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Conserved domains on  [gi|1330281852|ref|WP_102433086|]
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MULTISPECIES: succinylglutamate desuccinylase/aspartoacylase family protein [Vibrio]

Protein Classification

succinylglutamate desuccinylase/aspartoacylase family protein( domain architecture ID 11466477)

succinylglutamate desuccinylase (ASTE)/aspartoacylase (ASPA) family protein which belongs to the ASTE/ASPA subfamily of the M14 family of metallocarboxypeptidases; ASTE cleaves N-succinyl-L-glutamate into succinate and L-glutamate (the last step in the arginine succinyltransferase (AST) pathway for the catabolism of arginine), and ASPA cleaves N-acetyl L-aspartic acid into aspartate and acetate

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
COG3608 COG3608
Predicted deacylase [General function prediction only];
32-337 4.90e-88

Predicted deacylase [General function prediction only];


:

Pssm-ID: 442826 [Multi-domain]  Cd Length: 296  Bit Score: 266.33  E-value: 4.90e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330281852  32 WFQVTSDGLGQPKNMPVSVFKGSQDGPKLMITAGIHGDELNGVLAAQQIIRDLVGKTLKGTVTIVPTVNLSGLLNHSRDF 111
Cdd:COG3608     1 RLPLSRLASGTPVSLPVTVFRGAGPGPTLLITAGIHGDELNGIEALRRLLRELDPGELRGTVILVPVANPPGFLQGSRYL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330281852 112 ISSDPgscpaNLNRLFPGDENGLAAERFVSSLWERLLKHnATFAVDLHTQTRGAVYPLYVFADYRIEQCLDMARLMQPDC 191
Cdd:COG3608    81 PIDGR-----DLNRSFPGDADGSLAERIAHALFEEILPD-ADYVIDLHSGGIARDNLPHVRAGPGDEELRALARAFGAPV 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330281852 192 VLN-DPGDPGILETVWNRSGIPSITVEVGMGKFTQPDMIQRAVDGVLNMLSYYEMLevDGQDPLEVKQLPsmdwIEGNNV 270
Cdd:COG3608   155 ILDsPEGGDGSLREAAAEAGIPALTLELGGGGRFDEESIEAGVRGILNVLRHLGML--DGEAPPPPLAPP----VLARGS 228

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1330281852 271 VSIRADIGGFVLPQVELLQSVEQGDLLAIQYDAFGNECRRYHAPSAGRVLSYNVDALREPGALVCRL 337
Cdd:COG3608   229 EWVRAPAGGLFEPLVELGDRVKKGDVLGRITDPFGEEVEEVRAPVDGIVIGRRTNPLVNPGDALFHI 295
 
Name Accession Description Interval E-value
COG3608 COG3608
Predicted deacylase [General function prediction only];
32-337 4.90e-88

Predicted deacylase [General function prediction only];


Pssm-ID: 442826 [Multi-domain]  Cd Length: 296  Bit Score: 266.33  E-value: 4.90e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330281852  32 WFQVTSDGLGQPKNMPVSVFKGSQDGPKLMITAGIHGDELNGVLAAQQIIRDLVGKTLKGTVTIVPTVNLSGLLNHSRDF 111
Cdd:COG3608     1 RLPLSRLASGTPVSLPVTVFRGAGPGPTLLITAGIHGDELNGIEALRRLLRELDPGELRGTVILVPVANPPGFLQGSRYL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330281852 112 ISSDPgscpaNLNRLFPGDENGLAAERFVSSLWERLLKHnATFAVDLHTQTRGAVYPLYVFADYRIEQCLDMARLMQPDC 191
Cdd:COG3608    81 PIDGR-----DLNRSFPGDADGSLAERIAHALFEEILPD-ADYVIDLHSGGIARDNLPHVRAGPGDEELRALARAFGAPV 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330281852 192 VLN-DPGDPGILETVWNRSGIPSITVEVGMGKFTQPDMIQRAVDGVLNMLSYYEMLevDGQDPLEVKQLPsmdwIEGNNV 270
Cdd:COG3608   155 ILDsPEGGDGSLREAAAEAGIPALTLELGGGGRFDEESIEAGVRGILNVLRHLGML--DGEAPPPPLAPP----VLARGS 228

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1330281852 271 VSIRADIGGFVLPQVELLQSVEQGDLLAIQYDAFGNECRRYHAPSAGRVLSYNVDALREPGALVCRL 337
Cdd:COG3608   229 EWVRAPAGGLFEPLVELGDRVKKGDVLGRITDPFGEEVEEVRAPVDGIVIGRRTNPLVNPGDALFHI 295
M14_ASTE_ASPA-like cd06251
Peptidase M14 Succinylglutamate desuccinylase (ASTE)/aspartoacylase (ASPA)-like; ...
 46-246 9.01e-81

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: 243.99  E-value: 9.01e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330281852  46 MPVSVFKGSQDGPKLMITAGIHGDELNGVLAAQQIIRDLVGKTLKGTVTIVPTVNLSGLLNHSRDFISSdpgscPANLNR 125
Cdd:cd06251     1 VPVLVARGAKPGPTLLLTAAIHGDELNGIEVIQRLLEDLDPSKLRGTLIAIPVVNPLGFENNSRYLPDD-----GRDLNR 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330281852 126 LFPGDENGLAAERFVSSLWERLLKHnATFAVDLHTQTRGAVYPLYVFADYRIEQCLDMARLMQPDCVLNDPGDPGILETV 205
Cdd:cd06251    76 SFPGSEKGSLASRLAHLLWNEIVKK-ADYVIDLHTASTGRTNLPYVRADLRDPESRRMAEAFGAPVIVDDPGEDGSLRGA 154

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1330281852 206 WNRSGIPSITVEVGMGKFTQPDMIQRAVDGVLNMLSYYEML 246
Cdd:cd06251   155 AVELGIPAITVELGEALRFDEDIIRRGVEGVLNVLRHLGML 195
AstE_AspA pfam04952
Succinylglutamate desuccinylase / Aspartoacylase family; This family includes ...
 56-337 3.85e-60

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


Pssm-ID: 428216 [Multi-domain]  Cd Length: 289  Bit Score: 194.49  E-value: 3.85e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330281852  56 DGPKLMITAGIHGDELNGVLAAQQIIRDLVGKTLKGTVTIVPTVNLSGLLNHSRDfissdpgsCPANLNRLFPGDENGL- 134
Cdd:pfam04952   1 PGPTLLLSAGIHGNETNGVELLRRLLRQLDPGDIAGERTLVPLANPPAFRAGSRY--------IPRDLNRSFPGRALGAs 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330281852 135 --------AAERFVSSLWeRLLKHNATFAVDLHTQTRGAVYPLYVFADYRIE--QCLDMARLMQPD--CVLNDPGDPGIL 202
Cdd:pfam04952  73 sdepyratRAERLADLFF-PALLPRADIVLDLHTGTRGMGHLLFALAPIRDDplHLLALLRAFGAPavLKLHSKPSAGFS 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330281852 203 ETVWNRSGIPSITVEVGMGKFTQPDMIQRAVDGVLNMLSYYEML--EVDGQDPLEVKQLPSMdwieGNNVVSIRADIGGF 280
Cdd:pfam04952 152 AFSAEELGAPGFTLELGGAGPFGANLISRTAAGVLNVLRLIGVLngGPDAFEPPKLYRVLRE----IDRPRDIRAELAGL 227

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1330281852 281 VLPQVELLQSVEQGDLLA--IQYDAFGNECRRYHAPSAGRVLSYNVDALREPGALVCRL 337
Cdd:pfam04952 228 VEFALNLGDDVDAGPLLPggPLFAPFGGEETEYRAPEDGYPVFPNEAAYVGKGAALALV 286
Zn_pept smart00631
Zn_pept domain;
58-168 1.17e-04

Zn_pept domain;


Pssm-ID: 214748 [Multi-domain]  Cd Length: 277  Bit Score: 43.09  E-value: 1.17e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330281852   58 PKLMITAGIHGDELNGVLAAQQIIRDLV---------GKTLKGT-VTIVPTVNLSGL-LNHSRDFIS----SDPGSC-PA 121
Cdd:smart00631  50 PAIFIDAGIHAREWIGPATALYLINQLLenygrdprvTNLLDKTdIYIVPVLNPDGYeYTHTGDRLWrknrSPNSNCrGV 129

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1330281852  122 NLNRLFPGDEN-----------GLAAE-----RFVSSLWERLLkhNATFAVDLHTQTRGAVYP 168
Cdd:smart00631 130 DLNRNFPFHWGetgnpcsetyaGPSPFsepetKAVRDFIRSNR--RFKLYIDLHSYSQLILYP 190
PRK05324 PRK05324
succinylglutamate desuccinylase; Provisional
 60-168 4.95e-04

succinylglutamate desuccinylase; Provisional


Pssm-ID: 235408  Cd Length: 329  Bit Score: 41.32  E-value: 4.95e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330281852  60 LMITAGIHGDE------LNgvlaaqQIIRDLvgktLKGtvTIVPTV-------NLSGLLNHSRdFISSDpgscpanLNRL 126
Cdd:PRK05324   50 LVLSAGIHGNEtapielLD------QLVRDL----LAG--ELPLRArllvilgNPPAMRAGKR-YLDED-------LNRL 109

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1330281852 127 F--------PGDENGLAAE------RFVSSLWERLLKHnatfaVDLHTQTRG------AVYP 168
Cdd:PRK05324  110 FggrhqqfpGSDEARRAAEleqaveDFFAAGAERVRWH-----YDLHTAIRGskheqfAVLP 166
 
Name Accession Description Interval E-value
COG3608 COG3608
Predicted deacylase [General function prediction only];
32-337 4.90e-88

Predicted deacylase [General function prediction only];


Pssm-ID: 442826 [Multi-domain]  Cd Length: 296  Bit Score: 266.33  E-value: 4.90e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330281852  32 WFQVTSDGLGQPKNMPVSVFKGSQDGPKLMITAGIHGDELNGVLAAQQIIRDLVGKTLKGTVTIVPTVNLSGLLNHSRDF 111
Cdd:COG3608     1 RLPLSRLASGTPVSLPVTVFRGAGPGPTLLITAGIHGDELNGIEALRRLLRELDPGELRGTVILVPVANPPGFLQGSRYL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330281852 112 ISSDPgscpaNLNRLFPGDENGLAAERFVSSLWERLLKHnATFAVDLHTQTRGAVYPLYVFADYRIEQCLDMARLMQPDC 191
Cdd:COG3608    81 PIDGR-----DLNRSFPGDADGSLAERIAHALFEEILPD-ADYVIDLHSGGIARDNLPHVRAGPGDEELRALARAFGAPV 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330281852 192 VLN-DPGDPGILETVWNRSGIPSITVEVGMGKFTQPDMIQRAVDGVLNMLSYYEMLevDGQDPLEVKQLPsmdwIEGNNV 270
Cdd:COG3608   155 ILDsPEGGDGSLREAAAEAGIPALTLELGGGGRFDEESIEAGVRGILNVLRHLGML--DGEAPPPPLAPP----VLARGS 228

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1330281852 271 VSIRADIGGFVLPQVELLQSVEQGDLLAIQYDAFGNECRRYHAPSAGRVLSYNVDALREPGALVCRL 337
Cdd:COG3608   229 EWVRAPAGGLFEPLVELGDRVKKGDVLGRITDPFGEEVEEVRAPVDGIVIGRRTNPLVNPGDALFHI 295
M14_ASTE_ASPA-like cd06251
Peptidase M14 Succinylglutamate desuccinylase (ASTE)/aspartoacylase (ASPA)-like; ...
 46-246 9.01e-81

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: 243.99  E-value: 9.01e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330281852  46 MPVSVFKGSQDGPKLMITAGIHGDELNGVLAAQQIIRDLVGKTLKGTVTIVPTVNLSGLLNHSRDFISSdpgscPANLNR 125
Cdd:cd06251     1 VPVLVARGAKPGPTLLLTAAIHGDELNGIEVIQRLLEDLDPSKLRGTLIAIPVVNPLGFENNSRYLPDD-----GRDLNR 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330281852 126 LFPGDENGLAAERFVSSLWERLLKHnATFAVDLHTQTRGAVYPLYVFADYRIEQCLDMARLMQPDCVLNDPGDPGILETV 205
Cdd:cd06251    76 SFPGSEKGSLASRLAHLLWNEIVKK-ADYVIDLHTASTGRTNLPYVRADLRDPESRRMAEAFGAPVIVDDPGEDGSLRGA 154

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1330281852 206 WNRSGIPSITVEVGMGKFTQPDMIQRAVDGVLNMLSYYEML 246
Cdd:cd06251   155 AVELGIPAITVELGEALRFDEDIIRRGVEGVLNVLRHLGML 195
AstE_AspA pfam04952
Succinylglutamate desuccinylase / Aspartoacylase family; This family includes ...
 56-337 3.85e-60

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


Pssm-ID: 428216 [Multi-domain]  Cd Length: 289  Bit Score: 194.49  E-value: 3.85e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330281852  56 DGPKLMITAGIHGDELNGVLAAQQIIRDLVGKTLKGTVTIVPTVNLSGLLNHSRDfissdpgsCPANLNRLFPGDENGL- 134
Cdd:pfam04952   1 PGPTLLLSAGIHGNETNGVELLRRLLRQLDPGDIAGERTLVPLANPPAFRAGSRY--------IPRDLNRSFPGRALGAs 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330281852 135 --------AAERFVSSLWeRLLKHNATFAVDLHTQTRGAVYPLYVFADYRIE--QCLDMARLMQPD--CVLNDPGDPGIL 202
Cdd:pfam04952  73 sdepyratRAERLADLFF-PALLPRADIVLDLHTGTRGMGHLLFALAPIRDDplHLLALLRAFGAPavLKLHSKPSAGFS 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330281852 203 ETVWNRSGIPSITVEVGMGKFTQPDMIQRAVDGVLNMLSYYEML--EVDGQDPLEVKQLPSMdwieGNNVVSIRADIGGF 280
Cdd:pfam04952 152 AFSAEELGAPGFTLELGGAGPFGANLISRTAAGVLNVLRLIGVLngGPDAFEPPKLYRVLRE----IDRPRDIRAELAGL 227

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1330281852 281 VLPQVELLQSVEQGDLLA--IQYDAFGNECRRYHAPSAGRVLSYNVDALREPGALVCRL 337
Cdd:pfam04952 228 VEFALNLGDDVDAGPLLPggPLFAPFGGEETEYRAPEDGYPVFPNEAAYVGKGAALALV 286
M14_ASTE_ASPA-like cd06254
Peptidase M14 Succinylglutamate desuccinylase (ASTE)/aspartoacylase (ASPA)-like; ...
 47-243 6.52e-36

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: 128.85  E-value: 6.52e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330281852  47 PVSVFKGSQDGPKLMITAGIHGDELNGVLAAQQIIRDLVGKTLKGTVTIVPTVNLSGLLNHsRDFISSDPGscpANLNRL 126
Cdd:cd06254     1 PVTLINGAKPGPTLLITAGIHGGEYPGILAAIRLARELDPADVKGTLIIVHIANVSGFEAR-TPFVVPEDG---KNLNRV 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330281852 127 FPGDENGLAAERFVSSLWERLLKhNATFAVDLHT-QTRGAVYP-LYVFADYRIEQC---LDMARLMQ-PDCVLNDPGDPG 200
Cdd:cd06254    77 FPGDPDGTLTERIAYFLTREIIS-RADFLIDLHGgDANEALTPfVYYPGGASEEVNdisRAAAQALGlPYIVISSSEKGT 155

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1330281852 201 ILETVWNRSGIPSITVEVGMGKFTQPDMIQRAVDGVLNMLSYY 243
Cdd:cd06254   156 GYYSYAALRGIPSILVERGGLGTCDEEDVQAHKDGIKNLLRHL 198
M14_ASTE_ASPA_like cd06230
Peptidase M14 Succinylglutamate desuccinylase (ASTE)/aspartoacylase (ASPA) subfamily; The ...
 60-238 3.50e-35

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: 126.27  E-value: 3.50e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330281852  60 LMITAGIHGDELNGVLAAQQIIRDLVGKTLKGTVTIVPTVNLSGLLNHSRdfisSDPGScPANLNRLFPGDENGLAAERF 139
Cdd:cd06230     1 LLILAGVHGDEYEGVEAIRRLLAELDPSELKGTVVLVPVANPPAFEAGTR----YTPLD-GLDLNRIFPGDPDGSPTERL 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330281852 140 VSSLWERLLKHnATFAVDLHTQTRGAVYPlYVFADYRIEQC---LDMARLMQ-PDCVLNDPGDPGILETVWNRSGIPSIT 215
Cdd:cd06230    76 AHELTELILKH-ADALIDLHSGGTGRLVP-YAILDYDSDAReksRELARAFGgTPVIWGGDPPGGTPVAAARSAGIPAIT 153

                         170       180
                  ....*....|....*....|...
gi 1330281852 216 VEVGMGKFTQPDMIQRAVDGVLN 238
Cdd:cd06230   154 VELGGGGRLRAERLERYLRGIRN 176
M14_ASTE_ASPA-like cd06255
Peptidase M14 Succinylglutamate desuccinylase (ASTE)/aspartoacylase (ASPA)-like; ...
 35-246 8.99e-35

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: 349473  Cd Length: 223  Bit Score: 126.67  E-value: 8.99e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330281852  35 VTSDGLGQPKNMPVSVFKGSQDGPKLMITAGIHGDELNGVLAAQQIIRDLVGKTLKGTVTIVPTVNLSGLLNHSRDFISS 114
Cdd:cd06255     1 VGELASGAPVTIPVIVVRGAKPGPCLWINGAVHGDELNGPLAALELFRELDPAQLSGTLVATPIANPLAFQGRQKFSPQD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330281852 115 DPgscpaNLNRLFPGDENGLAAERFVSSLWERlLKHNATFAVDLHTQ---TRGAVYPLY-VFADYRIEQC---LDMARL- 186
Cdd:cd06255    81 GE-----DLDQSFPGDPDGLITERMAHALFSE-VKEVADYLIDFHTGgtpFDANPYTVYkLFPESGPVEEkrlLRLARAf 154

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1330281852 187 -MQPDCVLNDPGD--------PGILETVWNRSGIPSITVEVGMGKFTQPDMIQRAVDGVLNMLSYYEML 246
Cdd:cd06255   155 gVHANCRVDVSGAggelpgntAGALDYQCMAQGIPAFMVELGGGGRAEEEAVRFAARGLRNLLRYLGML 223
M14_ASTE_ASPA-like cd06252
Peptidase M14 Succinylglutamate desuccinylase (ASTE)/aspartoacylase (ASPA)-like; ...
 46-246 1.07e-27

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: 107.66  E-value: 1.07e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330281852  46 MPVSVFKGsQDGPKLMITAGIHGDELNGVLAAQQIIRDLVGKTLKGTVTIVPTVNLSGLLNHSRDfiSSDPGscpANLNR 125
Cdd:cd06252    24 IPITVINN-GSGPTVLLTGGNHGDEYEGPIALRRLARDLDPEDVRGRLIIVPALNLPAVRAGTRT--SPLDG---GNLNR 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330281852 126 LFPGDENGLAAER---FVSS-LWERllkhnATFAVDLHTQTRGAVYPLYVFADY-----RIEQCLDMARLMQ-PDC-VLN 194
Cdd:cd06252    98 AFPGDADGTPTERiahFLETvLLPR-----ADAVIDLHSGGSSLDFVPCAAVHLlpdpaQRARSLALAEAFGaPLSvVVD 172

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1330281852 195 DPGDPGILETVWNRSGIPSITVEVGMGKFTQPDMIQRAVDGVLNMLSYYEML 246
Cdd:cd06252   173 NVDAPGTLDSAAERAGKIFVSTELGGGGTVTPAALRIAERGVLNVLIHLGVL 224
M14_ASTE_ASPA_like cd18174
Peptidase M14 Succinylglutamate desuccinylase (ASTE)/aspartoacylase (ASPA)-like; ...
 60-240 8.94e-27

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: 104.25  E-value: 8.94e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330281852  60 LMITAGIHGDELNGVLAAQQIIRDLVGKTLKGTVTIVPTVNLSGLLNHSrdfissdPGSCPA---NLNRLFPGDENGLAA 136
Cdd:cd18174     1 LLVTAGVHGYEYASIEALQRLIKELDPAKLSGTVIVVPIANIPAFEGRS-------IYVNPLdgkNLNRSFPGDPDGTPT 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330281852 137 ERFVSSLWERLLKhNATFAVDLHT-QTRGAVYPlYVFADYRIEQCLD-----MARLMQPDCVLNDPGDPGILE------T 204
Cdd:cd18174    74 ERLAHWLTTNVIA-RADYYIDLHGgDLNEDLRP-FVYYYETGNAALDaasreMAEAFGLDHIVFYKARLKASRgslytqA 151

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1330281852 205 VWNRSGIPSITVEVG-MGKfTQPDMIQRAVDGVLNML 240
Cdd:cd18174   152 AALLRGIPAILVEAGgLGS-RDEEDVARHVEGVLNVL 187
M14_ASTE_ASPA-like cd06253
Peptidase M14 Succinylglutamate desuccinylase (ASTE)/aspartoacylase (ASPA)-like; ...
 40-242 6.54e-26

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: 102.68  E-value: 6.54e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330281852  40 LGQPKNMPVSVFKGSQDGPKLMITAGIHGDELNGVLAAQQIIRDL-----VGKTLKGTVTIVPTVNLSGLLNHSRD--FI 112
Cdd:cd06253     5 FREPLEVKGFRFGGGNAEPRIAIVAGIHGDELNGLYVCSRLIRFLkeleeGGYKLKGKVLVIPAVNPLGINSGTRFwpFD 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330281852 113 SSDpgscpanLNRLFPGDENGLAAERFVSSLWERLLkhNATFAVDLHTQtrgavyplYVFADY----RI-----EQCLDM 183
Cdd:cd06253    85 NLD-------MNRMFPGYNKGETTERIAAALFEDLK--GADYGIDLHSS--------NDFLREipqvRViesgaQDLLPL 147

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1330281852 184 ARLMQPDCVLNDPG---DPGILETVWNRSGIPSITVEVGMGKFTQPDMIQRAVDGVLNMLSY 242
Cdd:cd06253   148 AKFLGLDVVWVHPAstvDTGTLAYNWNEWGTKALVLEMGVGMRIDKEYCEQLFEGILRFLLK 209
M14_PaAOTO_like cd06250
Peptidase M14 Succinylglutamate desuccinylase (ASTE)/aspartoacylase (ASPA)-like subfamily; ...
 33-242 2.74e-14

Peptidase M14 Succinylglutamate desuccinylase (ASTE)/aspartoacylase (ASPA)-like subfamily; subgroup includes Pseudomonas aeruginosa AotO; An uncharacterized subgroup of the Succinylglutamate desuccinylase (ASTE)/aspartoacylase (ASPA) subfamily which is part of the the M14 family of metallocarboxypeptidases. This subgroup includes Pseudomonas aeruginosa AotO and related proteins. 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. The gene encoding P. aeruginosa AotO was characterized as part of an operon encoding an arginine and ornithine transport system, however it is not essential for arginine and ornithine uptake.


Pssm-ID: 349468  Cd Length: 267  Bit Score: 71.88  E-value: 2.74e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330281852  33 FQVTSDGLGQPKNMPVSVFKGSQDGPKLMITAGIHGDELNGVLAAQQIIR-----DLVGKtLKGTVTIVPTVNLSGLLNH 107
Cdd:cd06250     3 IPLDSPAPGTERSLTVFRFGGAGAGPKVYIQAALHADELPGNLVIHHLLErlkalEAAGR-IKGEIVLVPQANPIGLSQK 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330281852 108 SR-------DFISSDpgscpaNLNRLFP------GDENG---------------------LAAERFVSSLwERL------ 147
Cdd:cd06250    82 IGgyhqgrfDLATGD------NFNRNFPdlakavAARVEerlgddaaanvaliraalkeaLDALPPRTEL-QRLkltllr 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330281852 148 LKHNATFAVDLHTQTRGAVYpLYVfADYRIEQCLDMARLMQPDCVL--NDPGDPGILET---VWNR-----------SGI 211
Cdd:cd06250   155 LALDADIVLDLHCDDEALRH-LYT-PPALWPAAEDLAAALGAPAVLlaDNSGGGAFDEAfskPWLRlaeafpgapipLAC 232

                         250       260       270
                  ....*....|....*....|....*....|.
gi 1330281852 212 PSITVEVGMGKFTQPDMIQRAVDGVLNMLSY 242
Cdd:cd06250   233 FSATVELRGQADVDDELARADAEGILRFLAA 263
Peptidase_M14_like cd00596
M14 family of metallocarboxypeptidases and related proteins; The M14 family of ...
 60-234 3.25e-11

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: 62.09  E-value: 3.25e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330281852  60 LMITAGIHGDELNGVLAAQQIIRDLVGKTLKGTVT---------IVPTVNLSGLLNHSRDFISSdpGSCPANLNRLFPGD 130
Cdd:cd00596     1 ILITGGIHGNEVIGVELALALIEYLLENYGNDPLKrlldnvelwIVPLVNPDGFARVIDSGGRK--NANGVDLNRNFPYN 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330281852 131 EN-------------GLAAE-----RFVSSLWERllkHNATFAVDLHTQTRGAVYP----LYVFADYRI--EQCLDMARL 186
Cdd:cd00596    79 WGkdgtsgpssptyrGPAPFsepetQALRDLAKS---HRFDLAVSYHSSSEAILYPygytNEPPPDFSEfqELAAGLARA 155

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1330281852 187 MQPDCVLNDPGDPGILET------VWNRSGIPSITVEVG-MGKFTQPDMIQRAVD 234
Cdd:cd00596   156 LGAGEYGYGYSYTWYSTTgtaddwLYGELGILAFTVELGtADYPLPGTLLDRRLE 210
M14_ASTE_ASPA_like cd18430
Succinylglutamate desuccinylase/aspartoacylase; uncharacterized; A functionally ...
 60-219 1.24e-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: 59.38  E-value: 1.24e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330281852  60 LMITAGIHGDELNGVLAAQQIIRDLV-GKTLKGTVTIVPTVNLSgllnhsrdfISSDPGSCPANLNRLFPGDENGLAAE- 137
Cdd:cd18430     1 LAVLGAVHGNETCGTRAVERLLAELPsGALQKGPVTLVPANERA---------YAEGVRFCEEDLNRVFPGDPDPDTYEr 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330281852 138 RFVSSLWERLLKHNATFavDLH-TQTRGavyPLYVFADYRIEQCLDMARlmqpdCVLNDPGDPgILETVWNRS------- 209
Cdd:cd18430    72 RLANRLCPELEGHDVVL--DLHsTHSGG---QPFAILDYGDKASRRLAR-----SVGIPKGWR-VVYGRDLGYahgggkt 140

                         170
                  ....*....|
gi 1330281852 210 GIPSITVEVG 219
Cdd:cd18430   141 EVTGVTVECG 150
M14_REP34-like cd06231
Peptidase M14-like domain similar to rapid encystment phenotype 34 (REP34); This family ...
 53-174 3.57e-09

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: 56.55  E-value: 3.57e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330281852  53 GSQDGPKLMITAGIHGDELNGVLAAQQIIRDLVGKTLKG-TVTIVPTVNLSGLLNHSRDfissdpGSCPANLNRLF---P 128
Cdd:cd06231    38 PRGDKPRVLISAGIHGDEPAGVEALLRFLESLAEKYLRRvNLLVLPCVNPWGFERNTRE------NADGIDLNRSFlkdS 111

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1330281852 129 GDENGLAAERFVSSLWERLLkhnatfAVDLH--TQTRGaVYpLYVFAD 174
Cdd:cd06231   112 PSPEVRALMEFLASLGRFDL------HLDLHedWDSDG-FY-LYELGP 151
M14_MpaA-like cd06904
Peptidase M14-like domain of Escherichia coli Murein Peptide Amidase A and related proteins; ...
 44-240 3.90e-09

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: 56.13  E-value: 3.90e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330281852  44 KNMPVSVFK-GSQDGPKLMITAGIHGDELNGVLAAQQIIRDLVGKTLKG--TVTIVPTVNLSGLLNHS----------RD 110
Cdd:cd06904     9 KGRPILAYKfGPGSRARILIIGGIHGDEPEGVSLVEHLLRWLKNHPASGdfHIVVVPCLNPDGLAAGTrtnangvdlnRN 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330281852 111 FISSD--PGSCPANLNRLFPGDENGLAAE-RFVSSLWERLlkhNATFAVDLHTqtrgavyPLYVFADYRIEQCLdmARLM 187
Cdd:cd06904    89 FPTKNwePDARKPKDPRYYPGPKPASEPEtRALVELIERF---KPDRIISLHA-------PYLVNYDGPAKSLL--AEKL 156

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1330281852 188 QPDCVLNDPGD----PGILET-VWNRSGIPSITVEVGMGKfTQPDMIQRAVDGVLNML 240
Cdd:cd06904   157 AQATGYPVVGDvgytPGSLGTyAGIERNIPVITLELPEAV-SIDELWQDLKRALIEAI 213
AstE COG2988
Succinylglutamate desuccinylase [Amino acid transport and metabolism];
57-253 1.24e-08

Succinylglutamate desuccinylase [Amino acid transport and metabolism];


Pssm-ID: 442227  Cd Length: 305  Bit Score: 55.62  E-value: 1.24e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330281852  57 GPKLMITAGIHGDELNGVLAAQQIIRDLVgktlkgTVTIVPTVNLSGLL------NHSRDFIssdpgscPANLNRLFPGD 130
Cdd:COG2988    24 IKAVVISGGIHGNETAPIELLDKLLQDLL------LGERPLSFRLLLILgnpaamRAGRRYL-------DEDLNRLFGGR 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330281852 131 --ENGLAAERF-----VSSLWERLLKHNATFAV-DLHTQTRGAVYPLyvFADYRIEQ---CLDMARLMQ---PDCVL--N 194
Cdd:COG2988    91 hlQNPESYEAArakelEQAVGPFFAAGGRVRLHiDLHTAIRNSGHER--FAVYPFRGrpfDLALLAYLAaagPEAVVlhH 168

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1330281852 195 DPG--DPGILETVWNRSGipsITVEVG-MGKFTQPDM--IQRAVDGVLNMLSYYEMLEVDGQDP 253
Cdd:COG2988   169 APGgtFSHFSAELCGAQA---FTLELGkVRPFGQNDLsrFAATEEALRALLSGAELPEHPAQDL 229
M14_CP_Csd4-like cd06243
Peptidase M14 carboxypeptidase Csd4 and similar proteins; This family includes peptidase M14 ...
 47-116 2.80e-08

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: 53.52  E-value: 2.80e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1330281852  47 PVSVFKGSQDGPKLMITAGIHGDELNGVLAAqQIIRDLvgKTLKGTVTIVPTVNL-SGLLNH-------SRDFISSDP 116
Cdd:cd06243     6 PFTRLEGREPGPTLLIIGGIQGDEPGGFLAA-DLLADL--YLVKGNVIVVPRLNFpSILRNHrglngdmNRKFAALDK 80
MpaA COG2866
Murein tripeptide amidase MpaA [Cell wall/membrane/envelope biogenesis];
58-177 6.21e-07

Murein tripeptide amidase MpaA [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442113 [Multi-domain]  Cd Length: 337  Bit Score: 50.46  E-value: 6.21e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330281852  58 PKLMITAGIHGDELNGVLAAQQIIRDLVG-------KTLKG-TVTIVPTVNLSGLLNHSRDFISsdpgscPANLNRLFPg 129
Cdd:COG2866    66 PKVLLNAQQHGNEWTGTEALLGLLEDLLDnydplirALLDNvTLYIVPMLNPDGAERNTRTNAN------GVDLNRDWP- 138

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1330281852 130 deNGLAAERFVSSLWERLLKHNATFAVDLHTQtRGAVYPLYVFADYRI 177
Cdd:COG2866   139 --APWLSEPETRALRDLLDEHDPDFVLDLHGQ-GELFYWFVGTTEPTG 183
M14_ASTE cd03855
Peptidase M14 Succinylglutamate desuccinylase (ASTE) subfamily; Peptidase M14 ...
 60-175 2.88e-06

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: 47.58  E-value: 2.88e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330281852  60 LMITAGIHGDElngvLAAQQIIRDLVGKTLKGTVTI-VPTV----NLSGLLNHSRdFISsdpgscpANLNRLFPGDENGL 134
Cdd:cd03855    46 VVLSAGIHGNE----TAPIEILDQLINDLIRGELALaHRLLfifgNPPAIRQGKR-FIE-------ENLNRLFSGRHSKL 113

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1330281852 135 --------------AAERFVSSLWERLLKHnatfaVDLHTQTRGAVYPlyVFADY 175
Cdd:cd03855   114 ppsyetaraaeleqAVADFFAKASGEVRWH-----LDLHTAIRGSKHE--QFAVY 161
M14_ASTE_ASPA-like cd06256
Peptidase M14 Succinylglutamate desuccinylase (ASTE)/aspartoacylase (ASPA)-like; ...
 55-219 3.36e-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: 349474  Cd Length: 204  Bit Score: 44.21  E-value: 3.36e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330281852  55 QDGPKLMITAGIHGDELNGVLAAQQIIRDLvGKTLKGTVTIVpTVNLSG------LLNHSRDFissdpgscpanlNRLFP 128
Cdd:cd06256    32 RRPRPLFVSTLLHGNEPTGLRAVQRLLKTG-QAPLPRTLLLF-IGNVDAakagvrRLPGQPDY------------NRCWP 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330281852 129 G----DENGLAAErfvssLWERLLKHNATFAVDLHTQTrgAVYPLYVFADYRIEQCLDMARLMQPDCVLNDPGDpGILET 204
Cdd:cd06256    98 GpfetPEGRLAAA-----VLERLDTLRPFASIDIHNNT--GKNPHYACVNRLDAAHLRLASLFSRTLVYFTRPL-GVLSE 169

                         170
                  ....*....|....*
gi 1330281852 205 VWNRsGIPSITVEVG 219
Cdd:cd06256   170 ALAA-LCPAVTVECG 183
Zn_pept smart00631
Zn_pept domain;
58-168 1.17e-04

Zn_pept domain;


Pssm-ID: 214748 [Multi-domain]  Cd Length: 277  Bit Score: 43.09  E-value: 1.17e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330281852   58 PKLMITAGIHGDELNGVLAAQQIIRDLV---------GKTLKGT-VTIVPTVNLSGL-LNHSRDFIS----SDPGSC-PA 121
Cdd:smart00631  50 PAIFIDAGIHAREWIGPATALYLINQLLenygrdprvTNLLDKTdIYIVPVLNPDGYeYTHTGDRLWrknrSPNSNCrGV 129

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1330281852  122 NLNRLFPGDEN-----------GLAAE-----RFVSSLWERLLkhNATFAVDLHTQTRGAVYP 168
Cdd:smart00631 130 DLNRNFPFHWGetgnpcsetyaGPSPFsepetKAVRDFIRSNR--RFKLYIDLHSYSQLILYP 190
PRK05324 PRK05324
succinylglutamate desuccinylase; Provisional
 60-168 4.95e-04

succinylglutamate desuccinylase; Provisional


Pssm-ID: 235408  Cd Length: 329  Bit Score: 41.32  E-value: 4.95e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330281852  60 LMITAGIHGDE------LNgvlaaqQIIRDLvgktLKGtvTIVPTV-------NLSGLLNHSRdFISSDpgscpanLNRL 126
Cdd:PRK05324   50 LVLSAGIHGNEtapielLD------QLVRDL----LAG--ELPLRArllvilgNPPAMRAGKR-YLDED-------LNRL 109

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1330281852 127 F--------PGDENGLAAE------RFVSSLWERLLKHnatfaVDLHTQTRG------AVYP 168
Cdd:PRK05324  110 FggrhqqfpGSDEARRAAEleqaveDFFAAGAERVRWH-----YDLHTAIRGskheqfAVLP 166
M14-like cd06242
Peptidase M14-like domain; uncharacterized subgroup; Peptidase M14-like domain of a ...
 57-109 5.06e-04

Peptidase M14-like domain; uncharacterized subgroup; Peptidase M14-like domain of 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: 349461 [Multi-domain]  Cd Length: 220  Bit Score: 40.75  E-value: 5.06e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1330281852  57 GPKLMITAGIHGDELNGVLAAQQIIRDLVGKTL------KGTVTIVPTVNLSGLLNHSR 109
Cdd:cd06242     1 KPTVLLVGQQHGNEPAGREAALALARDLAFGDDarelleKVNVLVVPRANPDGRAANTR 59
 
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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