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Conserved domains on  [gi|1083056171|gb|OGD55916|]
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hypothetical protein A3K81_04970 [Candidatus Bathyarchaeota archaeon RBG_13_60_20]

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];
22-315 1.13e-82

Predicted deacylase [General function prediction only];


:

Pssm-ID: 442826 [Multi-domain]  Cd Length: 296  Bit Score: 251.69  E-value: 1.13e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083056171  22 AGTTSVNTYRVPLAVINGSRKGKTIGIIGGTHGTEFASIDAVIRAIKELDPKKMKGTVLAVPVLNGPQFEHKTQFLsPFD 101
Cdd:COG3608     5 SRLASGTPVSLPVTVFRGAGPGPTLLITAGIHGDELNGIEALRRLLRELDPGELRGTVILVPVANPPGFLQGSRYL-PID 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083056171 102 QLNQNRVFPGDKEGTLTHRIAYTVFENVIKRCDALLDCHGGDINEDIRGFTLAGKGDDEAvnkvaLDMARCFPARYINLF 181
Cdd:COG3608    84 GRDLNRSFPGDADGSLAERIAHALFEEILPDADYVIDLHSGGIARDNLPHVRAGPGDEEL-----RALARAFGAPVILDS 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083056171 182 QVAPTGLSMCAQARLGIPCVISEAGTPFPVREDEVRFHYEGIMNVLRYFGVIEGKP---RMVEPVTSKGSARLRAEQGGI 258
Cdd:COG3608   159 PEGGDGSLREAAAEAGIPALTLELGGGGRFDEESIEAGVRGILNVLRHLGMLDGEApppPLAPPVLARGSEWVRAPAGGL 238

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1083056171 259 WKPAVSTDQMVKAGDVLGVVTDLFGEVKQTVKAPHGGVVGMMRCFYSVNCGESLVSV 315
Cdd:COG3608   239 FEPLVELGDRVKKGDVLGRITDPFGEEVEEVRAPVDGIVIGRRTNPLVNPGDALFHI 295
 
Name Accession Description Interval E-value
COG3608 COG3608
Predicted deacylase [General function prediction only];
22-315 1.13e-82

Predicted deacylase [General function prediction only];


Pssm-ID: 442826 [Multi-domain]  Cd Length: 296  Bit Score: 251.69  E-value: 1.13e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083056171  22 AGTTSVNTYRVPLAVINGSRKGKTIGIIGGTHGTEFASIDAVIRAIKELDPKKMKGTVLAVPVLNGPQFEHKTQFLsPFD 101
Cdd:COG3608     5 SRLASGTPVSLPVTVFRGAGPGPTLLITAGIHGDELNGIEALRRLLRELDPGELRGTVILVPVANPPGFLQGSRYL-PID 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083056171 102 QLNQNRVFPGDKEGTLTHRIAYTVFENVIKRCDALLDCHGGDINEDIRGFTLAGKGDDEAvnkvaLDMARCFPARYINLF 181
Cdd:COG3608    84 GRDLNRSFPGDADGSLAERIAHALFEEILPDADYVIDLHSGGIARDNLPHVRAGPGDEEL-----RALARAFGAPVILDS 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083056171 182 QVAPTGLSMCAQARLGIPCVISEAGTPFPVREDEVRFHYEGIMNVLRYFGVIEGKP---RMVEPVTSKGSARLRAEQGGI 258
Cdd:COG3608   159 PEGGDGSLREAAAEAGIPALTLELGGGGRFDEESIEAGVRGILNVLRHLGMLDGEApppPLAPPVLARGSEWVRAPAGGL 238

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1083056171 259 WKPAVSTDQMVKAGDVLGVVTDLFGEVKQTVKAPHGGVVGMMRCFYSVNCGESLVSV 315
Cdd:COG3608   239 FEPLVELGDRVKKGDVLGRITDPFGEEVEEVRAPVDGIVIGRRTNPLVNPGDALFHI 295
M14_ASTE_ASPA_like cd18174
Peptidase M14 Succinylglutamate desuccinylase (ASTE)/aspartoacylase (ASPA)-like; ...
 46-227 1.81e-82

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: 247.54  E-value: 1.81e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083056171  46 IGIIGGTHGTEFASIDAVIRAIKELDPKKMKGTVLAVPVLNGPQFEHKTQFLSPFDQLNQNRVFPGDKEGTLTHRIAYTV 125
Cdd:cd18174     1 LLVTAGVHGYEYASIEALQRLIKELDPAKLSGTVIVVPIANIPAFEGRSIYVNPLDGKNLNRSFPGDPDGTPTERLAHWL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083056171 126 FENVIKRCDALLDCHGGDINEDIRGFTLAGKGDDEAVNKVALDMARCFPARYINLFQVAP---TGLSMCAQA--RLGIPC 200
Cdd:cd18174    81 TTNVIARADYYIDLHGGDLNEDLRPFVYYYETGNAALDAASREMAEAFGLDHIVFYKARLkasRGSLYTQAAalLRGIPA 160

                         170       180
                  ....*....|....*....|....*..
gi 1083056171 201 VISEAGTPFPVREDEVRFHYEGIMNVL 227
Cdd:cd18174   161 ILVEAGGLGSRDEEDVARHVEGVLNVL 187
AstE_AspA pfam04952
Succinylglutamate desuccinylase / Aspartoacylase family; This family includes ...
 43-297 2.31e-28

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: 110.90  E-value: 2.31e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083056171  43 GKTIGIIGGTHGTEFASIDAVIRAIKELDPKKMKGTVLAVPVLNGPQFEHKTQFLspfDQlNQNRVFPGDKEG------- 115
Cdd:pfam04952   2 GPTLLLSAGIHGNETNGVELLRRLLRQLDPGDIAGERTLVPLANPPAFRAGSRYI---PR-DLNRSFPGRALGassdepy 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083056171 116 --TLTHRIAYTVFENVIKRCDALLDCHGGDINediRGFTLAGKGDDEAVNKVALDMARCFPARYI-NLFQVAPTGLSMCA 192
Cdd:pfam04952  78 raTRAERLADLFFPALLPRADIVLDLHTGTRG---MGHLLFALAPIRDDPLHLLALLRAFGAPAVlKLHSKPSAGFSAFS 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083056171 193 QARLGIPCVISEAGTPFPVREDEVRFHYEGIMNVLRYFGVIEGKPRMVEP-------VTSKGSARLRAEQGGIWKPAVST 265
Cdd:pfam04952 155 AEELGAPGFTLELGGAGPFGANLISRTAAGVLNVLRLIGVLNGGPDAFEPpklyrvlREIDRPRDIRAELAGLVEFALNL 234

                         250       260       270
                  ....*....|....*....|....*....|....
gi 1083056171 266 DQMVKAGDVL--GVVTDLFGEVKQTVKAPHGGVV 297
Cdd:pfam04952 235 GDDVDAGPLLpgGPLFAPFGGEETEYRAPEDGYP 268
 
Name Accession Description Interval E-value
COG3608 COG3608
Predicted deacylase [General function prediction only];
22-315 1.13e-82

Predicted deacylase [General function prediction only];


Pssm-ID: 442826 [Multi-domain]  Cd Length: 296  Bit Score: 251.69  E-value: 1.13e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083056171  22 AGTTSVNTYRVPLAVINGSRKGKTIGIIGGTHGTEFASIDAVIRAIKELDPKKMKGTVLAVPVLNGPQFEHKTQFLsPFD 101
Cdd:COG3608     5 SRLASGTPVSLPVTVFRGAGPGPTLLITAGIHGDELNGIEALRRLLRELDPGELRGTVILVPVANPPGFLQGSRYL-PID 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083056171 102 QLNQNRVFPGDKEGTLTHRIAYTVFENVIKRCDALLDCHGGDINEDIRGFTLAGKGDDEAvnkvaLDMARCFPARYINLF 181
Cdd:COG3608    84 GRDLNRSFPGDADGSLAERIAHALFEEILPDADYVIDLHSGGIARDNLPHVRAGPGDEEL-----RALARAFGAPVILDS 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083056171 182 QVAPTGLSMCAQARLGIPCVISEAGTPFPVREDEVRFHYEGIMNVLRYFGVIEGKP---RMVEPVTSKGSARLRAEQGGI 258
Cdd:COG3608   159 PEGGDGSLREAAAEAGIPALTLELGGGGRFDEESIEAGVRGILNVLRHLGMLDGEApppPLAPPVLARGSEWVRAPAGGL 238

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1083056171 259 WKPAVSTDQMVKAGDVLGVVTDLFGEVKQTVKAPHGGVVGMMRCFYSVNCGESLVSV 315
Cdd:COG3608   239 FEPLVELGDRVKKGDVLGRITDPFGEEVEEVRAPVDGIVIGRRTNPLVNPGDALFHI 295
M14_ASTE_ASPA_like cd18174
Peptidase M14 Succinylglutamate desuccinylase (ASTE)/aspartoacylase (ASPA)-like; ...
 46-227 1.81e-82

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: 247.54  E-value: 1.81e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083056171  46 IGIIGGTHGTEFASIDAVIRAIKELDPKKMKGTVLAVPVLNGPQFEHKTQFLSPFDQLNQNRVFPGDKEGTLTHRIAYTV 125
Cdd:cd18174     1 LLVTAGVHGYEYASIEALQRLIKELDPAKLSGTVIVVPIANIPAFEGRSIYVNPLDGKNLNRSFPGDPDGTPTERLAHWL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083056171 126 FENVIKRCDALLDCHGGDINEDIRGFTLAGKGDDEAVNKVALDMARCFPARYINLFQVAP---TGLSMCAQA--RLGIPC 200
Cdd:cd18174    81 TTNVIARADYYIDLHGGDLNEDLRPFVYYYETGNAALDAASREMAEAFGLDHIVFYKARLkasRGSLYTQAAalLRGIPA 160

                         170       180
                  ....*....|....*....|....*..
gi 1083056171 201 VISEAGTPFPVREDEVRFHYEGIMNVL 227
Cdd:cd18174   161 ILVEAGGLGSRDEEDVARHVEGVLNVL 187
M14_ASTE_ASPA-like cd06254
Peptidase M14 Succinylglutamate desuccinylase (ASTE)/aspartoacylase (ASPA)-like; ...
 33-230 3.50e-62

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: 195.88  E-value: 3.50e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083056171  33 PLAVINGSRKGKTIGIIGGTHGTEFASIDAVIRAIKELDPKKMKGTVLAVPVLNGPQFEHKTQFLSPFDQLNQNRVFPGD 112
Cdd:cd06254     1 PVTLINGAKPGPTLLITAGIHGGEYPGILAAIRLARELDPADVKGTLIIVHIANVSGFEARTPFVVPEDGKNLNRVFPGD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083056171 113 KEGTLTHRIAYTVFENVIKRCDALLDCHGGDINEDIRGFTLAGKGDDEAVNKVALDMARCFPARYINLFQVAPTGLSMCA 192
Cdd:cd06254    81 PDGTLTERIAYFLTREIISRADFLIDLHGGDANEALTPFVYYPGGASEEVNDISRAAAQALGLPYIVISSSEKGTGYYSY 160

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1083056171 193 QARLGIPCVISEAGTPFPVREDEVRFHYEGIMNVLRYF 230
Cdd:cd06254   161 AALRGIPSILVERGGLGTCDEEDVQAHKDGIKNLLRHL 198
M14_ASTE_ASPA-like cd06251
Peptidase M14 Succinylglutamate desuccinylase (ASTE)/aspartoacylase (ASPA)-like; ...
 32-233 1.69e-48

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: 160.78  E-value: 1.69e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083056171  32 VPLAVINGSRKGKTIGIIGGTHGTEFASIDAVIRAIKELDPKKMKGTVLAVPVLNGPQFEHKTQFLsPFDQLNQNRVFPG 111
Cdd:cd06251     1 VPVLVARGAKPGPTLLLTAAIHGDELNGIEVIQRLLEDLDPSKLRGTLIAIPVVNPLGFENNSRYL-PDDGRDLNRSFPG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083056171 112 DKEGTLTHRIAYTVFENVIKRCDALLDCHGGDINEDIRGFTLAgKGDDEAVNKvaldMARCFPARYINLFQVAPTGLSMC 191
Cdd:cd06251    80 SEKGSLASRLAHLLWNEIVKKADYVIDLHTASTGRTNLPYVRA-DLRDPESRR----MAEAFGAPVIVDDPGEDGSLRGA 154

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1083056171 192 AqARLGIPCVISEAGTPFPVREDEVRFHYEGIMNVLRYFGVI 233
Cdd:cd06251   155 A-VELGIPAITVELGEALRFDEDIIRRGVEGVLNVLRHLGML 195
M14_ASTE_ASPA-like cd06255
Peptidase M14 Succinylglutamate desuccinylase (ASTE)/aspartoacylase (ASPA)-like; ...
 31-233 1.36e-38

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: 135.92  E-value: 1.36e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083056171  31 RVPLAVINGSRKGKTIGIIGGTHGTEFASIDAVIRAIKELDPKKMKGTVLAVPVLNGPQFEHKTQFlSPFDQLNQNRVFP 110
Cdd:cd06255    11 TIPVIVVRGAKPGPCLWINGAVHGDELNGPLAALELFRELDPAQLSGTLVATPIANPLAFQGRQKF-SPQDGEDLDQSFP 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083056171 111 GDKEGTLTHRIAYTVFENVIKRCDALLDCHGGDINEDIRGFTLAG--KGDDEAVNKVALDMARCFPARYINLFQVAP--- 185
Cdd:cd06255    90 GDPDGLITERMAHALFSEVKEVADYLIDFHTGGTPFDANPYTVYKlfPESGPVEEKRLLRLARAFGVHANCRVDVSGagg 169

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1083056171 186 ------TGLSMCAQARLGIPCVISEAGTPFPVREDEVRFHYEGIMNVLRYFGVI 233
Cdd:cd06255   170 elpgntAGALDYQCMAQGIPAFMVELGGGGRAEEEAVRFAARGLRNLLRYLGML 223
M14_ASTE_ASPA-like cd06252
Peptidase M14 Succinylglutamate desuccinylase (ASTE)/aspartoacylase (ASPA)-like; ...
 31-233 8.00e-38

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: 134.24  E-value: 8.00e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083056171  31 RVPLAVINGsRKGKTIGIIGGTHGTEFASIDAVIRAIKELDPKKMKGTVLAVPVLNGPQFEHKTQfLSPFDQLNQNRVFP 110
Cdd:cd06252    23 PIPITVINN-GSGPTVLLTGGNHGDEYEGPIALRRLARDLDPEDVRGRLIIVPALNLPAVRAGTR-TSPLDGGNLNRAFP 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083056171 111 GDKEGTLTHRIAYTVFENVIKRCDALLDCHGGDINEDIRGFTLAGKGDDEAVNKVALDMARCFPARYINLFQ-VAPTGLS 189
Cdd:cd06252   101 GDADGTPTERIAHFLETVLLPRADAVIDLHSGGSSLDFVPCAAVHLLPDPAQRARSLALAEAFGAPLSVVVDnVDAPGTL 180

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1083056171 190 MCAQARLGIPCVISEAGTPFPVREDEVRFHYEGIMNVLRYFGVI 233
Cdd:cd06252   181 DSAAERAGKIFVSTELGGGGTVTPAALRIAERGVLNVLIHLGVL 224
M14_ASTE_ASPA_like cd06230
Peptidase M14 Succinylglutamate desuccinylase (ASTE)/aspartoacylase (ASPA) subfamily; The ...
 48-226 8.91e-37

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: 129.74  E-value: 8.91e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083056171  48 IIGGTHGTEFASIDAVIRAIKELDPKKMKGTVLAVPVLNGPQFEHKTQFlSPFDQLNQNRVFPGDKEGTLTHRIAYTVFE 127
Cdd:cd06230     3 ILAGVHGDEYEGVEAIRRLLAELDPSELKGTVVLVPVANPPAFEAGTRY-TPLDGLDLNRIFPGDPDGSPTERLAHELTE 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083056171 128 NVIKRCDALLDCHGGDINeDIRGFTLagKGDDEAVNKVALDMARCFPARYINLFQVAPTGLSMCAQARLGIPCVISEAGT 207
Cdd:cd06230    82 LILKHADALIDLHSGGTG-RLVPYAI--LDYDSDAREKSRELARAFGGTPVIWGGDPPGGTPVAAARSAGIPAITVELGG 158

                         170
                  ....*....|....*....
gi 1083056171 208 PFPVREDEVRFHYEGIMNV 226
Cdd:cd06230   159 GGRLRAERLERYLRGIRNV 177
AstE_AspA pfam04952
Succinylglutamate desuccinylase / Aspartoacylase family; This family includes ...
 43-297 2.31e-28

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: 110.90  E-value: 2.31e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083056171  43 GKTIGIIGGTHGTEFASIDAVIRAIKELDPKKMKGTVLAVPVLNGPQFEHKTQFLspfDQlNQNRVFPGDKEG------- 115
Cdd:pfam04952   2 GPTLLLSAGIHGNETNGVELLRRLLRQLDPGDIAGERTLVPLANPPAFRAGSRYI---PR-DLNRSFPGRALGassdepy 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083056171 116 --TLTHRIAYTVFENVIKRCDALLDCHGGDINediRGFTLAGKGDDEAVNKVALDMARCFPARYI-NLFQVAPTGLSMCA 192
Cdd:pfam04952  78 raTRAERLADLFFPALLPRADIVLDLHTGTRG---MGHLLFALAPIRDDPLHLLALLRAFGAPAVlKLHSKPSAGFSAFS 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083056171 193 QARLGIPCVISEAGTPFPVREDEVRFHYEGIMNVLRYFGVIEGKPRMVEP-------VTSKGSARLRAEQGGIWKPAVST 265
Cdd:pfam04952 155 AEELGAPGFTLELGGAGPFGANLISRTAAGVLNVLRLIGVLNGGPDAFEPpklyrvlREIDRPRDIRAELAGLVEFALNL 234

                         250       260       270
                  ....*....|....*....|....*....|....
gi 1083056171 266 DQMVKAGDVL--GVVTDLFGEVKQTVKAPHGGVV 297
Cdd:pfam04952 235 GDDVDAGPLLpgGPLFAPFGGEETEYRAPEDGYP 268
M14_ASTE_ASPA-like cd06253
Peptidase M14 Succinylglutamate desuccinylase (ASTE)/aspartoacylase (ASPA)-like; ...
 29-231 3.82e-19

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: 84.19  E-value: 3.82e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083056171  29 TYRVPLAVIN----GSRKGKTIGIIGGTHGTEFASI---DAVIRAIKELDPK--KMKGTVLAVPVLNGPQFEHKTQFlSP 99
Cdd:cd06253     4 PFREPLEVKGfrfgGGNAEPRIAIVAGIHGDELNGLyvcSRLIRFLKELEEGgyKLKGKVLVIPAVNPLGINSGTRF-WP 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083056171 100 FDQLNQNRVFPGDKEGTLTHRIAYTVFENvIKRCDALLDCHGGDINED----IRGFtlagkgddEAVNKVALDMARCFPA 175
Cdd:cd06253    83 FDNLDMNRMFPGYNKGETTERIAAALFED-LKGADYGIDLHSSNDFLReipqVRVI--------ESGAQDLLPLAKFLGL 153

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1083056171 176 RYINLFQVAP--TGLSMCAQARLGIPCVISEAGTPFPVREDEVRFHYEGIMNVLRYFG 231
Cdd:cd06253   154 DVVWVHPASTvdTGTLAYNWNEWGTKALVLEMGVGMRIDKEYCEQLFEGILRFLLKMG 211
M14_ASTE_ASPA_like cd18430
Succinylglutamate desuccinylase/aspartoacylase; uncharacterized; A functionally ...
 48-140 6.84e-05

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: 42.82  E-value: 6.84e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083056171  48 IIGGTHGTEFASIDAVIRAIKELDPKKM-KGTVLAVPVlNGPQFEHKTQFLspfdQLNQNRVFPGDKEGTlTH--RIAYT 124
Cdd:cd18430     3 VLGAVHGNETCGTRAVERLLAELPSGALqKGPVTLVPA-NERAYAEGVRFC----EEDLNRVFPGDPDPD-TYerRLANR 76

                          90
                  ....*....|....*.
gi 1083056171 125 VFEnVIKRCDALLDCH 140
Cdd:cd18430    77 LCP-ELEGHDVVLDLH 91
M14_CP_Csd4-like cd06243
Peptidase M14 carboxypeptidase Csd4 and similar proteins; This family includes peptidase M14 ...
 30-86 6.99e-04

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: 40.42  E-value: 6.99e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1083056171  30 YRVPLAVINGSRKGKTIGIIGGTHGTEfasIDAVIRAIKELDPKKMKGTVLAVPVLN 86
Cdd:cd06243     3 IEKPFTRLEGREPGPTLLIIGGIQGDE---PGGFLAADLLADLYLVKGNVIVVPRLN 56
 
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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