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Conserved domains on  [gi|763177151|ref|WP_044056798|]
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allantoate amidohydrolase [Alteromonas australica]

Protein Classification

Zn-dependent hydrolase( domain architecture ID 11483787)

M20 family Zn-dependent hydrolase similar to allantoate amidohydrolase, which converts allantoate to (S)-ureidoglycolate and ammonia

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK09290 PRK09290
allantoate amidohydrolase; Reviewed
 5-408 0e+00

allantoate amidohydrolase; Reviewed


:

Pssm-ID: 236456 [Multi-domain]  Cd Length: 413  Bit Score: 530.11  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763177151   5 ADAAAQVMARCETLGTL-SQDPSCLDRRYLTEQHKLANQLTSGWMIEAGMTTWQDAAGNIWGRYSSAVPNAPRMILGSHL 83
Cdd:PRK09290   3 RIDAERLWARLDELAKIgATPDGGVTRLALSPEDLQARDLFAEWMEAAGLTVRVDAVGNLFGRLEGRDPDAPAVLTGSHL 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763177151  84 DTVPNGGKYDGMLGVVAAITLVALFNGEQKKFPYHIDIVGFCDEEGTRFGTTLLGSRALTGKW-QDEWRRLKDENGVSLE 162
Cdd:PRK09290  83 DTVPNGGRFDGPLGVLAGLEAVRTLNERGIRPRRPIEVVAFTNEEGSRFGPAMLGSRVFTGALtPEDALALRDADGVSFA 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763177151 163 QAMAEFGLNFDEVPSAAIPATDVLAYLELHIEQGPVLEQENLPIGVVSAIAGAKRFNINVQGMAGHAGTVPMSMRHDALC 242
Cdd:PRK09290 163 EALAAIGYDGDEAVGAARARRDIKAFVELHIEQGPVLEAEGLPIGVVTGIVGQRRYRVTFTGEANHAGTTPMALRRDALL 242

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763177151 243 ASAEMLLAVESISQQRA-GVVATVGKIENAPNGVNVISGKTVFSLDIRSEDDNLRDAVLAEILQKFEHIAALRNVKLEIE 321
Cdd:PRK09290 243 AAAEIILAVERIAAAHGpDLVATVGRLEVKPNSVNVIPGEVTFTLDIRHPDDAVLDALVAELRAAAEAIAARRGVEVEIE 322

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763177151 322 QTHSAPAVLCDEALKAALVKGVEASNIPAKILASGAGHDAMAMAELCPVAMLFTRCKGGISHHPAESITHQDVEASLSAL 401
Cdd:PRK09290 323 LISRRPPVPFDPGLVAALEEAAERLGLSYRRLPSGAGHDAQILAAVVPTAMIFVPSVGGISHNPAEFTSPEDCAAGANVL 402


                 ....*..
gi 763177151 402 HHTIGAL 408
Cdd:PRK09290 403 LHALLEL 409
 
Name Accession Description Interval E-value
PRK09290 PRK09290
allantoate amidohydrolase; Reviewed
 5-408 0e+00

allantoate amidohydrolase; Reviewed


Pssm-ID: 236456 [Multi-domain]  Cd Length: 413  Bit Score: 530.11  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763177151   5 ADAAAQVMARCETLGTL-SQDPSCLDRRYLTEQHKLANQLTSGWMIEAGMTTWQDAAGNIWGRYSSAVPNAPRMILGSHL 83
Cdd:PRK09290   3 RIDAERLWARLDELAKIgATPDGGVTRLALSPEDLQARDLFAEWMEAAGLTVRVDAVGNLFGRLEGRDPDAPAVLTGSHL 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763177151  84 DTVPNGGKYDGMLGVVAAITLVALFNGEQKKFPYHIDIVGFCDEEGTRFGTTLLGSRALTGKW-QDEWRRLKDENGVSLE 162
Cdd:PRK09290  83 DTVPNGGRFDGPLGVLAGLEAVRTLNERGIRPRRPIEVVAFTNEEGSRFGPAMLGSRVFTGALtPEDALALRDADGVSFA 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763177151 163 QAMAEFGLNFDEVPSAAIPATDVLAYLELHIEQGPVLEQENLPIGVVSAIAGAKRFNINVQGMAGHAGTVPMSMRHDALC 242
Cdd:PRK09290 163 EALAAIGYDGDEAVGAARARRDIKAFVELHIEQGPVLEAEGLPIGVVTGIVGQRRYRVTFTGEANHAGTTPMALRRDALL 242

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763177151 243 ASAEMLLAVESISQQRA-GVVATVGKIENAPNGVNVISGKTVFSLDIRSEDDNLRDAVLAEILQKFEHIAALRNVKLEIE 321
Cdd:PRK09290 243 AAAEIILAVERIAAAHGpDLVATVGRLEVKPNSVNVIPGEVTFTLDIRHPDDAVLDALVAELRAAAEAIAARRGVEVEIE 322

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763177151 322 QTHSAPAVLCDEALKAALVKGVEASNIPAKILASGAGHDAMAMAELCPVAMLFTRCKGGISHHPAESITHQDVEASLSAL 401
Cdd:PRK09290 323 LISRRPPVPFDPGLVAALEEAAERLGLSYRRLPSGAGHDAQILAAVVPTAMIFVPSVGGISHNPAEFTSPEDCAAGANVL 402


                 ....*..
gi 763177151 402 HHTIGAL 408
Cdd:PRK09290 403 LHALLEL 409
M20_bAS cd03884
M20 Peptidase beta-alanine synthase, an amidohydrolase; Peptidase M20 family, beta-alanine ...
 11-405 2.63e-176

M20 Peptidase beta-alanine synthase, an amidohydrolase; Peptidase M20 family, beta-alanine synthase (bAS; N-carbamoyl-beta-alanine amidohydrolase and beta-ureidopropionase; EC 3.5.1.6) subfamily. bAS is an amidohydrolase and is the final enzyme in the pyrimidine catabolic pathway, which is involved in the regulation of the cellular pyrimidine pool. bAS catalyzes the irreversible hydrolysis of the N-carbamylated beta-amino acids to beta-alanine or aminoisobutyrate with the release of carbon dioxide and ammonia. Also included in this subfamily is allantoate amidohydrolase (allantoate deiminase), which catalyzes the conversion of allantoate to (S)-ureidoglycolate, one of the crucial alternate steps in purine metabolism. It is possible that these two enzymes arose from the same ancestral peptidase that evolved into two structurally related enzymes with distinct catalytic properties and biochemical roles within the cell. Downstream enzyme (S)-ureidoglycolate amidohydrolase (UAH) is homologous in structure and sequence with AAH and catalyzes the conversion of (S)-ureidoglycolate into glyoxylate, releasing two molecules of ammonia as by-products. Yeast requires beta-alanine as a precursor of pantothenate and coenzyme A biosynthesis, but generates it mostly via degradation of spermine. Disorders in pyrimidine degradation and beta-alanine metabolism caused by beta-ureidopropionase deficiency (UPB1 gene) in humans are normally associated with neurological disorders.


Pssm-ID: 349880 [Multi-domain]  Cd Length: 398  Bit Score: 497.43  E-value: 2.63e-176
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763177151  11 VMARCETLGTLSQDPSC-LDRRYLTEQHKLANQLTSGWMIEAGMTTWQDAAGNIWGRYSSAVPNAPRMILGSHLDTVPNG 89
Cdd:cd03884    1 LWDRLEELAAIGATPAGgVTRLALTDEDRAARDLFVEWMEEAGLSVRVDAVGNLFGRLEGTDPDAPPVLTGSHLDTVPNG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763177151  90 GKYDGMLGVVAAITLVALFNGEQKKFPYHIDIVGFCDEEGTRFGTTLLGSRALTGKWQDEW-RRLKDENGVSLEQAMAEF 168
Cdd:cd03884   81 GRYDGILGVLAGLEALRALKEAGIRPRRPIEVVAFTNEEGSRFPPSMLGSRAFAGTLDLEElLSLRDADGVSLAEALKAI 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763177151 169 GLNFDEVPSAaIPATDVLAYLELHIEQGPVLEQENLPIGVVSAIAGAKRFNINVQGMAGHAGTVPMSMRHDALCASAEML 248
Cdd:cd03884  161 GYDGDRPASA-RRPGDIKAYVELHIEQGPVLEEEGLPIGVVTGIAGQRWLEVTVTGEAGHAGTTPMALRRDALLAAAELI 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763177151 249 LAVESISQQRA-GVVATVGKIENAPNGVNVISGKTVFSLDIRSEDDNLRDAVLAEILQKFEHIAALRNVKLEIEQTHSAP 327
Cdd:cd03884  240 LAVEEIALEHGdDLVATVGRIEVKPNAVNVIPGEVEFTLDLRHPDDAVLDAMVERIRAEAEAIAAERGVEVEVERLWDSP 319

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 763177151 328 AVLCDEALKAALVKGVEASNIPAKILASGAGHDAMAMAELCPVAMLFTRCKGGISHHPAESITHQDVEASLSALHHTI 405
Cdd:cd03884  320 PVPFDPELVAALEAAAEALGLSYRRMPSGAGHDAMFMARICPTAMIFVPSRDGISHNPAEYTSPEDLAAGVQVLLHAL 397
hydantase TIGR01879
amidase, hydantoinase/carbamoylase family; Enzymes in this subfamily hydrolize the amide bonds ...
 14-405 7.46e-127

amidase, hydantoinase/carbamoylase family; Enzymes in this subfamily hydrolize the amide bonds of compounds containing carbamoyl groups or hydantoin rings. These enzymes are members of the broader family of amidases represented by pfam01546.


Pssm-ID: 200138 [Multi-domain]  Cd Length: 400  Bit Score: 372.22  E-value: 7.46e-127
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763177151   14 RCETLGTLSQDPSC-LDRRYLTEQHKLANQLTSGWMIEAGMTTWQDAAGNIWGRYSSAVPNAPRMILGSHLDTVPNGGKY 92
Cdd:TIGR01879   6 TLMWLGEVGADPAGgMTRLALSPEDREAQDLFKKRMRAAGLEVRFDEVGNLIGRKEGTEPPLEVVLSGSHLDTVVNGGNF 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763177151   93 DGMLGVVAAITLVALFNgEQKKFPYH-IDIVGFCDEEGTRFGTTLLGSRALTG--KWQDeWRRLKDENGVSLEQAMAEFG 169
Cdd:TIGR01879  86 DGQLGVLAGIEVVDALK-EAYVVPLHpIEVVAFTEEEGSRFPYGMWGSRNMVGlaNPED-VRNICDAKGISFAEAMKACG 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763177151  170 lnFDEVPSAAIPATDVLAYLELHIEQGPVLEQENLPIGVVSAIAGAKRFNINVQGMAGHAGTVPMSMRHDALCASAEMLL 249
Cdd:TIGR01879 164 --PDLPNQPLRPRGDIKAYVELHIEQGPVLESNGQPIGVVNAIAGQRWYKVTLNGESNHAGTTPMSLRRDPLVAASRIIH 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763177151  250 AVESISQQRAGVVATVGKIENAPNGVNVISGKTVFSLDIRSEDDNLRDAVLAEILQKFEHIAALRNVKLEIEQTHSAPAV 329
Cdd:TIGR01879 242 QVEEKAKRGDPTVGTVGKVEARPNGVNVIPGKVTFTLDLRHTDAAVLRDFTQQLENDIKAISDERDIGIDIERWMDEPPV 321

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 763177151  330 LCDEALKAALVKGVEASNIPAKILASGAGHDAMAMAELCPVAMLFTRCKGGISHHPAESITHQDVEASLSALHHTI 405
Cdd:TIGR01879 322 PCSEELVAALTELCERLGYNARVMVSGAGHDAQILAPIVPIGMIFIPSINGISHNPAEWSNITDCAEGAKVLYLMV 397
Peptidase_M20 pfam01546
Peptidase family M20/M25/M40; This family includes a range of zinc metallopeptidases belonging ...
 78-405 3.62e-46

Peptidase family M20/M25/M40; This family includes a range of zinc metallopeptidases belonging to several families in the peptidase classification. Family M20 are Glutamate carboxypeptidases. Peptidase family M25 contains X-His dipeptidases.


Pssm-ID: 460247 [Multi-domain]  Cd Length: 315  Bit Score: 161.36  E-value: 3.62e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763177151   78 ILGSHLDTVPNG------------------GKYDGMLGVVAAITLVALFNgEQKKFPYHIDIVGFCDEEGTrfgttLLGS 139
Cdd:pfam01546   1 LLRGHMDVVPDEetwgwpfkstedgklygrGHDDMKGGLLAALEALRALK-EEGLKKGTVKLLFQPDEEGG-----MGGA 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763177151  140 RALTGKWQDEWRRLKdengvsleqamaefglnfdevpsaaipatdvlAYLELHIEQGPVLEqENLPIGVVSAIAGAKRFN 219
Cdd:pfam01546  75 RALIEDGLLEREKVD--------------------------------AVFGLHIGEPTLLE-GGIAIGVVTGHRGSLRFR 121

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763177151  220 INVQGMAGHAGTVPMsmRHDALCASAEMLLAVESISQQRAG----VVATVGKIENAPNGVNVISGKTVFSLDIRSEDDNL 295
Cdd:pfam01546 122 VTVKGKGGHASTPHL--GVNAIVAAARLILALQDIVSRNVDpldpAVVTVGNITGIPGGVNVIPGEAELKGDIRLLPGED 199

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763177151  296 RDAVLAEILQKFEHIAALRNVKLEIEQTHSAPAVLC-DEALKAALVKGV-EASNIPAKILASG--AGHDAMAMAELCPVA 371
Cdd:pfam01546 200 LEELEERIREILEAIAAAYGVKVEVEYVEGGAPPLVnDSPLVAALREAAkELFGLKVELIVSGsmGGTDAAFFLLGVPPT 279

                         330       340       350
                  ....*....|....*....|....*....|....
gi 763177151  372 MLFTRCKGGISHHPAESITHQDVEASLSALHHTI 405
Cdd:pfam01546 280 VVFFGPGSGLAHSPNEYVDLDDLEKGAKVLARLL 313
PepD2 COG2195
Di- or tripeptidase [Amino acid transport and metabolism];
35-397 1.34e-13

Di- or tripeptidase [Amino acid transport and metabolism];


Pssm-ID: 441798 [Multi-domain]  Cd Length: 364  Bit Score: 71.62  E-value: 1.34e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763177151  35 EQHKLANQLTSgWMIEAGMTTWQDAAGNIWGRYSSAVP-NAPRMILGSHLDTVP-----------NGG--KYDGM--LGV 98
Cdd:COG2195   21 HEEALADYLVE-ELKELGLEVEEDEAGNVIATLPATPGyNVPTIGLQAHMDTVPqfpgdgikpqiDGGliTADGTttLGA 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763177151  99 -----VAAItLVALFNGEQKKFPyHIDI-VGFC-DEEgtrfgTTLLGSRALTGKWqdewrrLKdengvsleqamAEFGLN 171
Cdd:COG2195  100 ddkagVAAI-LAALEYLKEPEIP-HGPIeVLFTpDEE-----IGLRGAKALDVSK------LG-----------ADFAYT 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763177151 172 FDevpsaaipatdvlaylelhieQGPV--LEQENlpigvvsaiAGAKRFNINVQGMAGHAGTVPMSMrhdalcASAeMLL 249
Cdd:COG2195  156 LD---------------------GGEEgeLEYEC---------AGAADAKITIKGKGGHSGDAKEKM------INA-IKL 198

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763177151 250 AVESISQQRAGVV-----ATVGKIE--NAPNGvnvISGKTVFSLDIRSEDDNLRDAVLAEILQKFEHIAALRNV-KLEIE 321
Cdd:COG2195  199 AARFLAALPLGRIpeeteGNEGFIHggSATNA---IPREAEAVYIIRDHDREKLEARKAELEEAFEEENAKYGVgVVEVE 275

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763177151 322 QTHSAPAV-------LCDEALKAAlvkgvEASNIPAKILASGAGHDA-----MAMaelcPVAMLFTrckgGIS--HHPAE 387
Cdd:COG2195  276 IEDQYPNWkpepdspIVDLAKEAY-----EELGIEPKIKPIRGGLDGgilsfKGL----PTPNLGP----GGHnfHSPDE 342

                        410
                 ....*....|
gi 763177151 388 SITHQDVEAS 397
Cdd:COG2195  343 RVSIESMEKA 352
 
Name Accession Description Interval E-value
PRK09290 PRK09290
allantoate amidohydrolase; Reviewed
 5-408 0e+00

allantoate amidohydrolase; Reviewed


Pssm-ID: 236456 [Multi-domain]  Cd Length: 413  Bit Score: 530.11  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763177151   5 ADAAAQVMARCETLGTL-SQDPSCLDRRYLTEQHKLANQLTSGWMIEAGMTTWQDAAGNIWGRYSSAVPNAPRMILGSHL 83
Cdd:PRK09290   3 RIDAERLWARLDELAKIgATPDGGVTRLALSPEDLQARDLFAEWMEAAGLTVRVDAVGNLFGRLEGRDPDAPAVLTGSHL 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763177151  84 DTVPNGGKYDGMLGVVAAITLVALFNGEQKKFPYHIDIVGFCDEEGTRFGTTLLGSRALTGKW-QDEWRRLKDENGVSLE 162
Cdd:PRK09290  83 DTVPNGGRFDGPLGVLAGLEAVRTLNERGIRPRRPIEVVAFTNEEGSRFGPAMLGSRVFTGALtPEDALALRDADGVSFA 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763177151 163 QAMAEFGLNFDEVPSAAIPATDVLAYLELHIEQGPVLEQENLPIGVVSAIAGAKRFNINVQGMAGHAGTVPMSMRHDALC 242
Cdd:PRK09290 163 EALAAIGYDGDEAVGAARARRDIKAFVELHIEQGPVLEAEGLPIGVVTGIVGQRRYRVTFTGEANHAGTTPMALRRDALL 242

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763177151 243 ASAEMLLAVESISQQRA-GVVATVGKIENAPNGVNVISGKTVFSLDIRSEDDNLRDAVLAEILQKFEHIAALRNVKLEIE 321
Cdd:PRK09290 243 AAAEIILAVERIAAAHGpDLVATVGRLEVKPNSVNVIPGEVTFTLDIRHPDDAVLDALVAELRAAAEAIAARRGVEVEIE 322

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763177151 322 QTHSAPAVLCDEALKAALVKGVEASNIPAKILASGAGHDAMAMAELCPVAMLFTRCKGGISHHPAESITHQDVEASLSAL 401
Cdd:PRK09290 323 LISRRPPVPFDPGLVAALEEAAERLGLSYRRLPSGAGHDAQILAAVVPTAMIFVPSVGGISHNPAEFTSPEDCAAGANVL 402


                 ....*..
gi 763177151 402 HHTIGAL 408
Cdd:PRK09290 403 LHALLEL 409
M20_bAS cd03884
M20 Peptidase beta-alanine synthase, an amidohydrolase; Peptidase M20 family, beta-alanine ...
 11-405 2.63e-176

M20 Peptidase beta-alanine synthase, an amidohydrolase; Peptidase M20 family, beta-alanine synthase (bAS; N-carbamoyl-beta-alanine amidohydrolase and beta-ureidopropionase; EC 3.5.1.6) subfamily. bAS is an amidohydrolase and is the final enzyme in the pyrimidine catabolic pathway, which is involved in the regulation of the cellular pyrimidine pool. bAS catalyzes the irreversible hydrolysis of the N-carbamylated beta-amino acids to beta-alanine or aminoisobutyrate with the release of carbon dioxide and ammonia. Also included in this subfamily is allantoate amidohydrolase (allantoate deiminase), which catalyzes the conversion of allantoate to (S)-ureidoglycolate, one of the crucial alternate steps in purine metabolism. It is possible that these two enzymes arose from the same ancestral peptidase that evolved into two structurally related enzymes with distinct catalytic properties and biochemical roles within the cell. Downstream enzyme (S)-ureidoglycolate amidohydrolase (UAH) is homologous in structure and sequence with AAH and catalyzes the conversion of (S)-ureidoglycolate into glyoxylate, releasing two molecules of ammonia as by-products. Yeast requires beta-alanine as a precursor of pantothenate and coenzyme A biosynthesis, but generates it mostly via degradation of spermine. Disorders in pyrimidine degradation and beta-alanine metabolism caused by beta-ureidopropionase deficiency (UPB1 gene) in humans are normally associated with neurological disorders.


Pssm-ID: 349880 [Multi-domain]  Cd Length: 398  Bit Score: 497.43  E-value: 2.63e-176
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763177151  11 VMARCETLGTLSQDPSC-LDRRYLTEQHKLANQLTSGWMIEAGMTTWQDAAGNIWGRYSSAVPNAPRMILGSHLDTVPNG 89
Cdd:cd03884    1 LWDRLEELAAIGATPAGgVTRLALTDEDRAARDLFVEWMEEAGLSVRVDAVGNLFGRLEGTDPDAPPVLTGSHLDTVPNG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763177151  90 GKYDGMLGVVAAITLVALFNGEQKKFPYHIDIVGFCDEEGTRFGTTLLGSRALTGKWQDEW-RRLKDENGVSLEQAMAEF 168
Cdd:cd03884   81 GRYDGILGVLAGLEALRALKEAGIRPRRPIEVVAFTNEEGSRFPPSMLGSRAFAGTLDLEElLSLRDADGVSLAEALKAI 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763177151 169 GLNFDEVPSAaIPATDVLAYLELHIEQGPVLEQENLPIGVVSAIAGAKRFNINVQGMAGHAGTVPMSMRHDALCASAEML 248
Cdd:cd03884  161 GYDGDRPASA-RRPGDIKAYVELHIEQGPVLEEEGLPIGVVTGIAGQRWLEVTVTGEAGHAGTTPMALRRDALLAAAELI 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763177151 249 LAVESISQQRA-GVVATVGKIENAPNGVNVISGKTVFSLDIRSEDDNLRDAVLAEILQKFEHIAALRNVKLEIEQTHSAP 327
Cdd:cd03884  240 LAVEEIALEHGdDLVATVGRIEVKPNAVNVIPGEVEFTLDLRHPDDAVLDAMVERIRAEAEAIAAERGVEVEVERLWDSP 319

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 763177151 328 AVLCDEALKAALVKGVEASNIPAKILASGAGHDAMAMAELCPVAMLFTRCKGGISHHPAESITHQDVEASLSALHHTI 405
Cdd:cd03884  320 PVPFDPELVAALEAAAEALGLSYRRMPSGAGHDAMFMARICPTAMIFVPSRDGISHNPAEYTSPEDLAAGVQVLLHAL 397
PRK12890 PRK12890
allantoate amidohydrolase; Reviewed
 1-408 1.93e-153

allantoate amidohydrolase; Reviewed


Pssm-ID: 237248 [Multi-domain]  Cd Length: 414  Bit Score: 440.11  E-value: 1.93e-153
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763177151   1 MTEFADAAAQVMARCETLGTLSQDPSCLDRRYLTEQHKLANQLTSGWMIEAGMTTWQDAAGNIWGRYSSAVPNAPRMILG 80
Cdd:PRK12890   1 TTPPPINGERLLARLEELAAIGRDGPGWTRLALSDEERAARALLAAWMRAAGLEVRRDAAGNLFGRLPGRDPDLPPLMTG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763177151  81 SHLDTVPNGGKYDGMLGVVAAITLVALFNGEQKKFPYHIDIVGFCDEEGTRFGTTLLGSRALTGKWQDEW-RRLKDENGV 159
Cdd:PRK12890  81 SHLDTVPNGGRYDGILGVLAGLEVVAALREAGIRPPHPLEVIAFTNEEGVRFGPSMIGSRALAGTLDVEAvLATRDDDGT 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763177151 160 SLEQAMAEFGLNFDEVPSAAIPATDVLAYLELHIEQGPVLEQENLPIGVVSAIAGAKRFNINVQGMAGHAGTVPMSMRHD 239
Cdd:PRK12890 161 TLAEALRRIGGDPDALPGALRPPGAVAAFLELHIEQGPVLEAEGLPIGVVTAIQGIRRQAVTVEGEANHAGTTPMDLRRD 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763177151 240 ALCASAEMLLAVES-ISQQRAGVVATVGKIENAPNGVNVISGKTVFSLDIRSEDDNLRDAVLAEILQKFEHIAALRNVKL 318
Cdd:PRK12890 241 ALVAAAELVTAMERrARALLHDLVATVGRLDVEPNAINVVPGRVVFTLDLRSPDDAVLEAAEAALLAELEAIAAARGVRI 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763177151 319 EIEQTHSAPAVLCDEALKAALVKGVEASNIPAKILASGAGHDAMAMAELCPVAMLFTRCKGGISHHPAESITHQDVEASL 398
Cdd:PRK12890 321 ELERLSRSEPVPCDPALVDAVEAAAARLGYPSRRMPSGAGHDAAAIARIGPSAMIFVPCRGGISHNPEEAMDPEDLAAGA 400

                        410
                 ....*....|
gi 763177151 399 SALHHTIGAL 408
Cdd:PRK12890 401 RVLLDAVLRL 410
PRK12893 PRK12893
Zn-dependent hydrolase;
30-404 3.97e-142

Zn-dependent hydrolase;


Pssm-ID: 237250 [Multi-domain]  Cd Length: 412  Bit Score: 411.20  E-value: 3.97e-142
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763177151  30 RRYLTEQHKLANQLTSGWMIEAGMTTWQDAAGNIWGRYSSAVPNAPRMILGSHLDTVPNGGKYDGMLGVVAAITLVALFN 109
Cdd:PRK12893  32 RLALTDEDREARDLLAQWMEEAGLTVSVDAIGNLFGRRAGTDPDAPPVLIGSHLDTQPTGGRFDGALGVLAALEVVRTLN 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763177151 110 GEQKKFPYHIDIVGFCDEEGTRFGTTLLGSRALTGKW-QDEWRRLKDENGVSLEQAMAEFGLnfdeVPSAAIPATDVLAY 188
Cdd:PRK12893 112 DAGIRTRRPIEVVSWTNEEGARFAPAMLGSGVFTGALpLDDALARRDADGITLGEALARIGY----RGTARVGRRAVDAY 187

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763177151 189 LELHIEQGPVLEQENLPIGVVSAIAGAKRFNINVQGMAGHAGTVPMSMRHDALCASAEMLLAVESISQQRA-GVVATVGK 267
Cdd:PRK12893 188 LELHIEQGPVLEAEGLPIGVVTGIQGIRWLEVTVEGQAAHAGTTPMAMRRDALVAAARIILAVERIAAALApDGVATVGR 267

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763177151 268 IENAPNGVNVISGKTVFSLDIRSEDDNLRDAVLAEILQKFEHIAALRNVKLEIEQTHSAPAVLCDEALKAALVKGVEASN 347
Cdd:PRK12893 268 LRVEPNSRNVIPGKVVFTVDIRHPDDARLDAMEAALRAACAKIAAARGVQVTVETVWDFPPVPFDPALVALVEAAAEALG 347

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 763177151 348 IPAKILASGAGHDAMAMAELCPVAMLFTRCKGGISHHPAESITHQDVEASLSALHHT 404
Cdd:PRK12893 348 LSHMRMVSGAGHDAMFLARVAPAAMIFVPCRGGISHNEAEDTEPADLAAGANVLLHA 404
hydantase TIGR01879
amidase, hydantoinase/carbamoylase family; Enzymes in this subfamily hydrolize the amide bonds ...
 14-405 7.46e-127

amidase, hydantoinase/carbamoylase family; Enzymes in this subfamily hydrolize the amide bonds of compounds containing carbamoyl groups or hydantoin rings. These enzymes are members of the broader family of amidases represented by pfam01546.


Pssm-ID: 200138 [Multi-domain]  Cd Length: 400  Bit Score: 372.22  E-value: 7.46e-127
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763177151   14 RCETLGTLSQDPSC-LDRRYLTEQHKLANQLTSGWMIEAGMTTWQDAAGNIWGRYSSAVPNAPRMILGSHLDTVPNGGKY 92
Cdd:TIGR01879   6 TLMWLGEVGADPAGgMTRLALSPEDREAQDLFKKRMRAAGLEVRFDEVGNLIGRKEGTEPPLEVVLSGSHLDTVVNGGNF 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763177151   93 DGMLGVVAAITLVALFNgEQKKFPYH-IDIVGFCDEEGTRFGTTLLGSRALTG--KWQDeWRRLKDENGVSLEQAMAEFG 169
Cdd:TIGR01879  86 DGQLGVLAGIEVVDALK-EAYVVPLHpIEVVAFTEEEGSRFPYGMWGSRNMVGlaNPED-VRNICDAKGISFAEAMKACG 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763177151  170 lnFDEVPSAAIPATDVLAYLELHIEQGPVLEQENLPIGVVSAIAGAKRFNINVQGMAGHAGTVPMSMRHDALCASAEMLL 249
Cdd:TIGR01879 164 --PDLPNQPLRPRGDIKAYVELHIEQGPVLESNGQPIGVVNAIAGQRWYKVTLNGESNHAGTTPMSLRRDPLVAASRIIH 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763177151  250 AVESISQQRAGVVATVGKIENAPNGVNVISGKTVFSLDIRSEDDNLRDAVLAEILQKFEHIAALRNVKLEIEQTHSAPAV 329
Cdd:TIGR01879 242 QVEEKAKRGDPTVGTVGKVEARPNGVNVIPGKVTFTLDLRHTDAAVLRDFTQQLENDIKAISDERDIGIDIERWMDEPPV 321

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 763177151  330 LCDEALKAALVKGVEASNIPAKILASGAGHDAMAMAELCPVAMLFTRCKGGISHHPAESITHQDVEASLSALHHTI 405
Cdd:TIGR01879 322 PCSEELVAALTELCERLGYNARVMVSGAGHDAQILAPIVPIGMIFIPSINGISHNPAEWSNITDCAEGAKVLYLMV 397
PRK13590 PRK13590
putative bifunctional OHCU decarboxylase/allantoate amidohydrolase; Provisional
 9-413 1.98e-123

putative bifunctional OHCU decarboxylase/allantoate amidohydrolase; Provisional


Pssm-ID: 184168 [Multi-domain]  Cd Length: 591  Bit Score: 369.85  E-value: 1.98e-123
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763177151   9 AQVMARCETLGTLSqDPSCLDR-----RYLTEQHKLANQLTSGWMIEAGMTTWQ-DAAGNIWGRYSSAVPNAPRMILGSH 82
Cdd:PRK13590 181 NDVWDWAERLAAHS-DPGYAEKgqltvTYLTDAHRACAQQISHWMRDCGFDEVHiDAVGNVVGRYKGSTPQAKRLLTGSH 259

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763177151  83 LDTVPNGGKYDGMLGVVAAITLVALFNGEQKKFPYHIDIVGFCDEEGTRFGTTLLGSRALTGKWQDEWRRLKDENGVSLE 162
Cdd:PRK13590 260 YDTVRNGGKYDGRLGIFVPMACVRELHRQGRRLPFGLEVVGFAEEEGQRYKATFLGSGALIGDFDPAWLDQKDADGITMR 339

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763177151 163 QAMAEFGLNFDEVPSAAIPATDVLAYLELHIEQGPVLEQENLPIGVVSAIAGAKRFNINVQGMAGHAGTVPMSMRHDALC 242
Cdd:PRK13590 340 EAMQHAGLCIDDIPKLRRDPARYLGFVEVHIEQGPVLNELDLPLGIVTSINGSVRYVGEMIGMASHAGTTPMDRRRDAAA 419

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763177151 243 ASAEMLLAVESISQQRAGVVATVGKIeNAPNG-VNVISGKTVFSLDIRSEDDNLRDAVLAEILQKFEHIAALRNVKLEIE 321
Cdd:PRK13590 420 AVAELALYVEQRAAQDGDSVGTVGML-EVPGGsINVVPGRCRFSLDIRAPTDAQRDAMVADVLAELEAICERRGLRYTLE 498

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763177151 322 QTHSAPAVLCDEALKAALVKGVEASNIPAKILASGAGHDAMAMAELCPVAMLFTRC-KGGISHHPAESITHQDVEASLSA 400
Cdd:PRK13590 499 ETMRAAAAPSAPAWQQRWEAAVAALGLPLFRMPSGAGHDAMKLHEIMPQAMLFVRGeNAGISHNPLESSTADDMQLAVQA 578

                        410
                 ....*....|...
gi 763177151 401 LHHTIGALHSNIS 413
Cdd:PRK13590 579 FQHLLDQLAAEQP 591
PRK13799 PRK13799
unknown domain/N-carbamoyl-L-amino acid hydrolase fusion protein; Provisional
 32-408 4.08e-121

unknown domain/N-carbamoyl-L-amino acid hydrolase fusion protein; Provisional


Pssm-ID: 106740 [Multi-domain]  Cd Length: 591  Bit Score: 363.95  E-value: 4.08e-121
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763177151  32 YLTEQHKLANQLTSGWMIEAGMTTWQ-DAAGNIWGRYSSAVPNAPRMILGSHLDTVPNGGKYDGMLGVVAAITLVALFNG 110
Cdd:PRK13799 208 YLSDAHRACANQISDWMRDAGFDEVEiDAVGNVVGRYKAADDDAKTLITGSHYDTVRNGGKYDGREGIFLAIACVKELHE 287

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763177151 111 EQKKFPYHIDIVGFCDEEGTRFGTTLLGSRALTGKWQDEWRRLKDENGVSLEQAMAEFGLNFDEVPSAAIPATDVLAYLE 190
Cdd:PRK13799 288 QGERLPFHFEVIAFAEEEGQRFKATFLGSGALIGDFNMELLDIKDADGISLREAIQHAGHCIDAIPKIARDPADVLGFIE 367

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763177151 191 LHIEQGPVLEQENLPIGVVSAIAGAKRFNINVQGMAGHAGTVPMSMRHDALCASAEMLLAVE--SISQQRAGVVATVGKI 268
Cdd:PRK13799 368 VHIEQGPVLLELDIPLGIVTSIAGSARYICEFIGMASHAGTTPMDMRKDAAAAAAEIALYIEkrAAQDQHASLVATMGQL 447

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763177151 269 eNAPNG-VNVISGKTVFSLDIRSEDDNLRDAVLAEILQKFEHIAALRNVKLEIEQTHSAPAVLCDEALKAALVKGVEASN 347
Cdd:PRK13799 448 -NVPSGsTNVIPGRCQFSLDIRAATDEIRDAAVADILAEIAAIAARRGIEYKAELAMKAAAAPCAPELMKQLEAATDAAG 526

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 763177151 348 IPAKILASGAGHDAMAMAELCPVAMLFTRC-KGGISHHPAESITHQDVEASLSALHHTIGAL 408
Cdd:PRK13799 527 VPLFELASGAGHDAMKIAEIMDQAMLFTRCgNAGISHNPLESMTADDMELSADAFLDFLNNF 588
PRK12892 PRK12892
allantoate amidohydrolase; Reviewed
 2-405 1.81e-107

allantoate amidohydrolase; Reviewed


Pssm-ID: 183817 [Multi-domain]  Cd Length: 412  Bit Score: 322.81  E-value: 1.81e-107
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763177151   2 TEFADAAAQVMARCETLGTLSQDPSCLDRRYLTEQHKLANQLTSGWMIEAGMTTWQDAAGNIWGRYSSAVPnAPRMILGS 81
Cdd:PRK12892   3 AMLRIDGQRVLDDLMELAAIGAAKTGVHRPTYSDAHVAARRRLAAWCEAAGLAVRIDGIGNVFGRLPGPGP-GPALLVGS 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763177151  82 HLDTVPNGGKYDGMLGVVAAITLVALFNGEQKKFPYHIDIVGFCDEEGTRFGTTLLGSRALTGKW--QDEWRRLKDENGV 159
Cdd:PRK12892  82 HLDSQNLGGRYDGALGVVAGLEAARALNEHGIATRHPLDVVAWCDEEGSRFTPGFLGSRAYAGRLdpADALAARCRSDGV 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763177151 160 SLEQAMAEFGLNFDEVPsAAIPAtDVLAYLELHIEQGPVLEQENLPIGVVSAIAGAKRFNINVQGMAGHAGTVPMSMRHD 239
Cdd:PRK12892 162 PLRDALAAAGLAGRPRP-AADRA-RPKGYLEAHIEQGPVLEQAGLPVGVVTGIVGIWQYRITVTGEAGHAGTTPMALRRD 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763177151 240 ALCASAEMLLAVESISQQRAG-VVATVGKIENAPNGVNVISGKTVFSLDIRSEDDNLRDAVLAEILQKFEHIAALRNVKL 318
Cdd:PRK12892 240 AGLAAAEMIAAIDEHFPRVCGpAVVTVGRVALDPGSPSIIPGRVEFSFDARHPSPPVLQRLVALLEALCREIARRRGCRV 319

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763177151 319 EIEQTHSAPAVLCDEALKAALVKGVEASNIPAKILASGAGHDAMAMAELCPVAMLFTRCKGGISHHPAESITHQDVEASL 398
Cdd:PRK12892 320 SVDRIAEYAPAPCDAALVDALRAAAEAAGGPYLEMPSGAGHDAQNMARIAPSAMLFVPSKGGISHNPAEDTSPADLAQGA 399


                 ....*..
gi 763177151 399 SALHHTI 405
Cdd:PRK12892 400 RVLADTL 406
PRK12891 PRK12891
allantoate amidohydrolase; Reviewed
 7-407 2.10e-81

allantoate amidohydrolase; Reviewed


Pssm-ID: 237249  Cd Length: 414  Bit Score: 256.28  E-value: 2.10e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763177151   7 AAAQVMARCETLGTLSQDPSC-LDRRYLTEQHKLANQLTSGWMIEAGMTTWQDAAGNIWGRYSSAVPNAPRMILGSHLDT 85
Cdd:PRK12891   8 DGERLWASLERMAQIGATPKGgVCRLALTDGDREARDLFVAWARDAGCTVRVDAMGNLFARRAGRDPDAAPVMTGSHADS 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763177151  86 VPNGGKYDGMLGVVAAITLVALFNGEQKKFPYHIDIVGFCDEEGTRFGTTLLGSRALTGKWQDEWRRLK-DENGVSLEQA 164
Cdd:PRK12891  88 QPTGGRYDGIYGVLGGLEVVRALNDAGIETERPVDVVIWTNEEGSRFAPSMVGSGVFFGVYPLEYLLSRrDDTGRTLGEH 167

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763177151 165 MAEFGLNFDEvpsaAIPATDVLAYLELHIEQGPVLEQENLPIGVVSAIAGAKRFNINVQGMAGHAGTVPMSMRHDALCAS 244
Cdd:PRK12891 168 LARIGYAGAE----PVGGYPVHAAYELHIEQGAILERAGKTIGVVTAGQGQRWYEVTLTGVDAHAGTTPMAFRRDALVGA 243

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763177151 245 AEMLLAVESISQQRA-GVVATVGKIENAPNGVNVISGKTVFSLDIRSEDDNLRDAVLAEILQKFEHIAALRNVKLEIEQT 323
Cdd:PRK12891 244 ARMIAFLDALGRRDApDARATVGMIDARPNSRNTVPGECFFTVEFRHPDDAVLDRLDAALRAELARIADETGLRADIEQI 323

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763177151 324 HSAPAVLCDEALKAALVKGVEASNIPAKILASGAGHDAMAMAELCPVAMLFTRCKGGISHHPAESITHQDVEASLSALHH 403
Cdd:PRK12891 324 FGYAPAPFAPGCIDAVRDAARALGLSHMDIVSGAGHDACFAARGAPTGMIFVPCVDGLSHNEAEAITPEWFAAGADVLLR 403


                 ....
gi 763177151 404 TIGA 407
Cdd:PRK12891 404 AVLQ 407
Peptidase_M20 pfam01546
Peptidase family M20/M25/M40; This family includes a range of zinc metallopeptidases belonging ...
 78-405 3.62e-46

Peptidase family M20/M25/M40; This family includes a range of zinc metallopeptidases belonging to several families in the peptidase classification. Family M20 are Glutamate carboxypeptidases. Peptidase family M25 contains X-His dipeptidases.


Pssm-ID: 460247 [Multi-domain]  Cd Length: 315  Bit Score: 161.36  E-value: 3.62e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763177151   78 ILGSHLDTVPNG------------------GKYDGMLGVVAAITLVALFNgEQKKFPYHIDIVGFCDEEGTrfgttLLGS 139
Cdd:pfam01546   1 LLRGHMDVVPDEetwgwpfkstedgklygrGHDDMKGGLLAALEALRALK-EEGLKKGTVKLLFQPDEEGG-----MGGA 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763177151  140 RALTGKWQDEWRRLKdengvsleqamaefglnfdevpsaaipatdvlAYLELHIEQGPVLEqENLPIGVVSAIAGAKRFN 219
Cdd:pfam01546  75 RALIEDGLLEREKVD--------------------------------AVFGLHIGEPTLLE-GGIAIGVVTGHRGSLRFR 121

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763177151  220 INVQGMAGHAGTVPMsmRHDALCASAEMLLAVESISQQRAG----VVATVGKIENAPNGVNVISGKTVFSLDIRSEDDNL 295
Cdd:pfam01546 122 VTVKGKGGHASTPHL--GVNAIVAAARLILALQDIVSRNVDpldpAVVTVGNITGIPGGVNVIPGEAELKGDIRLLPGED 199

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763177151  296 RDAVLAEILQKFEHIAALRNVKLEIEQTHSAPAVLC-DEALKAALVKGV-EASNIPAKILASG--AGHDAMAMAELCPVA 371
Cdd:pfam01546 200 LEELEERIREILEAIAAAYGVKVEVEYVEGGAPPLVnDSPLVAALREAAkELFGLKVELIVSGsmGGTDAAFFLLGVPPT 279

                         330       340       350
                  ....*....|....*....|....*....|....
gi 763177151  372 MLFTRCKGGISHHPAESITHQDVEASLSALHHTI 405
Cdd:pfam01546 280 VVFFGPGSGLAHSPNEYVDLDDLEKGAKVLARLL 313
amidohydrolases TIGR01891
amidohydrolase; This model represents a subfamily of amidohydrolases which are a subset of ...
 89-391 5.93e-17

amidohydrolase; This model represents a subfamily of amidohydrolases which are a subset of those sequences detected by pfam01546. Included within this group are hydrolases of hippurate (N-benzylglycine), indoleacetic acid (IAA) N-conjugates of amino acids, N-acetyl-L-amino acids and aminobenzoylglutamate. These hydrolases are of the carboxypeptidase-type, most likely utilizing a zinc ion in the active site. [Protein fate, Degradation of proteins, peptides, and glycopeptides]


Pssm-ID: 273857 [Multi-domain]  Cd Length: 363  Bit Score: 81.62  E-value: 5.93e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763177151   89 GGKYDGMLGVVAAITlvALFNGEQKKFPYHIDIVGFCDEEG-TRFGTTLLGSRALTGKWQDEWR---RL---KDENGVSL 161
Cdd:TIGR01891  52 GGKPGPVVALRADMD--ALPIQEQTDLPYKSTNPGVMHACGhDLHTAILLGTAKLLKKLADLLEgtvRLifqPAEEGGGG 129

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763177151  162 EQAMAEFGLnFDevpsaaipatDVLAYLELHIEqgPVLEQENLPIGVVSAIAGAKRFNINVQGMAGHAGTVPMSMrhDAL 241
Cdd:TIGR01891 130 ATKMIEDGV-LD----------DVDAILGLHPD--PSIPAGTVGLRPGTIMAAADKFEVTIHGKGAHAARPHLGR--DAL 194

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763177151  242 CASAEMLLAVE-----SISQQRAGVVaTVGKIEnAPNGVNVISGKTVFSLDIRSEDDNLRDAVLAEILQKFEHIAALRNV 316
Cdd:TIGR01891 195 DAAAQLVVALQqivsrNVDPSRPAVV-SVGIIE-AGGAPNVIPDKASMSGTVRSLDPEVRDQIIDRIERIVEGAAAMYGA 272

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763177151  317 KLEIEQTHSAPAVLCDEA----LKAALVKGVEASNIPAKILASGAGHDAMAMAELCPVAMLFTRCKG---GIS---HHPA 386
Cdd:TIGR01891 273 KVELNYDRGLPAVTNDPAltqiLKEVARHVVGPENVAEDPEVTMGSEDFAYYSQKVPGAFFFLGIGNegtGLShplHHPR 352


                  ....*
gi 763177151  387 ESITH 391
Cdd:TIGR01891 353 FDIDE 357
M20_Acy1 cd03886
M20 Peptidase Aminoacylase 1 family; Peptidase M20 family, Aminoacylase 1 (ACY1; hippuricase; ...
 204-343 1.61e-15

M20 Peptidase Aminoacylase 1 family; Peptidase M20 family, Aminoacylase 1 (ACY1; hippuricase; acylase I; amido acid deacylase; IAA-amino acid hydrolase; dehydropeptidase II; N-acyl-L-amino-acid amidohydrolase; EC 3.5.1.14) subfamily. ACY1 is the most abundant of the aminoacylases, a class of zinc binding homodimeric enzymes involved in the hydrolysis of N-acetylated proteins. It is encoded by the aminoacylase 1 gene (Acy1) on chromosome 3p21 that comprises 15 exons. N-terminal acetylation of proteins is a widespread and highly conserved process that is involved in the protection and stability of proteins. Several types of aminoacylases can be distinguished on the basis of substrate specificity; substrates include indoleacetic acid (IAA) N-conjugates of amino acids, N-acetyl-L-amino acids and aminobenzoylglutamate. ACY1 breaks down cytosolic aliphatic N-acyl-alpha-amino acids (except L-aspartate), especially N-acetyl-methionine and acetyl-glutamate into L-amino acids and an acyl group. However, ACY1 can also catalyze the reverse reaction, the synthesis of acetylated amino acids. ACY1 may also play a role in xenobiotic bioactivation as well as the inter-organ processing of amino acid-conjugated xenobiotic derivatives (S-substituted-N-acetyl-L-cysteine). ACY1 appears to physically interact with Sphingosine kinase type 1 (SphK1) and may influence its physiological functions; SphK1 and its product sphingosine-1-phosphate have been shown to promote cell growth and inhibit apoptosis of tumor cells. Strong expression of the human gene and its mouse ortholog Acy1 in brain, liver, and kidney, suggest a role of the enzyme in amino acid metabolism of these organs. Defects in ACY1 are the cause of aminoacylase-1 deficiency (ACY1D), resulting in a metabolic disorder manifesting encephalopathy and psychomotor delay.


Pssm-ID: 349882 [Multi-domain]  Cd Length: 371  Bit Score: 77.26  E-value: 1.61e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763177151 204 LPIGVV-----SAIAGAKRFNINVQGMAGHAGTVPMSMrhDALCASAEMLLAVESISQQRA----GVVATVGKIeNAPNG 274
Cdd:cd03886  155 LPVGTVgvrsgALMASADEFEITVKGKGGHGASPHLGV--DPIVAAAQIVLALQTVVSRELdplePAVVTVGKF-HAGTA 231

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 763177151 275 VNVISGKTVFSLDIRSEDDNLRDAVLAEILQKFEHIAALRNVKLEIEQTHSAPAVLCDEALkAALVKGV 343
Cdd:cd03886  232 FNVIPDTAVLEGTIRTFDPEVREALEARIKRLAEGIAAAYGATVELEYGYGYPAVINDPEL-TELVREA 299
PepD2 COG2195
Di- or tripeptidase [Amino acid transport and metabolism];
35-397 1.34e-13

Di- or tripeptidase [Amino acid transport and metabolism];


Pssm-ID: 441798 [Multi-domain]  Cd Length: 364  Bit Score: 71.62  E-value: 1.34e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763177151  35 EQHKLANQLTSgWMIEAGMTTWQDAAGNIWGRYSSAVP-NAPRMILGSHLDTVP-----------NGG--KYDGM--LGV 98
Cdd:COG2195   21 HEEALADYLVE-ELKELGLEVEEDEAGNVIATLPATPGyNVPTIGLQAHMDTVPqfpgdgikpqiDGGliTADGTttLGA 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763177151  99 -----VAAItLVALFNGEQKKFPyHIDI-VGFC-DEEgtrfgTTLLGSRALTGKWqdewrrLKdengvsleqamAEFGLN 171
Cdd:COG2195  100 ddkagVAAI-LAALEYLKEPEIP-HGPIeVLFTpDEE-----IGLRGAKALDVSK------LG-----------ADFAYT 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763177151 172 FDevpsaaipatdvlaylelhieQGPV--LEQENlpigvvsaiAGAKRFNINVQGMAGHAGTVPMSMrhdalcASAeMLL 249
Cdd:COG2195  156 LD---------------------GGEEgeLEYEC---------AGAADAKITIKGKGGHSGDAKEKM------INA-IKL 198

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763177151 250 AVESISQQRAGVV-----ATVGKIE--NAPNGvnvISGKTVFSLDIRSEDDNLRDAVLAEILQKFEHIAALRNV-KLEIE 321
Cdd:COG2195  199 AARFLAALPLGRIpeeteGNEGFIHggSATNA---IPREAEAVYIIRDHDREKLEARKAELEEAFEEENAKYGVgVVEVE 275

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763177151 322 QTHSAPAV-------LCDEALKAAlvkgvEASNIPAKILASGAGHDA-----MAMaelcPVAMLFTrckgGIS--HHPAE 387
Cdd:COG2195  276 IEDQYPNWkpepdspIVDLAKEAY-----EELGIEPKIKPIRGGLDGgilsfKGL----PTPNLGP----GGHnfHSPDE 342

                        410
                 ....*....|
gi 763177151 388 SITHQDVEAS 397
Cdd:COG2195  343 RVSIESMEKA 352
ArgE COG0624
Acetylornithine deacetylase/Succinyl-diaminopimelate desuccinylase or related deacylase [Amino ...
 46-408 3.50e-12

Acetylornithine deacetylase/Succinyl-diaminopimelate desuccinylase or related deacylase [Amino acid transport and metabolism]; Acetylornithine deacetylase/Succinyl-diaminopimelate desuccinylase or related deacylase is part of the Pathway/BioSystem: Arginine biosynthesis


Pssm-ID: 440389 [Multi-domain]  Cd Length: 388  Bit Score: 67.60  E-value: 3.50e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763177151  46 GWMIEAGMTTW----QDAAGNIWGRYSSAvPNAPRMILGSHLDTVPNGGKY------------DGML----------GVV 99
Cdd:COG0624   40 ELLEALGFEVErlevPPGRPNLVARRPGD-GGGPTLLLYGHLDVVPPGDLElwtsdpfeptieDGRLygrgaadmkgGLA 118

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763177151 100 AAITLVALFNGEQKKFPYHIDIVGFCDEEgtrfgTTLLGSRALtgkwqdewrrlkdengvsLEQAMAEFGlnfdevPSAA 179
Cdd:COG0624  119 AMLAALRALLAAGLRLPGNVTLLFTGDEE-----VGSPGARAL------------------VEELAEGLK------ADAA 169

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763177151 180 IpatdvlaylelhieqgpVLEQENLPiGVVSAIAGAKRFNINVQGMAGHAGTVPMSmrHDALCASAEMLLAVESISQQRA 259
Cdd:COG0624  170 I-----------------VGEPTGVP-TIVTGHKGSLRFELTVRGKAAHSSRPELG--VNAIEALARALAALRDLEFDGR 229

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763177151 260 G------VVATVGKIEnAPNGVNVISGKTVFSLDIRSEDDNLRDAVLAEILQKFEHIAALRNVKLEIeQTHSAPAVLCDE 333
Cdd:COG0624  230 AdplfgrTTLNVTGIE-GGTAVNVIPDEAEAKVDIRLLPGEDPEEVLAALRALLAAAAPGVEVEVEV-LGDGRPPFETPP 307

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763177151 334 --ALKAALVKGV-EASNIPAKILASGAGHDAMAMAEL--CPVAMLFTrckGGIS--HHPAESITHQDVEASLSALHHTIG 406
Cdd:COG0624  308 dsPLVAAARAAIrEVTGKEPVLSGVGGGTDARFFAEAlgIPTVVFGP---GDGAgaHAPDEYVELDDLEKGARVLARLLE 384


                 ..
gi 763177151 407 AL 408
Cdd:COG0624  385 RL 386
M20_Acy1_YxeP-like cd05669
M20 Peptidase aminoacyclase-1 YxeP-like proteins, including YxeP, YtnL, YjiB and HipO2; ...
 204-336 2.05e-10

M20 Peptidase aminoacyclase-1 YxeP-like proteins, including YxeP, YtnL, YjiB and HipO2; Peptidase M20 family, aminoacyclase-1 YxeP-like subfamily including YxeP, YtnL, YjiB and HipO2, most of which have not been well characterized to date. N-terminal acetylation of proteins is a widespread and highly conserved process that is involved in the protection and stability of proteins. Several types of aminoacylases can be distinguished on the basis of substrate specificity; substrates include indoleacetic acid (IAA) N-conjugates of amino acids, N-acetyl-L-amino acids and aminobenzoylglutamate. ACY1 breaks down cytosolic aliphatic N-acyl-alpha-amino acids (except L-aspartate), especially N-acetyl-methionine and acetyl-glutamate into L-amino acids and an acyl group. However, ACY1 can also catalyze the reverse reaction, the synthesis of acetylated amino acids. ACY1 may also play a role in xenobiotic bioactivation as well as in the inter-organ processing of amino acid-conjugated xenobiotic derivatives (S-substituted-N-acetyl-L-cysteine). ACY1 appears to physically interact with Sphingosine kinase type 1 (SphK1) and may influence its physiological functions; SphK1 and its product sphingosine-1-phosphate have been shown to promote cell growth and inhibit apoptosis of tumor cells. Strong expression of the human gene and its mouse ortholog Acy1 in brain, liver, and kidney suggest a role of the enzyme in amino acid metabolism of these organs.


Pssm-ID: 349919 [Multi-domain]  Cd Length: 371  Bit Score: 61.93  E-value: 2.05e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763177151 204 LPIGVVSA-----IAGAKRFNINVQGMAGHAGTVPMSMrhDALCASAEMLLAVESI-----SQQRAGVVaTVGKIeNAPN 273
Cdd:cd05669  156 LPVGTIGLksgalMAAVDRFEIEIAGKGAHAAKPENGV--DPIVAASQIINALQTIvsrniSPLESAVV-SVTRI-HAGN 231

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 763177151 274 GVNVISGKTVFSLDIRSEDDNLRDAVLAEILQKFEHIAALRNVKLEIEQTHSAPAVLCDEALK 336
Cdd:cd05669  232 TWNVIPDSAELEGTVRTFDAEVRQLVKERFEQIVEGIAAAFGAKIEFKWHSGPPAVINDEELT 294
M20_CPDG2 cd03885
M20 Peptidase Glutamate carboxypeptidase, a periplasmic enzyme; Peptidase M20 family, ...
 208-328 2.84e-09

M20 Peptidase Glutamate carboxypeptidase, a periplasmic enzyme; Peptidase M20 family, Glutamate carboxypeptidase (carboxypeptidase G; carboxypeptidase G1; carboxypeptidase G2; CPDG2; CPG2; Folate hydrolase G2; Pteroylmonoglutamic acid hydrolase G2; Glucarpidase; E.C. 3.4.17.11) subfamily. CPDG2 is a periplasmic enzyme that is synthesized with a signal peptide. It is a dimeric zinc-dependent exopeptidase, with two domains, a catalytic domain, which provides the ligands for the two zinc ions in the active site, and a dimerization domain. CPDG2 cleaves the C-terminal glutamate moiety from a wide range of N-acyl groups, including peptidyl, aminoacyl, benzoyl, benzyloxycarbonyl, folyl, and pteroyl groups to release benzoic acid, phenol, and aniline mustards. It is used clinically to treat methotrexate toxicity by hydrolyzing it to inactive and non-toxic metabolites. It is also proposed for use in antibody-directed enzyme prodrug therapy; for example, glutamate can be cleaved from glutamated benzoyl nitrogen mustards, producing nitrogen mustards with effective cytotoxicity against tumor cells.


Pssm-ID: 349881 [Multi-domain]  Cd Length: 362  Bit Score: 58.37  E-value: 2.84e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763177151 208 VVSAIAGAKRFNINVQGMAGHAGTVPMSMRhDALCASAEMLLAVESISQQRAGVVATVGKIEnAPNGVNVISGKTVFSLD 287
Cdd:cd03885  164 LVTARKGIGRFRLTVKGRAAHAGNAPEKGR-SAIYELAHQVLALHALTDPEKGTTVNVGVIS-GGTRVNVVPDHAEAQVD 241

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 763177151 288 IRSEDDNLRDAVLAEIlQKFEHIAALRNVKLEIEQTHSAPA 328
Cdd:cd03885  242 VRFATAEEADRVEEAL-RAIVATTLVPGTSVELTGGLNRPP 281
PRK07338 PRK07338
hydrolase;
197-328 6.32e-09

hydrolase;


Pssm-ID: 235995 [Multi-domain]  Cd Length: 402  Bit Score: 57.28  E-value: 6.32e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763177151 197 PVLEQENLpigvVSAIAGAKRFNINVQGMAGHAGTVPMSMRhDALCASAEMLLAVESISQQRAGVVATVGKIENApNGVN 276
Cdd:PRK07338 189 PALPDGTL----AGARKGSGNFTIVVTGRAAHAGRAFDEGR-NAIVAAAELALALHALNGQRDGVTVNVAKIDGG-GPLN 262

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 763177151 277 VISGKTVFSLDIRSEDDNLRDAVLAEILQKFEHIAALRNVKLEIEQTHSAPA 328
Cdd:PRK07338 263 VVPDNAVLRFNIRPPTPEDAAWAEAELKKLIAQVNQRHGVSLHLHGGFGRPP 314
M20_Acy1-like cd05664
M20 Peptidase aminoacylase 1 subfamily; Peptidase M20 family, Uncharacterized subfamily of ...
 83-339 1.59e-08

M20 Peptidase aminoacylase 1 subfamily; Peptidase M20 family, Uncharacterized subfamily of proteins predicted as putative amidohydrolases or hippurate hydrolases. These are a class of zinc binding homodimeric enzymes involved in the hydrolysis of N-acetylated proteins. N-terminal acetylation of proteins is a widespread and highly conserved process that is involved in the protection and stability of proteins. Several types of aminoacylases can be distinguished on the basis of substrate specificity. Aminoacylase 1 (ACY1) breaks down cytosolic aliphatic N-acyl-alpha-amino acids (except L-aspartate), especially N-acetyl-methionine and acetyl-glutamate into L-amino acids and an acyl group. However, ACY1 can also catalyze the reverse reaction, the synthesis of acetylated amino acids. ACY1 may also play a role in xenobiotic bioactivation as well as in the inter-organ processing of amino acid-conjugated xenobiotic derivatives (S-substituted-N-acetyl-L-cysteine).


Pssm-ID: 349914 [Multi-domain]  Cd Length: 399  Bit Score: 56.19  E-value: 1.59e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763177151  83 LDTVPNGGKYdgmlGVVAAITlvalfNGEQKKFPYHIDI----------------VGFCDEEGTRFG-----------TT 135
Cdd:cd05664   36 FEVTTGIGGT----GVVAVLR-----NGEGPTVLLRADMdalpveentglpyastVRMKDWDGKEVPvmhacghdmhvAA 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763177151 136 LLGSRALTGKWQDEWRRL------KDENGVSLEQAMAEFGLnFDEvpsaaIPATDVlaYLELHIEQGPVleqenlpiGVV 209
Cdd:cd05664  107 LLGAARLLVEAKDAWSGTliavfqPAEETGGGAQAMVDDGL-YDK-----IPKPDV--VLAQHVMPGPA--------GTV 170

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763177151 210 -----SAIAGAKRFNINVQGMAGHaGTVPMSMRhDALCASAEMLLAVESI-----SQQRAGVVaTVGKIeNAPNGVNVIS 279
Cdd:cd05664  171 gtrpgRFLSAADSLDITIFGRGGH-GSMPHLTI-DPVVMAASIVTRLQTIvsrevDPQEFAVV-TVGSI-QAGSAENIIP 246

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 763177151 280 GKTVFSLDIRSEDDNLRDAVLAEILQKFEHIAALRNV--KLEIEQTHSAPAVLCDEALKAAL 339
Cdd:cd05664  247 DEAELKLNVRTFDPEVREKVLNAIKRIVRAECAASGApkPPEFTYTDSFPATVNDEDATARL 308
M20_Acy1-like cd05667
M20 Peptidase aminoacylase 1 subfamily; Peptidase M20 family, uncharacterized subfamily of ...
 206-374 4.23e-08

M20 Peptidase aminoacylase 1 subfamily; Peptidase M20 family, uncharacterized subfamily of bacterial proteins that have been predicted as N-acyl-L-amino acid amidohydrolase (amaA), thermostable carboxypeptidase (cpsA-1, cpsA-2 in Sulfolobus solfataricus) and abgB (aminobenzoyl-glutamate utilization protein B), and generally are involved in the urea cycle and metabolism of amino groups. Aminoacylases 1 (ACY1s) comprise a class of zinc binding homodimeric enzymes involved in the hydrolysis of N-acetylated proteins. N-terminal acetylation of proteins is a widespread and is a highly conserved process that is involved in the protection and stability of proteins. Several types of aminoacylases can be distinguished on the basis of substrate specificity. ACY1 breaks down cytosolic aliphatic N-acyl-alpha-amino acids (except L-aspartate), especially N-acetyl-methionine and acetyl-glutamate into L-amino acids and an acyl group. However, ACY1 can also catalyze the reverse reaction, the synthesis of acetylated amino acids. ACY1 may also play a role in xenobiotic bioactivation as well as the inter-organ processing of amino acid-conjugated xenobiotic derivatives (S-substituted-N-acetyl-L-cysteine).


Pssm-ID: 349917 [Multi-domain]  Cd Length: 403  Bit Score: 54.74  E-value: 4.23e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763177151 206 IGVVS--AIAGAKRFNINVQGMAGHaGTVPMSMRhDALCASAEMLLAVESISQQRAGV-----VATVGKIENAPNGvNVI 278
Cdd:cd05667  184 LGYRSgpIMASADRFRITVKGKQTH-GSRPWDGI-DPIMASAQIIQGLQTIISRRIDLtkepaVISIGKINGGTRG-NII 260

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763177151 279 SGKTVFSLDIRSEDDNLRDAVLAEILQKFEHIAALRNVKLEIEQTHSAPAVLCDEAL----KAALVKGVEASNIPAKILA 354
Cdd:cd05667  261 PEDAEMVGTIRTFDPEMREDIFARLKTIAEHIAKAYGATAEVEFANGYPVTYNDPALtakmLPTLQKAVGKADLVVLPPT 340

                        170       180
                 ....*....|....*....|
gi 763177151 355 SGAGHDAMAMAELCPVAMLF 374
Cdd:cd05667  341 QTGAEDFSFYAEQVPGMFFF 360
M20_Acy1-like cd08019
M20 Peptidase aminoacylase 1 subfamily; Peptidase M20 family, uncharacterized subfamily of ...
 203-335 5.27e-08

M20 Peptidase aminoacylase 1 subfamily; Peptidase M20 family, uncharacterized subfamily of bacterial proteins predicted as putative amidohydrolases. These are a class of zinc binding homodimeric enzymes involved in hydrolysis of N-acetylated proteins. N-terminal acetylation of proteins is a widespread and highly conserved process that is involved in protection and stability of proteins. Several types of aminoacylases can be distinguished on the basis of substrate specificity. Aminoacylase 1 (ACY1) breaks down cytosolic aliphatic N-acyl-alpha-amino acids (except L-aspartate), especially N-acetyl-methionine and acetyl-glutamate into L-amino acids and an acyl group. However, ACY1 can also catalyze the reverse reaction, the synthesis of acetylated amino acids. ACY1 may also play a role in xenobiotic bioactivation as well as the inter-organ processing of amino acid-conjugated xenobiotic derivatives (S-substituted-N-acetyl-L-cysteine).


Pssm-ID: 349940 [Multi-domain]  Cd Length: 372  Bit Score: 54.27  E-value: 5.27e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763177151 203 NLPIGVVSA-----IAGAKRFNINVQGMAGHAGTVPMSmrHDALCASAEMLLAVESI-SQQ---RAGVVATVGKIeNAPN 273
Cdd:cd08019  151 DVPAGKISVeagprMASADIFKIEVKGKGGHGSMPHQG--IDAVLAAASIVMNLQSIvSREidpLEPVVVTVGKL-NSGT 227

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 763177151 274 GVNVISGKTVFSLDIRSEDDNLRDAVLAEILQKFEHIAALRNVKLEIEQTHSAPAVLCDEAL 335
Cdd:cd08019  228 RFNVIADEAKIEGTLRTFNPETREKTPEIIERIAKHTAASYGAEAELTYGAATPPVINDEKL 289
M20_Acy1-like cd05666
M20 Peptidase aminoacylase 1 subfamily; Peptidase M20 family, uncharacterized subfamily of ...
 213-386 1.26e-07

M20 Peptidase aminoacylase 1 subfamily; Peptidase M20 family, uncharacterized subfamily of bacterial proteins predicted as putative amidohydrolases or hippurate hydrolases. These are a class of zinc binding homodimeric enzymes involved in hydrolysis of N-acetylated proteins. N-terminal acetylation of proteins is a widespread and highly conserved process that is involved in protection and stability of proteins. Several types of aminoacylases can be distinguished on the basis of substrate specificity. Aminoacylase 1 (ACY1) breaks down cytosolic aliphatic N-acyl-alpha-amino acids (except L-aspartate), especially N-acetyl-methionine and acetyl-glutamate into L-amino acids and an acyl group. However, ACY1 can also catalyze the reverse reaction, the synthesis of acetylated amino acids. ACY1 may also play a role in xenobiotic bioactivation as well as the inter-organ processing of amino acid-conjugated xenobiotic derivatives (S-substituted-N-acetyl-L-cysteine).


Pssm-ID: 349916 [Multi-domain]  Cd Length: 373  Bit Score: 53.30  E-value: 1.26e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763177151 213 AGAKRFNINVQGMAGHAgtvpmSMRH---DALCASAEMLLAVESI-----SQQRAGVVaTVGKIeNAPNGVNVISGKTVF 284
Cdd:cd05666  170 ASADTFEITIRGKGGHA-----AMPHlgvDPIVAAAQLVQALQTIvsrnvDPLDAAVV-SVTQI-HAGDAYNVIPDTAEL 242

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763177151 285 SLDIRSEDDNLRDAVLAEILQKFEHIAALRNVKLEIEQTHSAPAVLCDEALKA----ALVKGVEASNIPAKILASGAGHD 360
Cdd:cd05666  243 RGTVRAFDPEVRDLIEERIREIADGIAAAYGATAEVDYRRGYPVTVNDAEETAfaaeVAREVVGAENVDTDVRPSMGSED 322

                        170       180       190
                 ....*....|....*....|....*....|
gi 763177151 361 AMAMAELCPVAMLFT---RCKGGIS-HHPA 386
Cdd:cd05666  323 FAFMLEARPGAYVFLgngDGEGGCPlHNPG 352
M20_Acy1_YhaA-like cd08021
M20 Peptidase aminoacylase 1 subfamily, includes Bacillus subtilis YhaA and Staphylococcus ...
 203-403 1.44e-07

M20 Peptidase aminoacylase 1 subfamily, includes Bacillus subtilis YhaA and Staphylococcus aureus amidohydrolase, SACOL0085; Peptidase M20 family, uncharacterized subfamily of bacterial proteins predicted as putative amidohydrolases or hippurate hydrolases. These are a class of zinc binding homodimeric enzymes involved in hydrolysis of N-acetylated proteins. N-terminal acetylation of proteins is a widespread and highly conserved process that is involved in protection and stability of proteins. Several types of aminoacylases can be distinguished on the basis of substrate specificity. Aminoacylase 1 (ACY1) breaks down cytosolic aliphatic N-acyl-alpha-amino acids (except L-aspartate), especially N-acetyl-methionine and acetyl-glutamate into L-amino acids and an acyl group. However, ACY1 can also catalyze the reverse reaction, the synthesis of acetylated amino acids. ACY1 may also play a role in xenobiotic bioactivation as well as the inter-organ processing of amino acid-conjugated xenobiotic derivatives (S-substituted-N-acetyl-L-cysteine). This family includes Staphylococcus aureus amidohydrolase, SACOL0085, which contains two manganese ions in the active site, and forms a homotetramer with variations in interdomain orientation which possibly plays a role in the regulation of catalytic activity.


Pssm-ID: 349941 [Multi-domain]  Cd Length: 384  Bit Score: 53.05  E-value: 1.44e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763177151 203 NLPIGVV-----SAIAGAKRFNINVQGMAGHAgtvpmSMRH---DALCASAEMLLAVESISQQR-----AGVVaTVGKIE 269
Cdd:cd08021  164 TLPTGTIavrpgAIMAAPDEFDITIKGKGGHG-----SMPHetvDPIVIAAQIVTALQTIVSRRvdpldPAVV-TIGTFQ 237

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763177151 270 nAPNGVNVISGKTVFSLDIRSEDDNLRDAVLAEILQKFEHIAALRNVKLEIEQTHSAPAVLCDEALKAALVKGVEASNIP 349
Cdd:cd08021  238 -GGTSFNVIPDTVELKGTVRTFDEEVREQVPKRIERIVKGICEAYGASYELEYQPGYPVVYNDPEVTELVKKAAKEVLIG 316

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 763177151 350 AKILAS---GAGHDAMAMAELCPVAMLFTRC----KGGI-SHHPAESITHQDVEASLSALHH 403
Cdd:cd08021  317 VENVEPqlmMGGEDFSYYLKEVPGCFFFLGAgneeKGCIyPHHSPKFDIDESALKIGVKVHV 378
M20_ArgE_DapE-like cd08659
Peptidase M20 acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase (ArgE/DapE) ...
 36-397 1.69e-07

Peptidase M20 acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase (ArgE/DapE)-like; Peptidase M20 acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase (ArgE/DapE) like family of enzymes catalyze analogous reactions and share a common activator, the metal ion (usually Co2+ or Zn2+). ArgE catalyzes a broad range of substrates, including N-acetylornithine, alpha-N-acetylmethionine and alpha-N-formylmethionine, while DapE catalyzes the hydrolysis of N-succinyl-L,L-diaminopimelate (L,L-SDAP) to L,L-diaminopimelate and succinate. Proteins in this family are mostly bacterial and have been inferred by homology as being related to both ArgE and DapE. This family also includes N-acetyl-L-citrulline deacetylase (ACDase; acetylcitrulline deacetylase), a unique, novel enzyme found in Xanthomonas campestris, a plant pathogen, in which N-acetyl-L-ornithine is the substrate for transcarbamoylation reaction, and the product is N-acetyl-L-citrulline. Thus, in the arginine biosynthesis pathway, ACDase subsequently catalyzes the hydrolysis of N-acetyl-L-citrulline to acetate and L-citrulline.


Pssm-ID: 349944 [Multi-domain]  Cd Length: 361  Bit Score: 52.69  E-value: 1.69e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763177151  36 QHKLANQLTS-GWMIEagmTTWQDAAGNIWGRYSSAvpNAPRMILGSHLDTVPNGGKY------------DGML------ 96
Cdd:cd08659   20 AEYLAELLAKrGYGIE---STIVEGRGNLVATVGGG--DGPVLLLNGHIDTVPPGDGDkwsfppfsgrirDGRLygrgac 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763177151  97 ----GVVAAITLVALFNGEQKKFPYHIDIVGFCDEEgtrfgTTLLGSRALtgkwqdewrrlkdengvsLEQAMAEfglnf 172
Cdd:cd08659   95 dmkgGLAAMVAALIELKEAGALLGGRVALLATVDEE-----VGSDGARAL------------------LEAGYAD----- 146

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763177151 173 devpsaaipatDVLAYLelhieqgpVLEQENLpiGVVSAIAGAKRFNINVQGMAGHAgtvpmSMRH---DALCASAEMLL 249
Cdd:cd08659  147 -----------RLDALI--------VGEPTGL--DVVYAHKGSLWLRVTVHGKAAHS-----SMPElgvNAIYALADFLA 200

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763177151 250 AVESISQQRA------GVVATVGKIeNAPNGVNVISGKTVFSLDIRS--EDDNlrdavlAEILQKFEHIAALRNVKLEIE 321
Cdd:cd08659  201 ELRTLFEELPahpllgPPTLNVGVI-NGGTQVNSIPDEATLRVDIRLvpGETN------EGVIARLEAILEEHEAKLTVE 273

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763177151 322 QTHSAPAVLC---DEALKAALVKGVEASNIPAKILASGAGHDA--MAMAELCPVAMLftrckG----GISHHPAESITHQ 392
Cdd:cd08659  274 VSLDGDPPFFtdpDHPLVQALQAAARALGGDPVVRPFTGTTDAsyFAKDLGFPVVVY-----GpgdlALAHQPDEYVSLE 348


                 ....*
gi 763177151 393 DVEAS 397
Cdd:cd08659  349 DLLRA 353
M20_Acy1_IAAspH cd05665
M20 Peptidases aminoacyclase-1 indole-3-acetic-L-aspartic acid hydrolase; Peptidase M20 family, ...
 156-350 2.03e-06

M20 Peptidases aminoacyclase-1 indole-3-acetic-L-aspartic acid hydrolase; Peptidase M20 family, bacterial and archaeal aminoacyclase-1 indole-3-acetic-L-aspartic acid hydrolase (IAA-Asp hydrolase; IAAspH; IAAH; IAA amidohydrolase; EC 3.5.1.-) subfamily. IAAspH hydrolyzes indole-3-acetyl-N-aspartic acid (IAA or auxin) to indole-3-acetic acid. Genes encoding IAA-amidohydrolases were first cloned from Arabidopsis; ILR1, IAR3, ILL1 and ILL2 encode active IAA- amino acid hydrolases, and three additional amidohydrolase-like genes (ILL3, ILL5, ILL6) have been isolated. In higher plants, the growth regulator indole-3-acetic acid (IAA or auxin) is found both free and conjugated via amide bonding to a variety of amino acids and peptides, and via an ester linkage to carbohydrates. IAA-Asp conjugates are involved in homeostatic control, protection, storing and subsequent use of free IAA. IAA-Asp is also found in some plants as a unique intermediate for entering into IAA non-decarboxylative oxidative pathway. IAA amidohydrolase cleaves the amide bond between the auxin and the conjugated amino acid. Enterobacter agglomerans IAAspH has very strong enzyme activity and substrate specificity towards IAA-Asp, although its substrate affinity is weaker compared to Arabidopsis enzymes of the ILR1 gene family. Enhanced IAA-hydrolase activity has been observed during clubroot disease in Chinese cabbage.


Pssm-ID: 349915 [Multi-domain]  Cd Length: 415  Bit Score: 49.62  E-value: 2.03e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763177151 156 ENGVSLEQAMAEFGLnfdevpsaaipATDVLAYLELHIEQGpvleqenLPIGVVsaIAGAKRF------NINVQGMAGHA 229
Cdd:cd05665  171 EEGVRGARAMAEAGV-----------VDDVDYFLASHIGFG-------VPSGEV--VCGPDNFlattklDARFTGVSAHA 230

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763177151 230 GTVPmSMRHDALCASAEMLLAVESISQQRAGVV-ATVGKIeNAPNGVNVISGKTVFSLDIRSEDDNLRDAVLAEILQKFE 308
Cdd:cd05665  231 GAAP-EDGRNALLAAATAALNLHAIPRHGEGATrINVGVL-GAGEGRNVIPASAELQVETRGETTAINEYMFEQAQRVIK 308

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 763177151 309 HIAALRNVKLEIEQTHSAP---------AVLCDEALKAALVKGVEASNIPA 350
Cdd:cd05665  309 GAATMYGVTVEIRTMGEAIsaesdpelvALLREQAARVPGVQAVIDSAAFG 359
M20_Acy1_amhX-like cd08018
M20 Peptidase aminoacylase 1 amhX-like subfamily; Peptidase M20 family, uncharacterized ...
 275-337 1.62e-05

M20 Peptidase aminoacylase 1 amhX-like subfamily; Peptidase M20 family, uncharacterized subfamily of proteins predicted as putative amidohydrolases, including the amhX gene product from Bacillus subtilis. These are a class of zinc binding homodimeric enzymes involved in hydrolysis of N-acetylated proteins. N-terminal acetylation of proteins is a widespread and highly conserved process that is involved in protection and stability of proteins. Several types of aminoacylases can be distinguished on the basis of substrate specificity. Aminoacylase 1 (ACY1) breaks down cytosolic aliphatic N-acyl-alpha-amino acids (except L-aspartate), especially N-acetyl-methionine and acetyl-glutamate into L-amino acids and an acyl group. However, ACY1 can also catalyze the reverse reaction, the synthesis of acetylated amino acids. ACY1 may also play a role in xenobiotic bioactivation as well as the inter-organ processing of amino acid-conjugated xenobiotic derivatives (S-substituted-N-acetyl-L-cysteine).


Pssm-ID: 349939 [Multi-domain]  Cd Length: 365  Bit Score: 46.51  E-value: 1.62e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 763177151 275 VNVISGKTVFSLDIRSEDDNLRDAVLAEILQKFEHIAALRNVKLEIEQTHSAPAVLCDEALKA 337
Cdd:cd08018  226 TNIIPDKAKFALDLRAQSNEAMEELKEKVEHAIEAAAALYGASIEITEKGGMPAAEYDEEAVE 288
M20_18_42 cd18669
M20, M18 and M42 Zn-peptidases include aminopeptidases and carboxypeptidases; This family ...
 62-146 2.23e-05

M20, M18 and M42 Zn-peptidases include aminopeptidases and carboxypeptidases; This family corresponds to the MEROPS MH clan families M18, M20, and M42. The peptidase M20 family contains exopeptidases, including carboxypeptidases such as the glutamate carboxypeptidase from Pseudomonas, the thermostable carboxypeptidase Ss1 of broad specificity from archaea and yeast Gly-X carboxypeptidase, dipeptidases such as bacterial dipeptidase, peptidase V (PepV), a eukaryotic, non-specific dipeptidase, and two Xaa-His dipeptidases (carnosinases). This family also includes the bacterial aminopeptidase peptidase T (PepT) that acts only on tripeptide substrates and has therefore been termed a tripeptidase. These peptidases generally hydrolyze the late products of protein degradation so as to complete the conversion of proteins to free amino acids. Glutamate carboxypeptidase hydrolyzes folate analogs such as methotrexate, and therefore can be used to treat methotrexate toxicity. Peptidase families M18 and M42 contain metallo-aminopeptidases. M18 (aspartyl aminopeptidase, DAP) family cleaves only unblocked N-terminal acidic amino-acid residues and is highly selective for hydrolyzing aspartate or glutamate residues. Some M42 (also known as glutamyl aminopeptidase) enzymes exhibit aminopeptidase specificity while others also have acylaminoacyl-peptidase activity (i.e. hydrolysis of acylated N-terminal residues).


Pssm-ID: 349948 [Multi-domain]  Cd Length: 198  Bit Score: 45.12  E-value: 2.23e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763177151  62 NIWGRYSSAvPNAPRMILGSHLDTVPNG----------------------GKYDGMLGVVAAITLVALFNGEQKKFPYHI 119
Cdd:cd18669    1 NVIARYGGG-GGGKRVLLGAHIDVVPAGegdprdppffvdtveegrlygrGALDDKGGVAAALEALKLLKENGFKLKGTV 79

                         90       100
                 ....*....|....*....|....*..
gi 763177151 120 DIVGFCDEEGTRFGTTLLGSRALTGKW 146
Cdd:cd18669   80 VVAFTPDEEVGSGAGKGLLSKDALEED 106
Zinc_peptidase_like cd03873
Zinc peptidases M18, M20, M28, and M42; Zinc peptidases play vital roles in metabolic and ...
 62-146 2.29e-05

Zinc peptidases M18, M20, M28, and M42; Zinc peptidases play vital roles in metabolic and signaling pathways throughout all kingdoms of life. This hierarchy contains zinc peptidases that correspond to the MH clan in the MEROPS database, which contains 4 families (M18, M20, M28, M42). The peptidase M20 family includes carboxypeptidases such as the glutamate carboxypeptidase from Pseudomonas, the thermostable carboxypeptidase Ss1 of broad specificity from archaea and yeast Gly-X carboxypeptidase. The dipeptidases include bacterial dipeptidase, peptidase V (PepV), a non-specific eukaryotic dipeptidase, and two Xaa-His dipeptidases (carnosinases). There is also the bacterial aminopeptidase, peptidase T (PepT) that acts only on tripeptide substrates and has therefore been termed a tripeptidase. Peptidase family M28 contains aminopeptidases and carboxypeptidases, and has co-catalytic zinc ions. However, several enzymes in this family utilize other first row transition metal ions such as cobalt and manganese. Each zinc ion is tetrahedrally co-ordinated, with three amino acid ligands plus activated water; one aspartate residue binds both metal ions. The aminopeptidases in this family are also called bacterial leucyl aminopeptidases, but are able to release a variety of N-terminal amino acids. IAP aminopeptidase and aminopeptidase Y preferentially release basic amino acids while glutamate carboxypeptidase II preferentially releases C-terminal glutamates. Glutamate carboxypeptidase II and plasma glutamate carboxypeptidase hydrolyze dipeptides. Peptidase families M18 and M42 contain metallo-aminopeptidases. M18 is widely distributed in bacteria and eukaryotes. However, only yeast aminopeptidase I and mammalian aspartyl aminopeptidase have been characterized in detail. Some M42 (also known as glutamyl aminopeptidase) enzymes exhibit aminopeptidase specificity while others also have acylaminoacyl-peptidase activity (i.e. hydrolysis of acylated N-terminal residues).


Pssm-ID: 349870 [Multi-domain]  Cd Length: 200  Bit Score: 45.11  E-value: 2.29e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763177151  62 NIWGRYSSAVPNaPRMILGSHLDTVPNG----------------------GKYDGMLGVVAAITLVALFNGEQKKFPYHI 119
Cdd:cd03873    1 NLIARLGGGEGG-KSVALGAHLDVVPAGegdnrdppfaedteeegrlygrGALDDKGGVAAALEALKRLKENGFKPKGTI 79

                         90       100
                 ....*....|....*....|....*..
gi 763177151 120 DIVGFCDEEGTRFGTTLLGSRALTGKW 146
Cdd:cd03873   80 VVAFTADEEVGSGGGKGLLSKFLLAED 106
M20_Acy1-like cd08014
M20 Peptidase aminoacylase 1 subfamily; Peptidase M20 family, uncharacterized subfamily of ...
 203-385 3.69e-05

M20 Peptidase aminoacylase 1 subfamily; Peptidase M20 family, uncharacterized subfamily of uncharacterized bacterial proteins predicted as putative amidohydrolases. These are a class of zinc binding homodimeric enzymes involved in hydrolysis of N-acetylated proteins. N-terminal acetylation of proteins is a widespread and highly conserved process that is involved in protection and stability of proteins. Several types of aminoacylases can be distinguished on the basis of substrate specificity. Aminoacylase 1 (ACY1) breaks down cytosolic aliphatic N-acyl-alpha-amino acids (except L-aspartate), especially N-acetyl-methionine and acetyl-glutamate into L-amino acids and an acyl group. However, ACY1 can also catalyze the reverse reaction, the synthesis of acetylated amino acids. ACY1 may also play a role in xenobiotic bioactivation as well as the inter-organ processing of amino acid-conjugated xenobiotic derivatives (S-substituted-N-acetyl-L-cysteine).


Pssm-ID: 349936 [Multi-domain]  Cd Length: 371  Bit Score: 45.34  E-value: 3.69e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763177151 203 NLPIGVVSAIAG-----AKRFNINVQGMAGHAgtvpmSMRH---DALCASAEMLLAVESISQQ----RAGVVATVGKIE- 269
Cdd:cd08014  153 RLPVGRVGVRYGpitaaADSLEIRIQGEGGHG-----ARPHltvDLVWAAAQVVTDLPQAISRridpRSPVVLTWGSIEg 227

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763177151 270 -NAPNgvnVISGKTVFSLDIRSEDDNLRDAVLAEILQKFEHIAALRNVKLEIEQTHSAPAVLCDEALKAALVKGVEA--- 345
Cdd:cd08014  228 gRAPN---VIPDSVELSGTVRTLDPDTWAQLPDLVEEIVAGICAPYGAKYELEYRRGVPPVINDPASTALLEAAVREilg 304

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 763177151 346 -SNIPAKILASGAGHDAMAMAELCPVAM--LFTRCKGGIS---HHP 385
Cdd:cd08014  305 eDNVVALAEPSMGGEDFAWYLEHVPGAMarLGVWGGDGTSyplHHP 350
PRK08651 PRK08651
succinyl-diaminopimelate desuccinylase; Reviewed
 214-358 6.91e-05

succinyl-diaminopimelate desuccinylase; Reviewed


Pssm-ID: 236323 [Multi-domain]  Cd Length: 394  Bit Score: 44.60  E-value: 6.91e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763177151 214 GAKRFNINVQGMAGHAGTVPMSmrHDALCASAEMLLAVESISQQR-----------AGVVATVG-KIENAPNGVNVISGK 281
Cdd:PRK08651 183 GLVWGVVKVYGKQAHASTPWLG--INAFEAAAKIAERLKSSLSTIkskyeyddergAKPTVTLGgPTVEGGTKTNIVPGY 260

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763177151 282 TVFSLDIRS--EDDNlrDAVLAEILQKFEHIAALRNVKLEIEQTHSAPAVLCD------EALKAAL--VKGVEasniPAK 351
Cdd:PRK08651 261 CAFSIDRRLipEETA--EEVRDELEALLDEVAPELGIEVEFEITPFSEAFVTDpdselvKALREAIreVLGVE----PKK 334


                 ....*..
gi 763177151 352 ILASGAG 358
Cdd:PRK08651 335 TISLGGT 341
M20_peptT_like cd05683
M20 Peptidase T like enzymes specifically cleave tripeptides; Peptidase M20 family, PeptT ...
 217-361 1.83e-04

M20 Peptidase T like enzymes specifically cleave tripeptides; Peptidase M20 family, PeptT (tripeptide aminopeptidase; tripeptidase)-like subfamily. This group includes bacterial tripeptidases as well as predicted tripeptidases. Peptidase T acts only on tripeptide substrates, and is thus called a tripeptidase. It catalyzes the release of N-terminal amino acids with hydrophobic side chains from tripeptides with high specificity; dipeptides, tetrapeptides or tripeptides with the N-terminus blocked are not cleaved. Tripeptidases are known to function at the final stage of proteolysis in lactococcal bacteria and release amino acids from tripeptides produced during the digestion of milk proteins such as casein.


Pssm-ID: 349932 [Multi-domain]  Cd Length: 368  Bit Score: 43.21  E-value: 1.83e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763177151 217 RFNINVQGMAGHAGTVPmsmrHDALCAsaeMLLAVESISQQRAGVV-----ATVGKIENApNGVNVISGKTVFSLDIRSE 291
Cdd:cd05683  180 KINAKIYGKTAHAGTSP----EKGISA---INIAAKAISNMKLGRIdeettANIGKFQGG-TATNIVTDEVNIEAEARSL 251

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 763177151 292 DDNLRDAVLAEILQKFEHIAALRNVKLEIEQTHSAPA--VLCDEALKAALVKGVEASNIPAKILASGAGHDA 361
Cdd:cd05683  252 DEEKLDAQVKHMKETFETTAKEKGAHAEVEVETSYPGfkINEDEEVVKLAKRAANNLGLEINTTYSGGGSDA 323
M28 cd02690
M28 Zn-peptidases include aminopeptidases and carboxypeptidases; Peptidase M28 family (also ...
 62-142 1.70e-03

M28 Zn-peptidases include aminopeptidases and carboxypeptidases; Peptidase M28 family (also called aminopeptidase Y family) contains aminopeptidases as well as carboxypeptidases. They have co-catalytic zinc ions; each zinc ion is tetrahedrally co-ordinated, with three amino acid ligands plus activated water; one aspartate residue binds both metal ions. The aminopeptidases in this family are also called bacterial leucyl aminopeptidases, but are able to release a variety of N-terminal amino acids. IAP aminopeptidase and aminopeptidase Y preferentially release basic amino acids while glutamate carboxypeptidase II preferentially releases C-terminal glutamates. Plasma glutamate carboxypeptidase (PGCP) and glutamate carboxypeptidase II (NAALADase) hydrolyze dipeptides. Several members of the M28 peptidase family have PA domain inserts which may participate in substrate binding and/or in promoting conformational changes, which influence the stability and accessibility of the site to substrate. These include prostate-specific membrane antigen (PSMA), yeast aminopeptidase S (SGAP), human transferrin receptors (TfR1 and TfR2), plasma glutamate carboxypeptidase (PGCP) and several predicted aminopeptidases where relatively little is known about them. Also included in the M28 family are glutaminyl cyclases (QC), which are involved in N-terminal glutamine cyclization of many endocrine peptides. Nicastrin and nicalin belong to this family but lack the amino-acid conservation required for catalytically active aminopeptidases.


Pssm-ID: 349868 [Multi-domain]  Cd Length: 202  Bit Score: 39.25  E-value: 1.70e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763177151  62 NIWGRYSSAVPNAPRMILGSHLDTVPNG-GKYDGMLGvVAAITLVA-LFNGEQKKFPYHIDIVGFCDEEgtrFGttLLGS 139
Cdd:cd02690    3 NVIATIKGSDKPDEVILIGAHYDSVPLSpGANDNASG-VAVLLELArVLSKLQLKPKRSIRFAFWDAEE---LG--LLGS 76


                 ...
gi 763177151 140 RAL 142
Cdd:cd02690   77 KYY 79
Peptidase_M28 pfam04389
Peptidase family M28;
76-142 1.78e-03

Peptidase family M28;


Pssm-ID: 461288 [Multi-domain]  Cd Length: 192  Bit Score: 39.19  E-value: 1.78e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 763177151   76 RMILGSHLDTVPNG-GKYDGMLGVVAAITLVALFNGEQkKFPYHIDIVGFCDEEgtrFGttLLGSRAL 142
Cdd:pfam04389  14 VVLLSAHYDSVGTGpGADDNASGVAALLELARVLAAGQ-RPKRSVRFLFFDAEE---AG--LLGSHHF 75
M20_like cd02697
M20 Zn-peptidases include exopeptidases; Peptidase M20 family; uncharacterized subfamily. ...
 208-312 1.94e-03

M20 Zn-peptidases include exopeptidases; Peptidase M20 family; uncharacterized subfamily. These hypothetical proteins have been inferred by homology to be exopeptidases: carboxypeptidases, dipeptidases and a specialized aminopeptidase. In general, the peptidase hydrolyzes the late products of protein degradation in order to complete the conversion of proteins to free amino acids. Members of this subfamily may bind metal ions such as zinc.


Pssm-ID: 349869 [Multi-domain]  Cd Length: 394  Bit Score: 40.23  E-value: 1.94e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763177151 208 VVSAIAGAKRFNINVQGMAGHAGtVPMSmRHDALCASAEMLLAV-------ESISQQRAGVVA---TVGKIENAPNgVNV 277
Cdd:cd02697  177 VVTAHNGCLQMEVTVHGKQAHAA-IPDT-GVDALQGAVAILNALyalnaqyRQVSSQVEGITHpylNVGRIEGGTN-TNV 253

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 763177151 278 ISGKTVFSLDIRSEDDNLRDAVLAEILQKFEHIAA 312
Cdd:cd02697  254 VPGKVTFKLDRRMIPEENPVEVEAEIRRVIADAAA 288
M28_like cd05640
M28 Zn-peptidase; uncharacterized subfamily; Peptidase family M28 (also called aminopeptidase ...
 53-183 2.33e-03

M28 Zn-peptidase; uncharacterized subfamily; Peptidase family M28 (also called aminopeptidase Y family), uncharacterized subfamily. The M28 family contains aminopeptidases as well as carboxypeptidases. They have co-catalytic zinc ions; each zinc ion is tetrahedrally co-ordinated, with three amino acid ligands plus activated water; one aspartate residue binds both metal ions.


Pssm-ID: 349893 [Multi-domain]  Cd Length: 281  Bit Score: 39.74  E-value: 2.33e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763177151  53 MTTWQDAAGNIW--------GRYSsavpNAPRMILGSHLDTVPNG-GKYDGMLGVVAAITLVALFNGEQKKFPyhIDIVG 123
Cdd:cd05640   41 TSHFFSHQEGVYanliadlpGSYS----QDKLILIGAHYDTVPGSpGADDNASGVAALLELARLLATLDPNHT--LRFVA 114

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 763177151 124 FCDEEGTRFGTTLLGSRALTGKWQdewRRLKDENG-VSLEQAMaefglNFDEVP-SAAIPAT 183
Cdd:cd05640  115 FDLEEYPFFARGLMGSHAYAEDLL---RPLTPIVGmLSLEMIG-----YYDPFPhSQAYPAG 168
M20_IAA_Hyd cd08017
M20 Peptidase Indole-3-acetic acid amino acid hydrolase; Peptidase M20 family, plant ...
 204-402 4.70e-03

M20 Peptidase Indole-3-acetic acid amino acid hydrolase; Peptidase M20 family, plant aminoacyclase-1 indole-3-acetic-L-aspartic acid hydrolase (IAA-Asp hydrolase; IAAspH; IAAH; IAA amidohydrolase; EC 3.5.1.-) subfamily. IAAspH hydrolyzes indole-3-acetyl-N-aspartic acid (IAA or auxin) to indole-3-acetic acid. Genes encoding IAA-amidohydrolases were first cloned from Arabidopsis; ILR1, IAR3, ILL1 and ILL2 encode active IAA- amino acid hydrolases, and three additional amidohydrolase-like genes (ILL3, ILL5, ILL6) have been isolated. In higher plants, the growth regulator indole-3-acetic acid (IAA or auxin) is found both free and conjugated via amide bonding to a variety of amino acids and peptides, and via an ester linkage to carbohydrates. IAA-Asp conjugates are involved in homeostatic control, protection, storing and subsequent use of free IAA. IAA-Asp is also found in some plants as a unique intermediate for entering into IAA non-decarboxylative oxidative pathway. IAA amidohydrolase cleaves the amide bond between the auxin and the conjugated amino acid. Enterobacter agglomerans IAAspH has very strong enzyme activity and substrate specificity towards IAA-Asp, although its substrate affinity is weaker compared to Arabidopsis enzymes of the ILR1 gene family. Enhanced IAA-hydrolase activity has been observed during clubroot disease in Chinese cabbage.


Pssm-ID: 349938 [Multi-domain]  Cd Length: 376  Bit Score: 38.84  E-value: 4.70e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763177151 204 LPIGVVSAI-----AGAKRFNINVQGMAGHAGtVPMSMRhDALCASAEMLLAVESISQQRA----GVVATVGKIeNAPNG 274
Cdd:cd08017  152 LPTGTIASRpgpflAGAGRFEVVIRGKGGHAA-MPHHTV-DPVVAASSAVLALQQLVSRETdpldSQVVSVTRF-NGGHA 228

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763177151 275 VNVISGKTVFSLDIRSeddnLRDAVLAEILQKFEHIAALR--------NVKLEIEQTHSAPAVLCDEALK------AALV 340
Cdd:cd08017  229 FNVIPDSVTFGGTLRA----LTTEGFYRLRQRIEEVIEGQaavhrcnaTVDFSEDERPPYPPTVNDERMYehakkvAADL 304

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 763177151 341 KGVEASNIPAKILasgAGHDAMAMAELCPVAMLF--TRCKGGISHHPAESITHQDVEASL---SALH 402
Cdd:cd08017  305 LGPENVKIAPPVM---GAEDFAFYAEKIPAAFFFlgIRNETAGSVHSLHSPYFFLDEEVLpvgAALH 368
M20_dimer pfam07687
Peptidase dimerization domain; This domain consists of 4 beta strands and two alpha helices ...
 214-312 7.71e-03

Peptidase dimerization domain; This domain consists of 4 beta strands and two alpha helices which make up the dimerization surface of members of the M20 family of peptidases. This family includes a range of zinc metallopeptidases belonging to several families in the peptidase classification. Family M20 are Glutamate carboxypeptidases. Peptidase family M25 contains X-His dipeptidases.


Pssm-ID: 400158 [Multi-domain]  Cd Length: 107  Bit Score: 35.78  E-value: 7.71e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763177151  214 GAKRFNINVQGMAGHAGtvpmsMRHDALCASAEMLLAVESISQQRAGVVA-------TVGKIEnAPNGVNVISGKTVFSL 286
Cdd:pfam07687   5 GLAGGHLTVKGKAGHSG-----APGKGVNAIKLLARLLAELPAEYGDIGFdfprttlNITGIE-GGTATNVIPAEAEAKF 78

                          90       100
                  ....*....|....*....|....*.
gi 763177151  287 DIRSEDDNLRDAVLAEILQKFEHIAA 312
Cdd:pfam07687  79 DIRLLPGEDLEELLEEIEAILEKELP 104
M20_ArgE_DapE-like cd05651
M20 peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ...
 35-128 8.72e-03

M20 peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate desuccinylases; Peptidase M20 family, uncharacterized protein subfamily with similarity to acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase (ArgE/DapE) subfamily. ArgE/DapE enzymes catalyze analogous reactions and share a common activator, the metal ion (usually Co2+ or Zn2+). ArgE catalyzes a broad range of substrates, including N-acetylornithine, alpha-N-acetylmethionine and alpha-N-formylmethionine, while DapE catalyzes the hydrolysis of N-succinyl-L,L-diaminopimelate (L,L-SDAP) to L,L-diaminopimelate and succinate. Proteins in this subfamily are bacterial, and have been inferred by homology as being related to both ArgE and DapE.


Pssm-ID: 349902 [Multi-domain]  Cd Length: 341  Bit Score: 38.06  E-value: 8.72e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 763177151  35 EQHKLANqLTSGWMIEAGMTTwQDAAGNIWGRYSSAVPNAPRMILGSHLDTV-PNGG---------KYDGML-------- 96
Cdd:cd05651   18 EEHKTAD-LIENYLEQKGIPF-KRKGNNVWAENGHFDEGKPTLLLNSHHDTVkPNAGwtkdpfepvEKGGKLyglgsnda 95

                         90       100       110
                 ....*....|....*....|....*....|...
gi 763177151  97 -GVVAAITLVALFNGEQKKFPYHIDIVGFCDEE 128
Cdd:cd05651   96 gASVVSLLATFLHLYSEGPLNYNLIYAASAEEE 128
 
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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