|
Name |
Accession |
Description |
Interval |
E-value |
| PRK05324 |
PRK05324 |
succinylglutamate desuccinylase; Provisional |
1-340 |
0e+00 |
|
succinylglutamate desuccinylase; Provisional
Pssm-ID: 235408 Cd Length: 329 Bit Score: 510.88 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890126646 1 MIPQHDFLALTRSHEWQLEPfEFALPDGARVSVWDTGVLCLEPASGtddqpgGRKDIVLSCGIHGNETAPIEICNQLLSR 80
Cdd:PRK05324 1 MLAMDDFLALTLAGHPPAVT-EFGLGNGVRWRWLGEGVLELTPAAP------STKALVLSAGIHGNETAPIELLDQLVRD 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890126646 81 LLSGELSARHRVLFLFGNPAAMNLGLREVEENMNRLFSGAHSKGEGLCnrERIRAMRLEQYVSRFFA-DPARPRYHYDLH 159
Cdd:PRK05324 74 LLAGELPLRARLLVILGNPPAMRAGKRYLDEDLNRLFGGRHQQFPGSD--EARRAAELEQAVEDFFAaGAERVRWHYDLH 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890126646 160 TAIRGSRHEKFAVYPFPHeRPHCREQVQFLGACGVRTILLSASPTTTFSYYSSRQHGAHAFTVELGKVRPFGENDMTRFI 239
Cdd:PRK05324 152 TAIRGSKHEQFAVLPQRG-RPWSREQLAWLGAAGIEAVLLHNAPGGTFSHFSSEHFGALACTLELGKVLPFGQNDLSRFA 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890126646 240 ETRQALQELVTQDEvaLEPWRADDFTLFAIDRVITKKSADFRFLFASDVDNFTEFPQGFVLAEDGELRYTVEKPREAVVF 319
Cdd:PRK05324 231 ATDQALRALISGEE--LPERSADPPRLYRVVRQITKHSDDFELHFADDVENFTAFPKGTLLAEDGDERYVVEHDGERIVF 308
|
330 340
....*....|....*....|.
gi 1890126646 320 PNANVAIGQRTVLMVVPTRLW 340
Cdd:PRK05324 309 PNPNVAIGLRAGLMLVPTTLD 329
|
|
| AstE |
COG2988 |
Succinylglutamate desuccinylase [Amino acid transport and metabolism]; |
29-340 |
1.55e-142 |
|
Succinylglutamate desuccinylase [Amino acid transport and metabolism];
Pssm-ID: 442227 Cd Length: 305 Bit Score: 405.00 E-value: 1.55e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890126646 29 ARVSVWDTGVLCLEPASGtddqpgGRKDIVLSCGIHGNETAPIEICNQLLSRLLSGELSARHRVLFLFGNPAAMNLGLRE 108
Cdd:COG2988 5 ALTRWLDEGVLELTPHAP------GIKAVVISGGIHGNETAPIELLDKLLQDLLLGERPLSFRLLLILGNPAAMRAGRRY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890126646 109 VEENMNRLFSGAHSKGEGlcNRERIRAMRLEQYVSRFFADPARPRYHYDLHTAIRGSRHEKFAVYPFpHERPHCREQVQF 188
Cdd:COG2988 79 LDEDLNRLFGGRHLQNPE--SYEAARAKELEQAVGPFFAAGGRVRLHIDLHTAIRNSGHERFAVYPF-RGRPFDLALLAY 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890126646 189 LGACGVRTILLSASPTTTFSYYSSRQHGAHAFTVELGKVRPFGENDMTRFIETRQALQELVtqDEVALEPWRADDFTLFA 268
Cdd:COG2988 156 LAAAGPEAVVLHHAPGGTFSHFSAELCGAQAFTLELGKVRPFGQNDLSRFAATEEALRALL--SGAELPEHPAQDLDLYR 233
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1890126646 269 IDRVITKKSADFRFLFASDVDNFTEFPQGFVLAEDGELRYTVEKPREAVVFPNANVAIGQRTVLMVVPTRLW 340
Cdd:COG2988 234 VVQQIIKHGDDFMLHPDLDTLNFTPLPPGTLLAEDGGKEYRVEGDEERIVFPNEAVYYGQRAALLLTPKELI 305
|
|
| M14_ASTE |
cd03855 |
Peptidase M14 Succinylglutamate desuccinylase (ASTE) subfamily; Peptidase M14 ... |
6-251 |
4.26e-130 |
|
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: 371.15 E-value: 4.26e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890126646 6 DFLALTRSHEWQLEPFEFALPDGARVSVWDTGVLCLEPASGTDdqpggrKDIVLSCGIHGNETAPIEICNQLLSRLLSGE 85
Cdd:cd03855 1 DFLALTLSGSEPAEGELAAVSNGTRVRWLATGVLELTPAASAS------KSVVLSAGIHGNETAPIEILDQLINDLIRGE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890126646 86 LSARHRVLFLFGNPAAMNLGLREVEENMNRLFSGAHSKGEglCNRERIRAMRLEQYVSRFFADPA-RPRYHYDLHTAIRG 164
Cdd:cd03855 75 LALAHRLLFIFGNPPAIRQGKRFIEENLNRLFSGRHSKLP--PSYETARAAELEQAVADFFAKASgEVRWHLDLHTAIRG 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890126646 165 SRHEKFAVYPFPHERPHCREQVQFLGACGVRTILLSASPTTTFSYYSSRQHGAHAFTVELGKVRPFGENDMTRFIETRQA 244
Cdd:cd03855 153 SKHEQFAVYPFLEGRPHDREQLDFLGAAGIEAVLLSNSPGGTFSYYSSEHFGAAAFTVELGKVRPFGQNDLSQFAAIDQA 232
|
....*..
gi 1890126646 245 LQELVTQ 251
Cdd:cd03855 233 LRALISG 239
|
|
| arg_catab_astE |
TIGR03242 |
succinylglutamate desuccinylase; Members of this protein family are succinylglutamate ... |
6-335 |
5.39e-123 |
|
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: 356.29 E-value: 5.39e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890126646 6 DFLALTRSHEwqlEPF-EFALPDGARVSVWDTGVLCLEPASGtddqpgGRKDIVLSCGIHGNETAPIEICNQLLSRLLSG 84
Cdd:TIGR03242 1 DFLALTLTGK---KPHvTQGETNNVRWRWLGEGVLELTPHAP------PQKSLVISAGIHGNETAPIEILEQLLGDIAAG 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890126646 85 ELSARHRVLFLFGNPAAMNLGLREVEENMNRLFSGAHSKGEGlcNRERIRAMRLEQYVSRFFADP--ARPRYHYDLHTAI 162
Cdd:TIGR03242 72 KLPLRVRLLVILGNPPAMRTGKRYLHDDLNRMFGGRYQQLAP--SFETCRAAELEQCVEDFFSQGgrSVARWHYDLHTAI 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890126646 163 RGSRHEKFAVYPFpHERPHCREQVQFLGACGVRTILLSASPTTTFSYYSSRQHGAHAFTVELGKVRPFGENDMTRFIETR 242
Cdd:TIGR03242 150 RGSLHEQFALLPY-QGRPWDREFLTWLGAAGLDALVFHTEPGGTFSHFSSEHFGALACTLELGKALPFGQNDLSQFAAIT 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890126646 243 QALQELVTqdEVALEPWRADDFTLFAIDRVITKKSADFRFLFASDVDNFTEFPQGFVLAEDGELRYTVEKPREAVVFPNA 322
Cdd:TIGR03242 229 SALRALIS--DEAIPARRTDPLRLFRVVSSITKHSDSFELHVASDTLNFTPFPKGTLLATDGNERYRVTHEGERILFPNP 306
|
330
....*....|...
gi 1890126646 323 NVAIGQRTVLMVV 335
Cdd:TIGR03242 307 NVANGLRAGLMLV 319
|
|
| AstE_AspA |
pfam04952 |
Succinylglutamate desuccinylase / Aspartoacylase family; This family includes ... |
55-338 |
7.25e-65 |
|
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: 206.82 E-value: 7.25e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890126646 55 KDIVLSCGIHGNETAPIEICNQLLSRLLSGELSARhRVLFLFGNPAAMNLGLREVEENMNRLFSGAHskgEGLCNRERIR 134
Cdd:pfam04952 3 PTLLLSAGIHGNETNGVELLRRLLRQLDPGDIAGE-RTLVPLANPPAFRAGSRYIPRDLNRSFPGRA---LGASSDEPYR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890126646 135 AMRLEQYVSRFF-ADPARPRYHYDLHTAIRGSRHEKFAVYPFpheRPHCREQVQFLGACGVRTILLSAS-PTTTFSYYSS 212
Cdd:pfam04952 79 ATRAERLADLFFpALLPRADIVLDLHTGTRGMGHLLFALAPI---RDDPLHLLALLRAFGAPAVLKLHSkPSAGFSAFSA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890126646 213 RQHGAHAFTVELGKVRPFGENDMTRFIETRQALQELVTQdeVALEPWRADDFTLFAIDRVITKKSA---------DFRFL 283
Cdd:pfam04952 156 EELGAPGFTLELGGAGPFGANLISRTAAGVLNVLRLIGV--LNGGPDAFEPPKLYRVLREIDRPRDiraelaglvEFALN 233
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1890126646 284 FASDVDNFTEFPQGFVLAEDGELRYTVEKPR-EAVVFPNANVAIGQRTVLMVVPTR 338
Cdd:pfam04952 234 LGDDVDAGPLLPGGPLFAPFGGEETEYRAPEdGYPVFPNEAAYVGKGAALALVAKF 289
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK05324 |
PRK05324 |
succinylglutamate desuccinylase; Provisional |
1-340 |
0e+00 |
|
succinylglutamate desuccinylase; Provisional
Pssm-ID: 235408 Cd Length: 329 Bit Score: 510.88 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890126646 1 MIPQHDFLALTRSHEWQLEPfEFALPDGARVSVWDTGVLCLEPASGtddqpgGRKDIVLSCGIHGNETAPIEICNQLLSR 80
Cdd:PRK05324 1 MLAMDDFLALTLAGHPPAVT-EFGLGNGVRWRWLGEGVLELTPAAP------STKALVLSAGIHGNETAPIELLDQLVRD 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890126646 81 LLSGELSARHRVLFLFGNPAAMNLGLREVEENMNRLFSGAHSKGEGLCnrERIRAMRLEQYVSRFFA-DPARPRYHYDLH 159
Cdd:PRK05324 74 LLAGELPLRARLLVILGNPPAMRAGKRYLDEDLNRLFGGRHQQFPGSD--EARRAAELEQAVEDFFAaGAERVRWHYDLH 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890126646 160 TAIRGSRHEKFAVYPFPHeRPHCREQVQFLGACGVRTILLSASPTTTFSYYSSRQHGAHAFTVELGKVRPFGENDMTRFI 239
Cdd:PRK05324 152 TAIRGSKHEQFAVLPQRG-RPWSREQLAWLGAAGIEAVLLHNAPGGTFSHFSSEHFGALACTLELGKVLPFGQNDLSRFA 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890126646 240 ETRQALQELVTQDEvaLEPWRADDFTLFAIDRVITKKSADFRFLFASDVDNFTEFPQGFVLAEDGELRYTVEKPREAVVF 319
Cdd:PRK05324 231 ATDQALRALISGEE--LPERSADPPRLYRVVRQITKHSDDFELHFADDVENFTAFPKGTLLAEDGDERYVVEHDGERIVF 308
|
330 340
....*....|....*....|.
gi 1890126646 320 PNANVAIGQRTVLMVVPTRLW 340
Cdd:PRK05324 309 PNPNVAIGLRAGLMLVPTTLD 329
|
|
| AstE |
COG2988 |
Succinylglutamate desuccinylase [Amino acid transport and metabolism]; |
29-340 |
1.55e-142 |
|
Succinylglutamate desuccinylase [Amino acid transport and metabolism];
Pssm-ID: 442227 Cd Length: 305 Bit Score: 405.00 E-value: 1.55e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890126646 29 ARVSVWDTGVLCLEPASGtddqpgGRKDIVLSCGIHGNETAPIEICNQLLSRLLSGELSARHRVLFLFGNPAAMNLGLRE 108
Cdd:COG2988 5 ALTRWLDEGVLELTPHAP------GIKAVVISGGIHGNETAPIELLDKLLQDLLLGERPLSFRLLLILGNPAAMRAGRRY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890126646 109 VEENMNRLFSGAHSKGEGlcNRERIRAMRLEQYVSRFFADPARPRYHYDLHTAIRGSRHEKFAVYPFpHERPHCREQVQF 188
Cdd:COG2988 79 LDEDLNRLFGGRHLQNPE--SYEAARAKELEQAVGPFFAAGGRVRLHIDLHTAIRNSGHERFAVYPF-RGRPFDLALLAY 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890126646 189 LGACGVRTILLSASPTTTFSYYSSRQHGAHAFTVELGKVRPFGENDMTRFIETRQALQELVtqDEVALEPWRADDFTLFA 268
Cdd:COG2988 156 LAAAGPEAVVLHHAPGGTFSHFSAELCGAQAFTLELGKVRPFGQNDLSRFAATEEALRALL--SGAELPEHPAQDLDLYR 233
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1890126646 269 IDRVITKKSADFRFLFASDVDNFTEFPQGFVLAEDGELRYTVEKPREAVVFPNANVAIGQRTVLMVVPTRLW 340
Cdd:COG2988 234 VVQQIIKHGDDFMLHPDLDTLNFTPLPPGTLLAEDGGKEYRVEGDEERIVFPNEAVYYGQRAALLLTPKELI 305
|
|
| M14_ASTE |
cd03855 |
Peptidase M14 Succinylglutamate desuccinylase (ASTE) subfamily; Peptidase M14 ... |
6-251 |
4.26e-130 |
|
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: 371.15 E-value: 4.26e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890126646 6 DFLALTRSHEWQLEPFEFALPDGARVSVWDTGVLCLEPASGTDdqpggrKDIVLSCGIHGNETAPIEICNQLLSRLLSGE 85
Cdd:cd03855 1 DFLALTLSGSEPAEGELAAVSNGTRVRWLATGVLELTPAASAS------KSVVLSAGIHGNETAPIEILDQLINDLIRGE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890126646 86 LSARHRVLFLFGNPAAMNLGLREVEENMNRLFSGAHSKGEglCNRERIRAMRLEQYVSRFFADPA-RPRYHYDLHTAIRG 164
Cdd:cd03855 75 LALAHRLLFIFGNPPAIRQGKRFIEENLNRLFSGRHSKLP--PSYETARAAELEQAVADFFAKASgEVRWHLDLHTAIRG 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890126646 165 SRHEKFAVYPFPHERPHCREQVQFLGACGVRTILLSASPTTTFSYYSSRQHGAHAFTVELGKVRPFGENDMTRFIETRQA 244
Cdd:cd03855 153 SKHEQFAVYPFLEGRPHDREQLDFLGAAGIEAVLLSNSPGGTFSYYSSEHFGAAAFTVELGKVRPFGQNDLSQFAAIDQA 232
|
....*..
gi 1890126646 245 LQELVTQ 251
Cdd:cd03855 233 LRALISG 239
|
|
| arg_catab_astE |
TIGR03242 |
succinylglutamate desuccinylase; Members of this protein family are succinylglutamate ... |
6-335 |
5.39e-123 |
|
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: 356.29 E-value: 5.39e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890126646 6 DFLALTRSHEwqlEPF-EFALPDGARVSVWDTGVLCLEPASGtddqpgGRKDIVLSCGIHGNETAPIEICNQLLSRLLSG 84
Cdd:TIGR03242 1 DFLALTLTGK---KPHvTQGETNNVRWRWLGEGVLELTPHAP------PQKSLVISAGIHGNETAPIEILEQLLGDIAAG 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890126646 85 ELSARHRVLFLFGNPAAMNLGLREVEENMNRLFSGAHSKGEGlcNRERIRAMRLEQYVSRFFADP--ARPRYHYDLHTAI 162
Cdd:TIGR03242 72 KLPLRVRLLVILGNPPAMRTGKRYLHDDLNRMFGGRYQQLAP--SFETCRAAELEQCVEDFFSQGgrSVARWHYDLHTAI 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890126646 163 RGSRHEKFAVYPFpHERPHCREQVQFLGACGVRTILLSASPTTTFSYYSSRQHGAHAFTVELGKVRPFGENDMTRFIETR 242
Cdd:TIGR03242 150 RGSLHEQFALLPY-QGRPWDREFLTWLGAAGLDALVFHTEPGGTFSHFSSEHFGALACTLELGKALPFGQNDLSQFAAIT 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890126646 243 QALQELVTqdEVALEPWRADDFTLFAIDRVITKKSADFRFLFASDVDNFTEFPQGFVLAEDGELRYTVEKPREAVVFPNA 322
Cdd:TIGR03242 229 SALRALIS--DEAIPARRTDPLRLFRVVSSITKHSDSFELHVASDTLNFTPFPKGTLLATDGNERYRVTHEGERILFPNP 306
|
330
....*....|...
gi 1890126646 323 NVAIGQRTVLMVV 335
Cdd:TIGR03242 307 NVANGLRAGLMLV 319
|
|
| AstE_AspA |
pfam04952 |
Succinylglutamate desuccinylase / Aspartoacylase family; This family includes ... |
55-338 |
7.25e-65 |
|
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: 206.82 E-value: 7.25e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890126646 55 KDIVLSCGIHGNETAPIEICNQLLSRLLSGELSARhRVLFLFGNPAAMNLGLREVEENMNRLFSGAHskgEGLCNRERIR 134
Cdd:pfam04952 3 PTLLLSAGIHGNETNGVELLRRLLRQLDPGDIAGE-RTLVPLANPPAFRAGSRYIPRDLNRSFPGRA---LGASSDEPYR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890126646 135 AMRLEQYVSRFF-ADPARPRYHYDLHTAIRGSRHEKFAVYPFpheRPHCREQVQFLGACGVRTILLSAS-PTTTFSYYSS 212
Cdd:pfam04952 79 ATRAERLADLFFpALLPRADIVLDLHTGTRGMGHLLFALAPI---RDDPLHLLALLRAFGAPAVLKLHSkPSAGFSAFSA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890126646 213 RQHGAHAFTVELGKVRPFGENDMTRFIETRQALQELVTQdeVALEPWRADDFTLFAIDRVITKKSA---------DFRFL 283
Cdd:pfam04952 156 EELGAPGFTLELGGAGPFGANLISRTAAGVLNVLRLIGV--LNGGPDAFEPPKLYRVLREIDRPRDiraelaglvEFALN 233
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1890126646 284 FASDVDNFTEFPQGFVLAEDGELRYTVEKPR-EAVVFPNANVAIGQRTVLMVVPTR 338
Cdd:pfam04952 234 LGDDVDAGPLLPGGPLFAPFGGEETEYRAPEdGYPVFPNEAAYVGKGAALALVAKF 289
|
|
| COG3608 |
COG3608 |
Predicted deacylase [General function prediction only]; |
52-329 |
6.11e-16 |
|
Predicted deacylase [General function prediction only];
Pssm-ID: 442826 [Multi-domain] Cd Length: 296 Bit Score: 76.81 E-value: 6.11e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890126646 52 GGRKD---IVLSCGIHGNETAPIEICNQLLSRLLSGELSArhRVLFL-FGNPAAMNLGLR---EVEENMNRLFSGaHSKG 124
Cdd:COG3608 21 RGAGPgptLLITAGIHGDELNGIEALRRLLRELDPGELRG--TVILVpVANPPGFLQGSRylpIDGRDLNRSFPG-DADG 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890126646 125 EglcnreriramrLEQYVSRFFADPARPRYHY--DLHTAIRGSRHEKFAVYPFPHERphCREQVQFLGAcgvRTILLS-A 201
Cdd:COG3608 98 S------------LAERIAHALFEEILPDADYviDLHSGGIARDNLPHVRAGPGDEE--LRALARAFGA---PVILDSpE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890126646 202 SPTTTFSYYSSRQhGAHAFTVELGKVRPFGENDMTRFIE-TRQALQEL-VTQDEValEPWRADDFTLFAIDRVITKKSAD 279
Cdd:COG3608 161 GGDGSLREAAAEA-GIPALTLELGGGGRFDEESIEAGVRgILNVLRHLgMLDGEA--PPPPLAPPVLARGSEWVRAPAGG 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1890126646 280 frfLFASDVDNFTEFPQGFVLAE----DGELRYTVEKPREAVVF---PNANVAIGQR 329
Cdd:COG3608 238 ---LFEPLVELGDRVKKGDVLGRitdpFGEEVEEVRAPVDGIVIgrrTNPLVNPGDA 291
|
|
| M14_ASTE_ASPA_like |
cd06230 |
Peptidase M14 Succinylglutamate desuccinylase (ASTE)/aspartoacylase (ASPA) subfamily; The ... |
57-226 |
9.30e-15 |
|
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: 71.19 E-value: 9.30e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890126646 57 IVLSCGIHGNETAPIEICNQLLSRLLSGELSARHRVLFLFgNPAAMNLGLREVEE---NMNRLFSGAHSKGEGlcnrERI 133
Cdd:cd06230 1 LLILAGVHGDEYEGVEAIRRLLAELDPSELKGTVVLVPVA-NPPAFEAGTRYTPLdglDLNRIFPGDPDGSPT----ERL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890126646 134 RAMRLEQyvsrfFADPArpRYHYDLHTAIRGSRHEKFAVYPFPHERPHCREQVQFLGACGVrtILLS-ASPTTTFSYYSS 212
Cdd:cd06230 76 AHELTEL-----ILKHA--DALIDLHSGGTGRLVPYAILDYDSDAREKSRELARAFGGTPV--IWGGdPPGGTPVAAARS 146
|
170
....*....|....
gi 1890126646 213 rqHGAHAFTVELGK 226
Cdd:cd06230 147 --AGIPAITVELGG 158
|
|
| Peptidase_M14_like |
cd00596 |
M14 family of metallocarboxypeptidases and related proteins; The M14 family of ... |
57-235 |
1.58e-09 |
|
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: 57.08 E-value: 1.58e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890126646 57 IVLSCGIHGNETAPIEICNQLLSRLLSG-------ELSARHRVLFLFG-NPAAMNLGLR------EVEENMNRLFSGAHS 122
Cdd:cd00596 1 ILITGGIHGNEVIGVELALALIEYLLENygndplkRLLDNVELWIVPLvNPDGFARVIDsggrknANGVDLNRNFPYNWG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890126646 123 KGEGLCNRER------------IRAMRleQYVSRFfadpaRPRYHYDLHTAIrgsrheKFAVYPFPHERP------HCRE 184
Cdd:cd00596 81 KDGTSGPSSPtyrgpapfsepeTQALR--DLAKSH-----RFDLAVSYHSSS------EAILYPYGYTNEpppdfsEFQE 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1890126646 185 QVQ------FLGACGVRTILLSASPTTTFSYYSSRQHGAHAFTVELGKVRPFGENDM 235
Cdd:cd00596 148 LAAglaralGAGEYGYGYSYTWYSTTGTADDWLYGELGILAFTVELGTADYPLPGTL 204
|
|
| M14_ASTE_ASPA_like |
cd18430 |
Succinylglutamate desuccinylase/aspartoacylase; uncharacterized; A functionally ... |
57-119 |
8.02e-08 |
|
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: 51.29 E-value: 8.02e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1890126646 57 IVLSCgIHGNETAPIEICNQLLSRLLSGELSARhRVLFLFGNPAAMNLGLREVEENMNRLFSG 119
Cdd:cd18430 2 AVLGA-VHGNETCGTRAVERLLAELPSGALQKG-PVTLVPANERAYAEGVRFCEEDLNRVFPG 62
|
|
| M14_ASPA |
cd06909 |
Peptidase M14 Aspartoacylase (ASPA) subfamily; Aspartoacylase (ASPA) belongs to the ... |
55-227 |
1.32e-07 |
|
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: 51.05 E-value: 1.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890126646 55 KDIVLSCGIHGNETAPIEICNQLLSrllSGELSARH--RVLFLFGNPAAMNLGLREVEENMNRLFSGAHSK-GEGLCNRE 131
Cdd:cd06909 1 KRVAIVGGTHGNELTGVYLVKHWLK---NPELIERKsfEVHPLLANPRAVEQCRRYIDTDLNRCFSLENLSsAPSSLPYE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890126646 132 RIRAMRLEQyvsrFFADPARPRYHY--DLHTA--------IRGSRHE---KFAVYPFpHERPHCReqvqflgacgvrtIL 198
Cdd:cd06909 78 VRRAREINQ----ILGPKGNPACDFiiDLHNTtsnmgitlILSSSDDftlKLAAYLQ-QRLPPVR-------------VL 139
|
170 180
....*....|....*....|....*....
gi 1890126646 199 LSASPTTTFSYYSSRqhGAHAFTVELGKV 227
Cdd:cd06909 140 LHESPSKESPFLRSV--AKHGFTIEVGPV 166
|
|
| PRK02259 |
PRK02259 |
aspartoacylase; Provisional |
55-135 |
1.45e-06 |
|
aspartoacylase; Provisional
Pssm-ID: 235019 Cd Length: 288 Bit Score: 49.10 E-value: 1.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890126646 55 KDIVLSCGIHGNETAPIEICNQLLSrllSGELSARHR--VLFLFGNPAAMNLGLREVEENMNRLFSGAHSKGEGLCNRER 132
Cdd:PRK02259 3 NRVAIVGGTHGNEITGIYLVKKWQQ---QPNLINRKGleVQTVIGNPEAIEAGRRYIDRDLNRSFRLDLLQNPDLSGYEQ 79
|
...
gi 1890126646 133 IRA 135
Cdd:PRK02259 80 LRA 82
|
|
| M14_ASTE_ASPA-like |
cd06251 |
Peptidase M14 Succinylglutamate desuccinylase (ASTE)/aspartoacylase (ASPA)-like; ... |
53-240 |
2.65e-06 |
|
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: 47.15 E-value: 2.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890126646 53 GRKD---IVLSCGIHGNETAPIEICNQLLSRL----LSGELSARHRVlflfgNPAAMNLGLREV---EENMNRLFSGAHS 122
Cdd:cd06251 8 GAKPgptLLLTAAIHGDELNGIEVIQRLLEDLdpskLRGTLIAIPVV-----NPLGFENNSRYLpddGRDLNRSFPGSEK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890126646 123 KGEGlcnreriramrlEQYVSRFF------ADparprYHYDLHTAIRGSRHekfavYPFPHERPHCREQVQFLGACGVRT 196
Cdd:cd06251 83 GSLA------------SRLAHLLWneivkkAD-----YVIDLHTASTGRTN-----LPYVRADLRDPESRRMAEAFGAPV 140
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1890126646 197 ILLSASPTTTFsyyssrqHGAH------AFTVELGKVRPFGENDMTRFIE 240
Cdd:cd06251 141 IVDDPGEDGSL-------RGAAvelgipAITVELGEALRFDEDIIRRGVE 183
|
|
| M14_ASTE_ASPA-like |
cd06253 |
Peptidase M14 Succinylglutamate desuccinylase (ASTE)/aspartoacylase (ASPA)-like; ... |
62-226 |
1.35e-04 |
|
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: 1.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890126646 62 GIHGNETAPIEICNQL---LSRLLSGELSARHRVLFL-FGNPAAMNLGLREVEE---NMNRLFSGAhSKGEglcnrerir 134
Cdd:cd06253 30 GIHGDELNGLYVCSRLirfLKELEEGGYKLKGKVLVIpAVNPLGINSGTRFWPFdnlDMNRMFPGY-NKGE--------- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890126646 135 amrLEQYVSR-FFADPARPRYHYDLHTAIrgsRHEKFA----VYPFPHERPhcREQVQFLGACGVRTILLSASPTTTFsY 209
Cdd:cd06253 100 ---TTERIAAaLFEDLKGADYGIDLHSSN---DFLREIpqvrVIESGAQDL--LPLAKFLGLDVVWVHPASTVDTGTL-A 170
|
170
....*....|....*..
gi 1890126646 210 YSSRQHGAHAFTVELGK 226
Cdd:cd06253 171 YNWNEWGTKALVLEMGV 187
|
|
| M14_MpaA-like |
cd06904 |
Peptidase M14-like domain of Escherichia coli Murein Peptide Amidase A and related proteins; ... |
32-107 |
4.60e-03 |
|
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: 38.03 E-value: 4.60e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1890126646 32 SVWDTGVLCLEPasgtddQPGGRKDIVLSCGIHGNETAPIEICNQLLSRLL-SGELSARHRVLFLFGNPAAMNLGLR 107
Cdd:cd06904 7 SVKGRPILAYKF------GPGSRARILIIGGIHGDEPEGVSLVEHLLRWLKnHPASGDFHIVVVPCLNPDGLAAGTR 77
|
|
| |
