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Conserved domains on  [gi|479606324|gb|ENR78842|]
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hydantoinase/carbamoylase family amidase [Brucella abortus 65/157]

Protein Classification

Zn-dependent hydrolase( domain architecture ID 11486255)

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK12893 PRK12893
Zn-dependent hydrolase;
4-414 0e+00

Zn-dependent hydrolase;


:

Pssm-ID: 237250 [Multi-domain]  Cd Length: 412  Bit Score: 638.46  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479606324   4 TSNLRVNGDRLWDSLMEMAKIGPGLRGGNNRQTLTDEDGEGRRLFQNWCEKAGLSMGVDTMGNMFFTRPGEDSDADPVYM 83
Cdd:PRK12893   2 GRNLRINGERLWDSLMALARIGATPGGGVTRLALTDEDREARDLLAQWMEEAGLTVSVDAIGNLFGRRAGTDPDAPPVLI 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479606324  84 GSHLDTQPTGGKFDGVLGVLGGLEVMRTLNDMNIRTKRPIVVVNWTNEEGTRFAPAMLASGVFAGVLDQNWAYERTDAKG 163
Cdd:PRK12893  82 GSHLDTQPTGGRFDGALGVLAALEVVRTLNDAGIRTRRPIEVVSWTNEEGARFAPAMLGSGVFTGALPLDDALARRDADG 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479606324 164 KTFGEELVRIGWKGDEPVGSRKIHAMFELHIEQGPILEAEHKDIGVVTHGQGLWWLQVTLTGKEAHTGSTPMRMRKNASL 243
Cdd:PRK12893 162 ITLGEALARIGYRGTARVGRRAVDAYLELHIEQGPVLEAEGLPIGVVTGIQGIRWLEVTVEGQAAHAGTTPMAMRRDALV 241

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479606324 244 GLGKLLQLVNEIAMAHQPDAVGGVGHIDVSPNSRNVLPGQIVFTVDFRSPNQATLDGMKARFEKEAPKIAEELGIGIEIE 323
Cdd:PRK12893 242 AAARIILAVERIAAALAPDGVATVGRLRVEPNSRNVIPGKVVFTVDIRHPDDARLDAMEAALRAACAKIAAARGVQVTVE 321

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479606324 324 VAGHFDPVTFDTGCVEAIRNAAERLGYSHRNIVSGAGHDACWVNRVAPTAMVMCPCVDGLSHNEDEDISKEWASAGTDVL 403
Cdd:PRK12893 322 TVWDFPPVPFDPALVALVEAAAEALGLSHMRMVSGAGHDAMFLARVAPAAMIFVPCRGGISHNEAEDTEPADLAAGANVL 401

                        410
                 ....*....|.
gi 479606324 404 LHAVLETAEIV 414
Cdd:PRK12893 402 LHAVLELAGRA 412
 
Name Accession Description Interval E-value
PRK12893 PRK12893
Zn-dependent hydrolase;
4-414 0e+00

Zn-dependent hydrolase;


Pssm-ID: 237250 [Multi-domain]  Cd Length: 412  Bit Score: 638.46  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479606324   4 TSNLRVNGDRLWDSLMEMAKIGPGLRGGNNRQTLTDEDGEGRRLFQNWCEKAGLSMGVDTMGNMFFTRPGEDSDADPVYM 83
Cdd:PRK12893   2 GRNLRINGERLWDSLMALARIGATPGGGVTRLALTDEDREARDLLAQWMEEAGLTVSVDAIGNLFGRRAGTDPDAPPVLI 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479606324  84 GSHLDTQPTGGKFDGVLGVLGGLEVMRTLNDMNIRTKRPIVVVNWTNEEGTRFAPAMLASGVFAGVLDQNWAYERTDAKG 163
Cdd:PRK12893  82 GSHLDTQPTGGRFDGALGVLAALEVVRTLNDAGIRTRRPIEVVSWTNEEGARFAPAMLGSGVFTGALPLDDALARRDADG 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479606324 164 KTFGEELVRIGWKGDEPVGSRKIHAMFELHIEQGPILEAEHKDIGVVTHGQGLWWLQVTLTGKEAHTGSTPMRMRKNASL 243
Cdd:PRK12893 162 ITLGEALARIGYRGTARVGRRAVDAYLELHIEQGPVLEAEGLPIGVVTGIQGIRWLEVTVEGQAAHAGTTPMAMRRDALV 241

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479606324 244 GLGKLLQLVNEIAMAHQPDAVGGVGHIDVSPNSRNVLPGQIVFTVDFRSPNQATLDGMKARFEKEAPKIAEELGIGIEIE 323
Cdd:PRK12893 242 AAARIILAVERIAAALAPDGVATVGRLRVEPNSRNVIPGKVVFTVDIRHPDDARLDAMEAALRAACAKIAAARGVQVTVE 321

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479606324 324 VAGHFDPVTFDTGCVEAIRNAAERLGYSHRNIVSGAGHDACWVNRVAPTAMVMCPCVDGLSHNEDEDISKEWASAGTDVL 403
Cdd:PRK12893 322 TVWDFPPVPFDPALVALVEAAAEALGLSHMRMVSGAGHDAMFLARVAPAAMIFVPCRGGISHNEAEDTEPADLAAGANVL 401

                        410
                 ....*....|.
gi 479606324 404 LHAVLETAEIV 414
Cdd:PRK12893 402 LHAVLELAGRA 412
M20_bAS cd03884
M20 Peptidase beta-alanine synthase, an amidohydrolase; Peptidase M20 family, beta-alanine ...
 14-408 0e+00

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


Pssm-ID: 349880 [Multi-domain]  Cd Length: 398  Bit Score: 569.85  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479606324  14 LWDSLMEMAKIGPGLRGGNNRQTLTDEDGEGRRLFQNWCEKAGLSMGVDTMGNMFFTRPGEDSDADPVYMGSHLDTQPTG 93
Cdd:cd03884    1 LWDRLEELAAIGATPAGGVTRLALTDEDRAARDLFVEWMEEAGLSVRVDAVGNLFGRLEGTDPDAPPVLTGSHLDTVPNG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479606324  94 GKFDGVLGVLGGLEVMRTLNDMNIRTKRPIVVVNWTNEEGTRFAPAMLASGVFAGVLDQNWAYERTDAKGKTFGEELVRI 173
Cdd:cd03884   81 GRYDGILGVLAGLEALRALKEAGIRPRRPIEVVAFTNEEGSRFPPSMLGSRAFAGTLDLEELLSLRDADGVSLAEALKAI 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479606324 174 GWKGDEPVGSRK---IHAMFELHIEQGPILEAEHKDIGVVTHGQGLWWLQVTLTGKEAHTGSTPMRMRKNASLGLGKLLQ 250
Cdd:cd03884  161 GYDGDRPASARRpgdIKAYVELHIEQGPVLEEEGLPIGVVTGIAGQRWLEVTVTGEAGHAGTTPMALRRDALLAAAELIL 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479606324 251 LVNEIAMAHQPDAVGGVGHIDVSPNSRNVLPGQIVFTVDFRSPNQATLDGMKARFEKEAPKIAEELGIGIEIEVAGHFDP 330
Cdd:cd03884  241 AVEEIALEHGDDLVATVGRIEVKPNAVNVIPGEVEFTLDLRHPDDAVLDAMVERIRAEAEAIAAERGVEVEVERLWDSPP 320

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 479606324 331 VTFDTGCVEAIRNAAERLGYSHRNIVSGAGHDACWVNRVAPTAMVMCPCVDGLSHNEDEDISKEWASAGTDVLLHAVL 408
Cdd:cd03884  321 VPFDPELVAALEAAAEALGLSYRRMPSGAGHDAMFMARICPTAMIFVPSRDGISHNPAEYTSPEDLAAGVQVLLHALL 398
hydantase TIGR01879
amidase, hydantoinase/carbamoylase family; Enzymes in this subfamily hydrolize the amide bonds ...
 13-409 2.40e-124

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


Pssm-ID: 200138 [Multi-domain]  Cd Length: 400  Bit Score: 365.67  E-value: 2.40e-124
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479606324   13 RLWDSLMEMAKIGPGLRGGNNRQTLTDEDGEGRRLFQNWCEKAGLSMGVDTMGNMFFTRPGEDSDADPVYMGSHLDTQPT 92
Cdd:TIGR01879   2 RLWETLMWLGEVGADPAGGMTRLALSPEDREAQDLFKKRMRAAGLEVRFDEVGNLIGRKEGTEPPLEVVLSGSHLDTVVN 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479606324   93 GGKFDGVLGVLGGLEVMRTLNDMNIRTKRPIVVVNWTNEEGTRFAPAMLASGVFAGVLDQNWAYERTDAKGKTFGEELVR 172
Cdd:TIGR01879  82 GGNFDGQLGVLAGIEVVDALKEAYVVPLHPIEVVAFTEEEGSRFPYGMWGSRNMVGLANPEDVRNICDAKGISFAEAMKA 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479606324  173 IG--WKGDEPVGSRKIHAMFELHIEQGPILEAEHKDIGVVTHGQGLWWLQVTLTGKEAHTGSTPMRMRKNASLGLGKLLQ 250
Cdd:TIGR01879 162 CGpdLPNQPLRPRGDIKAYVELHIEQGPVLESNGQPIGVVNAIAGQRWYKVTLNGESNHAGTTPMSLRRDPLVAASRIIH 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479606324  251 LVNEIAMAHQPdAVGGVGHIDVSPNSRNVLPGQIVFTVDFRSPNQATLDGMKARFEKEAPKIAEELGIGIEIEVAGHFDP 330
Cdd:TIGR01879 242 QVEEKAKRGDP-TVGTVGKVEARPNGVNVIPGKVTFTLDLRHTDAAVLRDFTQQLENDIKAISDERDIGIDIERWMDEPP 320

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 479606324  331 VTFDTGCVEAIRNAAERLGYSHRNIVSGAGHDACWVNRVAPTAMVMCPCVDGLSHNEDEDISKEWASAGTDVLLHAVLE 409
Cdd:TIGR01879 321 VPCSEELVAALTELCERLGYNARVMVSGAGHDAQILAPIVPIGMIFIPSINGISHNPAEWSNITDCAEGAKVLYLMVYQ 399
Peptidase_M20 pfam01546
Peptidase family M20/M25/M40; This family includes a range of zinc metallopeptidases belonging ...
 84-409 1.00e-53

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: 181.01  E-value: 1.00e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479606324   84 GSHLDTQPTG--------GKFDGVL----------GVLGGLEVMRTLNDMNIRtKRPIVVVNWTNEEGTRF-APAMLASG 144
Cdd:pfam01546   3 RGHMDVVPDEetwgwpfkSTEDGKLygrghddmkgGLLAALEALRALKEEGLK-KGTVKLLFQPDEEGGMGgARALIEDG 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479606324  145 VFAGvldqnwayertdakgktfgeelvrigwkgdepvgsRKIHAMFELHIEQGPILEaEHKDIGVVTHGQGLWWLQVTLT 224
Cdd:pfam01546  82 LLER-----------------------------------EKVDAVFGLHIGEPTLLE-GGIAIGVVTGHRGSLRFRVTVK 125

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479606324  225 GKEAHtGSTPmRMRKNASLGLGKLLQLVNEIAMAHQPD---AVGGVGHIDVSPNSRNVLPGQIVFTVDFRSPNQATLDGM 301
Cdd:pfam01546 126 GKGGH-ASTP-HLGVNAIVAAARLILALQDIVSRNVDPldpAVVTVGNITGIPGGVNVIPGEAELKGDIRLLPGEDLEEL 203

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479606324  302 KARFEKEAPKIAEELGIGIEIEVAGHFDPVTFDTG-CVEAIRNAAERL-GYSHRNIVSG--AGHDACWV-NRVAPTAMVM 376
Cdd:pfam01546 204 EERIREILEAIAAAYGVKVEVEYVEGGAPPLVNDSpLVAALREAAKELfGLKVELIVSGsmGGTDAAFFlLGVPPTVVFF 283

                         330       340       350
                  ....*....|....*....|....*....|...
gi 479606324  377 CPCvDGLSHNEDEDISKEWASAGTDVLLHAVLE 409
Cdd:pfam01546 284 GPG-SGLAHSPNEYVDLDDLEKGAKVLARLLLK 315
ArgE COG0624
Acetylornithine deacetylase/Succinyl-diaminopimelate desuccinylase or related deacylase [Amino ...
 36-394 2.42e-16

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: 79.93  E-value: 2.42e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479606324  36 TLTDEDGEGRRLFQNWCEKAGLSM----GVDTMGNMFFTRPGEDSDADPVYMGsHLDTQPTGGKFDgvlgvlgglevmrt 111
Cdd:COG0624   26 SVSGEEAAAAELLAELLEALGFEVerleVPPGRPNLVARRPGDGGGPTLLLYG-HLDVVPPGDLEL-------------- 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479606324 112 lndmnirtkrpivvvnWTneegtrfapamlaSGVFAGVLDQNWAYER--TDAKG------KTFgEELVRIGWK------- 176
Cdd:COG0624   91 ----------------WT-------------SDPFEPTIEDGRLYGRgaADMKGglaamlAAL-RALLAAGLRlpgnvtl 140

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479606324 177 ---GDEPVGSRKIHAMFELHIEQGP-----ILEAEhkDIGVVTHGQ-GLWWLQVTLTGKEAHtGSTPMRMRkNASLGLGK 247
Cdd:COG0624  141 lftGDEEVGSPGARALVEELAEGLKadaaiVGEPT--GVPTIVTGHkGSLRFELTVRGKAAH-SSRPELGV-NAIEALAR 216

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479606324 248 LLQLVNEIAMAHQPDAVGG-----VGHIDvSPNSRNVLPGQIVFTVDFRSPNQATLDGMKARFEKEAPKIAEELGIGIEI 322
Cdd:COG0624  217 ALAALRDLEFDGRADPLFGrttlnVTGIE-GGTAVNVIPDEAEAKVDIRLLPGEDPEEVLAALRALLAAAAPGVEVEVEV 295

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 479606324 323 eVAGHFDPVTFDTGC--VEAIRNAAERL-GYSHRNIVSGAGHDACWVNRVAPTAMVMCPCVDG-LSHNEDEDISKE 394
Cdd:COG0624  296 -LGDGRPPFETPPDSplVAAARAAIREVtGKEPVLSGVGGGTDARFFAEALGIPTVVFGPGDGaGAHAPDEYVELD 370
 
Name Accession Description Interval E-value
PRK12893 PRK12893
Zn-dependent hydrolase;
4-414 0e+00

Zn-dependent hydrolase;


Pssm-ID: 237250 [Multi-domain]  Cd Length: 412  Bit Score: 638.46  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479606324   4 TSNLRVNGDRLWDSLMEMAKIGPGLRGGNNRQTLTDEDGEGRRLFQNWCEKAGLSMGVDTMGNMFFTRPGEDSDADPVYM 83
Cdd:PRK12893   2 GRNLRINGERLWDSLMALARIGATPGGGVTRLALTDEDREARDLLAQWMEEAGLTVSVDAIGNLFGRRAGTDPDAPPVLI 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479606324  84 GSHLDTQPTGGKFDGVLGVLGGLEVMRTLNDMNIRTKRPIVVVNWTNEEGTRFAPAMLASGVFAGVLDQNWAYERTDAKG 163
Cdd:PRK12893  82 GSHLDTQPTGGRFDGALGVLAALEVVRTLNDAGIRTRRPIEVVSWTNEEGARFAPAMLGSGVFTGALPLDDALARRDADG 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479606324 164 KTFGEELVRIGWKGDEPVGSRKIHAMFELHIEQGPILEAEHKDIGVVTHGQGLWWLQVTLTGKEAHTGSTPMRMRKNASL 243
Cdd:PRK12893 162 ITLGEALARIGYRGTARVGRRAVDAYLELHIEQGPVLEAEGLPIGVVTGIQGIRWLEVTVEGQAAHAGTTPMAMRRDALV 241

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479606324 244 GLGKLLQLVNEIAMAHQPDAVGGVGHIDVSPNSRNVLPGQIVFTVDFRSPNQATLDGMKARFEKEAPKIAEELGIGIEIE 323
Cdd:PRK12893 242 AAARIILAVERIAAALAPDGVATVGRLRVEPNSRNVIPGKVVFTVDIRHPDDARLDAMEAALRAACAKIAAARGVQVTVE 321

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479606324 324 VAGHFDPVTFDTGCVEAIRNAAERLGYSHRNIVSGAGHDACWVNRVAPTAMVMCPCVDGLSHNEDEDISKEWASAGTDVL 403
Cdd:PRK12893 322 TVWDFPPVPFDPALVALVEAAAEALGLSHMRMVSGAGHDAMFLARVAPAAMIFVPCRGGISHNEAEDTEPADLAAGANVL 401

                        410
                 ....*....|.
gi 479606324 404 LHAVLETAEIV 414
Cdd:PRK12893 402 LHAVLELAGRA 412
PRK09290 PRK09290
allantoate amidohydrolase; Reviewed
 6-414 0e+00

allantoate amidohydrolase; Reviewed


Pssm-ID: 236456 [Multi-domain]  Cd Length: 413  Bit Score: 629.50  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479606324   6 NLRVNGDRLWDSLMEMAKIGPGLRGGNNRQTLTDEDGEGRRLFQNWCEKAGLSMGVDTMGNMFFTRPGEDSDADPVYMGS 85
Cdd:PRK09290   1 MLRIDAERLWARLDELAKIGATPDGGVTRLALSPEDLQARDLFAEWMEAAGLTVRVDAVGNLFGRLEGRDPDAPAVLTGS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479606324  86 HLDTQPTGGKFDGVLGVLGGLEVMRTLNDMNIRTKRPIVVVNWTNEEGTRFAPAMLASGVFAGVLDQNWAYERTDAKGKT 165
Cdd:PRK09290  81 HLDTVPNGGRFDGPLGVLAGLEAVRTLNERGIRPRRPIEVVAFTNEEGSRFGPAMLGSRVFTGALTPEDALALRDADGVS 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479606324 166 FGEELVRIGWKGDEPVGSR----KIHAMFELHIEQGPILEAEHKDIGVVTHGQGLWWLQVTLTGKEAHTGSTPMRMRKNA 241
Cdd:PRK09290 161 FAEALAAIGYDGDEAVGAArarrDIKAFVELHIEQGPVLEAEGLPIGVVTGIVGQRRYRVTFTGEANHAGTTPMALRRDA 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479606324 242 SLGLGKLLQLVNEIAMAHQPDAVGGVGHIDVSPNSRNVLPGQIVFTVDFRSPNQATLDGMKARFEKEAPKIAEELGIGIE 321
Cdd:PRK09290 241 LLAAAEIILAVERIAAAHGPDLVATVGRLEVKPNSVNVIPGEVTFTLDIRHPDDAVLDALVAELRAAAEAIAARRGVEVE 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479606324 322 IEVAGHFDPVTFDTGCVEAIRNAAERLGYSHRNIVSGAGHDACWVNRVAPTAMVMCPCVDGLSHNEDEDISKEWASAGTD 401
Cdd:PRK09290 321 IELISRRPPVPFDPGLVAALEEAAERLGLSYRRLPSGAGHDAQILAAVVPTAMIFVPSVGGISHNPAEFTSPEDCAAGAN 400

                        410
                 ....*....|...
gi 479606324 402 VLLHAVLETAEIV 414
Cdd:PRK09290 401 VLLHALLELAEEG 413
M20_bAS cd03884
M20 Peptidase beta-alanine synthase, an amidohydrolase; Peptidase M20 family, beta-alanine ...
 14-408 0e+00

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


Pssm-ID: 349880 [Multi-domain]  Cd Length: 398  Bit Score: 569.85  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479606324  14 LWDSLMEMAKIGPGLRGGNNRQTLTDEDGEGRRLFQNWCEKAGLSMGVDTMGNMFFTRPGEDSDADPVYMGSHLDTQPTG 93
Cdd:cd03884    1 LWDRLEELAAIGATPAGGVTRLALTDEDRAARDLFVEWMEEAGLSVRVDAVGNLFGRLEGTDPDAPPVLTGSHLDTVPNG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479606324  94 GKFDGVLGVLGGLEVMRTLNDMNIRTKRPIVVVNWTNEEGTRFAPAMLASGVFAGVLDQNWAYERTDAKGKTFGEELVRI 173
Cdd:cd03884   81 GRYDGILGVLAGLEALRALKEAGIRPRRPIEVVAFTNEEGSRFPPSMLGSRAFAGTLDLEELLSLRDADGVSLAEALKAI 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479606324 174 GWKGDEPVGSRK---IHAMFELHIEQGPILEAEHKDIGVVTHGQGLWWLQVTLTGKEAHTGSTPMRMRKNASLGLGKLLQ 250
Cdd:cd03884  161 GYDGDRPASARRpgdIKAYVELHIEQGPVLEEEGLPIGVVTGIAGQRWLEVTVTGEAGHAGTTPMALRRDALLAAAELIL 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479606324 251 LVNEIAMAHQPDAVGGVGHIDVSPNSRNVLPGQIVFTVDFRSPNQATLDGMKARFEKEAPKIAEELGIGIEIEVAGHFDP 330
Cdd:cd03884  241 AVEEIALEHGDDLVATVGRIEVKPNAVNVIPGEVEFTLDLRHPDDAVLDAMVERIRAEAEAIAAERGVEVEVERLWDSPP 320

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 479606324 331 VTFDTGCVEAIRNAAERLGYSHRNIVSGAGHDACWVNRVAPTAMVMCPCVDGLSHNEDEDISKEWASAGTDVLLHAVL 408
Cdd:cd03884  321 VPFDPELVAALEAAAEALGLSYRRMPSGAGHDAMFMARICPTAMIFVPSRDGISHNPAEYTSPEDLAAGVQVLLHALL 398
PRK12891 PRK12891
allantoate amidohydrolase; Reviewed
 8-411 4.27e-159

allantoate amidohydrolase; Reviewed


Pssm-ID: 237249  Cd Length: 414  Bit Score: 454.66  E-value: 4.27e-159
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479606324   8 RVNGDRLWDSLMEMAKIGPGLRGGNNRQTLTDEDGEGRRLFQNWCEKAGLSMGVDTMGNMFFTRPGEDSDADPVYMGSHL 87
Cdd:PRK12891   6 RVDGERLWASLERMAQIGATPKGGVCRLALTDGDREARDLFVAWARDAGCTVRVDAMGNLFARRAGRDPDAAPVMTGSHA 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479606324  88 DTQPTGGKFDGVLGVLGGLEVMRTLNDMNIRTKRPIVVVNWTNEEGTRFAPAMLASGVFAGVLDQNWAYERTDAKGKTFG 167
Cdd:PRK12891  86 DSQPTGGRYDGIYGVLGGLEVVRALNDAGIETERPVDVVIWTNEEGSRFAPSMVGSGVFFGVYPLEYLLSRRDDTGRTLG 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479606324 168 EELVRIGWKGDEPVGSRKIHAMFELHIEQGPILEAEHKDIGVVTHGQGLWWLQVTLTGKEAHTGSTPMRMRKNASLGLGK 247
Cdd:PRK12891 166 EHLARIGYAGAEPVGGYPVHAAYELHIEQGAILERAGKTIGVVTAGQGQRWYEVTLTGVDAHAGTTPMAFRRDALVGAAR 245

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479606324 248 LLQLVNEIAMAHQPDAVGGVGHIDVSPNSRNVLPGQIVFTVDFRSPNQATLDGMKARFEKEAPKIAEELGIGIEIEVAGH 327
Cdd:PRK12891 246 MIAFLDALGRRDAPDARATVGMIDARPNSRNTVPGECFFTVEFRHPDDAVLDRLDAALRAELARIADETGLRADIEQIFG 325

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479606324 328 FDPVTFDTGCVEAIRNAAERLGYSHRNIVSGAGHDACWVNRVAPTAMVMCPCVDGLSHNEDEDISKEWASAGTDVLLHAV 407
Cdd:PRK12891 326 YAPAPFAPGCIDAVRDAARALGLSHMDIVSGAGHDACFAARGAPTGMIFVPCVDGLSHNEAEAITPEWFAAGADVLLRAV 405


                 ....
gi 479606324 408 LETA 411
Cdd:PRK12891 406 LQSA 409
PRK12890 PRK12890
allantoate amidohydrolase; Reviewed
 4-412 3.00e-151

allantoate amidohydrolase; Reviewed


Pssm-ID: 237248 [Multi-domain]  Cd Length: 414  Bit Score: 434.33  E-value: 3.00e-151
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479606324   4 TSNLRVNGDRLWDSLMEMAKIGPGlRGGNNRQTLTDEDGEGRRLFQNWCEKAGLSMGVDTMGNMFFTRPGEDSDADPVYM 83
Cdd:PRK12890   1 TTPPPINGERLLARLEELAAIGRD-GPGWTRLALSDEERAARALLAAWMRAAGLEVRRDAAGNLFGRLPGRDPDLPPLMT 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479606324  84 GSHLDTQPTGGKFDGVLGVLGGLEVMRTLNDMNIRTKRPIVVVNWTNEEGTRFAPAMLASGVFAGVLDQNWAYERTDAKG 163
Cdd:PRK12890  80 GSHLDTVPNGGRYDGILGVLAGLEVVAALREAGIRPPHPLEVIAFTNEEGVRFGPSMIGSRALAGTLDVEAVLATRDDDG 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479606324 164 KTFGEELVRIGWKGDEPVGSRKIH----AMFELHIEQGPILEAEHKDIGVVTHGQGLWWLQVTLTGKEAHTGSTPMRMRK 239
Cdd:PRK12890 160 TTLAEALRRIGGDPDALPGALRPPgavaAFLELHIEQGPVLEAEGLPIGVVTAIQGIRRQAVTVEGEANHAGTTPMDLRR 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479606324 240 NASLGLGKLLQLVNEIAMAHQPDAVGGVGHIDVSPNSRNVLPGQIVFTVDFRSPNQATLDGMKARFEKEAPKIAEELGIG 319
Cdd:PRK12890 240 DALVAAAELVTAMERRARALLHDLVATVGRLDVEPNAINVVPGRVVFTLDLRSPDDAVLEAAEAALLAELEAIAAARGVR 319

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479606324 320 IEIEVAGHFDPVTFDTGCVEAIRNAAERLGYSHRNIVSGAGHDACWVNRVAPTAMVMCPCVDGLSHNEDEDISKEWASAG 399
Cdd:PRK12890 320 IELERLSRSEPVPCDPALVDAVEAAAARLGYPSRRMPSGAGHDAAAIARIGPSAMIFVPCRGGISHNPEEAMDPEDLAAG 399

                        410
                 ....*....|...
gi 479606324 400 TDVLLHAVLETAE 412
Cdd:PRK12890 400 ARVLLDAVLRLDR 412
hydantase TIGR01879
amidase, hydantoinase/carbamoylase family; Enzymes in this subfamily hydrolize the amide bonds ...
 13-409 2.40e-124

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


Pssm-ID: 200138 [Multi-domain]  Cd Length: 400  Bit Score: 365.67  E-value: 2.40e-124
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479606324   13 RLWDSLMEMAKIGPGLRGGNNRQTLTDEDGEGRRLFQNWCEKAGLSMGVDTMGNMFFTRPGEDSDADPVYMGSHLDTQPT 92
Cdd:TIGR01879   2 RLWETLMWLGEVGADPAGGMTRLALSPEDREAQDLFKKRMRAAGLEVRFDEVGNLIGRKEGTEPPLEVVLSGSHLDTVVN 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479606324   93 GGKFDGVLGVLGGLEVMRTLNDMNIRTKRPIVVVNWTNEEGTRFAPAMLASGVFAGVLDQNWAYERTDAKGKTFGEELVR 172
Cdd:TIGR01879  82 GGNFDGQLGVLAGIEVVDALKEAYVVPLHPIEVVAFTEEEGSRFPYGMWGSRNMVGLANPEDVRNICDAKGISFAEAMKA 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479606324  173 IG--WKGDEPVGSRKIHAMFELHIEQGPILEAEHKDIGVVTHGQGLWWLQVTLTGKEAHTGSTPMRMRKNASLGLGKLLQ 250
Cdd:TIGR01879 162 CGpdLPNQPLRPRGDIKAYVELHIEQGPVLESNGQPIGVVNAIAGQRWYKVTLNGESNHAGTTPMSLRRDPLVAASRIIH 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479606324  251 LVNEIAMAHQPdAVGGVGHIDVSPNSRNVLPGQIVFTVDFRSPNQATLDGMKARFEKEAPKIAEELGIGIEIEVAGHFDP 330
Cdd:TIGR01879 242 QVEEKAKRGDP-TVGTVGKVEARPNGVNVIPGKVTFTLDLRHTDAAVLRDFTQQLENDIKAISDERDIGIDIERWMDEPP 320

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 479606324  331 VTFDTGCVEAIRNAAERLGYSHRNIVSGAGHDACWVNRVAPTAMVMCPCVDGLSHNEDEDISKEWASAGTDVLLHAVLE 409
Cdd:TIGR01879 321 VPCSEELVAALTELCERLGYNARVMVSGAGHDAQILAPIVPIGMIFIPSINGISHNPAEWSNITDCAEGAKVLYLMVYQ 399
PRK12892 PRK12892
allantoate amidohydrolase; Reviewed
 7-403 1.31e-115

allantoate amidohydrolase; Reviewed


Pssm-ID: 183817 [Multi-domain]  Cd Length: 412  Bit Score: 343.61  E-value: 1.31e-115
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479606324   7 LRVNGDRLWDSLMEMAKIGpGLRGGNNRQTLTDEDGEGRRLFQNWCEKAGLSMGVDTMGNMFFTRPGEDSDAdPVYMGSH 86
Cdd:PRK12892   5 LRIDGQRVLDDLMELAAIG-AAKTGVHRPTYSDAHVAARRRLAAWCEAAGLAVRIDGIGNVFGRLPGPGPGP-ALLVGSH 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479606324  87 LDTQPTGGKFDGVLGVLGGLEVMRTLNDMNIRTKRPIVVVNWTNEEGTRFAPAMLASGVFAGVLDQNWAY-ERTDAKGKT 165
Cdd:PRK12892  83 LDSQNLGGRYDGALGVVAGLEAARALNEHGIATRHPLDVVAWCDEEGSRFTPGFLGSRAYAGRLDPADALaARCRSDGVP 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479606324 166 FGEELVRIGWKGDePVGSR---KIHAMFELHIEQGPILEAEHKDIGVVTHGQGLWWLQVTLTGKEAHTGSTPMRMRKNAS 242
Cdd:PRK12892 163 LRDALAAAGLAGR-PRPAAdraRPKGYLEAHIEQGPVLEQAGLPVGVVTGIVGIWQYRITVTGEAGHAGTTPMALRRDAG 241

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479606324 243 LGLGKLLQLVNEIAMAHQPDAVGGVGHIDVSPNSRNVLPGQIVFTVDFRSPNQATLDGMKARFEKEAPKIAEELGIGIEI 322
Cdd:PRK12892 242 LAAAEMIAAIDEHFPRVCGPAVVTVGRVALDPGSPSIIPGRVEFSFDARHPSPPVLQRLVALLEALCREIARRRGCRVSV 321

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479606324 323 EVAGHFDPVTFDTGCVEAIRNAAERLGYSHRNIVSGAGHDACWVNRVAPTAMVMCPCVDGLSHNEDEDISKEWASAGTDV 402
Cdd:PRK12892 322 DRIAEYAPAPCDAALVDALRAAAEAAGGPYLEMPSGAGHDAQNMARIAPSAMLFVPSKGGISHNPAEDTSPADLAQGARV 401


                 .
gi 479606324 403 L 403
Cdd:PRK12892 402 L 402
Peptidase_M20 pfam01546
Peptidase family M20/M25/M40; This family includes a range of zinc metallopeptidases belonging ...
 84-409 1.00e-53

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: 181.01  E-value: 1.00e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479606324   84 GSHLDTQPTG--------GKFDGVL----------GVLGGLEVMRTLNDMNIRtKRPIVVVNWTNEEGTRF-APAMLASG 144
Cdd:pfam01546   3 RGHMDVVPDEetwgwpfkSTEDGKLygrghddmkgGLLAALEALRALKEEGLK-KGTVKLLFQPDEEGGMGgARALIEDG 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479606324  145 VFAGvldqnwayertdakgktfgeelvrigwkgdepvgsRKIHAMFELHIEQGPILEaEHKDIGVVTHGQGLWWLQVTLT 224
Cdd:pfam01546  82 LLER-----------------------------------EKVDAVFGLHIGEPTLLE-GGIAIGVVTGHRGSLRFRVTVK 125

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479606324  225 GKEAHtGSTPmRMRKNASLGLGKLLQLVNEIAMAHQPD---AVGGVGHIDVSPNSRNVLPGQIVFTVDFRSPNQATLDGM 301
Cdd:pfam01546 126 GKGGH-ASTP-HLGVNAIVAAARLILALQDIVSRNVDPldpAVVTVGNITGIPGGVNVIPGEAELKGDIRLLPGEDLEEL 203

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479606324  302 KARFEKEAPKIAEELGIGIEIEVAGHFDPVTFDTG-CVEAIRNAAERL-GYSHRNIVSG--AGHDACWV-NRVAPTAMVM 376
Cdd:pfam01546 204 EERIREILEAIAAAYGVKVEVEYVEGGAPPLVNDSpLVAALREAAKELfGLKVELIVSGsmGGTDAAFFlLGVPPTVVFF 283

                         330       340       350
                  ....*....|....*....|....*....|...
gi 479606324  377 CPCvDGLSHNEDEDISKEWASAGTDVLLHAVLE 409
Cdd:pfam01546 284 GPG-SGLAHSPNEYVDLDDLEKGAKVLARLLLK 315
PRK13799 PRK13799
unknown domain/N-carbamoyl-L-amino acid hydrolase fusion protein; Provisional
 11-412 9.78e-50

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


Pssm-ID: 106740 [Multi-domain]  Cd Length: 591  Bit Score: 177.13  E-value: 9.78e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479606324  11 GDRLWD---SLMEMAKIGPGLRGGNNRQTLTDEDGEGRRLFQNWCEKAGL-SMGVDTMGNMFFTRPGEDSDADPVYMGSH 86
Cdd:PRK13799 180 GADVMDwaeDIAAHSDPGYADEGALTCTYLSDAHRACANQISDWMRDAGFdEVEIDAVGNVVGRYKAADDDAKTLITGSH 259

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479606324  87 LDTQPTGGKFDGVLGVLGGLEVMRTLNDMNIRTKRPIVVVNWTNEEGTRFAPAMLASGVFAGVLDQNWaYERTDAKGKTF 166
Cdd:PRK13799 260 YDTVRNGGKYDGREGIFLAIACVKELHEQGERLPFHFEVIAFAEEEGQRFKATFLGSGALIGDFNMEL-LDIKDADGISL 338

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479606324 167 GEELVRIGWKGDE-PVGSR---KIHAMFELHIEQGPILEAEHKDIGVVTHGQGLWWLQVTLTGKEAHTGSTPMRMRKNAS 242
Cdd:PRK13799 339 REAIQHAGHCIDAiPKIARdpaDVLGFIEVHIEQGPVLLELDIPLGIVTSIAGSARYICEFIGMASHAGTTPMDMRKDAA 418

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479606324 243 LGLGKLLQLVNEIAMAHQP-DAVGGVGHIDVSPNSRNVLPGQIVFTVDFRSPNQATLDGMKARFEKEAPKIAEELGIGIE 321
Cdd:PRK13799 419 AAAAEIALYIEKRAAQDQHaSLVATMGQLNVPSGSTNVIPGRCQFSLDIRAATDEIRDAAVADILAEIAAIAARRGIEYK 498

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479606324 322 IEVAGHFDPVTFDTGCVEAIRNAAERLGYSHRNIVSGAGHDACWVNRVAPTAMVMCPCVD-GLSHNEDEDISKEWASAGT 400
Cdd:PRK13799 499 AELAMKAAAAPCAPELMKQLEAATDAAGVPLFELASGAGHDAMKIAEIMDQAMLFTRCGNaGISHNPLESMTADDMELSA 578

                        410
                 ....*....|..
gi 479606324 401 DVLLHAVLETAE 412
Cdd:PRK13799 579 DAFLDFLNNFAE 590
PRK13590 PRK13590
putative bifunctional OHCU decarboxylase/allantoate amidohydrolase; Provisional
 11-405 2.36e-48

putative bifunctional OHCU decarboxylase/allantoate amidohydrolase; Provisional


Pssm-ID: 184168 [Multi-domain]  Cd Length: 591  Bit Score: 173.40  E-value: 2.36e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479606324  11 GDRLWD---SLMEMAKIGPGLRGGNNRQTLTDEDGEGRRLFQNWCEKAGL-SMGVDTMGNMFFTRPGEDSDADPVYMGSH 86
Cdd:PRK13590 180 GNDVWDwaeRLAAHSDPGYAEKGQLTVTYLTDAHRACAQQISHWMRDCGFdEVHIDAVGNVVGRYKGSTPQAKRLLTGSH 259

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479606324  87 LDTQPTGGKFDGVLGVLGGLEVMRTLNDMNIRTKRPIVVVNWTNEEGTRFAPAMLASGVFAGVLDQNWaYERTDAKGKTF 166
Cdd:PRK13590 260 YDTVRNGGKYDGRLGIFVPMACVRELHRQGRRLPFGLEVVGFAEEEGQRYKATFLGSGALIGDFDPAW-LDQKDADGITM 338

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479606324 167 GEELVRIGWKGDEPVGSRKIHAMF----ELHIEQGPILEAEHKDIGVVTHGQGLWWLQVTLTGKEAHTGSTPMRMRKNAS 242
Cdd:PRK13590 339 REAMQHAGLCIDDIPKLRRDPARYlgfvEVHIEQGPVLNELDLPLGIVTSINGSVRYVGEMIGMASHAGTTPMDRRRDAA 418

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479606324 243 LGLGKLLQLVNEIAmAHQPDAVGGVGHIDVSPNSRNVLPGQIVFTVDFRSPNQATLDGMKARFEKEAPKIAEELGIGIEI 322
Cdd:PRK13590 419 AAVAELALYVEQRA-AQDGDSVGTVGMLEVPGGSINVVPGRCRFSLDIRAPTDAQRDAMVADVLAELEAICERRGLRYTL 497

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479606324 323 EVAGHFDPVTFDTGCVEAIRNAAERLGYSHRNIVSGAGHDACWVNRVAPTAMVMCPCVD-GLSHNEDEDISKEWASAGTD 401
Cdd:PRK13590 498 EETMRAAAAPSAPAWQQRWEAAVAALGLPLFRMPSGAGHDAMKLHEIMPQAMLFVRGENaGISHNPLESSTADDMQLAVQ 577


                 ....
gi 479606324 402 VLLH 405
Cdd:PRK13590 578 AFQH 581
ArgE COG0624
Acetylornithine deacetylase/Succinyl-diaminopimelate desuccinylase or related deacylase [Amino ...
 36-394 2.42e-16

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: 79.93  E-value: 2.42e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479606324  36 TLTDEDGEGRRLFQNWCEKAGLSM----GVDTMGNMFFTRPGEDSDADPVYMGsHLDTQPTGGKFDgvlgvlgglevmrt 111
Cdd:COG0624   26 SVSGEEAAAAELLAELLEALGFEVerleVPPGRPNLVARRPGDGGGPTLLLYG-HLDVVPPGDLEL-------------- 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479606324 112 lndmnirtkrpivvvnWTneegtrfapamlaSGVFAGVLDQNWAYER--TDAKG------KTFgEELVRIGWK------- 176
Cdd:COG0624   91 ----------------WT-------------SDPFEPTIEDGRLYGRgaADMKGglaamlAAL-RALLAAGLRlpgnvtl 140

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479606324 177 ---GDEPVGSRKIHAMFELHIEQGP-----ILEAEhkDIGVVTHGQ-GLWWLQVTLTGKEAHtGSTPMRMRkNASLGLGK 247
Cdd:COG0624  141 lftGDEEVGSPGARALVEELAEGLKadaaiVGEPT--GVPTIVTGHkGSLRFELTVRGKAAH-SSRPELGV-NAIEALAR 216

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479606324 248 LLQLVNEIAMAHQPDAVGG-----VGHIDvSPNSRNVLPGQIVFTVDFRSPNQATLDGMKARFEKEAPKIAEELGIGIEI 322
Cdd:COG0624  217 ALAALRDLEFDGRADPLFGrttlnVTGIE-GGTAVNVIPDEAEAKVDIRLLPGEDPEEVLAALRALLAAAAPGVEVEVEV 295

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 479606324 323 eVAGHFDPVTFDTGC--VEAIRNAAERL-GYSHRNIVSGAGHDACWVNRVAPTAMVMCPCVDG-LSHNEDEDISKE 394
Cdd:COG0624  296 -LGDGRPPFETPPDSplVAAARAAIREVtGKEPVLSGVGGGTDARFFAEALGIPTVVFGPGDGaGAHAPDEYVELD 370
PRK08651 PRK08651
succinyl-diaminopimelate desuccinylase; Reviewed
 215-389 4.19e-11

succinyl-diaminopimelate desuccinylase; Reviewed


Pssm-ID: 236323 [Multi-domain]  Cd Length: 394  Bit Score: 64.24  E-value: 4.19e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479606324 215 GLWWLQVTLTGKEAHtGSTPMRMRkNASLGLGKLLQ-LVNEIAMAHQP----DAVGGVGHIDV------SPNSRNVLPGQ 283
Cdd:PRK08651 183 GLVWGVVKVYGKQAH-ASTPWLGI-NAFEAAAKIAErLKSSLSTIKSKyeydDERGAKPTVTLggptveGGTKTNIVPGY 260

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479606324 284 IVFTVDFRSPNQATLDGMKARFEKEAPKIAEELGIGIEIEV-----AGHFDPvtfDTGCVEAIRNAAER-LGYSHRNIVS 357
Cdd:PRK08651 261 CAFSIDRRLIPEETAEEVRDELEALLDEVAPELGIEVEFEItpfseAFVTDP---DSELVKALREAIREvLGVEPKKTIS 337

                        170       180       190
                 ....*....|....*....|....*....|...
gi 479606324 358 GAGHDA-CWVNRVAPTAmVMCPCVDGLSHNEDE 389
Cdd:PRK08651 338 LGGTDArFFGAKGIPTV-VYGPGELELAHAPDE 369
M20_peptT_like cd05683
M20 Peptidase T like enzymes specifically cleave tripeptides; Peptidase M20 family, PeptT ...
 10-367 4.78e-09

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: 57.46  E-value: 4.78e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479606324  10 NGDRLWDSLMEMAKIgpglrggnnrQTLTDEDGEGRRLFQNWCEKAGLSMGVDTM--------GNMFFTRPGEDSDADPV 81
Cdd:cd05683    1 NEDRLINTFLELVQI----------DSETLHEKEISKVLKKKFENLGLSVIEDDAgkttgggaGNLICTLKADKEEVPKI 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479606324  82 YMGSHLDTQPTG------GKFDGVL-----GVLGG---------LEVMRTLNDMNIRTKRPIVVVNWTNEEGTrfapaml 141
Cdd:cd05683   71 LFTSHMDTVTPGinvkppQIADGYIysdgtTILGAddkagiaaiLEAIRVIKEKNIPHGQIQFVITVGEESGL------- 143

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479606324 142 asgVFAGVLDqnwaYERTDAKgktFGEELvrigwKGDEPVGSRKIHAMFELHIeqgpileaehkdigvvthgqglwwlQV 221
Cdd:cd05683  144 ---VGAKALD----PELIDAD---YGYAL-----DSEGDVGTIIVGAPTQDKI-------------------------NA 183

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479606324 222 TLTGKEAHTGSTPMRMrknaslglgkllqlVNEIAMAHQPDAVGGVGHID--VSPN--------SRNVLPGQIVFTVDFR 291
Cdd:cd05683  184 KIYGKTAHAGTSPEKG--------------ISAINIAAKAISNMKLGRIDeeTTANigkfqggtATNIVTDEVNIEAEAR 249

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 479606324 292 SPNQATLDGMKARFEKEAPKIAEELGIGIEIEVAGHFDPVTFDTG--CVEAIRNAAERLGYSHRNIVSGAGHDACWVN 367
Cdd:cd05683  250 SLDEEKLDAQVKHMKETFETTAKEKGAHAEVEVETSYPGFKINEDeeVVKLAKRAANNLGLEINTTYSGGGSDANIIN 327
M20_ArgE_DapE-like cd08659
Peptidase M20 acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase (ArgE/DapE) ...
 34-394 4.78e-07

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


Pssm-ID: 349944 [Multi-domain]  Cd Length: 361  Bit Score: 51.53  E-value: 4.78e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479606324  34 RQTLTDEDGEGRRLFQNWCEKAGL---SMGVDTMGNMFFTRPGEDsdADPVYMGSHLDTQPTGgkfdgvlgvlgglevmr 110
Cdd:cd08659    9 IPSVNPPEAEVAEYLAELLAKRGYgieSTIVEGRGNLVATVGGGD--GPVLLLNGHIDTVPPG----------------- 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479606324 111 tlndmnirtkrpivvvnwtNEEGTRFAPamlasgvFAGVLDQNWAYER--TDAKGK-----TFGEELVRIGWK------- 176
Cdd:cd08659   70 -------------------DGDKWSFPP-------FSGRIRDGRLYGRgaCDMKGGlaamvAALIELKEAGALlggrval 123

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479606324 177 ---GDEPVGSRKIHAMfelhIEQGPILE------AEHKDIGVVTHGQGLWWLQVTLTGKEAHtGSTPMRmRKNASLGLGK 247
Cdd:cd08659  124 latVDEEVGSDGARAL----LEAGYADRldalivGEPTGLDVVYAHKGSLWLRVTVHGKAAH-SSMPEL-GVNAIYALAD 197

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479606324 248 LLQLVNEI---AMAHQPdaVGG----VGHIDVSPNSrNVLPGQIVFTVDFRSPNQATLDGMKARFEkeapKIAEELGIGI 320
Cdd:cd08659  198 FLAELRTLfeeLPAHPL--LGPptlnVGVINGGTQV-NSIPDEATLRVDIRLVPGETNEGVIARLE----AILEEHEAKL 270

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 479606324 321 EIEVAGHFDPVTFDTG---CVEAIRNAAERLGYSHRNIVSGAGHDAC-WVNRVAPTAMVMCPCVDGLSHNEDEDISKE 394
Cdd:cd08659  271 TVEVSLDGDPPFFTDPdhpLVQALQAAARALGGDPVVRPFTGTTDASyFAKDLGFPVVVYGPGDLALAHQPDEYVSLE 348
M28 cd02690
M28 Zn-peptidases include aminopeptidases and carboxypeptidases; Peptidase M28 family (also ...
 66-132 9.89e-06

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


Pssm-ID: 349868 [Multi-domain]  Cd Length: 202  Bit Score: 46.18  E-value: 9.89e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 479606324  66 NMFFTRPGEDSDADPVYMGSHLDTQPTG-GKFDGVLGVLGGLEVMRTLNDMNIRTKRPIVVVNWTNEE 132
Cdd:cd02690    3 NVIATIKGSDKPDEVILIGAHYDSVPLSpGANDNASGVAVLLELARVLSKLQLKPKRSIRFAFWDAEE 70
M28_like cd05640
M28 Zn-peptidase; uncharacterized subfamily; Peptidase family M28 (also called aminopeptidase ...
 66-193 1.49e-05

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


Pssm-ID: 349893 [Multi-domain]  Cd Length: 281  Bit Score: 46.29  E-value: 1.49e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479606324  66 NMFFTRPGEDSDADPVYMGSHLDTQP-TGGKFDGVLGVLGGLEVMRTLNDMniRTKRPIVVVNWTNEEGTRFAPAMLASG 144
Cdd:cd05640   54 NLIADLPGSYSQDKLILIGAHYDTVPgSPGADDNASGVAALLELARLLATL--DPNHTLRFVAFDLEEYPFFARGLMGSH 131

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 479606324 145 VFAGVLdqnwayERTDAKGK-TFGEELvrIGWKGDEPvGSRKIHAMFELH 193
Cdd:cd05640  132 AYAEDL------LRPLTPIVgMLSLEM--IGYYDPFP-HSQAYPAGFELH 172
M20_PepV cd03888
M20 Peptidase Xaa-His dipeptidase (PepV) degrades hydrophobic dipeptides; Peptidase M20 family, ...
 181-394 2.27e-05

M20 Peptidase Xaa-His dipeptidase (PepV) degrades hydrophobic dipeptides; Peptidase M20 family, Peptidase V (Xaa-His dipeptidase; PepV g.p. (Lactobacillus lactis); X-His dipeptidase; beta-Ala-His dipeptidase; carnosinase) subfamily. The PepV group of proteins is widely distributed in lactic acid bacteria. PepV, along with PepT, functions at the end of the proteolytic processing system. PepV is a monomeric metalloenzyme that preferentially degrades hydrophobic dipeptides. The Streptococcus gordonii PepV gene is homologous to the PepV gene family from Lactobacillus and Lactococcus spp. PepV recognizes and fixes the dipeptide backbone, while the side chains are not specifically probed and can vary, rendering it a nonspecific dipeptidase. It has been shown that Lactococcus lactis subspecies lactis (L9) PepV does not hydrolyze dipeptides containing Pro or D-amino acids at the C-terminus, while PepV from Lactobaccilus has been shown to have L-carnosine hydrolyzing activity. The mammalian PepV also acts on anserine and homocarnosine (but not on homoanserine), and to a lesser extent on some other aminoacyl-L-histidine dipeptides. Also included is the Staphylococcus aureus metallopeptidase, Sapep, a Mn(2+)-dependent dipeptidase where large interdomain movements could potentially regulate the activity of this enzyme.


Pssm-ID: 349884 [Multi-domain]  Cd Length: 449  Bit Score: 46.47  E-value: 2.27e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479606324 181 VGSRKIHAMFELHIEQGPILEAEHKDIGVVthgqglwwlqVTLTGKEAHtGSTP-------MRMRK-----NASLGLGKL 248
Cdd:cd03888  216 VIPGKDKEELALSAATDLKGNIEIDDGGVE----------LTVTGKSAH-ASAPekgvnaiTLLAKflaelNKDGNDKDF 284

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479606324 249 LQLVNE-IAMAHQPDAVGG------VGHIDVSPNSRNVLPGQIVFTVDFRSPNQATLDGMKARFEKEAPKiaeelgIGIE 321
Cdd:cd03888  285 IKFLAKnLHEDYNGKKLGInfedevMGELTLNPGIITLDDGKLELGLNVRYPVGTSAEDIIKQIEEALEK------YGVE 358

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 479606324 322 IEVAGHFDPVTF--DTGCVEAIRNAAER-LGYSHRNIVSGAGHDACWVNR-VAPTAMVmcPCVDGLSHNEDEDISKE 394
Cdd:cd03888  359 VEGHKHQKPLYVpkDSPLVKTLLKVYEEqTGKEGEPVAIGGGTYARELPNgVAFGPEF--PGQKDTMHQANEFIPID 433
M28_like cd08015
M28 Zn-peptidase-like; uncharacterized subfamily; Peptidase family M28 (also called ...
 66-132 2.72e-05

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


Pssm-ID: 349937 [Multi-domain]  Cd Length: 218  Bit Score: 44.89  E-value: 2.72e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 479606324  66 NMFFTRPGEDSDADPVYMGSHLDTQPTG-GKFDGVLGVLGGLEVMRTLNDMNIRTKRPIVVVNWTNEE 132
Cdd:cd08015    3 NVIAEIPGSDKKDEVVILGAHLDSWHGAtGATDNGAGTAVMMEAMRILKAIGSKPKRTIRVALWGSEE 70
Zinc_peptidase_like cd03873
Zinc peptidases M18, M20, M28, and M42; Zinc peptidases play vital roles in metabolic and ...
 66-143 3.37e-05

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


Pssm-ID: 349870 [Multi-domain]  Cd Length: 200  Bit Score: 44.34  E-value: 3.37e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479606324  66 NMFFTRPGEDSDAdPVYMGSHLDTQPTG----------------------GKFDGVLGVLGGLEVMRTLNDMNIRTKRPI 123
Cdd:cd03873    1 NLIARLGGGEGGK-SVALGAHLDVVPAGegdnrdppfaedteeegrlygrGALDDKGGVAAALEALKRLKENGFKPKGTI 79

                         90       100
                 ....*....|....*....|
gi 479606324 124 VVVNWTNEEGTRFAPAMLAS 143
Cdd:cd03873   80 VVAFTADEEVGSGGGKGLLS 99
Iap COG2234
Zn-dependent amino- or carboxypeptidase, M28 family [Posttranslational modification, protein ...
 70-132 4.99e-05

Zn-dependent amino- or carboxypeptidase, M28 family [Posttranslational modification, protein turnover, chaperones, Amino acid transport and metabolism];


Pssm-ID: 441835 [Multi-domain]  Cd Length: 257  Bit Score: 44.74  E-value: 4.99e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 479606324  70 TRPGEDSDADPVYMGSHLDTQPTG--GKFDGVLGVLGGLEVMRTLNDMNIRTKRPIVVVNWTNEE 132
Cdd:COG2234   52 EIPGTDPPDEVVVLGAHYDSVGSIgpGADDNASGVAALLELARALAALGPKPKRTIRFVAFGAEE 116
M20_dimer pfam07687
Peptidase dimerization domain; This domain consists of 4 beta strands and two alpha helices ...
 215-315 1.38e-04

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


Pssm-ID: 400158 [Multi-domain]  Cd Length: 107  Bit Score: 40.79  E-value: 1.38e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479606324  215 GLWWLQVTLTGKEAHtGSTPMRMRkNAslgLGKLLQLVNEIAmAHQPDAVGGVGHIDVSP------NSRNVLPGQIVFTV 288
Cdd:pfam07687   5 GLAGGHLTVKGKAGH-SGAPGKGV-NA---IKLLARLLAELP-AEYGDIGFDFPRTTLNItgieggTATNVIPAEAEAKF 78

                          90       100
                  ....*....|....*....|....*..
gi 479606324  289 DFRSPNQATLDGMKARFEKEAPKIAEE 315
Cdd:pfam07687  79 DIRLLPGEDLEELLEEIEAILEKELPE 105
M20_18_42 cd18669
M20, M18 and M42 Zn-peptidases include aminopeptidases and carboxypeptidases; This family ...
 66-148 1.87e-04

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: 42.42  E-value: 1.87e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479606324  66 NMFFTRPGEDSDAdPVYMGSHLDTQPTG----------------------GKFDGVLGVLGGLEVMRTLNDMNIRTKRPI 123
Cdd:cd18669    1 NVIARYGGGGGGK-RVLLGAHIDVVPAGegdprdppffvdtveegrlygrGALDDKGGVAAALEALKLLKENGFKLKGTV 79

                         90       100
                 ....*....|....*....|....*
gi 479606324 124 VVVNWTNEEGTRFAPAMLASGVFAG 148
Cdd:cd18669   80 VVAFTPDEEVGSGAGKGLLSKDALE 104
M20_Acy1_YxeP-like cd05669
M20 Peptidase aminoacyclase-1 YxeP-like proteins, including YxeP, YtnL, YjiB and HipO2; ...
 263-376 2.10e-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: 43.05  E-value: 2.10e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479606324 263 AVGGVGHIDvSPNSRNVLPGQIVFTVDFRSPNQATLDGMKARFEKEAPKIAEELGIGIEIEVaGHFDPVTFDTG-CVEAI 341
Cdd:cd05669  220 AVVSVTRIH-AGNTWNVIPDSAELEGTVRTFDAEVRQLVKERFEQIVEGIAAAFGAKIEFKW-HSGPPAVINDEeLTDLA 297

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 479606324 342 RNAAERLGYSHRNIV-SGAGHDACWVNRVAPTAMVM 376
Cdd:cd05669  298 SEVAAQAGYEVVHAEpSLGGEDFAFYQQKIPGVFAF 333
M28_Pgcp_like cd03883
M28 Zn-Peptidase Plasma glutamate carboxypeptidase; Peptidase M28 family; Plasma glutamate ...
 81-132 2.72e-04

M28 Zn-Peptidase Plasma glutamate carboxypeptidase; Peptidase M28 family; Plasma glutamate carboxypeptidase (PGCP; blood plasma glutamate carboxypeptidase; EC 3.4.17.21) subfamily. PGCP is a 56kDa glutamate carboxypeptidase that is mainly produced in mammalian placenta and kidney, the majority of which is thought to be secreted into the bloodstream. Similar proteins are also found in other species, including bacteria. These proteins contain protease-associated (PA) domain inserts between the first and second strands of the central beta sheet in the protease-like domain. The PA domains may participate in substrate binding and/or promoting conformational changes, which influence the stability and accessibility of the site to substrate. The exact physiological substrates of PGCP are unknown, although this enzyme may play an important role in the hydrolysis of circulating peptides. Its closest homolog encodes an important brain glutamate carboxypeptidase II (NAALADase) identical to the prostate-specific membrane antigen (PSMA), which serves as a marker for prostatic cancer metastasis. Hypermethylation of PGCP gene has been associated with human bronchial epithelial (HBE) cell immortalization and lung cancer. PGCP also provides an attractive target for serological analysis in hepatitis C virus (HCV)-induced hepatocellular carcinoma (HCC) patients.


Pssm-ID: 349879 [Multi-domain]  Cd Length: 425  Bit Score: 43.07  E-value: 2.72e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 479606324  81 VYMGSHLDTQPTG-GKFDGVLGVLGGLEVMRTLNDMNIRTKRPIVVVNWTNEE 132
Cdd:cd03883  243 VLVGGHLDSWDVGtGAMDDGGGVAISWEALKLIKDLGLKPKRTIRVVLWTGEE 295
M20_Acy1 cd03886
M20 Peptidase Aminoacylase 1 family; Peptidase M20 family, Aminoacylase 1 (ACY1; hippuricase; ...
 219-408 8.31e-04

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: 41.43  E-value: 8.31e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479606324 219 LQVTLTGKEAHtGSTPmRMRKN----ASLGLGKLLQLVNEIAMAHQPdAVGGVGHIDvSPNSRNVLPGQIVFTVDFRSPN 294
Cdd:cd03886  174 FEITVKGKGGH-GASP-HLGVDpivaAAQIVLALQTVVSRELDPLEP-AVVTVGKFH-AGTAFNVIPDTAVLEGTIRTFD 249

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479606324 295 QATLDGMKARFEKEAPKIAEELGIGIEIEVAGHFDPVTFDTGCVEAIRNAAERLG---YSHRNIVSGAGHDACWVNRVAP 371
Cdd:cd03886  250 PEVREALEARIKRLAEGIAAAYGATVELEYGYGYPAVINDPELTELVREAAKELLgeeAVVEPEPVMGSEDFAYYLEKVP 329

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 479606324 372 TAMVMCPCVDGLS-----HNEDEDISKEWASAGTDVLLHAVL 408
Cdd:cd03886  330 GAFFWLGAGEPDGenpglHSPTFDFDEDALPIGAALLAELAL 371
Peptidase_M28 pfam04389
Peptidase family M28;
70-132 1.34e-03

Peptidase family M28;


Pssm-ID: 461288 [Multi-domain]  Cd Length: 192  Bit Score: 39.58  E-value: 1.34e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 479606324   70 TRPGEDSDaDPVYMGSHLDTQPTG-GKFDGVLGVLGGLEVMRTLNDMNiRTKRPIVVVNWTNEE 132
Cdd:pfam04389   5 KLPGKAPD-EVVLLSAHYDSVGTGpGADDNASGVAALLELARVLAAGQ-RPKRSVRFLFFDAEE 66
M20_ArgE_DapE-like cd08011
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ...
 215-392 1.49e-03

M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate desuccinylases; Peptidase M20 family, uncharacterized protein subfamily with similarity to acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase (ArgE/DapE) subfamily. 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: 40.45  E-value: 1.49e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479606324 215 GLWWLQVTLTGKEAHtGSTPMRMRkNASLGLGKLLQ-LVNEIAMAHQPDAVGGVghidvspnSRNVLPGQIVFTVDFRSP 293
Cdd:cd08011  174 GLVWVIIEITGKPAH-GSLPHRGE-SAVKAAMKLIErLYELEKTVNPGVIKGGV--------KVNLVPDYCEFSVDIRLP 243

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479606324 294 NQATLDGMKARFEKEAPKIAEelgIGIEIEVAGHFDPVTFDTGCVEAIRNAA-ERLGYSHRNIVSGAGHDACWVNRVAPT 372
Cdd:cd08011  244 PGISTDEVLSRIIDHLDSIEE---VSFEIKSFYSPTVSNPDSEIVKKTEEAItEVLGIRPKEVISVGASDARFYRNAGIP 320

                        170       180
                 ....*....|....*....|
gi 479606324 373 AMVMCPCVDGLSHNEDEDIS 392
Cdd:cd08011  321 AIVYGPGRLGQMHAPNEYVE 340
M20_PAAh_like cd03896
M20 Peptidases, Poly(aspartic acid) hydrolase-like proteins; Peptidase M20 family, Poly ...
 143-411 3.32e-03

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


Pssm-ID: 349891 [Multi-domain]  Cd Length: 357  Bit Score: 39.39  E-value: 3.32e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479606324 143 SGVFAGVLDQNWAYERTDAKgktFGEELVRIGWKGDEPVGS-RKIHAMFELHieqGPILE----AEHKDIGVVTHGQGLW 217
Cdd:cd03896   91 KGSLACLLAMARAMKEAGAA---LKGDVVFAANVGEEGLGDlRGARYLLSAH---GARLDyfvvAEGTDGVPHTGAVGSK 164

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479606324 218 WLQVTLTGKEAHTgSTPMRMrKNASLGLGKLLQLVNEIAMAHQPDAVGGVGHIDVsPNSRNVLPGQIVFTVDFRSPNQAT 297
Cdd:cd03896  165 RFRITTVGPGGHS-YGAFGS-PSAIVAMAKLVEALYEWAAPYVPKTTFAAIRGGG-GTSVNRIANLCSMYLDIRSNPDAE 241

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479606324 298 LDGMKARFEKEAPKIAEELGiGIEIEVAGHFDPVTFDTGCVEAIRNAAERlgySHRNIVSGAGHDACWVNRVAPTAMVMc 377
Cdd:cd03896  242 LADVQREVEAVVSKLAAKHL-RVKARVKPVGDRPGGEAQGTEPLVNAAVA---AHREVGGDPRPGSSSTDANPANSLGI- 316

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 479606324 378 PCV------DGLSHNEDEDISKEWASAGTDVLLHAVLETA 411
Cdd:cd03896  317 PAVtyglgrGGNAHRGDEYVLKDDMLKGAKAYLMLAAALC 356
 
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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