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Conserved domains on  [gi|1498198185|gb|RMG53228|]
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succinylglutamate desuccinylase [Acidobacteria bacterium]

Protein Classification

M14_ASTE_ASPA_like and Biotinyl_lipoyl_domains domain-containing protein( domain architecture ID 13031230)

M14_ASTE_ASPA_like and Biotinyl_lipoyl_domains domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
M14_ASTE_ASPA_like cd18174
Peptidase M14 Succinylglutamate desuccinylase (ASTE)/aspartoacylase (ASPA)-like; ...
 64-250 6.14e-103

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


:

Pssm-ID: 349484  Cd Length: 187  Bit Score: 300.31  E-value: 6.14e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198185  64 LALIAGNHGYEYAPILALQRLRGRLDPEALAGTIIMVHVANMPSFLRRTIYYSPIDGKNLNRVYPGKKDGTVSERIAYAI 143
Cdd:cd18174     1 LLVTAGVHGYEYASIEALQRLIKELDPAKLSGTVIVVPIANIPAFEGRSIYVNPLDGKNLNRSFPGDPDGTPTERLAHWL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198185 144 TQHVIERCDYLIDLHCGDGNESLRPYTYWPKTGNAQLDERAKQMALAFGLDHIVIDTDRPTDPRHSIYCSNTATTRGKPA 223
Cdd:cd18174    81 TTNVIARADYYIDLHGGDLNEDLRPFVYYYETGNAALDAASREMAEAFGLDHIVFYKARLKASRGSLYTQAAALLRGIPA 160

                         170       180
                  ....*....|....*....|....*..
gi 1498198185 224 ITTESGGLGQTDEPSIARIERGVMSVL 250
Cdd:cd18174   161 ILVEAGGLGSRDEEDVARHVEGVLNVL 187
Biotinyl_lipoyl_domains super family cl11404
Biotinyl_lipoyl_domains are present in biotin-dependent carboxylases/decarboxylases, the ...
 274-339 6.35e-03

Biotinyl_lipoyl_domains are present in biotin-dependent carboxylases/decarboxylases, the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases, and the H-protein of the glycine cleavage system (GCS). These domains transport CO2, acyl, or methylamine, respectively, between components of the complex/protein via a biotinyl or lipoyl group, which is covalently attached to a highly conserved lysine residue.


The actual alignment was detected with superfamily member cd06850:

Pssm-ID: 448245 [Multi-domain]  Cd Length: 67  Bit Score: 34.70  E-value: 6.35e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1498198185 274 VIRSRVTGLFY-PLVKKGIAVTKGTVLGYItdffgrrIA-----DVRAPLSGIVLYILGTP--PVSPNEPLAFV 339
Cdd:cd06850     1 EVTAPMPGTVVkVLVKEGDKVEAGQPLAVL-------EAmkmenEVTAPVAGVVKEILVKEgdQVEAGQLLVVI 67
 
Name Accession Description Interval E-value
M14_ASTE_ASPA_like cd18174
Peptidase M14 Succinylglutamate desuccinylase (ASTE)/aspartoacylase (ASPA)-like; ...
 64-250 6.14e-103

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


Pssm-ID: 349484  Cd Length: 187  Bit Score: 300.31  E-value: 6.14e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198185  64 LALIAGNHGYEYAPILALQRLRGRLDPEALAGTIIMVHVANMPSFLRRTIYYSPIDGKNLNRVYPGKKDGTVSERIAYAI 143
Cdd:cd18174     1 LLVTAGVHGYEYASIEALQRLIKELDPAKLSGTVIVVPIANIPAFEGRSIYVNPLDGKNLNRSFPGDPDGTPTERLAHWL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198185 144 TQHVIERCDYLIDLHCGDGNESLRPYTYWPKTGNAQLDERAKQMALAFGLDHIVIDTDRPTDPRHSIYCSNTATTRGKPA 223
Cdd:cd18174    81 TTNVIARADYYIDLHGGDLNEDLRPFVYYYETGNAALDAASREMAEAFGLDHIVFYKARLKASRGSLYTQAAALLRGIPA 160

                         170       180
                  ....*....|....*....|....*..
gi 1498198185 224 ITTESGGLGQTDEPSIARIERGVMSVL 250
Cdd:cd18174   161 ILVEAGGLGSRDEEDVARHVEGVLNVL 187
COG3608 COG3608
Predicted deacylase [General function prediction only];
47-340 1.39e-101

Predicted deacylase [General function prediction only];


Pssm-ID: 442826 [Multi-domain]  Cd Length: 296  Bit Score: 301.00  E-value: 1.39e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198185  47 GTRIPISVLHGRRPGPVLALIAGNHGYEYAPILALQRLRGRLDPEALAGTIIMVHVANMPSFLRRTiYYSPIDGKNLNRV 126
Cdd:COG3608    12 PVSLPVTVFRGAGPGPTLLITAGIHGDELNGIEALRRLLRELDPGELRGTVILVPVANPPGFLQGS-RYLPIDGRDLNRS 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198185 127 YPGKKDGTVSERIAYAITQHVIERCDYLIDLHCGDGNESLRPYTYWPKTgnaqlDERAKQMALAFGLDHIVIDTDRPTDP 206
Cdd:COG3608    91 FPGDADGSLAERIAHALFEEILPDADYVIDLHSGGIARDNLPHVRAGPG-----DEELRALARAFGAPVILDSPEGGDGS 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198185 207 RhsiycSNTATTRGKPAITTESGGLGQTDEPSIARIERGVMSVLRWLHMLDGE--PRFVEHPIWIDRSEVIRSRVTGLFY 284
Cdd:COG3608   166 L-----REAAAEAGIPALTLELGGGGRFDEESIEAGVRGILNVLRHLGMLDGEapPPPLAPPVLARGSEWVRAPAGGLFE 240

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1498198185 285 PLVKKGIAVTKGTVLGYITDFFGRRIADVRAPLSGIVLYILGTPPVSPNEPLAFVG 340
Cdd:COG3608   241 PLVELGDRVKKGDVLGRITDPFGEEVEEVRAPVDGIVIGRRTNPLVNPGDALFHIA 296
AstE_AspA pfam04952
Succinylglutamate desuccinylase / Aspartoacylase family; This family includes ...
 60-340 1.40e-40

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: 144.03  E-value: 1.40e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198185  60 PGPVLALIAGNHGYEYAPILALQRLRGRLDPEALAGTIIMVHVANMPSFL--RRTIYyspidgKNLNRVYPGKKDG---- 133
Cdd:pfam04952   1 PGPTLLLSAGIHGNETNGVELLRRLLRQLDPGDIAGERTLVPLANPPAFRagSRYIP------RDLNRSFPGRALGassd 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198185 134 -----TVSERIAYAITQHVIERCDYLIDLHCGDGNESLRPYTYWPktgnaQLDERAKQMAL--AFGLDHIVIDTDRPTDP 206
Cdd:pfam04952  75 epyraTRAERLADLFFPALLPRADIVLDLHTGTRGMGHLLFALAP-----IRDDPLHLLALlrAFGAPAVLKLHSKPSAG 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198185 207 rhsiYCSNTATTRGKPAITTESGGLGQTDEPSIARIERGVMSVLRWLHMLDGEPRFVEHPIW------IDRSEVIRSRVT 280
Cdd:pfam04952 150 ----FSAFSAEELGAPGFTLELGGAGPFGANLISRTAAGVLNVLRLIGVLNGGPDAFEPPKLyrvlreIDRPRDIRAELA 225

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1498198185 281 GLFYPLVKKGIAVTKGTVL--GYITDFFGRRIADVRAPLSGIVLYILGTPPVSPNEPLAFVG 340
Cdd:pfam04952 226 GLVEFALNLGDDVDAGPLLpgGPLFAPFGGEETEYRAPEDGYPVFPNEAAYVGKGAALALVA 287
biotinyl_domain cd06850
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all ...
 274-339 6.35e-03

The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all biotin-dependent enzymes, such as acetyl-CoA carboxylase, pyruvate carboxylase, propionyl-CoA carboxylase, methylcrotonyl-CoA carboxylase, geranyl-CoA carboxylase, oxaloacetate decarboxylase, methylmalonyl-CoA decarboxylase, transcarboxylase and urea amidolyase. This domain functions in transferring CO2 from one subsite to another, allowing carboxylation, decarboxylation, or transcarboxylation. During this process, biotin is covalently attached to a specific lysine.


Pssm-ID: 133459 [Multi-domain]  Cd Length: 67  Bit Score: 34.70  E-value: 6.35e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1498198185 274 VIRSRVTGLFY-PLVKKGIAVTKGTVLGYItdffgrrIA-----DVRAPLSGIVLYILGTP--PVSPNEPLAFV 339
Cdd:cd06850     1 EVTAPMPGTVVkVLVKEGDKVEAGQPLAVL-------EAmkmenEVTAPVAGVVKEILVKEgdQVEAGQLLVVI 67
 
Name Accession Description Interval E-value
M14_ASTE_ASPA_like cd18174
Peptidase M14 Succinylglutamate desuccinylase (ASTE)/aspartoacylase (ASPA)-like; ...
 64-250 6.14e-103

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


Pssm-ID: 349484  Cd Length: 187  Bit Score: 300.31  E-value: 6.14e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198185  64 LALIAGNHGYEYAPILALQRLRGRLDPEALAGTIIMVHVANMPSFLRRTIYYSPIDGKNLNRVYPGKKDGTVSERIAYAI 143
Cdd:cd18174     1 LLVTAGVHGYEYASIEALQRLIKELDPAKLSGTVIVVPIANIPAFEGRSIYVNPLDGKNLNRSFPGDPDGTPTERLAHWL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198185 144 TQHVIERCDYLIDLHCGDGNESLRPYTYWPKTGNAQLDERAKQMALAFGLDHIVIDTDRPTDPRHSIYCSNTATTRGKPA 223
Cdd:cd18174    81 TTNVIARADYYIDLHGGDLNEDLRPFVYYYETGNAALDAASREMAEAFGLDHIVFYKARLKASRGSLYTQAAALLRGIPA 160

                         170       180
                  ....*....|....*....|....*..
gi 1498198185 224 ITTESGGLGQTDEPSIARIERGVMSVL 250
Cdd:cd18174   161 ILVEAGGLGSRDEEDVARHVEGVLNVL 187
COG3608 COG3608
Predicted deacylase [General function prediction only];
47-340 1.39e-101

Predicted deacylase [General function prediction only];


Pssm-ID: 442826 [Multi-domain]  Cd Length: 296  Bit Score: 301.00  E-value: 1.39e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198185  47 GTRIPISVLHGRRPGPVLALIAGNHGYEYAPILALQRLRGRLDPEALAGTIIMVHVANMPSFLRRTiYYSPIDGKNLNRV 126
Cdd:COG3608    12 PVSLPVTVFRGAGPGPTLLITAGIHGDELNGIEALRRLLRELDPGELRGTVILVPVANPPGFLQGS-RYLPIDGRDLNRS 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198185 127 YPGKKDGTVSERIAYAITQHVIERCDYLIDLHCGDGNESLRPYTYWPKTgnaqlDERAKQMALAFGLDHIVIDTDRPTDP 206
Cdd:COG3608    91 FPGDADGSLAERIAHALFEEILPDADYVIDLHSGGIARDNLPHVRAGPG-----DEELRALARAFGAPVILDSPEGGDGS 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198185 207 RhsiycSNTATTRGKPAITTESGGLGQTDEPSIARIERGVMSVLRWLHMLDGE--PRFVEHPIWIDRSEVIRSRVTGLFY 284
Cdd:COG3608   166 L-----REAAAEAGIPALTLELGGGGRFDEESIEAGVRGILNVLRHLGMLDGEapPPPLAPPVLARGSEWVRAPAGGLFE 240

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1498198185 285 PLVKKGIAVTKGTVLGYITDFFGRRIADVRAPLSGIVLYILGTPPVSPNEPLAFVG 340
Cdd:COG3608   241 PLVELGDRVKKGDVLGRITDPFGEEVEEVRAPVDGIVIGRRTNPLVNPGDALFHIA 296
M14_ASTE_ASPA-like cd06254
Peptidase M14 Succinylglutamate desuccinylase (ASTE)/aspartoacylase (ASPA)-like; ...
 51-253 1.80e-89

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: 266.75  E-value: 1.80e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198185  51 PISVLHGRRPGPVLALIAGNHGYEYAPILALQRLRGRLDPEALAGTIIMVHVANMPSFLRRTIYYSPIDGKNLNRVYPGK 130
Cdd:cd06254     1 PVTLINGAKPGPTLLITAGIHGGEYPGILAAIRLARELDPADVKGTLIIVHIANVSGFEARTPFVVPEDGKNLNRVFPGD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198185 131 KDGTVSERIAYAITQHVIERCDYLIDLHCGDGNESLRPYTYWPKTGNAQLDERAKQMALAFGLDHIVIdtdrpTDPRHSI 210
Cdd:cd06254    81 PDGTLTERIAYFLTREIISRADFLIDLHGGDANEALTPFVYYPGGASEEVNDISRAAAQALGLPYIVI-----SSSEKGT 155

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1498198185 211 YCSNTATTRGKPAITTESGGLGQTDEPSIARIERGVMSVLRWL 253
Cdd:cd06254   156 GYYSYAALRGIPSILVERGGLGTCDEEDVQAHKDGIKNLLRHL 198
M14_ASTE_ASPA-like cd06251
Peptidase M14 Succinylglutamate desuccinylase (ASTE)/aspartoacylase (ASPA)-like; ...
 50-256 8.06e-51

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: 167.72  E-value: 8.06e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198185  50 IPISVLHGRRPGPVLALIAGNHGYEYAPILALQRLRGRLDPEALAGTIIMVHVANMPSFLRRTIYYsPIDGKNLNRVYPG 129
Cdd:cd06251     1 VPVLVARGAKPGPTLLLTAAIHGDELNGIEVIQRLLEDLDPSKLRGTLIAIPVVNPLGFENNSRYL-PDDGRDLNRSFPG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198185 130 KKDGTVSERIAYAITQHVIERCDYLIDLHCGDGNESLRPYTYwpktgnAQL-DERAKQMALAFGLDHIVIDTDRPtdprH 208
Cdd:cd06251    80 SEKGSLASRLAHLLWNEIVKKADYVIDLHTASTGRTNLPYVR------ADLrDPESRRMAEAFGAPVIVDDPGED----G 149

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1498198185 209 SIycSNTATTRGKPAITTESGGLGQTDEPSIARIERGVMSVLRWLHML 256
Cdd:cd06251   150 SL--RGAAVELGIPAITVELGEALRFDEDIIRRGVEGVLNVLRHLGML 195
M14_ASTE_ASPA-like cd06252
Peptidase M14 Succinylglutamate desuccinylase (ASTE)/aspartoacylase (ASPA)-like; ...
 36-256 1.37e-49

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: 165.44  E-value: 1.37e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198185  36 GFIEVPPGVDEGT----RIPISVLHGRrPGPVLALIAGNHGYEYAPILALQRLRGRLDPEALAGTIIMVHVANMPSFL-- 109
Cdd:cd06252     6 GFLRLPLSDDRSAwgaiPIPITVINNG-SGPTVLLTGGNHGDEYEGPIALRRLARDLDPEDVRGRLIIVPALNLPAVRag 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198185 110 RRTiyySPIDGKNLNRVYPGKKDGTVSERIAYAITQHVIERCDYLIDLHCGDGNESLRPYTYWPKTGNAQLDERAKQMAL 189
Cdd:cd06252    85 TRT---SPLDGGNLNRAFPGDADGTPTERIAHFLETVLLPRADAVIDLHSGGSSLDFVPCAAVHLLPDPAQRARSLALAE 161

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1498198185 190 AFGLDHIVIDTDRPTDPrhsiYCSNTATTRGKPAITTESGGLGQTDEPSIARIERGVMSVLRWLHML 256
Cdd:cd06252   162 AFGAPLSVVVDNVDAPG----TLDSAAERAGKIFVSTELGGGGTVTPAALRIAERGVLNVLIHLGVL 224
M14_ASTE_ASPA_like cd06230
Peptidase M14 Succinylglutamate desuccinylase (ASTE)/aspartoacylase (ASPA) subfamily; The ...
 64-246 3.47e-47

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: 157.47  E-value: 3.47e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198185  64 LALIAGNHGYEYAPILALQRLRGRLDPEALAGTIIMVHVANMPSFLRRTiYYSPIDGKNLNRVYPGKKDGTVSERIAYAI 143
Cdd:cd06230     1 LLILAGVHGDEYEGVEAIRRLLAELDPSELKGTVVLVPVANPPAFEAGT-RYTPLDGLDLNRIFPGDPDGSPTERLAHEL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198185 144 TQHVIERCDYLIDLHCGdGNESLRPYTYWPKTGNAqlDERAKQMALAFG-LDHIVIDTDRPTDPRHsiycsnTATTRGKP 222
Cdd:cd06230    80 TELILKHADALIDLHSG-GTGRLVPYAILDYDSDA--REKSRELARAFGgTPVIWGGDPPGGTPVA------AARSAGIP 150

                         170       180
                  ....*....|....*....|....
gi 1498198185 223 AITTESGGLGQTDEPSIARIERGV 246
Cdd:cd06230   151 AITVELGGGGRLRAERLERYLRGI 174
M14_ASTE_ASPA-like cd06255
Peptidase M14 Succinylglutamate desuccinylase (ASTE)/aspartoacylase (ASPA)-like; ...
 49-256 3.16e-43

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: 149.01  E-value: 3.16e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198185  49 RIPISVLHGRRPGPVLALIAGNHGYEYAPILALQRLRGRLDPEALAGTIIMVHVANMPSFLRRTiYYSPIDGKNLNRVYP 128
Cdd:cd06255    11 TIPVIVVRGAKPGPCLWINGAVHGDELNGPLAALELFRELDPAQLSGTLVATPIANPLAFQGRQ-KFSPQDGEDLDQSFP 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198185 129 GKKDGTVSERIAYAITQHVIERCDYLIDLHCGDGNESLRPYTYW--PKTGNAQLDERAKQMALAFGLD-HIVIDTDRPTD 205
Cdd:cd06255    90 GDPDGLITERMAHALFSEVKEVADYLIDFHTGGTPFDANPYTVYklFPESGPVEEKRLLRLARAFGVHaNCRVDVSGAGG 169

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1498198185 206 ---PRHSIYCSNTATTRGKPAITTESGGLGQTDEPSIARIERGVMSVLRWLHML 256
Cdd:cd06255   170 elpGNTAGALDYQCMAQGIPAFMVELGGGGRAEEEAVRFAARGLRNLLRYLGML 223
AstE_AspA pfam04952
Succinylglutamate desuccinylase / Aspartoacylase family; This family includes ...
 60-340 1.40e-40

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: 144.03  E-value: 1.40e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198185  60 PGPVLALIAGNHGYEYAPILALQRLRGRLDPEALAGTIIMVHVANMPSFL--RRTIYyspidgKNLNRVYPGKKDG---- 133
Cdd:pfam04952   1 PGPTLLLSAGIHGNETNGVELLRRLLRQLDPGDIAGERTLVPLANPPAFRagSRYIP------RDLNRSFPGRALGassd 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198185 134 -----TVSERIAYAITQHVIERCDYLIDLHCGDGNESLRPYTYWPktgnaQLDERAKQMAL--AFGLDHIVIDTDRPTDP 206
Cdd:pfam04952  75 epyraTRAERLADLFFPALLPRADIVLDLHTGTRGMGHLLFALAP-----IRDDPLHLLALlrAFGAPAVLKLHSKPSAG 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198185 207 rhsiYCSNTATTRGKPAITTESGGLGQTDEPSIARIERGVMSVLRWLHMLDGEPRFVEHPIW------IDRSEVIRSRVT 280
Cdd:pfam04952 150 ----FSAFSAEELGAPGFTLELGGAGPFGANLISRTAAGVLNVLRLIGVLNGGPDAFEPPKLyrvlreIDRPRDIRAELA 225

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1498198185 281 GLFYPLVKKGIAVTKGTVL--GYITDFFGRRIADVRAPLSGIVLYILGTPPVSPNEPLAFVG 340
Cdd:pfam04952 226 GLVEFALNLGDDVDAGPLLpgGPLFAPFGGEETEYRAPEDGYPVFPNEAAYVGKGAALALVA 287
M14_ASTE_ASPA-like cd06253
Peptidase M14 Succinylglutamate desuccinylase (ASTE)/aspartoacylase (ASPA)-like; ...
 38-253 2.94e-20

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: 87.65  E-value: 2.94e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198185  38 IEVPpgVDEGTRIPISVLHGRRPGPVLALIAGNHGYEYAPILALQRLRGRLD-----PEALAGTIIMVHVANMPSFLRRT 112
Cdd:cd06253     1 LESP--FREPLEVKGFRFGGGNAEPRIAIVAGIHGDELNGLYVCSRLIRFLKeleegGYKLKGKVLVIPAVNPLGINSGT 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198185 113 iYYSPIDGKNLNRVYPGKKDGTVSERIAYAITQHvIERCDYLIDLHCGDGneslrPYTYWP-----KTGNAQLDErakqM 187
Cdd:cd06253    79 -RFWPFDNLDMNRMFPGYNKGETTERIAAALFED-LKGADYGIDLHSSND-----FLREIPqvrviESGAQDLLP----L 147

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1498198185 188 ALAFGLDHIVIDTDRPTDprhsiycsnTAT------TRGKPAITTESGGLGQTDEPSIARIERGVMSVLRWL 253
Cdd:cd06253   148 AKFLGLDVVWVHPASTVD---------TGTlaynwnEWGTKALVLEMGVGMRIDKEYCEQLFEGILRFLLKM 210
M14_ASTE_ASPA_like cd18430
Succinylglutamate desuccinylase/aspartoacylase; uncharacterized; A functionally ...
 64-158 2.41e-06

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: 47.05  E-value: 2.41e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198185  64 LALIAGNHGYEYAPILALQRLRGRLDPEAL-AGTIIMVhVANMPSFLRRTIYyspIDgKNLNRVYPGKKDGTVSE-RIAY 141
Cdd:cd18430     1 LAVLGAVHGNETCGTRAVERLLAELPSGALqKGPVTLV-PANERAYAEGVRF---CE-EDLNRVFPGDPDPDTYErRLAN 75

                          90
                  ....*....|....*..
gi 1498198185 142 AITQhVIERCDYLIDLH 158
Cdd:cd18430    76 RLCP-ELEGHDVVLDLH 91
M14_CP_Csd4-like cd06243
Peptidase M14 carboxypeptidase Csd4 and similar proteins; This family includes peptidase M14 ...
 57-208 5.14e-06

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: 46.97  E-value: 5.14e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198185  57 GRRPGPVLALIAGNHGYEYAPILALQRLRgrlDPEALAGTIIMVHVANMPSFLRRTIYYspiDGkNLNR----VYPGKKD 132
Cdd:cd06243    12 GREPGPTLLIIGGIQGDEPGGFLAADLLA---DLYLVKGNVIVVPRLNFPSILRNHRGL---NG-DMNRkfaaLDKKDPE 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198185 133 GTVSERIAYAITQhviERCDYLIDLHCGDG------NESLRPYTYWpktGNAqlderakqmalafgldhIVIDTDRPTDP 206
Cdd:cd06243    85 YKTIQEIKSLIAD---FRPDVVLHLHDGSGfyrpnyVDAMRNPKRW---GQS-----------------IIIDQDRYKTA 141


                  ..
gi 1498198185 207 RH 208
Cdd:cd06243   142 KF 143
M14_PaAOTO_like cd06250
Peptidase M14 Succinylglutamate desuccinylase (ASTE)/aspartoacylase (ASPA)-like subfamily; ...
 42-254 6.61e-05

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: 43.76  E-value: 6.61e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198185  42 PGVDEGTRIPISVLH--GRRPGPVLALIAGNHGYEYAPILALQRLRGRLD----PEALAGTIIMVHVANmPSFLRRTIY- 114
Cdd:cd06250     6 DSPAPGTERSLTVFRfgGAGAGPKVYIQAALHADELPGNLVIHHLLERLKaleaAGRIKGEIVLVPQAN-PIGLSQKIGg 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198185 115 -----YSPIDGKNLNRVYP----------GKKDGTVSERIAYAITQHVIERC-----------------------DYLID 156
Cdd:cd06250    85 yhqgrFDLATGDNFNRNFPdlakavaarvEERLGDDAAANVALIRAALKEALdalpprtelqrlkltllrlaldaDIVLD 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198185 157 LHCGDgnESLRpYTYwpktGNAQLDERAKQMALAFGLDHIVI---DTDRPTDPRHSI-------YCSNTATTRGKPAITT 226
Cdd:cd06250   165 LHCDD--EALR-HLY----TPPALWPAAEDLAAALGAPAVLLadnSGGGAFDEAFSKpwlrlaeAFPGAPIPLACFSATV 237

                         250       260
                  ....*....|....*....|....*....
gi 1498198185 227 ESGglGQTD-EPSIARIErgVMSVLRWLH 254
Cdd:cd06250   238 ELR--GQADvDDELARAD--AEGILRFLA 262
M14_ASTE_ASPA-like cd06256
Peptidase M14 Succinylglutamate desuccinylase (ASTE)/aspartoacylase (ASPA)-like; ...
 53-251 9.75e-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: 9.75e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198185  53 SVLH--GRRPGPVL--ALIagnHGYEYAPILALQRL----RGRLdPEALAGTIIMVHVANMPsfLRRtiyyspIDGK-NL 123
Cdd:cd06256    25 TLIHlpGRRPRPLFvsTLL---HGNEPTGLRAVQRLlktgQAPL-PRTLLLFIGNVDAAKAG--VRR------LPGQpDY 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498198185 124 NRVYPGKKDgTVSERIAyaitQHVIERCDYL-----IDLHcgdGNESLRPytywPKTGNAQLDERAKQMALAFGLDHIVI 198
Cdd:cd06256    93 NRCWPGPFE-TPEGRLA----AAVLERLDTLrpfasIDIH---NNTGKNP----HYACVNRLDAAHLRLASLFSRTLVYF 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1498198185 199 DTDRPTdprhsiycSNTATTRGKPAITTESGGLGqtDEPSIARIERGVMSVLR 251
Cdd:cd06256   161 TRPLGV--------LSEALAALCPAVTVECGKPG--DAEGEEHAAEGLDAFLH 203
biotinyl_domain cd06850
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all ...
 274-339 6.35e-03

The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all biotin-dependent enzymes, such as acetyl-CoA carboxylase, pyruvate carboxylase, propionyl-CoA carboxylase, methylcrotonyl-CoA carboxylase, geranyl-CoA carboxylase, oxaloacetate decarboxylase, methylmalonyl-CoA decarboxylase, transcarboxylase and urea amidolyase. This domain functions in transferring CO2 from one subsite to another, allowing carboxylation, decarboxylation, or transcarboxylation. During this process, biotin is covalently attached to a specific lysine.


Pssm-ID: 133459 [Multi-domain]  Cd Length: 67  Bit Score: 34.70  E-value: 6.35e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1498198185 274 VIRSRVTGLFY-PLVKKGIAVTKGTVLGYItdffgrrIA-----DVRAPLSGIVLYILGTP--PVSPNEPLAFV 339
Cdd:cd06850     1 EVTAPMPGTVVkVLVKEGDKVEAGQPLAVL-------EAmkmenEVTAPVAGVVKEILVKEgdQVEAGQLLVVI 67
 
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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