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Conserved domains on  [gi|1952200691|ref|WP_199529101|]
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succinylglutamate desuccinylase [Pseudoalteromonas sp. bablab_jr010]

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

 Zoom to residue level

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List of domain hits

 Name Accession Description Interval E-value
PRK05324 PRK05324
succinylglutamate desuccinylase; Provisional
 16-344 3.90e-171

succinylglutamate desuccinylase; Provisional


:

Pssm-ID: 235408  Cd Length: 329  Bit Score: 478.91  E-value: 3.90e-171
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200691  16 GDFLTLTRNNEFSLEPcAFTLENGTDVTVHDTGIIEFQPAQQTNKDIVLSSAVHGNETAPIEICDQLIKSIVTEQLTLQQ 95
Cdd:PRK05324    5 DDFLALTLAGHPPAVT-EFGLGNGVRWRWLGEGVLELTPAAPSTKALVLSAGIHGNETAPIELLDQLVRDLLAGELPLRA 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200691  96 RVLFIYGNPKSINIGKRFVDENLNRLFNG-HHTVEGIasnPERVRAKLLEDVVTDFFArGNQDSERFHYDLHTAIRGSKN 174
Cdd:PRK05324   84 RLLVILGNPPAMRAGKRYLDEDLNRLFGGrHQQFPGS---DEARRAAELEQAVEDFFA-AGAERVRWHYDLHTAIRGSKH 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200691 175 EKFAVYPFlHGKPWKKSQLQFLLSCGVNTVLMMKSAATTFSYYSSFVHGADSFTVELGQVKPFGENDMSRFEKTKQTLIA 254
Cdd:PRK05324  160 EQFAVLPQ-RGRPWSREQLAWLGAAGIEAVLLHNAPGGTFSHFSSEHFGALACTLELGKVLPFGQNDLSRFAATDQALRA 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200691 255 LISQKyvEYKEFNAEDFELFSVYRTINRTCEDFSFPFADDVENFTGFAKGELMATDGQTRYEAEVDGEAIIFPNADVALG 334
Cdd:PRK05324  239 LISGE--ELPERSADPPRLYRVVRQITKHSDDFELHFADDVENFTAFPKGTLLAEDGDERYVVEHDGERIVFPNPNVAIG 316

                         330
                  ....*....|
gi 1952200691 335 QRALLTVIPM 344
Cdd:PRK05324  317 LRAGLMLVPT 326
 
Name Accession Description Interval E-value
PRK05324 PRK05324
succinylglutamate desuccinylase; Provisional
 16-344 3.90e-171

succinylglutamate desuccinylase; Provisional


Pssm-ID: 235408  Cd Length: 329  Bit Score: 478.91  E-value: 3.90e-171
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200691  16 GDFLTLTRNNEFSLEPcAFTLENGTDVTVHDTGIIEFQPAQQTNKDIVLSSAVHGNETAPIEICDQLIKSIVTEQLTLQQ 95
Cdd:PRK05324    5 DDFLALTLAGHPPAVT-EFGLGNGVRWRWLGEGVLELTPAAPSTKALVLSAGIHGNETAPIELLDQLVRDLLAGELPLRA 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200691  96 RVLFIYGNPKSINIGKRFVDENLNRLFNG-HHTVEGIasnPERVRAKLLEDVVTDFFArGNQDSERFHYDLHTAIRGSKN 174
Cdd:PRK05324   84 RLLVILGNPPAMRAGKRYLDEDLNRLFGGrHQQFPGS---DEARRAAELEQAVEDFFA-AGAERVRWHYDLHTAIRGSKH 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200691 175 EKFAVYPFlHGKPWKKSQLQFLLSCGVNTVLMMKSAATTFSYYSSFVHGADSFTVELGQVKPFGENDMSRFEKTKQTLIA 254
Cdd:PRK05324  160 EQFAVLPQ-RGRPWSREQLAWLGAAGIEAVLLHNAPGGTFSHFSSEHFGALACTLELGKVLPFGQNDLSRFAATDQALRA 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200691 255 LISQKyvEYKEFNAEDFELFSVYRTINRTCEDFSFPFADDVENFTGFAKGELMATDGQTRYEAEVDGEAIIFPNADVALG 334
Cdd:PRK05324  239 LISGE--ELPERSADPPRLYRVVRQITKHSDDFELHFADDVENFTAFPKGTLLAEDGDERYVVEHDGERIVFPNPNVAIG 316

                         330
                  ....*....|
gi 1952200691 335 QRALLTVIPM 344
Cdd:PRK05324  317 LRAGLMLVPT 326
AstE COG2988
Succinylglutamate desuccinylase [Amino acid transport and metabolism];
17-347 5.66e-137

Succinylglutamate desuccinylase [Amino acid transport and metabolism];


Pssm-ID: 442227  Cd Length: 305  Bit Score: 391.52  E-value: 5.66e-137
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200691  17 DFLTLTRnnefslepcaftlengtdvtVHDTGIIEFQPAQQTNKDIVLSSAVHGNETAPIEICDQLIKSIVTEQLTLQQR 96
Cdd:COG2988     2 DFLALTR--------------------WLDEGVLELTPHAPGIKAVVISGGIHGNETAPIELLDKLLQDLLLGERPLSFR 61

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200691  97 VLFIYGNPKSINIGKRFVDENLNRLFNGHHTVEgiASNPERVRAKLLEDVVTDFFARGNQdsERFHYDLHTAIRGSKNEK 176
Cdd:COG2988    62 LLLILGNPAAMRAGRRYLDEDLNRLFGGRHLQN--PESYEAARAKELEQAVGPFFAAGGR--VRLHIDLHTAIRNSGHER 137

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200691 177 FAVYPFlHGKPWKKSQLQFLLSCGVNTVLMMKSAATTFSYYSSFVHGADSFTVELGQVKPFGENDMSRFEKTKQTLIALI 256
Cdd:COG2988   138 FAVYPF-RGRPFDLALLAYLAAAGPEAVVLHHAPGGTFSHFSAELCGAQAFTLELGKVRPFGQNDLSRFAATEEALRALL 216

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200691 257 SqkYVEYKEFNAEDFELFSVYRTINRTCEDFSFPFADDVENFTGFAKGELMATDGQTRYEAEVDGEAIIFPNADVALGQR 336
Cdd:COG2988   217 S--GAELPEHPAQDLDLYRVVQQIIKHGDDFMLHPDLDTLNFTPLPPGTLLAEDGGKEYRVEGDEERIVFPNEAVYYGQR 294

                         330
                  ....*....|.
gi 1952200691 337 ALLTVIPMQVD 347
Cdd:COG2988   295 AALLLTPKELI 305
M14_ASTE cd03855
Peptidase M14 Succinylglutamate desuccinylase (ASTE) subfamily; Peptidase M14 ...
 17-258 4.45e-129

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: 368.84  E-value: 4.45e-129
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200691  17 DFLTLTRNNEFSLE-PCAFtLENGTDVTVHDTGIIEFQPAQQTNKDIVLSSAVHGNETAPIEICDQLIKSIVTEQLTLQQ 95
Cdd:cd03855     1 DFLALTLSGSEPAEgELAA-VSNGTRVRWLATGVLELTPAASASKSVVLSAGIHGNETAPIEILDQLINDLIRGELALAH 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200691  96 RVLFIYGNPKSINIGKRFVDENLNRLFNGHHTVegIASNPERVRAKLLEDVVTDFFARGnQDSERFHYDLHTAIRGSKNE 175
Cdd:cd03855    80 RLLFIFGNPPAIRQGKRFIEENLNRLFSGRHSK--LPPSYETARAAELEQAVADFFAKA-SGEVRWHLDLHTAIRGSKHE 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200691 176 KFAVYPFLHGKPWKKSQLQFLLSCGVNTVLMMKSAATTFSYYSSFVHGADSFTVELGQVKPFGENDMSRFEKTKQTLIAL 255
Cdd:cd03855   157 QFAVYPFLEGRPHDREQLDFLGAAGIEAVLLSNSPGGTFSYYSSEHFGAAAFTVELGKVRPFGQNDLSQFAAIDQALRAL 236


                  ...
gi 1952200691 256 ISQ 258
Cdd:cd03855   237 ISG 239
arg_catab_astE TIGR03242
succinylglutamate desuccinylase; Members of this protein family are succinylglutamate ...
 17-342 6.55e-116

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: 338.57  E-value: 6.55e-116
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200691  17 DFLTLTRNNEFSlepcafTLENGTDVTVH----DTGIIEFQPAQQTNKDIVLSSAVHGNETAPIEICDQLIKSIVTEQLT 92
Cdd:TIGR03242   1 DFLALTLTGKKP------HVTQGETNNVRwrwlGEGVLELTPHAPPQKSLVISAGIHGNETAPIEILEQLLGDIAAGKLP 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200691  93 LQQRVLFIYGNPKSINIGKRFVDENLNRLFNGHHtvEGIASNPERVRAKLLEDVVTDFFARGNQDSERFHYDLHTAIRGS 172
Cdd:TIGR03242  75 LRVRLLVILGNPPAMRTGKRYLHDDLNRMFGGRY--QQLAPSFETCRAAELEQCVEDFFSQGGRSVARWHYDLHTAIRGS 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200691 173 KNEKFAVYPFLhGKPWKKSQLQFLLSCGVNTVLMMKSAATTFSYYSSFVHGADSFTVELGQVKPFGENDMSRFEKTKQTL 252
Cdd:TIGR03242 153 LHEQFALLPYQ-GRPWDREFLTWLGAAGLDALVFHTEPGGTFSHFSSEHFGALACTLELGKALPFGQNDLSQFAAITSAL 231

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200691 253 IALISQKYVEYKEFnaEDFELFSVYRTINRTCEDFSFPFADDVENFTGFAKGELMATDGQTRYEAEVDGEAIIFPNADVA 332
Cdd:TIGR03242 232 RALISDEAIPARRT--DPLRLFRVVSSITKHSDSFELHVASDTLNFTPFPKGTLLATDGNERYRVTHEGERILFPNPNVA 309

                         330
                  ....*....|
gi 1952200691 333 LGQRALLTVI 342
Cdd:TIGR03242 310 NGLRAGLMLV 319
AstE_AspA pfam04952
Succinylglutamate desuccinylase / Aspartoacylase family; This family includes ...
 60-345 1.20e-60

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: 196.42  E-value: 1.20e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200691  60 KDIVLSSAVHGNETAPIEICDQLIKSIVTEQLtLQQRVLFIYGNPKSINIGKRFVDENLNRLFNGHHtvEGiASNPERVR 139
Cdd:pfam04952   3 PTLLLSAGIHGNETNGVELLRRLLRQLDPGDI-AGERTLVPLANPPAFRAGSRYIPRDLNRSFPGRA--LG-ASSDEPYR 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200691 140 AKLLEDVVTDFFARGNQdSERFHYDLHTAIRGSKNEKFAVYPFlhgKPWKKSQLQFLLSCGVNTVLMMKSA-ATTFSYYS 218
Cdd:pfam04952  79 ATRAERLADLFFPALLP-RADIVLDLHTGTRGMGHLLFALAPI---RDDPLHLLALLRAFGAPAVLKLHSKpSAGFSAFS 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200691 219 SFVHGADSFTVELGQVKPFGENDMSRFEKTKQTLIALISQkyVEYKEFNAEDFELFSVYRTINRTCE---------DFSF 289
Cdd:pfam04952 155 AEELGAPGFTLELGGAGPFGANLISRTAAGVLNVLRLIGV--LNGGPDAFEPPKLYRVLREIDRPRDiraelaglvEFAL 232

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1952200691 290 PFADDVENFTGFAKGELMATDG--QTRYEAEVDGeAIIFPNADVALGQRALLTVIPMQ 345
Cdd:pfam04952 233 NLGDDVDAGPLLPGGPLFAPFGgeETEYRAPEDG-YPVFPNEAAYVGKGAALALVAKF 289
 
Name Accession Description Interval E-value
PRK05324 PRK05324
succinylglutamate desuccinylase; Provisional
 16-344 3.90e-171

succinylglutamate desuccinylase; Provisional


Pssm-ID: 235408  Cd Length: 329  Bit Score: 478.91  E-value: 3.90e-171
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200691  16 GDFLTLTRNNEFSLEPcAFTLENGTDVTVHDTGIIEFQPAQQTNKDIVLSSAVHGNETAPIEICDQLIKSIVTEQLTLQQ 95
Cdd:PRK05324    5 DDFLALTLAGHPPAVT-EFGLGNGVRWRWLGEGVLELTPAAPSTKALVLSAGIHGNETAPIELLDQLVRDLLAGELPLRA 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200691  96 RVLFIYGNPKSINIGKRFVDENLNRLFNG-HHTVEGIasnPERVRAKLLEDVVTDFFArGNQDSERFHYDLHTAIRGSKN 174
Cdd:PRK05324   84 RLLVILGNPPAMRAGKRYLDEDLNRLFGGrHQQFPGS---DEARRAAELEQAVEDFFA-AGAERVRWHYDLHTAIRGSKH 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200691 175 EKFAVYPFlHGKPWKKSQLQFLLSCGVNTVLMMKSAATTFSYYSSFVHGADSFTVELGQVKPFGENDMSRFEKTKQTLIA 254
Cdd:PRK05324  160 EQFAVLPQ-RGRPWSREQLAWLGAAGIEAVLLHNAPGGTFSHFSSEHFGALACTLELGKVLPFGQNDLSRFAATDQALRA 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200691 255 LISQKyvEYKEFNAEDFELFSVYRTINRTCEDFSFPFADDVENFTGFAKGELMATDGQTRYEAEVDGEAIIFPNADVALG 334
Cdd:PRK05324  239 LISGE--ELPERSADPPRLYRVVRQITKHSDDFELHFADDVENFTAFPKGTLLAEDGDERYVVEHDGERIVFPNPNVAIG 316

                         330
                  ....*....|
gi 1952200691 335 QRALLTVIPM 344
Cdd:PRK05324  317 LRAGLMLVPT 326
AstE COG2988
Succinylglutamate desuccinylase [Amino acid transport and metabolism];
17-347 5.66e-137

Succinylglutamate desuccinylase [Amino acid transport and metabolism];


Pssm-ID: 442227  Cd Length: 305  Bit Score: 391.52  E-value: 5.66e-137
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200691  17 DFLTLTRnnefslepcaftlengtdvtVHDTGIIEFQPAQQTNKDIVLSSAVHGNETAPIEICDQLIKSIVTEQLTLQQR 96
Cdd:COG2988     2 DFLALTR--------------------WLDEGVLELTPHAPGIKAVVISGGIHGNETAPIELLDKLLQDLLLGERPLSFR 61

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200691  97 VLFIYGNPKSINIGKRFVDENLNRLFNGHHTVEgiASNPERVRAKLLEDVVTDFFARGNQdsERFHYDLHTAIRGSKNEK 176
Cdd:COG2988    62 LLLILGNPAAMRAGRRYLDEDLNRLFGGRHLQN--PESYEAARAKELEQAVGPFFAAGGR--VRLHIDLHTAIRNSGHER 137

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200691 177 FAVYPFlHGKPWKKSQLQFLLSCGVNTVLMMKSAATTFSYYSSFVHGADSFTVELGQVKPFGENDMSRFEKTKQTLIALI 256
Cdd:COG2988   138 FAVYPF-RGRPFDLALLAYLAAAGPEAVVLHHAPGGTFSHFSAELCGAQAFTLELGKVRPFGQNDLSRFAATEEALRALL 216

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200691 257 SqkYVEYKEFNAEDFELFSVYRTINRTCEDFSFPFADDVENFTGFAKGELMATDGQTRYEAEVDGEAIIFPNADVALGQR 336
Cdd:COG2988   217 S--GAELPEHPAQDLDLYRVVQQIIKHGDDFMLHPDLDTLNFTPLPPGTLLAEDGGKEYRVEGDEERIVFPNEAVYYGQR 294

                         330
                  ....*....|.
gi 1952200691 337 ALLTVIPMQVD 347
Cdd:COG2988   295 AALLLTPKELI 305
M14_ASTE cd03855
Peptidase M14 Succinylglutamate desuccinylase (ASTE) subfamily; Peptidase M14 ...
 17-258 4.45e-129

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: 368.84  E-value: 4.45e-129
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200691  17 DFLTLTRNNEFSLE-PCAFtLENGTDVTVHDTGIIEFQPAQQTNKDIVLSSAVHGNETAPIEICDQLIKSIVTEQLTLQQ 95
Cdd:cd03855     1 DFLALTLSGSEPAEgELAA-VSNGTRVRWLATGVLELTPAASASKSVVLSAGIHGNETAPIEILDQLINDLIRGELALAH 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200691  96 RVLFIYGNPKSINIGKRFVDENLNRLFNGHHTVegIASNPERVRAKLLEDVVTDFFARGnQDSERFHYDLHTAIRGSKNE 175
Cdd:cd03855    80 RLLFIFGNPPAIRQGKRFIEENLNRLFSGRHSK--LPPSYETARAAELEQAVADFFAKA-SGEVRWHLDLHTAIRGSKHE 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200691 176 KFAVYPFLHGKPWKKSQLQFLLSCGVNTVLMMKSAATTFSYYSSFVHGADSFTVELGQVKPFGENDMSRFEKTKQTLIAL 255
Cdd:cd03855   157 QFAVYPFLEGRPHDREQLDFLGAAGIEAVLLSNSPGGTFSYYSSEHFGAAAFTVELGKVRPFGQNDLSQFAAIDQALRAL 236


                  ...
gi 1952200691 256 ISQ 258
Cdd:cd03855   237 ISG 239
arg_catab_astE TIGR03242
succinylglutamate desuccinylase; Members of this protein family are succinylglutamate ...
 17-342 6.55e-116

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: 338.57  E-value: 6.55e-116
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200691  17 DFLTLTRNNEFSlepcafTLENGTDVTVH----DTGIIEFQPAQQTNKDIVLSSAVHGNETAPIEICDQLIKSIVTEQLT 92
Cdd:TIGR03242   1 DFLALTLTGKKP------HVTQGETNNVRwrwlGEGVLELTPHAPPQKSLVISAGIHGNETAPIEILEQLLGDIAAGKLP 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200691  93 LQQRVLFIYGNPKSINIGKRFVDENLNRLFNGHHtvEGIASNPERVRAKLLEDVVTDFFARGNQDSERFHYDLHTAIRGS 172
Cdd:TIGR03242  75 LRVRLLVILGNPPAMRTGKRYLHDDLNRMFGGRY--QQLAPSFETCRAAELEQCVEDFFSQGGRSVARWHYDLHTAIRGS 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200691 173 KNEKFAVYPFLhGKPWKKSQLQFLLSCGVNTVLMMKSAATTFSYYSSFVHGADSFTVELGQVKPFGENDMSRFEKTKQTL 252
Cdd:TIGR03242 153 LHEQFALLPYQ-GRPWDREFLTWLGAAGLDALVFHTEPGGTFSHFSSEHFGALACTLELGKALPFGQNDLSQFAAITSAL 231

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200691 253 IALISQKYVEYKEFnaEDFELFSVYRTINRTCEDFSFPFADDVENFTGFAKGELMATDGQTRYEAEVDGEAIIFPNADVA 332
Cdd:TIGR03242 232 RALISDEAIPARRT--DPLRLFRVVSSITKHSDSFELHVASDTLNFTPFPKGTLLATDGNERYRVTHEGERILFPNPNVA 309

                         330
                  ....*....|
gi 1952200691 333 LGQRALLTVI 342
Cdd:TIGR03242 310 NGLRAGLMLV 319
AstE_AspA pfam04952
Succinylglutamate desuccinylase / Aspartoacylase family; This family includes ...
 60-345 1.20e-60

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: 196.42  E-value: 1.20e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200691  60 KDIVLSSAVHGNETAPIEICDQLIKSIVTEQLtLQQRVLFIYGNPKSINIGKRFVDENLNRLFNGHHtvEGiASNPERVR 139
Cdd:pfam04952   3 PTLLLSAGIHGNETNGVELLRRLLRQLDPGDI-AGERTLVPLANPPAFRAGSRYIPRDLNRSFPGRA--LG-ASSDEPYR 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200691 140 AKLLEDVVTDFFARGNQdSERFHYDLHTAIRGSKNEKFAVYPFlhgKPWKKSQLQFLLSCGVNTVLMMKSA-ATTFSYYS 218
Cdd:pfam04952  79 ATRAERLADLFFPALLP-RADIVLDLHTGTRGMGHLLFALAPI---RDDPLHLLALLRAFGAPAVLKLHSKpSAGFSAFS 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200691 219 SFVHGADSFTVELGQVKPFGENDMSRFEKTKQTLIALISQkyVEYKEFNAEDFELFSVYRTINRTCE---------DFSF 289
Cdd:pfam04952 155 AEELGAPGFTLELGGAGPFGANLISRTAAGVLNVLRLIGV--LNGGPDAFEPPKLYRVLREIDRPRDiraelaglvEFAL 232

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1952200691 290 PFADDVENFTGFAKGELMATDG--QTRYEAEVDGeAIIFPNADVALGQRALLTVIPMQ 345
Cdd:pfam04952 233 NLGDDVDAGPLLPGGPLFAPFGgeETEYRAPEDG-YPVFPNEAAYVGKGAALALVAKF 289
M14_ASTE_ASPA_like cd06230
Peptidase M14 Succinylglutamate desuccinylase (ASTE)/aspartoacylase (ASPA) subfamily; The ...
 62-233 5.52e-12

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: 63.48  E-value: 5.52e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200691  62 IVLSSAVHGNETAPIEICDQLIKSIVTEQL--TLqqrVLFIYGNPKSINIGKRFVDE---NLNRLFNGHH--TVEgiasn 134
Cdd:cd06230     1 LLILAGVHGDEYEGVEAIRRLLAELDPSELkgTV---VLVPVANPPAFEAGTRYTPLdglDLNRIFPGDPdgSPT----- 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200691 135 pERVRAKLLEDVVtdffargnqDSERFHYDLHTAIRGSKNEKFAVYPFLHGKPWKKSQLQFLLSCGV---NTVlmmkSAA 211
Cdd:cd06230    73 -ERLAHELTELIL---------KHADALIDLHSGGTGRLVPYAILDYDSDAREKSRELARAFGGTPViwgGDP----PGG 138

                         170       180
                  ....*....|....*....|..
gi 1952200691 212 TTFSYYSSfvHGADSFTVELGQ 233
Cdd:cd06230   139 TPVAAARS--AGIPAITVELGG 158
COG3608 COG3608
Predicted deacylase [General function prediction only];
62-233 6.94e-12

Predicted deacylase [General function prediction only];


Pssm-ID: 442826 [Multi-domain]  Cd Length: 296  Bit Score: 65.25  E-value: 6.94e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200691  62 IVLSSAVHGNETAPIEICDQLIKSIvtEQLTLQQRVLFI-YGNPKSINIGKRF---VDENLNRLFNGHHTvegiASNPER 137
Cdd:COG3608    29 LLITAGIHGDELNGIEALRRLLREL--DPGELRGTVILVpVANPPGFLQGSRYlpiDGRDLNRSFPGDAD----GSLAER 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200691 138 VRAKLLEDVVtdffargnqdsERFHY--DLHTAIRGSKNEKFAVYPFLHGKpwkksQLQFLLSCGVNTVLMMK-SAATTF 214
Cdd:COG3608   103 IAHALFEEIL-----------PDADYviDLHSGGIARDNLPHVRAGPGDEE-----LRALARAFGAPVILDSPeGGDGSL 166

                         170
                  ....*....|....*....
gi 1952200691 215 SYYSSfVHGADSFTVELGQ 233
Cdd:COG3608   167 REAAA-EAGIPALTLELGG 184
M14_ASTE_ASPA_like cd18430
Succinylglutamate desuccinylase/aspartoacylase; uncharacterized; A functionally ...
 67-125 1.39e-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: 56.30  E-value: 1.39e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1952200691  67 AVHGNETAPIEICDQLIKSIVTEQLTlQQRVLFIYGNPKSINIGKRFVDENLNRLFNGH 125
Cdd:cd18430     6 AVHGNETCGTRAVERLLAELPSGALQ-KGPVTLVPANERAYAEGVRFCEEDLNRVFPGD 63
Peptidase_M14_like cd00596
M14 family of metallocarboxypeptidases and related proteins; The M14 family of ...
 62-242 1.04e-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: 54.77  E-value: 1.04e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200691  62 IVLSSAVHGNETAPIEICDQLIKSIVTEQLT------LQQRVLFI------YGNPKSINIGKRF----VDenLNRLFNGH 125
Cdd:cd00596     1 ILITGGIHGNEVIGVELALALIEYLLENYGNdplkrlLDNVELWIvplvnpDGFARVIDSGGRKnangVD--LNRNFPYN 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200691 126 HTVEGI-------------ASNPErVRAklledvVTDFFARGNQDserFHYDLHTAIrgskneKFAVYPFLH----GKPW 188
Cdd:cd00596    79 WGKDGTsgpssptyrgpapFSEPE-TQA------LRDLAKSHRFD---LAVSYHSSS------EAILYPYGYtnepPPDF 142

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1952200691 189 --------KKSQLQFLLSCGVNTVLMMKSAATTFSYYSSFVHGADSFTVELGQVKPFGENDM 242
Cdd:cd00596   143 sefqelaaGLARALGAGEYGYGYSYTWYSTTGTADDWLYGELGILAFTVELGTADYPLPGTL 204
PRK02259 PRK02259
aspartoacylase; Provisional
 60-167 3.57e-08

aspartoacylase; Provisional


Pssm-ID: 235019  Cd Length: 288  Bit Score: 54.11  E-value: 3.57e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200691  60 KDIVLSSAVHGNETAPIEICDQLIKsivteQLTLQQR----VLFIYGNPKSINIGKRFVDENLNRLFnghhTVEGIASNP 135
Cdd:PRK02259    3 NRVAIVGGTHGNEITGIYLVKKWQQ-----QPNLINRkgleVQTVIGNPEAIEAGRRYIDRDLNRSF----RLDLLQNPD 73

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1952200691 136 ----ERVRAKLLedvvTDFFARGNQDSERFHYDLHT 167
Cdd:PRK02259   74 lsgyEQLRAKEL----VQQLGPKGNSPCDFIIDLHS 105
M14_ASTE_ASPA-like cd06254
Peptidase M14 Succinylglutamate desuccinylase (ASTE)/aspartoacylase (ASPA)-like; ...
 56-233 7.74e-08

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: 51.81  E-value: 7.74e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200691  56 QQTNKDIVLSSAVHGNETAPIEICDQLIKSIVTEQLtlQQRVLFI--------YGNPKSINigkrFVDE-NLNRLFNGHh 126
Cdd:cd06254     8 AKPGPTLLITAGIHGGEYPGILAAIRLARELDPADV--KGTLIIVhianvsgfEARTPFVV----PEDGkNLNRVFPGD- 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200691 127 tVEGIASnpERVRAKLledvVTDFFARGNqdserFHYDLHTairGSKNEK---FAVYPFLHGKPWKKSQLQFLLSCGVnT 203
Cdd:cd06254    81 -PDGTLT--ERIAYFL----TREIISRAD-----FLIDLHG---GDANEAltpFVYYPGGASEEVNDISRAAAQALGL-P 144

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1952200691 204 VLMMKSAATTFSYYSSFVH-GADSFTVELGQ 233
Cdd:cd06254   145 YIVISSSEKGTGYYSYAALrGIPSILVERGG 175
M14_ASTE_ASPA-like cd06251
Peptidase M14 Succinylglutamate desuccinylase (ASTE)/aspartoacylase (ASPA)-like; ...
 62-174 9.76e-07

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: 48.69  E-value: 9.76e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200691  62 IVLSSAVHGNETAPIEICDQLIKSIVTEQL--TLqqrVLFIYGNPKSINIGKRFV---DENLNRLFNGHHTvegiASNPE 136
Cdd:cd06251    15 LLLTAAIHGDELNGIEVIQRLLEDLDPSKLrgTL---IAIPVVNPLGFENNSRYLpddGRDLNRSFPGSEK----GSLAS 87

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1952200691 137 RVRAKLLEDVVTDFfargnqDserFHYDLHTAIRGSKN 174
Cdd:cd06251    88 RLAHLLWNEIVKKA------D---YVIDLHTASTGRTN 116
M14_ASTE_ASPA-like cd06253
Peptidase M14 Succinylglutamate desuccinylase (ASTE)/aspartoacylase (ASPA)-like; ...
 62-146 2.54e-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: 44.51  E-value: 2.54e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200691  62 IVlsSAVHGNETAPIEICDQLIKSIvteqLTLQQRVLFIYG--------NPKSINIGKRFV---DENLNRLFNGhhTVEG 130
Cdd:cd06253    27 IV--AGIHGDELNGLYVCSRLIRFL----KELEEGGYKLKGkvlvipavNPLGINSGTRFWpfdNLDMNRMFPG--YNKG 98

                          90
                  ....*....|....*.
gi 1952200691 131 iaSNPERVRAKLLEDV 146
Cdd:cd06253    99 --ETTERIAAALFEDL 112
M14_ASTE_ASPA_like cd18174
Peptidase M14 Succinylglutamate desuccinylase (ASTE)/aspartoacylase (ASPA)-like; ...
 64-244 3.75e-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: 349484  Cd Length: 187  Bit Score: 43.77  E-value: 3.75e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200691  64 LSSAVHGNETAPIEICDQLIKSIVTEQLT-------------LQQRVlfIYGNPksinigkrfVD-ENLNRLFNGHhtVE 129
Cdd:cd18174     3 VTAGVHGYEYASIEALQRLIKELDPAKLSgtvivvpianipaFEGRS--IYVNP---------LDgKNLNRSFPGD--PD 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200691 130 GiaSNPERVRAKLLEDVVT--DFFArgnqdserfhyDLHTairGSKNEK---FAVYPFLHGKPWKKSQLQFLLSCGVNTV 204
Cdd:cd18174    70 G--TPTERLAHWLTTNVIAraDYYI-----------DLHG---GDLNEDlrpFVYYYETGNAALDAASREMAEAFGLDHI 133

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1952200691 205 LM-----MKSAATTFSYYSSFVHGADSFTVELGQVKPFGENDMSR 244
Cdd:cd18174   134 VFykarlKASRGSLYTQAAALLRGIPAILVEAGGLGSRDEEDVAR 178
M14_ASPA cd06909
Peptidase M14 Aspartoacylase (ASPA) subfamily; Aspartoacylase (ASPA) belongs to the ...
 60-167 5.88e-05

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: 43.35  E-value: 5.88e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200691  60 KDIVLSSAVHGNETAPIEICDQLIKsivteQLTLQQR----VLFIYGNPKSINIGKRFVDENLNRLFnghhTVEGIASNP 135
Cdd:cd06909     1 KRVAIVGGTHGNELTGVYLVKHWLK-----NPELIERksfeVHPLLANPRAVEQCRRYIDTDLNRCF----SLENLSSAP 71

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1952200691 136 -----ERVRAKLLEDVVtdffarGNQDSERFHY--DLHT 167
Cdd:cd06909    72 sslpyEVRRAREINQIL------GPKGNPACDFiiDLHN 104
M14_ASTE_ASPA-like cd06910
Peptidase M14 Succinylglutamate desuccinylase (ASTE)/aspartoacylase (ASPA)-like; ...
 61-181 3.39e-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: 3.39e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952200691  61 DIVLSSAVHGNETAPIEICDQLIKSIVTeqlTLQQRVLFIYGNPKSIN-------IGKRFVDENLNRLFnGHHTVEGIAS 133
Cdd:cd06910    26 HVMINALTHGNEICGAIALDWLLKNGVR---PLRGRLTFCFANVEAYErfdparpTASRFVDEDLNRVW-GPELLDGPEQ 101

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1952200691 134 NPERVRAKLLEDVVtdffargnqDSERFHYDLHTAirGSKNEKFAVYP 181
Cdd:cd06910   102 SIELRRARELRPVV---------DTVDYLLDIHSM--QEKVPPLALAG 138
 
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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