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Conserved domains on  [gi|648533720|ref|WP_026225471|]
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MULTISPECIES: succinylglutamate desuccinylase [Paraburkholderia]

Protein Classification

succinylglutamate desuccinylase( domain architecture ID 10012321)

succinylglutamate desuccinylase catalyzes the formation of succinate and L-glutamate from N-succinyl-L-glutamate in the fifth and final reaction of the ammonia-producing arginine catabolic pathway, L-arginine degradation II (AST pathway)

EC:  3.5.1.96
Gene Ontology:  GO:0008270|GO:0016788|GO:0009017|GO:0019545

Graphical summary

 Zoom to residue level

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List of domain hits

 Name Accession Description Interval E-value
PRK05324 PRK05324
succinylglutamate desuccinylase; Provisional
 13-354 0e+00

succinylglutamate desuccinylase; Provisional


:

Pssm-ID: 235408  Cd Length: 329  Bit Score: 520.89  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648533720  13 SAMLDDFLAWTLAGSRPAahQAQGTCANGVRWTWQGDGVLVIEPAERHAdiRSVLVSAGVHGDETAPIELLSRIVADIAQ 92
Cdd:PRK05324   1 MLAMDDFLALTLAGHPPA--VTEFGLGNGVRWRWLGEGVLELTPAAPST--KALVLSAGIHGNETAPIELLDQLVRDLLA 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648533720  93 GRAVLACRLLVILGNIEAMRDGGRYRDDDLNRLFSGRHLQLPHSHEAPRAAALEQAATRFFAdaSAAPGARWHIDMHTAI 172
Cdd:PRK05324  77 GELPLRARLLVILGNPPAMRAGKRYLDEDLNRLFGGRHQQFPGSDEARRAAELEQAVEDFFA--AGAERVRWHYDLHTAI 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648533720 173 RASVFERFALLPHTGKPFSRAMFEWLGDARISAVLLHTTKGNTYSHFTAQACGADACTLELGKVRPFGENDLTRFEGADL 252
Cdd:PRK05324 155 RGSKHEQFAVLPQRGRPWSREQLAWLGAAGIEAVLLHNAPGGTFSHFSSEHFGALACTLELGKVLPFGQNDLSRFAATDQ 234

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648533720 253 AVRALLAGTRVDSRAntqadaqAALPRVFTVVDQLTKQSDAFELLLAPDVPNFTPLVKGSLLARDGDYQYTVQRDQERIV 332
Cdd:PRK05324 235 ALRALISGEELPERS-------ADPPRLYRVVRQITKHSDDFELHFADDVENFTAFPKGTLLAEDGDERYVVEHDGERIV 307

                        330       340
                 ....*....|....*....|..
gi 648533720 333 FPNPTVKPGLRAGLLVVDTTAD 354
Cdd:PRK05324 308 FPNPNVAIGLRAGLMLVPTTLD 329
 
Name Accession Description Interval E-value
PRK05324 PRK05324
succinylglutamate desuccinylase; Provisional
 13-354 0e+00

succinylglutamate desuccinylase; Provisional


Pssm-ID: 235408  Cd Length: 329  Bit Score: 520.89  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648533720  13 SAMLDDFLAWTLAGSRPAahQAQGTCANGVRWTWQGDGVLVIEPAERHAdiRSVLVSAGVHGDETAPIELLSRIVADIAQ 92
Cdd:PRK05324   1 MLAMDDFLALTLAGHPPA--VTEFGLGNGVRWRWLGEGVLELTPAAPST--KALVLSAGIHGNETAPIELLDQLVRDLLA 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648533720  93 GRAVLACRLLVILGNIEAMRDGGRYRDDDLNRLFSGRHLQLPHSHEAPRAAALEQAATRFFAdaSAAPGARWHIDMHTAI 172
Cdd:PRK05324  77 GELPLRARLLVILGNPPAMRAGKRYLDEDLNRLFGGRHQQFPGSDEARRAAELEQAVEDFFA--AGAERVRWHYDLHTAI 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648533720 173 RASVFERFALLPHTGKPFSRAMFEWLGDARISAVLLHTTKGNTYSHFTAQACGADACTLELGKVRPFGENDLTRFEGADL 252
Cdd:PRK05324 155 RGSKHEQFAVLPQRGRPWSREQLAWLGAAGIEAVLLHNAPGGTFSHFSSEHFGALACTLELGKVLPFGQNDLSRFAATDQ 234

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648533720 253 AVRALLAGTRVDSRAntqadaqAALPRVFTVVDQLTKQSDAFELLLAPDVPNFTPLVKGSLLARDGDYQYTVQRDQERIV 332
Cdd:PRK05324 235 ALRALISGEELPERS-------ADPPRLYRVVRQITKHSDDFELHFADDVENFTAFPKGTLLAEDGDERYVVEHDGERIV 307

                        330       340
                 ....*....|....*....|..
gi 648533720 333 FPNPTVKPGLRAGLLVVDTTAD 354
Cdd:PRK05324 308 FPNPNVAIGLRAGLMLVPTTLD 329
arg_catab_astE TIGR03242
succinylglutamate desuccinylase; Members of this protein family are succinylglutamate ...
 18-349 2.39e-153

succinylglutamate desuccinylase; Members of this protein family are succinylglutamate desuccinylase, the fifth and final enzyme of the arginine succinyltransferase (AST) pathway for arginine catabolism. This model excludes the related protein aspartoacylase. [Energy metabolism, Amino acids and amines]


Pssm-ID: 132286  Cd Length: 319  Bit Score: 434.10  E-value: 2.39e-153
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648533720   18 DFLAWTLAGSRPaaHQAQGTcANGVRWTWQGDGVLVIEPAERHAdiRSVLVSAGVHGDETAPIELLSRIVADIAQGRAVL 97
Cdd:TIGR03242   1 DFLALTLTGKKP--HVTQGE-TNNVRWRWLGEGVLELTPHAPPQ--KSLVISAGIHGNETAPIEILEQLLGDIAAGKLPL 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648533720   98 ACRLLVILGNIEAMRDGGRYRDDDLNRLFSGRHLQLPHSHEAPRAAALEQAATRFFADASAApGARWHIDMHTAIRASVF 177
Cdd:TIGR03242  76 RVRLLVILGNPPAMRTGKRYLHDDLNRMFGGRYQQLAPSFETCRAAELEQCVEDFFSQGGRS-VARWHYDLHTAIRGSLH 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648533720  178 ERFALLPHTGKPFSRAMFEWLGDARISAVLLHTTKGNTYSHFTAQACGADACTLELGKVRPFGENDLTRFEGADLAVRAL 257
Cdd:TIGR03242 155 EQFALLPYQGRPWDREFLTWLGAAGLDALVFHTEPGGTFSHFSSEHFGALACTLELGKALPFGQNDLSQFAAITSALRAL 234

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648533720  258 LAGTRVDSRANTQAdaqaalpRVFTVVDQLTKQSDAFELLLAPDVPNFTPLVKGSLLARDGDYQYTVQRDQERIVFPNPT 337
Cdd:TIGR03242 235 ISDEAIPARRTDPL-------RLFRVVSSITKHSDSFELHVASDTLNFTPFPKGTLLATDGNERYRVTHEGERILFPNPN 307

                         330
                  ....*....|..
gi 648533720  338 VKPGLRAGLLVV 349
Cdd:TIGR03242 308 VANGLRAGLMLV 319
AstE COG2988
Succinylglutamate desuccinylase [Amino acid transport and metabolism];
45-351 3.62e-129

Succinylglutamate desuccinylase [Amino acid transport and metabolism];


Pssm-ID: 442227  Cd Length: 305  Bit Score: 371.87  E-value: 3.62e-129
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648533720  45 TWQGDGVLVIEPAerHADIRSVLVSAGVHGDETAPIELLSRIVADIAQGRAVLACRLLVILGNIEAMRDGGRYRDDDLNR 124
Cdd:COG2988    8 RWLDEGVLELTPH--APGIKAVVISGGIHGNETAPIELLDKLLQDLLLGERPLSFRLLLILGNPAAMRAGRRYLDEDLNR 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648533720 125 LFSGRHLQLPHSHEAPRAAALEQAATRFFADASaapGARWHIDMHTAIRASVFERFALLPHTGKPFSRAMFEWLGDARIS 204
Cdd:COG2988   86 LFGGRHLQNPESYEAARAKELEQAVGPFFAAGG---RVRLHIDLHTAIRNSGHERFAVYPFRGRPFDLALLAYLAAAGPE 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648533720 205 AVLLHTTKGNTYSHFTAQACGADACTLELGKVRPFGENDLTRFEGADLAVRALLAGTRVDSRANTQadaqaalPRVFTVV 284
Cdd:COG2988  163 AVVLHHAPGGTFSHFSAELCGAQAFTLELGKVRPFGQNDLSRFAATEEALRALLSGAELPEHPAQD-------LDLYRVV 235

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 648533720 285 DQLTKQSDAFELLLAPDVPNFTPLVKGSLLARDGDYQYTVQRDQERIVFPNPTVKPGLRAGLLVVDT 351
Cdd:COG2988  236 QQIIKHGDDFMLHPDLDTLNFTPLPPGTLLAEDGGKEYRVEGDEERIVFPNEAVYYGQRAALLLTPK 302
M14_ASTE cd03855
Peptidase M14 Succinylglutamate desuccinylase (ASTE) subfamily; Peptidase M14 ...
 18-260 2.14e-112

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: 326.85  E-value: 2.14e-112
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648533720  18 DFLAWTLAGSrPAAHQAQGTCANGVRWTWQGDGVLVIEPAERHAdiRSVLVSAGVHGDETAPIELLSRIVADIAQGRAVL 97
Cdd:cd03855    1 DFLALTLSGS-EPAEGELAAVSNGTRVRWLATGVLELTPAASAS--KSVVLSAGIHGNETAPIEILDQLINDLIRGELAL 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648533720  98 ACRLLVILGNIEAMRDGGRYRDDDLNRLFSGRHLQLPHSHEAPRAAALEQAATRFFADASAAPgaRWHIDMHTAIRASVF 177
Cdd:cd03855   78 AHRLLFIFGNPPAIRQGKRFIEENLNRLFSGRHSKLPPSYETARAAELEQAVADFFAKASGEV--RWHLDLHTAIRGSKH 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648533720 178 ERFALLPHT-GKPFSRAMFEWLGDARISAVLLHTTKGNTYSHFTAQACGADACTLELGKVRPFGENDLTRFEGADLAVRA 256
Cdd:cd03855  156 EQFAVYPFLeGRPHDREQLDFLGAAGIEAVLLSNSPGGTFSYYSSEHFGAAAFTVELGKVRPFGQNDLSQFAAIDQALRA 235


                 ....
gi 648533720 257 LLAG 260
Cdd:cd03855  236 LISG 239
AstE_AspA pfam04952
Succinylglutamate desuccinylase / Aspartoacylase family; This family includes ...
 62-349 2.83e-59

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: 192.95  E-value: 2.83e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648533720   62 DIRSVLVSAGVHGDETAPIELLSRIVADIAQGrAVLACRLLVILGNIEAMRDGGRYRDDDLNRLFSGRHLQLPhSHEAPR 141
Cdd:pfam04952   1 PGPTLLLSAGIHGNETNGVELLRRLLRQLDPG-DIAGERTLVPLANPPAFRAGSRYIPRDLNRSFPGRALGAS-SDEPYR 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648533720  142 AAALEQAATRFFADASaaPGARWHIDMHTAIRASVFERFALLPHtgKPFSRAMFEWLGDARISAVLLHTTKGN-TYSHFT 220
Cdd:pfam04952  79 ATRAERLADLFFPALL--PRADIVLDLHTGTRGMGHLLFALAPI--RDDPLHLLALLRAFGAPAVLKLHSKPSaGFSAFS 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648533720  221 AQACGADACTLELGKVRPFGENDLTRFEGADLAVRALLagtrvdSRANTQADAqAALPRVFTVVDQLTKQSD-------- 292
Cdd:pfam04952 155 AEELGAPGFTLELGGAGPFGANLISRTAAGVLNVLRLI------GVLNGGPDA-FEPPKLYRVLREIDRPRDiraelagl 227

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 648533720  293 -AFELLLAPDVPNFTPLVKGSLLARDGDYQYTVQRDQ-ERIVFPNPTVKPGLRAGLLVV 349
Cdd:pfam04952 228 vEFALNLGDDVDAGPLLPGGPLFAPFGGEETEYRAPEdGYPVFPNEAAYVGKGAALALV 286
 
Name Accession Description Interval E-value
PRK05324 PRK05324
succinylglutamate desuccinylase; Provisional
 13-354 0e+00

succinylglutamate desuccinylase; Provisional


Pssm-ID: 235408  Cd Length: 329  Bit Score: 520.89  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648533720  13 SAMLDDFLAWTLAGSRPAahQAQGTCANGVRWTWQGDGVLVIEPAERHAdiRSVLVSAGVHGDETAPIELLSRIVADIAQ 92
Cdd:PRK05324   1 MLAMDDFLALTLAGHPPA--VTEFGLGNGVRWRWLGEGVLELTPAAPST--KALVLSAGIHGNETAPIELLDQLVRDLLA 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648533720  93 GRAVLACRLLVILGNIEAMRDGGRYRDDDLNRLFSGRHLQLPHSHEAPRAAALEQAATRFFAdaSAAPGARWHIDMHTAI 172
Cdd:PRK05324  77 GELPLRARLLVILGNPPAMRAGKRYLDEDLNRLFGGRHQQFPGSDEARRAAELEQAVEDFFA--AGAERVRWHYDLHTAI 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648533720 173 RASVFERFALLPHTGKPFSRAMFEWLGDARISAVLLHTTKGNTYSHFTAQACGADACTLELGKVRPFGENDLTRFEGADL 252
Cdd:PRK05324 155 RGSKHEQFAVLPQRGRPWSREQLAWLGAAGIEAVLLHNAPGGTFSHFSSEHFGALACTLELGKVLPFGQNDLSRFAATDQ 234

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648533720 253 AVRALLAGTRVDSRAntqadaqAALPRVFTVVDQLTKQSDAFELLLAPDVPNFTPLVKGSLLARDGDYQYTVQRDQERIV 332
Cdd:PRK05324 235 ALRALISGEELPERS-------ADPPRLYRVVRQITKHSDDFELHFADDVENFTAFPKGTLLAEDGDERYVVEHDGERIV 307

                        330       340
                 ....*....|....*....|..
gi 648533720 333 FPNPTVKPGLRAGLLVVDTTAD 354
Cdd:PRK05324 308 FPNPNVAIGLRAGLMLVPTTLD 329
arg_catab_astE TIGR03242
succinylglutamate desuccinylase; Members of this protein family are succinylglutamate ...
 18-349 2.39e-153

succinylglutamate desuccinylase; Members of this protein family are succinylglutamate desuccinylase, the fifth and final enzyme of the arginine succinyltransferase (AST) pathway for arginine catabolism. This model excludes the related protein aspartoacylase. [Energy metabolism, Amino acids and amines]


Pssm-ID: 132286  Cd Length: 319  Bit Score: 434.10  E-value: 2.39e-153
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648533720   18 DFLAWTLAGSRPaaHQAQGTcANGVRWTWQGDGVLVIEPAERHAdiRSVLVSAGVHGDETAPIELLSRIVADIAQGRAVL 97
Cdd:TIGR03242   1 DFLALTLTGKKP--HVTQGE-TNNVRWRWLGEGVLELTPHAPPQ--KSLVISAGIHGNETAPIEILEQLLGDIAAGKLPL 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648533720   98 ACRLLVILGNIEAMRDGGRYRDDDLNRLFSGRHLQLPHSHEAPRAAALEQAATRFFADASAApGARWHIDMHTAIRASVF 177
Cdd:TIGR03242  76 RVRLLVILGNPPAMRTGKRYLHDDLNRMFGGRYQQLAPSFETCRAAELEQCVEDFFSQGGRS-VARWHYDLHTAIRGSLH 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648533720  178 ERFALLPHTGKPFSRAMFEWLGDARISAVLLHTTKGNTYSHFTAQACGADACTLELGKVRPFGENDLTRFEGADLAVRAL 257
Cdd:TIGR03242 155 EQFALLPYQGRPWDREFLTWLGAAGLDALVFHTEPGGTFSHFSSEHFGALACTLELGKALPFGQNDLSQFAAITSALRAL 234

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648533720  258 LAGTRVDSRANTQAdaqaalpRVFTVVDQLTKQSDAFELLLAPDVPNFTPLVKGSLLARDGDYQYTVQRDQERIVFPNPT 337
Cdd:TIGR03242 235 ISDEAIPARRTDPL-------RLFRVVSSITKHSDSFELHVASDTLNFTPFPKGTLLATDGNERYRVTHEGERILFPNPN 307

                         330
                  ....*....|..
gi 648533720  338 VKPGLRAGLLVV 349
Cdd:TIGR03242 308 VANGLRAGLMLV 319
AstE COG2988
Succinylglutamate desuccinylase [Amino acid transport and metabolism];
45-351 3.62e-129

Succinylglutamate desuccinylase [Amino acid transport and metabolism];


Pssm-ID: 442227  Cd Length: 305  Bit Score: 371.87  E-value: 3.62e-129
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648533720  45 TWQGDGVLVIEPAerHADIRSVLVSAGVHGDETAPIELLSRIVADIAQGRAVLACRLLVILGNIEAMRDGGRYRDDDLNR 124
Cdd:COG2988    8 RWLDEGVLELTPH--APGIKAVVISGGIHGNETAPIELLDKLLQDLLLGERPLSFRLLLILGNPAAMRAGRRYLDEDLNR 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648533720 125 LFSGRHLQLPHSHEAPRAAALEQAATRFFADASaapGARWHIDMHTAIRASVFERFALLPHTGKPFSRAMFEWLGDARIS 204
Cdd:COG2988   86 LFGGRHLQNPESYEAARAKELEQAVGPFFAAGG---RVRLHIDLHTAIRNSGHERFAVYPFRGRPFDLALLAYLAAAGPE 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648533720 205 AVLLHTTKGNTYSHFTAQACGADACTLELGKVRPFGENDLTRFEGADLAVRALLAGTRVDSRANTQadaqaalPRVFTVV 284
Cdd:COG2988  163 AVVLHHAPGGTFSHFSAELCGAQAFTLELGKVRPFGQNDLSRFAATEEALRALLSGAELPEHPAQD-------LDLYRVV 235

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 648533720 285 DQLTKQSDAFELLLAPDVPNFTPLVKGSLLARDGDYQYTVQRDQERIVFPNPTVKPGLRAGLLVVDT 351
Cdd:COG2988  236 QQIIKHGDDFMLHPDLDTLNFTPLPPGTLLAEDGGKEYRVEGDEERIVFPNEAVYYGQRAALLLTPK 302
M14_ASTE cd03855
Peptidase M14 Succinylglutamate desuccinylase (ASTE) subfamily; Peptidase M14 ...
 18-260 2.14e-112

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: 326.85  E-value: 2.14e-112
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648533720  18 DFLAWTLAGSrPAAHQAQGTCANGVRWTWQGDGVLVIEPAERHAdiRSVLVSAGVHGDETAPIELLSRIVADIAQGRAVL 97
Cdd:cd03855    1 DFLALTLSGS-EPAEGELAAVSNGTRVRWLATGVLELTPAASAS--KSVVLSAGIHGNETAPIEILDQLINDLIRGELAL 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648533720  98 ACRLLVILGNIEAMRDGGRYRDDDLNRLFSGRHLQLPHSHEAPRAAALEQAATRFFADASAAPgaRWHIDMHTAIRASVF 177
Cdd:cd03855   78 AHRLLFIFGNPPAIRQGKRFIEENLNRLFSGRHSKLPPSYETARAAELEQAVADFFAKASGEV--RWHLDLHTAIRGSKH 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648533720 178 ERFALLPHT-GKPFSRAMFEWLGDARISAVLLHTTKGNTYSHFTAQACGADACTLELGKVRPFGENDLTRFEGADLAVRA 256
Cdd:cd03855  156 EQFAVYPFLeGRPHDREQLDFLGAAGIEAVLLSNSPGGTFSYYSSEHFGAAAFTVELGKVRPFGQNDLSQFAAIDQALRA 235


                 ....
gi 648533720 257 LLAG 260
Cdd:cd03855  236 LISG 239
AstE_AspA pfam04952
Succinylglutamate desuccinylase / Aspartoacylase family; This family includes ...
 62-349 2.83e-59

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: 192.95  E-value: 2.83e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648533720   62 DIRSVLVSAGVHGDETAPIELLSRIVADIAQGrAVLACRLLVILGNIEAMRDGGRYRDDDLNRLFSGRHLQLPhSHEAPR 141
Cdd:pfam04952   1 PGPTLLLSAGIHGNETNGVELLRRLLRQLDPG-DIAGERTLVPLANPPAFRAGSRYIPRDLNRSFPGRALGAS-SDEPYR 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648533720  142 AAALEQAATRFFADASaaPGARWHIDMHTAIRASVFERFALLPHtgKPFSRAMFEWLGDARISAVLLHTTKGN-TYSHFT 220
Cdd:pfam04952  79 ATRAERLADLFFPALL--PRADIVLDLHTGTRGMGHLLFALAPI--RDDPLHLLALLRAFGAPAVLKLHSKPSaGFSAFS 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648533720  221 AQACGADACTLELGKVRPFGENDLTRFEGADLAVRALLagtrvdSRANTQADAqAALPRVFTVVDQLTKQSD-------- 292
Cdd:pfam04952 155 AEELGAPGFTLELGGAGPFGANLISRTAAGVLNVLRLI------GVLNGGPDA-FEPPKLYRVLREIDRPRDiraelagl 227

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 648533720  293 -AFELLLAPDVPNFTPLVKGSLLARDGDYQYTVQRDQ-ERIVFPNPTVKPGLRAGLLVV 349
Cdd:pfam04952 228 vEFALNLGDDVDAGPLLPGGPLFAPFGGEETEYRAPEdGYPVFPNEAAYVGKGAALALV 286
M14_ASTE_ASPA_like cd06230
Peptidase M14 Succinylglutamate desuccinylase (ASTE)/aspartoacylase (ASPA) subfamily; The ...
 66-257 4.66e-21

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: 88.91  E-value: 4.66e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648533720  66 VLVSAGVHGDETAPIELLSRIVADIAQGRavLACRLLVI-LGNIEAMRDGGRYRDD---DLNRLFSGRHLQlphSHEAPR 141
Cdd:cd06230    1 LLILAGVHGDEYEGVEAIRRLLAELDPSE--LKGTVVLVpVANPPAFEAGTRYTPLdglDLNRIFPGDPDG---SPTERL 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648533720 142 AAALEQAATRfFADAsaapgarwHIDMHTAIRASVFERFAL-LPHTGKPFSRAMFEWLGDARIsaVLLHTTKGNTYSHfT 220
Cdd:cd06230   76 AHELTELILK-HADA--------LIDLHSGGTGRLVPYAILdYDSDAREKSRELARAFGGTPV--IWGGDPPGGTPVA-A 143

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 648533720 221 AQACGADACTLELGKVrpfGENDLTRFEGADLAVRAL 257
Cdd:cd06230  144 ARSAGIPAITVELGGG---GRLRAERLERYLRGIRNV 177
COG3608 COG3608
Predicted deacylase [General function prediction only];
66-341 2.41e-12

Predicted deacylase [General function prediction only];


Pssm-ID: 442826 [Multi-domain]  Cd Length: 296  Bit Score: 66.79  E-value: 2.41e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648533720  66 VLVSAGVHGDETAPIELLSRIVADIAQGRavLACRLLVI-LGNIEAMRDGGRY--RDD-DLNRLFSGRhlqLPHSHEAPR 141
Cdd:COG3608   29 LLITAGIHGDELNGIEALRRLLRELDPGE--LRGTVILVpVANPPGFLQGSRYlpIDGrDLNRSFPGD---ADGSLAERI 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648533720 142 AAALEQAatrffadasAAPGARWHIDMHTAIRASVFERFALLpHTGKPFSRAMFEWLGdarISAVLLHTTKGNTYSHFTA 221
Cdd:COG3608  104 AHALFEE---------ILPDADYVIDLHSGGIARDNLPHVRA-GPGDEELRALARAFG---APVILDSPEGGDGSLREAA 170

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648533720 222 QACGADACTLELGkvrpfGENDLTRfEGADLAVRALLagtRV-------DSRANTQADAQAALPRVFTVVdqLTKQSDAF 294
Cdd:COG3608  171 AEAGIPALTLELG-----GGGRFDE-ESIEAGVRGIL---NVlrhlgmlDGEAPPPPLAPPVLARGSEWV--RAPAGGLF 239

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 648533720 295 ElllaPDVPNFTPLVKGSLLAR----DGDYQYTVQRDQERIVF---PNPTVKPG 341
Cdd:COG3608  240 E----PLVELGDRVKKGDVLGRitdpFGEEVEEVRAPVDGIVIgrrTNPLVNPG 289
M14_ASTE_ASPA-like cd06251
Peptidase M14 Succinylglutamate desuccinylase (ASTE)/aspartoacylase (ASPA)-like; ...
 51-247 1.10e-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: 349469 [Multi-domain]  Cd Length: 195  Bit Score: 54.47  E-value: 1.10e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648533720  51 VLVIEPAErhaDIRSVLVSAGVHGDETAPIELLSRIVADIAqgRAVLACRLLVILG-NIEAMRDGGRY---RDDDLNRLF 126
Cdd:cd06251    3 VLVARGAK---PGPTLLLTAAIHGDELNGIEVIQRLLEDLD--PSKLRGTLIAIPVvNPLGFENNSRYlpdDGRDLNRSF 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648533720 127 SGrhlqlphsHEAPRAAalEQAATRFFADASAAPGArwHIDMHTA--IRASVFERFALLPHtgkPFSRAMFEWLGdariS 204
Cdd:cd06251   78 PG--------SEKGSLA--SRLAHLLWNEIVKKADY--VIDLHTAstGRTNLPYVRADLRD---PESRRMAEAFG----A 138

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 648533720 205 AVLLHTTKGNTYSHFTAQACGADACTLELGKVRPFGENDLTRF 247
Cdd:cd06251  139 PVIVDDPGEDGSLRGAAVELGIPAITVELGEALRFDEDIIRRG 181
PRK02259 PRK02259
aspartoacylase; Provisional
 63-147 1.35e-07

aspartoacylase; Provisional


Pssm-ID: 235019  Cd Length: 288  Bit Score: 52.18  E-value: 1.35e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648533720  63 IRSVLVSAGVHGDETAPIELLSRIVA--DIAQgRAVLACrlLVILGNIEAMRDGGRYRDDDLNRLFSGRHLQLP--HSHE 138
Cdd:PRK02259   2 INRVAIVGGTHGNEITGIYLVKKWQQqpNLIN-RKGLEV--QTVIGNPEAIEAGRRYIDRDLNRSFRLDLLQNPdlSGYE 78


                 ....*....
gi 648533720 139 APRAAALEQ 147
Cdd:PRK02259  79 QLRAKELVQ 87
M14_ASTE_ASPA_like cd18430
Succinylglutamate desuccinylase/aspartoacylase; uncharacterized; A functionally ...
 66-145 2.25e-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: 50.14  E-value: 2.25e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648533720  66 VLVSAGVHGDETAPIELLSRIVADIAQGrAVLACRLLVILGNIEAMRDGGRYRDDDLNRLFSGRhlQLPHSHEAPRAAAL 145
Cdd:cd18430    1 LAVLGAVHGNETCGTRAVERLLAELPSG-ALQKGPVTLVPANERAYAEGVRFCEEDLNRVFPGD--PDPDTYERRLANRL 77
Peptidase_M14_like cd00596
M14 family of metallocarboxypeptidases and related proteins; The M14 family of ...
 66-244 9.36e-07

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: 49.00  E-value: 9.36e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648533720  66 VLVSAGVHGDETAPIELLSRIVADIAQGRA-------VLACRLLVI-----LGNIEAMRDGGRY--RDDDLNRLF----S 127
Cdd:cd00596    1 ILITGGIHGNEVIGVELALALIEYLLENYGndplkrlLDNVELWIVplvnpDGFARVIDSGGRKnaNGVDLNRNFpynwG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648533720 128 GRHLQLPHSHEAPRAAALEQAATRFFADASAAPGARWHIDMHTAIRASVFerfallPHTGKPFSRAMFEWLGD--ARISA 205
Cdd:cd00596   81 KDGTSGPSSPTYRGPAPFSEPETQALRDLAKSHRFDLAVSYHSSSEAILY------PYGYTNEPPPDFSEFQElaAGLAR 154

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 648533720 206 VLLHTTKGNTYSH-----------FTAQACGADACTLELGKVRPFGENDL 244
Cdd:cd00596  155 ALGAGEYGYGYSYtwysttgtaddWLYGELGILAFTVELGTADYPLPGTL 204
M14_ASPA cd06909
Peptidase M14 Aspartoacylase (ASPA) subfamily; Aspartoacylase (ASPA) belongs to the ...
 64-170 9.72e-07

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: 48.74  E-value: 9.72e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648533720  64 RSVLVSAGVHGDETAPIELLSRIVADIAQ-GRAVLACRLLviLGNIEAMRDGGRYRDDDLNRLFSGRHLQLPHS---HEA 139
Cdd:cd06909    1 KRVAIVGGTHGNELTGVYLVKHWLKNPELiERKSFEVHPL--LANPRAVEQCRRYIDTDLNRCFSLENLSSAPSslpYEV 78

                         90       100       110
                 ....*....|....*....|....*....|.
gi 648533720 140 PRAAALEQaatrFFADAsAAPGARWHIDMHT 170
Cdd:cd06909   79 RRAREINQ----ILGPK-GNPACDFIIDLHN 104
M14_ASTE_ASPA-like cd06254
Peptidase M14 Succinylglutamate desuccinylase (ASTE)/aspartoacylase (ASPA)-like; ...
 66-234 4.47e-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: 349472  Cd Length: 198  Bit Score: 43.72  E-value: 4.47e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648533720  66 VLVSAGVHGDETAPIELLSRIVADIAQGRavLACRLLVI-LGNIEAM---------RDGgryrdDDLNRLFSGRhlqlPH 135
Cdd:cd06254   14 LLITAGIHGGEYPGILAAIRLARELDPAD--VKGTLIIVhIANVSGFeartpfvvpEDG-----KNLNRVFPGD----PD 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648533720 136 SHEAPRAAALeqAATRFFadasaaPGARWHIDMHTAIRASVFERFALLPHTGKP----FSRAMFEWLGdarISAVLLHTT 211
Cdd:cd06254   83 GTLTERIAYF--LTREII------SRADFLIDLHGGDANEALTPFVYYPGGASEevndISRAAAQALG---LPYIVISSS 151

                        170       180
                 ....*....|....*....|...
gi 648533720 212 KGNTYSHFTAQACGADACTLELG 234
Cdd:cd06254  152 EKGTGYYSYAALRGIPSILVERG 174
M14_REP34-like cd06231
Peptidase M14-like domain similar to rapid encystment phenotype 34 (REP34); This family ...
 51-169 6.40e-05

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: 43.84  E-value: 6.40e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648533720  51 VLVIEPAERHADIRsVLVSAGVHGDETAP----IELLSRIVADIAQGRAVLACRLLvilgNIEAMRDGGRYRDD--DLNR 124
Cdd:cd06231   31 FALKSPNPRGDKPR-VLISAGIHGDEPAGvealLRFLESLAEKYLRRVNLLVLPCV----NPWGFERNTRENADgiDLNR 105

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 648533720 125 LFSgrhlqlpHSHEAPRAAALEQaatrffadaSAAPGARW--HIDMH 169
Cdd:cd06231  106 SFL-------KDSPSPEVRALME---------FLASLGRFdlHLDLH 136
M14_ASTE_ASPA-like cd06256
Peptidase M14 Succinylglutamate desuccinylase (ASTE)/aspartoacylase (ASPA)-like; ...
 56-128 2.53e-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: 41.51  E-value: 2.53e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 648533720  56 PAERHadiRSVLVSAGVHGDETAPIELLSRIVADiaqGRAVLACRLLVILGNIEAMRDGGRYRDD--DLNRLFSG 128
Cdd:cd06256   30 PGRRP---RPLFVSTLLHGNEPTGLRAVQRLLKT---GQAPLPRTLLLFIGNVDAAKAGVRRLPGqpDYNRCWPG 98
M14_MpaA-like cd06904
Peptidase M14-like domain of Escherichia coli Murein Peptide Amidase A and related proteins; ...
 60-126 5.87e-04

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: 40.72  E-value: 5.87e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648533720  60 HADIRSVLVSAGVHGDETAPIELLSRIVADIAQGRAVLACRLLVI-LGNIEAMRDGGRY--RDDDLNRLF 126
Cdd:cd06904   20 PGSRARILIIGGIHGDEPEGVSLVEHLLRWLKNHPASGDFHIVVVpCLNPDGLAAGTRTnaNGVDLNRNF 89
M14_ASTE_ASPA_like cd18174
Peptidase M14 Succinylglutamate desuccinylase (ASTE)/aspartoacylase (ASPA)-like; ...
 66-234 6.99e-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: 349484  Cd Length: 187  Bit Score: 40.30  E-value: 6.99e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648533720  66 VLVSAGVHGDETAPIELLSRIVADI--AQGRAVLacrLLVILGNIEAMR---------DGgryrdDDLNRLFSGRhlqlp 134
Cdd:cd18174    1 LLVTAGVHGYEYASIEALQRLIKELdpAKLSGTV---IVVPIANIPAFEgrsiyvnplDG-----KNLNRSFPGD----- 67

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648533720 135 hsheaPRAAALEQAA----TRFFADASAApgarwhIDMHTAIRASVFERFALLPHTGKPF----SRAMFEWLGDARI--S 204
Cdd:cd18174   68 -----PDGTPTERLAhwltTNVIARADYY------IDLHGGDLNEDLRPFVYYYETGNAAldaaSREMAEAFGLDHIvfY 136

                        170       180       190
                 ....*....|....*....|....*....|
gi 648533720 205 AVLLHTTKGNTYSHFTAQACGADACTLELG 234
Cdd:cd18174  137 KARLKASRGSLYTQAAALLRGIPAILVEAG 166
 
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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