|
Name |
Accession |
Description |
Interval |
E-value |
| PRK05324 |
PRK05324 |
succinylglutamate desuccinylase; Provisional |
14-343 |
1.11e-174 |
|
succinylglutamate desuccinylase; Provisional
Pssm-ID: 235408 Cd Length: 329 Bit Score: 487.77 E-value: 1.11e-174
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658755925 14 SGDFLTLSRDNEWHLEAsEFALENGTRVTVHDTGVIEFQPQGTTTKDVVLSSAVHGNETAPIEICDELIKTIIKGELALN 93
Cdd:PRK05324 4 MDDFLALTLAGHPPAVT-EFGLGNGVRWRWLGEGVLELTPAAPSTKALVLSAGIHGNETAPIELLDQLVRDLLAGELPLR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658755925 94 QRVLFIFGNPKSINIGLRFVEENLNRLFNGHHTVegVPMNDERKRAAKLEEYVTDFFtRGEQGSARYHYDLHTAIRGSKN 173
Cdd:PRK05324 83 ARLLVILGNPPAMRAGKRYLDEDLNRLFGGRHQQ--FPGSDEARRAAELEQAVEDFF-AAGAERVRWHYDLHTAIRGSKH 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658755925 174 EKFAVYPYlHGKPWKKSQLQFLLSCGVNTVLMMKSPATTFSYYSSFVHGADSFTVELGQVKPFGENDMARFAKTKQTLTA 253
Cdd:PRK05324 160 EQFAVLPQ-RGRPWSREQLAWLGAAGIEAVLLHNAPGGTFSHFSSEHFGALACTLELGKVLPFGQNDLSRFAATDQALRA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658755925 254 LISQKEvqYPQFNASDFELFAVHRTINRTQQDFSFPFSDDAENFTGFAKGELLATDGDTPYYADVEGEAIIFPNAHVALG 333
Cdd:PRK05324 239 LISGEE--LPERSADPPRLYRVVRQITKHSDDFELHFADDVENFTAFPKGTLLAEDGDERYVVEHDGERIVFPNPNVAIG 316
|
330
....*....|
gi 658755925 334 QRALLTVIPM 343
Cdd:PRK05324 317 LRAGLMLVPT 326
|
|
| AstE |
COG2988 |
Succinylglutamate desuccinylase [Amino acid transport and metabolism]; |
39-346 |
1.84e-134 |
|
Succinylglutamate desuccinylase [Amino acid transport and metabolism];
Pssm-ID: 442227 Cd Length: 305 Bit Score: 384.97 E-value: 1.84e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658755925 39 TRVTVHDTGVIEFQPQGTTTKDVVLSSAVHGNETAPIEICDELIKTIIKGELALNQRVLFIFGNPKSINIGLRFVEENLN 118
Cdd:COG2988 5 ALTRWLDEGVLELTPHAPGIKAVVISGGIHGNETAPIELLDKLLQDLLLGERPLSFRLLLILGNPAAMRAGRRYLDEDLN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658755925 119 RLFNGHHTVEgvPMNDERKRAAKLEEYVTDFFtrGEQGSARYHYDLHTAIRGSKNEKFAVYPYlHGKPWKKSQLQFLLSC 198
Cdd:COG2988 85 RLFGGRHLQN--PESYEAARAKELEQAVGPFF--AAGGRVRLHIDLHTAIRNSGHERFAVYPF-RGRPFDLALLAYLAAA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658755925 199 GVNTVLMMKSPATTFSYYSSFVHGADSFTVELGQVKPFGENDMARFAKTKQTLTALISqkEVQYPQFNASDFELFAVHRT 278
Cdd:COG2988 160 GPEAVVLHHAPGGTFSHFSAELCGAQAFTLELGKVRPFGQNDLSRFAATEEALRALLS--GAELPEHPAQDLDLYRVVQQ 237
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 658755925 279 INRTQQDFSFPFSDDAENFTGFAKGELLATDGDTPYYADVEGEAIIFPNAHVALGQRALLTVIPMQVD 346
Cdd:COG2988 238 IIKHGDDFMLHPDLDTLNFTPLPPGTLLAEDGGKEYRVEGDEERIVFPNEAVYYGQRAALLLTPKELI 305
|
|
| M14_ASTE |
cd03855 |
Peptidase M14 Succinylglutamate desuccinylase (ASTE) subfamily; Peptidase M14 ... |
16-257 |
3.49e-131 |
|
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: 374.23 E-value: 3.49e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658755925 16 DFLTLSRDNEWHLEASEFALENGTRVTVHDTGVIEFQPQGTTTKDVVLSSAVHGNETAPIEICDELIKTIIKGELALNQR 95
Cdd:cd03855 1 DFLALTLSGSEPAEGELAAVSNGTRVRWLATGVLELTPAASASKSVVLSAGIHGNETAPIEILDQLINDLIRGELALAHR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658755925 96 VLFIFGNPKSINIGLRFVEENLNRLFNGHHTVegVPMNDERKRAAKLEEYVTDFFTRGeQGSARYHYDLHTAIRGSKNEK 175
Cdd:cd03855 81 LLFIFGNPPAIRQGKRFIEENLNRLFSGRHSK--LPPSYETARAAELEQAVADFFAKA-SGEVRWHLDLHTAIRGSKHEQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658755925 176 FAVYPYLHGKPWKKSQLQFLLSCGVNTVLMMKSPATTFSYYSSFVHGADSFTVELGQVKPFGENDMARFAKTKQTLTALI 255
Cdd:cd03855 158 FAVYPFLEGRPHDREQLDFLGAAGIEAVLLSNSPGGTFSYYSSEHFGAAAFTVELGKVRPFGQNDLSQFAAIDQALRALI 237
|
..
gi 658755925 256 SQ 257
Cdd:cd03855 238 SG 239
|
|
| arg_catab_astE |
TIGR03242 |
succinylglutamate desuccinylase; Members of this protein family are succinylglutamate ... |
16-341 |
2.62e-117 |
|
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: 342.04 E-value: 2.62e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658755925 16 DFLTLSR-DNEWHLEASEfalENGTRVTVHDTGVIEFQPQGTTTKDVVLSSAVHGNETAPIEICDELIKTIIKGELALNQ 94
Cdd:TIGR03242 1 DFLALTLtGKKPHVTQGE---TNNVRWRWLGEGVLELTPHAPPQKSLVISAGIHGNETAPIEILEQLLGDIAAGKLPLRV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658755925 95 RVLFIFGNPKSINIGLRFVEENLNRLFNGHHtvEGVPMNDERKRAAKLEEYVTDFFTRGEQGSARYHYDLHTAIRGSKNE 174
Cdd:TIGR03242 78 RLLVILGNPPAMRTGKRYLHDDLNRMFGGRY--QQLAPSFETCRAAELEQCVEDFFSQGGRSVARWHYDLHTAIRGSLHE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658755925 175 KFAVYPYLhGKPWKKSQLQFLLSCGVNTVLMMKSPATTFSYYSSFVHGADSFTVELGQVKPFGENDMARFAKTKQTLTAL 254
Cdd:TIGR03242 156 QFALLPYQ-GRPWDREFLTWLGAAGLDALVFHTEPGGTFSHFSSEHFGALACTLELGKALPFGQNDLSQFAAITSALRAL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658755925 255 ISqkEVQYPQFNASDFELFAVHRTINRTQQDFSFPFSDDAENFTGFAKGELLATDGDTPYYADVEGEAIIFPNAHVALGQ 334
Cdd:TIGR03242 235 IS--DEAIPARRTDPLRLFRVVSSITKHSDSFELHVASDTLNFTPFPKGTLLATDGNERYRVTHEGERILFPNPNVANGL 312
|
....*..
gi 658755925 335 RALLTVI 341
Cdd:TIGR03242 313 RAGLMLV 319
|
|
| AstE_AspA |
pfam04952 |
Succinylglutamate desuccinylase / Aspartoacylase family; This family includes ... |
58-344 |
2.61e-62 |
|
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: 200.65 E-value: 2.61e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658755925 58 TKDVVLSSAVHGNETAPIEICDELIKTIIKGELAlNQRVLFIFGNPKSINIGLRFVEENLNRLFNGHHtvEGVPmNDERK 137
Cdd:pfam04952 2 GPTLLLSAGIHGNETNGVELLRRLLRQLDPGDIA-GERTLVPLANPPAFRAGSRYIPRDLNRSFPGRA--LGAS-SDEPY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658755925 138 RAAKLEEYVTDFFTRGEQgSARYHYDLHTAIRGSKNEKFAVYPYlhgKPWKKSQLQFLLSCGVNTVLMMKS-PATTFSYY 216
Cdd:pfam04952 78 RATRAERLADLFFPALLP-RADIVLDLHTGTRGMGHLLFALAPI---RDDPLHLLALLRAFGAPAVLKLHSkPSAGFSAF 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658755925 217 SSFVHGADSFTVELGQVKPFGENDMARFAKTKQTLTALISQKEVQYPQFNASdfELFAVHRTINRTQ---------QDFS 287
Cdd:pfam04952 154 SAEELGAPGFTLELGGAGPFGANLISRTAAGVLNVLRLIGVLNGGPDAFEPP--KLYRVLREIDRPRdiraelaglVEFA 231
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 658755925 288 FPFSDDAENFTGFAKGELLATD-GDTPYYADVEGEAIIFPNAHVALGQRALLTVIPMQ 344
Cdd:pfam04952 232 LNLGDDVDAGPLLPGGPLFAPFgGEETEYRAPEDGYPVFPNEAAYVGKGAALALVAKF 289
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK05324 |
PRK05324 |
succinylglutamate desuccinylase; Provisional |
14-343 |
1.11e-174 |
|
succinylglutamate desuccinylase; Provisional
Pssm-ID: 235408 Cd Length: 329 Bit Score: 487.77 E-value: 1.11e-174
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658755925 14 SGDFLTLSRDNEWHLEAsEFALENGTRVTVHDTGVIEFQPQGTTTKDVVLSSAVHGNETAPIEICDELIKTIIKGELALN 93
Cdd:PRK05324 4 MDDFLALTLAGHPPAVT-EFGLGNGVRWRWLGEGVLELTPAAPSTKALVLSAGIHGNETAPIELLDQLVRDLLAGELPLR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658755925 94 QRVLFIFGNPKSINIGLRFVEENLNRLFNGHHTVegVPMNDERKRAAKLEEYVTDFFtRGEQGSARYHYDLHTAIRGSKN 173
Cdd:PRK05324 83 ARLLVILGNPPAMRAGKRYLDEDLNRLFGGRHQQ--FPGSDEARRAAELEQAVEDFF-AAGAERVRWHYDLHTAIRGSKH 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658755925 174 EKFAVYPYlHGKPWKKSQLQFLLSCGVNTVLMMKSPATTFSYYSSFVHGADSFTVELGQVKPFGENDMARFAKTKQTLTA 253
Cdd:PRK05324 160 EQFAVLPQ-RGRPWSREQLAWLGAAGIEAVLLHNAPGGTFSHFSSEHFGALACTLELGKVLPFGQNDLSRFAATDQALRA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658755925 254 LISQKEvqYPQFNASDFELFAVHRTINRTQQDFSFPFSDDAENFTGFAKGELLATDGDTPYYADVEGEAIIFPNAHVALG 333
Cdd:PRK05324 239 LISGEE--LPERSADPPRLYRVVRQITKHSDDFELHFADDVENFTAFPKGTLLAEDGDERYVVEHDGERIVFPNPNVAIG 316
|
330
....*....|
gi 658755925 334 QRALLTVIPM 343
Cdd:PRK05324 317 LRAGLMLVPT 326
|
|
| AstE |
COG2988 |
Succinylglutamate desuccinylase [Amino acid transport and metabolism]; |
39-346 |
1.84e-134 |
|
Succinylglutamate desuccinylase [Amino acid transport and metabolism];
Pssm-ID: 442227 Cd Length: 305 Bit Score: 384.97 E-value: 1.84e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658755925 39 TRVTVHDTGVIEFQPQGTTTKDVVLSSAVHGNETAPIEICDELIKTIIKGELALNQRVLFIFGNPKSINIGLRFVEENLN 118
Cdd:COG2988 5 ALTRWLDEGVLELTPHAPGIKAVVISGGIHGNETAPIELLDKLLQDLLLGERPLSFRLLLILGNPAAMRAGRRYLDEDLN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658755925 119 RLFNGHHTVEgvPMNDERKRAAKLEEYVTDFFtrGEQGSARYHYDLHTAIRGSKNEKFAVYPYlHGKPWKKSQLQFLLSC 198
Cdd:COG2988 85 RLFGGRHLQN--PESYEAARAKELEQAVGPFF--AAGGRVRLHIDLHTAIRNSGHERFAVYPF-RGRPFDLALLAYLAAA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658755925 199 GVNTVLMMKSPATTFSYYSSFVHGADSFTVELGQVKPFGENDMARFAKTKQTLTALISqkEVQYPQFNASDFELFAVHRT 278
Cdd:COG2988 160 GPEAVVLHHAPGGTFSHFSAELCGAQAFTLELGKVRPFGQNDLSRFAATEEALRALLS--GAELPEHPAQDLDLYRVVQQ 237
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 658755925 279 INRTQQDFSFPFSDDAENFTGFAKGELLATDGDTPYYADVEGEAIIFPNAHVALGQRALLTVIPMQVD 346
Cdd:COG2988 238 IIKHGDDFMLHPDLDTLNFTPLPPGTLLAEDGGKEYRVEGDEERIVFPNEAVYYGQRAALLLTPKELI 305
|
|
| M14_ASTE |
cd03855 |
Peptidase M14 Succinylglutamate desuccinylase (ASTE) subfamily; Peptidase M14 ... |
16-257 |
3.49e-131 |
|
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: 374.23 E-value: 3.49e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658755925 16 DFLTLSRDNEWHLEASEFALENGTRVTVHDTGVIEFQPQGTTTKDVVLSSAVHGNETAPIEICDELIKTIIKGELALNQR 95
Cdd:cd03855 1 DFLALTLSGSEPAEGELAAVSNGTRVRWLATGVLELTPAASASKSVVLSAGIHGNETAPIEILDQLINDLIRGELALAHR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658755925 96 VLFIFGNPKSINIGLRFVEENLNRLFNGHHTVegVPMNDERKRAAKLEEYVTDFFTRGeQGSARYHYDLHTAIRGSKNEK 175
Cdd:cd03855 81 LLFIFGNPPAIRQGKRFIEENLNRLFSGRHSK--LPPSYETARAAELEQAVADFFAKA-SGEVRWHLDLHTAIRGSKHEQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658755925 176 FAVYPYLHGKPWKKSQLQFLLSCGVNTVLMMKSPATTFSYYSSFVHGADSFTVELGQVKPFGENDMARFAKTKQTLTALI 255
Cdd:cd03855 158 FAVYPFLEGRPHDREQLDFLGAAGIEAVLLSNSPGGTFSYYSSEHFGAAAFTVELGKVRPFGQNDLSQFAAIDQALRALI 237
|
..
gi 658755925 256 SQ 257
Cdd:cd03855 238 SG 239
|
|
| arg_catab_astE |
TIGR03242 |
succinylglutamate desuccinylase; Members of this protein family are succinylglutamate ... |
16-341 |
2.62e-117 |
|
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: 342.04 E-value: 2.62e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658755925 16 DFLTLSR-DNEWHLEASEfalENGTRVTVHDTGVIEFQPQGTTTKDVVLSSAVHGNETAPIEICDELIKTIIKGELALNQ 94
Cdd:TIGR03242 1 DFLALTLtGKKPHVTQGE---TNNVRWRWLGEGVLELTPHAPPQKSLVISAGIHGNETAPIEILEQLLGDIAAGKLPLRV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658755925 95 RVLFIFGNPKSINIGLRFVEENLNRLFNGHHtvEGVPMNDERKRAAKLEEYVTDFFTRGEQGSARYHYDLHTAIRGSKNE 174
Cdd:TIGR03242 78 RLLVILGNPPAMRTGKRYLHDDLNRMFGGRY--QQLAPSFETCRAAELEQCVEDFFSQGGRSVARWHYDLHTAIRGSLHE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658755925 175 KFAVYPYLhGKPWKKSQLQFLLSCGVNTVLMMKSPATTFSYYSSFVHGADSFTVELGQVKPFGENDMARFAKTKQTLTAL 254
Cdd:TIGR03242 156 QFALLPYQ-GRPWDREFLTWLGAAGLDALVFHTEPGGTFSHFSSEHFGALACTLELGKALPFGQNDLSQFAAITSALRAL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658755925 255 ISqkEVQYPQFNASDFELFAVHRTINRTQQDFSFPFSDDAENFTGFAKGELLATDGDTPYYADVEGEAIIFPNAHVALGQ 334
Cdd:TIGR03242 235 IS--DEAIPARRTDPLRLFRVVSSITKHSDSFELHVASDTLNFTPFPKGTLLATDGNERYRVTHEGERILFPNPNVANGL 312
|
....*..
gi 658755925 335 RALLTVI 341
Cdd:TIGR03242 313 RAGLMLV 319
|
|
| AstE_AspA |
pfam04952 |
Succinylglutamate desuccinylase / Aspartoacylase family; This family includes ... |
58-344 |
2.61e-62 |
|
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: 200.65 E-value: 2.61e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658755925 58 TKDVVLSSAVHGNETAPIEICDELIKTIIKGELAlNQRVLFIFGNPKSINIGLRFVEENLNRLFNGHHtvEGVPmNDERK 137
Cdd:pfam04952 2 GPTLLLSAGIHGNETNGVELLRRLLRQLDPGDIA-GERTLVPLANPPAFRAGSRYIPRDLNRSFPGRA--LGAS-SDEPY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658755925 138 RAAKLEEYVTDFFTRGEQgSARYHYDLHTAIRGSKNEKFAVYPYlhgKPWKKSQLQFLLSCGVNTVLMMKS-PATTFSYY 216
Cdd:pfam04952 78 RATRAERLADLFFPALLP-RADIVLDLHTGTRGMGHLLFALAPI---RDDPLHLLALLRAFGAPAVLKLHSkPSAGFSAF 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658755925 217 SSFVHGADSFTVELGQVKPFGENDMARFAKTKQTLTALISQKEVQYPQFNASdfELFAVHRTINRTQ---------QDFS 287
Cdd:pfam04952 154 SAEELGAPGFTLELGGAGPFGANLISRTAAGVLNVLRLIGVLNGGPDAFEPP--KLYRVLREIDRPRdiraelaglVEFA 231
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 658755925 288 FPFSDDAENFTGFAKGELLATD-GDTPYYADVEGEAIIFPNAHVALGQRALLTVIPMQ 344
Cdd:pfam04952 232 LNLGDDVDAGPLLPGGPLFAPFgGEETEYRAPEDGYPVFPNEAAYVGKGAALALVAKF 289
|
|
| COG3608 |
COG3608 |
Predicted deacylase [General function prediction only]; |
27-335 |
1.48e-11 |
|
Predicted deacylase [General function prediction only];
Pssm-ID: 442826 [Multi-domain] Cd Length: 296 Bit Score: 64.10 E-value: 1.48e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658755925 27 HLEASEFALENGTRVTVHdtgVIEFQPQGTTtkdVVLSSAVHGNETAPIEICDELIKTIIKGELAlnQRVLFI-FGNPKS 105
Cdd:COG3608 1 RLPLSRLASGTPVSLPVT---VFRGAGPGPT---LLITAGIHGDELNGIEALRRLLRELDPGELR--GTVILVpVANPPG 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658755925 106 INIGLRF---VEENLNRLFNG--HHTVEgvpmndERkRAAKLEEYVTDfftrgeqgSARYHYDLHTAIRGSKNEKFAVYP 180
Cdd:COG3608 73 FLQGSRYlpiDGRDLNRSFPGdaDGSLA------ER-IAHALFEEILP--------DADYVIDLHSGGIARDNLPHVRAG 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658755925 181 YLHGKpwkksQLQFLLSCGVNTVLMMK-SPATTFSYYSSfVHGADSFTVELGQVKPFGENDMARFAK-TKQTLTAL-ISQ 257
Cdd:COG3608 138 PGDEE-----LRALARAFGAPVILDSPeGGDGSLREAAA-EAGIPALTLELGGGGRFDEESIEAGVRgILNVLRHLgMLD 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658755925 258 KEVQYPQFNASdfelfavhRTINRTQQDFSfPFSD----DAENFTGFAKGELLAT------DGDTPYYADVEGEAI-IFP 326
Cdd:COG3608 212 GEAPPPPLAPP--------VLARGSEWVRA-PAGGlfepLVELGDRVKKGDVLGRitdpfgEEVEEVRAPVDGIVIgRRT 282
|
....*....
gi 658755925 327 NAHVALGQR 335
Cdd:COG3608 283 NPLVNPGDA 291
|
|
| M14_ASTE_ASPA_like |
cd06230 |
Peptidase M14 Succinylglutamate desuccinylase (ASTE)/aspartoacylase (ASPA) subfamily; The ... |
61-232 |
4.57e-11 |
|
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: 60.79 E-value: 4.57e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658755925 61 VVLSSAVHGNETAPIEICDELIKTI----IKGELalnqrVLFIFGNPKSINIGLRFVEE---NLNRLFNGHHTveGVPmn 133
Cdd:cd06230 1 LLILAGVHGDEYEGVEAIRRLLAELdpseLKGTV-----VLVPVANPPAFEAGTRYTPLdglDLNRIFPGDPD--GSP-- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658755925 134 dERKRAAKLEEYVTDFftrgeqgsARYHYDLHTAirGSKNEKFAVYPYLHGKPWKKSQLQFLLSCGVNTVLMMKSPA-TT 212
Cdd:cd06230 72 -TERLAHELTELILKH--------ADALIDLHSG--GTGRLVPYAILDYDSDAREKSRELARAFGGTPVIWGGDPPGgTP 140
|
170 180
....*....|....*....|
gi 658755925 213 FSYYSSfvHGADSFTVELGQ 232
Cdd:cd06230 141 VAAARS--AGIPAITVELGG 158
|
|
| M14_ASTE_ASPA_like |
cd18430 |
Succinylglutamate desuccinylase/aspartoacylase; uncharacterized; A functionally ... |
66-142 |
4.59e-09 |
|
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: 55.14 E-value: 4.59e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 658755925 66 AVHGNETAPIEICDELIKTIIKGELaLNQRVLFIFGNPKSINIGLRFVEENLNRLFNGHHTvegvPMNDERKRAAKL 142
Cdd:cd18430 6 AVHGNETCGTRAVERLLAELPSGAL-QKGPVTLVPANERAYAEGVRFCEEDLNRVFPGDPD----PDTYERRLANRL 77
|
|
| Peptidase_M14_like |
cd00596 |
M14 family of metallocarboxypeptidases and related proteins; The M14 family of ... |
61-241 |
2.95e-08 |
|
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: 53.62 E-value: 2.95e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658755925 61 VVLSSAVHGNETAPIEICDELIKTIIKG-------ELALNQRVLFIF-----GNPKSINIGLRF--VEENLNRLFNGHHT 126
Cdd:cd00596 1 ILITGGIHGNEVIGVELALALIEYLLENygndplkRLLDNVELWIVPlvnpdGFARVIDSGGRKnaNGVDLNRNFPYNWG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658755925 127 VEGVPMN--DERKRAAKLEE----YVTDFFtrgEQGSARYHYDLHTAIrgskneKFAVYPYLH----GKPW--------K 188
Cdd:cd00596 81 KDGTSGPssPTYRGPAPFSEpetqALRDLA---KSHRFDLAVSYHSSS------EAILYPYGYtnepPPDFsefqelaaG 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 658755925 189 KSQLQFLLSCGVNTVLMMKSPATTFSYYSSFVHGADSFTVELGQVKPFGENDM 241
Cdd:cd00596 152 LARALGAGEYGYGYSYTWYSTTGTADDWLYGELGILAFTVELGTADYPLPGTL 204
|
|
| PRK02259 |
PRK02259 |
aspartoacylase; Provisional |
59-200 |
4.28e-07 |
|
aspartoacylase; Provisional
Pssm-ID: 235019 Cd Length: 288 Bit Score: 50.64 E-value: 4.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658755925 59 KDVVLSSAVHGNETAPIEicdeLIKTIIKGELALNQR---VLFIFGNPKSINIGLRFVEENLNRLFnghhTVEGVPMND- 134
Cdd:PRK02259 3 NRVAIVGGTHGNEITGIY----LVKKWQQQPNLINRKgleVQTVIGNPEAIEAGRRYIDRDLNRSF----RLDLLQNPDl 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658755925 135 ---ERKRAAKLeeyvTDFFtrGEQGSARYHY--DLH--TAIRGS---------KNEKFAVY-----P---YLHGKPWKks 190
Cdd:PRK02259 75 sgyEQLRAKEL----VQQL--GPKGNSPCDFiiDLHstTANMGLslilygrrpFDLALAAYlqsrlPlpiYLHEKDED-- 146
|
170
....*....|...
gi 658755925 191 QLQFLLS---CGV 200
Cdd:PRK02259 147 QTGFLVElwpCGL 159
|
|
| M14_ASTE_ASPA-like |
cd06254 |
Peptidase M14 Succinylglutamate desuccinylase (ASTE)/aspartoacylase (ASPA)-like; ... |
59-232 |
6.27e-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: 349472 Cd Length: 198 Bit Score: 46.42 E-value: 6.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658755925 59 KDVVLSSAVHGNETAPIEICDELIKTI----IKGelalnqRVLFI-FGNPKSINIGLRFV----EENLNRLFNGhhtveg 129
Cdd:cd06254 12 PTLLITAGIHGGEYPGILAAIRLARELdpadVKG------TLIIVhIANVSGFEARTPFVvpedGKNLNRVFPG------ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658755925 130 vpmnderKRAAKLEEYVTDFFTRGEQGSARYHYDLHTairGSKNEK---FAVYPYLHGKPWKKSQLQFLLSCGVNTVLMM 206
Cdd:cd06254 80 -------DPDGTLTERIAYFLTREIISRADFLIDLHG---GDANEAltpFVYYPGGASEEVNDISRAAAQALGLPYIVIS 149
|
170 180
....*....|....*....|....*..
gi 658755925 207 KSPATTfSYYSSFVH-GADSFTVELGQ 232
Cdd:cd06254 150 SSEKGT-GYYSYAALrGIPSILVERGG 175
|
|
| M14_ASTE_ASPA-like |
cd06253 |
Peptidase M14 Succinylglutamate desuccinylase (ASTE)/aspartoacylase (ASPA)-like; ... |
50-231 |
1.41e-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: 1.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658755925 50 EFQPqGTTTKDVVLSSAVHGNETAPIEICDELIKTIIK---GELALNQRVLFI-FGNPKSINIGLRFVEE---NLNRLFn 122
Cdd:cd06253 15 RFGG-GNAEPRIAIVAGIHGDELNGLYVCSRLIRFLKEleeGGYKLKGKVLVIpAVNPLGINSGTRFWPFdnlDMNRMF- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658755925 123 ghhtvEGVPMNDERKR-AAKLEEYVTDFftrgeqgsaRYHYDLHTA---------IRGSKNEKFAVYPYlhgkpwkksQL 192
Cdd:cd06253 93 -----PGYNKGETTERiAAALFEDLKGA---------DYGIDLHSSndflreipqVRVIESGAQDLLPL---------AK 149
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 658755925 193 QFLLscgvnTVLMMKSPATTFS---YYSSFVHGADSFTVELG 231
Cdd:cd06253 150 FLGL-----DVVWVHPASTVDTgtlAYNWNEWGTKALVLEMG 186
|
|
| M14_ASTE_ASPA-like |
cd06251 |
Peptidase M14 Succinylglutamate desuccinylase (ASTE)/aspartoacylase (ASPA)-like; ... |
61-173 |
2.47e-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: 349469 [Multi-domain] Cd Length: 195 Bit Score: 41.37 E-value: 2.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658755925 61 VVLSSAVHGNETAPIEICDELIKTIIKGELA---------------LNQRVLFIFGnpksiniglrfveENLNRLFNGHH 125
Cdd:cd06251 15 LLLTAAIHGDELNGIEVIQRLLEDLDPSKLRgtliaipvvnplgfeNNSRYLPDDG-------------RDLNRSFPGSE 81
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 658755925 126 TVegvpmNDERKRAAKLEEYVTDFFTrgeqgsarYHYDLHTAIRGSKN 173
Cdd:cd06251 82 KG-----SLASRLAHLLWNEIVKKAD--------YVIDLHTASTGRTN 116
|
|
| M14_ASTE_ASPA-like |
cd06910 |
Peptidase M14 Succinylglutamate desuccinylase (ASTE)/aspartoacylase (ASPA)-like; ... |
60-213 |
3.34e-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: 349481 Cd Length: 208 Bit Score: 41.18 E-value: 3.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658755925 60 DVVLSSAVHGNETAPIEICDELIKTIIKgelALNQRVLFIFGNPKSIN-------IGLRFVEENLNRLFnGHHTVEGVPM 132
Cdd:cd06910 26 HVMINALTHGNEICGAIALDWLLKNGVR---PLRGRLTFCFANVEAYErfdparpTASRFVDEDLNRVW-GPELLDGPEQ 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658755925 133 NDERKRAAKLEEYVTdfftrgeqgSARYHYDLHTAirGSKNEKFAVYPylhgkpwkksqlqfLLSCGVNTVLMMKSPATT 212
Cdd:cd06910 102 SIELRRARELRPVVD---------TVDYLLDIHSM--QEKVPPLALAG--------------DKEKGRALARRVGSPAHL 156
|
.
gi 658755925 213 F 213
Cdd:cd06910 157 L 157
|
|
| M14_ASPA |
cd06909 |
Peptidase M14 Aspartoacylase (ASPA) subfamily; Aspartoacylase (ASPA) belongs to the ... |
59-255 |
8.36e-04 |
|
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: 39.88 E-value: 8.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658755925 59 KDVVLSSAVHGNETAPIEICDELIKTiikgeLALNQR----VLFIFGNPKSINIGLRFVEENLNRLFNgHHTVEGVPMND 134
Cdd:cd06909 1 KRVAIVGGTHGNELTGVYLVKHWLKN-----PELIERksfeVHPLLANPRAVEQCRRYIDTDLNRCFS-LENLSSAPSSL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658755925 135 --ERKRAAKLEEYVtdfftrGEQGSARYHY--DLHTA---------IRGSKNEKFAVYPYLhgkpwkksQLQFLlscGVN 201
Cdd:cd06909 75 pyEVRRAREINQIL------GPKGNPACDFiiDLHNTtsnmgitliLSSSDDFTLKLAAYL--------QQRLP---PVR 137
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 658755925 202 tVLMMKSPATTFSYY-SSFVHGadsFTVELGQVkPFGENDMARFAKTKQTLTALI 255
Cdd:cd06909 138 -VLLHESPSKESPFLrSVAKHG---FTIEVGPV-PQGVLRADIFEQTRKLVKAIL 187
|
|
| |
