NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|39654820|pdb|1R3N|H]
View 

Chain H, beta-alanine synthase

Protein Classification

M20 family metallo-hydrolase( domain architecture ID 10133867)

M20 family metallo-hydrolase functions as an amidohydrolase, catalyzing the hydrolysis of amide bonds in target substrates; similar to Bacillus subtilis allantoate amidohydrolase that converts allantoate to (S)-ureidoglycolate and ammonia

CATH:  3.40.630.10
Gene Ontology:  GO:0016787|GO:0008270
MEROPS:  M20
PubMed:  7674922|18429165|12773192

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
M20_bAS cd03884
M20 Peptidase beta-alanine synthase, an amidohydrolase; Peptidase M20 family, beta-alanine ...
 49-443 0e+00

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: 533.25  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1R3N_H       49 ARWGqESHEFGMRRLAGTALDGAMRDWFTNECESLGCKVKVDKIGNMFAVYPGKNGGKPT-ATGSHLDTQPEAGKYDGIL 127
Cdd:cd03884   9 AAIG-ATPAGGVTRLALTDEDRAARDLFVEWMEEAGLSVRVDAVGNLFGRLEGTDPDAPPvLTGSHLDTVPNGGRYDGIL 87

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1R3N_H      128 GVLAGLEVLRTFKDNNYVPNYDVCVVVWFNEEGARFARSCTGSSVWSHDLSLEEAYglmSVGEDKPESVYDSLKNIGYIG 207
Cdd:cd03884  88 GVLAGLEALRALKEAGIRPRRPIEVVAFTNEEGSRFPPSMLGSRAFAGTLDLEELL---SLRDADGVSLAEALKAIGYDG 164

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1R3N_H      208 DTPAS-YKENEIDAHFELHIEQGPILEDENKAIGIVTGVQAYNWQKVTVHGVGAHAGTTPWRLRKDALLMSSKMIVAASE 286
Cdd:cd03884 165 DRPASaRRPGDIKAYVELHIEQGPVLEEEGLPIGVVTGIAGQRWLEVTVTGEAGHAGTTPMALRRDALLAAAELILAVEE 244

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1R3N_H      287 IAQRH--NGLFTCGIIDAKPYSVNIIPGEVSFTLDFRHPSDDVLATMLKEAAAEFDrliKINDGGALSYESETLQVSPAV 364
Cdd:cd03884 245 IALEHgdDLVATVGRIEVKPNAVNVIPGEVEFTLDLRHPDDAVLDAMVERIRAEAE---AIAAERGVEVEVERLWDSPPV 321

                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
1R3N_H      365 NFHEVCIECVSRSAFAQfkKDQVRQIWSGAGHDSCQTAPHVPTSMIFIPSKDGLSHNYYEYSSPEEIENGFKVLLQAII 443
Cdd:cd03884 322 PFDPELVAALEAAAEAL--GLSYRRMPSGAGHDAMFMARICPTAMIFVPSRDGISHNPAEYTSPEDLAAGVQVLLHALL 398
 
Name Accession Description Interval E-value
M20_bAS cd03884
M20 Peptidase beta-alanine synthase, an amidohydrolase; Peptidase M20 family, beta-alanine ...
 49-443 0e+00

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: 533.25  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1R3N_H       49 ARWGqESHEFGMRRLAGTALDGAMRDWFTNECESLGCKVKVDKIGNMFAVYPGKNGGKPT-ATGSHLDTQPEAGKYDGIL 127
Cdd:cd03884   9 AAIG-ATPAGGVTRLALTDEDRAARDLFVEWMEEAGLSVRVDAVGNLFGRLEGTDPDAPPvLTGSHLDTVPNGGRYDGIL 87

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1R3N_H      128 GVLAGLEVLRTFKDNNYVPNYDVCVVVWFNEEGARFARSCTGSSVWSHDLSLEEAYglmSVGEDKPESVYDSLKNIGYIG 207
Cdd:cd03884  88 GVLAGLEALRALKEAGIRPRRPIEVVAFTNEEGSRFPPSMLGSRAFAGTLDLEELL---SLRDADGVSLAEALKAIGYDG 164

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1R3N_H      208 DTPAS-YKENEIDAHFELHIEQGPILEDENKAIGIVTGVQAYNWQKVTVHGVGAHAGTTPWRLRKDALLMSSKMIVAASE 286
Cdd:cd03884 165 DRPASaRRPGDIKAYVELHIEQGPVLEEEGLPIGVVTGIAGQRWLEVTVTGEAGHAGTTPMALRRDALLAAAELILAVEE 244

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1R3N_H      287 IAQRH--NGLFTCGIIDAKPYSVNIIPGEVSFTLDFRHPSDDVLATMLKEAAAEFDrliKINDGGALSYESETLQVSPAV 364
Cdd:cd03884 245 IALEHgdDLVATVGRIEVKPNAVNVIPGEVEFTLDLRHPDDAVLDAMVERIRAEAE---AIAAERGVEVEVERLWDSPPV 321

                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
1R3N_H      365 NFHEVCIECVSRSAFAQfkKDQVRQIWSGAGHDSCQTAPHVPTSMIFIPSKDGLSHNYYEYSSPEEIENGFKVLLQAII 443
Cdd:cd03884 322 PFDPELVAALEAAAEAL--GLSYRRMPSGAGHDAMFMARICPTAMIFVPSRDGISHNPAEYTSPEDLAAGVQVLLHALL 398
PRK09290 PRK09290
allantoate amidohydrolase; Reviewed
 26-446 3.34e-148

allantoate amidohydrolase; Reviewed


Pssm-ID: 236456 [Multi-domain]  Cd Length: 413  Bit Score: 428.42  E-value: 3.34e-148
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1R3N_H        26 PLSIASGRLNQTILETgSQFGGvarwgQESHefGMRRLAGTALDGAMRDWFTNECESLGCKVKVDKIGNMFAVYPGKNGG 105
Cdd:PRK09290   1 MLRIDAERLWARLDEL-AKIGA-----TPDG--GVTRLALSPEDLQARDLFAEWMEAAGLTVRVDAVGNLFGRLEGRDPD 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1R3N_H       106 KPT-ATGSHLDTQPEAGKYDGILGVLAGLEVLRTFKDNNYVPNYDVCVVVWFNEEGARFARSCTGSSVWSHDLSLEEAYG 184
Cdd:PRK09290  73 APAvLTGSHLDTVPNGGRFDGPLGVLAGLEAVRTLNERGIRPRRPIEVVAFTNEEGSRFGPAMLGSRVFTGALTPEDALA 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1R3N_H       185 LmsvgEDKP-ESVYDSLKNIGYIGDTP--ASYKENEIDAHFELHIEQGPILEDENKAIGIVTGVQAYNWQKVTVHGVGAH 261
Cdd:PRK09290 153 L----RDADgVSFAEALAAIGYDGDEAvgAARARRDIKAFVELHIEQGPVLEAEGLPIGVVTGIVGQRRYRVTFTGEANH 228

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1R3N_H       262 AGTTPWRLRKDALLMSSKMIVAASEIAQRHNG--LFTCGIIDAKPYSVNIIPGEVSFTLDFRHPSDDVLATMLKEAAAEF 339
Cdd:PRK09290 229 AGTTPMALRRDALLAAAEIILAVERIAAAHGPdlVATVGRLEVKPNSVNVIPGEVTFTLDIRHPDDAVLDALVAELRAAA 308

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1R3N_H       340 DRlikINDGGALSYESETLQVSPAVNFHEVCIECVSRSAFAQfkKDQVRQIWSGAGHDSCQTAPHVPTSMIFIPSKDGLS 419
Cdd:PRK09290 309 EA---IAARRGVEVEIELISRRPPVPFDPGLVAALEEAAERL--GLSYRRLPSGAGHDAQILAAVVPTAMIFVPSVGGIS 383

                        410       420
                 ....*....|....*....|....*..
1R3N_H       420 HNYYEYSSPEEIENGFKVLLQAIINYD 446
Cdd:PRK09290 384 HNPAEFTSPEDCAAGANVLLHALLELA 410
hydantase TIGR01879
amidase, hydantoinase/carbamoylase family; Enzymes in this subfamily hydrolize the amide bonds ...
 33-443 2.66e-109

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: 329.08  E-value: 2.66e-109
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1R3N_H         33 RLNQTILETGSqFGGVArwgqeshEFGMRRLAGTALDGAMRDWFTNECESLGCKVKVDKIGNMFAVYPGKN-GGKPTATG 111
Cdd:TIGR01879   2 RLWETLMWLGE-VGADP-------AGGMTRLALSPEDREAQDLFKKRMRAAGLEVRFDEVGNLIGRKEGTEpPLEVVLSG 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1R3N_H        112 SHLDTQPEAGKYDGILGVLAGLEVLRTFKDNNYVPNYDVCVVVWFNEEGARFARSCTGSSVWSHDLSLEEaygLMSVGED 191
Cdd:TIGR01879  74 SHLDTVVNGGNFDGQLGVLAGIEVVDALKEAYVVPLHPIEVVAFTEEEGSRFPYGMWGSRNMVGLANPED---VRNICDA 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1R3N_H        192 KPESVYDSLKNIGYIGDTPASYKENEIDAHFELHIEQGPILEDENKAIGIVTGVQAYNWQKVTVHGVGAHAGTTPWRLRK 271
Cdd:TIGR01879 151 KGISFAEAMKACGPDLPNQPLRPRGDIKAYVELHIEQGPVLESNGQPIGVVNAIAGQRWYKVTLNGESNHAGTTPMSLRR 230

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1R3N_H        272 DALLMSSKMIVAASEIAQRHN-GLFTCGIIDAKPYSVNIIPGEVSFTLDFRHPSDDVLATMLKEAAAEFDRlikINDGGA 350
Cdd:TIGR01879 231 DPLVAASRIIHQVEEKAKRGDpTVGTVGKVEARPNGVNVIPGKVTFTLDLRHTDAAVLRDFTQQLENDIKA---ISDERD 307

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1R3N_H        351 LSYESETLQVSPAVNFHEVCIECVSRSAFAQfkKDQVRQIWSGAGHDSCQTAPHVPTSMIFIPSKDGLSHNYYEYSSPEE 430
Cdd:TIGR01879 308 IGIDIERWMDEPPVPCSEELVAALTELCERL--GYNARVMVSGAGHDAQILAPIVPIGMIFIPSINGISHNPAEWSNITD 385

                         410
                  ....*....|...
1R3N_H        431 IENGFKVLLQAII 443
Cdd:TIGR01879 386 CAEGAKVLYLMVY 398
Peptidase_M20 pfam01546
Peptidase family M20/M25/M40; This family includes a range of zinc metallopeptidases belonging ...
 109-444 9.73e-44

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: 155.97  E-value: 9.73e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1R3N_H        109 ATGSHLDTQPE--------AGKYDGIL----------GVLAGLEVLRTFKDNNYVPnYDVCVVVWFNEEGarfarSCTGS 170
Cdd:pfam01546   1 LLRGHMDVVPDeetwgwpfKSTEDGKLygrghddmkgGLLAALEALRALKEEGLKK-GTVKLLFQPDEEG-----GMGGA 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1R3N_H        171 SVWSHDLSLEEayglmsvgedkpesvydslknigyigdtpasykeNEIDAHFELHIEQGPILEdENKAIGIVTGVQAYNW 250
Cdd:pfam01546  75 RALIEDGLLER----------------------------------EKVDAVFGLHIGEPTLLE-GGIAIGVVTGHRGSLR 119

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1R3N_H        251 QKVTVHGVGAHAGTTPwrLRKDALLMSSKMIVAASEIAQR-----HNGLFTCGIIDAKPYSVNIIPGEVSFTLDFRHPSD 325
Cdd:pfam01546 120 FRVTVKGKGGHASTPH--LGVNAIVAAARLILALQDIVSRnvdplDPAVVTVGNITGIPGGVNVIPGEAELKGDIRLLPG 197

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1R3N_H        326 DVLATMLKEAAAEFDrliKINDGGALSYE-SETLQVSPAVNFHEVCIECVSRSAFAQFKKDQVRQI-WSGAGHDSCQTAP 403
Cdd:pfam01546 198 EDLEELEERIREILE---AIAAAYGVKVEvEYVEGGAPPLVNDSPLVAALREAAKELFGLKVELIVsGSMGGTDAAFFLL 274

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|.
1R3N_H        404 HVPTSMIFIPSKDGLSHNYYEYSSPEEIENGFKVLLQAIIN 444
Cdd:pfam01546 275 GVPPTVVFFGPGSGLAHSPNEYVDLDDLEKGAKVLARLLLK 315
AbgB COG1473
Metal-dependent amidase/aminoacylase/carboxypeptidase [General function prediction only]; ...
 252-445 2.85e-14

Metal-dependent amidase/aminoacylase/carboxypeptidase [General function prediction only]; Metal-dependent amidase/aminoacylase/carboxypeptidase is part of the Pathway/BioSystem: Lysine biosynthesis


Pssm-ID: 441082 [Multi-domain]  Cd Length: 386  Bit Score: 74.00  E-value: 2.85e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1R3N_H      252 KVTVHGVGAHAGtTPWRLRkDALLMSSKMIVAASEIAQRH-----NGLFTCGIIDAKpYSVNIIPGEVSFTLDFRHPSDD 326
Cdd:COG1473 187 EITIKGKGGHAA-APHLGI-DPIVAAAQIVTALQTIVSRNvdpldPAVVTVGIIHGG-TAPNVIPDEAELEGTVRTFDPE 263

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1R3N_H      327 VLATMlkeaaaeFDRLIKINDGGALSY----ESETLQVSPAVNFHEVCIECVSRSAFAQFKKDQVRQIW-SGAGHDSCQT 401
Cdd:COG1473 264 VRELL-------EERIERIAEGIAAAYgataEVEYLRGYPPTVNDPELTELAREAAREVLGEENVVDAEpSMGSEDFAYY 336

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
1R3N_H      402 APHVPTSMIFIPSKDGLS----HNyYEYSSPEE-IENGFKVLLQAIINY 445
Cdd:COG1473 337 LQKVPGAFFFLGAGNPGTvpplHS-PKFDFDEKaLPIGAKALAALALDL 384
 
Name Accession Description Interval E-value
M20_bAS cd03884
M20 Peptidase beta-alanine synthase, an amidohydrolase; Peptidase M20 family, beta-alanine ...
 49-443 0e+00

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: 533.25  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1R3N_H       49 ARWGqESHEFGMRRLAGTALDGAMRDWFTNECESLGCKVKVDKIGNMFAVYPGKNGGKPT-ATGSHLDTQPEAGKYDGIL 127
Cdd:cd03884   9 AAIG-ATPAGGVTRLALTDEDRAARDLFVEWMEEAGLSVRVDAVGNLFGRLEGTDPDAPPvLTGSHLDTVPNGGRYDGIL 87

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1R3N_H      128 GVLAGLEVLRTFKDNNYVPNYDVCVVVWFNEEGARFARSCTGSSVWSHDLSLEEAYglmSVGEDKPESVYDSLKNIGYIG 207
Cdd:cd03884  88 GVLAGLEALRALKEAGIRPRRPIEVVAFTNEEGSRFPPSMLGSRAFAGTLDLEELL---SLRDADGVSLAEALKAIGYDG 164

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1R3N_H      208 DTPAS-YKENEIDAHFELHIEQGPILEDENKAIGIVTGVQAYNWQKVTVHGVGAHAGTTPWRLRKDALLMSSKMIVAASE 286
Cdd:cd03884 165 DRPASaRRPGDIKAYVELHIEQGPVLEEEGLPIGVVTGIAGQRWLEVTVTGEAGHAGTTPMALRRDALLAAAELILAVEE 244

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1R3N_H      287 IAQRH--NGLFTCGIIDAKPYSVNIIPGEVSFTLDFRHPSDDVLATMLKEAAAEFDrliKINDGGALSYESETLQVSPAV 364
Cdd:cd03884 245 IALEHgdDLVATVGRIEVKPNAVNVIPGEVEFTLDLRHPDDAVLDAMVERIRAEAE---AIAAERGVEVEVERLWDSPPV 321

                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
1R3N_H      365 NFHEVCIECVSRSAFAQfkKDQVRQIWSGAGHDSCQTAPHVPTSMIFIPSKDGLSHNYYEYSSPEEIENGFKVLLQAII 443
Cdd:cd03884 322 PFDPELVAALEAAAEAL--GLSYRRMPSGAGHDAMFMARICPTAMIFVPSRDGISHNPAEYTSPEDLAAGVQVLLHALL 398
PRK09290 PRK09290
allantoate amidohydrolase; Reviewed
 26-446 3.34e-148

allantoate amidohydrolase; Reviewed


Pssm-ID: 236456 [Multi-domain]  Cd Length: 413  Bit Score: 428.42  E-value: 3.34e-148
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1R3N_H        26 PLSIASGRLNQTILETgSQFGGvarwgQESHefGMRRLAGTALDGAMRDWFTNECESLGCKVKVDKIGNMFAVYPGKNGG 105
Cdd:PRK09290   1 MLRIDAERLWARLDEL-AKIGA-----TPDG--GVTRLALSPEDLQARDLFAEWMEAAGLTVRVDAVGNLFGRLEGRDPD 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1R3N_H       106 KPT-ATGSHLDTQPEAGKYDGILGVLAGLEVLRTFKDNNYVPNYDVCVVVWFNEEGARFARSCTGSSVWSHDLSLEEAYG 184
Cdd:PRK09290  73 APAvLTGSHLDTVPNGGRFDGPLGVLAGLEAVRTLNERGIRPRRPIEVVAFTNEEGSRFGPAMLGSRVFTGALTPEDALA 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1R3N_H       185 LmsvgEDKP-ESVYDSLKNIGYIGDTP--ASYKENEIDAHFELHIEQGPILEDENKAIGIVTGVQAYNWQKVTVHGVGAH 261
Cdd:PRK09290 153 L----RDADgVSFAEALAAIGYDGDEAvgAARARRDIKAFVELHIEQGPVLEAEGLPIGVVTGIVGQRRYRVTFTGEANH 228

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1R3N_H       262 AGTTPWRLRKDALLMSSKMIVAASEIAQRHNG--LFTCGIIDAKPYSVNIIPGEVSFTLDFRHPSDDVLATMLKEAAAEF 339
Cdd:PRK09290 229 AGTTPMALRRDALLAAAEIILAVERIAAAHGPdlVATVGRLEVKPNSVNVIPGEVTFTLDIRHPDDAVLDALVAELRAAA 308

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1R3N_H       340 DRlikINDGGALSYESETLQVSPAVNFHEVCIECVSRSAFAQfkKDQVRQIWSGAGHDSCQTAPHVPTSMIFIPSKDGLS 419
Cdd:PRK09290 309 EA---IAARRGVEVEIELISRRPPVPFDPGLVAALEEAAERL--GLSYRRLPSGAGHDAQILAAVVPTAMIFVPSVGGIS 383

                        410       420
                 ....*....|....*....|....*..
1R3N_H       420 HNYYEYSSPEEIENGFKVLLQAIINYD 446
Cdd:PRK09290 384 HNPAEFTSPEDCAAGANVLLHALLELA 410
PRK12893 PRK12893
Zn-dependent hydrolase;
49-441 8.99e-135

Zn-dependent hydrolase;


Pssm-ID: 237250 [Multi-domain]  Cd Length: 412  Bit Score: 394.25  E-value: 8.99e-135
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1R3N_H        49 ARWGQESHEfGMRRLAGTALDGAMRDWFTNECESLGCKVKVDKIGNMFAVYPGKNGGKPT-ATGSHLDTQPEAGKYDGIL 127
Cdd:PRK12893  20 ARIGATPGG-GVTRLALTDEDREARDLLAQWMEEAGLTVSVDAIGNLFGRRAGTDPDAPPvLIGSHLDTQPTGGRFDGAL 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1R3N_H       128 GVLAGLEVLRTFKDNNYVPNYDVCVVVWFNEEGARFARSCTGSSVWSHDLSLEEAYGLMSvgeDKPESVYDSLKNIGYIG 207
Cdd:PRK12893  99 GVLAALEVVRTLNDAGIRTRRPIEVVSWTNEEGARFAPAMLGSGVFTGALPLDDALARRD---ADGITLGEALARIGYRG 175

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1R3N_H       208 DTPAsyKENEIDAHFELHIEQGPILEDENKAIGIVTGVQAYNWQKVTVHGVGAHAGTTPWRLRKDALLMSSKMIVAASEI 287
Cdd:PRK12893 176 TARV--GRRAVDAYLELHIEQGPVLEAEGLPIGVVTGIQGIRWLEVTVEGQAAHAGTTPMAMRRDALVAAARIILAVERI 253

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1R3N_H       288 AQRHN--GLFTCGIIDAKPYSVNIIPGEVSFTLDFRHPSDDVLATMLkeaaAEFDRLI-KINDGGALSYESETLQVSPAV 364
Cdd:PRK12893 254 AAALApdGVATVGRLRVEPNSRNVIPGKVVFTVDIRHPDDARLDAME----AALRAACaKIAAARGVQVTVETVWDFPPV 329

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
1R3N_H       365 NFHEVCIECVSRSAFAQfkKDQVRQIWSGAGHDSCQTAPHVPTSMIFIPSKDGLSHNYYEYSSPEEIENGFKVLLQA 441
Cdd:PRK12893 330 PFDPALVALVEAAAEAL--GLSHMRMVSGAGHDAMFLARVAPAAMIFVPCRGGISHNEAEDTEPADLAAGANVLLHA 404
PRK12890 PRK12890
allantoate amidohydrolase; Reviewed
 25-446 4.47e-119

allantoate amidohydrolase; Reviewed


Pssm-ID: 237248 [Multi-domain]  Cd Length: 414  Bit Score: 354.21  E-value: 4.47e-119
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1R3N_H        25 APLSIASGRLNQTILEtgsqfggVARWGQEshEFGMRRLAGTALDGAMRDWFTNECESLGCKVKVDKIGNMFAVYPGKNG 104
Cdd:PRK12890   2 TPPPINGERLLARLEE-------LAAIGRD--GPGWTRLALSDEERAARALLAAWMRAAGLEVRRDAAGNLFGRLPGRDP 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1R3N_H       105 G-KPTATGSHLDTQPEAGKYDGILGVLAGLEVLRTFKDNNYVPNYDVCVVVWFNEEGARFARSCTGSSVWSHDLSLEEAy 183
Cdd:PRK12890  73 DlPPLMTGSHLDTVPNGGRYDGILGVLAGLEVVAALREAGIRPPHPLEVIAFTNEEGVRFGPSMIGSRALAGTLDVEAV- 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1R3N_H       184 gLMSVGEDKpESVYDSLKNIGYIGDTPASY--KENEIDAHFELHIEQGPILEDENKAIGIVTGVQAYNWQKVTVHGVGAH 261
Cdd:PRK12890 152 -LATRDDDG-TTLAEALRRIGGDPDALPGAlrPPGAVAAFLELHIEQGPVLEAEGLPIGVVTAIQGIRRQAVTVEGEANH 229

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1R3N_H       262 AGTTPWRLRKDALLMSSKMIVAASEIAQR--HNGLFTCGIIDAKPYSVNIIPGEVSFTLDFRHPSDDVLATMLKEAAAEF 339
Cdd:PRK12890 230 AGTTPMDLRRDALVAAAELVTAMERRARAllHDLVATVGRLDVEPNAINVVPGRVVFTLDLRSPDDAVLEAAEAALLAEL 309

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1R3N_H       340 DRlikINDGGALSYESETLQVSPAVNFHEVCIECVSRSAFAQfkKDQVRQIWSGAGHDSCQTAPHVPTSMIFIPSKDGLS 419
Cdd:PRK12890 310 EA---IAAARGVRIELERLSRSEPVPCDPALVDAVEAAAARL--GYPSRRMPSGAGHDAAAIARIGPSAMIFVPCRGGIS 384

                        410       420
                 ....*....|....*....|....*..
1R3N_H       420 HNYYEYSSPEEIENGFKVLLQAIINYD 446
Cdd:PRK12890 385 HNPEEAMDPEDLAAGARVLLDAVLRLD 411
hydantase TIGR01879
amidase, hydantoinase/carbamoylase family; Enzymes in this subfamily hydrolize the amide bonds ...
 33-443 2.66e-109

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: 329.08  E-value: 2.66e-109
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1R3N_H         33 RLNQTILETGSqFGGVArwgqeshEFGMRRLAGTALDGAMRDWFTNECESLGCKVKVDKIGNMFAVYPGKN-GGKPTATG 111
Cdd:TIGR01879   2 RLWETLMWLGE-VGADP-------AGGMTRLALSPEDREAQDLFKKRMRAAGLEVRFDEVGNLIGRKEGTEpPLEVVLSG 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1R3N_H        112 SHLDTQPEAGKYDGILGVLAGLEVLRTFKDNNYVPNYDVCVVVWFNEEGARFARSCTGSSVWSHDLSLEEaygLMSVGED 191
Cdd:TIGR01879  74 SHLDTVVNGGNFDGQLGVLAGIEVVDALKEAYVVPLHPIEVVAFTEEEGSRFPYGMWGSRNMVGLANPED---VRNICDA 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1R3N_H        192 KPESVYDSLKNIGYIGDTPASYKENEIDAHFELHIEQGPILEDENKAIGIVTGVQAYNWQKVTVHGVGAHAGTTPWRLRK 271
Cdd:TIGR01879 151 KGISFAEAMKACGPDLPNQPLRPRGDIKAYVELHIEQGPVLESNGQPIGVVNAIAGQRWYKVTLNGESNHAGTTPMSLRR 230

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1R3N_H        272 DALLMSSKMIVAASEIAQRHN-GLFTCGIIDAKPYSVNIIPGEVSFTLDFRHPSDDVLATMLKEAAAEFDRlikINDGGA 350
Cdd:TIGR01879 231 DPLVAASRIIHQVEEKAKRGDpTVGTVGKVEARPNGVNVIPGKVTFTLDLRHTDAAVLRDFTQQLENDIKA---ISDERD 307

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1R3N_H        351 LSYESETLQVSPAVNFHEVCIECVSRSAFAQfkKDQVRQIWSGAGHDSCQTAPHVPTSMIFIPSKDGLSHNYYEYSSPEE 430
Cdd:TIGR01879 308 IGIDIERWMDEPPVPCSEELVAALTELCERL--GYNARVMVSGAGHDAQILAPIVPIGMIFIPSINGISHNPAEWSNITD 385

                         410
                  ....*....|...
1R3N_H        431 IENGFKVLLQAII 443
Cdd:TIGR01879 386 CAEGAKVLYLMVY 398
PRK12891 PRK12891
allantoate amidohydrolase; Reviewed
 57-442 6.29e-100

allantoate amidohydrolase; Reviewed


Pssm-ID: 237249  Cd Length: 414  Bit Score: 305.59  E-value: 6.29e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1R3N_H        57 EFGMRRLAGTALDGAMRDWFTNECESLGCKVKVDKIGNMFAVYPGKNGGKPTA-TGSHLDTQPEAGKYDGILGVLAGLEV 135
Cdd:PRK12891  27 KGGVCRLALTDGDREARDLFVAWARDAGCTVRVDAMGNLFARRAGRDPDAAPVmTGSHADSQPTGGRYDGIYGVLGGLEV 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1R3N_H       136 LRTFKDNNYVPNYDVCVVVWFNEEGARFARSCTGSSVWSHDLSLEeaYGLmSVGEDKPESVYDSLKNIGYIGDTPAsyKE 215
Cdd:PRK12891 107 VRALNDAGIETERPVDVVIWTNEEGSRFAPSMVGSGVFFGVYPLE--YLL-SRRDDTGRTLGEHLARIGYAGAEPV--GG 181

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1R3N_H       216 NEIDAHFELHIEQGPILEDENKAIGIVTGVQAYNWQKVTVHGVGAHAGTTPWRLRKDALLMSSKMIVAASEIAQRH--NG 293
Cdd:PRK12891 182 YPVHAAYELHIEQGAILERAGKTIGVVTAGQGQRWYEVTLTGVDAHAGTTPMAFRRDALVGAARMIAFLDALGRRDapDA 261

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1R3N_H       294 LFTCGIIDAKPYSVNIIPGEVSFTLDFRHPSDDVLATMlkeAAAEFDRLIKINDGGALSYESETLQVSPAVNFHEVCIEC 373
Cdd:PRK12891 262 RATVGMIDARPNSRNTVPGECFFTVEFRHPDDAVLDRL---DAALRAELARIADETGLRADIEQIFGYAPAPFAPGCIDA 338

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
1R3N_H       374 VsRSAfAQFKKDQVRQIWSGAGHDSCQTAPHVPTSMIFIPSKDGLSHNYYEYSSPEEIENGFKVLLQAI 442
Cdd:PRK12891 339 V-RDA-ARALGLSHMDIVSGAGHDACFAARGAPTGMIFVPCVDGLSHNEAEAITPEWFAAGADVLLRAV 405
PRK12892 PRK12892
allantoate amidohydrolase; Reviewed
 59-453 2.00e-87

allantoate amidohydrolase; Reviewed


Pssm-ID: 183817 [Multi-domain]  Cd Length: 412  Bit Score: 273.12  E-value: 2.00e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1R3N_H        59 GMRRLAGTALDGAMRDWFTNECESLGCKVKVDKIGNMFAVYPGKNGGKPTATGSHLDTQPEAGKYDGILGVLAGLEVLRT 138
Cdd:PRK12892  28 GVHRPTYSDAHVAARRRLAAWCEAAGLAVRIDGIGNVFGRLPGPGPGPALLVGSHLDSQNLGGRYDGALGVVAGLEAARA 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1R3N_H       139 FKDNNYVPNYDVCVVVWFNEEGARFARSCTGSSVWSHDLSLEEAygLMSVGEDKPESVYDSLKNIGYIGDTPASYKENEI 218
Cdd:PRK12892 108 LNEHGIATRHPLDVVAWCDEEGSRFTPGFLGSRAYAGRLDPADA--LAARCRSDGVPLRDALAAAGLAGRPRPAADRARP 185

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1R3N_H       219 DAHFELHIEQGPILEDENKAIGIVTGVQAYnWQ-KVTVHGVGAHAGTTPWRLRKDALLMSSKMIVAASEIAQRHNG--LF 295
Cdd:PRK12892 186 KGYLEAHIEQGPVLEQAGLPVGVVTGIVGI-WQyRITVTGEAGHAGTTPMALRRDAGLAAAEMIAAIDEHFPRVCGpaVV 264

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1R3N_H       296 TCGIIDAKPYSVNIIPGEVSFTLDFRHPSDDVLATMLKEAAAEFDrliKINDGGALSYESETLQVSPAVNFHEVCIECVS 375
Cdd:PRK12892 265 TVGRVALDPGSPSIIPGRVEFSFDARHPSPPVLQRLVALLEALCR---EIARRRGCRVSVDRIAEYAPAPCDAALVDALR 341

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
1R3N_H       376 RSAFAQFKKdqVRQIWSGAGHDSCQTAPHVPTSMIFIPSKDGLSHNYYEYSSPEEIENGFKVLLQAIinydnYRVIRG 453
Cdd:PRK12892 342 AAAEAAGGP--YLEMPSGAGHDAQNMARIAPSAMLFVPSKGGISHNPAEDTSPADLAQGARVLADTL-----RRLARG 412
Peptidase_M20 pfam01546
Peptidase family M20/M25/M40; This family includes a range of zinc metallopeptidases belonging ...
 109-444 9.73e-44

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: 155.97  E-value: 9.73e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1R3N_H        109 ATGSHLDTQPE--------AGKYDGIL----------GVLAGLEVLRTFKDNNYVPnYDVCVVVWFNEEGarfarSCTGS 170
Cdd:pfam01546   1 LLRGHMDVVPDeetwgwpfKSTEDGKLygrghddmkgGLLAALEALRALKEEGLKK-GTVKLLFQPDEEG-----GMGGA 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1R3N_H        171 SVWSHDLSLEEayglmsvgedkpesvydslknigyigdtpasykeNEIDAHFELHIEQGPILEdENKAIGIVTGVQAYNW 250
Cdd:pfam01546  75 RALIEDGLLER----------------------------------EKVDAVFGLHIGEPTLLE-GGIAIGVVTGHRGSLR 119

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1R3N_H        251 QKVTVHGVGAHAGTTPwrLRKDALLMSSKMIVAASEIAQR-----HNGLFTCGIIDAKPYSVNIIPGEVSFTLDFRHPSD 325
Cdd:pfam01546 120 FRVTVKGKGGHASTPH--LGVNAIVAAARLILALQDIVSRnvdplDPAVVTVGNITGIPGGVNVIPGEAELKGDIRLLPG 197

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1R3N_H        326 DVLATMLKEAAAEFDrliKINDGGALSYE-SETLQVSPAVNFHEVCIECVSRSAFAQFKKDQVRQI-WSGAGHDSCQTAP 403
Cdd:pfam01546 198 EDLEELEERIREILE---AIAAAYGVKVEvEYVEGGAPPLVNDSPLVAALREAAKELFGLKVELIVsGSMGGTDAAFFLL 274

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|.
1R3N_H        404 HVPTSMIFIPSKDGLSHNYYEYSSPEEIENGFKVLLQAIIN 444
Cdd:pfam01546 275 GVPPTVVFFGPGSGLAHSPNEYVDLDDLEKGAKVLARLLLK 315
PRK13799 PRK13799
unknown domain/N-carbamoyl-L-amino acid hydrolase fusion protein; Provisional
 86-445 1.16e-35

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


Pssm-ID: 106740 [Multi-domain]  Cd Length: 591  Bit Score: 139.38  E-value: 1.16e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1R3N_H        86 KVKVDKIGNMFAVYPGKNG-GKPTATGSHLDTQPEAGKYDGILGVLAGLEVLRTFKDNNYVPNYDVCVVVWFNEEGARFA 164
Cdd:PRK13799 231 EVEIDAVGNVVGRYKAADDdAKTLITGSHYDTVRNGGKYDGREGIFLAIACVKELHEQGERLPFHFEVIAFAEEEGQRFK 310

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1R3N_H       165 RSCTGSSVWSHDLSLEeaygLMSVGEDKPESVYDSLKNIGYIGDTPASYKENEID--AHFELHIEQGPILEDENKAIGIV 242
Cdd:PRK13799 311 ATFLGSGALIGDFNME----LLDIKDADGISLREAIQHAGHCIDAIPKIARDPADvlGFIEVHIEQGPVLLELDIPLGIV 386

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1R3N_H       243 TGVQAYNWQKVTVHGVGAHAGTTPWRLRKDALLMSSKMIVAASEIAQR--HNGLF-TCGIIDAKPYSVNIIPGEVSFTLD 319
Cdd:PRK13799 387 TSIAGSARYICEFIGMASHAGTTPMDMRKDAAAAAAEIALYIEKRAAQdqHASLVaTMGQLNVPSGSTNVIPGRCQFSLD 466

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1R3N_H       320 FRHPSDDVLATMLKEAAAEFDRLIKINDggaLSYESETLQVSPAVNfhevCIECVSRSAFAQFKKDQVR--QIWSGAGHD 397
Cdd:PRK13799 467 IRAATDEIRDAAVADILAEIAAIAARRG---IEYKAELAMKAAAAP----CAPELMKQLEAATDAAGVPlfELASGAGHD 539

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*....
1R3N_H       398 SCQTAPHVPTSMIFIPSKD-GLSHNYYEYSSPEEIENGFKVLLQAIINY 445
Cdd:PRK13799 540 AMKIAEIMDQAMLFTRCGNaGISHNPLESMTADDMELSADAFLDFLNNF 588
PRK13590 PRK13590
putative bifunctional OHCU decarboxylase/allantoate amidohydrolase; Provisional
 54-432 1.30e-34

putative bifunctional OHCU decarboxylase/allantoate amidohydrolase; Provisional


Pssm-ID: 184168 [Multi-domain]  Cd Length: 591  Bit Score: 136.42  E-value: 1.30e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1R3N_H        54 ESHEFGMRRLAGTaldgaMRDwftneCeslGC-KVKVDKIGNMFAVYPGKN-GGKPTATGSHLDTQPEAGKYDGILGVLA 131
Cdd:PRK13590 211 DAHRACAQQISHW-----MRD-----C---GFdEVHIDAVGNVVGRYKGSTpQAKRLLTGSHYDTVRNGGKYDGRLGIFV 277

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1R3N_H       132 GLEVLRTFKDNNYVPNYDVCVVVWFNEEGARFARSCTGSSVWSHD-----LSLEEAYGLmsvgedkpeSVYDSLKNIGY- 205
Cdd:PRK13590 278 PMACVRELHRQGRRLPFGLEVVGFAEEEGQRYKATFLGSGALIGDfdpawLDQKDADGI---------TMREAMQHAGLc 348

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1R3N_H       206 IGDTPASYKE-NEIDAHFELHIEQGPILEDENKAIGIVTGVQAYNWQKVTVHGVGAHAGTTPWRLRKDALLMSSKMIV-A 283
Cdd:PRK13590 349 IDDIPKLRRDpARYLGFVEVHIEQGPVLNELDLPLGIVTSINGSVRYVGEMIGMASHAGTTPMDRRRDAAAAVAELALyV 428

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1R3N_H       284 ASEIAQRHNGLFTCGIIDAKPYSVNIIPGEVSFTLDFRHPSDDVLATMLKEAAAEFDRlikINDGGALSYE-SETLQVSP 362
Cdd:PRK13590 429 EQRAAQDGDSVGTVGMLEVPGGSINVVPGRCRFSLDIRAPTDAQRDAMVADVLAELEA---ICERRGLRYTlEETMRAAA 505

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
1R3N_H       363 AvnfhevciecVSRSAFAQFKKDQVR-------QIWSGAGHDSCQTAPHVPTSMIFIPSKD-GLSHNYYEYSSPEEIE 432
Cdd:PRK13590 506 A----------PSAPAWQQRWEAAVAalglplfRMPSGAGHDAMKLHEIMPQAMLFVRGENaGISHNPLESSTADDMQ 573
Zinc_peptidase_like cd03873
Zinc peptidases M18, M20, M28, and M42; Zinc peptidases play vital roles in metabolic and ...
 94-185 1.18e-16

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: 78.24  E-value: 1.18e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1R3N_H       94 NMFAVYPGKNGGKPTATGSHLDTQPE----------------------AGKYDGILGVLAGLEVLRTFKDNNYVPNYDVC 151
Cdd:cd03873   1 NLIARLGGGEGGKSVALGAHLDVVPAgegdnrdppfaedteeegrlygRGALDDKGGVAAALEALKRLKENGFKPKGTIV 80

                        90       100       110
                ....*....|....*....|....*....|....*
1R3N_H      152 VVVWFNEEGARFARSCTGSSVW-SHDLSLEEAYGL 185
Cdd:cd03873  81 VAFTADEEVGSGGGKGLLSKFLlAEDLKVDAAFVI 115
M20_18_42 cd18669
M20, M18 and M42 Zn-peptidases include aminopeptidases and carboxypeptidases; This family ...
 94-173 5.84e-16

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: 76.32  E-value: 5.84e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1R3N_H       94 NMFAVYPGKNGGKPTATGSHLDTQPE----------------------AGKYDGILGVLAGLEVLRTFKDNNYVPNYDVC 151
Cdd:cd18669   1 NVIARYGGGGGGKRVLLGAHIDVVPAgegdprdppffvdtveegrlygRGALDDKGGVAAALEALKLLKENGFKLKGTVV 80

                        90       100
                ....*....|....*....|..
1R3N_H      152 VVVWFNEEGARFARSCTGSSVW 173
Cdd:cd18669  81 VAFTPDEEVGSGAGKGLLSKDA 102
AbgB COG1473
Metal-dependent amidase/aminoacylase/carboxypeptidase [General function prediction only]; ...
 252-445 2.85e-14

Metal-dependent amidase/aminoacylase/carboxypeptidase [General function prediction only]; Metal-dependent amidase/aminoacylase/carboxypeptidase is part of the Pathway/BioSystem: Lysine biosynthesis


Pssm-ID: 441082 [Multi-domain]  Cd Length: 386  Bit Score: 74.00  E-value: 2.85e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1R3N_H      252 KVTVHGVGAHAGtTPWRLRkDALLMSSKMIVAASEIAQRH-----NGLFTCGIIDAKpYSVNIIPGEVSFTLDFRHPSDD 326
Cdd:COG1473 187 EITIKGKGGHAA-APHLGI-DPIVAAAQIVTALQTIVSRNvdpldPAVVTVGIIHGG-TAPNVIPDEAELEGTVRTFDPE 263

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1R3N_H      327 VLATMlkeaaaeFDRLIKINDGGALSY----ESETLQVSPAVNFHEVCIECVSRSAFAQFKKDQVRQIW-SGAGHDSCQT 401
Cdd:COG1473 264 VRELL-------EERIERIAEGIAAAYgataEVEYLRGYPPTVNDPELTELAREAAREVLGEENVVDAEpSMGSEDFAYY 336

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
1R3N_H      402 APHVPTSMIFIPSKDGLS----HNyYEYSSPEE-IENGFKVLLQAIINY 445
Cdd:COG1473 337 LQKVPGAFFFLGAGNPGTvpplHS-PKFDFDEKaLPIGAKALAALALDL 384
ArgE COG0624
Acetylornithine deacetylase/Succinyl-diaminopimelate desuccinylase or related deacylase [Amino ...
 69-345 6.84e-14

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: 73.00  E-value: 6.84e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1R3N_H       69 DGAMRDWFTNECESLGCKVKV----DKIGNMFAVYPGKNGGKPTATGSHLDTQPEAGKY------------DGIL----- 127
Cdd:COG0624  31 EAAAAELLAELLEALGFEVERlevpPGRPNLVARRPGDGGGPTLLLYGHLDVVPPGDLElwtsdpfeptieDGRLygrga 110

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1R3N_H      128 -----GVLAGLEVLRTFKDNNYVPNYDVCVVVWFNEEGarfarSCTGSsvwsHDLSLEEAYGLmsvgedKPESVYdslkn 202
Cdd:COG0624 111 admkgGLAAMLAALRALLAAGLRLPGNVTLLFTGDEEV-----GSPGA----RALVEELAEGL------KADAAI----- 170

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1R3N_H      203 igyIGDTPASYkeneidahfelhieqgpiledenkaiGIVTGVQAYNWQKVTVHGVGAHAGTtPWRLRkDALLMSSKMIV 282
Cdd:COG0624 171 ---VGEPTGVP--------------------------TIVTGHKGSLRFELTVRGKAAHSSR-PELGV-NAIEALARALA 219

                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
1R3N_H      283 AASEIAQ--RHNGLF-----TCGIIDAkPYSVNIIPGEVSFTLDFR----HPSDDVLAtMLKEAAAEFDRLIKI 345
Cdd:COG0624 220 ALRDLEFdgRADPLFgrttlNVTGIEG-GTAVNVIPDEAEAKVDIRllpgEDPEEVLA-ALRALLAAAAPGVEV 291
amidohydrolases TIGR01891
amidohydrolase; This model represents a subfamily of amidohydrolases which are a subset of ...
 216-420 6.82e-08

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: 54.27  E-value: 6.82e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1R3N_H        216 NEIDAHFELHIEqgPILEDENKAIGIVTGVQAYNWQKVTVHGVGAHAGtTPwRLRKDALLMSSKMIVAASEIAQRH---- 291
Cdd:TIGR01891 140 DDVDAILGLHPD--PSIPAGTVGLRPGTIMAAADKFEVTIHGKGAHAA-RP-HLGRDALDAAAQLVVALQQIVSRNvdps 215

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1R3N_H        292 -NGLFTCGIIDAKpYSVNIIPGEVSFTLDFRHPSDDVLATMlkeaaaeFDRLIKINDGGALSY----ESETLQVSPAVNF 366
Cdd:TIGR01891 216 rPAVVSVGIIEAG-GAPNVIPDKASMSGTVRSLDPEVRDQI-------IDRIERIVEGAAAMYgakvELNYDRGLPAVTN 287

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
1R3N_H        367 HEVCIECVSRSAFAQFKKDQV-RQIWSGAG-HDSCQTAPHVPTSMIFIPSK---DGLSH 420
Cdd:TIGR01891 288 DPALTQILKEVARHVVGPENVaEDPEVTMGsEDFAYYSQKVPGAFFFLGIGnegTGLSH 346
M28_like cd05640
M28 Zn-peptidase; uncharacterized subfamily; Peptidase family M28 (also called aminopeptidase ...
 94-225 2.91e-06

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: 48.60  E-value: 2.91e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1R3N_H       94 NMFAVYPGKNG-GKPTATGSHLDTQPEA-GKYDGILGVLAGLEVLRTFKDNnyVPNYDVCVVVWFNEEGARFARSCTGSS 171
Cdd:cd05640  54 NLIADLPGSYSqDKLILIGAHYDTVPGSpGADDNASGVAALLELARLLATL--DPNHTLRFVAFDLEEYPFFARGLMGSH 131

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*
1R3N_H      172 VWSHDLsleEAYGLMSVGedkpesVYdSLKNIGYIGDTPASYK-ENEIDAHFELH 225
Cdd:cd05640 132 AYAEDL---LRPLTPIVG------ML-SLEMIGYYDPFPHSQAyPAGFELHFYPH 176
M20_Acy1_amhX-like cd08018
M20 Peptidase aminoacylase 1 amhX-like subfamily; Peptidase M20 family, uncharacterized ...
 252-444 6.76e-06

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: 48.05  E-value: 6.76e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1R3N_H      252 KVTVHGVGAHaGTTPwRLRKDAllmsskmIVAASEIAQRHNGLFtcgIIDAKPYSV------------NIIPGEVSFTLD 319
Cdd:cd08018 171 EGTIKGKQAH-GARP-HLGINA-------IEAASAIVNAVNAIH---LDPNIPWSVkmtklqaggeatNIIPDKAKFALD 238

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1R3N_H      320 FRHPSDDVLATMLKEAAAEFDRLIKINDggaLSYESETLQVSPAVNFHEVCIECVSRSAFAQFKKDQVRQIWSGAG---- 395
Cdd:cd08018 239 LRAQSNEAMEELKEKVEHAIEAAAALYG---ASIEITEKGGMPAAEYDEEAVELMEEAITEVLGEEKLAGPCVTPGgedf 315

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
1R3N_H      396 HDSCQTAPHVPTSMIFIPS--KDGLSHNYYEYsSPEEIENGFKVLLQAIIN 444
Cdd:cd08018 316 HFYTKKKPELKATMIGLGCglTPGLHHPNMTF-DRDALENGVKILARAVLK 365
PRK08651 PRK08651
succinyl-diaminopimelate desuccinylase; Reviewed
 250-438 1.96e-05

succinyl-diaminopimelate desuccinylase; Reviewed


Pssm-ID: 236323 [Multi-domain]  Cd Length: 394  Bit Score: 46.52  E-value: 1.96e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1R3N_H       250 WQKVTVHGVGAHAGTtPWRLRkDALLMSSKMIVAASEIAQRHNGLFTcgIIDAK---------------PYSVNIIPGEV 314
Cdd:PRK08651 186 WGVVKVYGKQAHAST-PWLGI-NAFEAAAKIAERLKSSLSTIKSKYE--YDDERgakptvtlggptvegGTKTNIVPGYC 261

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1R3N_H       315 SFTLDFRHP----SDDV---LATMLKEAAAEfdrlikinDGGALSYE----SETLQVSPAVNFHEVCIECVSRSafaqFK 383
Cdd:PRK08651 262 AFSIDRRLIpeetAEEVrdeLEALLDEVAPE--------LGIEVEFEitpfSEAFVTDPDSELVKALREAIREV----LG 329

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
1R3N_H       384 KDQVRQIWSGAGHDSCQTAPHVPTsMIFIPSKDGLSHNYYEYSSPEEIENGFKVL 438
Cdd:PRK08651 330 VEPKKTISLGGTDARFFGAKGIPT-VVYGPGELELAHAPDEYVEVKDVEKAAKVY 383
PRK13983 PRK13983
M20 family metallo-hydrolase;
250-363 2.50e-05

M20 family metallo-hydrolase;


Pssm-ID: 237578 [Multi-domain]  Cd Length: 400  Bit Score: 46.38  E-value: 2.50e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1R3N_H       250 WQKVTVHGVGAHAgTTPwRLRKDALLMSSKMIVAASEIAQRH----NGLFTcgiidaKPYS-------------VNIIPG 312
Cdd:PRK13983 198 WLKFTVKGKQCHA-STP-ENGINAHRAAADFALELDEALHEKfnakDPLFD------PPYStfeptkkeanvdnINTIPG 269

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
1R3N_H       313 EVSFTLDFR----HPSDDVLATMlKEAAAEFDRLIKIndggalSYESETLQVSPA 363
Cdd:PRK13983 270 RDVFYFDCRvlpdYDLDEVLKDI-KEIADEFEEEYGV------KIEVEIVQREQA 317
M20_Acy1 cd03886
M20 Peptidase Aminoacylase 1 family; Peptidase M20 family, Aminoacylase 1 (ACY1; hippuricase; ...
 252-423 5.85e-05

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: 45.28  E-value: 5.85e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1R3N_H      252 KVTVHGVGAHAGtTPWrLRKDALLMSSKMIVA-----ASEIAQRHNGLFTCGIIDAKPySVNIIPGEVSFTLDFRHPSDD 326
Cdd:cd03886 175 EITVKGKGGHGA-SPH-LGVDPIVAAAQIVLAlqtvvSRELDPLEPAVVTVGKFHAGT-AFNVIPDTAVLEGTIRTFDPE 251

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1R3N_H      327 VLATMLKEAaaeFDRLIKINDGGALSYESETLQVSPAVNFHEVCIECVSRSAFAQFKKDQVRQIW-SGAGHDSCQTAPHV 405
Cdd:cd03886 252 VREALEARI---KRLAEGIAAAYGATVELEYGYGYPAVINDPELTELVREAAKELLGEEAVVEPEpVMGSEDFAYYLEKV 328

                       170
                ....*....|....*...
1R3N_H      406 PTSMIFIPSKDGLSHNYY 423
Cdd:cd03886 329 PGAFFWLGAGEPDGENPG 346
M20_Acy1-like cd05664
M20 Peptidase aminoacylase 1 subfamily; Peptidase M20 family, Uncharacterized subfamily of ...
 252-417 6.19e-05

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: 45.02  E-value: 6.19e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1R3N_H      252 KVTVHGVGAHaGTTPwRLRKDALLMSSKMI-----VAASEIAQRHNGLFTCGIIDAKpYSVNIIPGEVSFTLDFRHPSDD 326
Cdd:cd05664 185 DITIFGRGGH-GSMP-HLTIDPVVMAASIVtrlqtIVSREVDPQEFAVVTVGSIQAG-SAENIIPDEAELKLNVRTFDPE 261

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1R3N_H      327 VLATMLkeAAAEfdRLIK---INDGGALSYESETLQVSPAVNFHEVCIECVSRSAFAQFKKDQVRQIWSGAGHDSCQ--- 400
Cdd:cd05664 262 VREKVL--NAIK--RIVRaecAASGAPKPPEFTYTDSFPATVNDEDATARLAAAFREYFGEDRVVEVPPVSASEDFSila 337

                       170
                ....*....|....*..
1R3N_H      401 TAPHVPTSMIFIPSKDG 417
Cdd:cd05664 338 TAFGVPSVFWFIGGIDP 354
M20_CPDG2 cd03885
M20 Peptidase Glutamate carboxypeptidase, a periplasmic enzyme; Peptidase M20 family, ...
 71-339 9.38e-05

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: 44.50  E-value: 9.38e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1R3N_H       71 AMRDWFTNECESLGCKV---KVDKIGNM-FAVYPGKnGGKPTATGSHLDTQPEAG-------KYD-------GIL----G 128
Cdd:cd03885  23 RVAELLAEELEALGFTVerrPLGEFGDHlIATFKGT-GGKRVLLIGHMDTVFPEGtlafrpfTVDgdraygpGVAdmkgG 101

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1R3N_H      129 VLAGLEVLRTFKDNNYVPNYDVCVVVWFNEEgarfarscTGsSVWSHDLSLEEAYGlmsvgedkpesvydslknigyigd 208
Cdd:cd03885 102 LVVILHALKALKAAGGRDYLPITVLLNSDEE--------IG-SPGSRELIEEEAKG------------------------ 148

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1R3N_H      209 tpasykeneidAHFELHIEqgPILEDENkaigIVT---GVQAYnwqKVTVHGVGAHAGTTPWRLRkDALLMSSKMIVAAS 285
Cdd:cd03885 149 -----------ADYVLVFE--PARADGN----LVTarkGIGRF---RLTVKGRAAHAGNAPEKGR-SAIYELAHQVLALH 207

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*....
1R3N_H      286 EIAQRHNGL-FTCGIIDAKPySVNIIPGEVSFTLDFRHPS----DDVLATMLKEAAAEF 339
Cdd:cd03885 208 ALTDPEKGTtVNVGVISGGT-RVNVVPDHAEAQVDVRFATaeeaDRVEEALRAIVATTL 265
M28 cd02690
M28 Zn-peptidases include aminopeptidases and carboxypeptidases; Peptidase M28 family (also ...
 94-177 2.15e-04

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: 42.33  E-value: 2.15e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1R3N_H       94 NMFAVYPGKNGGKPT-ATGSHLDTQPEA-GKYDGILGVLAGLEVLRTFKDNNYVPNYDVcVVVWFNEEGarfaRSCTGSS 171
Cdd:cd02690   3 NVIATIKGSDKPDEViLIGAHYDSVPLSpGANDNASGVAVLLELARVLSKLQLKPKRSI-RFAFWDAEE----LGLLGSK 77


                ....*.
1R3N_H      172 VWSHDL 177
Cdd:cd02690  78 YYAEQL 83
M20_dimer pfam07687
Peptidase dimerization domain; This domain consists of 4 beta strands and two alpha helices ...
 252-342 5.05e-04

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: 39.64  E-value: 5.05e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1R3N_H        252 KVTVHGVGAHAGTtPWRLRkDALLMSSKMIVAASEIAQRHNGL-----FTCGIIDAKpYSVNIIPGEVSFTLDFRHPSDD 326
Cdd:pfam07687  10 HLTVKGKAGHSGA-PGKGV-NAIKLLARLLAELPAEYGDIGFDfprttLNITGIEGG-TATNVIPAEAEAKFDIRLLPGE 86

                          90
                  ....*....|....*.
1R3N_H        327 VLATMLKEAAAEFDRL 342
Cdd:pfam07687  87 DLEELLEEIEAILEKE 102
FrvX COG1363
Putative aminopeptidase FrvX [Amino acid transport and metabolism, Carbohydrate transport and ...
 71-116 5.32e-04

Putative aminopeptidase FrvX [Amino acid transport and metabolism, Carbohydrate transport and metabolism];


Pssm-ID: 440974 [Multi-domain]  Cd Length: 353  Bit Score: 42.04  E-value: 5.32e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*.
1R3N_H       71 AMRDWFTNECESLGCKVKVDKIGNMFAVYPGKNGGKPTATGSHLDT 116
Cdd:COG1363  23 EVREYIKEELEPLGDEVETDRLGNLIATKKGKGDGPKVMLAAHMDE 68
M20_Acy1_YhaA-like cd08021
M20 Peptidase aminoacylase 1 subfamily, includes Bacillus subtilis YhaA and Staphylococcus ...
 252-445 8.18e-04

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: 41.49  E-value: 8.18e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1R3N_H      252 KVTVHGVGAHAGtTPwRLRKDALLMSSKMIVAASEIAQRH-----NGLFTCGIIDAKpYSVNIIPGEVSFTLDFRHPSDD 326
Cdd:cd08021 185 DITIKGKGGHGS-MP-HETVDPIVIAAQIVTALQTIVSRRvdpldPAVVTIGTFQGG-TSFNVIPDTVELKGTVRTFDEE 261

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1R3N_H      327 VLATMLKeaaaEFDRLIK-IndggalsyeSETLQVSPAVNFHEVCIECVSRSAFAQFKKDQVRQIWSGAGHDSCQTAP-- 403
Cdd:cd08021 262 VREQVPK----RIERIVKgI---------CEAYGASYELEYQPGYPVVYNDPEVTELVKKAAKEVLIGVENVEPQLMMgg 328

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
1R3N_H      404 --------HVPTSMIFI----PSKDGLSHNYYEYSSPEE--IENGFKVLLQAIINY 445
Cdd:cd08021 329 edfsyylkEVPGCFFFLgagnEEKGCIYPHHSPKFDIDEsaLKIGVKVHVGAVLEL 384
PRK07522 PRK07522
acetylornithine deacetylase; Provisional
 244-350 8.77e-04

acetylornithine deacetylase; Provisional


Pssm-ID: 236039 [Multi-domain]  Cd Length: 385  Bit Score: 41.33  E-value: 8.77e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1R3N_H       244 GVQAYnwqKVTVHGVGAHAGTTPWRLrkDALLMSSKMIVAASEIAQR------HNGLFTcgiidaKPYS----------- 306
Cdd:PRK07522 176 GKAAY---RCTVRGRAAHSSLAPQGV--NAIEYAARLIAHLRDLADRlaapgpFDALFD------PPYStlqtgtiqggt 244

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
1R3N_H       307 -VNIIPGEVSFTLDFRHPS----DDVLATMLKEAAAEFDRLIKINDGGA 350
Cdd:PRK07522 245 aLNIVPAECEFDFEFRNLPgddpEAILARIRAYAEAELLPEMRAVHPEA 293
Peptidase_M28 pfam04389
Peptidase family M28;
94-163 5.59e-03

Peptidase family M28;


Pssm-ID: 461288 [Multi-domain]  Cd Length: 192  Bit Score: 38.04  E-value: 5.59e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
1R3N_H         94 NMFAVYPGKNGGKPTATGSHLDTQPEA-GKYDGILGVLAGLEVLRTFKdNNYVPNYDVcVVVWFN-EE----GARF 163
Cdd:pfam04389   1 NVIAKLPGKAPDEVVLLSAHYDSVGTGpGADDNASGVAALLELARVLA-AGQRPKRSV-RFLFFDaEEagllGSHH 74
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH