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Conserved domains on  [gi|1155024104|ref|WP_078929315|]
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M14 family metallopeptidase [Succinivibrio dextrinosolvens]

Protein Classification

M14 family metallopeptidase( domain architecture ID 10154712)

M14 family metallopeptidase is a zinc-binding carboxypeptidase which hydrolyzes a single, C-terminal amino acid from a polypeptide chain, and has a recognition site for the free C-terminal carboxyl group

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
M14_ASTE_ASPA-like cd06253
Peptidase M14 Succinylglutamate desuccinylase (ASTE)/aspartoacylase (ASPA)-like; ...
 9-218 1.13e-103

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: 301.83  E-value: 1.13e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1155024104   9 MKSPFRDDFKIIGYTFGEG--KKSLAIVGAMRGDEVAQQYVASQVVRELNSLERKGlISKNVSVTIIPSANPFSMNIEKR 86
Cdd:cd06253     1 LESPFREPLEVKGFRFGGGnaEPRIAIVAGIHGDELNGLYVCSRLIRFLKELEEGG-YKLKGKVLVIPAVNPLGINSGTR 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1155024104  87 FWAMDDTDINRMFPGYDKGETTQRIAAGLFKNLEGFEYGIQLASFYMPGDFIPHVRIIRTAIDDYTDEAKDFGLPYICVS 166
Cdd:cd06253    80 FWPFDNLDMNRMFPGYNKGETTERIAAALFEDLKGADYGIDLHSSNDFLREIPQVRVIESGAQDLLPLAKFLGLDVVWVH 159

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1155024104 167 DPHPFDTTLLNYNWQIWNTKTFSLYGGTNYRIEGLLCKNQVNAILRFMYKHG 218
Cdd:cd06253   160 PASTVDTGTLAYNWNEWGTKALVLEMGVGMRIDKEYCEQLFEGILRFLLKMG 211
 
Name Accession Description Interval E-value
M14_ASTE_ASPA-like cd06253
Peptidase M14 Succinylglutamate desuccinylase (ASTE)/aspartoacylase (ASPA)-like; ...
 9-218 1.13e-103

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: 301.83  E-value: 1.13e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1155024104   9 MKSPFRDDFKIIGYTFGEG--KKSLAIVGAMRGDEVAQQYVASQVVRELNSLERKGlISKNVSVTIIPSANPFSMNIEKR 86
Cdd:cd06253     1 LESPFREPLEVKGFRFGGGnaEPRIAIVAGIHGDELNGLYVCSRLIRFLKELEEGG-YKLKGKVLVIPAVNPLGINSGTR 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1155024104  87 FWAMDDTDINRMFPGYDKGETTQRIAAGLFKNLEGFEYGIQLASFYMPGDFIPHVRIIRTAIDDYTDEAKDFGLPYICVS 166
Cdd:cd06253    80 FWPFDNLDMNRMFPGYNKGETTERIAAALFEDLKGADYGIDLHSSNDFLREIPQVRVIESGAQDLLPLAKFLGLDVVWVH 159

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1155024104 167 DPHPFDTTLLNYNWQIWNTKTFSLYGGTNYRIEGLLCKNQVNAILRFMYKHG 218
Cdd:cd06253   160 PASTVDTGTLAYNWNEWGTKALVLEMGVGMRIDKEYCEQLFEGILRFLLKMG 211
COG3608 COG3608
Predicted deacylase [General function prediction only];
25-307 8.55e-66

Predicted deacylase [General function prediction only];


Pssm-ID: 442826 [Multi-domain]  Cd Length: 296  Bit Score: 208.16  E-value: 8.55e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1155024104  25 GEGKKsLAIVGAMRGDEVAQQYVASQVVRELNSLERKGlisknvSVTIIPSANPFSMNIEKRFWAMDDTDINRMFPGYDK 104
Cdd:COG3608    24 GPGPT-LLITAGIHGDELNGIEALRRLLRELDPGELRG------TVILVPVANPPGFLQGSRYLPIDGRDLNRSFPGDAD 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1155024104 105 GETTQRIAAGLFKN-LEGFEYGIQLASFYMPGDFIPHVRIIRTaiDDYTDE-AKDFGLPYIcVSDPHPFDTTlLNYNWQI 182
Cdd:COG3608    97 GSLAERIAHALFEEiLPDADYVIDLHSGGIARDNLPHVRAGPG--DEELRAlARAFGAPVI-LDSPEGGDGS-LREAAAE 172

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1155024104 183 WNTKTFSLYGGTNYRIEGLLCKNQVNAILRFMYKHGML-LKKSYDPAIASVVVNESdlVVVQAPCAGFFYRKKNAGDFVR 261
Cdd:COG3608   173 AGIPALTLELGGGGRFDEESIEAGVRGILNVLRHLGMLdGEAPPPPLAPPVLARGS--EWVRAPAGGLFEPLVELGDRVK 250

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 1155024104 262 KGDELGRIVDPYeGNVKARISAYVDGIMYFTHDSPLVMQNTPLFKI 307
Cdd:COG3608   251 KGDVLGRITDPF-GEEVEEVRAPVDGIVIGRRTNPLVNPGDALFHI 295
AstE_AspA pfam04952
Succinylglutamate desuccinylase / Aspartoacylase family; This family includes ...
 29-307 2.04e-17

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: 80.47  E-value: 2.04e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1155024104  29 KSLAIVGAMRGDEVAQQYVASQVVRELNSLERKGLIsknvsvTIIPSANPFSMNIEKRFwamDDTDINRMFPGYDKGET- 107
Cdd:pfam04952   3 PTLLLSAGIHGNETNGVELLRRLLRQLDPGDIAGER------TLVPLANPPAFRAGSRY---IPRDLNRSFPGRALGASs 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1155024104 108 --------TQRIAAGLFKN-LEGFEYGIQL-----ASFYMPGDFIPHvRIIRTAIDDYtdeAKDFGLPYICVSDPHPFDT 173
Cdd:pfam04952  74 depyratrAERLADLFFPAlLPRADIVLDLhtgtrGMGHLLFALAPI-RDDPLHLLAL---LRAFGAPAVLKLHSKPSAG 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1155024104 174 TLLNYNWQIWnTKTFSLYGGTNYRIEGLLCKNQVNAILRFMYKHGML---LKKSYDPAIASVVVNESDLVVVQAPCAGFF 250
Cdd:pfam04952 150 FSAFSAEELG-APGFTLELGGAGPFGANLISRTAAGVLNVLRLIGVLnggPDAFEPPKLYRVLREIDRPRDIRAELAGLV 228

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1155024104 251 YRKKNAGDFVRKGDELGR--IVDPYEGNvKARISAYVDGIMYFTHDSPLVMQNTPLFKI 307
Cdd:pfam04952 229 EFALNLGDDVDAGPLLPGgpLFAPFGGE-ETEYRAPEDGYPVFPNEAAYVGKGAALALV 286
Zn_pept smart00631
Zn_pept domain;
19-100 2.19e-04

Zn_pept domain;


Pssm-ID: 214748 [Multi-domain]  Cd Length: 277  Bit Score: 41.94  E-value: 2.19e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1155024104   19 IIGYTFGEGKKSLAIVGAMRGDEV----AQQYVASQVVRELNSLERKGLISKNVSVTIIPSANP--FSMNIEK-RFWAM- 90
Cdd:smart00631  40 KISNGGSHDKPAIFIDAGIHAREWigpaTALYLINQLLENYGRDPRVTNLLDKTDIYIVPVLNPdgYEYTHTGdRLWRKn 119

                           90
                   ....*....|....*..
gi 1155024104   91 -------DDTDINRMFP 100
Cdd:smart00631 120 rspnsncRGVDLNRNFP 136
 
Name Accession Description Interval E-value
M14_ASTE_ASPA-like cd06253
Peptidase M14 Succinylglutamate desuccinylase (ASTE)/aspartoacylase (ASPA)-like; ...
 9-218 1.13e-103

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: 301.83  E-value: 1.13e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1155024104   9 MKSPFRDDFKIIGYTFGEG--KKSLAIVGAMRGDEVAQQYVASQVVRELNSLERKGlISKNVSVTIIPSANPFSMNIEKR 86
Cdd:cd06253     1 LESPFREPLEVKGFRFGGGnaEPRIAIVAGIHGDELNGLYVCSRLIRFLKELEEGG-YKLKGKVLVIPAVNPLGINSGTR 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1155024104  87 FWAMDDTDINRMFPGYDKGETTQRIAAGLFKNLEGFEYGIQLASFYMPGDFIPHVRIIRTAIDDYTDEAKDFGLPYICVS 166
Cdd:cd06253    80 FWPFDNLDMNRMFPGYNKGETTERIAAALFEDLKGADYGIDLHSSNDFLREIPQVRVIESGAQDLLPLAKFLGLDVVWVH 159

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1155024104 167 DPHPFDTTLLNYNWQIWNTKTFSLYGGTNYRIEGLLCKNQVNAILRFMYKHG 218
Cdd:cd06253   160 PASTVDTGTLAYNWNEWGTKALVLEMGVGMRIDKEYCEQLFEGILRFLLKMG 211
COG3608 COG3608
Predicted deacylase [General function prediction only];
25-307 8.55e-66

Predicted deacylase [General function prediction only];


Pssm-ID: 442826 [Multi-domain]  Cd Length: 296  Bit Score: 208.16  E-value: 8.55e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1155024104  25 GEGKKsLAIVGAMRGDEVAQQYVASQVVRELNSLERKGlisknvSVTIIPSANPFSMNIEKRFWAMDDTDINRMFPGYDK 104
Cdd:COG3608    24 GPGPT-LLITAGIHGDELNGIEALRRLLRELDPGELRG------TVILVPVANPPGFLQGSRYLPIDGRDLNRSFPGDAD 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1155024104 105 GETTQRIAAGLFKN-LEGFEYGIQLASFYMPGDFIPHVRIIRTaiDDYTDE-AKDFGLPYIcVSDPHPFDTTlLNYNWQI 182
Cdd:COG3608    97 GSLAERIAHALFEEiLPDADYVIDLHSGGIARDNLPHVRAGPG--DEELRAlARAFGAPVI-LDSPEGGDGS-LREAAAE 172

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1155024104 183 WNTKTFSLYGGTNYRIEGLLCKNQVNAILRFMYKHGML-LKKSYDPAIASVVVNESdlVVVQAPCAGFFYRKKNAGDFVR 261
Cdd:COG3608   173 AGIPALTLELGGGGRFDEESIEAGVRGILNVLRHLGMLdGEAPPPPLAPPVLARGS--EWVRAPAGGLFEPLVELGDRVK 250

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 1155024104 262 KGDELGRIVDPYeGNVKARISAYVDGIMYFTHDSPLVMQNTPLFKI 307
Cdd:COG3608   251 KGDVLGRITDPF-GEEVEEVRAPVDGIVIGRRTNPLVNPGDALFHI 295
M14_ASTE_ASPA-like cd06251
Peptidase M14 Succinylglutamate desuccinylase (ASTE)/aspartoacylase (ASPA)-like; ...
 26-220 1.76e-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: 349469 [Multi-domain]  Cd Length: 195  Bit Score: 84.51  E-value: 1.76e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1155024104  26 EGKKsLAIVGAMRGDEVAQQYVASQVVRELNSLERKGlisknvSVTIIPSANPFSMNIEKRFWAMDDTDINRMFPGYDKG 105
Cdd:cd06251    11 PGPT-LLLTAAIHGDELNGIEVIQRLLEDLDPSKLRG------TLIAIPVVNPLGFENNSRYLPDDGRDLNRSFPGSEKG 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1155024104 106 ETTQRIAAGLFKNL-EGFEYGIQL--ASFYmpGDFIPHVRIirtaidDYTDE-----AKDFGLPYICVSD--PHPFDTTL 175
Cdd:cd06251    84 SLASRLAHLLWNEIvKKADYVIDLhtASTG--RTNLPYVRA------DLRDPesrrmAEAFGAPVIVDDPgeDGSLRGAA 155

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1155024104 176 LNYnwqiwNTKTFSLYGGTNYRIEGLLCKNQVNAILRFMYKHGML 220
Cdd:cd06251   156 VEL-----GIPAITVELGEALRFDEDIIRRGVEGVLNVLRHLGML 195
AstE_AspA pfam04952
Succinylglutamate desuccinylase / Aspartoacylase family; This family includes ...
 29-307 2.04e-17

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: 80.47  E-value: 2.04e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1155024104  29 KSLAIVGAMRGDEVAQQYVASQVVRELNSLERKGLIsknvsvTIIPSANPFSMNIEKRFwamDDTDINRMFPGYDKGET- 107
Cdd:pfam04952   3 PTLLLSAGIHGNETNGVELLRRLLRQLDPGDIAGER------TLVPLANPPAFRAGSRY---IPRDLNRSFPGRALGASs 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1155024104 108 --------TQRIAAGLFKN-LEGFEYGIQL-----ASFYMPGDFIPHvRIIRTAIDDYtdeAKDFGLPYICVSDPHPFDT 173
Cdd:pfam04952  74 depyratrAERLADLFFPAlLPRADIVLDLhtgtrGMGHLLFALAPI-RDDPLHLLAL---LRAFGAPAVLKLHSKPSAG 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1155024104 174 TLLNYNWQIWnTKTFSLYGGTNYRIEGLLCKNQVNAILRFMYKHGML---LKKSYDPAIASVVVNESDLVVVQAPCAGFF 250
Cdd:pfam04952 150 FSAFSAEELG-APGFTLELGGAGPFGANLISRTAAGVLNVLRLIGVLnggPDAFEPPKLYRVLREIDRPRDIRAELAGLV 228

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1155024104 251 YRKKNAGDFVRKGDELGR--IVDPYEGNvKARISAYVDGIMYFTHDSPLVMQNTPLFKI 307
Cdd:pfam04952 229 EFALNLGDDVDAGPLLPGgpLFAPFGGE-ETEYRAPEDGYPVFPNEAAYVGKGAALALV 286
M14_ASTE_ASPA_like cd06230
Peptidase M14 Succinylglutamate desuccinylase (ASTE)/aspartoacylase (ASPA) subfamily; The ...
 31-113 2.11e-12

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


Pssm-ID: 349449 [Multi-domain]  Cd Length: 177  Bit Score: 64.26  E-value: 2.11e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1155024104  31 LAIVGAMRGDEVAQQYVASQVVRELNSLERKGlisknvSVTIIPSANPFSMNIEKRFWAMDDTDINRMFPGYDKGETTQR 110
Cdd:cd06230     1 LLILAGVHGDEYEGVEAIRRLLAELDPSELKG------TVVLVPVANPPAFEAGTRYTPLDGLDLNRIFPGDPDGSPTER 74


                  ...
gi 1155024104 111 IAA 113
Cdd:cd06230    75 LAH 77
M14_ASTE_ASPA-like cd06255
Peptidase M14 Succinylglutamate desuccinylase (ASTE)/aspartoacylase (ASPA)-like; ...
 31-220 4.27e-09

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


Pssm-ID: 349473  Cd Length: 223  Bit Score: 55.79  E-value: 4.27e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1155024104  31 LAIVGAMRGDEVAQQYVASQVVRELNSLERKGlisknvSVTIIPSANPFSMNIEKRFWAMDDTDINRMFPGYDKGETTQR 110
Cdd:cd06255    26 LWINGAVHGDELNGPLAALELFRELDPAQLSG------TLVATPIANPLAFQGRQKFSPQDGEDLDQSFPGDPDGLITER 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1155024104 111 IAAGLFKNLEGF-EYGIQLASFYMPGDFIPHVR--IIRTAI----DDYTDEAKDFGLPYICVSD------PHPFDTTL-L 176
Cdd:cd06255   100 MAHALFSEVKEVaDYLIDFHTGGTPFDANPYTVykLFPESGpveeKRLLRLARAFGVHANCRVDvsgaggELPGNTAGaL 179

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1155024104 177 NYNWQIWNTKTFSLYGGTNYRIEGLLCKNQVNAILRFMYKHGML 220
Cdd:cd06255   180 DYQCMAQGIPAFMVELGGGGRAEEEAVRFAARGLRNLLRYLGML 223
M14_ASTE_ASPA-like cd06254
Peptidase M14 Succinylglutamate desuccinylase (ASTE)/aspartoacylase (ASPA)-like; ...
 29-169 1.45e-08

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


Pssm-ID: 349472  Cd Length: 198  Bit Score: 53.74  E-value: 1.45e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1155024104  29 KSLAIVGAMRGDEVAQQYVASQVVRELNSLERKGlisknvSVTIIPSANPFSmniekrFWA-------MDDTDINRMFPG 101
Cdd:cd06254    12 PTLLITAGIHGGEYPGILAAIRLARELDPADVKG------TLIIVHIANVSG------FEArtpfvvpEDGKNLNRVFPG 79

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1155024104 102 YDKGETTQRIAAGLFKNLEGF-EYGIQLASFYMPGDFIPHVRIIRTAIDDYTDE----AKDFGLPYICVSDPH 169
Cdd:cd06254    80 DPDGTLTERIAYFLTREIISRaDFLIDLHGGDANEALTPFVYYPGGASEEVNDIsraaAQALGLPYIVISSSE 152
M14_ASTE_ASPA-like cd06252
Peptidase M14 Succinylglutamate desuccinylase (ASTE)/aspartoacylase (ASPA)-like; ...
 25-175 2.55e-07

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


Pssm-ID: 349470  Cd Length: 224  Bit Score: 50.65  E-value: 2.55e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1155024104  25 GEGKKSLaIVGAMRGDEVAQQYVASQVVRELNSLERKGLIsknvsvTIIPSANPFSMNIEKRFWAMDDTDINRMFPGYDK 104
Cdd:cd06252    32 GSGPTVL-LTGGNHGDEYEGPIALRRLARDLDPEDVRGRL------IIVPALNLPAVRAGTRTSPLDGGNLNRAFPGDAD 104

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1155024104 105 GETTQRIAAGLFKNLegF---EYGIQLASFYMPGDFIPHVRIIRTAIDDYT----DEAKDFGLPYICVSDPHPFDTTL 175
Cdd:cd06252   105 GTPTERIAHFLETVL--LpraDAVIDLHSGGSSLDFVPCAAVHLLPDPAQRarslALAEAFGAPLSVVVDNVDAPGTL 180
M14_ASTE_ASPA_like cd18430
Succinylglutamate desuccinylase/aspartoacylase; uncharacterized; A functionally ...
 31-154 7.69e-07

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


Pssm-ID: 349486 [Multi-domain]  Cd Length: 168  Bit Score: 48.21  E-value: 7.69e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1155024104  31 LAIVGAMRGDEVAQQYVASQVVRELNSlerkGLISKNvSVTIIPsANPFSMNIEKRFwamDDTDINRMFPGYDKGET-TQ 109
Cdd:cd18430     1 LAVLGAVHGNETCGTRAVERLLAELPS----GALQKG-PVTLVP-ANERAYAEGVRF---CEEDLNRVFPGDPDPDTyER 71

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1155024104 110 RIAAGLFKNLEGFEYGIQLASFYMPGDfiPHVriIRTAIDDYTDE 154
Cdd:cd18430    72 RLANRLCPELEGHDVVLDLHSTHSGGQ--PFA--ILDYGDKASRR 112
M14_ASTE_ASPA_like cd18174
Peptidase M14 Succinylglutamate desuccinylase (ASTE)/aspartoacylase (ASPA)-like; ...
 31-178 1.80e-06

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


Pssm-ID: 349484  Cd Length: 187  Bit Score: 47.62  E-value: 1.80e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1155024104  31 LAIVGAMRGDEVAQQYVASQVVRELNSLERKGlisknvSVTIIPSANPFSMniEKR---FWAMDDTDINRMFPGYDKGET 107
Cdd:cd18174     1 LLVTAGVHGYEYASIEALQRLIKELDPAKLSG------TVIVVPIANIPAF--EGRsiyVNPLDGKNLNRSFPGDPDGTP 72

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1155024104 108 TQRIAAGLFKNL-EGFEYGIQLASFYMPGDFIPHVRIIRT---AIDDYTDE-AKDFGLPYICVSDPHPFDTTLLNY 178
Cdd:cd18174    73 TERLAHWLTTNViARADYYIDLHGGDLNEDLRPFVYYYETgnaALDAASREmAEAFGLDHIVFYKARLKASRGSLY 148
AstE COG2988
Succinylglutamate desuccinylase [Amino acid transport and metabolism];
26-101 9.80e-05

Succinylglutamate desuccinylase [Amino acid transport and metabolism];


Pssm-ID: 442227  Cd Length: 305  Bit Score: 43.30  E-value: 9.80e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1155024104  26 EGKKSLAIVGAMRGDEVAQQYVASQVVRELNSLERKglisKNVSVTIIpSANPFSMNIEKRFWamdDTDINRMFPG 101
Cdd:COG2988    22 PGIKAVVISGGIHGNETAPIELLDKLLQDLLLGERP----LSFRLLLI-LGNPAAMRAGRRYL---DEDLNRLFGG 89
Zn_pept smart00631
Zn_pept domain;
19-100 2.19e-04

Zn_pept domain;


Pssm-ID: 214748 [Multi-domain]  Cd Length: 277  Bit Score: 41.94  E-value: 2.19e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1155024104   19 IIGYTFGEGKKSLAIVGAMRGDEV----AQQYVASQVVRELNSLERKGLISKNVSVTIIPSANP--FSMNIEK-RFWAM- 90
Cdd:smart00631  40 KISNGGSHDKPAIFIDAGIHAREWigpaTALYLINQLLENYGRDPRVTNLLDKTDIYIVPVLNPdgYEYTHTGdRLWRKn 119

                           90
                   ....*....|....*..
gi 1155024104   91 -------DDTDINRMFP 100
Cdd:smart00631 120 rspnsncRGVDLNRNFP 136
M14_MpaA-like cd06904
Peptidase M14-like domain of Escherichia coli Murein Peptide Amidase A and related proteins; ...
 19-100 3.58e-03

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: 38.03  E-value: 3.58e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1155024104  19 IIGYTFGEGKKS-LAIVGAMRGDEVAQQYVASQVVRELNSLERkgliSKNVSVTIIPSANPFSMNIEKRFWAmDDTDINR 97
Cdd:cd06904    13 ILAYKFGPGSRArILIIGGIHGDEPEGVSLVEHLLRWLKNHPA----SGDFHIVVVPCLNPDGLAAGTRTNA-NGVDLNR 87


                  ...
gi 1155024104  98 MFP 100
Cdd:cd06904    88 NFP 90
 
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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