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Conserved domains on  [gi|1539368163|emb|VEA38689|]
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succinylglutamate desuccinylase [Salmonella enterica subsp. enterica]

Protein Classification

succinylglutamate desuccinylase( domain architecture ID 10012321)

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

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

Graphical summary

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List of domain hits

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

succinylglutamate desuccinylase; Provisional


:

Pssm-ID: 235408  Cd Length: 329  Bit Score: 545.16  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539368163   1 MDNFLALTLSGTTPRV-TQGKGAGFRWRWLGHGLLEFTPDAPVDRALILSAGIHGNETAPVEMLDKLLSALFSGSLMLTW 79
Cdd:PRK05324    4 MDDFLALTLAGHPPAVtEFGLGNGVRWRWLGEGVLELTPAAPSTKALVLSAGIHGNETAPIELLDQLVRDLLAGELPLRA 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539368163  80 RVLVVLGNPQALAAGIRYCHSDMNRMFGGRWQSFAESDETRRARELELSLETFFSSGQARVRWHLDLHTAIRGSHHLRFG 159
Cdd:PRK05324   84 RLLVILGNPPAMRAGKRYLDEDLNRLFGGRHQQFPGSDEARRAAELEQAVEDFFAAGAERVRWHYDLHTAIRGSKHEQFA 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539368163 160 VLPQRDRPWEADFLAWLGAAGLEALVFHQAPGGTFTHFSSEHFGALSCTLELGKALPFGQNDLTQFSITSQALSALLSGV 239
Cdd:PRK05324  164 VLPQRGRPWSREQLAWLGAAGIEAVLLHNAPGGTFSHFSSEHFGALACTLELGKVLPFGQNDLSRFAATDQALRALISGE 243

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539368163 240 E-TSTSSSPPLRYRVVSQITRHSDKFALYMDAQTLNFTAFAKGTLLAEEGDKRVTVTHDVEYVLFPNPSVACGLRAGLML 318
Cdd:PRK05324  244 ElPERSADPPRLYRVVRQITKHSDDFELHFADDVENFTAFPKGTLLAEDGDERYVVEHDGERIVFPNPNVAIGLRAGLML 323


                  ....
gi 1539368163 319 ERLP 322
Cdd:PRK05324  324 VPTT 327
 
Name Accession Description Interval E-value
PRK05324 PRK05324
succinylglutamate desuccinylase; Provisional
 1-322 0e+00

succinylglutamate desuccinylase; Provisional


Pssm-ID: 235408  Cd Length: 329  Bit Score: 545.16  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539368163   1 MDNFLALTLSGTTPRV-TQGKGAGFRWRWLGHGLLEFTPDAPVDRALILSAGIHGNETAPVEMLDKLLSALFSGSLMLTW 79
Cdd:PRK05324    4 MDDFLALTLAGHPPAVtEFGLGNGVRWRWLGEGVLELTPAAPSTKALVLSAGIHGNETAPIELLDQLVRDLLAGELPLRA 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539368163  80 RVLVVLGNPQALAAGIRYCHSDMNRMFGGRWQSFAESDETRRARELELSLETFFSSGQARVRWHLDLHTAIRGSHHLRFG 159
Cdd:PRK05324   84 RLLVILGNPPAMRAGKRYLDEDLNRLFGGRHQQFPGSDEARRAAELEQAVEDFFAAGAERVRWHYDLHTAIRGSKHEQFA 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539368163 160 VLPQRDRPWEADFLAWLGAAGLEALVFHQAPGGTFTHFSSEHFGALSCTLELGKALPFGQNDLTQFSITSQALSALLSGV 239
Cdd:PRK05324  164 VLPQRGRPWSREQLAWLGAAGIEAVLLHNAPGGTFSHFSSEHFGALACTLELGKVLPFGQNDLSRFAATDQALRALISGE 243

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539368163 240 E-TSTSSSPPLRYRVVSQITRHSDKFALYMDAQTLNFTAFAKGTLLAEEGDKRVTVTHDVEYVLFPNPSVACGLRAGLML 318
Cdd:PRK05324  244 ElPERSADPPRLYRVVRQITKHSDDFELHFADDVENFTAFPKGTLLAEDGDERYVVEHDGERIVFPNPNVAIGLRAGLML 323


                  ....
gi 1539368163 319 ERLP 322
Cdd:PRK05324  324 VPTT 327
arg_catab_astE TIGR03242
succinylglutamate desuccinylase; Members of this protein family are succinylglutamate ...
 3-319 1.64e-165

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: 462.99  E-value: 1.64e-165
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539368163   3 NFLALTLSGTTPRVTQGKGAGFRWRWLGHGLLEFTPDAPVDRALILSAGIHGNETAPVEMLDKLLSALFSGSLMLTWRVL 82
Cdd:TIGR03242   1 DFLALTLTGKKPHVTQGETNNVRWRWLGEGVLELTPHAPPQKSLVISAGIHGNETAPIEILEQLLGDIAAGKLPLRVRLL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539368163  83 VVLGNPQALAAGIRYCHSDMNRMFGGRWQSFAESDETRRARELELSLETFFS-SGQARVRWHLDLHTAIRGSHHLRFGVL 161
Cdd:TIGR03242  81 VILGNPPAMRTGKRYLHDDLNRMFGGRYQQLAPSFETCRAAELEQCVEDFFSqGGRSVARWHYDLHTAIRGSLHEQFALL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539368163 162 PQRDRPWEADFLAWLGAAGLEALVFHQAPGGTFTHFSSEHFGALSCTLELGKALPFGQNDLTQFSITSQALSALLSGVET 241
Cdd:TIGR03242 161 PYQGRPWDREFLTWLGAAGLDALVFHTEPGGTFSHFSSEHFGALACTLELGKALPFGQNDLSQFAAITSALRALISDEAI 240

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1539368163 242 STSSSPPLR-YRVVSQITRHSDKFALYMDAQTLNFTAFAKGTLLAEEGDKRVTVTHDVEYVLFPNPSVACGLRAGLMLE 319
Cdd:TIGR03242 241 PARRTDPLRlFRVVSSITKHSDSFELHVASDTLNFTPFPKGTLLATDGNERYRVTHEGERILFPNPNVANGLRAGLMLV 319
AstE COG2988
Succinylglutamate desuccinylase [Amino acid transport and metabolism];
27-322 2.10e-155

Succinylglutamate desuccinylase [Amino acid transport and metabolism];


Pssm-ID: 442227  Cd Length: 305  Bit Score: 436.97  E-value: 2.10e-155
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539368163  27 RWLGHGLLEFTPDAPVDRALILSAGIHGNETAPVEMLDKLLSALFSGSLMLTWRVLVVLGNPQALAAGIRYCHSDMNRMF 106
Cdd:COG2988     8 RWLDEGVLELTPHAPGIKAVVISGGIHGNETAPIELLDKLLQDLLLGERPLSFRLLLILGNPAAMRAGRRYLDEDLNRLF 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539368163 107 GGRWQSFAESDETRRARELELSLETFFSSGQaRVRWHLDLHTAIRGSHHLRFGVLPQRDRPWEADFLAWLGAAGLEALVF 186
Cdd:COG2988    88 GGRHLQNPESYEAARAKELEQAVGPFFAAGG-RVRLHIDLHTAIRNSGHERFAVYPFRGRPFDLALLAYLAAAGPEAVVL 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539368163 187 HQAPGGTFTHFSSEHFGALSCTLELGKALPFGQNDLTQFSITSQALSALLSGVETSTSSSPPLR-YRVVSQITRHSDKFA 265
Cdd:COG2988   167 HHAPGGTFSHFSAELCGAQAFTLELGKVRPFGQNDLSRFAATEEALRALLSGAELPEHPAQDLDlYRVVQQIIKHGDDFM 246

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1539368163 266 LYMDAQTLNFTAFAKGTLLAEEGDKRVTVTHDVEYVLFPNPSVACGLRAGLMLERLP 322
Cdd:COG2988   247 LHPDLDTLNFTPLPPGTLLAEDGGKEYRVEGDEERIVFPNEAVYYGQRAALLLTPKE 303
M14_ASTE cd03855
Peptidase M14 Succinylglutamate desuccinylase (ASTE) subfamily; Peptidase M14 ...
 3-238 5.50e-126

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: 359.98  E-value: 5.50e-126
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539368163   3 NFLALTLSGTTPRVTQG--KGAGFRWRWLGHGLLEFTPDAPVDRALILSAGIHGNETAPVEMLDKLLSALFSGSLMLTWR 80
Cdd:cd03855     1 DFLALTLSGSEPAEGELaaVSNGTRVRWLATGVLELTPAASASKSVVLSAGIHGNETAPIEILDQLINDLIRGELALAHR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539368163  81 VLVVLGNPQALAAGIRYCHSDMNRMFGGRWQSFAESDETRRARELELSLETFFSSGQARVRWHLDLHTAIRGSHHLRFGV 160
Cdd:cd03855    81 LLFIFGNPPAIRQGKRFIEENLNRLFSGRHSKLPPSYETARAAELEQAVADFFAKASGEVRWHLDLHTAIRGSKHEQFAV 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1539368163 161 LPQRD-RPWEADFLAWLGAAGLEALVFHQAPGGTFTHFSSEHFGALSCTLELGKALPFGQNDLTQFSITSQALSALLSG 238
Cdd:cd03855   161 YPFLEgRPHDREQLDFLGAAGIEAVLLSNSPGGTFSYYSSEHFGAAAFTVELGKVRPFGQNDLSQFAAIDQALRALISG 239
AstE_AspA pfam04952
Succinylglutamate desuccinylase / Aspartoacylase family; This family includes ...
 44-318 6.67e-93

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


Pssm-ID: 428216 [Multi-domain]  Cd Length: 289  Bit Score: 277.69  E-value: 6.67e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539368163  44 RALILSAGIHGNETAPVEMLDKLLSALFSGSLmLTWRVLVVLGNPQALAAGIRYCHSDMNRMFGGRWQSfAESDETRRAR 123
Cdd:pfam04952   3 PTLLLSAGIHGNETNGVELLRRLLRQLDPGDI-AGERTLVPLANPPAFRAGSRYIPRDLNRSFPGRALG-ASSDEPYRAT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539368163 124 ELELSLETFFSSGQARVRWHLDLHTAIRGSHHLRFGVLPQRDRPWeaDFLAWLGAAGLEALV-FHQAPGGTFTHFSSEHF 202
Cdd:pfam04952  81 RAERLADLFFPALLPRADIVLDLHTGTRGMGHLLFALAPIRDDPL--HLLALLRAFGAPAVLkLHSKPSAGFSAFSAEEL 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539368163 203 GALSCTLELGKALPFGQNDLTQFSITSQALSALLSGVETST-SSSPPLRYRVVSQITRHSD---------KFALYMDAQT 272
Cdd:pfam04952 159 GAPGFTLELGGAGPFGANLISRTAAGVLNVLRLIGVLNGGPdAFEPPKLYRVLREIDRPRDiraelaglvEFALNLGDDV 238

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 1539368163 273 LNFTAFAKGTLLAEE-GDKRVTVTHDVEYVLFPNPSVACGLRAGLML 318
Cdd:pfam04952 239 DAGPLLPGGPLFAPFgGEETEYRAPEDGYPVFPNEAAYVGKGAALAL 285
 
Name Accession Description Interval E-value
PRK05324 PRK05324
succinylglutamate desuccinylase; Provisional
 1-322 0e+00

succinylglutamate desuccinylase; Provisional


Pssm-ID: 235408  Cd Length: 329  Bit Score: 545.16  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539368163   1 MDNFLALTLSGTTPRV-TQGKGAGFRWRWLGHGLLEFTPDAPVDRALILSAGIHGNETAPVEMLDKLLSALFSGSLMLTW 79
Cdd:PRK05324    4 MDDFLALTLAGHPPAVtEFGLGNGVRWRWLGEGVLELTPAAPSTKALVLSAGIHGNETAPIELLDQLVRDLLAGELPLRA 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539368163  80 RVLVVLGNPQALAAGIRYCHSDMNRMFGGRWQSFAESDETRRARELELSLETFFSSGQARVRWHLDLHTAIRGSHHLRFG 159
Cdd:PRK05324   84 RLLVILGNPPAMRAGKRYLDEDLNRLFGGRHQQFPGSDEARRAAELEQAVEDFFAAGAERVRWHYDLHTAIRGSKHEQFA 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539368163 160 VLPQRDRPWEADFLAWLGAAGLEALVFHQAPGGTFTHFSSEHFGALSCTLELGKALPFGQNDLTQFSITSQALSALLSGV 239
Cdd:PRK05324  164 VLPQRGRPWSREQLAWLGAAGIEAVLLHNAPGGTFSHFSSEHFGALACTLELGKVLPFGQNDLSRFAATDQALRALISGE 243

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539368163 240 E-TSTSSSPPLRYRVVSQITRHSDKFALYMDAQTLNFTAFAKGTLLAEEGDKRVTVTHDVEYVLFPNPSVACGLRAGLML 318
Cdd:PRK05324  244 ElPERSADPPRLYRVVRQITKHSDDFELHFADDVENFTAFPKGTLLAEDGDERYVVEHDGERIVFPNPNVAIGLRAGLML 323


                  ....
gi 1539368163 319 ERLP 322
Cdd:PRK05324  324 VPTT 327
arg_catab_astE TIGR03242
succinylglutamate desuccinylase; Members of this protein family are succinylglutamate ...
 3-319 1.64e-165

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: 462.99  E-value: 1.64e-165
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539368163   3 NFLALTLSGTTPRVTQGKGAGFRWRWLGHGLLEFTPDAPVDRALILSAGIHGNETAPVEMLDKLLSALFSGSLMLTWRVL 82
Cdd:TIGR03242   1 DFLALTLTGKKPHVTQGETNNVRWRWLGEGVLELTPHAPPQKSLVISAGIHGNETAPIEILEQLLGDIAAGKLPLRVRLL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539368163  83 VVLGNPQALAAGIRYCHSDMNRMFGGRWQSFAESDETRRARELELSLETFFS-SGQARVRWHLDLHTAIRGSHHLRFGVL 161
Cdd:TIGR03242  81 VILGNPPAMRTGKRYLHDDLNRMFGGRYQQLAPSFETCRAAELEQCVEDFFSqGGRSVARWHYDLHTAIRGSLHEQFALL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539368163 162 PQRDRPWEADFLAWLGAAGLEALVFHQAPGGTFTHFSSEHFGALSCTLELGKALPFGQNDLTQFSITSQALSALLSGVET 241
Cdd:TIGR03242 161 PYQGRPWDREFLTWLGAAGLDALVFHTEPGGTFSHFSSEHFGALACTLELGKALPFGQNDLSQFAAITSALRALISDEAI 240

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1539368163 242 STSSSPPLR-YRVVSQITRHSDKFALYMDAQTLNFTAFAKGTLLAEEGDKRVTVTHDVEYVLFPNPSVACGLRAGLMLE 319
Cdd:TIGR03242 241 PARRTDPLRlFRVVSSITKHSDSFELHVASDTLNFTPFPKGTLLATDGNERYRVTHEGERILFPNPNVANGLRAGLMLV 319
AstE COG2988
Succinylglutamate desuccinylase [Amino acid transport and metabolism];
27-322 2.10e-155

Succinylglutamate desuccinylase [Amino acid transport and metabolism];


Pssm-ID: 442227  Cd Length: 305  Bit Score: 436.97  E-value: 2.10e-155
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539368163  27 RWLGHGLLEFTPDAPVDRALILSAGIHGNETAPVEMLDKLLSALFSGSLMLTWRVLVVLGNPQALAAGIRYCHSDMNRMF 106
Cdd:COG2988     8 RWLDEGVLELTPHAPGIKAVVISGGIHGNETAPIELLDKLLQDLLLGERPLSFRLLLILGNPAAMRAGRRYLDEDLNRLF 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539368163 107 GGRWQSFAESDETRRARELELSLETFFSSGQaRVRWHLDLHTAIRGSHHLRFGVLPQRDRPWEADFLAWLGAAGLEALVF 186
Cdd:COG2988    88 GGRHLQNPESYEAARAKELEQAVGPFFAAGG-RVRLHIDLHTAIRNSGHERFAVYPFRGRPFDLALLAYLAAAGPEAVVL 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539368163 187 HQAPGGTFTHFSSEHFGALSCTLELGKALPFGQNDLTQFSITSQALSALLSGVETSTSSSPPLR-YRVVSQITRHSDKFA 265
Cdd:COG2988   167 HHAPGGTFSHFSAELCGAQAFTLELGKVRPFGQNDLSRFAATEEALRALLSGAELPEHPAQDLDlYRVVQQIIKHGDDFM 246

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1539368163 266 LYMDAQTLNFTAFAKGTLLAEEGDKRVTVTHDVEYVLFPNPSVACGLRAGLMLERLP 322
Cdd:COG2988   247 LHPDLDTLNFTPLPPGTLLAEDGGKEYRVEGDEERIVFPNEAVYYGQRAALLLTPKE 303
M14_ASTE cd03855
Peptidase M14 Succinylglutamate desuccinylase (ASTE) subfamily; Peptidase M14 ...
 3-238 5.50e-126

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: 359.98  E-value: 5.50e-126
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539368163   3 NFLALTLSGTTPRVTQG--KGAGFRWRWLGHGLLEFTPDAPVDRALILSAGIHGNETAPVEMLDKLLSALFSGSLMLTWR 80
Cdd:cd03855     1 DFLALTLSGSEPAEGELaaVSNGTRVRWLATGVLELTPAASASKSVVLSAGIHGNETAPIEILDQLINDLIRGELALAHR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539368163  81 VLVVLGNPQALAAGIRYCHSDMNRMFGGRWQSFAESDETRRARELELSLETFFSSGQARVRWHLDLHTAIRGSHHLRFGV 160
Cdd:cd03855    81 LLFIFGNPPAIRQGKRFIEENLNRLFSGRHSKLPPSYETARAAELEQAVADFFAKASGEVRWHLDLHTAIRGSKHEQFAV 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1539368163 161 LPQRD-RPWEADFLAWLGAAGLEALVFHQAPGGTFTHFSSEHFGALSCTLELGKALPFGQNDLTQFSITSQALSALLSG 238
Cdd:cd03855   161 YPFLEgRPHDREQLDFLGAAGIEAVLLSNSPGGTFSYYSSEHFGAAAFTVELGKVRPFGQNDLSQFAAIDQALRALISG 239
AstE_AspA pfam04952
Succinylglutamate desuccinylase / Aspartoacylase family; This family includes ...
 44-318 6.67e-93

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


Pssm-ID: 428216 [Multi-domain]  Cd Length: 289  Bit Score: 277.69  E-value: 6.67e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539368163  44 RALILSAGIHGNETAPVEMLDKLLSALFSGSLmLTWRVLVVLGNPQALAAGIRYCHSDMNRMFGGRWQSfAESDETRRAR 123
Cdd:pfam04952   3 PTLLLSAGIHGNETNGVELLRRLLRQLDPGDI-AGERTLVPLANPPAFRAGSRYIPRDLNRSFPGRALG-ASSDEPYRAT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539368163 124 ELELSLETFFSSGQARVRWHLDLHTAIRGSHHLRFGVLPQRDRPWeaDFLAWLGAAGLEALV-FHQAPGGTFTHFSSEHF 202
Cdd:pfam04952  81 RAERLADLFFPALLPRADIVLDLHTGTRGMGHLLFALAPIRDDPL--HLLALLRAFGAPAVLkLHSKPSAGFSAFSAEEL 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539368163 203 GALSCTLELGKALPFGQNDLTQFSITSQALSALLSGVETST-SSSPPLRYRVVSQITRHSD---------KFALYMDAQT 272
Cdd:pfam04952 159 GAPGFTLELGGAGPFGANLISRTAAGVLNVLRLIGVLNGGPdAFEPPKLYRVLREIDRPRDiraelaglvEFALNLGDDV 238

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 1539368163 273 LNFTAFAKGTLLAEE-GDKRVTVTHDVEYVLFPNPSVACGLRAGLML 318
Cdd:pfam04952 239 DAGPLLPGGPLFAPFgGEETEYRAPEDGYPVFPNEAAYVGKGAALAL 285
PRK02259 PRK02259
aspartoacylase; Provisional
 48-148 5.11e-14

aspartoacylase; Provisional


Pssm-ID: 235019  Cd Length: 288  Bit Score: 71.06  E-value: 5.11e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539368163  48 LSAGIHGNETAPVEMLDKL---LSALFSGSLmltwRVLVVLGNPQALAAGIRYCHSDMNRMFGGrwQSFAESD----ETR 120
Cdd:PRK02259    7 IVGGTHGNEITGIYLVKKWqqqPNLINRKGL----EVQTVIGNPEAIEAGRRYIDRDLNRSFRL--DLLQNPDlsgyEQL 80

                          90       100
                  ....*....|....*....|....*...
gi 1539368163 121 RARELelsLETFFSSGQARVRWHLDLHT 148
Cdd:PRK02259   81 RAKEL---VQQLGPKGNSPCDFIIDLHS 105
M14_ASPA cd06909
Peptidase M14 Aspartoacylase (ASPA) subfamily; Aspartoacylase (ASPA) belongs to the ...
 48-148 6.76e-13

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: 66.08  E-value: 6.76e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539368163  48 LSAGIHGNETAPVEMLDKLLSalfSGSLMLTW--RVLVVLGNPQALAAGIRYCHSDMNRMFGGRWQSFAESD---ETRRA 122
Cdd:cd06909     5 IVGGTHGNELTGVYLVKHWLK---NPELIERKsfEVHPLLANPRAVEQCRRYIDTDLNRCFSLENLSSAPSSlpyEVRRA 81

                          90       100
                  ....*....|....*....|....*.
gi 1539368163 123 RELElslETFFSSGQARVRWHLDLHT 148
Cdd:cd06909    82 REIN---QILGPKGNPACDFIIDLHN 104
M14_ASTE_ASPA_like cd06230
Peptidase M14 Succinylglutamate desuccinylase (ASTE)/aspartoacylase (ASPA) subfamily; The ...
 46-225 4.77e-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: 4.77e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539368163  46 LILSAGIHGNETAPVEMLDKLLS----ALFSGSLmltwrVLVVLGNPQALAAGIRY---CHSDMNRMFGGRWQSFAESde 118
Cdd:cd06230     1 LLILAGVHGDEYEGVEAIRRLLAeldpSELKGTV-----VLVPVANPPAFEAGTRYtplDGLDLNRIFPGDPDGSPTE-- 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539368163 119 tRRARELElslETFFSsgQARVrwHLDLHTAirGSHHLRFGVLPQRDRPWEAD---FLAWLGAAGLeaLVFHQAPGGTFT 195
Cdd:cd06230    74 -RLAHELT---ELILK--HADA--LIDLHSG--GTGRLVPYAILDYDSDAREKsreLARAFGGTPV--IWGGDPPGGTPV 141

                         170       180       190
                  ....*....|....*....|....*....|
gi 1539368163 196 HFSSEHfGALSCTLELGKALPFGQNDLTQF 225
Cdd:cd06230   142 AAARSA-GIPAITVELGGGGRLRAERLERY 170
COG3608 COG3608
Predicted deacylase [General function prediction only];
46-311 9.45e-12

Predicted deacylase [General function prediction only];


Pssm-ID: 442826 [Multi-domain]  Cd Length: 296  Bit Score: 64.48  E-value: 9.45e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539368163  46 LILSAGIHGNETAPVEMLDKLLSAL----FSGSLmltwrVLVVLGNPQALAAGIRYCHSD---MNRMFGGRwqsfAESDE 118
Cdd:COG3608    29 LLITAGIHGDELNGIEALRRLLRELdpgeLRGTV-----ILVPVANPPGFLQGSRYLPIDgrdLNRSFPGD----ADGSL 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539368163 119 T-RRARelelsleTFFSSGQARVRWHLDLHTairGSHHLRFgvLPQ-RDRPWEADFLAWLGAAGLEALVFHQA-PGGTFT 195
Cdd:COG3608   100 AeRIAH-------ALFEEILPDADYVIDLHS---GGIARDN--LPHvRAGPGDEELRALARAFGAPVILDSPEgGDGSLR 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539368163 196 HfSSEHFGALSCTLELGkalpfGQNDLTQFSItSQALSAL---------LSGVETSTSSSPPLRYRVVSQITRHSDKFaL 266
Cdd:COG3608   168 E-AAAEAGIPALTLELG-----GGGRFDEESI-EAGVRGIlnvlrhlgmLDGEAPPPPLAPPVLARGSEWVRAPAGGL-F 239

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1539368163 267 YMDAQtlNFTAFAKGTLLAE----EGDKRVTVTHDVE---YVLFPNPSVACG 311
Cdd:COG3608   240 EPLVE--LGDRVKKGDVLGRitdpFGEEVEEVRAPVDgivIGRRTNPLVNPG 289
M14_ASTE_ASPA_like cd18430
Succinylglutamate desuccinylase/aspartoacylase; uncharacterized; A functionally ...
 46-148 3.74e-10

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


Pssm-ID: 349486 [Multi-domain]  Cd Length: 168  Bit Score: 57.84  E-value: 3.74e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539368163  46 LILSAGIHGNETAPVEMLDKLLSALFSGSLmLTWRVLVVLGNPQALAAGIRYCHSDMNRMFGGrwQSFAESDETRRAREL 125
Cdd:cd18430     1 LAVLGAVHGNETCGTRAVERLLAELPSGAL-QKGPVTLVPANERAYAEGVRFCEEDLNRVFPG--DPDPDTYERRLANRL 77

                          90       100
                  ....*....|....*....|...
gi 1539368163 126 ELSLEtffssgqaRVRWHLDLHT 148
Cdd:cd18430    78 CPELE--------GHDVVLDLHS 92
M14_ASTE_ASPA-like cd06253
Peptidase M14 Succinylglutamate desuccinylase (ASTE)/aspartoacylase (ASPA)-like; ...
 35-196 1.23e-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: 349471  Cd Length: 211  Bit Score: 48.36  E-value: 1.23e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539368163  35 EFTPDAPVDRALILsAGIHGNETAPV---EMLDKLLSALFSGSLMLTWRVLVV-LGNPQALAAGIRYCH---SDMNRMFG 107
Cdd:cd06253    15 RFGGGNAEPRIAIV-AGIHGDELNGLyvcSRLIRFLKELEEGGYKLKGKVLVIpAVNPLGINSGTRFWPfdnLDMNRMFP 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539368163 108 GrwqsFAESDETRR-ARELELSLETFfssgqarvRWHLDLHTAIRgshHLRFgvLPQ---------RDRPWeADFLawlg 177
Cdd:cd06253    94 G----YNKGETTERiAAALFEDLKGA--------DYGIDLHSSND---FLRE--IPQvrviesgaqDLLPL-AKFL---- 151

                         170       180
                  ....*....|....*....|..
gi 1539368163 178 aaGLEALVFHQAP---GGTFTH 196
Cdd:cd06253   152 --GLDVVWVHPAStvdTGTLAY 171
Peptidase_M14_like cd00596
M14 family of metallocarboxypeptidases and related proteins; The M14 family of ...
 46-235 1.05e-05

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: 45.91  E-value: 1.05e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539368163  46 LILSAGIHGNETAPVEMLDKLLSALFSGSLMLTWR--------VLVVLGNPQALAAGIRYCHS------DMNRMFGGRWQ 111
Cdd:cd00596     1 ILITGGIHGNEVIGVELALALIEYLLENYGNDPLKrlldnvelWIVPLVNPDGFARVIDSGGRknangvDLNRNFPYNWG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539368163 112 ---SFAESDETRRARELELSLET-----FFSsgQARVRWHLDLHTAI-------RGSHHlrfgvlPQRDRPWEADFLAWL 176
Cdd:cd00596    81 kdgTSGPSSPTYRGPAPFSEPETqalrdLAK--SHRFDLAVSYHSSSeailypyGYTNE------PPPDFSEFQELAAGL 152

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1539368163 177 GAA-GLEALVFHQAP-----GGTFTHFSSEHFGALSCTLELGKALPFGQNDLTQfSITSQALSAL 235
Cdd:cd00596   153 ARAlGAGEYGYGYSYtwystTGTADDWLYGELGILAFTVELGTADYPLPGTLLD-RRLERNLAAL 216
M14_MpaA-like cd06904
Peptidase M14-like domain of Escherichia coli Murein Peptide Amidase A and related proteins; ...
 33-106 2.33e-05

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


Pssm-ID: 349475 [Multi-domain]  Cd Length: 214  Bit Score: 44.57  E-value: 2.33e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1539368163  33 LLEFTPDAPVDRALILsAGIHGNETAPVEMLDKLLSALF--SGSLMLTWRVLVVLgNPQALAAGIRY--CHSDMNRMF 106
Cdd:cd06904    14 LAYKFGPGSRARILII-GGIHGDEPEGVSLVEHLLRWLKnhPASGDFHIVVVPCL-NPDGLAAGTRTnaNGVDLNRNF 89
M14_REP34-like cd06231
Peptidase M14-like domain similar to rapid encystment phenotype 34 (REP34); This family ...
 38-147 6.31e-05

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


Pssm-ID: 349450 [Multi-domain]  Cd Length: 239  Bit Score: 43.45  E-value: 6.31e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539368163  38 PDAPVDRALILSAGIHGNETAPVEMLDKLLSALFSGSLM-LTWRVLVVLgNPQALAAGIRYCHS--DMNRmfggrwqSFA 114
Cdd:cd06231    37 NPRGDKPRVLISAGIHGDEPAGVEALLRFLESLAEKYLRrVNLLVLPCV-NPWGFERNTRENADgiDLNR-------SFL 108

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1539368163 115 ESDETRRARelelSLETFFssgQARVRW--HLDLH 147
Cdd:cd06231   109 KDSPSPEVR----ALMEFL---ASLGRFdlHLDLH 136
M14_ASTE_ASPA-like cd06910
Peptidase M14 Succinylglutamate desuccinylase (ASTE)/aspartoacylase (ASPA)-like; ...
 46-148 8.62e-05

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


Pssm-ID: 349481  Cd Length: 208  Bit Score: 42.72  E-value: 8.62e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539368163  46 LILSAGIHGNETAPVEMLDKLLSalfSGSLMLTWRVLVVLGNPQALAA-------GIRYCHSDMNRMFGGRW-QSFAESD 117
Cdd:cd06910    27 VMINALTHGNEICGAIALDWLLK---NGVRPLRGRLTFCFANVEAYERfdparptASRFVDEDLNRVWGPELlDGPEQSI 103

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1539368163 118 ETRRARELELSLETffssgqarVRWHLDLHT 148
Cdd:cd06910   104 ELRRARELRPVVDT--------VDYLLDIHS 126
PRK10602 PRK10602
murein tripeptide amidase MpaA;
29-128 2.79e-04

murein tripeptide amidase MpaA;


Pssm-ID: 182582  Cd Length: 237  Bit Score: 41.55  E-value: 2.79e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539368163  29 LGHGLLEF-TPDAPVDRALILsAGIHGNETAPVEMLDKLLSALFSGSLmltwRVLVVLG-NPQALAAGIRyCHS---DMN 103
Cdd:PRK10602   25 LGAPLLWFpAPAASRESGLIL-AGTHGDETASVVTLSCALRTLTPSLR----RHHVVLAvNPDGCQLGLR-ANAngvDLN 98

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1539368163 104 RMF----------GGRWQSFAEsdetrrARELELS 128
Cdd:PRK10602   99 RNFpaanwkegetVYRWNSAAE------ERDVVLL 127
M14_ASTE_ASPA-like cd06251
Peptidase M14 Succinylglutamate desuccinylase (ASTE)/aspartoacylase (ASPA)-like; ...
 46-152 1.75e-03

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


Pssm-ID: 349469 [Multi-domain]  Cd Length: 195  Bit Score: 38.68  E-value: 1.75e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539368163  46 LILSAGIHGNETAPVEM----LDKLLSALFSGSLMLtwrVLVVlgNPQALAAGIRY---CHSDMNRMF-GGRWQSFAEsd 117
Cdd:cd06251    15 LLLTAAIHGDELNGIEViqrlLEDLDPSKLRGTLIA---IPVV--NPLGFENNSRYlpdDGRDLNRSFpGSEKGSLAS-- 87

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1539368163 118 etRRARELelsLETFFSSGQArvrwHLDLHTAIRG 152
Cdd:cd06251    88 --RLAHLL---WNEIVKKADY----VIDLHTASTG 113
M14_ASTE_ASPA_like cd18174
Peptidase M14 Succinylglutamate desuccinylase (ASTE)/aspartoacylase (ASPA)-like; ...
 46-109 2.88e-03

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


Pssm-ID: 349484  Cd Length: 187  Bit Score: 37.99  E-value: 2.88e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1539368163  46 LILSAGIHGNETAPVEMLDKLLS----ALFSGSLmltwrVLVVLGNPQALAA-GIRYCHSD---MNRMFGGR 109
Cdd:cd18174     1 LLVTAGVHGYEYASIEALQRLIKeldpAKLSGTV-----IVVPIANIPAFEGrSIYVNPLDgknLNRSFPGD 67
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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