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Conserved domains on  [gi|1002351805|pdb|5I4M|B]
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Chain B, Amidase, hydantoinase/carbamoylase family

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;
23-429 0e+00

Zn-dependent hydrolase;


:

Pssm-ID: 237250 [Multi-domain]  Cd Length: 412  Bit Score: 609.19  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5I4M_B        23 TSIKVDGRRLWDSLMEVAKIGATPKGGVCRLALTDLDKAARDLIVGWAKAAGCTVTVDTMGNVFMRRAGRVADAAPVVTG 102
Cdd:PRK12893   3 RNLRINGERLWDSLMALARIGATPGGGVTRLALTDEDREARDLLAQWMEEAGLTVSVDAIGNLFGRRAGTDPDAPPVLIG 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5I4M_B       103 SHADSQPTGGRFDGIYGVLGGLEVIRSLNDHGIETEHPVEVVIWTNEEGSRFAPAMVASGVFAGVFPLEYGLSRKDVDGK 182
Cdd:PRK12893  83 SHLDTQPTGGRFDGALGVLAALEVVRTLNDAGIRTRRPIEVVSWTNEEGARFAPAMLGSGVFTGALPLDDALARRDADGI 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5I4M_B       183 TIGEELARIGYAGDAPCGGRKLHAAFELHIEQGPILEAE*KTIGVVTDAQGQRWYEITFTGQEAHAGPTPMPRRRDALLG 262
Cdd:PRK12893 163 TLGEALARIGYRGTARVGRRAVDAYLELHIEQGPVLEAEGLPIGVVTGIQGIRWLEVTVEGQAAHAGTTPMAMRRDALVA 242

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5I4M_B       263 ASRVVDLVNRIGLDHAPYGCATVGMMQVHPNSRNVIPGRVFFTVDFRHPDDAVLAKMDAALRDGVARIAADIGLDTALEQ 342
Cdd:PRK12893 243 AARIILAVERIAAALAPDGVATVGRLRVEPNSRNVIPGKVVFTVDIRHPDDARLDAMEAALRAACAKIAAARGVQVTVET 322

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5I4M_B       343 IFYYAPIAFDSACVAAVRAAADRFGYSHRDIVSGAGHDACYLAQVAPTSMVFVPCIDGISHNEIEDATPAWIEAGANVLL 422
Cdd:PRK12893 323 VWDFPPVPFDPALVALVEAAAEALGLSHMRMVSGAGHDAMFLARVAPAAMIFVPCRGGISHNEAEDTEPADLAAGANVLL 402


                 ....*..
5I4M_B       423 HAMLSRA 429
Cdd:PRK12893 403 HAVLELA 409
 
Name Accession Description Interval E-value
PRK12893 PRK12893
Zn-dependent hydrolase;
23-429 0e+00

Zn-dependent hydrolase;


Pssm-ID: 237250 [Multi-domain]  Cd Length: 412  Bit Score: 609.19  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5I4M_B        23 TSIKVDGRRLWDSLMEVAKIGATPKGGVCRLALTDLDKAARDLIVGWAKAAGCTVTVDTMGNVFMRRAGRVADAAPVVTG 102
Cdd:PRK12893   3 RNLRINGERLWDSLMALARIGATPGGGVTRLALTDEDREARDLLAQWMEEAGLTVSVDAIGNLFGRRAGTDPDAPPVLIG 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5I4M_B       103 SHADSQPTGGRFDGIYGVLGGLEVIRSLNDHGIETEHPVEVVIWTNEEGSRFAPAMVASGVFAGVFPLEYGLSRKDVDGK 182
Cdd:PRK12893  83 SHLDTQPTGGRFDGALGVLAALEVVRTLNDAGIRTRRPIEVVSWTNEEGARFAPAMLGSGVFTGALPLDDALARRDADGI 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5I4M_B       183 TIGEELARIGYAGDAPCGGRKLHAAFELHIEQGPILEAE*KTIGVVTDAQGQRWYEITFTGQEAHAGPTPMPRRRDALLG 262
Cdd:PRK12893 163 TLGEALARIGYRGTARVGRRAVDAYLELHIEQGPVLEAEGLPIGVVTGIQGIRWLEVTVEGQAAHAGTTPMAMRRDALVA 242

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5I4M_B       263 ASRVVDLVNRIGLDHAPYGCATVGMMQVHPNSRNVIPGRVFFTVDFRHPDDAVLAKMDAALRDGVARIAADIGLDTALEQ 342
Cdd:PRK12893 243 AARIILAVERIAAALAPDGVATVGRLRVEPNSRNVIPGKVVFTVDIRHPDDARLDAMEAALRAACAKIAAARGVQVTVET 322

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5I4M_B       343 IFYYAPIAFDSACVAAVRAAADRFGYSHRDIVSGAGHDACYLAQVAPTSMVFVPCIDGISHNEIEDATPAWIEAGANVLL 422
Cdd:PRK12893 323 VWDFPPVPFDPALVALVEAAAEALGLSHMRMVSGAGHDAMFLARVAPAAMIFVPCRGGISHNEAEDTEPADLAAGANVLL 402


                 ....*..
5I4M_B       423 HAMLSRA 429
Cdd:PRK12893 403 HAVLELA 409
M20_bAS cd03884
M20 Peptidase beta-alanine synthase, an amidohydrolase; Peptidase M20 family, beta-alanine ...
 32-426 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: 590.26  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5I4M_B       32 LWDSLMEVAKIGATPKGGVCRLALTDLDKAARDLIVGWAKAAGCTVTVDTMGNVFMRRAGRVADAAPVVTGSHADSQPTG 111
Cdd:cd03884   1 LWDRLEELAAIGATPAGGVTRLALTDEDRAARDLFVEWMEEAGLSVRVDAVGNLFGRLEGTDPDAPPVLTGSHLDTVPNG 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5I4M_B      112 GRFDGIYGVLGGLEVIRSLNDHGIETEHPVEVVIWTNEEGSRFAPAMVASGVFAGVFPLEYGLSRKDVDGKTIGEELARI 191
Cdd:cd03884  81 GRYDGILGVLAGLEALRALKEAGIRPRRPIEVVAFTNEEGSRFPPSMLGSRAFAGTLDLEELLSLRDADGVSLAEALKAI 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5I4M_B      192 GYAGDAPC---GGRKLHAAFELHIEQGPILEAE*KTIGVVTDAQGQRWYEITFTGQEAHAGPTPMPRRRDALLGASRVVD 268
Cdd:cd03884 161 GYDGDRPAsarRPGDIKAYVELHIEQGPVLEEEGLPIGVVTGIAGQRWLEVTVTGEAGHAGTTPMALRRDALLAAAELIL 240

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5I4M_B      269 LVNRIGLDHAPYGCATVGMMQVHPNSRNVIPGRVFFTVDFRHPDDAVLAKMDAALRDGVARIAADIGLDTALEQIFYYAP 348
Cdd:cd03884 241 AVEEIALEHGDDLVATVGRIEVKPNAVNVIPGEVEFTLDLRHPDDAVLDAMVERIRAEAEAIAAERGVEVEVERLWDSPP 320

                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
5I4M_B      349 IAFDSACVAAVRAAADRFGYSHRDIVSGAGHDACYLAQVAPTSMVFVPCIDGISHNEIEDATPAWIEAGANVLLHAML 426
Cdd:cd03884 321 VPFDPELVAALEAAAEALGLSYRRMPSGAGHDAMFMARICPTAMIFVPSRDGISHNPAEYTSPEDLAAGVQVLLHALL 398
hydantase TIGR01879
amidase, hydantoinase/carbamoylase family; Enzymes in this subfamily hydrolize the amide bonds ...
 31-426 2.22e-134

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: 391.87  E-value: 2.22e-134
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5I4M_B         31 RLWDSLMEVAKIGATPKGGVCRLALTDLDKAARDLIVGWAKAAGCTVTVDTMGNVFMRRAGRVADAAPVVTGSHADSQPT 110
Cdd:TIGR01879   2 RLWETLMWLGEVGADPAGGMTRLALSPEDREAQDLFKKRMRAAGLEVRFDEVGNLIGRKEGTEPPLEVVLSGSHLDTVVN 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5I4M_B        111 GGRFDGIYGVLGGLEVIRSLNDHGIETEHPVEVVIWTNEEGSRFAPAMVASGVFAGVFPLEYGLSRKDVDGKTIGEELAR 190
Cdd:TIGR01879  82 GGNFDGQLGVLAGIEVVDALKEAYVVPLHPIEVVAFTEEEGSRFPYGMWGSRNMVGLANPEDVRNICDAKGISFAEAMKA 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5I4M_B        191 IG--YAGDAPCGGRKLHAAFELHIEQGPILEAE*KTIGVVTDAQGQRWYEITFTGQEAHAGPTPMPRRRDALLGASRVVD 268
Cdd:TIGR01879 162 CGpdLPNQPLRPRGDIKAYVELHIEQGPVLESNGQPIGVVNAIAGQRWYKVTLNGESNHAGTTPMSLRRDPLVAASRIIH 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5I4M_B        269 LVNRIGLDHAPyGCATVGMMQVHPNSRNVIPGRVFFTVDFRHPDDAVLAKMDAALRDGVARIAADIGLDTALEQIFYYAP 348
Cdd:TIGR01879 242 QVEEKAKRGDP-TVGTVGKVEARPNGVNVIPGKVTFTLDLRHTDAAVLRDFTQQLENDIKAISDERDIGIDIERWMDEPP 320

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
5I4M_B        349 IAFDSACVAAVRAAADRFGYSHRDIVSGAGHDACYLAQVAPTSMVFVPCIDGISHNEIEDATPAWIEAGANVLLHAML 426
Cdd:TIGR01879 321 VPCSEELVAALTELCERLGYNARVMVSGAGHDAQILAPIVPIGMIFIPSINGISHNPAEWSNITDCAEGAKVLYLMVY 398
Peptidase_M20 pfam01546
Peptidase family M20/M25/M40; This family includes a range of zinc metallopeptidases belonging ...
 100-426 1.04e-44

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


Pssm-ID: 460247 [Multi-domain]  Cd Length: 315  Bit Score: 157.89  E-value: 1.04e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5I4M_B        100 VTGSHADSQPTG------------------GRFDGIYGVLGGLEVIRSLNDHGIeTEHPVEVVIWTNEEGSRF-APAMVA 160
Cdd:pfam01546   1 LLRGHMDVVPDEetwgwpfkstedgklygrGHDDMKGGLLAALEALRALKEEGL-KKGTVKLLFQPDEEGGMGgARALIE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5I4M_B        161 SGVFAGvfpleyglsrkdvdgktigeelarigyagdapcggRKLHAAFELHIEQGPILEaE*KTIGVVTDAQGQRWYEIT 240
Cdd:pfam01546  80 DGLLER-----------------------------------EKVDAVFGLHIGEPTLLE-GGIAIGVVTGHRGSLRFRVT 123

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5I4M_B        241 FTGQEAHAGpTPmPRRRDALLGASRVV----DLVNRIgLDHAPYGCATVGMMQVHPNSRNVIPGRVFFTVDFRHPDDAVL 316
Cdd:pfam01546 124 VKGKGGHAS-TP-HLGVNAIVAAARLIlalqDIVSRN-VDPLDPAVVTVGNITGIPGGVNVIPGEAELKGDIRLLPGEDL 200

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5I4M_B        317 AKMDAALRDGVARIAADIGLDTALEQIFYYAPIAFDSACVAAV--RAAADRFGYSHRDIVSG--AGHDACYLAQ-VAPTS 391
Cdd:pfam01546 201 EELEERIREILEAIAAAYGVKVEVEYVEGGAPPLVNDSPLVAAlrEAAKELFGLKVELIVSGsmGGTDAAFFLLgVPPTV 280

                         330       340       350
                  ....*....|....*....|....*....|....*
5I4M_B        392 MVFVPCiDGISHNEIEDATPAWIEAGANVLLHAML 426
Cdd:pfam01546 281 VFFGPG-SGLAHSPNEYVDLDDLEKGAKVLARLLL 314
ArgE COG0624
Acetylornithine deacetylase/Succinyl-diaminopimelate desuccinylase or related deacylase [Amino ...
 59-393 2.43e-11

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: 64.91  E-value: 2.43e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5I4M_B       59 DKAARDLIVGWAKAAGCTVTV----DTMGNVFMRRAGRvADAAPVVTGSHADSQPTGGR-------FDG------IYG-- 119
Cdd:COG0624  31 EAAAAELLAELLEALGFEVERlevpPGRPNLVARRPGD-GGGPTLLLYGHLDVVPPGDLelwtsdpFEPtiedgrLYGrg 109

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5I4M_B      120 -------VLGGLEVIRSLNDHGIETEHPVEVVIWTNEE-GSRFAPAMVASGvfAGVFPLEYGLsrkdvdgktIGEelari 191
Cdd:COG0624 110 aadmkggLAAMLAALRALLAAGLRLPGNVTLLFTGDEEvGSPGARALVEEL--AEGLKADAAI---------VGE----- 173

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5I4M_B      192 GYAGDAPCGGRKlhaafelhieqgpileae*ktigvvtdaqGQRWYEITFTGQEAHAGptpMPRR-RDALLGASRVVDLV 270
Cdd:COG0624 174 PTGVPTIVTGHK-----------------------------GSLRFELTVRGKAAHSS---RPELgVNAIEALARALAAL 221

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5I4M_B      271 NRIGLD---HAPYGCAT--VGMMQVhPNSRNVIPGRVFFTVDFRHPDDAVLAKMDAALRDGVARIAADIGLDtaLEQIFY 345
Cdd:COG0624 222 RDLEFDgraDPLFGRTTlnVTGIEG-GTAVNVIPDEAEAKVDIRLLPGEDPEEVLAALRALLAAAAPGVEVE--VEVLGD 298

                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|..
5I4M_B      346 YAP---IAFDSACVAAVRAAADR-FGYSHRDIVSGAGHDACYLAQVAPTSMV 393
Cdd:COG0624 299 GRPpfeTPPDSPLVAAARAAIREvTGKEPVLSGVGGGTDARFFAEALGIPTV 350
 
Name Accession Description Interval E-value
PRK12893 PRK12893
Zn-dependent hydrolase;
23-429 0e+00

Zn-dependent hydrolase;


Pssm-ID: 237250 [Multi-domain]  Cd Length: 412  Bit Score: 609.19  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5I4M_B        23 TSIKVDGRRLWDSLMEVAKIGATPKGGVCRLALTDLDKAARDLIVGWAKAAGCTVTVDTMGNVFMRRAGRVADAAPVVTG 102
Cdd:PRK12893   3 RNLRINGERLWDSLMALARIGATPGGGVTRLALTDEDREARDLLAQWMEEAGLTVSVDAIGNLFGRRAGTDPDAPPVLIG 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5I4M_B       103 SHADSQPTGGRFDGIYGVLGGLEVIRSLNDHGIETEHPVEVVIWTNEEGSRFAPAMVASGVFAGVFPLEYGLSRKDVDGK 182
Cdd:PRK12893  83 SHLDTQPTGGRFDGALGVLAALEVVRTLNDAGIRTRRPIEVVSWTNEEGARFAPAMLGSGVFTGALPLDDALARRDADGI 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5I4M_B       183 TIGEELARIGYAGDAPCGGRKLHAAFELHIEQGPILEAE*KTIGVVTDAQGQRWYEITFTGQEAHAGPTPMPRRRDALLG 262
Cdd:PRK12893 163 TLGEALARIGYRGTARVGRRAVDAYLELHIEQGPVLEAEGLPIGVVTGIQGIRWLEVTVEGQAAHAGTTPMAMRRDALVA 242

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5I4M_B       263 ASRVVDLVNRIGLDHAPYGCATVGMMQVHPNSRNVIPGRVFFTVDFRHPDDAVLAKMDAALRDGVARIAADIGLDTALEQ 342
Cdd:PRK12893 243 AARIILAVERIAAALAPDGVATVGRLRVEPNSRNVIPGKVVFTVDIRHPDDARLDAMEAALRAACAKIAAARGVQVTVET 322

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5I4M_B       343 IFYYAPIAFDSACVAAVRAAADRFGYSHRDIVSGAGHDACYLAQVAPTSMVFVPCIDGISHNEIEDATPAWIEAGANVLL 422
Cdd:PRK12893 323 VWDFPPVPFDPALVALVEAAAEALGLSHMRMVSGAGHDAMFLARVAPAAMIFVPCRGGISHNEAEDTEPADLAAGANVLL 402


                 ....*..
5I4M_B       423 HAMLSRA 429
Cdd:PRK12893 403 HAVLELA 409
PRK09290 PRK09290
allantoate amidohydrolase; Reviewed
 25-432 0e+00

allantoate amidohydrolase; Reviewed


Pssm-ID: 236456 [Multi-domain]  Cd Length: 413  Bit Score: 608.31  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5I4M_B        25 IKVDGRRLWDSLMEVAKIGATPKGGVCRLALTDLDKAARDLIVGWAKAAGCTVTVDTMGNVFMRRAGRVADAAPVVTGSH 104
Cdd:PRK09290   2 LRIDAERLWARLDELAKIGATPDGGVTRLALSPEDLQARDLFAEWMEAAGLTVRVDAVGNLFGRLEGRDPDAPAVLTGSH 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5I4M_B       105 ADSQPTGGRFDGIYGVLGGLEVIRSLNDHGIETEHPVEVVIWTNEEGSRFAPAMVASGVFAGVFPLEYGLSRKDVDGKTI 184
Cdd:PRK09290  82 LDTVPNGGRFDGPLGVLAGLEAVRTLNERGIRPRRPIEVVAFTNEEGSRFGPAMLGSRVFTGALTPEDALALRDADGVSF 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5I4M_B       185 GEELARIGYAGDAPCGGR----KLHAAFELHIEQGPILEAE*KTIGVVTDAQGQRWYEITFTGQEAHAGPTPMPRRRDAL 260
Cdd:PRK09290 162 AEALAAIGYDGDEAVGAArarrDIKAFVELHIEQGPVLEAEGLPIGVVTGIVGQRRYRVTFTGEANHAGTTPMALRRDAL 241

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5I4M_B       261 LGASRVVDLVNRIGLDHAPYGCATVGMMQVHPNSRNVIPGRVFFTVDFRHPDDAVLAKMDAALRDGVARIAADIGLDTAL 340
Cdd:PRK09290 242 LAAAEIILAVERIAAAHGPDLVATVGRLEVKPNSVNVIPGEVTFTLDIRHPDDAVLDALVAELRAAAEAIAARRGVEVEI 321

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5I4M_B       341 EQIFYYAPIAFDSACVAAVRAAADRFGYSHRDIVSGAGHDACYLAQVAPTSMVFVPCIDGISHNEIEDATPAWIEAGANV 420
Cdd:PRK09290 322 ELISRRPPVPFDPGLVAALEEAAERLGLSYRRLPSGAGHDAQILAAVVPTAMIFVPSVGGISHNPAEFTSPEDCAAGANV 401

                        410
                 ....*....|..
5I4M_B       421 LLHAMLSRACEP 432
Cdd:PRK09290 402 LLHALLELAEEG 413
M20_bAS cd03884
M20 Peptidase beta-alanine synthase, an amidohydrolase; Peptidase M20 family, beta-alanine ...
 32-426 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: 590.26  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5I4M_B       32 LWDSLMEVAKIGATPKGGVCRLALTDLDKAARDLIVGWAKAAGCTVTVDTMGNVFMRRAGRVADAAPVVTGSHADSQPTG 111
Cdd:cd03884   1 LWDRLEELAAIGATPAGGVTRLALTDEDRAARDLFVEWMEEAGLSVRVDAVGNLFGRLEGTDPDAPPVLTGSHLDTVPNG 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5I4M_B      112 GRFDGIYGVLGGLEVIRSLNDHGIETEHPVEVVIWTNEEGSRFAPAMVASGVFAGVFPLEYGLSRKDVDGKTIGEELARI 191
Cdd:cd03884  81 GRYDGILGVLAGLEALRALKEAGIRPRRPIEVVAFTNEEGSRFPPSMLGSRAFAGTLDLEELLSLRDADGVSLAEALKAI 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5I4M_B      192 GYAGDAPC---GGRKLHAAFELHIEQGPILEAE*KTIGVVTDAQGQRWYEITFTGQEAHAGPTPMPRRRDALLGASRVVD 268
Cdd:cd03884 161 GYDGDRPAsarRPGDIKAYVELHIEQGPVLEEEGLPIGVVTGIAGQRWLEVTVTGEAGHAGTTPMALRRDALLAAAELIL 240

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5I4M_B      269 LVNRIGLDHAPYGCATVGMMQVHPNSRNVIPGRVFFTVDFRHPDDAVLAKMDAALRDGVARIAADIGLDTALEQIFYYAP 348
Cdd:cd03884 241 AVEEIALEHGDDLVATVGRIEVKPNAVNVIPGEVEFTLDLRHPDDAVLDAMVERIRAEAEAIAAERGVEVEVERLWDSPP 320

                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
5I4M_B      349 IAFDSACVAAVRAAADRFGYSHRDIVSGAGHDACYLAQVAPTSMVFVPCIDGISHNEIEDATPAWIEAGANVLLHAML 426
Cdd:cd03884 321 VPFDPELVAALEAAAEALGLSYRRMPSGAGHDAMFMARICPTAMIFVPSRDGISHNPAEYTSPEDLAAGVQVLLHALL 398
PRK12891 PRK12891
allantoate amidohydrolase; Reviewed
 26-429 0e+00

allantoate amidohydrolase; Reviewed


Pssm-ID: 237249  Cd Length: 414  Bit Score: 521.30  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5I4M_B        26 KVDGRRLWDSLMEVAKIGATPKGGVCRLALTDLDKAARDLIVGWAKAAGCTVTVDTMGNVFMRRAGRVADAAPVVTGSHA 105
Cdd:PRK12891   6 RVDGERLWASLERMAQIGATPKGGVCRLALTDGDREARDLFVAWARDAGCTVRVDAMGNLFARRAGRDPDAAPVMTGSHA 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5I4M_B       106 DSQPTGGRFDGIYGVLGGLEVIRSLNDHGIETEHPVEVVIWTNEEGSRFAPAMVASGVFAGVFPLEYGLSRKDVDGKTIG 185
Cdd:PRK12891  86 DSQPTGGRYDGIYGVLGGLEVVRALNDAGIETERPVDVVIWTNEEGSRFAPSMVGSGVFFGVYPLEYLLSRRDDTGRTLG 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5I4M_B       186 EELARIGYAGDAPCGGRKLHAAFELHIEQGPILEAE*KTIGVVTDAQGQRWYEITFTGQEAHAGPTPMPRRRDALLGASR 265
Cdd:PRK12891 166 EHLARIGYAGAEPVGGYPVHAAYELHIEQGAILERAGKTIGVVTAGQGQRWYEVTLTGVDAHAGTTPMAFRRDALVGAAR 245

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5I4M_B       266 VVDLVNRIGLDHAPYGCATVGMMQVHPNSRNVIPGRVFFTVDFRHPDDAVLAKMDAALRDGVARIAADIGLDTALEQIFY 345
Cdd:PRK12891 246 MIAFLDALGRRDAPDARATVGMIDARPNSRNTVPGECFFTVEFRHPDDAVLDRLDAALRAELARIADETGLRADIEQIFG 325

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5I4M_B       346 YAPIAFDSACVAAVRAAADRFGYSHRDIVSGAGHDACYLAQVAPTSMVFVPCIDGISHNEIEDATPAWIEAGANVLLHAM 425
Cdd:PRK12891 326 YAPAPFAPGCIDAVRDAARALGLSHMDIVSGAGHDACFAARGAPTGMIFVPCVDGLSHNEAEAITPEWFAAGADVLLRAV 405


                 ....
5I4M_B       426 LSRA 429
Cdd:PRK12891 406 LQSA 409
PRK12890 PRK12890
allantoate amidohydrolase; Reviewed
 23-429 3.83e-160

allantoate amidohydrolase; Reviewed


Pssm-ID: 237248 [Multi-domain]  Cd Length: 414  Bit Score: 457.83  E-value: 3.83e-160
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5I4M_B        23 TSIKVDGRRLWDSLMEVAKIGATPkGGVCRLALTDLDKAARDLIVGWAKAAGCTVTVDTMGNVFMRRAGRVADAAPVVTG 102
Cdd:PRK12890   2 TPPPINGERLLARLEELAAIGRDG-PGWTRLALSDEERAARALLAAWMRAAGLEVRRDAAGNLFGRLPGRDPDLPPLMTG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5I4M_B       103 SHADSQPTGGRFDGIYGVLGGLEVIRSLNDHGIETEHPVEVVIWTNEEGSRFAPAMVASGVFAGVFPLEYGLSRKDVDGK 182
Cdd:PRK12890  81 SHLDTVPNGGRYDGILGVLAGLEVVAALREAGIRPPHPLEVIAFTNEEGVRFGPSMIGSRALAGTLDVEAVLATRDDDGT 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5I4M_B       183 TIGEELARIGYAGDAPCGGRKLHAA----FELHIEQGPILEAE*KTIGVVTDAQGQRWYEITFTGQEAHAGPTPMPRRRD 258
Cdd:PRK12890 161 TLAEALRRIGGDPDALPGALRPPGAvaafLELHIEQGPVLEAEGLPIGVVTAIQGIRRQAVTVEGEANHAGTTPMDLRRD 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5I4M_B       259 ALLGASRVVDLVNRIGLDHAPYGCATVGMMQVHPNSRNVIPGRVFFTVDFRHPDDAVLAKMDAALRDGVARIAADIGLDT 338
Cdd:PRK12890 241 ALVAAAELVTAMERRARALLHDLVATVGRLDVEPNAINVVPGRVVFTLDLRSPDDAVLEAAEAALLAELEAIAAARGVRI 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5I4M_B       339 ALEQIFYYAPIAFDSACVAAVRAAADRFGYSHRDIVSGAGHDACYLAQVAPTSMVFVPCIDGISHNEIEDATPAWIEAGA 418
Cdd:PRK12890 321 ELERLSRSEPVPCDPALVDAVEAAAARLGYPSRRMPSGAGHDAAAIARIGPSAMIFVPCRGGISHNPEEAMDPEDLAAGA 400

                        410
                 ....*....|.
5I4M_B       419 NVLLHAMLSRA 429
Cdd:PRK12890 401 RVLLDAVLRLD 411
hydantase TIGR01879
amidase, hydantoinase/carbamoylase family; Enzymes in this subfamily hydrolize the amide bonds ...
 31-426 2.22e-134

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: 391.87  E-value: 2.22e-134
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5I4M_B         31 RLWDSLMEVAKIGATPKGGVCRLALTDLDKAARDLIVGWAKAAGCTVTVDTMGNVFMRRAGRVADAAPVVTGSHADSQPT 110
Cdd:TIGR01879   2 RLWETLMWLGEVGADPAGGMTRLALSPEDREAQDLFKKRMRAAGLEVRFDEVGNLIGRKEGTEPPLEVVLSGSHLDTVVN 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5I4M_B        111 GGRFDGIYGVLGGLEVIRSLNDHGIETEHPVEVVIWTNEEGSRFAPAMVASGVFAGVFPLEYGLSRKDVDGKTIGEELAR 190
Cdd:TIGR01879  82 GGNFDGQLGVLAGIEVVDALKEAYVVPLHPIEVVAFTEEEGSRFPYGMWGSRNMVGLANPEDVRNICDAKGISFAEAMKA 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5I4M_B        191 IG--YAGDAPCGGRKLHAAFELHIEQGPILEAE*KTIGVVTDAQGQRWYEITFTGQEAHAGPTPMPRRRDALLGASRVVD 268
Cdd:TIGR01879 162 CGpdLPNQPLRPRGDIKAYVELHIEQGPVLESNGQPIGVVNAIAGQRWYKVTLNGESNHAGTTPMSLRRDPLVAASRIIH 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5I4M_B        269 LVNRIGLDHAPyGCATVGMMQVHPNSRNVIPGRVFFTVDFRHPDDAVLAKMDAALRDGVARIAADIGLDTALEQIFYYAP 348
Cdd:TIGR01879 242 QVEEKAKRGDP-TVGTVGKVEARPNGVNVIPGKVTFTLDLRHTDAAVLRDFTQQLENDIKAISDERDIGIDIERWMDEPP 320

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
5I4M_B        349 IAFDSACVAAVRAAADRFGYSHRDIVSGAGHDACYLAQVAPTSMVFVPCIDGISHNEIEDATPAWIEAGANVLLHAML 426
Cdd:TIGR01879 321 VPCSEELVAALTELCERLGYNARVMVSGAGHDAQILAPIVPIGMIFIPSINGISHNPAEWSNITDCAEGAKVLYLMVY 398
PRK12892 PRK12892
allantoate amidohydrolase; Reviewed
 22-421 2.88e-117

allantoate amidohydrolase; Reviewed


Pssm-ID: 183817 [Multi-domain]  Cd Length: 412  Bit Score: 348.62  E-value: 2.88e-117
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5I4M_B        22 DTSIKVDGRRLWDSLMEVAKIGATpKGGVCRLALTDLDKAARDLIVGWAKAAGCTVTVDTMGNVFMRRAGrvADAAP-VV 100
Cdd:PRK12892   2 LAMLRIDGQRVLDDLMELAAIGAA-KTGVHRPTYSDAHVAARRRLAAWCEAAGLAVRIDGIGNVFGRLPG--PGPGPaLL 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5I4M_B       101 TGSHADSQPTGGRFDGIYGVLGGLEVIRSLNDHGIETEHPVEVVIWTNEEGSRFAPAMVASGVFAGVFPLEYGLSRK-DV 179
Cdd:PRK12892  79 VGSHLDSQNLGGRYDGALGVVAGLEAARALNEHGIATRHPLDVVAWCDEEGSRFTPGFLGSRAYAGRLDPADALAARcRS 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5I4M_B       180 DGKTIGEELARIGYAGDAPCGGRK--LHAAFELHIEQGPILEAE*KTIGVVTDAQGQRWYEITFTGQEAHAGPTPMPRRR 257
Cdd:PRK12892 159 DGVPLRDALAAAGLAGRPRPAADRarPKGYLEAHIEQGPVLEQAGLPVGVVTGIVGIWQYRITVTGEAGHAGTTPMALRR 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5I4M_B       258 DALLGASRVVDLVNRigldHAPYGCA----TVGMMQVHPNSRNVIPGRVFFTVDFRHPDDAVLAKMDAALRDGVARIAAD 333
Cdd:PRK12892 239 DAGLAAAEMIAAIDE----HFPRVCGpavvTVGRVALDPGSPSIIPGRVEFSFDARHPSPPVLQRLVALLEALCREIARR 314

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5I4M_B       334 IGLDTALEQIFYYAPIAFDSACVAAVRAAADRFGYSHRDIVSGAGHDACYLAQVAPTSMVFVPCIDGISHNEIEDATPAW 413
Cdd:PRK12892 315 RGCRVSVDRIAEYAPAPCDAALVDALRAAAEAAGGPYLEMPSGAGHDAQNMARIAPSAMLFVPSKGGISHNPAEDTSPAD 394


                 ....*...
5I4M_B       414 IEAGANVL 421
Cdd:PRK12892 395 LAQGARVL 402
PRK13799 PRK13799
unknown domain/N-carbamoyl-L-amino acid hydrolase fusion protein; Provisional
 29-425 1.31e-59

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


Pssm-ID: 106740 [Multi-domain]  Cd Length: 591  Bit Score: 204.47  E-value: 1.31e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5I4M_B        29 GRRLWDSLMEVAK---IGATPKGGVCRLALTDLDKAARDLIVGWAKAAGC-TVTVDTMGNVFMRRAGRVADAAPVVTGSH 104
Cdd:PRK13799 180 GADVMDWAEDIAAhsdPGYADEGALTCTYLSDAHRACANQISDWMRDAGFdEVEIDAVGNVVGRYKAADDDAKTLITGSH 259

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5I4M_B       105 ADSQPTGGRFDGIYGVLGGLEVIRSLNDHGIETEHPVEVVIWTNEEGSRFAPAMVASGVFAGVFPLEYgLSRKDVDGKTI 184
Cdd:PRK13799 260 YDTVRNGGKYDGREGIFLAIACVKELHEQGERLPFHFEVIAFAEEEGQRFKATFLGSGALIGDFNMEL-LDIKDADGISL 338

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5I4M_B       185 GEELARIGYAGDA-PCGGR---KLHAAFELHIEQGPILEAE*KTIGVVTDAQGQRWYEITFTGQEAHAGPTPMPRRRDAL 260
Cdd:PRK13799 339 REAIQHAGHCIDAiPKIARdpaDVLGFIEVHIEQGPVLLELDIPLGIVTSIAGSARYICEFIGMASHAGTTPMDMRKDAA 418

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5I4M_B       261 LGASRVVDLV-NRIGLDHAPYGCATVGMMQVHPNSRNVIPGRVFFTVDFRHPDDAVLAKMDAALRDGVARIAADIGLDTA 339
Cdd:PRK13799 419 AAAAEIALYIeKRAAQDQHASLVATMGQLNVPSGSTNVIPGRCQFSLDIRAATDEIRDAAVADILAEIAAIAARRGIEYK 498

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5I4M_B       340 LEQIFYYAPIAFDSACVAAVRAAADRFGYSHRDIVSGAGHDACYLAQVAPTSMVFVPCID-GISHNEIEDATPAWIEAGA 418
Cdd:PRK13799 499 AELAMKAAAAPCAPELMKQLEAATDAAGVPLFELASGAGHDAMKIAEIMDQAMLFTRCGNaGISHNPLESMTADDMELSA 578


                 ....*..
5I4M_B       419 NVLLHAM 425
Cdd:PRK13799 579 DAFLDFL 585
PRK13590 PRK13590
putative bifunctional OHCU decarboxylase/allantoate amidohydrolase; Provisional
 29-431 1.36e-56

putative bifunctional OHCU decarboxylase/allantoate amidohydrolase; Provisional


Pssm-ID: 184168 [Multi-domain]  Cd Length: 591  Bit Score: 196.51  E-value: 1.36e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5I4M_B        29 GRRLWD---SLMEVAKIGATPKGGVCRLALTDLDKAARDLIVGWAKAAGC-TVTVDTMGNVFMRRAGRVADAAPVVTGSH 104
Cdd:PRK13590 180 GNDVWDwaeRLAAHSDPGYAEKGQLTVTYLTDAHRACAQQISHWMRDCGFdEVHIDAVGNVVGRYKGSTPQAKRLLTGSH 259

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5I4M_B       105 ADSQPTGGRFDGIYGVLGGLEVIRSLNDHGIETEHPVEVVIWTNEEGSRFAPAMVASGVFAGVFPLEYgLSRKDVDGKTI 184
Cdd:PRK13590 260 YDTVRNGGKYDGRLGIFVPMACVRELHRQGRRLPFGLEVVGFAEEEGQRYKATFLGSGALIGDFDPAW-LDQKDADGITM 338

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5I4M_B       185 GEELARIGYAGDAPCGGRKLHAAF----ELHIEQGPILEAE*KTIGVVTDAQGQRWYEITFTGQEAHAGPTPMPRRRDAL 260
Cdd:PRK13590 339 REAMQHAGLCIDDIPKLRRDPARYlgfvEVHIEQGPVLNELDLPLGIVTSINGSVRYVGEMIGMASHAGTTPMDRRRDAA 418

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5I4M_B       261 LGASRVVDLV-NRIGLDhaPYGCATVGMMQVHPNSRNVIPGRVFFTVDFRHPDDAVLAKMDAALRDGVARIAADIGLDTA 339
Cdd:PRK13590 419 AAVAELALYVeQRAAQD--GDSVGTVGMLEVPGGSINVVPGRCRFSLDIRAPTDAQRDAMVADVLAELEAICERRGLRYT 496

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5I4M_B       340 LEQIFYYAPIAFDSACVAAVRAAADRFGYSHRDIVSGAGHDACYLAQVAPTSMVFVPCID-GISHNEIEDATPAWIEAGA 418
Cdd:PRK13590 497 LEETMRAAAAPSAPAWQQRWEAAVAALGLPLFRMPSGAGHDAMKLHEIMPQAMLFVRGENaGISHNPLESSTADDMQLAV 576

                        410
                 ....*....|...
5I4M_B       419 NVLLHAMLSRACE 431
Cdd:PRK13590 577 QAFQHLLDQLAAE 589
Peptidase_M20 pfam01546
Peptidase family M20/M25/M40; This family includes a range of zinc metallopeptidases belonging ...
 100-426 1.04e-44

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


Pssm-ID: 460247 [Multi-domain]  Cd Length: 315  Bit Score: 157.89  E-value: 1.04e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5I4M_B        100 VTGSHADSQPTG------------------GRFDGIYGVLGGLEVIRSLNDHGIeTEHPVEVVIWTNEEGSRF-APAMVA 160
Cdd:pfam01546   1 LLRGHMDVVPDEetwgwpfkstedgklygrGHDDMKGGLLAALEALRALKEEGL-KKGTVKLLFQPDEEGGMGgARALIE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5I4M_B        161 SGVFAGvfpleyglsrkdvdgktigeelarigyagdapcggRKLHAAFELHIEQGPILEaE*KTIGVVTDAQGQRWYEIT 240
Cdd:pfam01546  80 DGLLER-----------------------------------EKVDAVFGLHIGEPTLLE-GGIAIGVVTGHRGSLRFRVT 123

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5I4M_B        241 FTGQEAHAGpTPmPRRRDALLGASRVV----DLVNRIgLDHAPYGCATVGMMQVHPNSRNVIPGRVFFTVDFRHPDDAVL 316
Cdd:pfam01546 124 VKGKGGHAS-TP-HLGVNAIVAAARLIlalqDIVSRN-VDPLDPAVVTVGNITGIPGGVNVIPGEAELKGDIRLLPGEDL 200

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5I4M_B        317 AKMDAALRDGVARIAADIGLDTALEQIFYYAPIAFDSACVAAV--RAAADRFGYSHRDIVSG--AGHDACYLAQ-VAPTS 391
Cdd:pfam01546 201 EELEERIREILEAIAAAYGVKVEVEYVEGGAPPLVNDSPLVAAlrEAAKELFGLKVELIVSGsmGGTDAAFFLLgVPPTV 280

                         330       340       350
                  ....*....|....*....|....*....|....*
5I4M_B        392 MVFVPCiDGISHNEIEDATPAWIEAGANVLLHAML 426
Cdd:pfam01546 281 VFFGPG-SGLAHSPNEYVDLDDLEKGAKVLARLLL 314
ArgE COG0624
Acetylornithine deacetylase/Succinyl-diaminopimelate desuccinylase or related deacylase [Amino ...
 59-393 2.43e-11

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: 64.91  E-value: 2.43e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5I4M_B       59 DKAARDLIVGWAKAAGCTVTV----DTMGNVFMRRAGRvADAAPVVTGSHADSQPTGGR-------FDG------IYG-- 119
Cdd:COG0624  31 EAAAAELLAELLEALGFEVERlevpPGRPNLVARRPGD-GGGPTLLLYGHLDVVPPGDLelwtsdpFEPtiedgrLYGrg 109

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5I4M_B      120 -------VLGGLEVIRSLNDHGIETEHPVEVVIWTNEE-GSRFAPAMVASGvfAGVFPLEYGLsrkdvdgktIGEelari 191
Cdd:COG0624 110 aadmkggLAAMLAALRALLAAGLRLPGNVTLLFTGDEEvGSPGARALVEEL--AEGLKADAAI---------VGE----- 173

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5I4M_B      192 GYAGDAPCGGRKlhaafelhieqgpileae*ktigvvtdaqGQRWYEITFTGQEAHAGptpMPRR-RDALLGASRVVDLV 270
Cdd:COG0624 174 PTGVPTIVTGHK-----------------------------GSLRFELTVRGKAAHSS---RPELgVNAIEALARALAAL 221

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5I4M_B      271 NRIGLD---HAPYGCAT--VGMMQVhPNSRNVIPGRVFFTVDFRHPDDAVLAKMDAALRDGVARIAADIGLDtaLEQIFY 345
Cdd:COG0624 222 RDLEFDgraDPLFGRTTlnVTGIEG-GTAVNVIPDEAEAKVDIRLLPGEDPEEVLAALRALLAAAAPGVEVE--VEVLGD 298

                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|..
5I4M_B      346 YAP---IAFDSACVAAVRAAADR-FGYSHRDIVSGAGHDACYLAQVAPTSMV 393
Cdd:COG0624 299 GRPpfeTPPDSPLVAAARAAIREvTGKEPVLSGVGGGTDARFFAEALGIPTV 350
amidohydrolases TIGR01891
amidohydrolase; This model represents a subfamily of amidohydrolases which are a subset of ...
 149-397 2.90e-07

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: 52.35  E-value: 2.90e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5I4M_B        149 EEGSRFAPAMVASGVFagvfpleyglsrKDVDgktigeelarigyagdapcggrklhAAFELHIEqgPILEAE*KTIGVV 228
Cdd:TIGR01891 124 EEGGGGATKMIEDGVL------------DDVD-------------------------AILGLHPD--PSIPAGTVGLRPG 164

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5I4M_B        229 TDAQGQRWYEITFTGQEAHAGPTPMPRrrDALLGASRVVDLVNRIGLDHAP---YGCATVGMMQVHpNSRNVIPGRVFFT 305
Cdd:TIGR01891 165 TIMAAADKFEVTIHGKGAHAARPHLGR--DALDAAAQLVVALQQIVSRNVDpsrPAVVSVGIIEAG-GAPNVIPDKASMS 241

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5I4M_B        306 VDFRHPDDAVLAKMDAALRDGVARIAADIGLDTALEQIFYYAPIAFDSACVAAVRAAADR----FGYSHRDIVSGAGHDA 381
Cdd:TIGR01891 242 GTVRSLDPEVRDQIIDRIERIVEGAAAMYGAKVELNYDRGLPAVTNDPALTQILKEVARHvvgpENVAEDPEVTMGSEDF 321

                         250
                  ....*....|....*.
5I4M_B        382 CYLAQVAPTSMVFVPC 397
Cdd:TIGR01891 322 AYYSQKVPGAFFFLGI 337
AbgB COG1473
Metal-dependent amidase/aminoacylase/carboxypeptidase [General function prediction only]; ...
 149-348 1.34e-05

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: 47.03  E-value: 1.34e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5I4M_B      149 EEGSRFAPAMVASGVFagvfpleyglSRKDVDgktigeelarigyagdapcggrklhAAFELHIEQGpileAE*KTIGVV 228
Cdd:COG1473 135 EEGGGGAKAMIEDGLL----------DRPDVD-------------------------AIFGLHVWPG----LPVGTIGVR 175

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5I4M_B      229 TDAQ--GQRWYEITFTGQEAHAGptpMPRR-RDALLGASRVVDLVNRIGLDHAP---YGCATVGMMQVHpNSRNVIPGRV 302
Cdd:COG1473 176 PGPImaAADSFEITIKGKGGHAA---APHLgIDPIVAAAQIVTALQTIVSRNVDpldPAVVTVGIIHGG-TAPNVIPDEA 251

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
5I4M_B      303 FFTVDFRHPDDAVLAKMDAALRDGVARIAADIGLDTALEQIFYYAP 348
Cdd:COG1473 252 ELEGTVRTFDPEVRELLEERIERIAEGIAAAYGATAEVEYLRGYPP 297
Zinc_peptidase_like cd03873
Zinc peptidases M18, M20, M28, and M42; Zinc peptidases play vital roles in metabolic and ...
 84-155 7.67e-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: 43.57  E-value: 7.67e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5I4M_B       84 NVFMRRAGRVaDAAPVVTGSHADSQPTG----------------------GRFDGIYGVLGGLEVIRSLNDHGIETEHPV 141
Cdd:cd03873   1 NLIARLGGGE-GGKSVALGAHLDVVPAGegdnrdppfaedteeegrlygrGALDDKGGVAAALEALKRLKENGFKPKGTI 79

                        90
                ....*....|....
5I4M_B      142 EVVIWTNEEGSRFA 155
Cdd:cd03873  80 VVAFTADEEVGSGG 93
M20_Acy1 cd03886
M20 Peptidase Aminoacylase 1 family; Peptidase M20 family, Aminoacylase 1 (ACY1; hippuricase; ...
 149-395 1.98e-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: 43.36  E-value: 1.98e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5I4M_B      149 EEGSRFAPAMVASGVfagvfpleygLSRKDVDgktigeelarigyagdapcggrklhAAFELHIeqGPILEAe*KTIGV- 227
Cdd:cd03886 123 EEGPGGAKAMIEEGV----------LENPGVD-------------------------AAFGLHV--WPGLPV--GTVGVr 163

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5I4M_B      228 --VTDAQGQRWyEITFTGQEAHAGpTPmPRRRDALL-GASRVVDLVNRIGLDHAPYGCATVGMMQVHP-NSRNVIPGRVF 303
Cdd:cd03886 164 sgALMASADEF-EITVKGKGGHGA-SP-HLGVDPIVaAAQIVLALQTVVSRELDPLEPAVVTVGKFHAgTAFNVIPDTAV 240

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5I4M_B      304 FTVDFRHPDDAVLAKMDAALRDGVARIAADIGLDTALEQIFYYAPIAFDSACVAAVRAAADR-FGYSH--RDIVSGAGHD 380
Cdd:cd03886 241 LEGTIRTFDPEVREALEARIKRLAEGIAAAYGATVELEYGYGYPAVINDPELTELVREAAKElLGEEAvvEPEPVMGSED 320

                       250
                ....*....|....*
5I4M_B      381 ACYLAQVAPTSMVFV 395
Cdd:cd03886 321 FAYYLEKVPGAFFWL 335
M20_PAAh_like cd03896
M20 Peptidases, Poly(aspartic acid) hydrolase-like proteins; Peptidase M20 family, Poly ...
 228-335 2.19e-04

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: 43.24  E-value: 2.19e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5I4M_B      228 VTDAQGQRWYEITFTGQEAH-AGPTPMPRRRDALlgaSRVVDLVNRIGLDHAP---YGCATVGmmqvHPNSRNVIPGRVF 303
Cdd:cd03896 157 HTGAVGSKRFRITTVGPGGHsYGAFGSPSAIVAM---AKLVEALYEWAAPYVPkttFAAIRGG----GGTSVNRIANLCS 229

                        90       100       110
                ....*....|....*....|....*....|..
5I4M_B      304 FTVDFRHPDDAVLAKMDAALRDGVARIAADIG 335
Cdd:cd03896 230 MYLDIRSNPDAELADVQREVEAVVSKLAAKHL 261
M20_dimer pfam07687
Peptidase dimerization domain; This domain consists of 4 beta strands and two alpha helices ...
 233-325 3.38e-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: 40.02  E-value: 3.38e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5I4M_B        233 GQRWYEITFTGQEAHAGPTPmpRRRDALLGASRVVDLVNRIGLDHAPYGCAT---VGMMQvHPNSRNVIPGRVFFTVDFR 309
Cdd:pfam07687   5 GLAGGHLTVKGKAGHSGAPG--KGVNAIKLLARLLAELPAEYGDIGFDFPRTtlnITGIE-GGTATNVIPAEAEAKFDIR 81

                          90       100
                  ....*....|....*....|
5I4M_B        310 HPD----DAVLAKMDAALRD 325
Cdd:pfam07687  82 LLPgedlEELLEEIEAILEK 101
M28_like cd05640
M28 Zn-peptidase; uncharacterized subfamily; Peptidase family M28 (also called aminopeptidase ...
 84-211 5.24e-04

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: 41.66  E-value: 5.24e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5I4M_B       84 NVFMRRAGRVADAAPVVTGSHADSQP-TGGRFDGIYGVLGGLEVIRSLndHGIETEHPVEVVIWTNEEGSRFAPAMVASG 162
Cdd:cd05640  54 NLIADLPGSYSQDKLILIGAHYDTVPgSPGADDNASGVAALLELARLL--ATLDPNHTLRFVAFDLEEYPFFARGLMGSH 131

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
5I4M_B      163 VFAGvfplEYGLSRKDVDGKTIgeeLARIGYAGDAPcGGRKLHAAFELH 211
Cdd:cd05640 132 AYAE----DLLRPLTPIVGMLS---LEMIGYYDPFP-HSQAYPAGFELH 172
M20_18_42 cd18669
M20, M18 and M42 Zn-peptidases include aminopeptidases and carboxypeptidases; This family ...
 84-178 6.14e-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: 40.88  E-value: 6.14e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5I4M_B       84 NVFMRRAGRVaDAAPVVTGSHADSQPTG----------------------GRFDGIYGVLGGLEVIRSLNDHGIETEHPV 141
Cdd:cd18669   1 NVIARYGGGG-GGKRVLLGAHIDVVPAGegdprdppffvdtveegrlygrGALDDKGGVAAALEALKLLKENGFKLKGTV 79

                        90       100       110
                ....*....|....*....|....*....|....*..
5I4M_B      142 EVVIWTNEEGSRFApamvasGVFAGVFPLEYGLSRKD 178
Cdd:cd18669  80 VVAFTPDEEVGSGA------GKGLLSKDALEEDLKVD 110
M20_pepD cd03890
M20 Peptidase D has specificity for beta-alanyl-L-histidine dipeptide; Peptidase M20 family, ...
 60-150 2.66e-03

M20 Peptidase D has specificity for beta-alanyl-L-histidine dipeptide; Peptidase M20 family, Peptidase D (PepD, Xaa-His dipeptidase; X-His dipeptidase; aminoacylhistidine dipeptidase; dipeptidase D; Beta-alanyl-histidine dipeptidase; pepD g.p. (Escherichia coli); EC 3.4.13.3) subfamily. PepD is a cytoplasmic enzyme family characterized by its unusual specificity for the dipeptides beta-alanyl-L-histidine (L-carnosine or beta-Ala-His) and gamma-aminobutyryl histidine (L-homocarnosine or gamma-amino-butyl-His). Homocarnosine has been suggested as a precursor for the neurotransmitter gamma-aminobutyric acid (GABA), acting as a GABA reservoir, and may mediate anti-seizure effects of GABAergic therapies. It has also been reported that glucose metabolism could be influenced by L-carnosine. PepD also includes a lid domain that forms a homodimer; however, the physiological function of this extra domain remains unclear.


Pssm-ID: 349885 [Multi-domain]  Cd Length: 474  Bit Score: 39.81  E-value: 2.66e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5I4M_B       60 KAARDLIVGWAKAAGCTVTVDTMGNVFMRRAGRVA--DAAPVVTGSHAD--------------SQP-------------- 109
Cdd:cd03890  22 KQISDFLVKFAKKLGLEVIQDEVGNVIIRKPATPGyeNAPPVILQGHMDmvceknadsehdfeKDPiklridgdwlkatg 101

                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
5I4M_B      110 -TGGRFDGIyGVLGGLEVirsLNDHGIetEH-PVEVVIWTNEE 150
Cdd:cd03890 102 tTLGADNGI-GVAYALAI---LEDKDI--EHpPLEVLFTVDEE 138
PRK07338 PRK07338
hydrolase;
237-353 5.36e-03

hydrolase;


Pssm-ID: 235995 [Multi-domain]  Cd Length: 402  Bit Score: 38.79  E-value: 5.36e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5I4M_B       237 YEITFTGQEAHAGPTPMpRRRDALLGASRVVDLVNriGLDHAPYGCaTVGMMQVH---PNsrNVIPGRVFFTVDFRHPDD 313
Cdd:PRK07338 206 FTIVVTGRAAHAGRAFD-EGRNAIVAAAELALALH--ALNGQRDGV-TVNVAKIDgggPL--NVVPDNAVLRFNIRPPTP 279

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
5I4M_B       314 AVLAKMDAALRDGVARIAADIGLDTALEQIFYYAPIAFDS 353
Cdd:PRK07338 280 EDAAWAEAELKKLIAQVNQRHGVSLHLHGGFGRPPKPIDA 319
 
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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