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Conserved domains on  [gi|446998570|ref|WP_001075826|]
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MULTISPECIES: M20 family metallopeptidase [Staphylococcus]

Protein Classification

M20 family metallopeptidase( domain architecture ID 10168799)

M20 family metallopeptidase functions as an amidohydrolase, catalyzing the hydrolysis of amide bonds in target substrates

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
M20_Acy1_YhaA-like cd08021
M20 Peptidase aminoacylase 1 subfamily, includes Bacillus subtilis YhaA and Staphylococcus ...
5-388 0e+00

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: 599.26  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446998570   5 LIETLKSKEGKMIEIRRYLHQHPELSFHEDETAKYIAEFYKGKDVEVETNVGPRGIKVTIDSGKPGKTLAIRADFDALPI 84
Cdd:cd08021    1 LEELVDQLEDEMIQWRRHIHQYPELSFEEFETAAYIANELKKLGLEVETNVGGTGVVATLKGGKPGKTVALRADMDALPI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446998570  85 TEDTGLSFASQNKGVMHACGHDAHTAYMLVLAETLAEMKDSFTGKVVVIHQPAEEVPPGGAKTMIENGVLDGVDHVLGVH 164
Cdd:cd08021   81 EEETDLPFKSKNPGVMHACGHDGHTAMLLGAAKVLAENKDEIKGTVRFIFQPAEEVPPGGAKPMIEAGVLEGVDAVFGLH 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446998570 165 VMSTMKTGKVYYRPGYVQTGRAFFKLKVQGKGGHGSSPHMANDAIVAGSYFVTALQTVVSRRLSPFETGVVTIGSFDGKG 244
Cdd:cd08021  161 LWSTLPTGTIAVRPGAIMAAPDEFDITIKGKGGHGSMPHETVDPIVIAAQIVTALQTIVSRRVDPLDPAVVTIGTFQGGT 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446998570 245 QFNVIKDVVEIEGDVRGLTDATKATIEKEIKRLSKGLEDMYGVTCTLEYNDDYPALYNDPEFTEYVAKTLKEANldFGVE 324
Cdd:cd08021  241 SFNVIPDTVELKGTVRTFDEEVREQVPKRIERIVKGICEAYGASYELEYQPGYPVVYNDPEVTELVKKAAKEVL--IGVE 318
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446998570 325 MCEPQP--PSEDFAYYAKERPSAFIYTGAAVE-NGEIYPHHHPKFNISEKSLLIsAEAVGTVVLDYL 388
Cdd:cd08021  319 NVEPQLmmGGEDFSYYLKEVPGCFFFLGAGNEeKGCIYPHHSPKFDIDESALKI-GVKVHVGAVLEL 384
 
Name Accession Description Interval E-value
M20_Acy1_YhaA-like cd08021
M20 Peptidase aminoacylase 1 subfamily, includes Bacillus subtilis YhaA and Staphylococcus ...
5-388 0e+00

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: 599.26  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446998570   5 LIETLKSKEGKMIEIRRYLHQHPELSFHEDETAKYIAEFYKGKDVEVETNVGPRGIKVTIDSGKPGKTLAIRADFDALPI 84
Cdd:cd08021    1 LEELVDQLEDEMIQWRRHIHQYPELSFEEFETAAYIANELKKLGLEVETNVGGTGVVATLKGGKPGKTVALRADMDALPI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446998570  85 TEDTGLSFASQNKGVMHACGHDAHTAYMLVLAETLAEMKDSFTGKVVVIHQPAEEVPPGGAKTMIENGVLDGVDHVLGVH 164
Cdd:cd08021   81 EEETDLPFKSKNPGVMHACGHDGHTAMLLGAAKVLAENKDEIKGTVRFIFQPAEEVPPGGAKPMIEAGVLEGVDAVFGLH 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446998570 165 VMSTMKTGKVYYRPGYVQTGRAFFKLKVQGKGGHGSSPHMANDAIVAGSYFVTALQTVVSRRLSPFETGVVTIGSFDGKG 244
Cdd:cd08021  161 LWSTLPTGTIAVRPGAIMAAPDEFDITIKGKGGHGSMPHETVDPIVIAAQIVTALQTIVSRRVDPLDPAVVTIGTFQGGT 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446998570 245 QFNVIKDVVEIEGDVRGLTDATKATIEKEIKRLSKGLEDMYGVTCTLEYNDDYPALYNDPEFTEYVAKTLKEANldFGVE 324
Cdd:cd08021  241 SFNVIPDTVELKGTVRTFDEEVREQVPKRIERIVKGICEAYGASYELEYQPGYPVVYNDPEVTELVKKAAKEVL--IGVE 318
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446998570 325 MCEPQP--PSEDFAYYAKERPSAFIYTGAAVE-NGEIYPHHHPKFNISEKSLLIsAEAVGTVVLDYL 388
Cdd:cd08021  319 NVEPQLmmGGEDFSYYLKEVPGCFFFLGAGNEeKGCIYPHHSPKFDIDESALKI-GVKVHVGAVLEL 384
AbgB COG1473
Metal-dependent amidase/aminoacylase/carboxypeptidase [General function prediction only]; ...
4-389 1.87e-179

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: 503.88  E-value: 1.87e-179
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446998570   4 QLIETLKSKEGKMIEIRRYLHQHPELSFHEDETAKYIAEFYKGKDVEVETNVGPRGIKVTIDSGKPGKTLAIRADFDALP 83
Cdd:COG1473    1 KILALIDALAPELIALRRDLHAHPELSFEEFRTAAYVAEELRELGIEVTTGVGGTGVVAVLKGGKPGPTIALRADMDALP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446998570  84 ITEDTGLSFASQNKGVMHACGHDAHTAYMLVLAETLAEMKDSFTGKVVVIHQPAEEvPPGGAKTMIENGVLD--GVDHVL 161
Cdd:COG1473   81 IQEQTGLPYASKNPGVMHACGHDGHTAMLLGAAKALAELRDELKGTVRLIFQPAEE-GGGGAKAMIEDGLLDrpDVDAIF 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446998570 162 GVHVMSTMKTGKVYYRPGYVQTGRAFFKLKVQGKGGHGSSPHMANDAIVAGSYFVTALQTVVSRRLSPFETGVVTIGSFD 241
Cdd:COG1473  160 GLHVWPGLPVGTIGVRPGPIMAAADSFEITIKGKGGHAAAPHLGIDPIVAAAQIVTALQTIVSRNVDPLDPAVVTVGIIH 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446998570 242 GKGQFNVIKDVVEIEGDVRGLTDATKATIEKEIKRLSKGLEDMYGVTCTLEYNDDYPALYNDPEFTEYVAKTLKEANLDF 321
Cdd:COG1473  240 GGTAPNVIPDEAELEGTVRTFDPEVRELLEERIERIAEGIAAAYGATAEVEYLRGYPPTVNDPELTELAREAAREVLGEE 319
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446998570 322 GVEMCEPQPPSEDFAYYAKERPSAFIYTGAAVEnGEIYPHHHPKFNISEKSLLISAEAVGTVVLDYLK 389
Cdd:COG1473  320 NVVDAEPSMGSEDFAYYLQKVPGAFFFLGAGNP-GTVPPLHSPKFDFDEKALPIGAKALAALALDLLA 386
amidohydrolases TIGR01891
amidohydrolase; This model represents a subfamily of amidohydrolases which are a subset of ...
16-375 2.89e-126

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: 368.21  E-value: 2.89e-126
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446998570   16 MIEIRRYLHQHPELSFHEDETAKYIAEFYKGKDVEVETNV-GPRGIKVTIDSGKPGKTLAIRADFDALPITEDTGLSFAS 94
Cdd:TIGR01891   1 LTDIRRHLHEHPELSFEEFKTSSLIAEALESLGIEVRRGVgGATGVVATIGGGKPGPVVALRADMDALPIQEQTDLPYKS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446998570   95 QNKGVMHACGHDAHTAYMLVLAETLAEMKDSFTGKVVVIHQPAEEVPpGGAKTMIENGVLDGVDHVLGVHVMSTMKTGKV 174
Cdd:TIGR01891  81 TNPGVMHACGHDLHTAILLGTAKLLKKLADLLEGTVRLIFQPAEEGG-GGATKMIEDGVLDDVDAILGLHPDPSIPAGTV 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446998570  175 YYRPGYVQTGRAFFKLKVQGKGGHGSSPHMANDAIVAGSYFVTALQTVVSRRLSPFETGVVTIGSFDGKGQFNVIKDVVE 254
Cdd:TIGR01891 160 GLRPGTIMAAADKFEVTIHGKGAHAARPHLGRDALDAAAQLVVALQQIVSRNVDPSRPAVVSVGIIEAGGAPNVIPDKAS 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446998570  255 IEGDVRGLTDATKATIEKEIKRLSKGLEDMYGVTCTLEYNDDYPALYNDPEFTEYVAKTLKEANLDFGVeMCEPQPP--S 332
Cdd:TIGR01891 240 MSGTVRSLDPEVRDQIIDRIERIVEGAAAMYGAKVELNYDRGLPAVTNDPALTQILKEVARHVVGPENV-AEDPEVTmgS 318
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....
gi 446998570  333 EDFAYYAKERPSAFIYTGAAVE-NGEIYPHHHPKFNISEKSLLI 375
Cdd:TIGR01891 319 EDFAYYSQKVPGAFFFLGIGNEgTGLSHPLHHPRFDIDEEALAL 362
carboxypep_CpsA NF040868
carboxypeptidase CpsA;
3-389 1.61e-114

carboxypeptidase CpsA;


Pssm-ID: 468805 [Multi-domain]  Cd Length: 391  Bit Score: 339.40  E-value: 1.61e-114
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446998570   3 QQLIETLKSKEGKMIEIRRYLHQHPELSFHEDETAKYIAEFYKGKDVEVETNVG-PRGIKVTIDSGKPGKTLAIRADFDA 81
Cdd:NF040868   2 EKILKEAKEIEDKIIEIRRKIHENPELSYQEYRTAKLVAETLRSLGIEVREGVGlPTAVVGILRGKKKGKTVALRADMDA 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446998570  82 LPITEDTGLSFASQNKGVMHACGHDAHTAYMLVLAETLAEMKDSFTGKVVVIHQPAEEVPP-GGAKTMIENGVLDGVDHV 160
Cdd:NF040868  82 LPVQEETDLPFKSKVPGVMHACGHDAHVAMLLGAAYILSKHKDELSGEVRLIFQPAEEDGGrGGAKPMIEAGVMEGVDYV 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446998570 161 LGVHVMSTMKTGKVYYRPGYVQTGRAFFKLKVQGKGGHGSSPHMANDAIVAGSYFVTALQTVVSRRLSPFETGVVTIGSF 240
Cdd:NF040868 162 FGLHVSSSYPSGVFATRKGPLMAAPDSFKVEVHGKGGHGSAPHETIDPIFISAQIVNALQGIRSRQIDPLQPFVLSVTSI 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446998570 241 DGKGQFNVIKDVVEIEGDVRGLTDATKATIEKEIKRLSKGLEDMYGVTCTLEYNDD-YPALYNDPEFTEYVAKTLKEANl 319
Cdd:NF040868 242 HSGTKDNIIPDEAVMEGTIRTLDEDVREKALEYMRNIVESICEAYGAECKVEFKEDaYPVTVNDPETTKEVMDILSEIP- 320
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446998570 320 dfGVEMCEPQP--PSEDFAYYAKERPSAFIYTGAAVEN-GEIYPHHHPKFNISEKSLLISAEAVGTVVLDYLK 389
Cdd:NF040868 321 --GVKVVETDPvlGAEDFSRFLQKAPGTFIFLGTRNEKkGIIYPNHSSKFTVDEDVLKLGAAALALLAMKFSR 391
Peptidase_M20 pfam01546
Peptidase family M20/M25/M40; This family includes a range of zinc metallopeptidases belonging ...
74-386 8.25e-84

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: 258.05  E-value: 8.25e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446998570   74 AIRADFDALPITEDTGLSFASQNKGVMHACGHDAHTAYMLVLAETLAEMKDSF--TGKVVVIHQPAEEVPPGGAKTMIEN 151
Cdd:pfam01546   1 LLRGHMDVVPDEETWGWPFKSTEDGKLYGRGHDDMKGGLLAALEALRALKEEGlkKGTVKLLFQPDEEGGMGGARALIED 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446998570  152 GVLDG--VDHVLGVHVM-STMKTGKVYYRPGYVQTGRAFFKLKVQGKGGHGSSPHMANDAIVAGSYFVTALQTVVSRRLS 228
Cdd:pfam01546  81 GLLERekVDAVFGLHIGePTLLEGGIAIGVVTGHRGSLRFRVTVKGKGGHASTPHLGVNAIVAAARLILALQDIVSRNVD 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446998570  229 PFETGVVTIGSFDG-KGQFNVIKDVVEIEGDVRGLTDATKATIEKEIKRLSKGLEDMYGVTCTLEYNDD-YPALYNDPEF 306
Cdd:pfam01546 161 PLDPAVVTVGNITGiPGGVNVIPGEAELKGDIRLLPGEDLEELEERIREILEAIAAAYGVKVEVEYVEGgAPPLVNDSPL 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446998570  307 TEYVAKTLKEANLDFGVEMCEPQPPSEDFAYYAKERPSAFIYTGAaveNGEIYPHHHPKFniSEKSLLISAEAVGTVVLD 386
Cdd:pfam01546 241 VAALREAAKELFGLKVELIVSGSMGGTDAAFFLLGVPPTVVFFGP---GSGLAHSPNEYV--DLDDLEKGAKVLARLLLK 315
PLN02280 PLN02280
IAA-amino acid hydrolase
19-388 1.33e-66

IAA-amino acid hydrolase


Pssm-ID: 215158 [Multi-domain]  Cd Length: 478  Bit Score: 218.68  E-value: 1.33e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446998570  19 IRRYLHQHPELSFHEDETAKYIAEFYKGKDVEVETNVGPRGIKVTIDSGKPgKTLAIRADFDALPITEDTGLSFASQNKG 98
Cdd:PLN02280 102 VRRKIHENPELAFEEYKTSELVRSELDRMGIMYRYPLAKTGIRAWIGTGGP-PFVAVRADMDALPIQEAVEWEHKSKVAG 180
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446998570  99 VMHACGHDAHTAYMLVLAETLAEMKDSFTGKVVVIHQPAEEVPpGGAKTMIENGVLDGVDHVLGVHVMSTMKTGKVYYRP 178
Cdd:PLN02280 181 KMHACGHDAHVAMLLGAAKILKSREHLLKGTVVLLFQPAEEAG-NGAKRMIGDGALDDVEAIFAVHVSHEHPTAVIGSRP 259
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446998570 179 GYVQTGRAFFKLKVQGKGGHGSSPHMANDAIVAGSYFVTALQTVVSRRLSPFETGVVTIGSFDGKGQFNVIKDVVEIEGD 258
Cdd:PLN02280 260 GPLLAGCGFFRAVISGKKGRAGSPHHSVDLILAASAAVISLQGIVSREANPLDSQVVSVTTMDGGNNLDMIPDTVVLGGT 339
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446998570 259 VRGLTDATKATIEKEIKRLSKGLEDMYGVTCTLEY----NDDYPALYNDPEFTEYVAKTLKEANLDFGVEMCEPQPPSED 334
Cdd:PLN02280 340 FRAFSNTSFYQLLKRIQEVIVEQAGVFRCSATVDFfekqNTIYPPTVNNDAMYEHVRKVAIDLLGPANFTVVPPMMGAED 419
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 446998570 335 FAYYAKERPSAFIYTGAAVEN-GEIYPHHHPKFNISEKSLLISAEAVGTVVLDYL 388
Cdd:PLN02280 420 FSFYSQVVPAAFYYIGIRNETlGSTHTGHSPYFMIDEDVLPIGAAVHAAIAERYL 474
 
Name Accession Description Interval E-value
M20_Acy1_YhaA-like cd08021
M20 Peptidase aminoacylase 1 subfamily, includes Bacillus subtilis YhaA and Staphylococcus ...
5-388 0e+00

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: 599.26  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446998570   5 LIETLKSKEGKMIEIRRYLHQHPELSFHEDETAKYIAEFYKGKDVEVETNVGPRGIKVTIDSGKPGKTLAIRADFDALPI 84
Cdd:cd08021    1 LEELVDQLEDEMIQWRRHIHQYPELSFEEFETAAYIANELKKLGLEVETNVGGTGVVATLKGGKPGKTVALRADMDALPI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446998570  85 TEDTGLSFASQNKGVMHACGHDAHTAYMLVLAETLAEMKDSFTGKVVVIHQPAEEVPPGGAKTMIENGVLDGVDHVLGVH 164
Cdd:cd08021   81 EEETDLPFKSKNPGVMHACGHDGHTAMLLGAAKVLAENKDEIKGTVRFIFQPAEEVPPGGAKPMIEAGVLEGVDAVFGLH 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446998570 165 VMSTMKTGKVYYRPGYVQTGRAFFKLKVQGKGGHGSSPHMANDAIVAGSYFVTALQTVVSRRLSPFETGVVTIGSFDGKG 244
Cdd:cd08021  161 LWSTLPTGTIAVRPGAIMAAPDEFDITIKGKGGHGSMPHETVDPIVIAAQIVTALQTIVSRRVDPLDPAVVTIGTFQGGT 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446998570 245 QFNVIKDVVEIEGDVRGLTDATKATIEKEIKRLSKGLEDMYGVTCTLEYNDDYPALYNDPEFTEYVAKTLKEANldFGVE 324
Cdd:cd08021  241 SFNVIPDTVELKGTVRTFDEEVREQVPKRIERIVKGICEAYGASYELEYQPGYPVVYNDPEVTELVKKAAKEVL--IGVE 318
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446998570 325 MCEPQP--PSEDFAYYAKERPSAFIYTGAAVE-NGEIYPHHHPKFNISEKSLLIsAEAVGTVVLDYL 388
Cdd:cd08021  319 NVEPQLmmGGEDFSYYLKEVPGCFFFLGAGNEeKGCIYPHHSPKFDIDESALKI-GVKVHVGAVLEL 384
M20_Acy1 cd03886
M20 Peptidase Aminoacylase 1 family; Peptidase M20 family, Aminoacylase 1 (ACY1; hippuricase; ...
16-385 0e+00

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: 509.06  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446998570  16 MIEIRRYLHQHPELSFHEDETAKYIAEFYKGKDVEVETNVGPRGIKVTIDSGKPGKTLAIRADFDALPITEDTGLSFASQ 95
Cdd:cd03886    1 LIALRRDLHQHPELSFEEFRTAARIAEELRELGLEVRTGVGGTGVVATLKGGGPGPTVALRADMDALPIQEETGLPFASK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446998570  96 NKGVMHACGHDAHTAYMLVLAETLAEMKDSFTGKVVVIHQPAEEVPpGGAKTMIENGVLD--GVDHVLGVHVMSTMKTGK 173
Cdd:cd03886   81 HEGVMHACGHDGHTAMLLGAAKLLAERRDPLKGTVRFIFQPAEEGP-GGAKAMIEEGVLEnpGVDAAFGLHVWPGLPVGT 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446998570 174 VYYRPGYVQTGRAFFKLKVQGKGGHGSSPHMANDAIVAGSYFVTALQTVVSRRLSPFETGVVTIGSFDGKGQFNVIKDVV 253
Cdd:cd03886  160 VGVRSGALMASADEFEITVKGKGGHGASPHLGVDPIVAAAQIVLALQTVVSRELDPLEPAVVTVGKFHAGTAFNVIPDTA 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446998570 254 EIEGDVRGLTDATKATIEKEIKRLSKGLEDMYGVTCTLEYNDDYPALYNDPEFTEYVAKTLKEANLDFGVEMCEPQPPSE 333
Cdd:cd03886  240 VLEGTIRTFDPEVREALEARIKRLAEGIAAAYGATVELEYGYGYPAVINDPELTELVREAAKELLGEEAVVEPEPVMGSE 319
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|..
gi 446998570 334 DFAYYAKERPSAFIYTGAAVENGEIYPHHHPKFNISEKSLLISAEAVGTVVL 385
Cdd:cd03886  320 DFAYYLEKVPGAFFWLGAGEPDGENPGLHSPTFDFDEDALPIGAALLAELAL 371
AbgB COG1473
Metal-dependent amidase/aminoacylase/carboxypeptidase [General function prediction only]; ...
4-389 1.87e-179

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: 503.88  E-value: 1.87e-179
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446998570   4 QLIETLKSKEGKMIEIRRYLHQHPELSFHEDETAKYIAEFYKGKDVEVETNVGPRGIKVTIDSGKPGKTLAIRADFDALP 83
Cdd:COG1473    1 KILALIDALAPELIALRRDLHAHPELSFEEFRTAAYVAEELRELGIEVTTGVGGTGVVAVLKGGKPGPTIALRADMDALP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446998570  84 ITEDTGLSFASQNKGVMHACGHDAHTAYMLVLAETLAEMKDSFTGKVVVIHQPAEEvPPGGAKTMIENGVLD--GVDHVL 161
Cdd:COG1473   81 IQEQTGLPYASKNPGVMHACGHDGHTAMLLGAAKALAELRDELKGTVRLIFQPAEE-GGGGAKAMIEDGLLDrpDVDAIF 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446998570 162 GVHVMSTMKTGKVYYRPGYVQTGRAFFKLKVQGKGGHGSSPHMANDAIVAGSYFVTALQTVVSRRLSPFETGVVTIGSFD 241
Cdd:COG1473  160 GLHVWPGLPVGTIGVRPGPIMAAADSFEITIKGKGGHAAAPHLGIDPIVAAAQIVTALQTIVSRNVDPLDPAVVTVGIIH 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446998570 242 GKGQFNVIKDVVEIEGDVRGLTDATKATIEKEIKRLSKGLEDMYGVTCTLEYNDDYPALYNDPEFTEYVAKTLKEANLDF 321
Cdd:COG1473  240 GGTAPNVIPDEAELEGTVRTFDPEVRELLEERIERIAEGIAAAYGATAEVEYLRGYPPTVNDPELTELAREAAREVLGEE 319
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446998570 322 GVEMCEPQPPSEDFAYYAKERPSAFIYTGAAVEnGEIYPHHHPKFNISEKSLLISAEAVGTVVLDYLK 389
Cdd:COG1473  320 NVVDAEPSMGSEDFAYYLQKVPGAFFFLGAGNP-GTVPPLHSPKFDFDEKALPIGAKALAALALDLLA 386
amidohydrolases TIGR01891
amidohydrolase; This model represents a subfamily of amidohydrolases which are a subset of ...
16-375 2.89e-126

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: 368.21  E-value: 2.89e-126
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446998570   16 MIEIRRYLHQHPELSFHEDETAKYIAEFYKGKDVEVETNV-GPRGIKVTIDSGKPGKTLAIRADFDALPITEDTGLSFAS 94
Cdd:TIGR01891   1 LTDIRRHLHEHPELSFEEFKTSSLIAEALESLGIEVRRGVgGATGVVATIGGGKPGPVVALRADMDALPIQEQTDLPYKS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446998570   95 QNKGVMHACGHDAHTAYMLVLAETLAEMKDSFTGKVVVIHQPAEEVPpGGAKTMIENGVLDGVDHVLGVHVMSTMKTGKV 174
Cdd:TIGR01891  81 TNPGVMHACGHDLHTAILLGTAKLLKKLADLLEGTVRLIFQPAEEGG-GGATKMIEDGVLDDVDAILGLHPDPSIPAGTV 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446998570  175 YYRPGYVQTGRAFFKLKVQGKGGHGSSPHMANDAIVAGSYFVTALQTVVSRRLSPFETGVVTIGSFDGKGQFNVIKDVVE 254
Cdd:TIGR01891 160 GLRPGTIMAAADKFEVTIHGKGAHAARPHLGRDALDAAAQLVVALQQIVSRNVDPSRPAVVSVGIIEAGGAPNVIPDKAS 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446998570  255 IEGDVRGLTDATKATIEKEIKRLSKGLEDMYGVTCTLEYNDDYPALYNDPEFTEYVAKTLKEANLDFGVeMCEPQPP--S 332
Cdd:TIGR01891 240 MSGTVRSLDPEVRDQIIDRIERIVEGAAAMYGAKVELNYDRGLPAVTNDPALTQILKEVARHVVGPENV-AEDPEVTmgS 318
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....
gi 446998570  333 EDFAYYAKERPSAFIYTGAAVE-NGEIYPHHHPKFNISEKSLLI 375
Cdd:TIGR01891 319 EDFAYYSQKVPGAFFFLGIGNEgTGLSHPLHHPRFDIDEEALAL 362
M20_Acy1-like cd08019
M20 Peptidase aminoacylase 1 subfamily; Peptidase M20 family, uncharacterized subfamily of ...
16-388 1.95e-123

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: 361.27  E-value: 1.95e-123
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446998570  16 MIEIRRYLHQHPELSFHEDETAKYIAEFYKGKDVEVEtNVGPRGIKVTIDSGKPGKTLAIRADFDALPITEDTGLSFASQ 95
Cdd:cd08019    1 IIELRRYFHMHPELSLKEERTSKRIKEELDKLGIPYV-ETGGTGVIATIKGGKAGKTVALRADIDALPVEECTDLEYKSK 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446998570  96 NKGVMHACGHDAHTAYMLVLAETLAEMKDSFTGKVVVIHQPAEEVPpGGAKTMIENGVLDGVDHVLGVHVMSTMKTGKVY 175
Cdd:cd08019   80 NPGLMHACGHDGHTAMLLGAAKILNEIKDTIKGTVKLIFQPAEEVG-EGAKQMIEEGVLEDVDAVFGIHLWSDVPAGKIS 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446998570 176 YRPGYVQTGRAFFKLKVQGKGGHGSSPHMANDAIVAGSYFVTALQTVVSRRLSPFETGVVTIGSFDGKGQFNVIKDVVEI 255
Cdd:cd08019  159 VEAGPRMASADIFKIEVKGKGGHGSMPHQGIDAVLAAASIVMNLQSIVSREIDPLEPVVVTVGKLNSGTRFNVIADEAKI 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446998570 256 EGDVRGLTDATKATIEKEIKRLSKGLEDMYGVTCTLEYNDDYPALYNDPEFTEYVAKTlkeANLDFGVEMCEPQPP---S 332
Cdd:cd08019  239 EGTLRTFNPETREKTPEIIERIAKHTAASYGAEAELTYGAATPPVINDEKLSKIARQA---AIKIFGEDSLTEFEKttgS 315
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 446998570 333 EDFAYYAKERPSAFIYTGAA-VENGEIYPHHHPKFNISEKSLLISAEAVGTVVLDYL 388
Cdd:cd08019  316 EDFSYYLEEVPGVFAFVGSRnEEKGATYPHHHEFFNIDEDALKLGAALYVQFALDFL 372
M20_Acy1-like cd05666
M20 Peptidase aminoacylase 1 subfamily; Peptidase M20 family, uncharacterized subfamily of ...
16-377 5.41e-123

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: 360.30  E-value: 5.41e-123
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446998570  16 MIEIRRYLHQHPELSFHEDETAKYIAEFYKGKDVEVETNVGPRGIKVTIDSGKPGKTLAIRADFDALPITEDTGLSFASQ 95
Cdd:cd05666    3 LTAWRRDLHAHPELGFEEHRTSALVAEKLREWGIEVHRGIGGTGVVGVLRGGDGGRAIGLRADMDALPIQEATGLPYAST 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446998570  96 NKGVMHACGHDAHTAYMLVLAETLAEMKDsFTGKVVVIHQPAEEvPPGGAKTMIENGVLD--GVDHVLGVHVMSTMKTGK 173
Cdd:cd05666   83 HPGKMHACGHDGHTTMLLGAARYLAETRN-FDGTVHFIFQPAEE-GGGGAKAMIEDGLFErfPCDAVYGLHNMPGLPAGK 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446998570 174 VYYRPGYVQTGRAFFKLKVQGKGGHGSSPHMANDAIVAGSYFVTALQTVVSRRLSPFETGVVTIGSFDGKGQFNVIKDVV 253
Cdd:cd05666  161 FAVRPGPMMASADTFEITIRGKGGHAAMPHLGVDPIVAAAQLVQALQTIVSRNVDPLDAAVVSVTQIHAGDAYNVIPDTA 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446998570 254 EIEGDVRGLTDATKATIEKEIKRLSKGLEDMYGVTCTLEYNDDYPALYNDPEFTEYVAKTLKEAnldFGVEMCEPQPP-- 331
Cdd:cd05666  241 ELRGTVRAFDPEVRDLIEERIREIADGIAAAYGATAEVDYRRGYPVTVNDAEETAFAAEVAREV---VGAENVDTDVRps 317
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*...
gi 446998570 332 --SEDFAYYAKERPSAFIYTGAAVENGEIyPHHHPKFNISEKSLLISA 377
Cdd:cd05666  318 mgSEDFAFMLEARPGAYVFLGNGDGEGGC-PLHNPGYDFNDAILPIGA 364
M20_Acy1-like cd08014
M20 Peptidase aminoacylase 1 subfamily; Peptidase M20 family, uncharacterized subfamily of ...
16-388 3.28e-117

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: 345.41  E-value: 3.28e-117
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446998570  16 MIEIRRYLHQHPELSFHEDETAKYIAEFYKGKDVEVETNVGPRGIKVTIDSGKPGKTLAIRADFDALPITEDTGLSFASQ 95
Cdd:cd08014    1 LVEWRRHLHAHPELSGQEYRTTAFVAERLRDLGLKPKEFPGGTGLVCDIGGKRDGRTVALRADMDALPIQEQTGLPYRST 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446998570  96 NKGVMHACGHDAHTAYMLVLAETLAEMKDSFTGKVVVIHQPAEEVPPGGAKTMIENGVLDGVDHVLGVHVMSTMKTGKVY 175
Cdd:cd08014   81 VPGVMHACGHDAHTAIALGAALVLAALEEELPGRVRLIFQPAEETMPGGALDMIRAGALDGVSAIFALHVDPRLPVGRVG 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446998570 176 YRPGYVQTGRAFFKLKVQGKGGHGSSPHMANDAIVAGSYFVTALQTVVSRRLSPFETGVVTIGSFDGKGQFNVIKDVVEI 255
Cdd:cd08014  161 VRYGPITAAADSLEIRIQGEGGHGARPHLTVDLVWAAAQVVTDLPQAISRRIDPRSPVVLTWGSIEGGRAPNVIPDSVEL 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446998570 256 EGDVRGLTDATKATIEKEIKRLSKGLEDMYGVTCTLEYNDDYPALYNDPEFTEYVAKTLKEA-NLDFGVEMCEPQPPSED 334
Cdd:cd08014  241 SGTVRTLDPDTWAQLPDLVEEIVAGICAPYGAKYELEYRRGVPPVINDPASTALLEAAVREIlGEDNVVALAEPSMGGED 320
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....
gi 446998570 335 FAYYAKERPSAFIYTGAAVENGEIYPHHHPKFNISEkslliSAEAVGTVVLDYL 388
Cdd:cd08014  321 FAWYLEHVPGAMARLGVWGGDGTSYPLHHPDFDVDE-----RAIAIGVRVLAAA 369
carboxypep_CpsA NF040868
carboxypeptidase CpsA;
3-389 1.61e-114

carboxypeptidase CpsA;


Pssm-ID: 468805 [Multi-domain]  Cd Length: 391  Bit Score: 339.40  E-value: 1.61e-114
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446998570   3 QQLIETLKSKEGKMIEIRRYLHQHPELSFHEDETAKYIAEFYKGKDVEVETNVG-PRGIKVTIDSGKPGKTLAIRADFDA 81
Cdd:NF040868   2 EKILKEAKEIEDKIIEIRRKIHENPELSYQEYRTAKLVAETLRSLGIEVREGVGlPTAVVGILRGKKKGKTVALRADMDA 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446998570  82 LPITEDTGLSFASQNKGVMHACGHDAHTAYMLVLAETLAEMKDSFTGKVVVIHQPAEEVPP-GGAKTMIENGVLDGVDHV 160
Cdd:NF040868  82 LPVQEETDLPFKSKVPGVMHACGHDAHVAMLLGAAYILSKHKDELSGEVRLIFQPAEEDGGrGGAKPMIEAGVMEGVDYV 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446998570 161 LGVHVMSTMKTGKVYYRPGYVQTGRAFFKLKVQGKGGHGSSPHMANDAIVAGSYFVTALQTVVSRRLSPFETGVVTIGSF 240
Cdd:NF040868 162 FGLHVSSSYPSGVFATRKGPLMAAPDSFKVEVHGKGGHGSAPHETIDPIFISAQIVNALQGIRSRQIDPLQPFVLSVTSI 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446998570 241 DGKGQFNVIKDVVEIEGDVRGLTDATKATIEKEIKRLSKGLEDMYGVTCTLEYNDD-YPALYNDPEFTEYVAKTLKEANl 319
Cdd:NF040868 242 HSGTKDNIIPDEAVMEGTIRTLDEDVREKALEYMRNIVESICEAYGAECKVEFKEDaYPVTVNDPETTKEVMDILSEIP- 320
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446998570 320 dfGVEMCEPQP--PSEDFAYYAKERPSAFIYTGAAVEN-GEIYPHHHPKFNISEKSLLISAEAVGTVVLDYLK 389
Cdd:NF040868 321 --GVKVVETDPvlGAEDFSRFLQKAPGTFIFLGTRNEKkGIIYPNHSSKFTVDEDVLKLGAAALALLAMKFSR 391
M20_Acy1_YxeP-like cd05669
M20 Peptidase aminoacyclase-1 YxeP-like proteins, including YxeP, YtnL, YjiB and HipO2; ...
15-378 2.08e-111

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: 330.80  E-value: 2.08e-111
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446998570  15 KMIEIRRYLHQHPELSFHEDETAKYIAEFYKGKDVEV-----ETnvgprGIKVTIDSGKPgkTLAIRADFDALPITEDTG 89
Cdd:cd05669    5 QLIEWRRYLHQHPELSNQEFETTKKIRRWLEEKGIRIldlplKT-----GVVAEIGGGGP--IIALRADIDALPIEEETG 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446998570  90 LSFASQNKGVMHACGHDAHTAYMLVLAETLAEMKDSFTGKVVVIHQPAEEVPpGGAKTMIENGVLDGVDHVLGVHVMSTM 169
Cdd:cd05669   78 LPYASQNKGVMHACGHDFHTASLLGAAVLLKEREAELKGTVRLIFQPAEETG-AGAKKVIEAGALDDVSAIFGFHNKPDL 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446998570 170 KTGKVYYRPGYVQTGRAFFKLKVQGKGGHGSSPHMANDAIVAGSYFVTALQTVVSRRLSPFETGVVTIGSFDGKGQFNVI 249
Cdd:cd05669  157 PVGTIGLKSGALMAAVDRFEIEIAGKGAHAAKPENGVDPIVAASQIINALQTIVSRNISPLESAVVSVTRIHAGNTWNVI 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446998570 250 KDVVEIEGDVRGLTDATKATIEKEIKRLSKGLEDMYGVTCTLEYNDDYPALYNDPEFTEYVAKTLKEANLDfgVEMCEPQ 329
Cdd:cd05669  237 PDSAELEGTVRTFDAEVRQLVKERFEQIVEGIAAAFGAKIEFKWHSGPPAVINDEELTDLASEVAAQAGYE--VVHAEPS 314
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*....
gi 446998570 330 PPSEDFAYYAKERPSAFIYTGAaveNGEiYPHHHPKFNISEKSLLISAE 378
Cdd:cd05669  315 LGGEDFAFYQQKIPGVFAFIGS---NGT-YELHHPAFNPDEEALPVAAD 359
M20_Acy1-like cd05667
M20 Peptidase aminoacylase 1 subfamily; Peptidase M20 family, uncharacterized subfamily of ...
7-388 2.44e-111

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: 331.70  E-value: 2.44e-111
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446998570   7 ETLKSKEGKMIEIRRYLHQHPELSFHEDETAKYIAEFYKGKDVEVETNVGPRGIKVTIDSGKPGKTLAIRADFDALPITE 86
Cdd:cd05667    3 AAIQQVEPKVIEWRRDFHQNPELSNREFRTAALIAKELKSLGIEVRTGIAKTGVVGILKGGKPGPVIALRADMDALPVEE 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446998570  87 DTGLSFASQNK--------GVMHACGHDAHTAYMLVLAETLAEMKDSFTGKVVVIHQPAEEVPP----GGAKTMIENGVL 154
Cdd:cd05667   83 KTGLPFASKVKttylgqtvGVMHACGHDAHVAILLGAAEVLAANKDKIKGTVMFIFQPAEEGPPegeeGGAKLMLKEGAF 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446998570 155 DG--VDHVLGVHVMSTMKTGKVYYRPGYVQTGRAFFKLKVQGKGGHGSSPHMANDAIVAGSYFVTALQTVVSRRLS-PFE 231
Cdd:cd05667  163 KDykPEAIFGLHVGSGLPSGQLGYRSGPIMASADRFRITVKGKQTHGSRPWDGIDPIMASAQIIQGLQTIISRRIDlTKE 242
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446998570 232 TGVVTIGSFDGKGQFNVIKDVVEIEGDVRGLTDATKATIEKEIKRLSKGLEDMYGVTCTLEYNDDYPALYNDPEFTEYVA 311
Cdd:cd05667  243 PAVISIGKINGGTRGNIIPEDAEMVGTIRTFDPEMREDIFARLKTIAEHIAKAYGATAEVEFANGYPVTYNDPALTAKML 322
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446998570 312 KTLKEA-NLDFGVEMCEPQPPSEDFAYYAKERPSAFIYTGAAVENGEI---YPHHHPKFNISEKSLLISAEAVGTVVLDY 387
Cdd:cd05667  323 PTLQKAvGKADLVVLPPTQTGAEDFSFYAEQVPGMFFFLGGTPAGQEPataPPNHSPYFIVDESALKTGVKAHIQLVLDY 402

                 .
gi 446998570 388 L 388
Cdd:cd05667  403 L 403
M20_IAA_Hyd cd08017
M20 Peptidase Indole-3-acetic acid amino acid hydrolase; Peptidase M20 family, plant ...
16-388 1.45e-109

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: 326.20  E-value: 1.45e-109
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446998570  16 MIEIRRYLHQHPELSFHEDETAKYIAEFYKGKDVEVETNVGPRGIKVTIDSGKPgKTLAIRADFDALPITEDTGLSFASQ 95
Cdd:cd08017    1 LVRVRREIHENPELAFQEHETSALIRRELDALGIPYRYPVAKTGIVATIGSGSP-PVVALRADMDALPIQELVEWEHKSK 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446998570  96 NKGVMHACGHDAHTAYMLVLAETLAEMKDSFTGKVVVIHQPAEEvPPGGAKTMIENGVLDGVDHVLGVHVMSTMKTGKVY 175
Cdd:cd08017   80 VDGKMHACGHDAHVAMLLGAAKLLKARKHLLKGTVRLLFQPAEE-GGAGAKEMIKEGALDDVEAIFGMHVSPALPTGTIA 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446998570 176 YRPGYVQTGRAFFKLKVQGKGGHGSSPHMANDAIVAGSYFVTALQTVVSRRLSPFETGVVTIGSFDGKGQFNVIKDVVEI 255
Cdd:cd08017  159 SRPGPFLAGAGRFEVVIRGKGGHAAMPHHTVDPVVAASSAVLALQQLVSRETDPLDSQVVSVTRFNGGHAFNVIPDSVTF 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446998570 256 EGDVRGLTDATKATIEKEIKRLSKGLEDMYGVTCTLEYNDD----YPALYNDPEFTEYVAKTLKEAnldFGVEMCEPQPP 331
Cdd:cd08017  239 GGTLRALTTEGFYRLRQRIEEVIEGQAAVHRCNATVDFSEDerppYPPTVNDERMYEHAKKVAADL---LGPENVKIAPP 315
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446998570 332 ---SEDFAYYAKERPSAFIYTGAAVE-NGEIYPHHHPKFNISEKSLLISAEAVGTVVLDYL 388
Cdd:cd08017  316 vmgAEDFAFYAEKIPAAFFFLGIRNEtAGSVHSLHSPYFFLDEEVLPVGAALHAAVAERYL 376
M20_Acy1-like cd05664
M20 Peptidase aminoacylase 1 subfamily; Peptidase M20 family, Uncharacterized subfamily of ...
18-388 6.54e-103

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: 310.04  E-value: 6.54e-103
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446998570  18 EIRRYLHQHPELSFHEDETAKYIAEFYKGKDVEVETNVGPRGIKVTIDSGkPGKTLAIRADFDALPITEDTGLSFASQ-- 95
Cdd:cd05664    5 DLYKDFHAHPELSFQEHRTAAKIAEELRKLGFEVTTGIGGTGVVAVLRNG-EGPTVLLRADMDALPVEENTGLPYASTvr 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446998570  96 -------NKGVMHACGHDAHTAYMLVLAETLAEMKDSFTGKVVVIHQPAEEvPPGGAKTMIENGVLDGV---DHVLGVHV 165
Cdd:cd05664   84 mkdwdgkEVPVMHACGHDMHVAALLGAARLLVEAKDAWSGTLIAVFQPAEE-TGGGAQAMVDDGLYDKIpkpDVVLAQHV 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446998570 166 MStMKTGKVYYRPGYVQTGRAFFKLKVQGKGGHGSSPHMANDAIVAGSYFVTALQTVVSRRLSPFETGVVTIGSFDGKGQ 245
Cdd:cd05664  163 MP-GPAGTVGTRPGRFLSAADSLDITIFGRGGHGSMPHLTIDPVVMAASIVTRLQTIVSREVDPQEFAVVTVGSIQAGSA 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446998570 246 FNVIKDVVEIEGDVRGLTDATKATIEKEIKRLSKGLEDMYGVT--CTLEYNDDYPALYNDPEFTEYVAKTLKEANLDFGV 323
Cdd:cd05664  242 ENIIPDEAELKLNVRTFDPEVREKVLNAIKRIVRAECAASGAPkpPEFTYTDSFPATVNDEDATARLAAAFREYFGEDRV 321
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446998570 324 EMCEPQPPSEDFAYYAKE--RPSAFIYTG----------AAVENGEIYPHHHPKFNIS-EKSLLISAEAVGTVVLDYL 388
Cdd:cd05664  322 VEVPPVSASEDFSILATAfgVPSVFWFIGgidpqrwakaVKQKGKEIPGNHSPLFAPViEPTLRTGVEALTVAALAFL 399
M20_Acy1_YkuR-like cd05670
M20 Peptidase aminoacyclase-1 YkuR-like proteins, including YkuR and Ama/HipO/HyuC proteins; ...
17-380 9.19e-102

M20 Peptidase aminoacyclase-1 YkuR-like proteins, including YkuR and Ama/HipO/HyuC proteins; Peptidase M20 family, aminoacyclase-1 YkuR-like subfamily including YkuR and Ama/HipO/HyuC proteins, 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: 349920 [Multi-domain]  Cd Length: 367  Bit Score: 305.73  E-value: 9.19e-102
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446998570  17 IEIRRYLHQHPELSFHEDETAKYIAEF---YKGKDVEVETnVGPRGIKVTIDSGKPGKTLAIRADFDALPITEDTGLSFA 93
Cdd:cd05670    3 IKIRRDLHQIPELGLEEFKTQAYLLDViakLPQDNLEIKT-WCETGILVYVEGSNPERTIGYRADIDALPIEEETGLPFA 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446998570  94 SQNKGVMHACGHDAHTAYMLVLAETLAEMKDSftGKVVVIHQPAEEvPPGGAKTMIENGVLD--GVDHVLGVHVMSTMKT 171
Cdd:cd05670   82 SKHPGVMHACGHDGHMTIALGLLEYFAQHQPK--DNLLFIFQPAEE-GPGGAKRMYESGVFGkwRPDEIYGLHVNPDLPV 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446998570 172 GKVYYRPGYVQTGRAFFKLKVQGKGGHGSSPHMANDAIVAGSYFVTALQTVVSRRLSPFETGVVTIGSFDGKGQFNVIKD 251
Cdd:cd05670  159 GTIATRSGTLFAGTSELHIDFIGKSGHAAYPHNANDMVVAAANFVTQLQTIVSRNVDPIDGAVVTIGKIHAGTARNVIAG 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446998570 252 VVEIEGDVRGLTDATKATIEKEIKRLSKGLEDMYGVTCTLEYNDDYPALYNDPEFTEYVAKTLKEANlDFGVEMCEPQPP 331
Cdd:cd05670  239 TAHLEGTIRTLTQEMMELVKQRVRDIAEGIELAFDCEVKVDLGQGYYPVENDPDLTTEFIDFMKKAD-GVNFVEAEPAMT 317
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*....
gi 446998570 332 SEDFAYYAKERPSAFIYTGAAVEngeiYPHHHPKFNISEKSLLISAEAV 380
Cdd:cd05670  318 GEDFGYLLKKIPGTMFWLGVDSP----YGLHSATLNPDEEAILFGVNAY 362
Peptidase_M20 pfam01546
Peptidase family M20/M25/M40; This family includes a range of zinc metallopeptidases belonging ...
74-386 8.25e-84

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: 258.05  E-value: 8.25e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446998570   74 AIRADFDALPITEDTGLSFASQNKGVMHACGHDAHTAYMLVLAETLAEMKDSF--TGKVVVIHQPAEEVPPGGAKTMIEN 151
Cdd:pfam01546   1 LLRGHMDVVPDEETWGWPFKSTEDGKLYGRGHDDMKGGLLAALEALRALKEEGlkKGTVKLLFQPDEEGGMGGARALIED 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446998570  152 GVLDG--VDHVLGVHVM-STMKTGKVYYRPGYVQTGRAFFKLKVQGKGGHGSSPHMANDAIVAGSYFVTALQTVVSRRLS 228
Cdd:pfam01546  81 GLLERekVDAVFGLHIGePTLLEGGIAIGVVTGHRGSLRFRVTVKGKGGHASTPHLGVNAIVAAARLILALQDIVSRNVD 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446998570  229 PFETGVVTIGSFDG-KGQFNVIKDVVEIEGDVRGLTDATKATIEKEIKRLSKGLEDMYGVTCTLEYNDD-YPALYNDPEF 306
Cdd:pfam01546 161 PLDPAVVTVGNITGiPGGVNVIPGEAELKGDIRLLPGEDLEELEERIREILEAIAAAYGVKVEVEYVEGgAPPLVNDSPL 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446998570  307 TEYVAKTLKEANLDFGVEMCEPQPPSEDFAYYAKERPSAFIYTGAaveNGEIYPHHHPKFniSEKSLLISAEAVGTVVLD 386
Cdd:pfam01546 241 VAALREAAKELFGLKVELIVSGSMGGTDAAFFLLGVPPTVVFFGP---GSGLAHSPNEYV--DLDDLEKGAKVLARLLLK 315
M20_Acy1-like cd08660
M20 Peptidase Aminoacylase 1-like family; This family includes aminoacylase 1 (ACY1) and ...
16-378 1.24e-70

M20 Peptidase Aminoacylase 1-like family; This family includes aminoacylase 1 (ACY1) and Aminoacylase 1-like protein 2 (ACY1L2). Aminoacylase 1 proteins are a class of zinc binding homodimeric enzymes involved in hydrolysis of N-acetylated proteins. ACY1 (acyl-L-amino-acid amidohydrolase; EC 3.5.1.14) is the most abundant of the aminoacylases, a class of zinc binding homodimeric enzymes involved in 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 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. ACY1L2 family contains many uncharacterized proteins predicted as amidohydrolases, including gene products of abgA and abgB that catalyze the cleavage of p-aminobenzoyl-glutamate, a folate catabolite in E. coli, to p-aminobenzoate and glutamate. p-Aminobenzoyl-glutamate utilization is catalyzed by the abg region gene product, AbgT. Defects in ACY1 are the cause of aminoacylase-1 deficiency (ACY1D) resulting in a metabolic disorder manifesting with encephalopathy and psychomotor delay.


Pssm-ID: 349945 [Multi-domain]  Cd Length: 366  Bit Score: 225.97  E-value: 1.24e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446998570  16 MIEIRRYLHQHPELSFHEDETAKYIAEFYKGKDVEVETNVGPR-GIKVTIDSGKPGKTLAIRADFDALPITEDTGLSFAS 94
Cdd:cd08660    1 LINIRRDIHEHPELGFEEVETSKKIRRWLEEEQIEILDVPQLKtGVIAEIKGGEDGPVIAIRADIDALPIQEQTNLPFAS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446998570  95 QNKGVMHACGHDAHTAYMLVLAETLAEMKDSFTGKVVVIHQPAEEVPPGGAKtMIENGVLDGVDHVLGVHVMSTMKTGKV 174
Cdd:cd08660   81 KVDGT*HACGHDFHTTSIIGTA*LLNQRRAELKGTVVFIFQPAEEGAAGARK-VLEAGVLNGVSAIFGIHNKPDLPVGTI 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446998570 175 YYRPGYVQTGRAFFKLKVQGKGGHGSSPHMANDAIVAGSYFVTALQTVVSRRLSPFETGVVTIGSFDGKGQFNVIKDVVE 254
Cdd:cd08660  160 GVKEGPL*ASVDVFEIVIKGKGGHASIPNNSIDPIAAAGQIISGLQSVVSRNISSLQNAVVSITRVQGGTAWNVIPDQAE 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446998570 255 IEGDVRGLTDATKATIEKEIKRLSKGLEDMYGvtCTLEYN---DDYPALYNDPEFTEYVAKTLKEanLDFGVEMCEPQPP 331
Cdd:cd08660  240 *EGTVRAFTKEARQAVPEH*RRVAEGIAAGYG--CQAEFKwfpNGPSEVQNDGTLLNAFSKAAAR--LGYATVHAEQSPG 315
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*..
gi 446998570 332 SEDFAYYAKERPSAFIYTGAaveNGEIYPHHHPKFNISEKSLLISAE 378
Cdd:cd08660  316 SEDFALYQEKIPGFFVW*GT---NGRTEEWHHPAFRLDEEALTVGAQ 359
M20_Acy1_amhX-like cd08018
M20 Peptidase aminoacylase 1 amhX-like subfamily; Peptidase M20 family, uncharacterized ...
17-386 2.99e-69

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: 222.16  E-value: 2.99e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446998570  17 IEIRRYLHQHPELSFHEDETAKYIAEFYKGKDVEVETNVGPRGIKVTIDSGKPGKTLAIRADFDALPiTEDTGLSFASqn 96
Cdd:cd08018    7 VEVFTHLHQIPEISWEEYKTTEYLAKKLEEMGFRVTTFEGGTGVVAEIGSGKPGPVVALRADMDALW-QEVDGEFKAN-- 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446998570  97 kgvmHACGHDAHTAYMLVLAETLAEMKDSFTGKVVVIHQPAEEvPPGGAKTMIENGVLDGVDHVLGVHVMSTMKTGKVYY 176
Cdd:cd08018   84 ----HSCGHDAHMTMVLGAAELLKKIGLVKKGKLKFLFQPAEE-KGTGALKMIEDGVLDDVDYLFGVHLRPIQELPFGTA 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446998570 177 RPGYVQTGRAFFKLKVQGKGGHGSSPHMANDAIVAGSYFVTALQTVvsrRLSPFETGVVTIGSFDGKGQ-FNVIKDVVEI 255
Cdd:cd08018  159 APAIYHGASTFLEGTIKGKQAHGARPHLGINAIEAASAIVNAVNAI---HLDPNIPWSVKMTKLQAGGEaTNIIPDKAKF 235
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446998570 256 EGDVRGLTDATKATIEKEIKRLSKGLEDMYGVTCTLEYNDDYPALYNDPEFTEYVAKTLKEAnldFGVEMCEP---QPPS 332
Cdd:cd08018  236 ALDLRAQSNEAMEELKEKVEHAIEAAAALYGASIEITEKGGMPAAEYDEEAVELMEEAITEV---LGEEKLAGpcvTPGG 312
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 446998570 333 EDFAYYAKERPS---AFIYTGAAVENGeiypHHHPKFNISEKSLLISAEAVGTVVLD 386
Cdd:cd08018  313 EDFHFYTKKKPElkaTMIGLGCGLTPG----LHHPNMTFDRDALENGVKILARAVLK 365
PLN02280 PLN02280
IAA-amino acid hydrolase
19-388 1.33e-66

IAA-amino acid hydrolase


Pssm-ID: 215158 [Multi-domain]  Cd Length: 478  Bit Score: 218.68  E-value: 1.33e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446998570  19 IRRYLHQHPELSFHEDETAKYIAEFYKGKDVEVETNVGPRGIKVTIDSGKPgKTLAIRADFDALPITEDTGLSFASQNKG 98
Cdd:PLN02280 102 VRRKIHENPELAFEEYKTSELVRSELDRMGIMYRYPLAKTGIRAWIGTGGP-PFVAVRADMDALPIQEAVEWEHKSKVAG 180
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446998570  99 VMHACGHDAHTAYMLVLAETLAEMKDSFTGKVVVIHQPAEEVPpGGAKTMIENGVLDGVDHVLGVHVMSTMKTGKVYYRP 178
Cdd:PLN02280 181 KMHACGHDAHVAMLLGAAKILKSREHLLKGTVVLLFQPAEEAG-NGAKRMIGDGALDDVEAIFAVHVSHEHPTAVIGSRP 259
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446998570 179 GYVQTGRAFFKLKVQGKGGHGSSPHMANDAIVAGSYFVTALQTVVSRRLSPFETGVVTIGSFDGKGQFNVIKDVVEIEGD 258
Cdd:PLN02280 260 GPLLAGCGFFRAVISGKKGRAGSPHHSVDLILAASAAVISLQGIVSREANPLDSQVVSVTTMDGGNNLDMIPDTVVLGGT 339
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446998570 259 VRGLTDATKATIEKEIKRLSKGLEDMYGVTCTLEY----NDDYPALYNDPEFTEYVAKTLKEANLDFGVEMCEPQPPSED 334
Cdd:PLN02280 340 FRAFSNTSFYQLLKRIQEVIVEQAGVFRCSATVDFfekqNTIYPPTVNNDAMYEHVRKVAIDLLGPANFTVVPPMMGAED 419
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 446998570 335 FAYYAKERPSAFIYTGAAVEN-GEIYPHHHPKFNISEKSLLISAEAVGTVVLDYL 388
Cdd:PLN02280 420 FSFYSQVVPAAFYYIGIRNETlGSTHTGHSPYFMIDEDVLPIGAAVHAAIAERYL 474
PLN02693 PLN02693
IAA-amino acid hydrolase
1-389 1.49e-59

IAA-amino acid hydrolase


Pssm-ID: 178296 [Multi-domain]  Cd Length: 437  Bit Score: 199.12  E-value: 1.49e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446998570   1 MNQQLIETLKSKE--GKMIEIRRYLHQHPELSFHEDETAKYIAEFYKGKDVEVETNVGPRGIKVTIDSGKPgKTLAIRAD 78
Cdd:PLN02693  32 IQINLLELAKSPEvfDWMVRIRRKIHENPELGYEEFETSKLIRSELDLIGIKYRYPVAITGIIGYIGTGEP-PFVALRAD 110
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446998570  79 FDALPITEDTGLSFASQNKGVMHACGHDAHTAYMLVLAETLAEMKDSFTGKVVVIHQPAEEvPPGGAKTMIENGVLDGVD 158
Cdd:PLN02693 111 MDALPIQEAVEWEHKSKIPGKMHACGHDGHVAMLLGAAKILQEHRHHLQGTVVLIFQPAEE-GLSGAKKMREEGALKNVE 189
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446998570 159 HVLGVHVMSTMKTGKVYYRPGYVQTGRAFFKLKVQGKGGHGSSPHMANDAIVAGSYFVTALQTVVSRRLSPFETGVVTIG 238
Cdd:PLN02693 190 AIFGIHLSPRTPFGKAASRAGSFMAGAGVFEAVITGKGGHAAIPQHTIDPVVAASSIVLSLQQLVSRETDPLDSKVVTVS 269
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446998570 239 SFDGKGQFNVIKDVVEIEGDVRGLTDATKatIEKEIKRLSKGLEDMY----GVTCTLEYNDDYPALYNDPEFTEYVAKTL 314
Cdd:PLN02693 270 KVNGGNAFNVIPDSITIGGTLRAFTGFTQ--LQQRIKEIITKQAAVHrcnaSVNLTPNGREPMPPTVNNMDLYKQFKKVV 347
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446998570 315 KEANLDFGVEMCEPQPPSEDFAYYAKERPSAFIYTGAAVENGEIYPHHHPKFNISEKSLLISAEAVGTVVLDYLK 389
Cdd:PLN02693 348 RDLLGQEAFVEAAPEMGSEDFSYFAETIPGHFSLLGMQDETNGYASSHSPLYRINEDVLPYGAAIHATMAVQYLK 422
M20_Acy1_IAAspH cd05665
M20 Peptidases aminoacyclase-1 indole-3-acetic-L-aspartic acid hydrolase; Peptidase M20 family, ...
15-385 1.74e-54

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: 185.21  E-value: 1.74e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446998570  15 KMIEIRRYLHQHPELSFHEDETAKYIAEFYK--------GKDV------------EVETNVGPR---------------- 58
Cdd:cd05665    2 QLVRWRRDFHRYPESGWTEFRTASLIADYLEelgyelklGREVinadfrmglpddETLAAAFERareqgadeellekmeg 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446998570  59 ---GIKVTIDSGKPGKTLAIRADFDALPITEDTGLS-------FASQNKGVMHACGHDAHTAYMLVLAETLAEMKDSFTG 128
Cdd:cd05665   82 gftGVVATLDTGRPGPTIALRFDIDAVDVTESEDDShrpfkegFASRNDGCMHACGHDGHTAIGLGLAHALAQLKDSLSG 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446998570 129 KVVVIHQPAEEvPPGGAKTMIENGVLDGVDHVLGVHVMSTMKTGKVYYRP-GYVQTG--RAFFKlkvqGKGGH-GSSPHM 204
Cdd:cd05665  162 TIKLIFQPAEE-GVRGARAMAEAGVVDDVDYFLASHIGFGVPSGEVVCGPdNFLATTklDARFT----GVSAHaGAAPED 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446998570 205 ANDAIVAGSYFVTALQTVVSRRLSPFETGVVTIGSFDGKgqfNVIKDVVEIEGDVRGLTDATKATIEKEIKRLSKGLEDM 284
Cdd:cd05665  237 GRNALLAAATAALNLHAIPRHGEGATRINVGVLGAGEGR---NVIPASAELQVETRGETTAINEYMFEQAQRVIKGAATM 313
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446998570 285 YGVTCTLEYNDDYPALYNDPEFTEYVAKTLKEANLDFGVEMCEPQPPSEDfAYYAKER------PSAFIYTGAAVENGei 358
Cdd:cd05665  314 YGVTVEIRTMGEAISAESDPELVALLREQAARVPGVQAVIDSAAFGGSED-ATLLMARvqenggKASYVIFGTELAAG-- 390
                        410       420
                 ....*....|....*....|....*..
gi 446998570 359 ypHHHPKFNISEKSLLISAEAVGTVVL 385
Cdd:cd05665  391 --HHNEEFDFDEAVLAIAVELLTRAVL 415
M20_Acy1-like cd05668
M20 Peptidase aminoacylase 1 subfamily; Peptidase M20 family, uncharacterized subfamily of ...
13-367 9.00e-43

M20 Peptidase aminoacylase 1 subfamily; Peptidase M20 family, uncharacterized subfamily of bacterial uncharacterized 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: 349918 [Multi-domain]  Cd Length: 371  Bit Score: 153.45  E-value: 9.00e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446998570  13 EGKMIEIRRYLHQHPELSFHEDETAKYI-AEFYKGKDVEVETNVGPRGIKVTIDSGKPGKTLAIRADFDALPITEDTGLS 91
Cdd:cd05668    1 IAELSTFRHTLHRYPELSGQEKETAKRIlAFFEPLSPDEVLTGLGGHGVAFIFEGKAEGPTVLFRCELDALPIEEENDFA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446998570  92 FASQNKGVMHACGHDAHTAYMLVLAETLAEMKDSfTGKVVVIHQPAEEVPPgGAKTMIENGVLDGV--DHVLGVHVMSTM 169
Cdd:cd05668   81 HRSKIQGKSHLCGHDGHMAIVSGLGMELSQNRPQ-KGKVILLFQPAEETGE-GAAAVIADPKFKEIqpDFAFALHNLPGL 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446998570 170 KTGKVYYRPGYVQTGRAFFKLKVQGKGGHGSSPHMANDAIVAGSYFVTALQTVVSRrlSPFETGVVTIGSFDGKGQFNVI 249
Cdd:cd05668  159 ELGQIAVKKGPFNCASRGMIIRLKGRTSHAAHPEAGVSPAEAMAKLIVALPALPDA--MPKFTLVTVIHAKLGEAAFGTA 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446998570 250 KDVVEIEGDVRGLTDATKATIEKEIKRLSKGLEDMYGVTCTLEYNDDYPALYNDPEFTEYVAKTLKeaNLDFG-VEMCEP 328
Cdd:cd05668  237 PGEATVMATLRAHTNETMEQLVAEAEKLVQQIADAYGLGVSLEYTEVFAATHNHPEAWALGNQAAK--NLGLPtKHIRIP 314
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|
gi 446998570 329 QPPSEDFAYYAKERPSAFIYTGAavenGEIYPH-HHPKFN 367
Cdd:cd05668  315 FRWSEDFGQFGSVAKTALFVLGS----GEDQPQlHNPDFD 350
M20_Acy1L2 cd03887
M20 Peptidase Aminoacylase 1-like protein 2, amidohydrolase family; Peptidase M20 family, ...
10-363 4.61e-32

M20 Peptidase Aminoacylase 1-like protein 2, amidohydrolase family; Peptidase M20 family, Aminoacylase 1-like protein 2 (ACY1L2; amidohydrolase) subfamily. This group contains many uncharacterized proteins predicted as amidohydrolases, including gene products of abgA and abgB that catalyze the cleavage of p-aminobenzoyl-glutamate, a folate catabolite in Escherichia coli, to p-aminobenzoate and glutamate. p-Aminobenzoyl-glutamate utilization is catalyzed by the abg region gene product, AbgT. Aminoacylase 1 (ACY1) proteins 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 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: 349883 [Multi-domain]  Cd Length: 360  Bit Score: 124.23  E-value: 4.61e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446998570  10 KSKEGKMIEIRRYLHQHPELSFHEDETAKYIAEFYKGKDVEVETNVG--PRGIKVTIDSGKPGKTLAIRADFDALPited 87
Cdd:cd03887    1 DEHAEELIELSRDIHDNPELGYEEYKAHDLLTDFLEELGFDVTRGAYglETAFRAEYGSGKGGPTVAFLAEYDALP---- 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446998570  88 tglsfasqnkGVMHACGHDAHTAYMLVLAETLAE-MKDS-FTGKVVVIHQPAEEVppGGAK-TMIENGVLDGVDHVLGVH 164
Cdd:cd03887   77 ----------GIGHACGHNLIATASVAAALALKAaLKALgLPGTVVVLGTPAEEG--GGGKiDLIKAGAFDDVDIALMVH 144
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446998570 165 VMSTmktgkvyYRPGYVQTGRAFFKLKVQGKGGH-GSSPHM---ANDAIVAGSYFVTAL--QTVVSRRLSpfetGVVTig 238
Cdd:cd03887  145 PGPK-------DVAGPKSLAVSKLRVEFHGKAAHaAAAPWEginALDAAVLAYNNISALrqQLKPTVRVH----GIIT-- 211
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446998570 239 sfDGKGQFNVIKDVVEIEGDVRGLTDATKATIEKEIKRLSKGLEDMYGvtCTLEYNDDyPALYNDPEFTEYVAKTLKEAN 318
Cdd:cd03887  212 --EGGKAPNIIPDYAEAEFYVRAPTLKELEELTERVIACFEGAALATG--CEVEIEEL-EGYYDELLPNKTLANIYAENM 286
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*....
gi 446998570 319 LDFGVEMCEPQPP----SEDFAYYAKERPSafIYTGAAVENGEIYPHHH 363
Cdd:cd03887  287 EALGEEVLDGDEGvgsgSTDFGNVSYVVPG--IHPYFGIPPPGAANHTP 333
M20_ACY1L2-like cd05672
M20 Peptidase aminoacylase 1-like protein 2-like, amidohydrolase subfamily; Peptidase M20 ...
9-363 7.04e-25

M20 Peptidase aminoacylase 1-like protein 2-like, amidohydrolase subfamily; Peptidase M20 family, aminoacylase 1-like protein 2 (ACY1L2; amidohydrolase)-like subfamily. This group contains many uncharacterized proteins predicted as amidohydrolases, including gene products of abgA and abgB that catalyze the cleavage of p-aminobenzoyl-glutamate, a folate catabolite in Escherichia coli, to p-aminobenzoate and glutamate. p-Aminobenzoyl-glutamate utilization is catalyzed by the abg region gene product, AbgT. This subfamily includes Staphylococcus aureus antibiotic resistance factor HmrA that has been shown to participate in methicillin resistance mechanisms in vivo in the presence of beta-lactams. Aminoacylase 1 (ACY1) proteins 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 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: 349921 [Multi-domain]  Cd Length: 360  Bit Score: 104.18  E-value: 7.04e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446998570   9 LKSKEGKMIEIRRYLHQHPELSFHEDETAKYIAEFYKGKDVEVETNVG--PRGIKVTIDSgKPGKTLAIRADFDALPite 86
Cdd:cd05672    1 IDELADELRELSRDIHDNPELGFEEYKAHDLLTDFLEEHGFTVTRGAYglETAFRAEYGS-SGGPTVGFLAEYDALP--- 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446998570  87 dtglsfasqnkGVMHACGHD----AHTAYMLVLAETLAEmkDSFTGKVVVIHQPAEEvpPGGAK-TMIENGVLDGVDHVL 161
Cdd:cd05672   77 -----------GIGHACGHNliatASVAAALALKEALKA--LGLPGKVVVLGTPAEE--GGGGKiDLIKAGAFDDVDAAL 141
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446998570 162 GVHVMStmkTGKVYYRPGYVQTGRAFFKlkvqGKGGH-GSSPHM---ANDAIVAGSYFVTAL--QTVVSRRLSpfetGVV 235
Cdd:cd05672  142 MVHPGP---RDVAGVPSLAVDKLTVEFH----GKSAHaAAAPWEginALDAAVLAYNAISALrqQLKPTWRIH----GII 210
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446998570 236 TigsfDGKGQFNVIKDVVEIEGDVRGLTDATKATIEKEIKRLSKGLEDMYGvtCTLEYNDDYPALYN---DPEFTEYVAK 312
Cdd:cd05672  211 T----EGGKAPNIIPDYAEARFYVRAPTRKELEELRERVIACFEGAALATG--CTVEIEEDEPPYADlrpNKTLAEIYAE 284
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....
gi 446998570 313 TLKEANLDFgveMCEPQPP---SEDFAYYAKERPSafIYTGAAVENGEIYPHHH 363
Cdd:cd05672  285 NMEALGEEV---IDDPEGVgtgSTDMGNVSYVVPG--IHPYFGIPTPGAANHTP 333
M20_Acy1L2-like cd09849
M20 Peptidase aminoacylase 1-like protein 2, amidohydrolase family; Peptidase M20 family, ...
15-260 4.19e-20

M20 Peptidase aminoacylase 1-like protein 2, amidohydrolase family; Peptidase M20 family, aminoacylase 1-like protein 2 (ACY1L2; amidohydrolase)-like subfamily. This group contains many uncharacterized proteins predicted as amidohydrolases, including gene products of abgA and abgB that catalyze the cleavage of p-aminobenzoyl-glutamate, a folate catabolite in Escherichia coli , to p-aminobenzoate and glutamate. p-Aminobenzoyl-glutamate utilization is catalyzed by the abg region gene product, AbgT. Aminoacylase 1 (ACY1) proteins 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 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: 349947 [Multi-domain]  Cd Length: 389  Bit Score: 91.00  E-value: 4.19e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446998570  15 KMIEIRRYLHQHPELSFHEDETAKYIAEFYKG-KDVEVETNVGPRGIKVTIDSGKPGKTLAIRADFDALPITEDTGlsfA 93
Cdd:cd09849    6 KIIAIGQTIYDNPELGYKEFKTTETVADFFKNlLNLDVEKNIASTGCRATLNGDKKGPNIAVLGELDAISCPEHPD---A 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446998570  94 SQNKGVMHACGHDAHTAYMLVLAETLAEMK--DSFTGKVVVIHQPAEEVPP----------------GGAKTMIENGVLD 155
Cdd:cd09849   83 NEATGAAHACGHNIQIAGMLGAAVALFKSGvyEELDGKLTFIATPAEEFIElayrdqlkksgkisyfGGKQELIKRGVFD 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446998570 156 GVDHVLGVHVMStmkTGKVYYRPGYVQTGRAFFKLKVQGKGGH-GSSPHmanDAIVAGSYFVTALQTVVSRRLSPFETGV 234
Cdd:cd09849  163 DIDISLMFHALD---LGEDKALINPESNGFIGKKVKFTGKESHaGSAPF---SGINALNAATLAINNVNAQRETFKESDK 236
                        250       260
                 ....*....|....*....|....*...
gi 446998570 235 VTIGSFDGKGQ--FNVIKDVVEIEGDVR 260
Cdd:cd09849  237 VRFHPIITKGGdiVNVVPADVRVESYVR 264
ArgE COG0624
Acetylornithine deacetylase/Succinyl-diaminopimelate desuccinylase or related deacylase [Amino ...
3-324 1.04e-15

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: 78.00  E-value: 1.04e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446998570   3 QQLIETLKSKEGKMIEI-RRYLhQHPELSFHEDETAKYIAEFYK--GKDVEVETNVGPRG-IKVTIDSGKPGKTLAI--- 75
Cdd:COG0624    1 AAVLAAIDAHLDEALELlRELV-RIPSVSGEEAAAAELLAELLEalGFEVERLEVPPGRPnLVARRPGDGGGPTLLLygh 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446998570  76 ----------RADFDALPITEDTGLSF---ASQNKGvMHACghdahtayMLVLAETLAEMKDSFTGKVVVIHQPAEEVPP 142
Cdd:COG0624   80 ldvvppgdleLWTSDPFEPTIEDGRLYgrgAADMKG-GLAA--------MLAALRALLAAGLRLPGNVTLLFTGDEEVGS 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446998570 143 GGAKTMIENGV-LDGVDHVLgvhVMSTMKTGKVYYRpgyvQTGRAFFKLKVQGKGGHGSSPHMANDAIVAGSYFVTAL-Q 220
Cdd:COG0624  151 PGARALVEELAeGLKADAAI---VGEPTGVPTIVTG----HKGSLRFELTVRGKAAHSSRPELGVNAIEALARALAALrD 223
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446998570 221 TVVSRRLSP-FETGVVTIGSFDGKGQFNVIKDVVEIEGDVRGLTDATKATIEKEIKRLSKGLEdmYGVTCTLEY-NDDYP 298
Cdd:COG0624  224 LEFDGRADPlFGRTTLNVTGIEGGTAVNVIPDEAEAKVDIRLLPGEDPEEVLAALRALLAAAA--PGVEVEVEVlGDGRP 301
                        330       340
                 ....*....|....*....|....*...
gi 446998570 299 ALYNDP--EFTEYVAKTLKEAnldFGVE 324
Cdd:COG0624  302 PFETPPdsPLVAAARAAIREV---TGKE 326
M20_ArgE_DapE-like cd08659
Peptidase M20 acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase (ArgE/DapE) ...
25-340 3.54e-13

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: 70.02  E-value: 3.54e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446998570  25 QHPELSFHEDETAKYIAEFYKGKDVEVE-TNVGPRG-IKVTIDSGKpGKTLAIRADFDALPITEDTGLSF----ASQNKG 98
Cdd:cd08659    8 QIPSVNPPEAEVAEYLAELLAKRGYGIEsTIVEGRGnLVATVGGGD-GPVLLLNGHIDTVPPGDGDKWSFppfsGRIRDG 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446998570  99 VMH---ACGHDAHTAYMLVLAETLAEMKDSFTGKVVVIHQPAEEVPPGGAKTMIENGVLDGVDHVLgvhvmSTMKTGkvy 175
Cdd:cd08659   87 RLYgrgACDMKGGLAAMVAALIELKEAGALLGGRVALLATVDEEVGSDGARALLEAGYADRLDALI-----VGEPTG--- 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446998570 176 YRPGYVQTGRAFFKLKVQGKGGHGSSPHMANDAIVAGSYFVTALQTVVSRR-----LSPFetgVVTIGSFDGKGQFNVIK 250
Cdd:cd08659  159 LDVVYAHKGSLWLRVTVHGKAAHSSMPELGVNAIYALADFLAELRTLFEELpahplLGPP---TLNVGVINGGTQVNSIP 235
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446998570 251 DVVEIEGDVRGLTDATKATIekeIKRLSKGLEDmYGVTCTLEYNDDYPALYNDPEFTEYVAKTLKEANLDFGVEMCEPQP 330
Cdd:cd08659  236 DEATLRVDIRLVPGETNEGV---IARLEAILEE-HEAKLTVEVSLDGDPPFFTDPDHPLVQALQAAARALGGDPVVRPFT 311
                        330
                 ....*....|
gi 446998570 331 PSEDFAYYAK 340
Cdd:cd08659  312 GTTDASYFAK 321
M20_Acy1L2_AbgB cd05673
M20 Peptidase Aminoacylase 1-like protein 2 aminobenzoyl-glutamate utilization protein B ...
26-211 6.50e-11

M20 Peptidase Aminoacylase 1-like protein 2 aminobenzoyl-glutamate utilization protein B subfamily; Peptidase M20 family, ACY1L2 aminobenzoyl-glutamate utilization protein B (AbgB) subfamily. This group contains mostly bacterial amidohydrolases, including gene products of abgB that catalyze the cleavage of p-aminobenzoyl-glutamate, a folate catabolite in Escherichia coli, to p-aminobenzoate and glutamate. p-Aminobenzoyl-glutamate is a natural end product of folate catabolism, and its utilization is initiated by the abg region gene product, AbgT, by enabling uptake of its into the cell in a concentration-dependent, saturable manner. It is subsequently cleaved by AbgA and AbgB (sometimes referred to as AbgAB).


Pssm-ID: 349922 [Multi-domain]  Cd Length: 437  Bit Score: 63.47  E-value: 6.50e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446998570  26 HPELSFHEDETAKYIAEFYKGKDVEVETNVG--PRGIKVTIDSGKPgkTLAIRADFDALPitedtGLS---FASQNKGVM 100
Cdd:cd05673   18 FPELSFEEFRSAALLKEALEEEGFTVERGVAgiPTAFVASYGSGGP--VIAILGEYDALP-----GLSqeaGVAERKPVE 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446998570 101 -----HACGHD----AHTAYMLVLAETLAEMKdsFTGKVVVIHQPAEEVppGGAKT-MIENGVLDGVDHVLGVHVMSTmk 170
Cdd:cd05673   91 pgangHGCGHNllgtGSLGAAIAVKDYMEENN--LAGTVRFYGCPAEEG--GSGKTfMVRDGVFDDVDAAISWHPASF-- 164
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 446998570 171 tgKVYYRPGYVQTGRAFFKLKvqGKGGH-GSSPHMANDAIVA 211
Cdd:cd05673  165 --NGVWSTSSLANISVKFKFK--GISAHaAAAPHLGRSALDA 202
M20_bAS cd03884
M20 Peptidase beta-alanine synthase, an amidohydrolase; Peptidase M20 family, beta-alanine ...
188-321 7.00e-11

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: 63.31  E-value: 7.00e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446998570 188 FKLKVQGKGGH-GSSP-HMANDAIVAGSYFVTALQTVVsRRLSPfeTGVVTIGSFDGK-GQFNVIKDVVEIEGDVRGLTD 264
Cdd:cd03884  209 LEVTVTGEAGHaGTTPmALRRDALLAAAELILAVEEIA-LEHGD--DLVATVGRIEVKpNAVNVIPGEVEFTLDLRHPDD 285
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 446998570 265 ATKATIEKEIKRLSKGLEDMYGVTCTLEYNDDYPALYNDPEFTEYVAKTLKEANLDF 321
Cdd:cd03884  286 AVLDAMVERIRAEAEAIAAERGVEVEVERLWDSPPVPFDPELVAALEAAAEALGLSY 342
M20_ArgE_DapE-like cd08011
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ...
35-316 4.27e-10

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. This group includes the hypothetical protein ygeY from Escherichia coli, a putative deacetylase, but many in this subfamily are classified as unassigned peptidases. 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 mostly archaeal, and have been inferred by homology as being related to both ArgE and DapE.


Pssm-ID: 349933 [Multi-domain]  Cd Length: 355  Bit Score: 60.48  E-value: 4.27e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446998570  35 ETAKYIAEFYK--GKDVEV-ETNVGPRGIKVTIDSGKPGKTLAIRADFDALPITEDTGLSF----ASQNKGVMH---ACG 104
Cdd:cd08011   22 AIAAYIKLLLEdlGYPVELhEPPEEIYGVVSNIVGGRKGKRLLFNGHYDVVPAGDGEGWTVdpysGKIKDGKLYgrgSSD 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446998570 105 HDAHTAYMLVLAETLAEMKDSFTGKVVVIHQPAEE-VPPGGAKTMIENGVLDGVDhvlgvhVMSTMKTGKVYYRPGyvQT 183
Cdd:cd08011  102 MKGGIAASIIAVARLADAKAPWDLPVVLTFVPDEEtGGRAGTKYLLEKVRIKPND------VLIGEPSGSDNIRIG--EK 173
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446998570 184 GRAFFKLKVQGKGGHGSSPHMANDAIVAGSYFVTALQTVVSrrlspfetgVVTIGSFDGKGQFNVIKDVVEIEGDVRGLT 263
Cdd:cd08011  174 GLVWVIIEITGKPAHGSLPHRGESAVKAAMKLIERLYELEK---------TVNPGVIKGGVKVNLVPDYCEFSVDIRLPP 244
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 446998570 264 DATKATIEKEIKRLskgLEDMYGVTCTLEYNDDYPALYNDPEFTEYVAKTLKE 316
Cdd:cd08011  245 GISTDEVLSRIIDH---LDSIEEVSFEIKSFYSPTVSNPDSEIVKKTEEAITE 294
M20_dimer pfam07687
Peptidase dimerization domain; This domain consists of 4 beta strands and two alpha helices ...
184-279 4.71e-09

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: 53.50  E-value: 4.71e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446998570  184 GRAFFKLKVQGKGGHGSSPHMANDAIVAGSYFVTALQTVVSRRLSPFETGVVTIGSFDGKGQFNVIKDVVEIEGDVRGLT 263
Cdd:pfam07687   5 GLAGGHLTVKGKAGHSGAPGKGVNAIKLLARLLAELPAEYGDIGFDFPRTTLNITGIEGGTATNVIPAEAEAKFDIRLLP 84
                          90
                  ....*....|....*.
gi 446998570  264 DATKATIEKEIKRLSK 279
Cdd:pfam07687  85 GEDLEELLEEIEAILE 100
PRK12893 PRK12893
Zn-dependent hydrolase;
188-315 8.09e-08

Zn-dependent hydrolase;


Pssm-ID: 237250 [Multi-domain]  Cd Length: 412  Bit Score: 53.73  E-value: 8.09e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446998570 188 FKLKVQGKGGH-GSSP-HMANDAIVAGSYFVTALQTVVsRRLSPfeTGVVTIGSFDGK-GQFNVIKDVVEIEGDVRGLTD 264
Cdd:PRK12893 217 LEVTVEGQAAHaGTTPmAMRRDALVAAARIILAVERIA-AALAP--DGVATVGRLRVEpNSRNVIPGKVVFTVDIRHPDD 293
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 446998570 265 ATKATIEKEIKRLSKGLEDMYGVTCTLEYNDDYPALYNDPEFTEYVAKTLK 315
Cdd:PRK12893 294 ARLDAMEAALRAACAKIAAARGVQVTVETVWDFPPVPFDPALVALVEAAAE 344
PRK08588 PRK08588
succinyl-diaminopimelate desuccinylase; Reviewed
32-305 8.43e-07

succinyl-diaminopimelate desuccinylase; Reviewed


Pssm-ID: 181490 [Multi-domain]  Cd Length: 377  Bit Score: 50.65  E-value: 8.43e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446998570  32 HEDETAKYIAEFYKGKDVE---VETNVGPRGIKVTIDSGKPgkTLAI-------------RADFDALPITEDTGLSF--- 92
Cdd:PRK08588  20 NEIEVANYLQDLFAKHGIEskiVKVNDGRANLVAEIGSGSP--VLALsghmdvvaagdvdKWTYDPFELTEKDGKLYgrg 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446998570  93 ASQNKGVMHAcghdahtaymLVLAetLAEMKDS---FTGKVVVIHQPAEEVPPGGAKTMIENGVLDGVDHVlgvhVMSTM 169
Cdd:PRK08588  98 ATDMKSGLAA----------LVIA--MIELKEQgqlLNGTIRLLATAGEEVGELGAKQLTEKGYADDLDAL----IIGEP 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446998570 170 KTGKVYYrpgyVQTGRAFFKLKVQGKGGHGSSPHMANDAIVAGSYFVTALQT------VVSRRLSPFeTGVVTIgsFDGK 243
Cdd:PRK08588 162 SGHGIVY----AHKGSMDYKVTSTGKAAHSSMPELGVNAIDPLLEFYNEQKEyfdsikKHNPYLGGL-THVVTI--INGG 234
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446998570 244 GQFNVIKDVVEIEGDVRGLTDATKATIEKEIKRLSKGLEDMYGVTCTLEYNDDYPALYNDPE 305
Cdd:PRK08588 235 EQVNSVPDEAELEFNIRTIPEYDNDQVISLLQEIINEVNQNGAAQLSLDIYSNHRPVASDKD 296
M20_CPDG2 cd03885
M20 Peptidase Glutamate carboxypeptidase, a periplasmic enzyme; Peptidase M20 family, ...
184-300 3.74e-06

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: 48.36  E-value: 3.74e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446998570 184 GRAFFKLKVQGKGGH-GSSPHMANDAIVAGSYFVTALQTvvsrrLSPFETGV-VTIGSFDGKGQFNVIKDVVEIEGDVRG 261
Cdd:cd03885  170 GIGRFRLTVKGRAAHaGNAPEKGRSAIYELAHQVLALHA-----LTDPEKGTtVNVGVISGGTRVNVVPDHAEAQVDVRF 244
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 446998570 262 LTDATKATIEKEIKRLSKgLEDMYGVTCTLEYNDDYPAL 300
Cdd:cd03885  245 ATAEEADRVEEALRAIVA-TTLVPGTSVELTGGLNRPPM 282
PRK08651 PRK08651
succinyl-diaminopimelate desuccinylase; Reviewed
184-317 7.26e-06

succinyl-diaminopimelate desuccinylase; Reviewed


Pssm-ID: 236323 [Multi-domain]  Cd Length: 394  Bit Score: 47.68  E-value: 7.26e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446998570 184 GRAFFKLKVQGKGGHGSSPHMANDAIVAGSYFVTALQTVVSRRLSPFETG-------VVTIGSF--DGKGQFNVIKDVVE 254
Cdd:PRK08651 183 GLVWGVVKVYGKQAHASTPWLGINAFEAAAKIAERLKSSLSTIKSKYEYDdergakpTVTLGGPtvEGGTKTNIVPGYCA 262
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446998570 255 IEGDVRGLTDatkATIEKEIKRLSKGLEDM---YGVTCTLEYNDDYPALYNDP--EFTEYVAKTLKEA 317
Cdd:PRK08651 263 FSIDRRLIPE---ETAEEVRDELEALLDEVapeLGIEVEFEITPFSEAFVTDPdsELVKALREAIREV 327
PRK12890 PRK12890
allantoate amidohydrolase; Reviewed
188-292 5.14e-05

allantoate amidohydrolase; Reviewed


Pssm-ID: 237248 [Multi-domain]  Cd Length: 414  Bit Score: 44.89  E-value: 5.14e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446998570 188 FKLKVQGKGGH-GSSP-HMANDAIVAGSYFVTALQtvvsRRLSPFETGVV-TIGSFD-GKGQFNVIKDVVEIEGDVRGLT 263
Cdd:PRK12890 219 QAVTVEGEANHaGTTPmDLRRDALVAAAELVTAME----RRARALLHDLVaTVGRLDvEPNAINVVPGRVVFTLDLRSPD 294
                         90       100
                 ....*....|....*....|....*....
gi 446998570 264 DATKATIEKEIKRLSKGLEDMYGVTCTLE 292
Cdd:PRK12890 295 DAVLEAAEAALLAELEAIAAARGVRIELE 323
M20_18_42 cd18669
M20, M18 and M42 Zn-peptidases include aminopeptidases and carboxypeptidases; This family ...
59-208 5.66e-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: 43.58  E-value: 5.66e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446998570  59 GIKVTIDSGKPGKTLAIRADFDALPITEDTGLSFASQNKGV-------MHACGHDAHTAYMLVLAETLAEMKDSFTGKVV 131
Cdd:cd18669    1 NVIARYGGGGGGKRVLLGAHIDVVPAGEGDPRDPPFFVDTVeegrlygRGALDDKGGVAAALEALKLLKENGFKLKGTVV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446998570 132 VIHQPAEEVPPGGAKTMIEN---GVLDGVDHVLGVHVMSTMKTGKVYYRPGYVQTGRAFFklKVQGKGGHGSSPHMANDA 208
Cdd:cd18669   81 VAFTPDEEVGSGAGKGLLSKdalEEDLKVDYLFVGDATPAPQKGVGIRTPLVDALSEAAR--KVFGKPQHAEGTGGGTDG 158
Zinc_peptidase_like cd03873
Zinc peptidases M18, M20, M28, and M42; Zinc peptidases play vital roles in metabolic and ...
59-140 2.21e-04

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: 42.03  E-value: 2.21e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446998570  59 GIKVTIDSGKPGKTLAIRADFDALPITEDTGLSF-------ASQNKGVMHACGHDAHTAYMLVLAETLAEMKDSFTGKVV 131
Cdd:cd03873    1 NLIARLGGGEGGKSVALGAHLDVVPAGEGDNRDPpfaedteEEGRLYGRGALDDKGGVAAALEALKRLKENGFKPKGTIV 80

                 ....*....
gi 446998570 132 VIHQPAEEV 140
Cdd:cd03873   81 VAFTADEEV 89
PRK07338 PRK07338
hydrolase;
184-292 2.65e-04

hydrolase;


Pssm-ID: 235995 [Multi-domain]  Cd Length: 402  Bit Score: 42.64  E-value: 2.65e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446998570 184 GRAFFKLKVQGKGGH-GSSPHMANDAIVAGSYFVTALQtvvsrRLSPFETGV-VTIGSFDGKGQFNVIKDVVEIEGDVRG 261
Cdd:PRK07338 202 GSGNFTIVVTGRAAHaGRAFDEGRNAIVAAAELALALH-----ALNGQRDGVtVNVAKIDGGGPLNVVPDNAVLRFNIRP 276
                         90       100       110
                 ....*....|....*....|....*....|.
gi 446998570 262 LTDATKATIEKEIKRLSKGLEDMYGVTCTLE 292
Cdd:PRK07338 277 PTPEDAAWAEAELKKLIAQVNQRHGVSLHLH 307
M20_ArgE cd03894
M20 Peptidase acetylornithine deacetylase; Peptidase M20 family, acetylornithine deacetylase ...
184-312 8.01e-04

M20 Peptidase acetylornithine deacetylase; Peptidase M20 family, acetylornithine deacetylase (ArgE, Acetylornithinase, AO, N2-acetyl-L-ornithine amidohydrolase, EC 3.5.1.16) subfamily. ArgE catalyzes the conversion of N-acetylornithine to ornithine, which can then be incorporated into the urea cycle for the final stage of arginine synthesis. The substrate specificity of ArgE is quite broad; several alpha-N-acyl-L-amino acids can be hydrolyzed, including alpha-N-acetylmethionine and alpha-N-formylmethionine. ArgE shares significant sequence homology and biochemical features, and possibly a common origin, with glutamate carboxypeptidase (CPG2) and succinyl-diaminopimelate desuccinylase (DapE), and aminoacylase I (ACY1), having all metal ligand binding residues conserved.


Pssm-ID: 349889 [Multi-domain]  Cd Length: 367  Bit Score: 41.04  E-value: 8.01e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446998570 184 GRAFFKLKVQGKGGHGSSPHMANDAIVAGSYFVTAL-----QTVVSRRLSPFETG--VVTIGSFDGKGQFNVIKDVVEIE 256
Cdd:cd03894  169 GIASYRIRVRGRAAHSSLPPLGVNAIEAAARLIGKLreladRLAPGLRDPPFDPPypTLNVGLIHGGNAVNIVPAECEFE 248
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 446998570 257 GDVRGLTDATKATIEKEIKRLSKGLEDMYGVTCTLEYNDDYPALYNDP--EFTEYVAK 312
Cdd:cd03894  249 FEFRPLPGEDPEAIDARLRDYAEALLEFPEAGIEVEPLFEVPGLETDEdaPLVRLAAA 306
M20_peptT_like cd05683
M20 Peptidase T like enzymes specifically cleave tripeptides; Peptidase M20 family, PeptT ...
188-325 2.73e-03

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: 39.36  E-value: 2.73e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446998570 188 FKLKVQGKGGH-GSSPHMANDAIVAGSYFVTALQTVvsrRLSPFETGvvTIGSFDGKGQFNVIKDVVEIEGDVRGLtdaT 266
Cdd:cd05683  181 INAKIYGKTAHaGTSPEKGISAINIAAKAISNMKLG---RIDEETTA--NIGKFQGGTATNIVTDEVNIEAEARSL---D 252
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446998570 267 KATIEKEIKRLSKGLEDM---YGVTCTLEYNDDYPALynDPEFTEYVAKTLKEANLDFGVEM 325
Cdd:cd05683  253 EEKLDAQVKHMKETFETTakeKGAHAEVEVETSYPGF--KINEDEEVVKLAKRAANNLGLEI 312
M20_PAAh_like cd03896
M20 Peptidases, Poly(aspartic acid) hydrolase-like proteins; Peptidase M20 family, Poly ...
23-299 3.63e-03

M20 Peptidases, Poly(aspartic acid) hydrolase-like proteins; Peptidase M20 family, Poly(aspartic acid) hydrolase (PAA hydrolase)-like subfamily. PAA hydrolase enzymes are involved in alpha,beta-poly(D,L-aspartic acid) (tPAA) biodegradation. PAA is being extensively studied as a replacement for commercial polycarboxylate components since it can be degraded by enzymes from isolated tPAA degrading bacteria. Thus far, two types of PAA degrading bacteria (Sphingomonas sp. KT-1 and Pedobacter sp. KP-2) have been investigated in detail; the former can completely degrade tPAA of low-molecular weights below 5000, while the latter can degrade high molecular weight tPAA to release oligo(aspartic acid) (OAA) as a product, suggesting two kinds of PAA degrading enzymes. It has been shown that PAA hydrolase-1 from Sphingomonas sp. KT-1 hydrolyzes beta,beta-aspartic acid units in tPAA to produce OAA, and it is suggested that PAA hydrolase-2 hydrolyzes OAA to aspartic acid. Also included in this family is Bradyrhizobium 5-nitroanthranilic acid (5NAA)-aminohydrolase (5NAA-A), a biodegradation enzyme that converts 5NAA to 5-nitrosalicylic acid; 5NAA is a metabolite secreted by Streptomyces scabies, the bacterium responsible for potato scab, and metabolized by Bradyrhizobium species strain JS329.


Pssm-ID: 349891 [Multi-domain]  Cd Length: 357  Bit Score: 39.00  E-value: 3.63e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446998570  23 LHQHPELSFHEDETAKYIAEFYKG---KDVEV--ETNVGPRgikVTIDSGKPGKTLA------IRADFDALPITEDTGLS 91
Cdd:cd03896    7 LGEIPAPTFREGARADLVAEWMADlglGDVERdgRGNVVGR---LRGTGGGPALLFSahldtvFPGDTPATVRHEGGRIY 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446998570  92 FAS--QNKGVMhacghdahtAYMLVLAETLAEMKDSFTGKVVVIHQPAEEvppggaktmiENGVLDGVDHVLGVH--VMS 167
Cdd:cd03896   84 GPGigDNKGSL---------ACLLAMARAMKEAGAALKGDVVFAANVGEE----------GLGDLRGARYLLSAHgaRLD 144
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446998570 168 TMKTGKVY-YRPGYVQTGRAFFKLKVQGKGGHGSSPHMANDAIVAGSYFVTALQTVVSRRLSPFETGVVTIGsfdGKGQF 246
Cdd:cd03896  145 YFVVAEGTdGVPHTGAVGSKRFRITTVGPGGHSYGAFGSPSAIVAMAKLVEALYEWAAPYVPKTTFAAIRGG---GGTSV 221
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 446998570 247 NVIKDVVEIEGDVRGLTDATKATIEKEI-KRLSKGLEDMYGVTCTLEYNDDYPA 299
Cdd:cd03896  222 NRIANLCSMYLDIRSNPDAELADVQREVeAVVSKLAAKHLRVKARVKPVGDRPG 275
M20_ArgE_DapE-like cd05650
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ...
187-317 4.12e-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 mostly bacterial and archaeal, and have been inferred by homology as being related to both ArgE and DapE.


Pssm-ID: 349901 [Multi-domain]  Cd Length: 389  Bit Score: 38.98  E-value: 4.12e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446998570 187 FFKLKVQGKGGHGSSPHMANDAIVAGSYFVTALQTVVSRRLS--------PFETGVVTIGSfDGKGQFNVIKDVVEIEGD 258
Cdd:cd05650  190 WIKVNVKGKQCHASTPENGINAFVAASNFALELDELLHEKFDekddlfnpPYSTFEPTKKE-ANVPNVNTIPGYDVFYFD 268
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 446998570 259 VRGLTDATKATIEKEIKRLSKGLEDMYGVTCTLEYNDDYPALYNDPEFTEYVAKtLKEA 317
Cdd:cd05650  269 CRVLPTYKLDEVLKFVNKIISDFENSYGAGITYEIVQKEQAPPATPEDSEIVVR-LSKA 326
 
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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