSEHFGALSCTLELGKALPFRQNDLTQFNVTSQALSALLSG 238
Cdd:cd03855  161 YPFLEgRPHDREQLDFLGAAGIEAVLLSNSPGGTFSYYSSEHFGAAAFTVELGKVRPFGQNDLSQFAAIDQALRALISG 239
AstE_AspA pfam04952
Succinylglutamate desuccinylase / Aspartoacylase family; This family includes ...
 44-318 1.77e-93

Succinylglutamate desuccinylase / Aspartoacylase family; This family includes Succinylglutamate desuccinylase EC:3.1.-.- that catalyzes the fifth and last step in arginine catabolism by the arginine succinyltransferase pathway. The family also include aspartoacylase EC:3.5.1.15 which cleaves acylaspartate into a fatty acid and aspartate. Mutations in Swiss:P45381 lead to Canavan disease. This family is probably structurally related to pfam00246 (Bateman A pers. obs.).


Pssm-ID: 428216 [Multi-domain]  Cd Length: 289  Bit Score: 279.23  E-value: 1.77e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446290599   44 RALILSAGIHGNETAPVEMLDKLLSALYSGSLtLTWRVLVVLGNPQALAAGIRYCHSDMNRMFGGRWQSfAESDETRRAR 123
Cdd:pfam04952   3 PTLLLSAGIHGNETNGVELLRRLLRQLDPGDI-AGERTLVPLANPPAFRAGSRYIPRDLNRSFPGRALG-ASSDEPYRAT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446290599  124 ELELSLETFFSSGQARVRWHLDLHTAIRGSHHLRFGVLPQRDRPWetDFLAWLGAAGLEALV-FHQAPGGTFTHFSSEHF 202
Cdd:pfam04952  81 RAERLADLFFPALLPRADIVLDLHTGTRGMGHLLFALAPIRDDPL--HLLALLRAFGAPAVLkLHSKPSAGFSAFSAEEL 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446290599  203 GALSCTLELGKALPFRQNDLTQFNVTSQALSALLSGVETST-SFSPPLRYRVVSQITRHSD---------KFALYMDAQT 272
Cdd:pfam04952 159 GAPGFTLELGGAGPFGANLISRTAAGVLNVLRLIGVLNGGPdAFEPPKLYRVLREIDRPRDiraelaglvEFALNLGDDV 238

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 446290599  273 LNFTAFAKGTLLAEE-GDKRVTVTHDVEYVLFPNPSVACGLRAGLML 318
Cdd:pfam04952 239 DAGPLLPGGPLFAPFgGEETEYRAPEDGYPVFPNEAAYVGKGAALAL 285
 
Name Accession Description Interval E-value
PRK05324 PRK05324
succinylglutamate desuccinylase; Provisional
 1-322 0e+00

succinylglutamate desuccinylase; Provisional


Pssm-ID: 235408  Cd Length: 329  Bit Score: 539.00  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446290599   1 MDNFLALTLSGTTPRV-TQGKGAGFRWRWLGHGLLELTPDAPVDRALILSAGIHGNETAPVEMLDKLLSALYSGSLTLTW 79
Cdd:PRK05324   4 MDDFLALTLAGHPPAVtEFGLGNGVRWRWLGEGVLELTPAAPSTKALVLSAGIHGNETAPIELLDQLVRDLLAGELPLRA 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446290599  80 RVLVVLGNPQALAAGIRYCHSDMNRMFGGRWQSFAESDETRRARELELSLETFFSSGQARVRWHLDLHTAIRGSHHLRFG 159
Cdd:PRK05324  84 RLLVILGNPPAMRAGKRYLDEDLNRLFGGRHQQFPGSDEARRAAELEQAVEDFFAAGAERVRWHYDLHTAIRGSKHEQFA 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446290599 160 VLPQRDRPWETDFLAWLGAAGLEALVFHQAPGGTFTHFSSEHFGALSCTLELGKALPFRQNDLTQFNVTSQALSALLSGV 239
Cdd:PRK05324 164 VLPQRGRPWSREQLAWLGAAGIEAVLLHNAPGGTFSHFSSEHFGALACTLELGKVLPFGQNDLSRFAATDQALRALISGE 243

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446290599 240 E-TSTSFSPPLRYRVVSQITRHSDKFALYMDAQTLNFTAFAKGTLLAEEGDKRVTVTHDVEYVLFPNPSVACGLRAGLML 318
Cdd:PRK05324 244 ElPERSADPPRLYRVVRQITKHSDDFELHFADDVENFTAFPKGTLLAEDGDERYVVEHDGERIVFPNPNVAIGLRAGLML 323


                 ....
gi 446290599 319 ERLP 322
Cdd:PRK05324 324 VPTT 327
arg_catab_astE TIGR03242
succinylglutamate desuccinylase; Members of this protein family are succinylglutamate ...
 3-319 1.62e-163

succinylglutamate desuccinylase; Members of this protein family are succinylglutamate desuccinylase, the fifth and final enzyme of the arginine succinyltransferase (AST) pathway for arginine catabolism. This model excludes the related protein aspartoacylase. [Energy metabolism, Amino acids and amines]


Pssm-ID: 132286  Cd Length: 319  Bit Score: 457.98  E-value: 1.62e-163
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446290599    3 NFLALTLSGTTPRVTQGKGAGFRWRWLGHGLLELTPDAPVDRALILSAGIHGNETAPVEMLDKLLSALYSGSLTLTWRVL 82
Cdd:TIGR03242   1 DFLALTLTGKKPHVTQGETNNVRWRWLGEGVLELTPHAPPQKSLVISAGIHGNETAPIEILEQLLGDIAAGKLPLRVRLL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446290599   83 VVLGNPQALAAGIRYCHSDMNRMFGGRWQSFAESDETRRARELELSLETFFS-SGQARVRWHLDLHTAIRGSHHLRFGVL 161
Cdd:TIGR03242  81 VILGNPPAMRTGKRYLHDDLNRMFGGRYQQLAPSFETCRAAELEQCVEDFFSqGGRSVARWHYDLHTAIRGSLHEQFALL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446290599  162 PQRDRPWETDFLAWLGAAGLEALVFHQAPGGTFTHFSSEHFGALSCTLELGKALPFRQNDLTQFNVTSQALSALLSGVET 241
Cdd:TIGR03242 161 PYQGRPWDREFLTWLGAAGLDALVFHTEPGGTFSHFSSEHFGALACTLELGKALPFGQNDLSQFAAITSALRALISDEAI 240

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446290599  242 STSFSPPLR-YRVVSQITRHSDKFALYMDAQTLNFTAFAKGTLLAEEGDKRVTVTHDVEYVLFPNPSVACGLRAGLMLE 319
Cdd:TIGR03242 241 PARRTDPLRlFRVVSSITKHSDSFELHVASDTLNFTPFPKGTLLATDGNERYRVTHEGERILFPNPNVANGLRAGLMLV 319
AstE COG2988
Succinylglutamate desuccinylase [Amino acid transport and metabolism];
27-322 2.00e-153

Succinylglutamate desuccinylase [Amino acid transport and metabolism];


Pssm-ID: 442227  Cd Length: 305  Bit Score: 431.96  E-value: 2.00e-153
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446290599  27 RWLGHGLLELTPDAPVDRALILSAGIHGNETAPVEMLDKLLSALYSGSLTLTWRVLVVLGNPQALAAGIRYCHSDMNRMF 106
Cdd:COG2988    8 RWLDEGVLELTPHAPGIKAVVISGGIHGNETAPIELLDKLLQDLLLGERPLSFRLLLILGNPAAMRAGRRYLDEDLNRLF 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446290599 107 GGRWQSFAESDETRRARELELSLETFFSSGQaRVRWHLDLHTAIRGSHHLRFGVLPQRDRPWETDFLAWLGAAGLEALVF 186
Cdd:COG2988   88 GGRHLQNPESYEAARAKELEQAVGPFFAAGG-RVRLHIDLHTAIRNSGHERFAVYPFRGRPFDLALLAYLAAAGPEAVVL 166

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446290599 187 HQAPGGTFTHFSSEHFGALSCTLELGKALPFRQNDLTQFNVTSQALSALLSGVETS-TSFSPPLRYRVVSQITRHSDKFA 265
Cdd:COG2988  167 HHAPGGTFSHFSAELCGAQAFTLELGKVRPFGQNDLSRFAATEEALRALLSGAELPeHPAQDLDLYRVVQQIIKHGDDFM 246

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 446290599 266 LYMDAQTLNFTAFAKGTLLAEEGDKRVTVTHDVEYVLFPNPSVACGLRAGLMLERLP 322
Cdd:COG2988  247 LHPDLDTLNFTPLPPGTLLAEDGGKEYRVEGDEERIVFPNEAVYYGQRAALLLTPKE 303
M14_ASTE cd03855
Peptidase M14 Succinylglutamate desuccinylase (ASTE) subfamily; Peptidase M14 ...
 3-238 9.76e-125

Peptidase M14 Succinylglutamate desuccinylase (ASTE) subfamily; Peptidase M14 Succinylglutamate desuccinylase (ASTE, also known as N-succinyl-L-glutamate amidohydrolase, N2-succinylglutamate desuccinylase, and SGDS; EC 3.5.1.96) belongs to the Succinylglutamate desuccinylase (ASTE)/aspartoacylase (ASPA) subfamily of the M14 family of metallocarboxypeptidases. This group includes succinylglutamate desuccinylase that catalyzes the fifth and last step in arginine catabolism by the arginine succinyltransferase pathway. It hydrolyzes N-succinyl-L-glutamate to succinate and L-glutamate.


Pssm-ID: 349428  Cd Length: 239  Bit Score: 356.90  E-value: 9.76e-125
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446290599   3 NFLALTLSGTTPRVTQG--KGAGFRWRWLGHGLLELTPDAPVDRALILSAGIHGNETAPVEMLDKLLSALYSGSLTLTWR 80
Cdd:cd03855    1 DFLALTLSGSEPAEGELaaVSNGTRVRWLATGVLELTPAASASKSVVLSAGIHGNETAPIEILDQLINDLIRGELALAHR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446290599  81 VLVVLGNPQALAAGIRYCHSDMNRMFGGRWQSFAESDETRRARELELSLETFFSSGQARVRWHLDLHTAIRGSHHLRFGV 160
Cdd:cd03855   81 LLFIFGNPPAIRQGKRFIEENLNRLFSGRHSKLPPSYETARAAELEQAVADFFAKASGEVRWHLDLHTAIRGSKHEQFAV 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446290599 161 LPQRD-RPWETDFLAWLGAAGLEALVFHQAPGGTFTHFSSEHFGALSCTLELGKALPFRQNDLTQFNVTSQALSALLSG 238
Cdd:cd03855  161 YPFLEgRPHDREQLDFLGAAGIEAVLLSNSPGGTFSYYSSEHFGAAAFTVELGKVRPFGQNDLSQFAAIDQALRALISG 239
AstE_AspA pfam04952
Succinylglutamate desuccinylase / Aspartoacylase family; This family includes ...
 44-318 1.77e-93

Succinylglutamate desuccinylase / Aspartoacylase family; This family includes Succinylglutamate desuccinylase EC:3.1.-.- that catalyzes the fifth and last step in arginine catabolism by the arginine succinyltransferase pathway. The family also include aspartoacylase EC:3.5.1.15 which cleaves acylaspartate into a fatty acid and aspartate. Mutations in Swiss:P45381 lead to Canavan disease. This family is probably structurally related to pfam00246 (Bateman A pers. obs.).


Pssm-ID: 428216 [Multi-domain]  Cd Length: 289  Bit Score: 279.23  E-value: 1.77e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446290599   44 RALILSAGIHGNETAPVEMLDKLLSALYSGSLtLTWRVLVVLGNPQALAAGIRYCHSDMNRMFGGRWQSfAESDETRRAR 123
Cdd:pfam04952   3 PTLLLSAGIHGNETNGVELLRRLLRQLDPGDI-AGERTLVPLANPPAFRAGSRYIPRDLNRSFPGRALG-ASSDEPYRAT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446290599  124 ELELSLETFFSSGQARVRWHLDLHTAIRGSHHLRFGVLPQRDRPWetDFLAWLGAAGLEALV-FHQAPGGTFTHFSSEHF 202
Cdd:pfam04952  81 RAERLADLFFPALLPRADIVLDLHTGTRGMGHLLFALAPIRDDPL--HLLALLRAFGAPAVLkLHSKPSAGFSAFSAEEL 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446290599  203 GALSCTLELGKALPFRQNDLTQFNVTSQALSALLSGVETST-SFSPPLRYRVVSQITRHSD---------KFALYMDAQT 272
Cdd:pfam04952 159 GAPGFTLELGGAGPFGANLISRTAAGVLNVLRLIGVLNGGPdAFEPPKLYRVLREIDRPRDiraelaglvEFALNLGDDV 238

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 446290599  273 LNFTAFAKGTLLAEE-GDKRVTVTHDVEYVLFPNPSVACGLRAGLML 318
Cdd:pfam04952 239 DAGPLLPGGPLFAPFgGEETEYRAPEDGYPVFPNEAAYVGKGAALAL 285
PRK02259 PRK02259
aspartoacylase; Provisional
 48-148 1.25e-14

aspartoacylase; Provisional


Pssm-ID: 235019  Cd Length: 288  Bit Score: 72.99  E-value: 1.25e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446290599  48 LSAGIHGNETAPVEMLDKL---LSALYSGSLTltwrVLVVLGNPQALAAGIRYCHSDMNRMFGGrwQSFAESD----ETR 120
Cdd:PRK02259   7 IVGGTHGNEITGIYLVKKWqqqPNLINRKGLE----VQTVIGNPEAIEAGRRYIDRDLNRSFRL--DLLQNPDlsgyEQL 80

                         90       100
                 ....*....|....*....|....*...
gi 446290599 121 RARELelsLETFFSSGQARVRWHLDLHT 148
Cdd:PRK02259  81 RAKEL---VQQLGPKGNSPCDFIIDLHS 105
M14_ASTE_ASPA_like cd06230
Peptidase M14 Succinylglutamate desuccinylase (ASTE)/aspartoacylase (ASPA) subfamily; The ...
 46-225 8.24e-13

Peptidase M14 Succinylglutamate desuccinylase (ASTE)/aspartoacylase (ASPA) subfamily; The Peptidase M14 Succinylglutamate desuccinylase (ASTE)/aspartoacylase (ASPA) subfamily belongs to the M14 family of metallocarboxypeptidases (MCPs), and includes ASTE, which catalyzes the fifth and last step in arginine catabolism by the arginine succinyltransferase pathway, and aspartoacylase (ASPA, also known as aminoacylase 2, and ACY-2; EC:3.5.1.15) which cleaves N-acetyl L-aspartic acid (NAA) into aspartate and acetate. NAA is abundant in the brain, and hydrolysis of NAA by ASPA may help maintain white matter. ASPA is an NAA scavenger in other tissues. Mutations in the gene encoding ASPA cause Canavan disease (CD), a fatal progressive neurodegenerative disorder involving dysmyelination and spongiform degeneration of white matter in children. This enzyme binds zinc which is necessary for activity. Measurement of elevated NAA levels in urine is used in the diagnosis of CD.


Pssm-ID: 349449 [Multi-domain]  Cd Length: 177  Bit Score: 65.80  E-value: 8.24e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446290599  46 LILSAGIHGNETAPVEMLDKLLSALYSGSLTLTWRVLVVLgNPQALAAGIRY---CHSDMNRMFGGRWQSFAESdetRRA 122
Cdd:cd06230    1 LLILAGVHGDEYEGVEAIRRLLAELDPSELKGTVVLVPVA-NPPAFEAGTRYtplDGLDLNRIFPGDPDGSPTE---RLA 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446290599 123 RELElslETFFSsgQARVrwHLDLHTAIRGSHHLRFgVLPQRDRPWET--DFLAWLGAAGLeaLVFHQAPGGTFTHFSSE 200
Cdd:cd06230   77 HELT---ELILK--HADA--LIDLHSGGTGRLVPYA-ILDYDSDAREKsrELARAFGGTPV--IWGGDPPGGTPVAAARS 146

                        170       180
                 ....*....|....*....|....*
gi 446290599 201 HfGALSCTLELGKALPFRQNDLTQF 225
Cdd:cd06230  147 A-GIPAITVELGGGGRLRAERLERY 170
M14_ASPA cd06909
Peptidase M14 Aspartoacylase (ASPA) subfamily; Aspartoacylase (ASPA) belongs to the ...
 48-148 1.89e-12

Peptidase M14 Aspartoacylase (ASPA) subfamily; Aspartoacylase (ASPA) belongs to the Succinylglutamate desuccinylase/aspartoacylase subfamily of the M14 family of metallocarboxypeptidases. ASPA (also known as aminoacylase 2; EC:3.5.1.15) cleaves N-acetyl L-aspartic acid (NAA) into aspartate and acetate. NAA is abundant in the brain, and hydrolysis of NAA by ASPA may help maintain white matter. ASPA is an NAA scavenger in other tissues. Mutations in the gene encoding ASPA cause Canavan disease (CD), a fatal progressive neurodegenerative disorder involving dysmyelination and spongiform degeneration of white matter in children. This enzyme binds zinc which is necessary for activity. Measurement of elevated NAA levels in urine is used in the diagnosis of CD.


Pssm-ID: 349480  Cd Length: 190  Bit Score: 64.92  E-value: 1.89e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446290599  48 LSAGIHGNETAPVEMLDKLL---SALYSGSLTltwrVLVVLGNPQALAAGIRYCHSDMNRMFGGRWQSFAESD---ETRR 121
Cdd:cd06909    5 IVGGTHGNELTGVYLVKHWLknpELIERKSFE----VHPLLANPRAVEQCRRYIDTDLNRCFSLENLSSAPSSlpyEVRR 80

                         90       100
                 ....*....|....*....|....*..
gi 446290599 122 ARELElslETFFSSGQARVRWHLDLHT 148
Cdd:cd06909   81 AREIN---QILGPKGNPACDFIIDLHN 104
COG3608 COG3608
Predicted deacylase [General function prediction only];
46-311 5.03e-12

Predicted deacylase [General function prediction only];


Pssm-ID: 442826 [Multi-domain]  Cd Length: 296  Bit Score: 65.25  E-value: 5.03e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446290599  46 LILSAGIHGNETAPVEMLDKLLSALYSGSL--TLtwrVLVVLGNPQALAAGIRYCHSD---MNRMFGGRwqsfAESDET- 119
Cdd:COG3608   29 LLITAGIHGDELNGIEALRRLLRELDPGELrgTV---ILVPVANPPGFLQGSRYLPIDgrdLNRSFPGD----ADGSLAe 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446290599 120 RRARelelsleTFFSSGQARVRWHLDLHTAIRGSHHLRFGVLPQRDRpwetDFLAWLGAAGLEALVFHQA-PGGTFTHfS 198
Cdd:COG3608  102 RIAH-------ALFEEILPDADYVIDLHSGGIARDNLPHVRAGPGDE----ELRALARAFGAPVILDSPEgGDGSLRE-A 169

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446290599 199 SEHFGALSCTLELGKALPFRQNDLTQ-----FNVtsqaLSAL--LSGVETSTSFSPPLRYRVVSQITRHSDKFaLYMDAQ 271
Cdd:COG3608  170 AAEAGIPALTLELGGGGRFDEESIEAgvrgiLNV----LRHLgmLDGEAPPPPLAPPVLARGSEWVRAPAGGL-FEPLVE 244

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 446290599 272 tlNFTAFAKGTLLAE----EGDKRVTVTHDVE---YVLFPNPSVACG 311
Cdd:COG3608  245 --LGDRVKKGDVLGRitdpFGEEVEEVRAPVDgivIGRRTNPLVNPG 289
M14_ASTE_ASPA_like cd18430
Succinylglutamate desuccinylase/aspartoacylase; uncharacterized; A functionally ...
 46-148 3.33e-10

Succinylglutamate desuccinylase/aspartoacylase; uncharacterized; A functionally uncharacterized subgroup of the Succinylglutamate desuccinylase (ASTE)/aspartoacylase (ASPA) subfamily which is part of the M14 family of metallocarboxypeptidases. ASTE catalyzes the fifth and last step in arginine catabolism by the arginine succinyltransferase pathway, and aspartoacylase (ASPA, also known as aminoacylase 2, and ACY-2; EC:3.5.1.15) cleaves N-acetyl L-aspartic acid (NAA) into aspartate and acetate. NAA is abundant in the brain, and hydrolysis of NAA by ASPA may help maintain white matter. ASPA is an NAA scavenger in other tissues. Mutations in the gene encoding ASPA cause Canavan disease (CD), a fatal progressive neurodegenerative disorder involving dysmyelination and spongiform degeneration of white matter in children. This enzyme binds zinc which is necessary for activity. Measurement of elevated NAA levels in urine is used in the diagnosis of CD.


Pssm-ID: 349486 [Multi-domain]  Cd Length: 168  Bit Score: 58.23  E-value: 3.33e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446290599  46 LILSAGIHGNETAPVEMLDKLLSALYSGSLTlTWRVLVVLGNPQALAAGIRYCHSDMNRMFGGrwQSFAESDETRRAREL 125
Cdd:cd18430    1 LAVLGAVHGNETCGTRAVERLLAELPSGALQ-KGPVTLVPANERAYAEGVRFCEEDLNRVFPG--DPDPDTYERRLANRL 77

                         90       100
                 ....*....|....*....|...
gi 446290599 126 ELSLEtffssgqaRVRWHLDLHT 148
Cdd:cd18430   78 CPELE--------GHDVVLDLHS 92
Peptidase_M14_like cd00596
M14 family of metallocarboxypeptidases and related proteins; The M14 family of ...
 46-224 6.06e-06

M14 family of metallocarboxypeptidases and related proteins; The M14 family of metallocarboxypeptidases (MCPs), also known as funnelins, are zinc-binding carboxypeptidases (CPs) which hydrolyze single, C-terminal amino acids from polypeptide chains, and have a recognition site for the free C-terminal carboxyl group, which is a key determinant of specificity. Two major subfamilies of the M14 family, defined based on sequence and structural homology, are the A/B and N/E subfamilies. Enzymes belonging to the A/B subfamily are normally synthesized as inactive precursors containing preceding signal peptide, followed by an N-terminal pro-region linked to the enzyme; these proenzymes are called procarboxypeptidases. The A/B enzymes can be further divided based on their substrate specificity; Carboxypeptidase A-like (CPA-like) enzymes favor hydrophobic residues while carboxypeptidase B-like (CPB-like) enzymes only cleave the basic residues lysine or arginine. The A forms have slightly different specificities, with Carboxypeptidase A1 (CPA1) preferring aliphatic and small aromatic residues, and CPA2 preferring the bulky aromatic side chains. Enzymes belonging to the N/E subfamily enzymes are not produced as inactive precursors and instead rely on their substrate specificity and subcellular compartmentalization to prevent inappropriate cleavage. They contain an extra C-terminal transthyretin-like domain, thought to be involved in folding or formation of oligomers. MCPs can also be classified based on their involvement in specific physiological processes; the pancreatic MCPs participate only in alimentary digestion and include carboxypeptidase A and B (A/B subfamily), while others, namely regulatory MCPs or the N/E subfamily, are involved in more selective reactions, mainly in non-digestive tissues and fluids, acting on blood coagulation/fibrinolysis, inflammation and local anaphylaxis, pro-hormone and neuropeptide processing, cellular response and others. Another MCP subfamily, is that of succinylglutamate desuccinylase /aspartoacylase, which hydrolyzes N-acetyl-L-aspartate (NAA), and deficiency in which is the established cause of Canavan disease. Another subfamily (referred to as subfamily C) includes an exceptional type of activity in the MCP family, that of dipeptidyl-peptidase activity of gamma-glutamyl-(L)-meso-diaminopimelate peptidase I which is involved in bacterial cell wall metabolism.


Pssm-ID: 349427 [Multi-domain]  Cd Length: 216  Bit Score: 46.30  E-value: 6.06e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446290599  46 LILSAGIHGNETAPVEMLDKLLSALYSGSLTLTWR--------VLVVLGNPQALAAGIRYCHS------DMNRMFGGRWQ 111
Cdd:cd00596    1 ILITGGIHGNEVIGVELALALIEYLLENYGNDPLKrlldnvelWIVPLVNPDGFARVIDSGGRknangvDLNRNFPYNWG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446290599 112 ---SFAESDETRRARELELSLET-----FFSsgQARVRWHLDLHTAI-------RGSHHlrfgvlPQRDRPWETDFLAWL 176
Cdd:cd00596   81 kdgTSGPSSPTYRGPAPFSEPETqalrdLAK--SHRFDLAVSYHSSSeailypyGYTNE------PPPDFSEFQELAAGL 152

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 446290599 177 GAA-GLEALVFHQAP-----GGTFTHFSSEHFGALSCTLELGKALPFRQNDLTQ 224
Cdd:cd00596  153 ARAlGAGEYGYGYSYtwystTGTADDWLYGELGILAFTVELGTADYPLPGTLLD 206
M14_MpaA-like cd06904
Peptidase M14-like domain of Escherichia coli Murein Peptide Amidase A and related proteins; ...
 33-106 1.55e-05

Peptidase M14-like domain of Escherichia coli Murein Peptide Amidase A and related proteins; Peptidase M14-like domain of Escherichia coli Murein Peptide Amidase A (MpaA) and related proteins. MpaA is a member of the M14 family of metallocarboxypeptidases (MCPs), however it has an exceptional type of activity, it hydrolyzes the gamma-D-glutamyl-meso-diaminopimelic acid (gamma-D-Glu-Dap) bond in murein peptides. MpaA is specific for cleavage of the gamma-D-Glu-Dap bond of free murein tripeptide; it may also cleave murein tetrapeptide. MpaA has a different substrate specificity and cellular role than endopeptidase I, ENP1 (ENP1 does not belong to this group). MpaA works on free murein peptide in the recycling pathway.


Pssm-ID: 349475 [Multi-domain]  Cd Length: 214  Bit Score: 45.34  E-value: 1.55e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446290599  33 LLELTPDAPVDRALILsAGIHGNETAPVEMLDKLLSALY--SGSLTLTWRVLVVLgNPQALAAGIRY--CHSDMNRMF 106
Cdd:cd06904   14 LAYKFGPGSRARILII-GGIHGDEPEGVSLVEHLLRWLKnhPASGDFHIVVVPCL-NPDGLAAGTRTnaNGVDLNRNF 89
M14_ASTE_ASPA-like cd06910
Peptidase M14 Succinylglutamate desuccinylase (ASTE)/aspartoacylase (ASPA)-like; ...
 46-148 4.80e-05

Peptidase M14 Succinylglutamate desuccinylase (ASTE)/aspartoacylase (ASPA)-like; uncharacterized subgroup; A functionally uncharacterized subgroup of the Succinylglutamate desuccinylase (ASTE)/aspartoacylase (ASPA) subfamily which is part of the M14 family of metallocarboxypeptidases. ASTE catalyzes the fifth and last step in arginine catabolism by the arginine succinyltransferase pathway, and aspartoacylase (ASPA, also known as aminoacylase 2, and ACY-2; EC:3.5.1.15) cleaves N-acetyl L-aspartic acid (NAA) into aspartate and acetate. NAA is abundant in the brain, and hydrolysis of NAA by ASPA may help maintain white matter. ASPA is an NAA scavenger in other tissues. Mutations in the gene encoding ASPA cause Canavan disease (CD), a fatal progressive neurodegenerative disorder involving dysmyelination and spongiform degeneration of white matter in children. This enzyme binds zinc which is necessary for activity. Measurement of elevated NAA levels in urine is used in the diagnosis of CD.


Pssm-ID: 349481  Cd Length: 208  Bit Score: 43.49  E-value: 4.80e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446290599  46 LILSAGIHGNETAPVEMLDKLLSALYS---GSLTLTWrvlvvlGNPQALAA-------GIRYCHSDMNRMFGGRW-QSFA 114
Cdd:cd06910   27 VMINALTHGNEICGAIALDWLLKNGVRplrGRLTFCF------ANVEAYERfdparptASRFVDEDLNRVWGPELlDGPE 100

                         90       100       110
                 ....*....|....*....|....*....|....
gi 446290599 115 ESDETRRARELELSLETffssgqarVRWHLDLHT 148
Cdd:cd06910  101 QSIELRRARELRPVVDT--------VDYLLDIHS 126
M14_ASTE_ASPA-like cd06253
Peptidase M14 Succinylglutamate desuccinylase (ASTE)/aspartoacylase (ASPA)-like; ...
 35-163 9.70e-05

Peptidase M14 Succinylglutamate desuccinylase (ASTE)/aspartoacylase (ASPA)-like; uncharacterized subgroup; A functionally uncharacterized subgroup of the Succinylglutamate desuccinylase (ASTE)/aspartoacylase (ASPA) subfamily which is part of the M14 family of metallocarboxypeptidases. ASTE catalyzes the fifth and last step in arginine catabolism by the arginine succinyltransferase pathway, and aspartoacylase (ASPA, also known as aminoacylase 2, and ACY-2; EC:3.5.1.15) cleaves N-acetyl L-aspartic acid (NAA) into aspartate and acetate. NAA is abundant in the brain, and hydrolysis of NAA by ASPA may help maintain white matter. ASPA is an NAA scavenger in other tissues. Mutations in the gene encoding ASPA cause Canavan disease (CD), a fatal progressive neurodegenerative disorder involving dysmyelination and spongiform degeneration of white matter in children. This enzyme binds zinc which is necessary for activity. Measurement of elevated NAA levels in urine is used in the diagnosis of CD.


Pssm-ID: 349471  Cd Length: 211  Bit Score: 42.59  E-value: 9.70e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446290599  35 ELTPDAPVDRALILsAGIHGNETAPV---EMLDKLLSALYSGSLTLTWRVLVV-LGNPQALAAGIRYCH---SDMNRMFG 107
Cdd:cd06253   15 RFGGGNAEPRIAIV-AGIHGDELNGLyvcSRLIRFLKELEEGGYKLKGKVLVIpAVNPLGINSGTRFWPfdnLDMNRMFP 93

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 446290599 108 GrwqsFAESDETRR-ARELELSLETFfssgqarvRWHLDLHTAIRgshHLRFgvLPQ 163
Cdd:cd06253   94 G----YNKGETTERiAAALFEDLKGA--------DYGIDLHSSND---FLRE--IPQ 133
M14_REP34-like cd06231
Peptidase M14-like domain similar to rapid encystment phenotype 34 (REP34); This family ...
 38-147 1.07e-04

Peptidase M14-like domain similar to rapid encystment phenotype 34 (REP34); This family includes Francisella tularensis protein rapid encystment phenotype 34 (REP34) which is a zinc-containing monomeric protein demonstrating carboxypeptidase B-like activity. REP34 possesses a novel topology with its substrate binding pocket deviating from the canonical M14 peptidases with a possible catalytic role for a conserved tyrosine and distinct S1' recognition site. Thus, REP34, identified as an active carboxypeptidase and a potential key F. tularensis effector protein, may help elucidate a mechanistic understanding of F. tularensis infection of phagocytic cells. A functionally uncharacterized subgroup of the M14 family of metallocarboxypeptidases (MCPs). The M14 family are zinc-binding carboxypeptidases (CPs) which hydrolyze single, C-terminal amino acids from polypeptide chains, and have a recognition site for the free C-terminal carboxyl group, which is a key determinant of specificity. Two major subfamilies of the M14 family, defined based on sequence and structural homology, are the A/B and N/E subfamilies. Enzymes belonging to the A/B subfamily are normally synthesized as inactive precursors containing preceding signal peptide, followed by an N-terminal pro-region linked to the enzyme; these proenzymes are called procarboxypeptidases. The A/B enzymes can be further divided based on their substrate specificity; Carboxypeptidase A-like (CPA-like) enzymes favor hydrophobic residues while carboxypeptidase B-like (CPB-like) enzymes only cleave the basic residues lysine or arginine. The A forms have slightly different specificities, with Carboxypeptidase A1 (CPA1) preferring aliphatic and small aromatic residues, and CPA2 preferring the bulky aromatic side chains. Enzymes belonging to the N/E subfamily enzymes are not produced as inactive precursors and instead rely on their substrate specificity and subcellular compartmentalization to prevent inappropriate cleavages. They contain an extra C-terminal transthyretin-like domain, thought to be involved in folding or formation of oligomers. MCPs can also be classified based on their involvement in specific physiological processes; the pancreatic MCPs participate only in alimentary digestion and include carboxypeptidase A and B (A/B subfamily), while others, namely regulatory MCPs or the N/E subfamily, are involved in more selective reactions, mainly in non-digestive tissues and fluids, acting on blood coagulation/fibrinolysis, inflammation and local anaphylaxis, pro-hormone and neuropeptide processing, cellular response and others. Another MCP subfamily, is that of succinylglutamate desuccinylase /aspartoacylase, which hydrolyzes N-acetyl-L-aspartate (NAA), and deficiency in which is the established cause of Canavan disease. Another subfamily (referred to as subfamily C) includes an exceptional type of activity in the MCP family, that of dipeptidyl-peptidase activity of gamma-glutamyl-(L)-meso-diaminopimelate peptidase I which is involved in bacterial cell wall metabolism.


Pssm-ID: 349450 [Multi-domain]  Cd Length: 239  Bit Score: 43.06  E-value: 1.07e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446290599  38 PDAPVDRALILSAGIHGNETAPVEMLDKLLSALYSGSLT-LTWRVLVVLgNPQALAAGIRYCHS--DMNRmfggrwqSFA 114
Cdd:cd06231   37 NPRGDKPRVLISAGIHGDEPAGVEALLRFLESLAEKYLRrVNLLVLPCV-NPWGFERNTRENADgiDLNR-------SFL 108

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 446290599 115 ESDETRRARelelSLETFFssgQARVRW--HLDLH 147
Cdd:cd06231  109 KDSPSPEVR----ALMEFL---ASLGRFdlHLDLH 136
MpaA COG2866
Murein tripeptide amidase MpaA [Cell wall/membrane/envelope biogenesis];
33-148 4.52e-03

Murein tripeptide amidase MpaA [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442113 [Multi-domain]  Cd Length: 337  Bit Score: 38.52  E-value: 4.52e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446290599  33 LLELTPDAPVDRALILSAGIHGNETAPVEMLDKLLSAL---YSGSLT-----LTWRVLVVLgNP-------QALAAGIry 97
Cdd:COG2866   55 LLKIGDPAEGKPKVLLNAQQHGNEWTGTEALLGLLEDLldnYDPLIRalldnVTLYIVPML-NPdgaerntRTNANGV-- 131

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 446290599  98 chsDMNRMFGGRWQSfaeSDETRRARELelsLETFfssgqaRVRWHLDLHT 148
Cdd:COG2866  132 ---DLNRDWPAPWLS---EPETRALRDL---LDEH------DPDFVLDLHG 167
M14_ASTE_ASPA-like cd06251
Peptidase M14 Succinylglutamate desuccinylase (ASTE)/aspartoacylase (ASPA)-like; ...
 46-152 4.55e-03

Peptidase M14 Succinylglutamate desuccinylase (ASTE)/aspartoacylase (ASPA)-like; uncharacterized subgroup; A functionally uncharacterized subgroup of the Succinylglutamate desuccinylase (ASTE)/aspartoacylase (ASPA) subfamily which is part of the M14 family of metallocarboxypeptidases. ASTE catalyzes the fifth and last step in arginine catabolism by the arginine succinyltransferase pathway, and aspartoacylase (ASPA, also known as aminoacylase 2, and ACY-2; EC:3.5.1.15) cleaves N-acetyl L-aspartic acid (NAA) into aspartate and acetate. NAA is abundant in the brain, and hydrolysis of NAA by ASPA may help maintain white matter. ASPA is an NAA scavenger in other tissues. Mutations in the gene encoding ASPA cause Canavan disease (CD), a fatal progressive neurodegenerative disorder involving dysmyelination and spongiform degeneration of white matter in children. This enzyme binds zinc which is necessary for activity. Measurement of elevated NAA levels in urine is used in the diagnosis of CD.


Pssm-ID: 349469 [Multi-domain]  Cd Length: 195  Bit Score: 37.52  E-value: 4.55e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446290599  46 LILSAGIHGNETAPVEM----LDKLLSALYSGSLTLtwrVLVVlgNPQALAAGIRY---CHSDMNRMF-GGRWQSFAEsd 117
Cdd:cd06251   15 LLLTAAIHGDELNGIEViqrlLEDLDPSKLRGTLIA---IPVV--NPLGFENNSRYlpdDGRDLNRSFpGSEKGSLAS-- 87

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 446290599 118 etRRARELelsLETFFSSGQArvrwHLDLHTAIRG 152
Cdd:cd06251   88 --RLAHLL---WNEIVKKADY----VIDLHTASTG 113
PRK10602 PRK10602
murein tripeptide amidase MpaA;
38-128 4.83e-03

murein tripeptide amidase MpaA;


Pssm-ID: 182582  Cd Length: 237  Bit Score: 37.70  E-value: 4.83e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446290599  38 PDAPVDRALILsAGIHGNETAPVEMLDKLLSALYSGSLtltwRVLVVLG-NPQALAAGIRyCHS---DMNRMF------- 106
Cdd:PRK10602  35 PAASRESGLIL-AGTHGDETASVVTLSCALRTLTPSLR----RHHVVLAvNPDGCQLGLR-ANAngvDLNRNFpaanwke 108

                         90       100
                 ....*....|....*....|....*
gi 446290599 107 ---GGRWQSFAEsdetrrARELELS 128
Cdd:PRK10602 109 getVYRWNSAAE------ERDVVLL 127
M14_ASTE_ASPA_like cd18174
Peptidase M14 Succinylglutamate desuccinylase (ASTE)/aspartoacylase (ASPA)-like; ...
 46-109 9.10e-03

Peptidase M14 Succinylglutamate desuccinylase (ASTE)/aspartoacylase (ASPA)-like; uncharacterized subgroup; A functionally uncharacterized subgroup of the Succinylglutamate desuccinylase (ASTE)/aspartoacylase (ASPA) subfamily which is part of the M14 family of metallocarboxypeptidases. ASTE catalyzes the fifth and last step in arginine catabolism by the arginine succinyltransferase pathway, and aspartoacylase (ASPA, also known as aminoacylase 2, and ACY-2; EC:3.5.1.15) cleaves N-acetyl L-aspartic acid (NAA) into aspartate and acetate. NAA is abundant in the brain, and hydrolysis of NAA by ASPA may help maintain white matter. ASPA is an NAA scavenger in other tissues. Mutations in the gene encoding ASPA cause Canavan disease (CD), a fatal progressive neurodegenerative disorder involving dysmyelination and spongiform degeneration of white matter in children. This enzyme binds zinc which is necessary for activity. Measurement of elevated NAA levels in urine is used in the diagnosis of CD.


Pssm-ID: 349484  Cd Length: 187  Bit Score: 36.45  E-value: 9.10e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446290599  46 LILSAGIHGNETAPVEMLDKLLS----ALYSGSLtltwrVLVVLGNPQALAA-GIRYCHSD---MNRMFGGR 109
Cdd:cd18174    1 LLVTAGVHGYEYASIEALQRLIKeldpAKLSGTV-----IVVPIANIPAFEGrSIYVNPLDgknLNRSFPGD 67
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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