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Conserved domains on  [gi|1778701422|ref|WP_154871173|]
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succinylglutamate desuccinylase [Serratia nematodiphila]

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
 1-323 3.09e-173

succinylglutamate desuccinylase; Provisional


:

Pssm-ID: 235408  Cd Length: 329  Bit Score: 483.14  E-value: 3.09e-173
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778701422   1 MIDLLPLTLEGNEPVE-WQGETPQLRWRWQGEGVLELTPRQPYRQAMVMSAGVHGNETAPIELLNQLVGDLLAGRLPLTV 79
Cdd:PRK05324    4 MDDFLALTLAGHPPAVtEFGLGNGVRWRWLGEGVLELTPAAPSTKALVLSAGIHGNETAPIELLDQLVRDLLAGELPLRA 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778701422  80 RLLVVLGNPAAMRAGKRYLHSDMNRMFGGRYRNFAASGETVRAQQLERALAAFFDGE-QAARSHYDLHTAIRESRLPRFG 158
Cdd:PRK05324   84 RLLVILGNPPAMRAGKRYLDEDLNRLFGGRHQQFPGSDEARRAAELEQAVEDFFAAGaERVRWHYDLHTAIRGSKHEQFA 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778701422 159 ILPFQKRPYSEPMLKLLDAADLDALVVHSAPGGTFSHYSSEHLNAASCTLELGKARPFGSNDLQQFAAIDRALRAAVSEG 238
Cdd:PRK05324  164 VLPQRGRPWSREQLAWLGAAGIEAVLLHNAPGGTFSHFSSEHFGALACTLELGKVLPFGQNDLSRFAATDQALRALISGE 243

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778701422 239 ALPTRAGAEIRVFRVMHSLIKHSEDFKLHLDDDTANFTELQPGMLLCEQPQEDYRVGQEGAWILFPNPSVALGLRAGMLL 318
Cdd:PRK05324  244 ELPERSADPPRLYRVVRQITKHSDDFELHFADDVENFTAFPKGTLLAEDGDERYVVEHDGERIVFPNPNVAIGLRAGLML 323


                  ....*
gi 1778701422 319 SEVSR 323
Cdd:PRK05324  324 VPTTL 328
 
Name Accession Description Interval E-value
PRK05324 PRK05324
succinylglutamate desuccinylase; Provisional
 1-323 3.09e-173

succinylglutamate desuccinylase; Provisional


Pssm-ID: 235408  Cd Length: 329  Bit Score: 483.14  E-value: 3.09e-173
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778701422   1 MIDLLPLTLEGNEPVE-WQGETPQLRWRWQGEGVLELTPRQPYRQAMVMSAGVHGNETAPIELLNQLVGDLLAGRLPLTV 79
Cdd:PRK05324    4 MDDFLALTLAGHPPAVtEFGLGNGVRWRWLGEGVLELTPAAPSTKALVLSAGIHGNETAPIELLDQLVRDLLAGELPLRA 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778701422  80 RLLVVLGNPAAMRAGKRYLHSDMNRMFGGRYRNFAASGETVRAQQLERALAAFFDGE-QAARSHYDLHTAIRESRLPRFG 158
Cdd:PRK05324   84 RLLVILGNPPAMRAGKRYLDEDLNRLFGGRHQQFPGSDEARRAAELEQAVEDFFAAGaERVRWHYDLHTAIRGSKHEQFA 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778701422 159 ILPFQKRPYSEPMLKLLDAADLDALVVHSAPGGTFSHYSSEHLNAASCTLELGKARPFGSNDLQQFAAIDRALRAAVSEG 238
Cdd:PRK05324  164 VLPQRGRPWSREQLAWLGAAGIEAVLLHNAPGGTFSHFSSEHFGALACTLELGKVLPFGQNDLSRFAATDQALRALISGE 243

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778701422 239 ALPTRAGAEIRVFRVMHSLIKHSEDFKLHLDDDTANFTELQPGMLLCEQPQEDYRVGQEGAWILFPNPSVALGLRAGMLL 318
Cdd:PRK05324  244 ELPERSADPPRLYRVVRQITKHSDDFELHFADDVENFTAFPKGTLLAEDGDERYVVEHDGERIVFPNPNVAIGLRAGLML 323


                  ....*
gi 1778701422 319 SEVSR 323
Cdd:PRK05324  324 VPTTL 328
arg_catab_astE TIGR03242
succinylglutamate desuccinylase; Members of this protein family are succinylglutamate ...
 3-318 7.71e-155

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: 436.41  E-value: 7.71e-155
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778701422   3 DLLPLTLEGNEPVEWQGETPQLRWRWQGEGVLELTPRQPYRQAMVMSAGVHGNETAPIELLNQLVGDLLAGRLPLTVRLL 82
Cdd:TIGR03242   1 DFLALTLTGKKPHVTQGETNNVRWRWLGEGVLELTPHAPPQKSLVISAGIHGNETAPIEILEQLLGDIAAGKLPLRVRLL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778701422  83 VVLGNPAAMRAGKRYLHSDMNRMFGGRYRNFAASGETVRAQQLERALAAFFD--GEQAARSHYDLHTAIRESRLPRFGIL 160
Cdd:TIGR03242  81 VILGNPPAMRTGKRYLHDDLNRMFGGRYQQLAPSFETCRAAELEQCVEDFFSqgGRSVARWHYDLHTAIRGSLHEQFALL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778701422 161 PFQKRPYSEPMLKLLDAADLDALVVHSAPGGTFSHYSSEHLNAASCTLELGKARPFGSNDLQQFAAIDRALRAAVSEGAL 240
Cdd:TIGR03242 161 PYQGRPWDREFLTWLGAAGLDALVFHTEPGGTFSHFSSEHFGALACTLELGKALPFGQNDLSQFAAITSALRALISDEAI 240

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1778701422 241 PTRAGAEIRVFRVMHSLIKHSEDFKLHLDDDTANFTELQPGMLLCEQPQEDYRVGQEGAWILFPNPSVALGLRAGMLL 318
Cdd:TIGR03242 241 PARRTDPLRLFRVVSSITKHSDSFELHVASDTLNFTPFPKGTLLATDGNERYRVTHEGERILFPNPNVANGLRAGLML 318
AstE COG2988
Succinylglutamate desuccinylase [Amino acid transport and metabolism];
27-322 6.85e-146

Succinylglutamate desuccinylase [Amino acid transport and metabolism];


Pssm-ID: 442227  Cd Length: 305  Bit Score: 413.09  E-value: 6.85e-146
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778701422  27 RWQGEGVLELTPRQPYRQAMVMSAGVHGNETAPIELLNQLVGDLLAGRLPLTVRLLVVLGNPAAMRAGKRYLHSDMNRMF 106
Cdd:COG2988     8 RWLDEGVLELTPHAPGIKAVVISGGIHGNETAPIELLDKLLQDLLLGERPLSFRLLLILGNPAAMRAGRRYLDEDLNRLF 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778701422 107 GGRYRNFAASGETVRAQQLERALAAFFDGEQAARSHYDLHTAIRESRLPRFGILPFQKRPYSEPMLKLLDAADLDALVVH 186
Cdd:COG2988    88 GGRHLQNPESYEAARAKELEQAVGPFFAAGGRVRLHIDLHTAIRNSGHERFAVYPFRGRPFDLALLAYLAAAGPEAVVLH 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778701422 187 SAPGGTFSHYSSEHLNAASCTLELGKARPFGSNDLQQFAAIDRALRAAVSEGALPTRAGAEIRVFRVMHSLIKHSEDFKL 266
Cdd:COG2988   168 HAPGGTFSHFSAELCGAQAFTLELGKVRPFGQNDLSRFAATEEALRALLSGAELPEHPAQDLDLYRVVQQIIKHGDDFML 247

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1778701422 267 HLDDDTANFTELQPGMLLCEQPQEDYRVGQEGAWILFPNPSVALGLRAGMLLSEVS 322
Cdd:COG2988   248 HPDLDTLNFTPLPPGTLLAEDGGKEYRVEGDEERIVFPNEAVYYGQRAALLLTPKE 303
M14_ASTE cd03855
Peptidase M14 Succinylglutamate desuccinylase (ASTE) subfamily; Peptidase M14 ...
 3-237 1.39e-110

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: 321.08  E-value: 1.39e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778701422   3 DLLPLTLEGNEPVEWQGETPQ--LRWRWQGEGVLELTPRQPYRQAMVMSAGVHGNETAPIELLNQLVGDLLAGRLPLTVR 80
Cdd:cd03855     1 DFLALTLSGSEPAEGELAAVSngTRVRWLATGVLELTPAASASKSVVLSAGIHGNETAPIEILDQLINDLIRGELALAHR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778701422  81 LLVVLGNPAAMRAGKRYLHSDMNRMFGGRYRNFAASGETVRAQQLERALAAFFD-GEQAARSHYDLHTAIRESRLPRFGI 159
Cdd:cd03855    81 LLFIFGNPPAIRQGKRFIEENLNRLFSGRHSKLPPSYETARAAELEQAVADFFAkASGEVRWHLDLHTAIRGSKHEQFAV 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1778701422 160 LPFQ-KRPYSEPMLKLLDAADLDALVVHSAPGGTFSHYSSEHLNAASCTLELGKARPFGSNDLQQFAAIDRALRAAVSE 237
Cdd:cd03855   161 YPFLeGRPHDREQLDFLGAAGIEAVLLSNSPGGTFSYYSSEHFGAAAFTVELGKVRPFGQNDLSQFAAIDQALRALISG 239
AstE_AspA pfam04952
Succinylglutamate desuccinylase / Aspartoacylase family; This family includes ...
 47-321 7.33e-64

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: 203.74  E-value: 7.33e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778701422  47 VMSAGVHGNETAPIELLNQLVGDLLAGRLPlTVRLLVVLGNPAAMRAGKRYLHSDMNRMFGGRYRNfAASGETVRAQQLE 126
Cdd:pfam04952   6 LLSAGIHGNETNGVELLRRLLRQLDPGDIA-GERTLVPLANPPAFRAGSRYIPRDLNRSFPGRALG-ASSDEPYRATRAE 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778701422 127 RALAAFFD-GEQAARSHYDLHTAIRESRLPRFGILPFQKRPYSEPMLkLLDAADLDALVVHSAPGGTFSHYSSEHLNAAS 205
Cdd:pfam04952  84 RLADLFFPaLLPRADIVLDLHTGTRGMGHLLFALAPIRDDPLHLLAL-LRAFGAPAVLKLHSKPSAGFSAFSAEELGAPG 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778701422 206 CTLELGKARPFGSNDLQQFAAIDRALRAAVSEGALPTRAGAEIRVFRVMHSLIKHSE---------DFKLHLDDDTANFT 276
Cdd:pfam04952 163 FTLELGGAGPFGANLISRTAAGVLNVLRLIGVLNGGPDAFEPPKLYRVLREIDRPRDiraelaglvEFALNLGDDVDAGP 242

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 1778701422 277 ELQPGMLLCEQPQEDYRV-GQEGAWILFPNPSVALGLRAGMLLSEV 321
Cdd:pfam04952 243 LLPGGPLFAPFGGEETEYrAPEDGYPVFPNEAAYVGKGAALALVAK 288
 
Name Accession Description Interval E-value
PRK05324 PRK05324
succinylglutamate desuccinylase; Provisional
 1-323 3.09e-173

succinylglutamate desuccinylase; Provisional


Pssm-ID: 235408  Cd Length: 329  Bit Score: 483.14  E-value: 3.09e-173
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778701422   1 MIDLLPLTLEGNEPVE-WQGETPQLRWRWQGEGVLELTPRQPYRQAMVMSAGVHGNETAPIELLNQLVGDLLAGRLPLTV 79
Cdd:PRK05324    4 MDDFLALTLAGHPPAVtEFGLGNGVRWRWLGEGVLELTPAAPSTKALVLSAGIHGNETAPIELLDQLVRDLLAGELPLRA 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778701422  80 RLLVVLGNPAAMRAGKRYLHSDMNRMFGGRYRNFAASGETVRAQQLERALAAFFDGE-QAARSHYDLHTAIRESRLPRFG 158
Cdd:PRK05324   84 RLLVILGNPPAMRAGKRYLDEDLNRLFGGRHQQFPGSDEARRAAELEQAVEDFFAAGaERVRWHYDLHTAIRGSKHEQFA 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778701422 159 ILPFQKRPYSEPMLKLLDAADLDALVVHSAPGGTFSHYSSEHLNAASCTLELGKARPFGSNDLQQFAAIDRALRAAVSEG 238
Cdd:PRK05324  164 VLPQRGRPWSREQLAWLGAAGIEAVLLHNAPGGTFSHFSSEHFGALACTLELGKVLPFGQNDLSRFAATDQALRALISGE 243

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778701422 239 ALPTRAGAEIRVFRVMHSLIKHSEDFKLHLDDDTANFTELQPGMLLCEQPQEDYRVGQEGAWILFPNPSVALGLRAGMLL 318
Cdd:PRK05324  244 ELPERSADPPRLYRVVRQITKHSDDFELHFADDVENFTAFPKGTLLAEDGDERYVVEHDGERIVFPNPNVAIGLRAGLML 323


                  ....*
gi 1778701422 319 SEVSR 323
Cdd:PRK05324  324 VPTTL 328
arg_catab_astE TIGR03242
succinylglutamate desuccinylase; Members of this protein family are succinylglutamate ...
 3-318 7.71e-155

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: 436.41  E-value: 7.71e-155
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778701422   3 DLLPLTLEGNEPVEWQGETPQLRWRWQGEGVLELTPRQPYRQAMVMSAGVHGNETAPIELLNQLVGDLLAGRLPLTVRLL 82
Cdd:TIGR03242   1 DFLALTLTGKKPHVTQGETNNVRWRWLGEGVLELTPHAPPQKSLVISAGIHGNETAPIEILEQLLGDIAAGKLPLRVRLL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778701422  83 VVLGNPAAMRAGKRYLHSDMNRMFGGRYRNFAASGETVRAQQLERALAAFFD--GEQAARSHYDLHTAIRESRLPRFGIL 160
Cdd:TIGR03242  81 VILGNPPAMRTGKRYLHDDLNRMFGGRYQQLAPSFETCRAAELEQCVEDFFSqgGRSVARWHYDLHTAIRGSLHEQFALL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778701422 161 PFQKRPYSEPMLKLLDAADLDALVVHSAPGGTFSHYSSEHLNAASCTLELGKARPFGSNDLQQFAAIDRALRAAVSEGAL 240
Cdd:TIGR03242 161 PYQGRPWDREFLTWLGAAGLDALVFHTEPGGTFSHFSSEHFGALACTLELGKALPFGQNDLSQFAAITSALRALISDEAI 240

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1778701422 241 PTRAGAEIRVFRVMHSLIKHSEDFKLHLDDDTANFTELQPGMLLCEQPQEDYRVGQEGAWILFPNPSVALGLRAGMLL 318
Cdd:TIGR03242 241 PARRTDPLRLFRVVSSITKHSDSFELHVASDTLNFTPFPKGTLLATDGNERYRVTHEGERILFPNPNVANGLRAGLML 318
AstE COG2988
Succinylglutamate desuccinylase [Amino acid transport and metabolism];
27-322 6.85e-146

Succinylglutamate desuccinylase [Amino acid transport and metabolism];


Pssm-ID: 442227  Cd Length: 305  Bit Score: 413.09  E-value: 6.85e-146
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778701422  27 RWQGEGVLELTPRQPYRQAMVMSAGVHGNETAPIELLNQLVGDLLAGRLPLTVRLLVVLGNPAAMRAGKRYLHSDMNRMF 106
Cdd:COG2988     8 RWLDEGVLELTPHAPGIKAVVISGGIHGNETAPIELLDKLLQDLLLGERPLSFRLLLILGNPAAMRAGRRYLDEDLNRLF 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778701422 107 GGRYRNFAASGETVRAQQLERALAAFFDGEQAARSHYDLHTAIRESRLPRFGILPFQKRPYSEPMLKLLDAADLDALVVH 186
Cdd:COG2988    88 GGRHLQNPESYEAARAKELEQAVGPFFAAGGRVRLHIDLHTAIRNSGHERFAVYPFRGRPFDLALLAYLAAAGPEAVVLH 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778701422 187 SAPGGTFSHYSSEHLNAASCTLELGKARPFGSNDLQQFAAIDRALRAAVSEGALPTRAGAEIRVFRVMHSLIKHSEDFKL 266
Cdd:COG2988   168 HAPGGTFSHFSAELCGAQAFTLELGKVRPFGQNDLSRFAATEEALRALLSGAELPEHPAQDLDLYRVVQQIIKHGDDFML 247

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1778701422 267 HLDDDTANFTELQPGMLLCEQPQEDYRVGQEGAWILFPNPSVALGLRAGMLLSEVS 322
Cdd:COG2988   248 HPDLDTLNFTPLPPGTLLAEDGGKEYRVEGDEERIVFPNEAVYYGQRAALLLTPKE 303
M14_ASTE cd03855
Peptidase M14 Succinylglutamate desuccinylase (ASTE) subfamily; Peptidase M14 ...
 3-237 1.39e-110

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: 321.08  E-value: 1.39e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778701422   3 DLLPLTLEGNEPVEWQGETPQ--LRWRWQGEGVLELTPRQPYRQAMVMSAGVHGNETAPIELLNQLVGDLLAGRLPLTVR 80
Cdd:cd03855     1 DFLALTLSGSEPAEGELAAVSngTRVRWLATGVLELTPAASASKSVVLSAGIHGNETAPIEILDQLINDLIRGELALAHR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778701422  81 LLVVLGNPAAMRAGKRYLHSDMNRMFGGRYRNFAASGETVRAQQLERALAAFFD-GEQAARSHYDLHTAIRESRLPRFGI 159
Cdd:cd03855    81 LLFIFGNPPAIRQGKRFIEENLNRLFSGRHSKLPPSYETARAAELEQAVADFFAkASGEVRWHLDLHTAIRGSKHEQFAV 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1778701422 160 LPFQ-KRPYSEPMLKLLDAADLDALVVHSAPGGTFSHYSSEHLNAASCTLELGKARPFGSNDLQQFAAIDRALRAAVSE 237
Cdd:cd03855   161 YPFLeGRPHDREQLDFLGAAGIEAVLLSNSPGGTFSYYSSEHFGAAAFTVELGKVRPFGQNDLSQFAAIDQALRALISG 239
AstE_AspA pfam04952
Succinylglutamate desuccinylase / Aspartoacylase family; This family includes ...
 47-321 7.33e-64

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: 203.74  E-value: 7.33e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778701422  47 VMSAGVHGNETAPIELLNQLVGDLLAGRLPlTVRLLVVLGNPAAMRAGKRYLHSDMNRMFGGRYRNfAASGETVRAQQLE 126
Cdd:pfam04952   6 LLSAGIHGNETNGVELLRRLLRQLDPGDIA-GERTLVPLANPPAFRAGSRYIPRDLNRSFPGRALG-ASSDEPYRATRAE 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778701422 127 RALAAFFD-GEQAARSHYDLHTAIRESRLPRFGILPFQKRPYSEPMLkLLDAADLDALVVHSAPGGTFSHYSSEHLNAAS 205
Cdd:pfam04952  84 RLADLFFPaLLPRADIVLDLHTGTRGMGHLLFALAPIRDDPLHLLAL-LRAFGAPAVLKLHSKPSAGFSAFSAEELGAPG 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778701422 206 CTLELGKARPFGSNDLQQFAAIDRALRAAVSEGALPTRAGAEIRVFRVMHSLIKHSE---------DFKLHLDDDTANFT 276
Cdd:pfam04952 163 FTLELGGAGPFGANLISRTAAGVLNVLRLIGVLNGGPDAFEPPKLYRVLREIDRPRDiraelaglvEFALNLGDDVDAGP 242

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 1778701422 277 ELQPGMLLCEQPQEDYRV-GQEGAWILFPNPSVALGLRAGMLLSEV 321
Cdd:pfam04952 243 LLPGGPLFAPFGGEETEYrAPEDGYPVFPNEAAYVGKGAALALVAK 288
M14_ASTE_ASPA_like cd06230
Peptidase M14 Succinylglutamate desuccinylase (ASTE)/aspartoacylase (ASPA) subfamily; The ...
 47-232 2.52e-16

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: 75.43  E-value: 2.52e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778701422  47 VMSAGVHGNETAPIELLNQLVGDLLAGRLPLTVRLLVVLgNPAAMRAGKRYLHS---DMNRMFGGRYRNFAasgETVRAQ 123
Cdd:cd06230     2 LILAGVHGDEYEGVEAIRRLLAELDPSELKGTVVLVPVA-NPPAFEAGTRYTPLdglDLNRIFPGDPDGSP---TERLAH 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778701422 124 QLERALAAFfdgeqaARSHYDLHTAIREsRLPRFGILPFQ--KRPYSEPMLKllDAADLDALVVHSAPGGTFSHYSSEHL 201
Cdd:cd06230    78 ELTELILKH------ADALIDLHSGGTG-RLVPYAILDYDsdAREKSRELAR--AFGGTPVIWGGDPPGGTPVAAARSAG 148

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1778701422 202 nAASCTLELGKArpfGSNDLQQFAAIDRALR 232
Cdd:cd06230   149 -IPAITVELGGG---GRLRAERLERYLRGIR 175
M14_ASPA cd06909
Peptidase M14 Aspartoacylase (ASPA) subfamily; Aspartoacylase (ASPA) belongs to the ...
 49-147 7.34e-11

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: 60.30  E-value: 7.34e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778701422  49 SAGVHGNETAPIELLNQLV-GDLLAGRLPLTVRLLvvLGNPAAMRAGKRYLHSDMNRMFGGRYRNFAASG---ETVRAQQ 124
Cdd:cd06909     6 VGGTHGNELTGVYLVKHWLkNPELIERKSFEVHPL--LANPRAVEQCRRYIDTDLNRCFSLENLSSAPSSlpyEVRRARE 83

                          90       100
                  ....*....|....*....|...
gi 1778701422 125 LERALAAffDGEQAARSHYDLHT 147
Cdd:cd06909    84 INQILGP--KGNPACDFIIDLHN 104
PRK02259 PRK02259
aspartoacylase; Provisional
 47-147 1.57e-10

aspartoacylase; Provisional


Pssm-ID: 235019  Cd Length: 288  Bit Score: 61.04  E-value: 1.57e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778701422  47 VMSAGVHGNETAPIELLNQLV--GDLLAGRlplTVRLLVVLGNPAAMRAGKRYLHSDMNRMF--GGRYRNFAASGETVRA 122
Cdd:PRK02259    6 AIVGGTHGNEITGIYLVKKWQqqPNLINRK---GLEVQTVIGNPEAIEAGRRYIDRDLNRSFrlDLLQNPDLSGYEQLRA 82

                          90       100
                  ....*....|....*....|....*
gi 1778701422 123 QQLERALAafFDGEQAARSHYDLHT 147
Cdd:PRK02259   83 KELVQQLG--PKGNSPCDFIIDLHS 105
COG3608 COG3608
Predicted deacylase [General function prediction only];
49-311 2.42e-10

Predicted deacylase [General function prediction only];


Pssm-ID: 442826 [Multi-domain]  Cd Length: 296  Bit Score: 60.25  E-value: 2.42e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778701422  49 SAGVHGNETAPIELLNQLVGDLLAGRLPLTVRLLVVLgNPAAMRAGKRYLHSD---MNRMFGGRyrnfaASGEtvraqqL 125
Cdd:COG3608    32 TAGIHGDELNGIEALRRLLRELDPGELRGTVILVPVA-NPPGFLQGSRYLPIDgrdLNRSFPGD-----ADGS------L 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778701422 126 ERALAAFFDGEQAARSHY--DLHT-AIRESRLP--RFGILPfqkrPYSEPMLKlldaADLDALVVHSA--PGGTFSHYSS 198
Cdd:COG3608   100 AERIAHALFEEILPDADYviDLHSgGIARDNLPhvRAGPGD----EELRALAR----AFGAPVILDSPegGDGSLREAAA 171

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778701422 199 EhLNAASCTLELGKARPFgsndlqQFAAIDRALRAAVS--------EGALPTRAGAEIRVFRVMHSLIKHSEDFklhLDD 270
Cdd:COG3608   172 E-AGIPALTLELGGGGRF------DEESIEAGVRGILNvlrhlgmlDGEAPPPPLAPPVLARGSEWVRAPAGGL---FEP 241

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 1778701422 271 DTANFTELQPGMLLCE------QPQEDYRVGQEG-AWILFPNPSVALG 311
Cdd:COG3608   242 LVELGDRVKKGDVLGRitdpfgEEVEEVRAPVDGiVIGRRTNPLVNPG 289
M14_ASTE_ASPA-like cd06253
Peptidase M14 Succinylglutamate desuccinylase (ASTE)/aspartoacylase (ASPA)-like; ...
 50-146 9.25e-09

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: 54.53  E-value: 9.25e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778701422  50 AGVHGNETAPI---ELLNQLVGDLLAGRLPLTVRLLVV-LGNPAAMRAGKRYLH---SDMNRMFGGryrnfAASGETVra 122
Cdd:cd06253    29 AGIHGDELNGLyvcSRLIRFLKELEEGGYKLKGKVLVIpAVNPLGINSGTRFWPfdnLDMNRMFPG-----YNKGETT-- 101

                          90       100
                  ....*....|....*....|....*.
gi 1778701422 123 qqlERALAAFFdgEQAARSHY--DLH 146
Cdd:cd06253   102 ---ERIAAALF--EDLKGADYgiDLH 122
M14_ASTE_ASPA_like cd18430
Succinylglutamate desuccinylase/aspartoacylase; uncharacterized; A functionally ...
 50-160 2.48e-07

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: 49.75  E-value: 2.48e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778701422  50 AGVHGNETAPIELLNQLVGDLLAGRLpLTVRLLVVLGNPAAMRAGKRYLHSDMNRMFGGryrnfaasgeTVRAQQLERAL 129
Cdd:cd18430     5 GAVHGNETCGTRAVERLLAELPSGAL-QKGPVTLVPANERAYAEGVRFCEEDLNRVFPG----------DPDPDTYERRL 73

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1778701422 130 AAFFDGE-QAARSHYDLHTAirESRLPRFGIL 160
Cdd:cd18430    74 ANRLCPElEGHDVVLDLHST--HSGGQPFAIL 103
M14_ASTE_ASPA-like cd06251
Peptidase M14 Succinylglutamate desuccinylase (ASTE)/aspartoacylase (ASPA)-like; ...
 47-148 3.62e-06

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


Pssm-ID: 349469 [Multi-domain]  Cd Length: 195  Bit Score: 46.76  E-value: 3.62e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778701422  47 VMSAGVHGNETAPIELLNQLVGDLLAGRLPLTVRLLVVLgNPAAMRAGKRYLHS---DMNRMF-GGRYRNFAasgetvra 122
Cdd:cd06251    16 LLTAAIHGDELNGIEVIQRLLEDLDPSKLRGTLIAIPVV-NPLGFENNSRYLPDdgrDLNRSFpGSEKGSLA-------- 86

                          90       100
                  ....*....|....*....|....*....
gi 1778701422 123 qqlERALAAFFDG--EQAarSHY-DLHTA 148
Cdd:cd06251    87 ---SRLAHLLWNEivKKA--DYViDLHTA 110
Peptidase_M14_like cd00596
M14 family of metallocarboxypeptidases and related proteins; The M14 family of ...
 47-221 1.39e-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: 45.53  E-value: 1.39e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778701422  47 VMSAGVHGNETAPIELLNQLVGDLLAG-------RLPLTVRLLVV-LGNPAAMRAGKRYLHS------DMNRMF------ 106
Cdd:cd00596     2 LITGGIHGNEVIGVELALALIEYLLENygndplkRLLDNVELWIVpLVNPDGFARVIDSGGRknangvDLNRNFpynwgk 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778701422 107 -GGRYRNFAASGETVRAQQLE-RALAAFFDGEQAARsHYDLHTAIrESRLPRFGILPFQKRPYSEPM---LKLLDAADLD 181
Cdd:cd00596    82 dGTSGPSSPTYRGPAPFSEPEtQALRDLAKSHRFDL-AVSYHSSS-EAILYPYGYTNEPPPDFSEFQelaAGLARALGAG 159

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1778701422 182 ALVVHSAP-----GGTFSHYSSEHLNAASCTLELGKARPFGSNDL 221
Cdd:cd00596   160 EYGYGYSYtwystTGTADDWLYGELGILAFTVELGTADYPLPGTL 204
M14_ASTE_ASPA-like cd06252
Peptidase M14 Succinylglutamate desuccinylase (ASTE)/aspartoacylase (ASPA)-like; ...
 47-148 5.16e-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: 349470  Cd Length: 224  Bit Score: 43.71  E-value: 5.16e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778701422  47 VMSAGVHGNE-TAPI---ELLNQLVGDLLAGRLpltvrLLVVLGNPAAMRAGKRYLHSD---MNRMFGGRyrnfAASGET 119
Cdd:cd06252    38 LLTGGNHGDEyEGPIalrRLARDLDPEDVRGRL-----IIVPALNLPAVRAGTRTSPLDggnLNRAFPGD----ADGTPT 108

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1778701422 120 VRaqqleraLAAFFDGEQAARSHY--DLHTA 148
Cdd:cd06252   109 ER-------IAHFLETVLLPRADAviDLHSG 132
M14_REP34-like cd06231
Peptidase M14-like domain similar to rapid encystment phenotype 34 (REP34); This family ...
 49-146 2.19e-04

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


Pssm-ID: 349450 [Multi-domain]  Cd Length: 239  Bit Score: 41.91  E-value: 2.19e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778701422  49 SAGVHGNETAP----IELLNQLVGDLLAGrlpltVRLLVV-LGNPAAMRAGKRYLHS--DMNrmfggryRNFAASGETVR 121
Cdd:cd06231    48 SAGIHGDEPAGvealLRFLESLAEKYLRR-----VNLLVLpCVNPWGFERNTRENADgiDLN-------RSFLKDSPSPE 115

                          90       100
                  ....*....|....*....|....*..
gi 1778701422 122 AQQLERALAAF--FDGeqaarsHYDLH 146
Cdd:cd06231   116 VRALMEFLASLgrFDL------HLDLH 136
M14_ASTE_ASPA-like cd06254
Peptidase M14 Succinylglutamate desuccinylase (ASTE)/aspartoacylase (ASPA)-like; ...
 47-146 4.74e-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: 349472  Cd Length: 198  Bit Score: 40.64  E-value: 4.74e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778701422  47 VMSAGVHGNETAPI----ELLNQLVGDLLAGRLpltvrLLVVLGNPAAMRAGKRYLHSD----MNRMFGGRyrnfAASGE 118
Cdd:cd06254    15 LITAGIHGGEYPGIlaaiRLARELDPADVKGTL-----IIVHIANVSGFEARTPFVVPEdgknLNRVFPGD----PDGTL 85

                          90       100       110
                  ....*....|....*....|....*....|
gi 1778701422 119 TVRaqqleraLAAFFDGEQAARSHY--DLH 146
Cdd:cd06254    86 TER-------IAYFLTREIISRADFliDLH 108
M14_CP_Csd4-like cd06243
Peptidase M14 carboxypeptidase Csd4 and similar proteins; This family includes peptidase M14 ...
 33-106 1.81e-03

Peptidase M14 carboxypeptidase Csd4 and similar proteins; This family includes peptidase M14 carboxypeptidase Csd4 from H. pylori which has been shown to be DL-carboxypeptidase with a modified zinc binding site containing a glutamine residue in place of a conserved histidine. It is an archetype of a new carboxypeptidase subfamily with a domain arrangement that differs from this family of peptide-cleaving enzymes. Csd4 plays a role in trimming uncrosslinked peptidoglycan peptide chains by cleaving the amide bond between meso-diaminopimelate and iso-D-glutamic acid in truncated peptidoglycan side chains. It acts as a cell shape determinant, similar to Campylobacter jejuni Pgp1. 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: 349462  Cd Length: 227  Bit Score: 39.27  E-value: 1.81e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1778701422  33 VLELTPRQPYRQAMVMsAGVHGNETApiellNQLVGDLLAGRLPLTVRLLVV-LGNPAAMRAGKRYLHSDMNRMF 106
Cdd:cd06243     7 FTRLEGREPGPTLLII-GGIQGDEPG-----GFLAADLLADLYLVKGNVIVVpRLNFPSILRNHRGLNGDMNRKF 75
M14_ASTE_ASPA_like cd18174
Peptidase M14 Succinylglutamate desuccinylase (ASTE)/aspartoacylase (ASPA)-like; ...
 48-146 3.96e-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: 37.61  E-value: 3.96e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778701422  48 MSAGVHGNETAPIELLNQLVGDLLAGRLPLTVrLLVVLGNPAAMRAGKRYLH----SDMNRMFGGRyrnfAASGETvraq 123
Cdd:cd18174     3 VTAGVHGYEYASIEALQRLIKELDPAKLSGTV-IVVPIANIPAFEGRSIYVNpldgKNLNRSFPGD----PDGTPT---- 73

                          90       100
                  ....*....|....*....|....*
gi 1778701422 124 qlERaLAAFFDGEQAARSHY--DLH 146
Cdd:cd18174    74 --ER-LAHWLTTNVIARADYyiDLH 95
 
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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