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Conserved domains on  [gi|2744372630|ref|WP_349775168|]
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M20/M25/M40 family metallo-hydrolase [Pantoea sp. YR343]

Protein Classification

zinc-binding metallopeptidase family protein( domain architecture ID 56613)

zinc-binding metallopeptidase family protein

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Zinc_peptidase_like super family cl14876
Zinc peptidases M18, M20, M28, and M42; Zinc peptidases play vital roles in metabolic and ...
1-249 2.34e-95

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).


The actual alignment was detected with superfamily member cd03885:

Pssm-ID: 472712 [Multi-domain]  Cd Length: 362  Bit Score: 284.10  E-value: 2.34e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2744372630   1 MQHHDLLAGKRIVFLCGSDEEVGSPSSSAWLSHHALGSAQVLVVEPAVAGsGALKTARKGTGQYEITINGLAAHAGNNPE 80
Cdd:cd03885   112 LKAAGGRDYLPITVLLNSDEEIGSPGSRELIEEEAKGADYVLVFEPARAD-GNLVTARKGIGRFRLTVKGRAAHAGNAPE 190
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2744372630  81 EGISAVQEMAHQIMFLHSLNAPERGTTVNVGIARGGNRINVVADKAVLGIDTRVTSEAEAERIHAEISQI--TPHLAGIK 158
Cdd:cd03885   191 KGRSAIYELAHQVLALHALTDPEKGTTVNVGVISGGTRVNVVPDHAEAQVDVRFATAEEADRVEEALRAIvaTTLVPGTS 270
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2744372630 159 LDISGAQSRPPMRQTPESLVLMERAQQVAEQLGFAVEGKAVGGGSDGNFTAALGIPTLDGLGATGAGIHARHEHIIIADI 238
Cdd:cd03885   271 VELTGGLNRPPMEETPASRRLLARAQEIAAELGLTLDWEATGGGSDANFTAALGVPTLDGLGPVGGGAHTEDEYLELDSL 350
                         250
                  ....*....|.
gi 2744372630 239 APRAALVAGLI 249
Cdd:cd03885   351 VPRIKLLARLL 361
 
Name Accession Description Interval E-value
M20_CPDG2 cd03885
M20 Peptidase Glutamate carboxypeptidase, a periplasmic enzyme; Peptidase M20 family, ...
1-249 2.34e-95

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: 284.10  E-value: 2.34e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2744372630   1 MQHHDLLAGKRIVFLCGSDEEVGSPSSSAWLSHHALGSAQVLVVEPAVAGsGALKTARKGTGQYEITINGLAAHAGNNPE 80
Cdd:cd03885   112 LKAAGGRDYLPITVLLNSDEEIGSPGSRELIEEEAKGADYVLVFEPARAD-GNLVTARKGIGRFRLTVKGRAAHAGNAPE 190
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2744372630  81 EGISAVQEMAHQIMFLHSLNAPERGTTVNVGIARGGNRINVVADKAVLGIDTRVTSEAEAERIHAEISQI--TPHLAGIK 158
Cdd:cd03885   191 KGRSAIYELAHQVLALHALTDPEKGTTVNVGVISGGTRVNVVPDHAEAQVDVRFATAEEADRVEEALRAIvaTTLVPGTS 270
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2744372630 159 LDISGAQSRPPMRQTPESLVLMERAQQVAEQLGFAVEGKAVGGGSDGNFTAALGIPTLDGLGATGAGIHARHEHIIIADI 238
Cdd:cd03885   271 VELTGGLNRPPMEETPASRRLLARAQEIAAELGLTLDWEATGGGSDANFTAALGVPTLDGLGPVGGGAHTEDEYLELDSL 350
                         250
                  ....*....|.
gi 2744372630 239 APRAALVAGLI 249
Cdd:cd03885   351 VPRIKLLARLL 361
PRK07338 PRK07338
hydrolase;
18-250 2.82e-51

hydrolase;


Pssm-ID: 235995 [Multi-domain]  Cd Length: 402  Bit Score: 172.07  E-value: 2.82e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2744372630  18 SDEEVGSPSSSAWLSHHALGSAQVLVVEPAVAgSGALKTARKGTGQYEITINGLAAHAGNNPEEGISAVQEMAHQIMFLH 97
Cdd:PRK07338  161 PDEEIGSPASAPLLAELARGKHAALTYEPALP-DGTLAGARKGSGNFTIVVTGRAAHAGRAFDEGRNAIVAAAELALALH 239
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2744372630  98 SLNAPERGTTVNVGIARGGNRINVVADKAVLGIDTRVTSEAEAERIHAEISQITPHLA---GIKLDISGAQSRPPMRQTP 174
Cdd:PRK07338  240 ALNGQRDGVTVNVAKIDGGGPLNVVPDNAVLRFNIRPPTPEDAAWAEAELKKLIAQVNqrhGVSLHLHGGFGRPPKPIDA 319
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2744372630 175 ESLVLMERAQQVAEQLGFAVEGKAVGGGSDGNFTAALGIPTLDGLGATGAGIHARHEHIIIADIAPRAALVAgLIL 250
Cdd:PRK07338  320 AQQRLFEAVQACGAALGLTIDWKDSGGVCDGNNLAAAGLPVVDTLGVRGGNIHSEDEFVILDSLVERAQLSA-LIL 394
ArgE COG0624
Acetylornithine deacetylase/Succinyl-diaminopimelate desuccinylase or related deacylase [Amino ...
11-250 9.76e-48

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: 162.36  E-value: 9.76e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2744372630  11 RIVFLCGSDEEVGSPSSSAWLSHHA--LGSAQVLVVEPAvaGSGALKTARKGTGQYEITINGLAAHAGNnPEEGISAVQE 88
Cdd:COG0624   137 NVTLLFTGDEEVGSPGARALVEELAegLKADAAIVGEPT--GVPTIVTGHKGSLRFELTVRGKAAHSSR-PELGVNAIEA 213
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2744372630  89 MAHQIMFLHSLNAPERG------TTVNVGIARGGNRINVVADKAVLGIDTRVTSEAEAERIHAEISQ-ITPHLAGIKLDI 161
Cdd:COG0624   214 LARALAALRDLEFDGRAdplfgrTTLNVTGIEGGTAVNVIPDEAEAKVDIRLLPGEDPEEVLAALRAlLAAAAPGVEVEV 293
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2744372630 162 S-GAQSRPPMRqTPESLVLMERAQQVAEQL-GFAVEGKAVGGGSDGNFTA-ALGIPTLD-GLGaTGAGIHARHEHIIIAD 237
Cdd:COG0624   294 EvLGDGRPPFE-TPPDSPLVAAARAAIREVtGKEPVLSGVGGGTDARFFAeALGIPTVVfGPG-DGAGAHAPDEYVELDD 371
                         250
                  ....*....|...
gi 2744372630 238 IAPRAALVAGLIL 250
Cdd:COG0624   372 LEKGARVLARLLE 384
Peptidase_M20 pfam01546
Peptidase family M20/M25/M40; This family includes a range of zinc metallopeptidases belonging ...
2-250 5.32e-25

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: 100.88  E-value: 5.32e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2744372630   2 QHHDLLAGKR-IVFLCGSDEEVGSPSSSAWLSHHALGSAQV------LVVEPAVAGSGA---LKTARKGTGQYEITINGL 71
Cdd:pfam01546  48 ALKEEGLKKGtVKLLFQPDEEGGMGGARALIEDGLLEREKVdavfglHIGEPTLLEGGIaigVVTGHRGSLRFRVTVKGK 127
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2744372630  72 AAHAGNnPEEGISAVQEMAHQIMFLHSLNAPERG-------TTVNVGIARGGnrINVVADKAVLGIDTRVTSEAEAERIH 144
Cdd:pfam01546 128 GGHAST-PHLGVNAIVAAARLILALQDIVSRNVDpldpavvTVGNITGIPGG--VNVIPGEAELKGDIRLLPGEDLEELE 204
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2744372630 145 AEISQITPHLA---GIKLDISGAQSRPPMRQTPESLVlmERAQQVAEQL-GFAVEGKAVG--GGSDGNFTAaLGIP-TLD 217
Cdd:pfam01546 205 ERIREILEAIAaayGVKVEVEYVEGGAPPLVNDSPLV--AALREAAKELfGLKVELIVSGsmGGTDAAFFL-LGVPpTVV 281
                         250       260       270
                  ....*....|....*....|....*....|...
gi 2744372630 218 GLGATGAGIHARHEHIIIADIAPRAALVAGLIL 250
Cdd:pfam01546 282 FFGPGSGLAHSPNEYVDLDDLEKGAKVLARLLL 314
PepT-like TIGR01883
peptidase T-like protein; This model represents a clade of enzymes closely related to ...
67-249 1.50e-12

peptidase T-like protein; This model represents a clade of enzymes closely related to Peptidase T, an aminotripeptidase found in bacteria. This clade consists of gram positive bacteria of which several additionally contain a Peptidase T gene.


Pssm-ID: 162579 [Multi-domain]  Cd Length: 361  Bit Score: 66.50  E-value: 1.50e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2744372630  67 TINGLAAHAGNNPEEGISA--VQEMAHQIMFLHSLnapERGTTVNVGIARGGNRINVVADKAVLGIDTRVTSEAEAErih 144
Cdd:TIGR01883 178 TIAGKDAHAGLVPEDGISAisVARMAIHAMRLGRI---DEETTANIGSFSGGVNTNIVQDEQLIVAEARSLSFRKAE--- 251
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2744372630 145 AEISQI------TPHLAGIKLDISGAQSRPPMRQTPESlVLMERAQQVAEQLGFAVEGKAVGGGSDGNFTAALGIPTLDg 218
Cdd:TIGR01883 252 AQVQTMrerfeqAAEKYGATLEEETRLIYEGFKIHPQH-PLMNIFKKAAKKIGLKTSEIFSGGGSDANVLNEKGVPTVN- 329
                         170       180       190
                  ....*....|....*....|....*....|.
gi 2744372630 219 LGATGAGIHARHEHIIIADIAPRAALVAGLI 249
Cdd:TIGR01883 330 LSAGYVHAHTEKETISIEQLVKLAELVIALA 360
 
Name Accession Description Interval E-value
M20_CPDG2 cd03885
M20 Peptidase Glutamate carboxypeptidase, a periplasmic enzyme; Peptidase M20 family, ...
1-249 2.34e-95

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: 284.10  E-value: 2.34e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2744372630   1 MQHHDLLAGKRIVFLCGSDEEVGSPSSSAWLSHHALGSAQVLVVEPAVAGsGALKTARKGTGQYEITINGLAAHAGNNPE 80
Cdd:cd03885   112 LKAAGGRDYLPITVLLNSDEEIGSPGSRELIEEEAKGADYVLVFEPARAD-GNLVTARKGIGRFRLTVKGRAAHAGNAPE 190
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2744372630  81 EGISAVQEMAHQIMFLHSLNAPERGTTVNVGIARGGNRINVVADKAVLGIDTRVTSEAEAERIHAEISQI--TPHLAGIK 158
Cdd:cd03885   191 KGRSAIYELAHQVLALHALTDPEKGTTVNVGVISGGTRVNVVPDHAEAQVDVRFATAEEADRVEEALRAIvaTTLVPGTS 270
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2744372630 159 LDISGAQSRPPMRQTPESLVLMERAQQVAEQLGFAVEGKAVGGGSDGNFTAALGIPTLDGLGATGAGIHARHEHIIIADI 238
Cdd:cd03885   271 VELTGGLNRPPMEETPASRRLLARAQEIAAELGLTLDWEATGGGSDANFTAALGVPTLDGLGPVGGGAHTEDEYLELDSL 350
                         250
                  ....*....|.
gi 2744372630 239 APRAALVAGLI 249
Cdd:cd03885   351 VPRIKLLARLL 361
PRK07338 PRK07338
hydrolase;
18-250 2.82e-51

hydrolase;


Pssm-ID: 235995 [Multi-domain]  Cd Length: 402  Bit Score: 172.07  E-value: 2.82e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2744372630  18 SDEEVGSPSSSAWLSHHALGSAQVLVVEPAVAgSGALKTARKGTGQYEITINGLAAHAGNNPEEGISAVQEMAHQIMFLH 97
Cdd:PRK07338  161 PDEEIGSPASAPLLAELARGKHAALTYEPALP-DGTLAGARKGSGNFTIVVTGRAAHAGRAFDEGRNAIVAAAELALALH 239
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2744372630  98 SLNAPERGTTVNVGIARGGNRINVVADKAVLGIDTRVTSEAEAERIHAEISQITPHLA---GIKLDISGAQSRPPMRQTP 174
Cdd:PRK07338  240 ALNGQRDGVTVNVAKIDGGGPLNVVPDNAVLRFNIRPPTPEDAAWAEAELKKLIAQVNqrhGVSLHLHGGFGRPPKPIDA 319
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2744372630 175 ESLVLMERAQQVAEQLGFAVEGKAVGGGSDGNFTAALGIPTLDGLGATGAGIHARHEHIIIADIAPRAALVAgLIL 250
Cdd:PRK07338  320 AQQRLFEAVQACGAALGLTIDWKDSGGVCDGNNLAAAGLPVVDTLGVRGGNIHSEDEFVILDSLVERAQLSA-LIL 394
ArgE COG0624
Acetylornithine deacetylase/Succinyl-diaminopimelate desuccinylase or related deacylase [Amino ...
11-250 9.76e-48

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: 162.36  E-value: 9.76e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2744372630  11 RIVFLCGSDEEVGSPSSSAWLSHHA--LGSAQVLVVEPAvaGSGALKTARKGTGQYEITINGLAAHAGNnPEEGISAVQE 88
Cdd:COG0624   137 NVTLLFTGDEEVGSPGARALVEELAegLKADAAIVGEPT--GVPTIVTGHKGSLRFELTVRGKAAHSSR-PELGVNAIEA 213
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2744372630  89 MAHQIMFLHSLNAPERG------TTVNVGIARGGNRINVVADKAVLGIDTRVTSEAEAERIHAEISQ-ITPHLAGIKLDI 161
Cdd:COG0624   214 LARALAALRDLEFDGRAdplfgrTTLNVTGIEGGTAVNVIPDEAEAKVDIRLLPGEDPEEVLAALRAlLAAAAPGVEVEV 293
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2744372630 162 S-GAQSRPPMRqTPESLVLMERAQQVAEQL-GFAVEGKAVGGGSDGNFTA-ALGIPTLD-GLGaTGAGIHARHEHIIIAD 237
Cdd:COG0624   294 EvLGDGRPPFE-TPPDSPLVAAARAAIREVtGKEPVLSGVGGGTDARFFAeALGIPTVVfGPG-DGAGAHAPDEYVELDD 371
                         250
                  ....*....|...
gi 2744372630 238 IAPRAALVAGLIL 250
Cdd:COG0624   372 LEKGARVLARLLE 384
PRK06133 PRK06133
glutamate carboxypeptidase; Reviewed
11-249 7.87e-43

glutamate carboxypeptidase; Reviewed


Pssm-ID: 235710 [Multi-domain]  Cd Length: 410  Bit Score: 150.17  E-value: 7.87e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2744372630  11 RIVFLCGSDEEVGSPSSSAWLSHHALGSAQVLVVEPAVAgSGALKTARKGTGQYEITINGLAAHAGNNPEEGISAVQEMA 90
Cdd:PRK06133  161 TLTVLFNPDEETGSPGSRELIAELAAQHDVVFSCEPGRA-KDALTLATSGIATALLEVKGKASHAGAAPELGRNALYELA 239
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2744372630  91 HQIMFLHSLNAPERGTTVNVGIARGGNRINVVADKAVLGIDTRVTSEAEAERIHAEISQITPH--LAGIKLDISGAQSRP 168
Cdd:PRK06133  240 HQLLQLRDLGDPAKGTTLNWTVAKAGTNRNVIPASASAQADVRYLDPAEFDRLEADLQEKVKNklVPDTEVTLRFERGRP 319
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2744372630 169 PMRQTPESLVLMERAQQVAEQLG--FAVEGKAVGGGSDGNFTAALG-IPTLDGLGATGAGIHARHEHIIIADIAPRAALV 245
Cdd:PRK06133  320 PLEANAASRALAEHAQGIYGELGrrLEPIDMGTGGGTDAAFAAGSGkAAVLEGFGLVGFGAHSNDEYIELNSIVPRLYLL 399

                  ....
gi 2744372630 246 AGLI 249
Cdd:PRK06133  400 TRMI 403
PRK07473 PRK07473
M20/M25/M40 family metallo-hydrolase;
12-250 1.13e-41

M20/M25/M40 family metallo-hydrolase;


Pssm-ID: 168961 [Multi-domain]  Cd Length: 376  Bit Score: 146.47  E-value: 1.13e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2744372630  12 IVFLCGSDEEVGSPSSSAWLSHHALGSAQVLVVEPAVAGSGALkTARKGTGQYEITINGLAAHAGNNPEEGISAVQEMAH 91
Cdd:PRK07473  138 ITVLFTPDEEVGTPSTRDLIEAEAARNKYVLVPEPGRPDNGVV-TGRYAIARFNLEATGRPSHAGATLSEGRSAIREMAR 216
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2744372630  92 QIMFLHSLNAPErgTTVNVGIARGGNRINVVADKAVLGIDTRVTSEAEAERIHAEISQITPHLAGIKLDISGAQSRPPMR 171
Cdd:PRK07473  217 QILAIDAMTTED--CTFSVGIVHGGQWVNCVATTCTGEALSMAKRQADLDRGVARMLALSGTEDDVTFTVTRGVTRPVWE 294
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2744372630 172 QTPESLVLMERAQQVAEQLGFAVEGKAVGGGSDGNFTAALGIPTLDGLGATGAGIHARHEHIIIADIAPRAALVAGLIL 250
Cdd:PRK07473  295 PDAGTMALYEKARAIAGQLGLSLPHGSAGGGSDGNFTGAMGIPTLDGLGVRGADYHTLNEHIEVDSLAERGRLMAGLLA 373
Peptidase_M20 pfam01546
Peptidase family M20/M25/M40; This family includes a range of zinc metallopeptidases belonging ...
2-250 5.32e-25

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: 100.88  E-value: 5.32e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2744372630   2 QHHDLLAGKR-IVFLCGSDEEVGSPSSSAWLSHHALGSAQV------LVVEPAVAGSGA---LKTARKGTGQYEITINGL 71
Cdd:pfam01546  48 ALKEEGLKKGtVKLLFQPDEEGGMGGARALIEDGLLEREKVdavfglHIGEPTLLEGGIaigVVTGHRGSLRFRVTVKGK 127
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2744372630  72 AAHAGNnPEEGISAVQEMAHQIMFLHSLNAPERG-------TTVNVGIARGGnrINVVADKAVLGIDTRVTSEAEAERIH 144
Cdd:pfam01546 128 GGHAST-PHLGVNAIVAAARLILALQDIVSRNVDpldpavvTVGNITGIPGG--VNVIPGEAELKGDIRLLPGEDLEELE 204
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2744372630 145 AEISQITPHLA---GIKLDISGAQSRPPMRQTPESLVlmERAQQVAEQL-GFAVEGKAVG--GGSDGNFTAaLGIP-TLD 217
Cdd:pfam01546 205 ERIREILEAIAaayGVKVEVEYVEGGAPPLVNDSPLV--AALREAAKELfGLKVELIVSGsmGGTDAAFFL-LGVPpTVV 281
                         250       260       270
                  ....*....|....*....|....*....|...
gi 2744372630 218 GLGATGAGIHARHEHIIIADIAPRAALVAGLIL 250
Cdd:pfam01546 282 FFGPGSGLAHSPNEYVDLDDLEKGAKVLARLLL 314
M20_ArgE_DapE-like cd08659
Peptidase M20 acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase (ArgE/DapE) ...
4-249 6.64e-23

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: 95.83  E-value: 6.64e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2744372630   4 HDLLAGkRIVFLCGSDEEVGSPSSSAWLSHHALGSAQVLVV-EPavaGSGALKTARKGTGQYEITINGLAAHAGNnPEEG 82
Cdd:cd08659   114 GALLGG-RVALLATVDEEVGSDGARALLEAGYADRLDALIVgEP---TGLDVVYAHKGSLWLRVTVHGKAAHSSM-PELG 188
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2744372630  83 ISAVQEMAHQIMFLHSL--NAPER----GTTVNVGIARGGNRINVVADKAVLGIDTRVTSEAEAERIHAEISQITPHlAG 156
Cdd:cd08659   189 VNAIYALADFLAELRTLfeELPAHpllgPPTLNVGVINGGTQVNSIPDEATLRVDIRLVPGETNEGVIARLEAILEE-HE 267
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2744372630 157 IKLDISGAQSRPPMRQTPESLVLMERAQQVAEQLGFAVEGKAVGGGSDG-NFTAALGIPTLdGLG-ATGAGIHARHEHII 234
Cdd:cd08659   268 AKLTVEVSLDGDPPFFTDPDHPLVQALQAAARALGGDPVVRPFTGTTDAsYFAKDLGFPVV-VYGpGDLALAHQPDEYVS 346
                         250
                  ....*....|....*
gi 2744372630 235 IADIAPRAALVAGLI 249
Cdd:cd08659   347 LEDLLRAAEIYKEII 361
PepD2 COG2195
Di- or tripeptidase [Amino acid transport and metabolism];
63-237 7.07e-22

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


Pssm-ID: 441798 [Multi-domain]  Cd Length: 364  Bit Score: 92.81  E-value: 7.07e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2744372630  63 QYEITINGLAAHAGNNPEEGISAVQEMAHQIMFLHSLNAPERgTTVNVGIARGGNRINVVADKAVLGIDTRVTSEAEAER 142
Cdd:COG2195   173 DAKITIKGKGGHSGDAKEKMINAIKLAARFLAALPLGRIPEE-TEGNEGFIHGGSATNAIPREAEAVYIIRDHDREKLEA 251
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2744372630 143 IHAEISQITPHLAG------IKLDISGaqSRPPMRQTPESLVLmERAQQVAEQLGFAVEGKAVGGGSDGNFTAALGIPTL 216
Cdd:COG2195   252 RKAELEEAFEEENAkygvgvVEVEIED--QYPNWKPEPDSPIV-DLAKEAYEELGIEPKIKPIRGGLDGGILSFKGLPTP 328
                         170       180
                  ....*....|....*....|.
gi 2744372630 217 DgLGATGAGIHARHEHIIIAD 237
Cdd:COG2195   329 N-LGPGGHNFHSPDERVSIES 348
M20_peptT_like cd05683
M20 Peptidase T like enzymes specifically cleave tripeptides; Peptidase M20 family, PeptT ...
67-249 2.64e-21

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: 91.36  E-value: 2.64e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2744372630  67 TINGLAAHAGNNPEEGISAVQEMAHQIMFLhSLNAPERGTTVNVGIARGGNRINVVADKAVLGIDTRVTSEAEAERIHAE 146
Cdd:cd05683   184 KIYGKTAHAGTSPEKGISAINIAAKAISNM-KLGRIDEETTANIGKFQGGTATNIVTDEVNIEAEARSLDEEKLDAQVKH 262
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2744372630 147 ISQITPHLA---GIKLDISGAQSRPPMRQTPESLVLmERAQQVAEQLGFAVEGKAVGGGSDGNFTAALGIPTLDgLGATG 223
Cdd:cd05683   263 MKETFETTAkekGAHAEVEVETSYPGFKINEDEEVV-KLAKRAANNLGLEINTTYSGGGSDANIINGLGIPTVN-LGIGY 340
                         170       180
                  ....*....|....*....|....*.
gi 2744372630 224 AGIHARHEHIIIADIAPRAALVAGLI 249
Cdd:cd05683   341 ENIHTTNERIPIEDLYDTAVLVVEII 366
M20_ArgE_DapE-like cd08011
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ...
12-238 4.03e-16

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: 76.66  E-value: 4.03e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2744372630  12 IVFLCGSDEEVGSPSSSAWLSHHALGS-AQVLVVEPAvaGSGALKTARKGTGQYEITINGLAAHAGNnPEEGISAVQEMA 90
Cdd:cd08011   127 VVLTFVPDEETGGRAGTKYLLEKVRIKpNDVLIGEPS--GSDNIRIGEKGLVWVIIEITGKPAHGSL-PHRGESAVKAAM 203
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2744372630  91 HQIMFLHSLNApergtTVNVGIARGGNRINVVADKAVLGIDTRVTSEAEAERIHAEISQITPHLAGIKLDISgAQSRPPM 170
Cdd:cd08011   204 KLIERLYELEK-----TVNPGVIKGGVKVNLVPDYCEFSVDIRLPPGISTDEVLSRIIDHLDSIEEVSFEIK-SFYSPTV 277
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2744372630 171 RQTPESLV-LMERAQQvaEQLGfaVEGKAV--GGGSDGNFTAALGIPTLD-GLGATGAgIHARHEHIIIADI 238
Cdd:cd08011   278 SNPDSEIVkKTEEAIT--EVLG--IRPKEVisVGASDARFYRNAGIPAIVyGPGRLGQ-MHAPNEYVEIDEL 344
M20_ArgE cd03894
M20 Peptidase acetylornithine deacetylase; Peptidase M20 family, acetylornithine deacetylase ...
12-216 8.47e-14

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: 69.93  E-value: 8.47e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2744372630  12 IVFLCGSDEEVGSPSSSAWLSHhalGSAQVLVVEPAVAG---SGALKTARKGTGQYEITINGLAAHAgNNPEEGISAVQE 88
Cdd:cd03894   121 LHLAFSYDEEVGCLGVRHLIAA---LAARGGRPDAAIVGeptSLQPVVAHKGIASYRIRVRGRAAHS-SLPPLGVNAIEA 196
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2744372630  89 MAHQIMFLHSLNAPER-----------GTTVNVGIARGGNRINVVADKAVLGIDTRVTSEAEAERIHAEISQItphlAGI 157
Cdd:cd03894   197 AARLIGKLRELADRLApglrdppfdppYPTLNVGLIHGGNAVNIVPAECEFEFEFRPLPGEDPEAIDARLRDY----AEA 272
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2744372630 158 KLDISGAQ------SRPPMRQTPESLVLMERAQQVAEQLGFAvegkAVGGGSDGNFTAALGIPTL 216
Cdd:cd03894   273 LLEFPEAGieveplFEVPGLETDEDAPLVRLAAALAGDNKVR----TVAYGTEAGLFQRAGIPTV 333
M20_like cd02697
M20 Zn-peptidases include exopeptidases; Peptidase M20 family; uncharacterized subfamily. ...
19-216 6.20e-13

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


Pssm-ID: 349869 [Multi-domain]  Cd Length: 394  Bit Score: 67.58  E-value: 6.20e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2744372630  19 DEEVGSPSSSAWLSHHALGSAQVLVvepAVAGSGALKTARKGTGQYEITINGLAAHAGNnPEEGISAVQEMAHQIMFLHS 98
Cdd:cd02697   145 DEEFGGELGPGWLLRQGLTKPDLLI---AAGFSYEVVTAHNGCLQMEVTVHGKQAHAAI-PDTGVDALQGAVAILNALYA 220
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2744372630  99 LNAPERGTT----------VNVGIARGGNRINVVADKAVLGIDTRVTSEAEAERIHAEISQITPHLA----GIKLDISGA 164
Cdd:cd02697   221 LNAQYRQVSsqvegithpyLNVGRIEGGTNTNVVPGKVTFKLDRRMIPEENPVEVEAEIRRVIADAAasmpGISVDIRRL 300
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2744372630 165 QSRPPMRQTPESLVLMERAQQVAEQL-GFAVEGKAVGGGSDGNFTAALGIPTL 216
Cdd:cd02697   301 LLANSMRPLPGNAPLVEAIQTHGEAVfGEPVPAMGTPLYTDVRLYAEAGIPGV 353
M20_dimer pfam07687
Peptidase dimerization domain; This domain consists of 4 beta strands and two alpha helices ...
56-150 7.40e-13

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: 63.13  E-value: 7.40e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2744372630  56 TARKGTGQYEITINGLAAHAGNnPEEGISAVQEMAHQIMFLHSLNAPER----GTTVNVGIARGGNRINVVADKAVLGID 131
Cdd:pfam07687   1 IGHKGLAGGHLTVKGKAGHSGA-PGKGVNAIKLLARLLAELPAEYGDIGfdfpRTTLNITGIEGGTATNVIPAEAEAKFD 79
                          90
                  ....*....|....*....
gi 2744372630 132 TRVTSEAEAERIHAEISQI 150
Cdd:pfam07687  80 IRLLPGEDLEELLEEIEAI 98
PepT-like TIGR01883
peptidase T-like protein; This model represents a clade of enzymes closely related to ...
67-249 1.50e-12

peptidase T-like protein; This model represents a clade of enzymes closely related to Peptidase T, an aminotripeptidase found in bacteria. This clade consists of gram positive bacteria of which several additionally contain a Peptidase T gene.


Pssm-ID: 162579 [Multi-domain]  Cd Length: 361  Bit Score: 66.50  E-value: 1.50e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2744372630  67 TINGLAAHAGNNPEEGISA--VQEMAHQIMFLHSLnapERGTTVNVGIARGGNRINVVADKAVLGIDTRVTSEAEAErih 144
Cdd:TIGR01883 178 TIAGKDAHAGLVPEDGISAisVARMAIHAMRLGRI---DEETTANIGSFSGGVNTNIVQDEQLIVAEARSLSFRKAE--- 251
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2744372630 145 AEISQI------TPHLAGIKLDISGAQSRPPMRQTPESlVLMERAQQVAEQLGFAVEGKAVGGGSDGNFTAALGIPTLDg 218
Cdd:TIGR01883 252 AQVQTMrerfeqAAEKYGATLEEETRLIYEGFKIHPQH-PLMNIFKKAAKKIGLKTSEIFSGGGSDANVLNEKGVPTVN- 329
                         170       180       190
                  ....*....|....*....|....*....|.
gi 2744372630 219 LGATGAGIHARHEHIIIADIAPRAALVAGLI 249
Cdd:TIGR01883 330 LSAGYVHAHTEKETISIEQLVKLAELVIALA 360
AbgB COG1473
Metal-dependent amidase/aminoacylase/carboxypeptidase [General function prediction only]; ...
60-190 1.72e-11

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: 63.21  E-value: 1.72e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2744372630  60 GTGQYEITINGLAAHAGnNPEEGISAVQEMAHQIMFLHSLNA----PERGTTVNVGIARGGNRINVVADKAVLGIDTRVT 135
Cdd:COG1473   182 AADSFEITIKGKGGHAA-APHLGIDPIVAAAQIVTALQTIVSrnvdPLDPAVVTVGIIHGGTAPNVIPDEAELEGTVRTF 260
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2744372630 136 SEAEAERIHAEISQITPHLA---GIKLDISGAQSRPPMRQTPEslvLMERAQQVAEQL 190
Cdd:COG1473   261 DPEVRELLEERIERIAEGIAaayGATAEVEYLRGYPPTVNDPE---LTELAREAAREV 315
M20_ArgE_DapE-like cd08013
M20 peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ...
33-249 2.42e-11

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 fungal and bacterial, and have been inferred by homology as being related to both ArgE and DapE.


Pssm-ID: 349935 [Multi-domain]  Cd Length: 379  Bit Score: 62.88  E-value: 2.42e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2744372630  33 HHALGSAQVL----------VVEPAvagSGALKTARKGTGQYEITINGLAAHaGNNPEEGISAVQEMAHQIMFLHSLNA- 101
Cdd:cd08013   140 DASLGTQEVLaagwradaaiVTEPT---NLQIIHAHKGFVWFEVDIHGRAAH-GSRPDLGVDAILKAGYFLVALEEYQQe 215
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2744372630 102 -PERGT-------TVNVGIARGGNRINVVADKAVLGIDTRVTSEAEAERIHAEISQITPHLAGIKLDISGAQ-----SRP 168
Cdd:cd08013   216 lPERPVdpllgraSVHASLIKGGEEPSSYPARCTLTIERRTIPGETDESVLAELTAILGELAQTVPNFSYREpritlSRP 295
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2744372630 169 PMRQTPESLVLMERAQQVAEQLGFAVEGKAVGGGSDGNFTAALGIPTLDgLGATGAGIHARHEHIIIADIAPRAALVAGL 248
Cdd:cd08013   296 PFEVPKEHPFVQLVAAHAAKVLGEAPQIRSETFWTDAALLAEAGIPSVV-FGPSGAGLHAKEEWVDVESIRQLREVLSAV 374

                  .
gi 2744372630 249 I 249
Cdd:cd08013   375 V 375
PRK08651 PRK08651
succinyl-diaminopimelate desuccinylase; Reviewed
19-238 1.33e-10

succinyl-diaminopimelate desuccinylase; Reviewed


Pssm-ID: 236323 [Multi-domain]  Cd Length: 394  Bit Score: 60.77  E-value: 1.33e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2744372630  19 DEEVGSPSSSAWLSHHALGSAQVLVVEPAvaGSGALKTARKGTGQYEITINGLAAHAGNnPEEGISAVQEMAHQIMFLHS 98
Cdd:PRK08651  144 DEETGGTGTGYLVEEGKVTPDYVIVGEPS--GLDNICIGHRGLVWGVVKVYGKQAHAST-PWLGINAFEAAAKIAERLKS 220
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2744372630  99 LNA---------PERGT--TVNVG--IARGGNRINVVADKAVLGIDTRV----TSEAEAERIHAEISQITPHLaGIKLDI 161
Cdd:PRK08651  221 SLStikskyeydDERGAkpTVTLGgpTVEGGTKTNIVPGYCAFSIDRRLipeeTAEEVRDELEALLDEVAPEL-GIEVEF 299
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2744372630 162 SGAQSRPPMRQTPES-LV-LMERAqqVAEQLGFAVEGKAVGGGSDGNFTAALGIPTLD-GLGATGAgIHARHEHIIIADI 238
Cdd:PRK08651  300 EITPFSEAFVTDPDSeLVkALREA--IREVLGVEPKKTISLGGTDARFFGAKGIPTVVyGPGELEL-AHAPDEYVEVKDV 376
PRK08588 PRK08588
succinyl-diaminopimelate desuccinylase; Reviewed
5-204 7.72e-10

succinyl-diaminopimelate desuccinylase; Reviewed


Pssm-ID: 181490 [Multi-domain]  Cd Length: 377  Bit Score: 58.36  E-value: 7.72e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2744372630   5 DLLAGkRIVFLCGSDEEVGSPSSSAWLSHHALGSAQVLVV-EPAvagSGALKTARKGTGQYEITINGLAAHAgNNPEEGI 83
Cdd:PRK08588  120 QLLNG-TIRLLATAGEEVGELGAKQLTEKGYADDLDALIIgEPS---GHGIVYAHKGSMDYKVTSTGKAAHS-SMPELGV 194
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2744372630  84 SAVQEMahqIMFLHSLN---------APERGTTV-NVGIARGGNRINVVADKAVLGIDTRVTSEAEAERIHAEISQITPH 153
Cdd:PRK08588  195 NAIDPL---LEFYNEQKeyfdsikkhNPYLGGLThVVTIINGGEQVNSVPDEAELEFNIRTIPEYDNDQVISLLQEIINE 271
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2744372630 154 L-----AGIKLDIsgAQSRPPMRQTPESLvLMERAQQVAEQ-LGFAVEGKAVGGGSD 204
Cdd:PRK08588  272 VnqngaAQLSLDI--YSNHRPVASDKDSK-LVQLAKDVAKSyVGQDIPLSAIPGATD 325
M20_Acy1 cd03886
M20 Peptidase Aminoacylase 1 family; Peptidase M20 family, Aminoacylase 1 (ACY1; hippuricase; ...
60-209 1.20e-09

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: 58.00  E-value: 1.20e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2744372630  60 GTGQYEITINGLAAHAGNnPEEGISAVQEMAHQIMFLHSLNA----PERGTTVNVGIARGGNRINVVADKAVLGIDTRVT 135
Cdd:cd03886   170 SADEFEITVKGKGGHGAS-PHLGVDPIVAAAQIVLALQTVVSreldPLEPAVVTVGKFHAGTAFNVIPDTAVLEGTIRTF 248
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2744372630 136 SEAEAERIHAEISQI---TPHLAGIKLDISGAQSRPPMRQTPESLVLMERAqqVAEQLGF--AVEGKAVGGGSD-GNFTA 209
Cdd:cd03886   249 DPEVREALEARIKRLaegIAAAYGATVELEYGYGYPAVINDPELTELVREA--AKELLGEeaVVEPEPVMGSEDfAYYLE 326
amidohydrolases TIGR01891
amidohydrolase; This model represents a subfamily of amidohydrolases which are a subset of ...
60-232 1.53e-09

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: 57.35  E-value: 1.53e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2744372630  60 GTGQYEITINGLAAHAGNnPEEGISAV---QEMAHQIMFLHSLNA-PERGTTVNVGIARGGNRINVVADKAVLGIDTRVT 135
Cdd:TIGR01891 169 AADKFEVTIHGKGAHAAR-PHLGRDALdaaAQLVVALQQIVSRNVdPSRPAVVSVGIIEAGGAPNVIPDKASMSGTVRSL 247
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2744372630 136 SEAEAERIHAEISQITPHLA---GIKLDISGAQSRPPMRQTPE-SLVLMERAQQVAEQLGFAVEGKAVGGGSD-GNFTAA 210
Cdd:TIGR01891 248 DPEVRDQIIDRIERIVEGAAamyGAKVELNYDRGLPAVTNDPAlTQILKEVARHVVGPENVAEDPEVTMGSEDfAYYSQK 327
                         170       180
                  ....*....|....*....|...
gi 2744372630 211 L-GIPTLDGLGATGAGIHARHEH 232
Cdd:TIGR01891 328 VpGAFFFLGIGNEGTGLSHPLHH 350
M20_Acy1_IAAspH cd05665
M20 Peptidases aminoacyclase-1 indole-3-acetic-L-aspartic acid hydrolase; Peptidase M20 family, ...
61-133 1.51e-08

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: 54.63  E-value: 1.51e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2744372630  61 TGQYEITINGLAAHAGNNPEEGISAVQEMAHQIMFLHSLnAPERG--TTVNVGIARGGNRINVVADKAVLGIDTR 133
Cdd:cd05665   216 TTKLDARFTGVSAHAGAAPEDGRNALLAAATAALNLHAI-PRHGEgaTRINVGVLGAGEGRNVIPASAELQVETR 289
M20_peptidase_T cd05645
M20 Peptidase T specifically cleaves tripeptides; Peptidase M20 family, Peptidase T (PepT; ...
12-249 2.07e-08

M20 Peptidase T specifically cleaves tripeptides; Peptidase M20 family, Peptidase T (PepT; tripeptide aminopeptidase; tripeptidase) subfamily and similar proteins. PepT acts only on tripeptide substrates, and is thus termed 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: 349897 [Multi-domain]  Cd Length: 400  Bit Score: 54.30  E-value: 2.07e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2744372630  12 IVFLCGSDEEVGSPSSSawLSHHALGSAQVLVVEPAvaGSGALKTARKGTGQYEITINGLAAHAGNNPEEGISAVQEMAH 91
Cdd:cd05645   162 IEVAFTPDEEVGKGAKH--FDVEAFTAKWAYTVDGG--GVGELEFENFNAASVNIKIVGNNVHPGTAKGVGVNALSLAAR 237
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2744372630  92 QIMFLHSLNAPE----RGTTVNVGIARGGnrinvvADKAVLGIDTRVTSEAEAERIHAEISQITPHLA-----GIKLDIS 162
Cdd:cd05645   238 IHAEVPADESPEgtegYEGFYHLASFKGT------VDRAQIHYIIRDFDRKQFEARKRK*KEIAKKVGkglhpDCYIELV 311
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2744372630 163 GAQSRPPMRQT-PESLVLMERAQQVAEQLGFAVEGKAVGGGSDGNFTAALGIPTLDgLGATGAGIHARHEHIIIADIAPR 241
Cdd:cd05645   312 IEDSYYNFREKvVEHPHILDIAQQAARDCGITPELKPIRGGTDGAQLSFHGLPCPN-LFTGGYNYHGKHEFVTLEGLEKA 390

                  ....*...
gi 2744372630 242 AALVAGLI 249
Cdd:cd05645   391 VQVIVRIA 398
PRK12890 PRK12890
allantoate amidohydrolase; Reviewed
64-239 2.67e-08

allantoate amidohydrolase; Reviewed


Pssm-ID: 237248 [Multi-domain]  Cd Length: 414  Bit Score: 53.75  E-value: 2.67e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2744372630  64 YEITINGLAAHAGNNPEEGIS-AVQEMAHQIMFLHSLNAP-ERGTTVNVG-IARGGNRINVVADKAVLGIDTRVTSEAEA 140
Cdd:PRK12890  219 QAVTVEGEANHAGTTPMDLRRdALVAAAELVTAMERRARAlLHDLVATVGrLDVEPNAINVVPGRVVFTLDLRSPDDAVL 298
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2744372630 141 ERIHAEISQITPHLA---GIKLDISGAQSRPPmrqTPESLVLMERAQQVAEQLGFAVEGKAVGGGSDGNFTAALG----- 212
Cdd:PRK12890  299 EAAEAALLAELEAIAaarGVRIELERLSRSEP---VPCDPALVDAVEAAAARLGYPSRRMPSGAGHDAAAIARIGpsami 375
                         170       180
                  ....*....|....*....|....*...
gi 2744372630 213 -IPTLDGLGatgagiHARHEHIIIADIA 239
Cdd:PRK12890  376 fVPCRGGIS------HNPEEAMDPEDLA 397
M20_Acy1-like cd08019
M20 Peptidase aminoacylase 1 subfamily; Peptidase M20 family, uncharacterized subfamily of ...
60-187 3.03e-08

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


Pssm-ID: 349940 [Multi-domain]  Cd Length: 372  Bit Score: 53.49  E-value: 3.03e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2744372630  60 GTGQYEITINGLAAHaGNNPEEGISAVQEMAHQIMFLHSL----NAPERGTTVNVGIARGGNRINVVADKAVLGIDTRVT 135
Cdd:cd08019   167 SADIFKIEVKGKGGH-GSMPHQGIDAVLAAASIVMNLQSIvsreIDPLEPVVVTVGKLNSGTRFNVIADEAKIEGTLRTF 245
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2744372630 136 SEAEAERIHAEISQITPHLA---GIKLDISGAQSRPPMRQTPEslvLMERAQQVA 187
Cdd:cd08019   246 NPETREKTPEIIERIAKHTAasyGAEAELTYGAATPPVINDEK---LSKIARQAA 297
M20_PAAh_like cd03896
M20 Peptidases, Poly(aspartic acid) hydrolase-like proteins; Peptidase M20 family, Poly ...
31-251 2.98e-07

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: 50.56  E-value: 2.98e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2744372630  31 LSHHALGSAQVLVVEPAvagSGALKTARKGTGQYEITINGLAAHAGNnPEEGISAVQEMAHQIMFLHSLNAPER-GTTVN 109
Cdd:cd03896   136 LSAHGARLDYFVVAEGT---DGVPHTGAVGSKRFRITTVGPGGHSYG-AFGSPSAIVAMAKLVEALYEWAAPYVpKTTFA 211
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2744372630 110 VGIARGGNRINVVADKAVLGIDTRVTSEAE----AERIHAEISQITPHLAGIKLDISGAQSRPPMRQTPESLVL--MERA 183
Cdd:cd03896   212 AIRGGGGTSVNRIANLCSMYLDIRSNPDAEladvQREVEAVVSKLAAKHLRVKARVKPVGDRPGGEAQGTEPLVnaAVAA 291
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2744372630 184 -QQVAEQLGFAvegkavGGGSDGNFTAALGIPTLD-GLGAtGAGIHARHEHIIIADIAPRAALVAGLILG 251
Cdd:cd03896   292 hREVGGDPRPG------SSSTDANPANSLGIPAVTyGLGR-GGNAHRGDEYVLKDDMLKGAKAYLMLAAA 354
M20_bAS cd03884
M20 Peptidase beta-alanine synthase, an amidohydrolase; Peptidase M20 family, beta-alanine ...
60-250 6.60e-07

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: 49.44  E-value: 6.60e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2744372630  60 GTGQYEITINGLAAHAGNNP-----------EEGISAVQEMAHQImflhslNAPERGTTVNVGIARGGnrINVVADKAVL 128
Cdd:cd03884   205 GQRWLEVTVTGEAGHAGTTPmalrrdallaaAELILAVEEIALEH------GDDLVATVGRIEVKPNA--VNVIPGEVEF 276
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2744372630 129 GIDTRVTSEAEAERIHAEISQITPHLA---GIKLDISGAQSRPPMRQTPEslvLMERAQQVAEQLGFAVEGKAVGGGSDG 205
Cdd:cd03884   277 TLDLRHPDDAVLDAMVERIRAEAEAIAaerGVEVEVERLWDSPPVPFDPE---LVAALEAAAEALGLSYRRMPSGAGHDA 353
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2744372630 206 NFTAALG------IPTLDGLGatgagiHARHEHIIIADIAPRAALVAGLIL 250
Cdd:cd03884   354 MFMARICptamifVPSRDGIS------HNPAEYTSPEDLAAGVQVLLHALL 398
PRK13004 PRK13004
YgeY family selenium metabolism-linked hydrolase;
41-150 6.97e-07

YgeY family selenium metabolism-linked hydrolase;


Pssm-ID: 183836 [Multi-domain]  Cd Length: 399  Bit Score: 49.55  E-value: 6.97e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2744372630  41 VLVVEPAvagSGALKTARKGTGQYEITINGLAAHAGNnPEEGISAVQEMAHQIMFLHSLNAPE-------RGTTVNVGIA 113
Cdd:PRK13004  166 VVITEPT---DLNIYRGQRGRMEIRVETKGVSCHGSA-PERGDNAIYKMAPILNELEELNPNLkedpflgKGTLTVSDIF 241
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 2744372630 114 RGGNRINVVADKAVLGIDTRVTSEAEAERIHAEISQI 150
Cdd:PRK13004  242 STSPSRCAVPDSCAISIDRRLTVGETWESVLAEIRAL 278
PRK12893 PRK12893
Zn-dependent hydrolase;
56-246 8.95e-07

Zn-dependent hydrolase;


Pssm-ID: 237250 [Multi-domain]  Cd Length: 412  Bit Score: 49.11  E-value: 8.95e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2744372630  56 TARKGTGQYEITINGLAAHAGNNP-EEGISAVQEMAHQIMFLHSLNAPERGTTV-NVG-IARGGNRINVVADKAVLGIDT 132
Cdd:PRK12893  209 TGIQGIRWLEVTVEGQAAHAGTTPmAMRRDALVAAARIILAVERIAAALAPDGVaTVGrLRVEPNSRNVIPGKVVFTVDI 288
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2744372630 133 RVTSEAEAERIHAEISQITPHLA---GIKLDISGAQSRPPMRQTPEslvLMERAQQVAEQLGFAVEGKAVGGGSDGNF-- 207
Cdd:PRK12893  289 RHPDDARLDAMEAALRAACAKIAaarGVQVTVETVWDFPPVPFDPA---LVALVEAAAEALGLSHMRMVSGAGHDAMFla 365
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 2744372630 208 ----TAALGIPTLDGLGatgagiHARHEHIIIADIAPRAALVA 246
Cdd:PRK12893  366 rvapAAMIFVPCRGGIS------HNEAEDTEPADLAAGANVLL 402
PRK08652 PRK08652
acetylornithine deacetylase; Provisional
12-150 1.69e-06

acetylornithine deacetylase; Provisional


Pssm-ID: 236324 [Multi-domain]  Cd Length: 347  Bit Score: 48.22  E-value: 1.69e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2744372630  12 IVFLcgSDEEVGSPSSSAWLShhALGSAQVLVVEPAvagSGALKTARKGTGQYEITINGLAAHaGNNPEEGISAVQEMAH 91
Cdd:PRK08652  113 IAFV--SDEEEGGRGSALFAE--RYRPKMAIVLEPT---DLKVAIAHYGNLEAYVEVKGKPSH-GACPESGVNAIEKAFE 184
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2744372630  92 QIMFLHSLN-APERGTTVNVGIAR--GGNRINVVADKAVLGIDTRVTSEAEAERIHAEISQI 150
Cdd:PRK08652  185 MLEKLKELLkALGKYFDPHIGIQEiiGGSPEYSIPALCRLRLDARIPPEVEVEDVLDEIDPI 246
Ac-peptdase-euk TIGR01880
N-acyl-L-amino-acid amidohydrolase; This model represents a family of eukaryotic ...
106-216 2.18e-06

N-acyl-L-amino-acid amidohydrolase; This model represents a family of eukaryotic N-acyl-L-amino-acid amidohydrolases active on fatty acid and acetyl amides of L-amino acids.


Pssm-ID: 273850 [Multi-domain]  Cd Length: 400  Bit Score: 48.25  E-value: 2.18e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2744372630 106 TTVNVGIARGGNRINVVADKAVLGIDTRVTSEAEAERIHAEISQ-ITPHLAGIKLDISGAQSRPPMRQTPESLVLMERAQ 184
Cdd:TIGR01880 248 TSVNLTKLKGGVQSNVIPSEAEAGFDIRLAPSVDFEEMENRLDEwCADAGEGVTYEFSQHSGKPLVTPHDDSNPWWVAFK 327
                          90       100       110
                  ....*....|....*....|....*....|..
gi 2744372630 185 QVAEQLGFAVEGKAVGGGSDGNFTAALGIPTL 216
Cdd:TIGR01880 328 DAVKEMGCTFKPEILPGSTDSRYIRAAGVPAL 359
M20_Acy1-like cd05664
M20 Peptidase aminoacylase 1 subfamily; Peptidase M20 family, Uncharacterized subfamily of ...
44-215 4.36e-06

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: 47.33  E-value: 4.36e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2744372630  44 VEPAVAGSGALKTARKGTG--QYEITINGLAAHaGNNPEEGISAVQEMAHQIMFLHSL----NAPERGTTVNVGIARGGN 117
Cdd:cd05664   162 VMPGPAGTVGTRPGRFLSAadSLDITIFGRGGH-GSMPHLTIDPVVMAASIVTRLQTIvsreVDPQEFAVVTVGSIQAGS 240
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2744372630 118 RINVVADKAVLGIDTRVTSEAEAERIHAEISQITPHLAgiklDISGAQSRP---PMRQTPESLVLMERAQQVAEQLG--- 191
Cdd:cd05664   241 AENIIPDEAELKLNVRTFDPEVREKVLNAIKRIVRAEC----AASGAPKPPeftYTDSFPATVNDEDATARLAAAFReyf 316
                         170       180
                  ....*....|....*....|....*...
gi 2744372630 192 ---FAVEGKAVGGGSD-GNFTAALGIPT 215
Cdd:cd05664   317 gedRVVEVPPVSASEDfSILATAFGVPS 344
M20_ArgE_DapE-like_fungal cd05652
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ...
52-154 5.33e-06

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 fungal, and have been inferred by similarity as being related to both ArgE and DapE.


Pssm-ID: 349903 [Multi-domain]  Cd Length: 340  Bit Score: 46.88  E-value: 5.33e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2744372630  52 GALKTARKGTGQYEITINGLAAHAGNnPEEGISAVQEMA---HQIMFLHSLNAPERG-TTVNVGIARGGNRINVVADKAV 127
Cdd:cd05652   155 LKLASGHKGMLGFKLTAKGKAGHSGY-PWLGISAIEILVealVKLIDADLPSSELLGpTTLNIGRISGGVAANVVPAAAE 233
                          90       100       110
                  ....*....|....*....|....*....|..
gi 2744372630 128 LGIDTRVTSEAE-----AERIHAEISQITPHL 154
Cdd:cd05652   234 ASVAIRLAAGPPevkdiVKEAVAGILTDTEDI 265
M20_DapE_proteobac cd03891
M20 Peptidase proteobacterial DapE encoded N-succinyl-L,L-diaminopimelic acid desuccinylase; ...
11-238 6.16e-05

M20 Peptidase proteobacterial DapE encoded N-succinyl-L,L-diaminopimelic acid desuccinylase; Peptidase M20 family, proteobacterial DapE encoded N-succinyl-L,L-diaminopimelic acid desuccinylase (DapE; aspartyl dipeptidase; succinyl-diaminopimelate desuccinylase) subfamily. DapE catalyzes the hydrolysis of N-succinyl-L,L-diaminopimelate (L,L-SDAP) to L,L-diaminopimelate and succinate. It has been shown that DapE is essential for cell growth and proliferation. DapEs have been purified from Escherichia coli and Haemophilus influenzae, while the genes that encode for DapEs have been sequenced from several bacterial sources such as Corynebacterium glutamicum, Helicobacter pylori, Neisseria meningitidis and Mycobacterium tuberculosis. DapE is a small, dimeric enzyme that requires two zinc atoms per molecule for full enzymatic activity. All of the amino acids that function as metal binding ligands are strictly conserved in DapE.


Pssm-ID: 349886 [Multi-domain]  Cd Length: 366  Bit Score: 43.65  E-value: 6.16e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2744372630  11 RIVFLCGSDEE-------------------------VGSPSSSawlshHALGSAqvlvvepavagsgaLKTARKGTGQYE 65
Cdd:cd03891   120 SISFLITSDEEgpaidgtkkvlewlkargekidyciVGEPTSE-----KKLGDT--------------IKIGRRGSLNGK 180
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2744372630  66 ITINGLAAHAG-----NNP-EEGISAVQEMAHQImfLHSLNAPERGTTVNVGIARGGNRI-NVVADKAVLGIDTRVTSEA 138
Cdd:cd03891   181 LTIKGKQGHVAyphlaDNPiHLLAPILAELTATV--LDEGNEFFPPSSLQITNIDVGNGAtNVIPGELKAKFNIRFNDEH 258
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2744372630 139 EAERIHAEISQItphLAGIKLD--ISGAQSRPPMRQTPESLV-LMERAqqVAEQLGFAVEGKAVGGGSDGNFTAALGIPT 215
Cdd:cd03891   259 TGESLKARIEAI---LDKHGLDydLEWKLSGEPFLTKPGKLVdAVSAA--IKEVTGITPELSTSGGTSDARFIASYGCPV 333
                         250       260
                  ....*....|....*....|...
gi 2744372630 216 LDgLGATGAGIHARHEHIIIADI 238
Cdd:cd03891   334 VE-FGLVNATIHKVNERVSVADL 355
M20_ArgE_DapE-like cd05649
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ...
41-147 6.24e-05

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 bacterial and archaeal, and have been inferred by homology as being related to both ArgE and DapE.


Pssm-ID: 349900 [Multi-domain]  Cd Length: 381  Bit Score: 43.56  E-value: 6.24e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2744372630  41 VLVVEPAvagSGALKTARKGTGQYEITINGLAAHaGNNPEEGISAVQEMAHQIMFLHSLNA--PE-----RGTTVNVGIA 113
Cdd:cd05649   150 VVSGEPT---DGNIYRGQRGRMEIRVDTKGVSCH-GSAPERGDNAVYKMADIIQDIRQLNPnfPEapflgRGTLTVTDIF 225
                          90       100       110
                  ....*....|....*....|....*....|....
gi 2744372630 114 RGGNRINVVADKAVLGIDTRVTSEAEAERIHAEI 147
Cdd:cd05649   226 STSPSRCAVPDSCRISIDRRLTVGETWEGCLEEI 259
PRK07522 PRK07522
acetylornithine deacetylase; Provisional
56-216 9.67e-05

acetylornithine deacetylase; Provisional


Pssm-ID: 236039 [Multi-domain]  Cd Length: 385  Bit Score: 42.87  E-value: 9.67e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2744372630  56 TARKGTGQYEITINGLAAHAGNNPEeGISAVQEMAHQIMFLHSLNAPER------------GTTVNVGIARGGNRINVVA 123
Cdd:PRK07522  172 VGHKGKAAYRCTVRGRAAHSSLAPQ-GVNAIEYAARLIAHLRDLADRLAapgpfdalfdppYSTLQTGTIQGGTALNIVP 250
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2744372630 124 DKAVLGIDTRVTSEAEAERIHAEI-----SQITPHL------AGIKLD-ISGAqsrPPMRqTPESLVLMERAQQVAEQLG 191
Cdd:PRK07522  251 AECEFDFEFRNLPGDDPEAILARIrayaeAELLPEMravhpeAAIEFEpLSAY---PGLD-TAEDAAAARLVRALTGDND 326
                         170       180
                  ....*....|....*....|....*
gi 2744372630 192 FAvegkAVGGGSDGNFTAALGIPTL 216
Cdd:PRK07522  327 LR----KVAYGTEAGLFQRAGIPTV 347
M20_Acy1_YhaA-like cd08021
M20 Peptidase aminoacylase 1 subfamily, includes Bacillus subtilis YhaA and Staphylococcus ...
64-204 1.35e-04

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


Pssm-ID: 349941 [Multi-domain]  Cd Length: 384  Bit Score: 42.64  E-value: 1.35e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2744372630  64 YEITINGLAAHAGNnPEEGISAVQEMAHQIMFLHSLNA----PERGTTVNVGIARGGNRINVVADKAVLGIDTRVTSEAE 139
Cdd:cd08021   184 FDITIKGKGGHGSM-PHETVDPIVIAAQIVTALQTIVSrrvdPLDPAVVTIGTFQGGTSFNVIPDTVELKGTVRTFDEEV 262
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2744372630 140 AERIHAEISQITPHLA---GIKLDISGAQSRPPMRQTPESLVLMERAQQVAEQLGFAVEGKAVGGGSD 204
Cdd:cd08021   263 REQVPKRIERIVKGICeayGASYELEYQPGYPVVYNDPEVTELVKKAAKEVLIGVENVEPQLMMGGED 330
M20_yscS_like cd05675
M20 Peptidase, carboxypeptidase yscS-like; Peptidase M20 family, yscS (GlyX-carboxypeptidase, ...
12-233 2.73e-04

M20 Peptidase, carboxypeptidase yscS-like; Peptidase M20 family, yscS (GlyX-carboxypeptidase, CPS1, carboxypeptidase S, carboxypeptidase a, carboxypeptidase yscS, glycine carboxypeptidase)-like subfamily. This group contains proteins that have been uncharacterized to date with similarity to vacuolar proteins involved in nitrogen metabolism which are essential for use of certain peptides that are sole nitrogen sources. YscS releases a C-terminal amino acid from a peptide that has glycine as the penultimate residue. It is synthesized as one polypeptide chain precursor which yields two active precursor molecules after carbohydrate modification in the secretory pathway. The proteolytically unprocessed forms are associated with the membrane, whereas the mature forms of the enzyme are soluble. Enzymes in this subfamily may also cleave intracellularly generated peptides in order to recycle amino acids for protein synthesis.


Pssm-ID: 349924 [Multi-domain]  Cd Length: 431  Bit Score: 41.58  E-value: 2.73e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2744372630  12 IVFLCGSDEEVGSPSSSAWLS-HHA------------LGSAQVLVVEPAVagSGALKTARKGTGQYEITINGLAAHAGN- 77
Cdd:cd05675   131 LVFAFVADEEAGGENGAKWLVdNHPelfdgatfalneGGGGSLPVGKGRR--LYPIQVAEKGIAWMKLTVRGRAGHGSRp 208
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2744372630  78 NPEEGISAVQEMAHQI-------------------------------------------MFLHS---LNAPERgTTVNVG 111
Cdd:cd05675   209 TDDNAITRLAEALRRLgahnfpvrltdetayfaqmaelaggeggalmltavpvldpalaKLGPSaplLNAMLR-NTASPT 287
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2744372630 112 IARGGNRINVVADKAVLGIDTRVTSEAEAERIHAEISQIT--PHLAgikldiSGAQSRPPMRQTPESLVLMERAQQVAEQ 189
Cdd:cd05675   288 MLDAGYATNVLPGRATAEVDCRILPGQSEEEVLDTLDKLLgdPDVS------VEAVHLEPATESPLDSPLVDAMEAAVQA 361
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2744372630 190 lgFAVEGKAV----GGGSDGNFTAALGIPT-------LDGLGATGAGIHARHEHI 233
Cdd:cd05675   362 --VDPGAPVVpymsPGGTDAKYFRRLGIPGygfaplfLPPELDYTGLFHGVDERV 414
M20_Acy1_YxeP-like cd05669
M20 Peptidase aminoacyclase-1 YxeP-like proteins, including YxeP, YtnL, YjiB and HipO2; ...
63-195 4.78e-04

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: 40.74  E-value: 4.78e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2744372630  63 QYEITINGLAAHAGnNPEEGISAVQEMAHQIMFLHSLNA----PERGTTVNVGIARGGNRINVVADKAVLGIDTRVTSEA 138
Cdd:cd05669   174 RFEIEIAGKGAHAA-KPENGVDPIVAASQIINALQTIVSrnisPLESAVVSVTRIHAGNTWNVIPDSAELEGTVRTFDAE 252
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2744372630 139 EAERIHAEISQITPHLA---GIKLDISGAQSRPPMRQTPEslvLMERAQQVAEQLGFAVE 195
Cdd:cd05669   253 VRQLVKERFEQIVEGIAaafGAKIEFKWHSGPPAVINDEE---LTDLASEVAAQAGYEVV 309
M20_AcylaseI_like cd05646
M20 Aminoacylase-I like subfamily; Peptidase M20 family, aminoacylase-I like (AcyI-like; ...
65-216 1.44e-03

M20 Aminoacylase-I like subfamily; Peptidase M20 family, aminoacylase-I like (AcyI-like; acylase I; N-acyl-L-amino-acid amidohydrolase; EC 3.5.1.14) subfamily. Acylase I is involved in the hydrolysis of N-acylated or N-acetylated amino acids (except L-aspartate) and is considered as a potential target of antimicrobial agents. Porcine AcyI is also shown to deacetylate certain quorum-sensing N-acylhomoserine lactones, while the rat enzyme has been implicated in degradation of chemotactic peptides of commensal bacteria. Prokaryotic arginine synthesis usually involves the transfer of an acetyl group to glutamate by ornithine acetyltransferase in order to form ornithine. However, Escherichia coli acetylornithine deacetylase (acetylornithinase, ArgE) (EC 3.5.1.16) catalyzes the deacylation of N2-acetyl-L-ornithine to yield ornithine and acetate. Phylogenetic evidence suggests that the clustering of the arg genes in one continuous sequence pattern arose in an ancestor common to Enterobacteriaceae and Vibrionaceae, where ornithine acetyltransferase was lost and replaced by a deacylase. Elevated levels of serum aminoacylase-1 autoantibody have been seen in the disease progression of chronic hepatitis B (CHB), making ACY1 autoantibody a valuable serum biomarker for discriminating hepatitis B virus (HBV) related liver cirrhosis from CHB.


Pssm-ID: 349898 [Multi-domain]  Cd Length: 391  Bit Score: 39.56  E-value: 1.44e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2744372630  65 EITINGLAAH--------AGNNPEEGISAVQEM-AHQIMFLHSLNAPERG--TTVNVGIARGGNRINVVADKAVLGIDTR 133
Cdd:cd05646   189 VITAPGTPGHgskllentAGEKLRKVIESIMEFrESQKQRLKSNPNLTLGdvTTVNLTMLKGGVQMNVVPSEAEAGFDLR 268
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2744372630 134 VTSEAEAERIHAEISQ-ITPHLAGIKLDIsgAQSRPPMRQTP--ESLVLMERAQQVAEQLGFAVEGKAVGGGSDGNFTAA 210
Cdd:cd05646   269 IPPTVDLEEFEKQIDEwCAEAGRGVTYEF--EQKSPEKDPTSldDSNPWWAAFKKAVKEMGLKLKPEIFPAATDSRYIRA 346

                  ....*.
gi 2744372630 211 LGIPTL 216
Cdd:cd05646   347 LGIPAL 352
PRK12891 PRK12891
allantoate amidohydrolase; Reviewed
56-239 2.33e-03

allantoate amidohydrolase; Reviewed


Pssm-ID: 237249  Cd Length: 414  Bit Score: 38.64  E-value: 2.33e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2744372630  56 TARKGTGQYEITINGLAAHAGNNPEE-GISAVQEMAHQIMFLHSL---NAPERGTTVNVGIARGGNRiNVVADKAVLGID 131
Cdd:PRK12891  209 TAGQGQRWYEVTLTGVDAHAGTTPMAfRRDALVGAARMIAFLDALgrrDAPDARATVGMIDARPNSR-NTVPGECFFTVE 287
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2744372630 132 TRVTSEAEAERIHAEISQ---ITPHLAGIKLDISGAQSRPPMRQTPEslvLMERAQQVAEQLGFAVEGKAVGGGSDGNFt 208
Cdd:PRK12891  288 FRHPDDAVLDRLDAALRAelaRIADETGLRADIEQIFGYAPAPFAPG---CIDAVRDAARALGLSHMDIVSGAGHDACF- 363
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 2744372630 209 AALGIPT-------LDGLGatgagiHARHEHIIIADIA 239
Cdd:PRK12891  364 AARGAPTgmifvpcVDGLS------HNEAEAITPEWFA 395
Zinc_peptidase_like cd03873
Zinc peptidases M18, M20, M28, and M42; Zinc peptidases play vital roles in metabolic and ...
178-238 2.80e-03

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: 37.79  E-value: 2.80e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2744372630 178 VLMERAQQVA-EQLGFAVEGKAVGGGSDGNFTAALGIPTLDGLGATGAGIHARHEHIIIADI 238
Cdd:cd03873   132 PLVDALRKAArEVGGKPQRASVIGGGTDGRLFAELGIPGVTLGPPGDKGAHSPNEFLNLDDL 193
PRK13009 PRK13009
succinyl-diaminopimelate desuccinylase; Reviewed
132-238 4.11e-03

succinyl-diaminopimelate desuccinylase; Reviewed


Pssm-ID: 237265 [Multi-domain]  Cd Length: 375  Bit Score: 38.14  E-value: 4.11e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2744372630 132 TRVTSEAEAERIHAEISQitphlAGIKLDISGAQSRPPMRQTPESLV-LMERAqqVAEQLGFAVEGKAVGGGSDGNFTAA 210
Cdd:PRK13009  260 TEHTAESLKARVEAILDK-----HGLDYTLEWTLSGEPFLTPPGKLVdAVVAA--IEAVTGITPELSTSGGTSDARFIAD 332
                          90       100
                  ....*....|....*....|....*...
gi 2744372630 211 LGIPTLDgLGATGAGIHARHEHIIIADI 238
Cdd:PRK13009  333 YGAQVVE-FGPVNATIHKVNECVSVADL 359
M20_18_42 cd18669
M20, M18 and M42 Zn-peptidases include aminopeptidases and carboxypeptidases; This family ...
178-238 6.46e-03

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: 36.64  E-value: 6.46e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2744372630 178 VLMERAQQVAEQL-GFAVEGKAVGGGSDGNFTAALGIPTLDGLGATGAGIHARHEHIIIADI 238
Cdd:cd18669   130 PLVDALSEAARKVfGKPQHAEGTGGGTDGRYLQELGIPGVTLGAGGGKGAHSPNERVNLEDL 191
PRK08737 PRK08737
acetylornithine deacetylase; Provisional
14-128 9.29e-03

acetylornithine deacetylase; Provisional


Pssm-ID: 181544 [Multi-domain]  Cd Length: 364  Bit Score: 36.72  E-value: 9.29e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2744372630  14 FLCGSDEEVGSPSSSAWLSHHALGSAQVLVVEPAVagSGALkTARKGTGQYEITINGLAAHAGNNPEEGISAVQEMA--- 90
Cdd:PRK08737  123 FLFSSDEEANDPRCVAAFLARGIPYEAVLVAEPTM--SEAV-LAHRGISSVLMRFAGRAGHASGKQDPSASALHQAMrwg 199
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 2744372630  91 -----HQIMFLHSLNAPERGTTVNVGIARGGNRINVVADKAVL 128
Cdd:PRK08737  200 gqaldHVESLAHARFGGLTGLRFNIGRVEGGIKANMIAPAAEL 242
 
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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