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Conserved domains on  [gi|1443750906|emb|SUV58544|]
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succinylglutamate desuccinylase [Bordetella parapertussis]

Protein Classification

M14 family metallopeptidase( domain architecture ID 13035105)

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 cd18430
Succinylglutamate desuccinylase/aspartoacylase; uncharacterized; A functionally ...
 26-231 5.41e-73

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: 223.09  E-value: 5.41e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443750906  26 LLVLGAVHGNEVCGTRAIERILAELESGALaiTRGQLTLLPvTNPLAYRKGERQGDRNLNRNLRVCATPTDYEDRIGNAL 105
Cdd:cd18430     1 LAVLGAVHGNETCGTRAVERLLAELPSGAL--QKGPVTLVP-ANERAYAEGVRFCEEDLNRVFPGDPDPDTYERRLANRL 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443750906 106 CPLLQAHDVLLDLHSFHTGGQPFAMLGPRDNqealepfaHAREEARLVAHLGPRRVVEGWMqayergvrrrreqnpgapa 185
Cdd:cd18430    78 CPELEGHDVVLDLHSTHSGGQPFAILDYGDK--------ASRRLARSVGIPKGWRVVYGRD------------------- 130

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1443750906 186 alLDAAYGVGSTEyfrahgGYGVTLECGQHDDPAAPEVAYRAIRQT 231
Cdd:cd18430   131 --LGYAHGGGKTE------VTGVTVECGYHDSEEAAEVAYRAILNT 168
 
Name Accession Description Interval E-value
M14_ASTE_ASPA_like cd18430
Succinylglutamate desuccinylase/aspartoacylase; uncharacterized; A functionally ...
 26-231 5.41e-73

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: 223.09  E-value: 5.41e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443750906  26 LLVLGAVHGNEVCGTRAIERILAELESGALaiTRGQLTLLPvTNPLAYRKGERQGDRNLNRNLRVCATPTDYEDRIGNAL 105
Cdd:cd18430     1 LAVLGAVHGNETCGTRAVERLLAELPSGAL--QKGPVTLVP-ANERAYAEGVRFCEEDLNRVFPGDPDPDTYERRLANRL 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443750906 106 CPLLQAHDVLLDLHSFHTGGQPFAMLGPRDNqealepfaHAREEARLVAHLGPRRVVEGWMqayergvrrrreqnpgapa 185
Cdd:cd18430    78 CPELEGHDVVLDLHSTHSGGQPFAILDYGDK--------ASRRLARSVGIPKGWRVVYGRD------------------- 130

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1443750906 186 alLDAAYGVGSTEyfrahgGYGVTLECGQHDDPAAPEVAYRAIRQT 231
Cdd:cd18430   131 --LGYAHGGGKTE------VTGVTVECGYHDSEEAAEVAYRAILNT 168
COG3608 COG3608
Predicted deacylase [General function prediction only];
3-317 3.63e-46

Predicted deacylase [General function prediction only];


Pssm-ID: 442826 [Multi-domain]  Cd Length: 296  Bit Score: 158.09  E-value: 3.63e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443750906   3 TPTPVSTDYlraHQFLGLQPGPRLLVLGAVHGNEVCGTRAIERILAELESGALaitRGQLTLLPVTNPLAYRKGER---Q 79
Cdd:COG3608     9 SGTPVSLPV---TVFRGAGPGPTLLITAGIHGDELNGIEALRRLLRELDPGEL---RGTVILVPVANPPGFLQGSRylpI 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443750906  80 GDRNLNRNLrvcatPTD----YEDRIGNALC-PLLQAHDVLLDLHSFHTGGQ--PFAMLGPRDnqEALEPFAHAreearl 152
Cdd:COG3608    83 DGRDLNRSF-----PGDadgsLAERIAHALFeEILPDADYVIDLHSGGIARDnlPHVRAGPGD--EELRALARA------ 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443750906 153 vahLGPRRVVEGWmqAYERGVRRRREQNPGAPAalldaaygvgsteyfrahggygVTLECGQHD--DPAAPEVAYRAIRQ 230
Cdd:COG3608   150 ---FGAPVILDSP--EGGDGSLREAAAEAGIPA----------------------LTLELGGGGrfDEESIEAGVRGILN 202

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443750906 231 TLALLGLADIALEPPRRDFETLCLVDVVDREADGDAFARPWASFDPVRQGELVGTRADG-----RQVLAPRDGYV--VFP 303
Cdd:COG3608   203 VLRHLGMLDGEAPPPPLAPPVLARGSEWVRAPAGGLFEPLVELGDRVKKGDVLGRITDPfgeevEEVRAPVDGIVigRRT 282

                         330
                  ....*....|....
gi 1443750906 304 NPRALAGNEWFYFA 317
Cdd:COG3608   283 NPLVNPGDALFHIA 296
AstE_AspA pfam04952
Succinylglutamate desuccinylase / Aspartoacylase family; This family includes ...
 22-311 3.67e-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: 80.09  E-value: 3.67e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443750906  22 PGPRLLVLGAVHGNEVCGTRAIERILAELESGALAitrGQLTLLPVTNPLAYRKGERQGDRNLNR-----------NLRV 90
Cdd:pfam04952   1 PGPTLLLSAGIHGNETNGVELLRRLLRQLDPGDIA---GERTLVPLANPPAFRAGSRYIPRDLNRsfpgralgassDEPY 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443750906  91 CATPTD-YEDRIGNAlcpLLQAHDVLLDLHSfhtggqpfamlGPRDNQEALEPFAHAREEARLVAHlgprrvvegWMQAY 169
Cdd:pfam04952  78 RATRAErLADLFFPA---LLPRADIVLDLHT-----------GTRGMGHLLFALAPIRDDPLHLLA---------LLRAF 134

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443750906 170 ergvrrrreqnpGAPAALLDAAYGVGSTEYFRAH--GGYGVTLECGQHdDPAAPEVAYRAIRQTLALLGLADIaLEPPRR 247
Cdd:pfam04952 135 ------------GAPAVLKLHSKPSAGFSAFSAEelGAPGFTLELGGA-GPFGANLISRTAAGVLNVLRLIGV-LNGGPD 200

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1443750906 248 DFETLCL---VDVVDREADGDAFARPWASF-----DPVRQGELVG-------TRADGRQVLAPRDGYVVFPNPRALAGN 311
Cdd:pfam04952 201 AFEPPKLyrvLREIDRPRDIRAELAGLVEFalnlgDDVDAGPLLPggplfapFGGEETEYRAPEDGYPVFPNEAAYVGK 279
PRK02259 PRK02259
aspartoacylase; Provisional
 25-120 1.70e-08

aspartoacylase; Provisional


Pssm-ID: 235019  Cd Length: 288  Bit Score: 54.88  E-value: 1.70e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443750906  25 RLLVLGAVHGNEVCGTRAIERILAELEsgalAITRGQLTLLPV-TNPLAYRKGERQGDRNLNRNLRV----CATPTDYED 99
Cdd:PRK02259    4 RVAIVGGTHGNEITGIYLVKKWQQQPN----LINRKGLEVQTViGNPEAIEAGRRYIDRDLNRSFRLdllqNPDLSGYEQ 79

                          90       100
                  ....*....|....*....|....*.
gi 1443750906 100 RIGNALCPLLQAH-----DVLLDLHS 120
Cdd:PRK02259   80 LRAKELVQQLGPKgnspcDFIIDLHS 105
 
Name Accession Description Interval E-value
M14_ASTE_ASPA_like cd18430
Succinylglutamate desuccinylase/aspartoacylase; uncharacterized; A functionally ...
 26-231 5.41e-73

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: 223.09  E-value: 5.41e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443750906  26 LLVLGAVHGNEVCGTRAIERILAELESGALaiTRGQLTLLPvTNPLAYRKGERQGDRNLNRNLRVCATPTDYEDRIGNAL 105
Cdd:cd18430     1 LAVLGAVHGNETCGTRAVERLLAELPSGAL--QKGPVTLVP-ANERAYAEGVRFCEEDLNRVFPGDPDPDTYERRLANRL 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443750906 106 CPLLQAHDVLLDLHSFHTGGQPFAMLGPRDNqealepfaHAREEARLVAHLGPRRVVEGWMqayergvrrrreqnpgapa 185
Cdd:cd18430    78 CPELEGHDVVLDLHSTHSGGQPFAILDYGDK--------ASRRLARSVGIPKGWRVVYGRD------------------- 130

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1443750906 186 alLDAAYGVGSTEyfrahgGYGVTLECGQHDDPAAPEVAYRAIRQT 231
Cdd:cd18430   131 --LGYAHGGGKTE------VTGVTVECGYHDSEEAAEVAYRAILNT 168
COG3608 COG3608
Predicted deacylase [General function prediction only];
3-317 3.63e-46

Predicted deacylase [General function prediction only];


Pssm-ID: 442826 [Multi-domain]  Cd Length: 296  Bit Score: 158.09  E-value: 3.63e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443750906   3 TPTPVSTDYlraHQFLGLQPGPRLLVLGAVHGNEVCGTRAIERILAELESGALaitRGQLTLLPVTNPLAYRKGER---Q 79
Cdd:COG3608     9 SGTPVSLPV---TVFRGAGPGPTLLITAGIHGDELNGIEALRRLLRELDPGEL---RGTVILVPVANPPGFLQGSRylpI 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443750906  80 GDRNLNRNLrvcatPTD----YEDRIGNALC-PLLQAHDVLLDLHSFHTGGQ--PFAMLGPRDnqEALEPFAHAreearl 152
Cdd:COG3608    83 DGRDLNRSF-----PGDadgsLAERIAHALFeEILPDADYVIDLHSGGIARDnlPHVRAGPGD--EELRALARA------ 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443750906 153 vahLGPRRVVEGWmqAYERGVRRRREQNPGAPAalldaaygvgsteyfrahggygVTLECGQHD--DPAAPEVAYRAIRQ 230
Cdd:COG3608   150 ---FGAPVILDSP--EGGDGSLREAAAEAGIPA----------------------LTLELGGGGrfDEESIEAGVRGILN 202

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443750906 231 TLALLGLADIALEPPRRDFETLCLVDVVDREADGDAFARPWASFDPVRQGELVGTRADG-----RQVLAPRDGYV--VFP 303
Cdd:COG3608   203 VLRHLGMLDGEAPPPPLAPPVLARGSEWVRAPAGGLFEPLVELGDRVKKGDVLGRITDPfgeevEEVRAPVDGIVigRRT 282

                         330
                  ....*....|....
gi 1443750906 304 NPRALAGNEWFYFA 317
Cdd:COG3608   283 NPLVNPGDALFHIA 296
M14_ASTE_ASPA_like cd06230
Peptidase M14 Succinylglutamate desuccinylase (ASTE)/aspartoacylase (ASPA) subfamily; The ...
 26-229 9.22e-20

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: 85.06  E-value: 9.22e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443750906  26 LLVLGAVHGNEVCGTRAIERILAELESGALaitRGQLTLLPVTNPLAYRKGERQGDR---NLNrnlRVCA--TPTDYEDR 100
Cdd:cd06230     1 LLILAGVHGDEYEGVEAIRRLLAELDPSEL---KGTVVLVPVANPPAFEAGTRYTPLdglDLN---RIFPgdPDGSPTER 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443750906 101 IGNALCPLLQAH-DVLLDLHSFHTGGQPFAMLGPRDnqeaLEPFAHAREEARLvahLGPRRVVegwmqayergvrRRREQ 179
Cdd:cd06230    75 LAHELTELILKHaDALIDLHSGGTGRLVPYAILDYD----SDAREKSRELARA---FGGTPVI------------WGGDP 135

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1443750906 180 NPGAPAAlldaaygvgsteYFRAHGGYGVTLECGQH--DDPAAPEVAYRAIR 229
Cdd:cd06230   136 PGGTPVA------------AARSAGIPAITVELGGGgrLRAERLERYLRGIR 175
AstE_AspA pfam04952
Succinylglutamate desuccinylase / Aspartoacylase family; This family includes ...
 22-311 3.67e-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: 80.09  E-value: 3.67e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443750906  22 PGPRLLVLGAVHGNEVCGTRAIERILAELESGALAitrGQLTLLPVTNPLAYRKGERQGDRNLNR-----------NLRV 90
Cdd:pfam04952   1 PGPTLLLSAGIHGNETNGVELLRRLLRQLDPGDIA---GERTLVPLANPPAFRAGSRYIPRDLNRsfpgralgassDEPY 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443750906  91 CATPTD-YEDRIGNAlcpLLQAHDVLLDLHSfhtggqpfamlGPRDNQEALEPFAHAREEARLVAHlgprrvvegWMQAY 169
Cdd:pfam04952  78 RATRAErLADLFFPA---LLPRADIVLDLHT-----------GTRGMGHLLFALAPIRDDPLHLLA---------LLRAF 134

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443750906 170 ergvrrrreqnpGAPAALLDAAYGVGSTEYFRAH--GGYGVTLECGQHdDPAAPEVAYRAIRQTLALLGLADIaLEPPRR 247
Cdd:pfam04952 135 ------------GAPAVLKLHSKPSAGFSAFSAEelGAPGFTLELGGA-GPFGANLISRTAAGVLNVLRLIGV-LNGGPD 200

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1443750906 248 DFETLCL---VDVVDREADGDAFARPWASF-----DPVRQGELVG-------TRADGRQVLAPRDGYVVFPNPRALAGN 311
Cdd:pfam04952 201 AFEPPKLyrvLREIDRPRDIRAELAGLVEFalnlgDDVDAGPLLPggplfapFGGEETEYRAPEDGYPVFPNEAAYVGK 279
M14_ASTE_ASPA-like cd06910
Peptidase M14 Succinylglutamate desuccinylase (ASTE)/aspartoacylase (ASPA)-like; ...
 10-224 1.40e-15

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


Pssm-ID: 349481  Cd Length: 208  Bit Score: 74.31  E-value: 1.40e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443750906  10 DYLraHQFLGLQPGPRLLVLGAVHGNEVCGTRAIERILAElesgALAITRGQLTLLpVTNPLAYRK-------GERQGDR 82
Cdd:cd06910    13 DYV--HRFDSGQPGPHVMINALTHGNEICGAIALDWLLKN----GVRPLRGRLTFC-FANVEAYERfdparptASRFVDE 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443750906  83 NLNR---NLRVCATPTDYEDRIGNALCPLLQAHDVLLDLHSFHTGGQPFAMLGPRDNqealepfahAREEARLVahlgpr 159
Cdd:cd06910    86 DLNRvwgPELLDGPEQSIELRRARELRPVVDTVDYLLDIHSMQEKVPPLALAGDKEK---------GRALARRV------ 150

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1443750906 160 rvvegwmqayergvrrrreqnpGAPAALLdaaYGVGSTEYFR----------AHGGYGVTLECGQHDDPAAPEVA 224
Cdd:cd06910   151 ----------------------GSPAHLL---IDAGHAEGLRlrdyagfgdpSSPKNALLVECGQHWERSAVVVA 200
AstE COG2988
Succinylglutamate desuccinylase [Amino acid transport and metabolism];
23-307 2.62e-15

Succinylglutamate desuccinylase [Amino acid transport and metabolism];


Pssm-ID: 442227  Cd Length: 305  Bit Score: 75.27  E-value: 2.62e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443750906  23 GPRLLVLGAVHGNEVCGTRAIERILAELESGALAITRGQLTLLpvTNPLAYRKGERQGDRNLNR--NLRVCATPTDYEDR 100
Cdd:COG2988    24 IKAVVISGGIHGNETAPIELLDKLLQDLLLGERPLSFRLLLIL--GNPAAMRAGRRYLDEDLNRlfGGRHLQNPESYEAA 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443750906 101 IGNALCPLLQAH-------DVLLDLHSfHTGGQP---FAMLGPRDNQealepfaHAREEARLVAHLGPRRVV----EGWM 166
Cdd:COG2988   102 RAKELEQAVGPFfaaggrvRLHIDLHT-AIRNSGherFAVYPFRGRP-------FDLALLAYLAAAGPEAVVlhhaPGGT 173

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443750906 167 QAYergvrrrreqnpgapaalldaaygvgsteYFRAHGGY-GVTLECGQ-----HDDPAAPEVAYRAIRQTLALLGLADI 240
Cdd:COG2988   174 FSH-----------------------------FSAELCGAqAFTLELGKvrpfgQNDLSRFAATEEALRALLSGAELPEH 224

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1443750906 241 ALEPPRRdFETlclVDVVDReaDGDAF----ARPWASFDPVRQGELVGTRADGRQVLAPRDGYVVFPNPRA 307
Cdd:COG2988   225 PAQDLDL-YRV---VQQIIK--HGDDFmlhpDLDTLNFTPLPPGTLLAEDGGKEYRVEGDEERIVFPNEAV 289
M14_ASTE_ASPA-like cd06255
Peptidase M14 Succinylglutamate desuccinylase (ASTE)/aspartoacylase (ASPA)-like; ...
 5-237 8.44e-15

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: 72.36  E-value: 8.44e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443750906   5 TPVSTDYLRAHqflGLQPGPRLLVLGAVHGNEVCGTRAIERILAELESGALAitrGQLTLLPVTNPLAYrkgerqgdRNL 84
Cdd:cd06255     8 APVTIPVIVVR---GAKPGPCLWINGAVHGDELNGPLAALELFRELDPAQLS---GTLVATPIANPLAF--------QGR 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443750906  85 NRNlrvcaTPTDYED---------------RIGNALCPLLQAH-DVLLDLHSFHTG--GQPFAM--LGPRDNQEAlepfa 144
Cdd:cd06255    74 QKF-----SPQDGEDldqsfpgdpdgliteRMAHALFSEVKEVaDYLIDFHTGGTPfdANPYTVykLFPESGPVE----- 143

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443750906 145 hAREEARLVAHLGPRrvVEGWMQAYergvrrrreqnpgaPAALLDAAYGVGSTEY-FRAHGGYGVTLECG--QHDDPAAP 221
Cdd:cd06255   144 -EKRLLRLARAFGVH--ANCRVDVS--------------GAGGELPGNTAGALDYqCMAQGIPAFMVELGggGRAEEEAV 206

                         250
                  ....*....|....*.
gi 1443750906 222 EVAYRAIRQTLALLGL 237
Cdd:cd06255   207 RFAARGLRNLLRYLGM 222
M14_ASTE_ASPA-like cd06251
Peptidase M14 Succinylglutamate desuccinylase (ASTE)/aspartoacylase (ASPA)-like; ...
 19-120 1.13e-13

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: 68.72  E-value: 1.13e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443750906  19 GLQPGPRLLVLGAVHGNEVCGTRAIERILAELESGALaitRGQLTLLPVTNPLAYRKGER---QGDRNLNRNLRVCATPT 95
Cdd:cd06251     8 GAKPGPTLLLTAAIHGDELNGIEVIQRLLEDLDPSKL---RGTLIAIPVVNPLGFENNSRylpDDGRDLNRSFPGSEKGS 84

                          90       100
                  ....*....|....*....|....*.
gi 1443750906  96 DYEdRIGNALCP-LLQAHDVLLDLHS 120
Cdd:cd06251    85 LAS-RLAHLLWNeIVKKADYVIDLHT 109
M14_ASTE_ASPA-like cd06252
Peptidase M14 Succinylglutamate desuccinylase (ASTE)/aspartoacylase (ASPA)-like; ...
 22-237 2.64e-11

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: 62.20  E-value: 2.64e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443750906  22 PGPRLLVLGAVHGNEVCGTRAIERILAELESGALaitRGQLTLLPVTNPLAYRKGERQ---GDRNLNRNL--RVCATPTd 96
Cdd:cd06252    33 SGPTVLLTGGNHGDEYEGPIALRRLARDLDPEDV---RGRLIIVPALNLPAVRAGTRTsplDGGNLNRAFpgDADGTPT- 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443750906  97 yeDRIGNALCP-LLQAHDVLLDLHSfhtGGQ-----PFAMLGPRDNQEalepfAHAREEARLVAhLGPRRVVegwmqaye 170
Cdd:cd06252   109 --ERIAHFLETvLLPRADAVIDLHS---GGSsldfvPCAAVHLLPDPA-----QRARSLALAEA-FGAPLSV-------- 169

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1443750906 171 rgvrrrREQNPGAPAALLDAAYGVG----STEYfrahGGYGVTlecgqhdDPAAPEVAYRAIRQTLALLGL 237
Cdd:cd06252   170 ------VVDNVDAPGTLDSAAERAGkifvSTEL----GGGGTV-------TPAALRIAERGVLNVLIHLGV 223
M14_ASPA cd06909
Peptidase M14 Aspartoacylase (ASPA) subfamily; Aspartoacylase (ASPA) belongs to the ...
 25-120 1.29e-08

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


Pssm-ID: 349480  Cd Length: 190  Bit Score: 54.14  E-value: 1.29e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443750906  25 RLLVLGAVHGNEVCGTRAIERILAELESgalaITRGQLTLLPV-TNPLAYRKGERQGDRNLNR-----NLRVCATPTDYE 98
Cdd:cd06909     2 RVAIVGGTHGNELTGVYLVKHWLKNPEL----IERKSFEVHPLlANPRAVEQCRRYIDTDLNRcfsleNLSSAPSSLPYE 77

                          90       100
                  ....*....|....*....|....*..
gi 1443750906  99 DRIGNALCPLLQAH-----DVLLDLHS 120
Cdd:cd06909    78 VRRAREINQILGPKgnpacDFIIDLHN 104
PRK02259 PRK02259
aspartoacylase; Provisional
 25-120 1.70e-08

aspartoacylase; Provisional


Pssm-ID: 235019  Cd Length: 288  Bit Score: 54.88  E-value: 1.70e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443750906  25 RLLVLGAVHGNEVCGTRAIERILAELEsgalAITRGQLTLLPV-TNPLAYRKGERQGDRNLNRNLRV----CATPTDYED 99
Cdd:PRK02259    4 RVAIVGGTHGNEITGIYLVKKWQQQPN----LINRKGLEVQTViGNPEAIEAGRRYIDRDLNRSFRLdllqNPDLSGYEQ 79

                          90       100
                  ....*....|....*....|....*.
gi 1443750906 100 RIGNALCPLLQAH-----DVLLDLHS 120
Cdd:PRK02259   80 LRAKELVQQLGPKgnspcDFIIDLHS 105
M14_ASTE_ASPA-like cd06254
Peptidase M14 Succinylglutamate desuccinylase (ASTE)/aspartoacylase (ASPA)-like; ...
 19-146 1.83e-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: 1.83e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443750906  19 GLQPGPRLLVLGAVHGNEVCGTRAIERILAELESGALaitRGQLTLLPVTNPLAYRKGERQ----GDRNLNRNLrvcatP 94
Cdd:cd06254     7 GAKPGPTLLITAGIHGGEYPGILAAIRLARELDPADV---KGTLIIVHIANVSGFEARTPFvvpeDGKNLNRVF-----P 78

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1443750906  95 TD----YEDRIGNALCPLLQAH-DVLLDLHSfhtGGQ-----PFAMLgPRDNQEALEPFAHA 146
Cdd:cd06254    79 GDpdgtLTERIAYFLTREIISRaDFLIDLHG---GDAnealtPFVYY-PGGASEEVNDISRA 136
M14_CP_Csd4-like cd06243
Peptidase M14 carboxypeptidase Csd4 and similar proteins; This family includes peptidase M14 ...
 16-119 1.92e-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: 53.90  E-value: 1.92e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443750906  16 QFLGLQPGPRLLVLGAVHGNEVCGTRAIErILAELEsgalaITRGQLTLLPVTNPLAYRKGERQGDRNLNRNLRVcATPT 95
Cdd:cd06243     9 RLEGREPGPTLLIIGGIQGDEPGGFLAAD-LLADLY-----LVKGNVIVVPRLNFPSILRNHRGLNGDMNRKFAA-LDKK 81

                          90       100
                  ....*....|....*....|....*.
gi 1443750906  96 DYEDRIGNALCPLLQAH--DVLLDLH 119
Cdd:cd06243    82 DPEYKTIQEIKSLIADFrpDVVLHLH 107
M14_ASTE_ASPA-like cd06253
Peptidase M14 Succinylglutamate desuccinylase (ASTE)/aspartoacylase (ASPA)-like; ...
 12-121 3.70e-06

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


Pssm-ID: 349471  Cd Length: 211  Bit Score: 47.21  E-value: 3.70e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443750906  12 LRAHQFLGLQPGPRLLVLGAVHGNEVCGT----RAIeRILAELESGALAITrGQLTLLPVTNPLAYRKGER---QGDRNL 84
Cdd:cd06253    11 VKGFRFGGGNAEPRIAIVAGIHGDELNGLyvcsRLI-RFLKELEEGGYKLK-GKVLVIPAVNPLGINSGTRfwpFDNLDM 88

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1443750906  85 NR-----NLrvcATPTdyeDRIGNALCPLLQAHDVLLDLHSF 121
Cdd:cd06253    89 NRmfpgyNK---GETT---ERIAAALFEDLKGADYGIDLHSS 124
M14_MpaA-like cd06904
Peptidase M14-like domain of Escherichia coli Murein Peptide Amidase A and related proteins; ...
 22-87 6.10e-06

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: 46.50  E-value: 6.10e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1443750906  22 PGPRLLVLGAVHGNEVCGTRAIERILAELeSGALAITRGQLTLLPVTNPLAYRKGERqGDRN---LNRN 87
Cdd:cd06904    22 SRARILIIGGIHGDEPEGVSLVEHLLRWL-KNHPASGDFHIVVVPCLNPDGLAAGTR-TNANgvdLNRN 88
M14_ASTE_ASPA_like cd18174
Peptidase M14 Succinylglutamate desuccinylase (ASTE)/aspartoacylase (ASPA)-like; ...
 26-148 8.98e-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: 349484  Cd Length: 187  Bit Score: 42.61  E-value: 8.98e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443750906  26 LLVLGAVHGNEVCGTRAIERILAELESGALaitRGQLTLLPVTNPLAYRkgERQG------DRNLNRNL--RVCATPTdy 97
Cdd:cd18174     1 LLVTAGVHGYEYASIEALQRLIKELDPAKL---SGTVIVVPIANIPAFE--GRSIyvnpldGKNLNRSFpgDPDGTPT-- 73

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1443750906  98 eDRIGNALCP-LLQAHDVLLDLHsfhtGGqpfamlgprDNQEALEPFAHARE 148
Cdd:cd18174    74 -ERLAHWLTTnVIARADYYIDLH----GG---------DLNEDLRPFVYYYE 111
M14_REP34-like cd06231
Peptidase M14-like domain similar to rapid encystment phenotype 34 (REP34); This family ...
 22-119 1.63e-04

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


Pssm-ID: 349450 [Multi-domain]  Cd Length: 239  Bit Score: 42.29  E-value: 1.63e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443750906  22 PGPRLLVLGAVHGNEVCGTRAierILAELESGALAITRG-QLTLLPVTNPLAYRKGER--QGDRNLNRNLrvCATPTDYE 98
Cdd:cd06231    41 DKPRVLISAGIHGDEPAGVEA---LLRFLESLAEKYLRRvNLLVLPCVNPWGFERNTRenADGIDLNRSF--LKDSPSPE 115

                          90       100
                  ....*....|....*....|.
gi 1443750906  99 DRIGNALCPLLQAHDVLLDLH 119
Cdd:cd06231   116 VRALMEFLASLGRFDLHLDLH 136
M14_ASTE cd03855
Peptidase M14 Succinylglutamate desuccinylase (ASTE) subfamily; Peptidase M14 ...
 16-233 1.69e-04

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: 42.19  E-value: 1.69e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443750906  16 QFLGLQPGPRLLVLGA-VHGNEvcgTRAIE---RILAELESGALAITrgQLTLLPVTNPLAYRKGERQGDRNLNR--NLR 89
Cdd:cd03855    35 ELTPAASASKSVVLSAgIHGNE---TAPIEildQLINDLIRGELALA--HRLLFIFGNPPAIRQGKRFIEENLNRlfSGR 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443750906  90 VCATPTDYEDRIGNALCPLLQA-----------HdvlLDLHSfhtggqpfAMLGPRDNQEALEPFAHAREearlvahlgp 158
Cdd:cd03855   110 HSKLPPSYETARAAELEQAVADffakasgevrwH---LDLHT--------AIRGSKHEQFAVYPFLEGRP---------- 168

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443750906 159 rrvvegwmqayergvrRRREQNPGAPAALLDAA------------YgvgSTEYFRAHggyGVTLECGQ-----HDDPAAP 221
Cdd:cd03855   169 ----------------HDREQLDFLGAAGIEAVllsnspggtfsyY---SSEHFGAA---AFTVELGKvrpfgQNDLSQF 226

                         250
                  ....*....|..
gi 1443750906 222 EVAYRAIRQTLA 233
Cdd:cd03855   227 AAIDQALRALIS 238
PRK05324 PRK05324
succinylglutamate desuccinylase; Provisional
 16-86 5.98e-04

succinylglutamate desuccinylase; Provisional


Pssm-ID: 235408  Cd Length: 329  Bit Score: 40.94  E-value: 5.98e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1443750906  16 QFLGLQPGPRLLVLGA-VHGNEvcgTRAIE---RILAELESGALAITrgQLTLLPVTNPLAYRKGERQGDRNLNR 86
Cdd:PRK05324   39 ELTPAAPSTKALVLSAgIHGNE---TAPIElldQLVRDLLAGELPLR--ARLLVILGNPPAMRAGKRYLDEDLNR 108
Peptidase_M14_like cd00596
M14 family of metallocarboxypeptidases and related proteins; The M14 family of ...
 26-235 9.05e-04

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: 40.14  E-value: 9.05e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443750906  26 LLVLGAVHGNEVCGTRA----IERILAELESGALAITRGQLTL--LPVTNPLAYRKGERQGDR------NLNRN------ 87
Cdd:cd00596     1 ILITGGIHGNEVIGVELalalIEYLLENYGNDPLKRLLDNVELwiVPLVNPDGFARVIDSGGRknangvDLNRNfpynwg 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443750906  88 ---LRVCATPTDY--------EDRignALCPLLQAH--DVLLDLHSF-HTGGQPFAmlgprDNQEALEPFAHAREEARLV 153
Cdd:cd00596    81 kdgTSGPSSPTYRgpapfsepETQ---ALRDLAKSHrfDLAVSYHSSsEAILYPYG-----YTNEPPPDFSEFQELAAGL 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443750906 154 AhlgprRVVEGWMQAYERGVRrrreqnpgapaalLDAAYGVGSTEYFRAHGGYGVTLECGQHDDPAAPEVAYRAIRQTLA 233
Cdd:cd00596   153 A-----RALGAGEYGYGYSYT-------------WYSTTGTADDWLYGELGILAFTVELGTADYPLPGTLLDRRLERNLA 214


                  ..
gi 1443750906 234 LL 235
Cdd:cd00596   215 AL 216
M14_ASTE_ASPA-like cd06256
Peptidase M14 Succinylglutamate desuccinylase (ASTE)/aspartoacylase (ASPA)-like; ...
 14-234 9.40e-04

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


Pssm-ID: 349474  Cd Length: 204  Bit Score: 39.97  E-value: 9.40e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443750906  14 AHQFLGLQPGPRLLVL-GA----------VHGNEVCGTRAIERILAELEsgalaitrgqlTLLPVTNPL------AYRKG 76
Cdd:cd06256    14 AAELLENLPGPTLIHLpGRrprplfvstlLHGNEPTGLRAVQRLLKTGQ-----------APLPRTLLLfignvdAAKAG 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443750906  77 ERQ--GDRNLNRNLRvcATPTDYEDRIGNALCPLLQAHDV--LLDLHSfHTGGQPFAMLGPRDNQEALepfahareeaRL 152
Cdd:cd06256    83 VRRlpGQPDYNRCWP--GPFETPEGRLAAAVLERLDTLRPfaSIDIHN-NTGKNPHYACVNRLDAAHL----------RL 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443750906 153 VAHLGPRRVVegwmqayergVRRRREqnpgapAALLDAAYGVGSteyfrahggygVTLECGQHDDPAAPEVAYRAIRQTL 232
Cdd:cd06256   150 ASLFSRTLVY----------FTRPLG------VLSEALAALCPA-----------VTVECGKPGDAEGEEHAAEGLDAFL 202


                  ..
gi 1443750906 233 AL 234
Cdd:cd06256   203 HL 204
M14-like cd06239
Peptidase M14-like domain; uncharacterized subgroup; Peptidase M14-like domain of a ...
 33-218 5.48e-03

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 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: 349458 [Multi-domain]  Cd Length: 194  Bit Score: 37.39  E-value: 5.48e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443750906  33 HGNEVCGTRAIERILAEL--ESGALAITRGQLTL--LPVTNPLAYRKGERQGDR--NLNRNLRVCATPTdyedriGNALC 106
Cdd:cd06239     9 HGNEPTGTEALLDLISYLrrERQEFEKILERLTLvaIPMLNPDGAELFTRHNAEgiDLNRDARALQTPE------SRALK 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443750906 107 PLLQAH--DVLLDLHS----FHTGGQ----PFAMLGPR-DNQEALEPFahaREEARLVAhlgprrvveGWMqayergVRR 175
Cdd:cd06239    83 AVLDSFspKFAFNLHDqrsiFGVGGTgkpaSLSLLAPAaDEEREDNPS---REKARKLI---------ASI------LEE 144

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1443750906 176 RREQNPGAPAALLDAAYGVGSTEYFRAHGGYGVTLECGQH-DDP 218
Cdd:cd06239   145 LEKIIPGQVARFDDSFYPRAFGDWFQELGIPTILIETGAYpNDY 188
M14_PaAOTO_like cd06250
Peptidase M14 Succinylglutamate desuccinylase (ASTE)/aspartoacylase (ASPA)-like subfamily; ...
 3-71 6.25e-03

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: 37.60  E-value: 6.25e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1443750906   3 TPTPVSTDYLRAHQFLGLQPGPRLLVLGAVHGNEVCGTRAI----ERILAELESGALAitrGQLTLLPVTNPL 71
Cdd:cd06250     7 SPAPGTERSLTVFRFGGAGAGPKVYIQAALHADELPGNLVIhhllERLKALEAAGRIK---GEIVLVPQANPI 76
 
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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