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Conserved domains on  [gi|518383840|ref|WP_019554047|]
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beta-aspartyl-peptidase [Propionispira raffinosivorans]

Protein Classification

amidohydrolase family protein( domain architecture ID 330)

metal-dependent amidohydrolase family protein having a conserved metal binding site, usually involving four histidines and one aspartic acid residue

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
metallo-dependent_hydrolases super family cl00281
Superfamily of metallo-dependent hydrolases (also called amidohydrolase superfamily) is a ...
 8-395 7.25e-176

Superfamily of metallo-dependent hydrolases (also called amidohydrolase superfamily) is a large group of proteins that show conservation in their 3-dimensional fold (TIM barrel) and in details of their active site. The vast majority of the members have a conserved metal binding site, involving four histidines and one aspartic acid residue. In the common reaction mechanism, the metal ion (or ions) deprotonate a water molecule for a nucleophilic attack on the substrate. The family includes urease alpha, adenosine deaminase, phosphotriesterase dihydroorotases, allantoinases, hydantoinases, AMP-, adenine and cytosine deaminases, imidazolonepropionase, aryldialkylphosphatase, chlorohydrolases, formylmethanofuran dehydrogenases and others.


The actual alignment was detected with superfamily member cd01308:

Pssm-ID: 469705 [Multi-domain]  Cd Length: 387  Bit Score: 494.99  E-value: 7.25e-176
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518383840   8 FTLLRNVKIVAPNDLGCQNILIAGDKVAAIGRNLTIPQGYCVEEIDLSGHTLMPGFIDSHVHMIGGGGEGGYATRTPEIV 87
Cdd:cd01308    1 FTLIKNAEVYAPEYLGKKDILIAGGKILAIEDQLNLPGYENVTVVDLHGKILVPGFIDQHVHIIGGGGEGGPSTRTPEVT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518383840  88 LSKVTTAGVTTLVGCLGTDGVTRHVESLLAKARGLEAEGLSTYIYTGAYEIPTPTITGSVRKDIIIIDKIIGAGELAMAD 167
Cdd:cd01308   81 LSDLTTAGVTTVVGCLGTDGISRSMEDLLAKARALEEEGITCFVYTGSYEVPTRTITGSIRKDLLLIDKVIGVGEIAISD 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518383840 168 HRSAQPTKDEYQKIAAEARVGGMLSAKAGIIDMHMGDGKDGMKLLFEITANGEIPKSQFLPTHVNRNKELFAQSIEWAKQ 247
Cdd:cd01308  161 HRSSQPTVEELARIAAEARVGGLLGGKAGIVHIHLGDGKRALSPIFELIEETEIPITQFLPTHINRTAPLFEQGVEFAKM 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518383840 248 GGMMDITSGVSPASGSVKAIKPSQAVKKALDAGVPLSQITMSSDGNGSMPIFDQQGNTIGVGVASQFSMLEEFRDMVQLE 327
Cdd:cd01308  241 GGTIDLTSSIDPQFRKEGEVRPSEALKRLLEQGVPLERITFSSDGNGSLPKFDENGNLVGLGVGSVDTLLREVREAVKCG 320

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 518383840 328 GIEISDAVQIITTNVAKILKIWPqKGSIQVGSDADFTIIDDEFVLQHVWAKGQHMVNAGKAVVLGTFE 395
Cdd:cd01308  321 DIPLEVALRVITSNVARILKLRK-KGEIQPGFDADLVILDKDLDINSVIAKGQIMVRNGKLLVKGTFE 387
 
Name Accession Description Interval E-value
Isoaspartyl-dipeptidase cd01308
Isoaspartyl dipeptidase hydrolyzes the beta-L-isoaspartyl linkages in dipeptides, as part of ...
 8-395 7.25e-176

Isoaspartyl dipeptidase hydrolyzes the beta-L-isoaspartyl linkages in dipeptides, as part of the degradative pathway to eliminate proteins with beta-L-isoaspartyl peptide bonds, bonds whereby the beta-group of an aspartate forms the peptide link with the amino group of the following amino acid. Formation of this bond is a spontaneous nonenzymatic reaction in nature and can profoundly effect the function of the protein. Isoaspartyl dipeptidase is an octameric enzyme that contains a binuclear zinc center in the active site of each subunit and shows a strong preference of hydrolyzing Asp-Leu dipeptides.


Pssm-ID: 238633 [Multi-domain]  Cd Length: 387  Bit Score: 494.99  E-value: 7.25e-176
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518383840   8 FTLLRNVKIVAPNDLGCQNILIAGDKVAAIGRNLTIPQGYCVEEIDLSGHTLMPGFIDSHVHMIGGGGEGGYATRTPEIV 87
Cdd:cd01308    1 FTLIKNAEVYAPEYLGKKDILIAGGKILAIEDQLNLPGYENVTVVDLHGKILVPGFIDQHVHIIGGGGEGGPSTRTPEVT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518383840  88 LSKVTTAGVTTLVGCLGTDGVTRHVESLLAKARGLEAEGLSTYIYTGAYEIPTPTITGSVRKDIIIIDKIIGAGELAMAD 167
Cdd:cd01308   81 LSDLTTAGVTTVVGCLGTDGISRSMEDLLAKARALEEEGITCFVYTGSYEVPTRTITGSIRKDLLLIDKVIGVGEIAISD 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518383840 168 HRSAQPTKDEYQKIAAEARVGGMLSAKAGIIDMHMGDGKDGMKLLFEITANGEIPKSQFLPTHVNRNKELFAQSIEWAKQ 247
Cdd:cd01308  161 HRSSQPTVEELARIAAEARVGGLLGGKAGIVHIHLGDGKRALSPIFELIEETEIPITQFLPTHINRTAPLFEQGVEFAKM 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518383840 248 GGMMDITSGVSPASGSVKAIKPSQAVKKALDAGVPLSQITMSSDGNGSMPIFDQQGNTIGVGVASQFSMLEEFRDMVQLE 327
Cdd:cd01308  241 GGTIDLTSSIDPQFRKEGEVRPSEALKRLLEQGVPLERITFSSDGNGSLPKFDENGNLVGLGVGSVDTLLREVREAVKCG 320

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 518383840 328 GIEISDAVQIITTNVAKILKIWPqKGSIQVGSDADFTIIDDEFVLQHVWAKGQHMVNAGKAVVLGTFE 395
Cdd:cd01308  321 DIPLEVALRVITSNVARILKLRK-KGEIQPGFDADLVILDKDLDINSVIAKGQIMVRNGKLLVKGTFE 387
isoAsp_dipep TIGR01975
isoaspartyl dipeptidase IadA; The L-isoaspartyl derivative of Asp arises non-enzymatically ...
 8-395 9.00e-154

isoaspartyl dipeptidase IadA; The L-isoaspartyl derivative of Asp arises non-enzymatically over time as a form of protein damage. In this isomerization, the connectivity of the polypeptide changes to pass through the beta-carboxyl of the side chain. Much but not all of this damage can be repaired by protein-L-isoaspartate (D-aspartate) O-methyltransferase. This model describes the isoaspartyl dipeptidase IadA, apparently one of two such enzymes in E. coli, an enzyme that degrades isoaspartyl dipeptides and may unblock degradation of proteins that cannot be repaired. This model also describes closely related proteins from other species (e.g. Clostridium perfringens, Thermoanaerobacter tengcongensis) that we assume to be equivalent in function. This family shows homology to dihydroorotases. [Protein fate, Degradation of proteins, peptides, and glycopeptides]


Pssm-ID: 131030  Cd Length: 389  Bit Score: 439.22  E-value: 9.00e-154
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518383840    8 FTLLRNVKIVAPNDLGCQNILIAGDKVAAIGRNLTIPQGYCVEEI--DLSGHTLMPGFIDSHVHMIGGGGEGGYATRTPE 85
Cdd:TIGR01975   1 FTLLKGAEVYAPEYIGKKDILIANDKIIAIADEIPSTKDFVPNCVvvGLEGMIAVPGFIDQHVHIIGGGGEGGPTTRTPE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518383840   86 IVLSKVTTAGVTTLVGCLGTDGVTRHVESLLAKARGLEAEGLSTYIYTGAYEIPTPTITGSVRKDIIIIDKIIGAGELAM 165
Cdd:TIGR01975  81 LTLSDITKGGVTTVVGLLGTDGITRHMESLLAKARALEEEGISCYMLTGAYHVPSRTITGSVESDLLLIDKVIGVGEIAI 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518383840  166 ADHRSAQPTKDEYQKIAAEARVGGMLSAKAGIIDMHMGDGKDGMKLLFEITANGEIPKSQFLPTHVNRNKELFAQSIEWA 245
Cdd:TIGR01975 161 SDHRSAQPTVEHLTNMAAEARVGGLLGGKPGIVNFHVGDSKRALQPIYELVENTDVPITQFLPTHINRNVPLFEAGLEFA 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518383840  246 KQGGMMDITSGVSPASGSVKAIKPSQAVKKALDAGVPLSQITMSSDGNGSMPIFDQQGNTIGVGVASQFSMLEEFRDMVQ 325
Cdd:TIGR01975 241 KKGGTIDLTSSIDPQFRKEGEVAPAEGIKKALEAGVPLEKVTFSSDGNGSQPFFDENGELTGLGVGSFETLFEEVREAVK 320

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518383840  326 LEGIEISDAVQIITTNVAKILKIWpQKGSIQVGSDADFTIIDDEFVLQHVWAKGQHMVNAGKAVVLGTFE 395
Cdd:TIGR01975 321 DGDVPLEKALRVITSNVAGVLNLT-GKGEISPGNDADLVVLDPDLRIHSVIARGKLMVKDGKACVKGTFE 389
HutI COG1228
Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport ...
 9-367 3.07e-22

Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 440841 [Multi-domain]  Cd Length: 386  Bit Score: 96.95  E-value: 3.07e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518383840   9 TLLRNVKIVAPND---LGCQNILIAGDKVAAIGRNLTIPQGYCVEEIDLSGHTLMPGFIDSHVHMIGGGGEGGYATRTPE 85
Cdd:COG1228   10 LLITNATLVDGTGggvIENGTVLVEDGKIAAVGPAADLAVPAGAEVIDATGKTVLPGLIDAHTHLGLGGGRAVEFEAGGG 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518383840  86 IVLSKVTT------------AGVTTLVGCLGTD-GVTRHV---ESLLAKARGLEAEGLSTYIYTGAYEIPTPTITGSVRK 149
Cdd:COG1228   90 ITPTVDLVnpadkrlrralaAGVTTVRDLPGGPlGLRDAIiagESKLLPGPRVLAAGPALSLTGGAHARGPEEARAALRE 169

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518383840 150 DiiiidkiigAGELA-----MADHRSAQPTKDEYQKIAAEARVGGMLSAkagiidMHmGDGKDGMKLLFE---ITAngei 221
Cdd:COG1228  170 L---------LAEGAdyikvFAEGGAPDFSLEELRAILEAAHALGLPVA------AH-AHQADDIRLAVEagvDSI---- 229

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518383840 222 pksqflpTHVNRNKELFAQsiEWAKQGGM----------MDITSGVSPASGSVKAIKPSQA--VKKALDAGVPlsqITMS 289
Cdd:COG1228  230 -------EHGTYLDDEVAD--LLAEAGTVvlvptlslflALLEGAAAPVAAKARKVREAALanARRLHDAGVP---VALG 297

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 518383840 290 SDGNGSMPIfdqqgntigvgvasQFSMLEEFRDMVQLeGIEISDAVQIITTNVAKILKIWPQKGSIQVGSDADFTIID 367
Cdd:COG1228  298 TDAGVGVPP--------------GRSLHRELALAVEA-GLTPEEALRAATINAAKALGLDDDVGSLEPGKLADLVLLD 360
Amidohydro_1 pfam01979
Amidohydrolase family; This family of enzymes are a a large metal dependent hydrolase ...
 58-380 5.03e-15

Amidohydrolase family; This family of enzymes are a a large metal dependent hydrolase superfamily. The family includes Adenine deaminase EC:3.5.4.2 that hydrolyses adenine to form hypoxanthine and ammonia. Adenine deaminases reaction is important for adenine utilization as a purine and also as a nitrogen source. This family also includes dihydroorotase and N-acetylglucosamine-6-phosphate deacetylases, EC:3.5.1.25 These enzymes catalyze the reaction N-acetyl-D-glucosamine 6-phosphate + H2O <=> D-glucosamine 6-phosphate + acetate. This family includes the catalytic domain of urease alpha subunit. Dihydroorotases (EC:3.5.2.3) are also included.


Pssm-ID: 460401 [Multi-domain]  Cd Length: 334  Bit Score: 75.62  E-value: 5.03e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518383840   58 TLMPGFIDSHVH-----MIGGGGEGGYATRTPEIVLSKVTTAGVTTLVGCLGTD--GVTRHVESLLAKARGLEAEGLSTY 130
Cdd:pfam01979   1 IVLPGLIDAHVHlemglLRGIPVPPEFAYEALRLGITTMLKSGTTTVLDMGATTstGIEALLEAAEELPLGLRFLGPGCS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518383840  131 IYT-GAYEIPTPTITGSVRKDIIIIDKIIGAGELAMADHRSAQPTKDEYQKIAAEARVGGMLsakagiIDMHMGDGKDGM 209
Cdd:pfam01979  81 LDTdGELEGRKALREKLKAGAEFIKGMADGVVFVGLAPHGAPTFSDDELKAALEEAKKYGLP------VAIHALETKGEV 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518383840  210 KLLFEITANGEIpksqfLPTHVNRNKELFA----------------QSIEWAKQGGMMDitSGVSPASGSVKAIKPSQAV 273
Cdd:pfam01979 155 EDAIAAFGGGIE-----HGTHLEVAESGGLldiiklilahgvhlspTEANLLAEHLKGA--GVAHCPFSNSKLRSGRIAL 227

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518383840  274 KKALDAGVPlsqITMSSDGNGSMpifdqqgntigvgvaSQFSMLEEFRDMVQLE-----GIEISDAVQIITTNVAKILKI 348
Cdd:pfam01979 228 RKALEDGVK---VGLGTDGAGSG---------------NSLNMLEELRLALELQfdpegGLSPLEALRMATINPAKALGL 289

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|...
gi 518383840  349 WPQKGSIQVGSDADFTIID-----------DEFVLQHVWAKGQ 380
Cdd:pfam01979 290 DDKVGSIEVGKDADLVVVDldplaaffglkPDGNVKKVIVKGK 332
PRK09237 PRK09237
amidohydrolase/deacetylase family metallohydrolase;
10-369 3.20e-11

amidohydrolase/deacetylase family metallohydrolase;


Pssm-ID: 236423 [Multi-domain]  Cd Length: 380  Bit Score: 64.10  E-value: 3.20e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518383840  10 LLRNVKIVAP-NDLGCQ-NILIAGDKVAAIGRNLTIPQGycVEEIDLSGHTLMPGFIDSHVHmiggggegGYATRTPE-I 86
Cdd:PRK09237   2 LLRGGRVIDPaNGIDGViDIAIEDGKIAAVAGDIDGSQA--KKVIDLSGLYVSPGWIDLHVH--------VYPGSTPYgD 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518383840  87 VLSKVTTA-GVTTLV--GCLGTDGV------------TRhVESLLAKARgleaeglsTYIYTGAYEiptptitgsvrkdi 151
Cdd:PRK09237  72 EPDEVGVRsGVTTVVdaGSAGADNFddfrkltieaskTR-VLAFLNISR--------IGLLAQDEL-------------- 128

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518383840 152 iiidkiigaGELAMADHRSAQPTKDEYQKIAaearVGgmLSAKAGIIDMHmGDGKDGMKLLFEITANGEIPksqfLPTHV 231
Cdd:PRK09237 129 ---------ADLEDIDADAVAEAVKRNPDFI----VG--IKARMSSSVVG-DNGIEPLELAKAIAAEANLP----LMVHI 188

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518383840 232 NRNKELFAQSIEWAKQGgmmDI--------TSGVSPASGSVKAikpsqAVKKALDAGVPLsqitmssD---GNGS----- 295
Cdd:PRK09237 189 GNPPPSLEEILELLRPG---DIlthcfngkPNRILDEDGELRP-----SVLEALERGVRL-------DvghGTASfsfkv 253

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518383840 296 -MPIFDQ------------QGNTIGVGVASQFSMLEEFRDMvqleGIEISDAVQIITTNVAKILKIwPQKGSIQVGSDAD 362
Cdd:PRK09237 254 aEAAIAAgilpdtistdiyCRNRINGPVYSLATVMSKFLAL----GMPLEEVIAAVTKNAADALRL-PELGRLQVGSDAD 328


                 ....*..
gi 518383840 363 FTIIDDE 369
Cdd:PRK09237 329 LTLFTLK 335
 
Name Accession Description Interval E-value
Isoaspartyl-dipeptidase cd01308
Isoaspartyl dipeptidase hydrolyzes the beta-L-isoaspartyl linkages in dipeptides, as part of ...
 8-395 7.25e-176

Isoaspartyl dipeptidase hydrolyzes the beta-L-isoaspartyl linkages in dipeptides, as part of the degradative pathway to eliminate proteins with beta-L-isoaspartyl peptide bonds, bonds whereby the beta-group of an aspartate forms the peptide link with the amino group of the following amino acid. Formation of this bond is a spontaneous nonenzymatic reaction in nature and can profoundly effect the function of the protein. Isoaspartyl dipeptidase is an octameric enzyme that contains a binuclear zinc center in the active site of each subunit and shows a strong preference of hydrolyzing Asp-Leu dipeptides.


Pssm-ID: 238633 [Multi-domain]  Cd Length: 387  Bit Score: 494.99  E-value: 7.25e-176
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518383840   8 FTLLRNVKIVAPNDLGCQNILIAGDKVAAIGRNLTIPQGYCVEEIDLSGHTLMPGFIDSHVHMIGGGGEGGYATRTPEIV 87
Cdd:cd01308    1 FTLIKNAEVYAPEYLGKKDILIAGGKILAIEDQLNLPGYENVTVVDLHGKILVPGFIDQHVHIIGGGGEGGPSTRTPEVT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518383840  88 LSKVTTAGVTTLVGCLGTDGVTRHVESLLAKARGLEAEGLSTYIYTGAYEIPTPTITGSVRKDIIIIDKIIGAGELAMAD 167
Cdd:cd01308   81 LSDLTTAGVTTVVGCLGTDGISRSMEDLLAKARALEEEGITCFVYTGSYEVPTRTITGSIRKDLLLIDKVIGVGEIAISD 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518383840 168 HRSAQPTKDEYQKIAAEARVGGMLSAKAGIIDMHMGDGKDGMKLLFEITANGEIPKSQFLPTHVNRNKELFAQSIEWAKQ 247
Cdd:cd01308  161 HRSSQPTVEELARIAAEARVGGLLGGKAGIVHIHLGDGKRALSPIFELIEETEIPITQFLPTHINRTAPLFEQGVEFAKM 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518383840 248 GGMMDITSGVSPASGSVKAIKPSQAVKKALDAGVPLSQITMSSDGNGSMPIFDQQGNTIGVGVASQFSMLEEFRDMVQLE 327
Cdd:cd01308  241 GGTIDLTSSIDPQFRKEGEVRPSEALKRLLEQGVPLERITFSSDGNGSLPKFDENGNLVGLGVGSVDTLLREVREAVKCG 320

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 518383840 328 GIEISDAVQIITTNVAKILKIWPqKGSIQVGSDADFTIIDDEFVLQHVWAKGQHMVNAGKAVVLGTFE 395
Cdd:cd01308  321 DIPLEVALRVITSNVARILKLRK-KGEIQPGFDADLVILDKDLDINSVIAKGQIMVRNGKLLVKGTFE 387
isoAsp_dipep TIGR01975
isoaspartyl dipeptidase IadA; The L-isoaspartyl derivative of Asp arises non-enzymatically ...
 8-395 9.00e-154

isoaspartyl dipeptidase IadA; The L-isoaspartyl derivative of Asp arises non-enzymatically over time as a form of protein damage. In this isomerization, the connectivity of the polypeptide changes to pass through the beta-carboxyl of the side chain. Much but not all of this damage can be repaired by protein-L-isoaspartate (D-aspartate) O-methyltransferase. This model describes the isoaspartyl dipeptidase IadA, apparently one of two such enzymes in E. coli, an enzyme that degrades isoaspartyl dipeptides and may unblock degradation of proteins that cannot be repaired. This model also describes closely related proteins from other species (e.g. Clostridium perfringens, Thermoanaerobacter tengcongensis) that we assume to be equivalent in function. This family shows homology to dihydroorotases. [Protein fate, Degradation of proteins, peptides, and glycopeptides]


Pssm-ID: 131030  Cd Length: 389  Bit Score: 439.22  E-value: 9.00e-154
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518383840    8 FTLLRNVKIVAPNDLGCQNILIAGDKVAAIGRNLTIPQGYCVEEI--DLSGHTLMPGFIDSHVHMIGGGGEGGYATRTPE 85
Cdd:TIGR01975   1 FTLLKGAEVYAPEYIGKKDILIANDKIIAIADEIPSTKDFVPNCVvvGLEGMIAVPGFIDQHVHIIGGGGEGGPTTRTPE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518383840   86 IVLSKVTTAGVTTLVGCLGTDGVTRHVESLLAKARGLEAEGLSTYIYTGAYEIPTPTITGSVRKDIIIIDKIIGAGELAM 165
Cdd:TIGR01975  81 LTLSDITKGGVTTVVGLLGTDGITRHMESLLAKARALEEEGISCYMLTGAYHVPSRTITGSVESDLLLIDKVIGVGEIAI 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518383840  166 ADHRSAQPTKDEYQKIAAEARVGGMLSAKAGIIDMHMGDGKDGMKLLFEITANGEIPKSQFLPTHVNRNKELFAQSIEWA 245
Cdd:TIGR01975 161 SDHRSAQPTVEHLTNMAAEARVGGLLGGKPGIVNFHVGDSKRALQPIYELVENTDVPITQFLPTHINRNVPLFEAGLEFA 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518383840  246 KQGGMMDITSGVSPASGSVKAIKPSQAVKKALDAGVPLSQITMSSDGNGSMPIFDQQGNTIGVGVASQFSMLEEFRDMVQ 325
Cdd:TIGR01975 241 KKGGTIDLTSSIDPQFRKEGEVAPAEGIKKALEAGVPLEKVTFSSDGNGSQPFFDENGELTGLGVGSFETLFEEVREAVK 320

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518383840  326 LEGIEISDAVQIITTNVAKILKIWpQKGSIQVGSDADFTIIDDEFVLQHVWAKGQHMVNAGKAVVLGTFE 395
Cdd:TIGR01975 321 DGDVPLEKALRVITSNVAGVLNLT-GKGEISPGNDADLVVLDPDLRIHSVIARGKLMVKDGKACVKGTFE 389
HutI COG1228
Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport ...
 9-367 3.07e-22

Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 440841 [Multi-domain]  Cd Length: 386  Bit Score: 96.95  E-value: 3.07e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518383840   9 TLLRNVKIVAPND---LGCQNILIAGDKVAAIGRNLTIPQGYCVEEIDLSGHTLMPGFIDSHVHMIGGGGEGGYATRTPE 85
Cdd:COG1228   10 LLITNATLVDGTGggvIENGTVLVEDGKIAAVGPAADLAVPAGAEVIDATGKTVLPGLIDAHTHLGLGGGRAVEFEAGGG 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518383840  86 IVLSKVTT------------AGVTTLVGCLGTD-GVTRHV---ESLLAKARGLEAEGLSTYIYTGAYEIPTPTITGSVRK 149
Cdd:COG1228   90 ITPTVDLVnpadkrlrralaAGVTTVRDLPGGPlGLRDAIiagESKLLPGPRVLAAGPALSLTGGAHARGPEEARAALRE 169

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518383840 150 DiiiidkiigAGELA-----MADHRSAQPTKDEYQKIAAEARVGGMLSAkagiidMHmGDGKDGMKLLFE---ITAngei 221
Cdd:COG1228  170 L---------LAEGAdyikvFAEGGAPDFSLEELRAILEAAHALGLPVA------AH-AHQADDIRLAVEagvDSI---- 229

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518383840 222 pksqflpTHVNRNKELFAQsiEWAKQGGM----------MDITSGVSPASGSVKAIKPSQA--VKKALDAGVPlsqITMS 289
Cdd:COG1228  230 -------EHGTYLDDEVAD--LLAEAGTVvlvptlslflALLEGAAAPVAAKARKVREAALanARRLHDAGVP---VALG 297

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 518383840 290 SDGNGSMPIfdqqgntigvgvasQFSMLEEFRDMVQLeGIEISDAVQIITTNVAKILKIWPQKGSIQVGSDADFTIID 367
Cdd:COG1228  298 TDAGVGVPP--------------GRSLHRELALAVEA-GLTPEEALRAATINAAKALGLDDDVGSLEPGKLADLVLLD 360
Amidohydro_1 pfam01979
Amidohydrolase family; This family of enzymes are a a large metal dependent hydrolase ...
 58-380 5.03e-15

Amidohydrolase family; This family of enzymes are a a large metal dependent hydrolase superfamily. The family includes Adenine deaminase EC:3.5.4.2 that hydrolyses adenine to form hypoxanthine and ammonia. Adenine deaminases reaction is important for adenine utilization as a purine and also as a nitrogen source. This family also includes dihydroorotase and N-acetylglucosamine-6-phosphate deacetylases, EC:3.5.1.25 These enzymes catalyze the reaction N-acetyl-D-glucosamine 6-phosphate + H2O <=> D-glucosamine 6-phosphate + acetate. This family includes the catalytic domain of urease alpha subunit. Dihydroorotases (EC:3.5.2.3) are also included.


Pssm-ID: 460401 [Multi-domain]  Cd Length: 334  Bit Score: 75.62  E-value: 5.03e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518383840   58 TLMPGFIDSHVH-----MIGGGGEGGYATRTPEIVLSKVTTAGVTTLVGCLGTD--GVTRHVESLLAKARGLEAEGLSTY 130
Cdd:pfam01979   1 IVLPGLIDAHVHlemglLRGIPVPPEFAYEALRLGITTMLKSGTTTVLDMGATTstGIEALLEAAEELPLGLRFLGPGCS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518383840  131 IYT-GAYEIPTPTITGSVRKDIIIIDKIIGAGELAMADHRSAQPTKDEYQKIAAEARVGGMLsakagiIDMHMGDGKDGM 209
Cdd:pfam01979  81 LDTdGELEGRKALREKLKAGAEFIKGMADGVVFVGLAPHGAPTFSDDELKAALEEAKKYGLP------VAIHALETKGEV 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518383840  210 KLLFEITANGEIpksqfLPTHVNRNKELFA----------------QSIEWAKQGGMMDitSGVSPASGSVKAIKPSQAV 273
Cdd:pfam01979 155 EDAIAAFGGGIE-----HGTHLEVAESGGLldiiklilahgvhlspTEANLLAEHLKGA--GVAHCPFSNSKLRSGRIAL 227

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518383840  274 KKALDAGVPlsqITMSSDGNGSMpifdqqgntigvgvaSQFSMLEEFRDMVQLE-----GIEISDAVQIITTNVAKILKI 348
Cdd:pfam01979 228 RKALEDGVK---VGLGTDGAGSG---------------NSLNMLEELRLALELQfdpegGLSPLEALRMATINPAKALGL 289

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|...
gi 518383840  349 WPQKGSIQVGSDADFTIID-----------DEFVLQHVWAKGQ 380
Cdd:pfam01979 290 DDKVGSIEVGKDADLVVVDldplaaffglkPDGNVKKVIVKGK 332
D-hydantoinase TIGR02033
D-hydantoinase; This model represents the D-hydantoinase (dihydropyrimidinase) which primarily ...
 10-383 5.65e-15

D-hydantoinase; This model represents the D-hydantoinase (dihydropyrimidinase) which primarily converts 5,6-dihydrouracil to 3-ureidopropanoate but also acts on dihydrothymine and hydantoin. The enzyme is a metalloenzyme.


Pssm-ID: 273937 [Multi-domain]  Cd Length: 454  Bit Score: 76.27  E-value: 5.65e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518383840   10 LLRNVKIVAPNDLGCQNILIAGDKVAAIGRNLTIPQGycVEEIDLSGHTLMPGFIDSHVHMigggGEGGYATRTPEIVLS 89
Cdd:TIGR02033   2 LIKGGTVVNADDVFQADVLIEGGKIVAVGDNLIPPDA--VEVIDATGKYVLPGGIDVHTHL----EMPFGGTTTADDFFT 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518383840   90 --KVTTAGVTTLVGCLGTDGVTRHVESLLAKARGLeAEGLSTYIYtgAYEIPTPTITGSVRKDIIIIDKIIGAGELA--M 165
Cdd:TIGR02033  76 gtKAAAAGGTTTIIDFVVPEKGSSLTEALETWHEK-AEGKSVIDY--GFHMDITHWNDSVLEEHIPEVKEEGINSFKvfM 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518383840  166 ADHRSAQPTKDEYQKIAAEAR-VGGMLSAKA---GIIDMHMGD----GKDGMK-------LLFEITANG------EIPKS 224
Cdd:TIGR02033 153 AYKNLLMVDDEELFEILKRLKeLGALLQVHAengDIIAELQARmlaqGITGPEyhalsrpPELEAEAVAraitlaALADA 232

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518383840  225 QFLPTHVN--RNKELFAQS--------IEWAKQGGMMDITSGVSPASGSVKAI-KP---SQAVKKALDAGVPLSQI-TMS 289
Cdd:TIGR02033 233 PLYVVHVStkDAADEIAQArkkgqpvfGETCPQYLVLDDTHYDKPGFEGAKYVcSPplrEPEDQDALWSALSSGALqTVG 312

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518383840  290 SD---------GNGSMPIFDQQGNTiGVGVASQFSMLeeFRDMVQLEGIEISDAVQIITTNVAKILKIWPQKGSIQVGSD 360
Cdd:TIGR02033 313 SDhctfnfaqkKAIGKDDFTKIPNG-GPGVEERMSLL--FDEGVAKGRITLEKFVEVTSTNPAKIFNLYPRKGTIAVGSD 389

                         410       420
                  ....*....|....*....|...
gi 518383840  361 ADFTIIDDEfVLQHVWAKGQHMV 383
Cdd:TIGR02033 390 ADIVIWDPN-RTTVISAETHHSN 411
AllB COG0044
Dihydroorotase or related cyclic amidohydrolase [Nucleotide transport and metabolism]; ...
 10-70 1.12e-14

Dihydroorotase or related cyclic amidohydrolase [Nucleotide transport and metabolism]; Dihydroorotase or related cyclic amidohydrolase is part of the Pathway/BioSystem: Pyrimidine biosynthesis


Pssm-ID: 439814 [Multi-domain]  Cd Length: 439  Bit Score: 75.13  E-value: 1.12e-14
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 518383840  10 LLRNVKIVAPNDLGCQNILIAGDKVAAIGRNLTIPQGycVEEIDLSGHTLMPGFIDSHVHM 70
Cdd:COG0044    1 LIKNGRVVDPGGLERADVLIEDGRIAAIGPDLAAPEA--AEVIDATGLLVLPGLIDLHVHL 59
NagA COG1820
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism];
315-380 2.99e-13

N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism];


Pssm-ID: 441425 [Multi-domain]  Cd Length: 373  Bit Score: 70.51  E-value: 2.99e-13
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 518383840 315 SMLEEFRDMVQLEGIEISDAVQIITTNVAKILKIWPQKGSIQVGSDADFTIIDDEFVLQHVWAKGQ 380
Cdd:COG1820  308 TMDDAVRNLVEWTGLPLEEAVRMASLNPARALGLDDRKGSIAPGKDADLVVLDDDLNVRATWVGGE 373
NagA cd00854
N-acetylglucosamine-6-phosphate deacetylase, NagA, catalyzes the hydrolysis of the N-acetyl ...
 9-379 1.91e-12

N-acetylglucosamine-6-phosphate deacetylase, NagA, catalyzes the hydrolysis of the N-acetyl group of N-acetyl-glucosamine-6-phosphate (GlcNAc-6-P) to glucosamine 6-phosphate and acetate. This is the first committed step in the biosynthetic pathway to amino-sugar-nucleotides, which is needed for cell wall peptidoglycan and teichoic acid biosynthesis. Deacetylation of N-acetylglucosamine is also important in lipopolysaccharide synthesis and cell wall recycling.


Pssm-ID: 238434 [Multi-domain]  Cd Length: 374  Bit Score: 67.99  E-value: 1.91e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518383840   9 TLLRNVKIVAPNDLGCQNILIAGDKVAAIGRNLTIPQGYCVeeIDLSGHTLMPGFIDSHVHmiggggeggyatrtpeivl 88
Cdd:cd00854    1 LIIKNARILTPGGLEDGAVLVEDGKIVAIGPEDELEEADEI--IDLKGQYLVPGFIDIHIH------------------- 59

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518383840  89 skvttagvttlvGCLGTDGVTRHVESLLAKARGLEAEGLSTYIytgayeiPTpTITGS-------VRKDIIIIDKIIGAG 161
Cdd:cd00854   60 ------------GGGGADFMDGTAEALKTIAEALAKHGTTSFL-------PT-TVTAPpeeiakaLAAIAEAIAEGQGAE 119

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518383840 162 ELAM--------ADHRSAQ-------PTKDEYQKiaaearvggMLSAKAGIIDMhmgdgkdgmkllfeITANGEIPKS-Q 225
Cdd:cd00854  120 ILGIhlegpfisPEKKGAHppeylraPDPEELKK---------WLEAAGGLIKL--------------VTLAPELDGAlE 176

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518383840 226 FLPTHVNRNKEL--------FAQSIEWAKQG---------GMMDITS---GVSPASGSVKAIK----------PSQAVKK 275
Cdd:cd00854  177 LIRYLVERGIIVsighsdatYEQAVAAFEAGathvthlfnAMSPLHHrepGVVGAALSDDDVYaeliadgihvHPAAVRL 256

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518383840 276 ALDAgVPLSQITMSSDgngSMP---------IFDQQGNTIGVGVA---------SQFSMLEEFRDMVQLEGIEISDAVQI 337
Cdd:cd00854  257 AYRA-KGADKIVLVTD---AMAaaglpdgeyELGGQTVTVKDGVArladgtlagSTLTMDQAVRNMVKWGGCPLEEAVRM 332

                        410       420       430       440
                 ....*....|....*....|....*....|....*....|..
gi 518383840 338 ITTNVAKILKIWPQKGSIQVGSDADFTIIDDEFVLQHVWAKG 379
Cdd:cd00854  333 ASLNPAKLLGLDDRKGSLKPGKDADLVVLDDDLNVKATWING 374
metallo-dependent_hydrolases cd01292
Superfamily of metallo-dependent hydrolases (also called amidohydrolase superfamily) is a ...
 63-345 1.88e-11

Superfamily of metallo-dependent hydrolases (also called amidohydrolase superfamily) is a large group of proteins that show conservation in their 3-dimensional fold (TIM barrel) and in details of their active site. The vast majority of the members have a conserved metal binding site, involving four histidines and one aspartic acid residue. In the common reaction mechanism, the metal ion (or ions) deprotonate a water molecule for a nucleophilic attack on the substrate. The family includes urease alpha, adenosine deaminase, phosphotriesterase dihydroorotases, allantoinases, hydantoinases, AMP-, adenine and cytosine deaminases, imidazolonepropionase, aryldialkylphosphatase, chlorohydrolases, formylmethanofuran dehydrogenases and others.


Pssm-ID: 238617 [Multi-domain]  Cd Length: 275  Bit Score: 64.28  E-value: 1.88e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518383840  63 FIDSHVH---------------MIGGGGEGGYATRTPEIVLSKVTTAGVTTLVGCLGTDGVTRHVESLLAKARGL-EAEG 126
Cdd:cd01292    1 FIDTHVHldgsalrgtrlnlelKEAEELSPEDLYEDTLRALEALLAGGVTTVVDMGSTPPPTTTKAAIEAVAEAArASAG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518383840 127 LSTYIYTGAYEIPTP--TITGSVRKDIIIIDKIIGAGELAMADHRSAQPTKDEY-QKIAAEARVGGMlsakagIIDMHMG 203
Cdd:cd01292   81 IRVVLGLGIPGVPAAvdEDAEALLLELLRRGLELGAVGLKLAGPYTATGLSDESlRRVLEEARKLGL------PVVIHAG 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518383840 204 DGKDGMKLLFEITANGEIPKSqFLPTHVNRnkeLFAQSIEWAKQGGM-MDITSGVSPASGSVKAikPSQAVKKALDAGVp 282
Cdd:cd01292  155 ELPDPTRALEDLVALLRLGGR-VVIGHVSH---LDPELLELLKEAGVsLEVCPLSNYLLGRDGE--GAEALRRLLELGI- 227

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 518383840 283 lsQITMSSDGNGSmpifdqqgntigvgvASQFSMLEEFRDMVQLEGIEIS--DAVQIITTNVAKI 345
Cdd:cd01292  228 --RVTLGTDGPPH---------------PLGTDLLALLRLLLKVLRLGLSleEALRLATINPARA 275
ATZ_TRZ_like cd01298
TRZ/ATZ family contains enzymes from the atrazine degradation pathway and related hydrolases. ...
 9-70 3.17e-11

TRZ/ATZ family contains enzymes from the atrazine degradation pathway and related hydrolases. Atrazine, a chlorinated herbizide, can be catabolized by a variety of different bacteria. The first three steps of the atrazine dehalogenation pathway are catalyzed by atrazine chlorohydrolase (AtzA), hydroxyatrazine ethylaminohydrolase (AtzB), and N-isopropylammelide N-isopropylaminohydrolase (AtzC). All three enzymes belong to the superfamily of metal dependent hydrolases. AtzA and AtzB, beside other related enzymes are represented in this CD.


Pssm-ID: 238623 [Multi-domain]  Cd Length: 411  Bit Score: 64.53  E-value: 3.17e-11
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 518383840   9 TLLRNVKIVAPND---LGCQNILIAGDKVAAIGRNLTIPQGYCVEEIDLSGHTLMPGFIDSHVHM 70
Cdd:cd01298    1 ILIRNGTIVTTDPrrvLEDGDVLVEDGRIVAVGPALPLPAYPADEVIDAKGKVVMPGLVNTHTHL 65
PRK09237 PRK09237
amidohydrolase/deacetylase family metallohydrolase;
10-369 3.20e-11

amidohydrolase/deacetylase family metallohydrolase;


Pssm-ID: 236423 [Multi-domain]  Cd Length: 380  Bit Score: 64.10  E-value: 3.20e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518383840  10 LLRNVKIVAP-NDLGCQ-NILIAGDKVAAIGRNLTIPQGycVEEIDLSGHTLMPGFIDSHVHmiggggegGYATRTPE-I 86
Cdd:PRK09237   2 LLRGGRVIDPaNGIDGViDIAIEDGKIAAVAGDIDGSQA--KKVIDLSGLYVSPGWIDLHVH--------VYPGSTPYgD 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518383840  87 VLSKVTTA-GVTTLV--GCLGTDGV------------TRhVESLLAKARgleaeglsTYIYTGAYEiptptitgsvrkdi 151
Cdd:PRK09237  72 EPDEVGVRsGVTTVVdaGSAGADNFddfrkltieaskTR-VLAFLNISR--------IGLLAQDEL-------------- 128

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518383840 152 iiidkiigaGELAMADHRSAQPTKDEYQKIAaearVGgmLSAKAGIIDMHmGDGKDGMKLLFEITANGEIPksqfLPTHV 231
Cdd:PRK09237 129 ---------ADLEDIDADAVAEAVKRNPDFI----VG--IKARMSSSVVG-DNGIEPLELAKAIAAEANLP----LMVHI 188

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518383840 232 NRNKELFAQSIEWAKQGgmmDI--------TSGVSPASGSVKAikpsqAVKKALDAGVPLsqitmssD---GNGS----- 295
Cdd:PRK09237 189 GNPPPSLEEILELLRPG---DIlthcfngkPNRILDEDGELRP-----SVLEALERGVRL-------DvghGTASfsfkv 253

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518383840 296 -MPIFDQ------------QGNTIGVGVASQFSMLEEFRDMvqleGIEISDAVQIITTNVAKILKIwPQKGSIQVGSDAD 362
Cdd:PRK09237 254 aEAAIAAgilpdtistdiyCRNRINGPVYSLATVMSKFLAL----GMPLEEVIAAVTKNAADALRL-PELGRLQVGSDAD 328


                 ....*..
gi 518383840 363 FTIIDDE 369
Cdd:PRK09237 329 LTLFTLK 335
D-HYD cd01314
D-hydantoinases (D-HYD) also called dihydropyrimidases (DHPase) and related proteins; DHPases ...
 9-70 6.52e-11

D-hydantoinases (D-HYD) also called dihydropyrimidases (DHPase) and related proteins; DHPases are a family of enzymes that catalyze the reversible hydrolytic ring opening of the amide bond in five- or six-membered cyclic diamides, like dihydropyrimidine or hydantoin. The hydrolysis of dihydropyrimidines is the second step of reductive catabolism of pyrimidines in human. The hydrolysis of 5-substituted hydantoins in microorganisms leads to enantiomerically pure N-carbamyl amino acids, which are used for the production of antibiotics, peptide hormones, pyrethroids, and pesticides. HYDs are classified depending on their stereoselectivity. This family also includes collapsin response regulators (CRMPs), cytosolic proteins involved in neuronal differentiation and axonal guidance which have strong homology to DHPases, but lack most of the active site residues.


Pssm-ID: 238639 [Multi-domain]  Cd Length: 447  Bit Score: 63.39  E-value: 6.52e-11
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 518383840   9 TLLRNVKIVAPNDLGCQNILIAGDKVAAIGRNLTIPQGycVEEIDLSGHTLMPGFIDSHVHM 70
Cdd:cd01314    1 LIIKNGTIVTADGSFKADILIEDGKIVAIGPNLEAPGG--VEVIDATGKYVLPGGIDPHTHL 60
YtcJ COG1574
Predicted amidohydrolase YtcJ [General function prediction only];
9-71 4.77e-10

Predicted amidohydrolase YtcJ [General function prediction only];


Pssm-ID: 441182 [Multi-domain]  Cd Length: 535  Bit Score: 60.97  E-value: 4.77e-10
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518383840   9 TLLRNVKI--VAPNDLGCQNILIAGDKVAAIG-----RNLTIPQgycVEEIDLSGHTLMPGFIDSHVHMI 71
Cdd:COG1574   10 LLLTNGRIytMDPAQPVAEAVAVRDGRIVAVGsdaevRALAGPA---TEVIDLGGKTVLPGFIDAHVHLL 76
Met_dep_hydrolase_A cd01299
Metallo-dependent hydrolases, subgroup A is part of the superfamily of metallo-dependent ...
 49-367 1.56e-09

Metallo-dependent hydrolases, subgroup A is part of the superfamily of metallo-dependent hydrolases, a large group of proteins that show conservation in their 3-dimensional fold (TIM barrel) and in details of their active site. The vast majority of the members have a conserved metal binding site, involving four histidines and one aspartic acid residue. In the common reaction mechanism, the metal ion (or ions) deprotonate a water molecule for a nucleophilic attack on the substrate. The function of this subgroup is unknown.


Pssm-ID: 238624 [Multi-domain]  Cd Length: 342  Bit Score: 58.84  E-value: 1.56e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518383840  49 VEEIDLSGHTLMPGFIDSHVHMIGGGGEGGYATRTPEIVLSKVTT--------AGVTTlVGCLGTDGVtrhveSLLAKA- 119
Cdd:cd01299    1 AQVIDLGGKTLMPGLIDAHTHLGSDPGDLPLDLALPVEYRTIRATrqaraalrAGFTT-VRDAGGADY-----GLLRDAi 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518383840 120 -RGLEA--------EGLSTyiyTGAYEIPTPTITGSVRKDIIII-------------DKIIGAGEL-AMADHRSAQPTK- 175
Cdd:cd01299   75 dAGLIPgprvfasgRALSQ---TGGHGDPRGLSGLFPAGGLAAVvdgveevraavreQLRRGADQIkIMATGGVLSPGDp 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518383840 176 --------DEYQKIAAEA-RVGGMLSAKAGiidmhmgdGKDGMKLLFEITANGeIpksqflpTHVNrnkELFAQSIEWAK 246
Cdd:cd01299  152 ppdtqfseEELRAIVDEAhKAGLYVAAHAY--------GAEAIRRAIRAGVDT-I-------EHGF---LIDDETIELMK 212

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518383840 247 QGGM---MDITSGVS----------PASGSVKAIKPSQ----AVKKALDAGVPlsqITMSSDgngsmpifdqqgntIGVG 309
Cdd:cd01299  213 EKGIflvPTLATYEAlaaegaapglPADSAEKVALVLEagrdALRRAHKAGVK---IAFGTD--------------AGFP 275

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 518383840 310 VASQFSMLEEFRDMVQLeGIEISDAVQIITTNVAKILKIWPQKGSIQVGSDADFTIID 367
Cdd:cd01299  276 VPPHGWNARELELLVKA-GGTPAEALRAATANAAELLGLSDELGVIEAGKLADLLVVD 332
SsnA COG0402
Cytosine/adenosine deaminase or related metal-dependent hydrolase [Nucleotide transport and ...
 9-70 2.11e-09

Cytosine/adenosine deaminase or related metal-dependent hydrolase [Nucleotide transport and metabolism, General function prediction only]; Cytosine/adenosine deaminase or related metal-dependent hydrolase is part of the Pathway/BioSystem: Pyrimidine salvage


Pssm-ID: 440171 [Multi-domain]  Cd Length: 416  Bit Score: 58.68  E-value: 2.11e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 518383840   9 TLLRNVKIVAPNDLGC----QNILIAGDKVAAIGRNLTIPQGY-CVEEIDLSGHTLMPGFIDSHVHM 70
Cdd:COG0402    2 LLIRGAWVLTMDPAGGvledGAVLVEDGRIAAVGPGAELPARYpAAEVIDAGGKLVLPGLVNTHTHL 68
Cyclic_amidohydrolases cd01302
Cyclic amidohydrolases, including hydantoinase, dihydropyrimidinase, allantoinase, and ...
 59-386 2.93e-09

Cyclic amidohydrolases, including hydantoinase, dihydropyrimidinase, allantoinase, and dihydroorotase, are involved in the metabolism of pyrimidines and purines, sharing the property of hydrolyzing the cyclic amide bond of each substrate to the corresponding N-carbamyl amino acids. Allantoinases catalyze the degradation of purines, while dihydropyrimidinases and hydantoinases, a microbial counterpart of dihydropyrimidinase, are involved in pyrimidine degradation. Dihydroorotase participates in the de novo synthesis of pyrimidines.


Pssm-ID: 238627 [Multi-domain]  Cd Length: 337  Bit Score: 58.17  E-value: 2.93e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518383840  59 LMPGFIDSHVHMIGGggeggYATRTPEIVLSKVTTA---GVTTLVGCLGTDGVTRHVESLLAKARGLEAEGLSTY-IYTG 134
Cdd:cd01302    3 VLPGFIDIHVHLRDP-----GGTTYKEDFESGSRAAaagGVTTVIDMPNTGPPPIDLPAIELKIKLAEESSYVDFsFHAG 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518383840 135 AYEI-PTPTITGSVRKDIIIIDKIIGAGELAMADHRSAQpTKDEYQKIAAearVGGMLSAKAGIIdmhmgdgkdgMKLLF 213
Cdd:cd01302   78 IGPGdVTDELKKLFDAGINSLKVFMNYYFGELFDVDDGT-LMRTFLEIAS---RGGPVMVHAERA----------AQLAE 143

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518383840 214 EITANGEIpksqflpTHVNRNKELFAqsIEWAKQGGMmDITSGVSP-----------ASGSVKAIKP---SQAVKKALDA 279
Cdd:cd01302  144 EAGANVHI-------AHVSSGEALEL--IKFAKNKGV-KVTCEVCPhhlfldesmlrLNGAWGKVNPplrSKEDREALWE 213

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518383840 280 GVPLSQI-TMSSDGNGSmPIFDQQGNT---------IGVGVASQFsMLEEFRDmvqlEGIEISDAVQIITTNVAKILKIW 349
Cdd:cd01302  214 GVKNGKIdTIASDHAPH-SKEEKESGKdiwkappgfPGLETRLPI-LLTEGVK----RGLSLETLVEILSENPARIFGLY 287

                        330       340       350
                 ....*....|....*....|....*....|....*..
gi 518383840 350 PqKGSIQVGSDADFTIIDDEfvLQHVWAKGQHMVNAG 386
Cdd:cd01302  288 P-KGTIAVGYDADLVIVDPK--KEWKVTAEEIESKAD 321
PRK08323 PRK08323
phenylhydantoinase; Validated
 9-70 2.99e-09

phenylhydantoinase; Validated


Pssm-ID: 236240 [Multi-domain]  Cd Length: 459  Bit Score: 58.26  E-value: 2.99e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 518383840   9 TLLRNVKIVAPNDLGCQNILIAGDKVAAIGRNltipQGycVEEIDLSGHTLMPGFIDSHVHM 70
Cdd:PRK08323   3 TLIKNGTVVTADDTYKADVLIEDGKIAAIGAN----LG--DEVIDATGKYVMPGGIDPHTHM 58
COG3964 COG3964
Predicted amidohydrolase [General function prediction only];
10-69 4.18e-09

Predicted amidohydrolase [General function prediction only];


Pssm-ID: 443164 [Multi-domain]  Cd Length: 376  Bit Score: 57.87  E-value: 4.18e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 518383840  10 LLRNVKIVAP--NDLGCQNILIAGDKVAAIGRNLTIPQGycVEEIDLSGHTLMPGFIDSHVH 69
Cdd:COG3964    3 LIKGGRVIDPanGIDGVMDIAIKDGKIAAVAKDIDAAEA--KKVIDASGLYVTPGLIDLHTH 62
D-aminoacylase cd01297
D-aminoacylases (N-acyl-D-Amino acid amidohydrolases) catalyze the hydrolysis of ...
 9-109 1.26e-08

D-aminoacylases (N-acyl-D-Amino acid amidohydrolases) catalyze the hydrolysis of N-acyl-D-amino acids to produce the corresponding D-amino acids, which are used as intermediates in the synthesis of pesticides, bioactive peptides, and antibiotics.


Pssm-ID: 238622 [Multi-domain]  Cd Length: 415  Bit Score: 56.54  E-value: 1.26e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518383840   9 TLLRNVKIV----APNDLGcqNILIAGDKVAAIGRNLTIPqgyCVEEIDLSGHTLMPGFIDSHVHmiggggEGGYATRTP 84
Cdd:cd01297    2 LVIRNGTVVdgtgAPPFTA--DVGIRDGRIAAIGPILSTS---AREVIDAAGLVVAPGFIDVHTH------YDGQVFWDP 70

                         90       100
                 ....*....|....*....|....*
gi 518383840  85 EivLSKVTTAGVTTLVgcLGTDGVT 109
Cdd:cd01297   71 D--LRPSSRQGVTTVV--LGNCGVS 91
PRK08323 PRK08323
phenylhydantoinase; Validated
 335-382 3.88e-08

phenylhydantoinase; Validated


Pssm-ID: 236240 [Multi-domain]  Cd Length: 459  Bit Score: 54.79  E-value: 3.88e-08
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 518383840 335 VQIITTNVAKILKIWPQKGSIQVGSDADFTIIDDEfVLQHVWAKGQHM 382
Cdd:PRK08323 362 VELTSTNPAKIFGLYPRKGTIAVGADADIVIWDPN-ATKTISASTLHS 408
L-HYD_ALN cd01315
L-Hydantoinases (L-HYDs) and Allantoinase (ALN); L-Hydantoinases are a member of the ...
 9-71 5.17e-08

L-Hydantoinases (L-HYDs) and Allantoinase (ALN); L-Hydantoinases are a member of the dihydropyrimidinase family, which catalyzes the reversible hydrolytic ring opening of dihydropyrimidines and hydantoins (five-membered cyclic diamides used in biotechnology). But L-HYDs differ by having an L-enantio specificity and by lacking activity on possible natural substrates such as dihydropyrimidines. Allantoinase catalyzes the hydrolytic cleavage of the five-member ring of allantoin (5-ureidohydantoin) to form allantoic acid.


Pssm-ID: 238640 [Multi-domain]  Cd Length: 447  Bit Score: 54.60  E-value: 5.17e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 518383840   9 TLLRNVKIVAPNDLGCQNILIAGDKVAAIGRNLTIPQGYcvEEIDLSGHTLMPGFIDSHVHMI 71
Cdd:cd01315    2 LVIKNGRVVTPDGVREADIAVKGGKIAAIGPDIANTEAE--EVIDAGGLVVMPGLIDTHVHIN 62
pyrC PRK09357
dihydroorotase; Validated
 9-69 5.42e-08

dihydroorotase; Validated


Pssm-ID: 236479 [Multi-domain]  Cd Length: 423  Bit Score: 54.43  E-value: 5.42e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 518383840   9 TLLRNVKIVAPNDLGCQ-NILIAGDKVAAIGRNLTIPQgycVEEIDLSGHTLMPGFIDSHVH 69
Cdd:PRK09357   3 ILIKNGRVIDPKGLDEVaDVLIDDGKIAAIGENIEAEG---AEVIDATGLVVAPGLVDLHVH 61
Bact_CD cd01293
Bacterial cytosine deaminase and related metal-dependent hydrolases. Cytosine deaminases (CDs) ...
 10-70 7.31e-08

Bacterial cytosine deaminase and related metal-dependent hydrolases. Cytosine deaminases (CDs) catalyze the deamination of cytosine, producing uracil and ammonia. They play an important role in pyrimidine salvage. CDs are present in prokaryotes and fungi, but not mammalian cells. The bacterial enzymes, but not the fungal enzymes, are related to the adenosine deaminases (ADA). The bacterial enzymes are iron dependent and hexameric.


Pssm-ID: 238618 [Multi-domain]  Cd Length: 398  Bit Score: 53.79  E-value: 7.31e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 518383840  10 LLRNVKIVAPnDLGCQNILIAGDKVAAIGRNLTIPQGYcvEEIDLSGHTLMPGFIDSHVHM 70
Cdd:cd01293    1 LLRNARLADG-GTALVDIAIEDGRIAAIGPALAVPPDA--EEVDAKGRLVLPAFVDPHIHL 58
COG3653 COG3653
N-acyl-D-aspartate/D-glutamate deacylase [Secondary metabolites biosynthesis, transport and ...
 26-109 7.49e-08

N-acyl-D-aspartate/D-glutamate deacylase [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 442870 [Multi-domain]  Cd Length: 528  Bit Score: 54.02  E-value: 7.49e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518383840  26 NILIAGDKVAAIGRNLTIPqgyCVEEIDLSGHTLMPGFIDSHVHmiggggeggY---ATRTPEiVLSKVTTaGVTTLVgc 102
Cdd:COG3653   23 DVAIKGGRIVAVGDLAAAE---AARVIDATGLVVAPGFIDIHTH---------YdlqLLWDPR-LEPSLRQ-GVTTVV-- 86


                 ....*..
gi 518383840 103 LGTDGVT 109
Cdd:COG3653   87 MGNCGVS 93
PRK07575 PRK07575
dihydroorotase; Provisional
 9-69 1.01e-07

dihydroorotase; Provisional


Pssm-ID: 236055 [Multi-domain]  Cd Length: 438  Bit Score: 53.52  E-value: 1.01e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 518383840   9 TLLRNVKIVAPN-DLGCQNILIAGDKVAAIGRNLTIPQGycVEEIDLSGHTLMPGFIDSHVH 69
Cdd:PRK07575   5 LLIRNARILLPSgELLLGDVLVEDGKIVAIAPEISATAV--DTVIDAEGLTLLPGVIDPQVH 64
AdeC COG1001
Adenine deaminase [Nucleotide transport and metabolism];
9-70 1.55e-07

Adenine deaminase [Nucleotide transport and metabolism];


Pssm-ID: 440625 [Multi-domain]  Cd Length: 559  Bit Score: 53.18  E-value: 1.55e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 518383840   9 TLLRNVKIV-------APNDlgcqnILIAGDKVAAIGRnlTIPQGycVEEIDLSGHTLMPGFIDSHVHM 70
Cdd:COG1001    7 LVIKNGRLVnvftgeiLEGD-----IAIAGGRIAGVGD--YIGEA--TEVIDAAGRYLVPGFIDGHVHI 66
YtcJ_like cd01300
YtcJ_like metal dependent amidohydrolases. YtcJ is a Bacillus subtilis ORF of unknown function. ...
 27-71 1.66e-07

YtcJ_like metal dependent amidohydrolases. YtcJ is a Bacillus subtilis ORF of unknown function. The Arabidopsis homolog LAF3 has been identified as a factor required for phytochrome A signalling.


Pssm-ID: 238625 [Multi-domain]  Cd Length: 479  Bit Score: 53.08  E-value: 1.66e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 518383840  27 ILIAGDKVAAIGRNLTIPQ--GYCVEEIDLSGHTLMPGFIDSHVHMI 71
Cdd:cd01300    2 VAVRDGRIVAVGSDAEAKAlkGPATEVIDLKGKTVLPGFIDSHSHLL 48
PRK05985 PRK05985
cytosine deaminase; Provisional
 9-69 3.61e-07

cytosine deaminase; Provisional


Pssm-ID: 180337 [Multi-domain]  Cd Length: 391  Bit Score: 51.86  E-value: 3.61e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 518383840   9 TLLRNVKivaPNDLGCQNILIAGDKVAAIGRNLTIPQGycVEEIDLSGHTLMPGFIDSHVH 69
Cdd:PRK05985   4 LLFRNVR---PAGGAAVDILIRDGRIAAIGPALAAPPG--AEVEDGGGALALPGLVDGHIH 59
PRK13404 PRK13404
dihydropyrimidinase; Provisional
 7-70 8.29e-07

dihydropyrimidinase; Provisional


Pssm-ID: 184033 [Multi-domain]  Cd Length: 477  Bit Score: 50.85  E-value: 8.29e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 518383840   7 FFTLLRNVKIVAPNDLGCQNILIAGDKVAAIGRNLtipqGYCVEEIDLSGHTLMPGFIDSHVHM 70
Cdd:PRK13404   4 FDLVIRGGTVVTATDTFQADIGIRGGRIAALGEGL----GPGAREIDATGRLVLPGGVDSHCHI 63
PRK02382 PRK02382
dihydroorotase; Provisional
 10-69 9.39e-07

dihydroorotase; Provisional


Pssm-ID: 179417 [Multi-domain]  Cd Length: 443  Bit Score: 50.42  E-value: 9.39e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 518383840  10 LLRNVKIVAPNDLGCQNILIAGDKVAAIGRNLTIPQGYcvEEIDLSGHTLMPGFIDSHVH 69
Cdd:PRK02382   5 LLKDGRVYYNNSLQPRDVRIDGGKITAVGKDLDGSSSE--EVIDARGMLLLPGGIDVHVH 62
PLN02942 PLN02942
dihydropyrimidinase
 323-367 1.21e-06

dihydropyrimidinase


Pssm-ID: 178530  Cd Length: 486  Bit Score: 50.23  E-value: 1.21e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 518383840 323 MVQLEGIEISDAVQIITTNVAKILKIWPQKGSIQVGSDADFTIID 367
Cdd:PLN02942 356 MVESGQISPTDYVRVTSTECAKIFNIYPRKGAILAGSDADIIILN 400
PRK07572 PRK07572
cytosine deaminase; Validated
 10-70 3.90e-06

cytosine deaminase; Validated


Pssm-ID: 181039  Cd Length: 426  Bit Score: 48.48  E-value: 3.90e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 518383840  10 LLRNVKIvaPNDLGCQNILIAGDKVAAIGRNLTIPQGycvEEIDLSGHTLMPGFIDSHVHM 70
Cdd:PRK07572   5 IVRNANL--PDGRTGIDIGIAGGRIAAVEPGLQAEAA---EEIDAAGRLVSPPFVDPHFHM 60
PRK08204 PRK08204
hypothetical protein; Provisional
 9-69 5.61e-06

hypothetical protein; Provisional


Pssm-ID: 181288 [Multi-domain]  Cd Length: 449  Bit Score: 48.07  E-value: 5.61e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 518383840   9 TLLRNVKIV----APNDLGCQNILIAGDKVAAIGRNLTIPQgycVEEIDLSGHTLMPGFIDSHVH 69
Cdd:PRK08204   4 TLIRGGTVLtmdpAIGDLPRGDILIEGDRIAAVAPSIEAPD---AEVVDARGMIVMPGLVDTHRH 65
PRK09060 PRK09060
dihydroorotase; Validated
 3-69 6.11e-06

dihydroorotase; Validated


Pssm-ID: 181632 [Multi-domain]  Cd Length: 444  Bit Score: 47.99  E-value: 6.11e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 518383840   3 QSKIFFTLLRNVKIVAPNDLGCQNILIAGDKVAAIGRNLTIPQGycvEEIDLSGHTLMPGFIDSHVH 69
Cdd:PRK09060   1 MTQTFDLILKGGTVVNPDGEGRADIGIRDGRIAAIGDLSGASAG---EVIDCRGLHVLPGVIDSQVH 64
Amidohydro_3 pfam07969
Amidohydrolase family;
268-371 7.35e-06

Amidohydrolase family;


Pssm-ID: 400360 [Multi-domain]  Cd Length: 464  Bit Score: 47.91  E-value: 7.35e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518383840  268 KPSQAVKKALDAGVPLSqitMSSDGNGSM--PIFdqqgnTIGVGVASQFSMLEEFRDMvqLEGIEISDAVQIITTNVAKI 345
Cdd:pfam07969 346 RGLTPVKELLNAGVKVA---LGSDAPVGPfdPWP-----RIGAAVMRQTAGGGEVLGP--DEELSLEEALALYTSGPAKA 415

                          90       100
                  ....*....|....*....|....*.
gi 518383840  346 LKIWPQKGSIQVGSDADFTIIDDEFV 371
Cdd:pfam07969 416 LGLEDRKGTLGVGKDADLVVLDDDPL 441
PRK09236 PRK09236
dihydroorotase; Reviewed
 9-69 7.74e-06

dihydroorotase; Reviewed


Pssm-ID: 181716  Cd Length: 444  Bit Score: 47.56  E-value: 7.74e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 518383840   9 TLLRNVKIVAPNDLGCQNILIAGDKVAAIGRNltIPQGYCVEEIDLSGHTLMPGFIDSHVH 69
Cdd:PRK09236   4 ILIKNARIVNEGKIFEGDVLIENGRIAKIASS--ISAKSADTVIDAAGRYLLPGMIDDQVH 62
PRK13404 PRK13404
dihydropyrimidinase; Provisional
 293-367 1.20e-05

dihydropyrimidinase; Provisional


Pssm-ID: 184033 [Multi-domain]  Cd Length: 477  Bit Score: 47.00  E-value: 1.20e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 518383840 293 NGSMPIFDQQGNTIGvGVASQFSMLeeFRDMVQLEGIEISDAVQIITTNVAKILKIWPQKGSIQVGSDADFTIID 367
Cdd:PRK13404 332 AGANPSFKAIANGIP-GIETRLPLL--FSEGVVKGRISLNRFVALTSTNPAKLYGLYPRKGAIAIGADADIAIWD 403
PRK06189 PRK06189
allantoinase; Provisional
 270-367 1.23e-05

allantoinase; Provisional


Pssm-ID: 235732 [Multi-domain]  Cd Length: 451  Bit Score: 47.00  E-value: 1.23e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518383840 270 SQAVKKALDAGVPLSQITM-SSDGNGSMP-------IFDQQGNTIGVgvasQFSMLEEFRDMVQLEGIEISDAVQIITTN 341
Cdd:PRK06189 290 SRSQKEELWRGLLAGEIDMiSSDHSPCPPelkegddFFLVWGGISGG----QSTLLVMLTEGYIERGIPLETIARLLATN 365

                         90       100
                 ....*....|....*....|....*.
gi 518383840 342 VAKILKIwPQKGSIQVGSDADFTIID 367
Cdd:PRK06189 366 PAKRFGL-PQKGRLEVGADADFVLVD 390
Met_dep_hydrolase_B cd01307
Metallo-dependent hydrolases, subgroup B is part of the superfamily of metallo-dependent ...
 26-368 1.65e-05

Metallo-dependent hydrolases, subgroup B is part of the superfamily of metallo-dependent hydrolases, a large group of proteins that show conservation in their 3-dimensional fold (TIM barrel) and in details of their active site. The vast majority of the members have a conserved metal binding site, involving four histidines and one aspartic acid residue. In the common reaction mechanism, the metal ion (or ions) deprotonate a water molecule for a nucleophilic attack on the substrate. The function of this subgroup is unknown.


Pssm-ID: 238632 [Multi-domain]  Cd Length: 338  Bit Score: 46.55  E-value: 1.65e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518383840  26 NILIAGDKVAAIGRNLTIPQGycVEEIDLSGHTLMPGFIDSHVHMigGGGEGGYATRTPEIVLSKvttaGVTTLV----- 100
Cdd:cd01307    1 DVAIENGKIAAVGAALAAPAA--TQIVDAGGCYVSPGWIDLHVHV--YQGGTRYGDRPDMIGVKS----GVTTVVdagsa 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518383840 101 GCLGTDGVTRHVesllakargLEAEGLSTYIYTGAYEIptptitGSVRKdiiiidkiigagelamadHRSAQPTKDEYQK 180
Cdd:cd01307   73 GADNIDGFRYTV---------IERSATRVYAFLNISRV------GLVAQ------------------DELPDPDNIDEDA 119

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518383840 181 IAAEAR------VGgmLSAKAGIIDmhMGD-GKDGMKLLFEITANGEIP-----------KSQFLP--------TH---- 230
Cdd:cd01307  120 VVAAAReypdviVG--LKARASKSV--VGEwGIKPLELAKKIAKEADLPlmvhigspppiLDEVVPllrrgdvlTHcfng 195

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518383840 231 -----VNRNKELFAQSIEWAKQGGMMDITSGVSPASGSVkaikpsqaVKKALDAGvpLSQITMSSDGNGSmpifdqqgNT 305
Cdd:cd01307  196 kpngiVDEEGEVLPLVRRARERGVIFDVGHGTASFSFRV--------ARAAIAAG--LLPDTISSDIHGR--------NR 257

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 518383840 306 IGVGVASQFSMLEEFRDMvqleGIEISDAVQIITTNVAKILKIwPQKGSIQVGSDADFTIIDD 368
Cdd:cd01307  258 TNGPVYALATTLSKLLAL----GMPLEEVIEAVTANPARMLGL-AEIGTLAVGYDADLTVFDL 315
PRK09228 PRK09228
guanine deaminase; Provisional
 27-69 2.06e-05

guanine deaminase; Provisional


Pssm-ID: 236419 [Multi-domain]  Cd Length: 433  Bit Score: 46.34  E-value: 2.06e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 518383840  27 ILIAGDKVAAIG--RNL--TIPQGycVEEIDLSGHTLMPGFIDSHVH 69
Cdd:PRK09228  34 LLVEDGRIVAAGpyAELraQLPAD--AEVTDYRGKLILPGFIDTHIH 78
ade TIGR01178
adenine deaminase; The family described by this model includes an experimentally characterized ...
 26-70 2.84e-05

adenine deaminase; The family described by this model includes an experimentally characterized adenine deaminase of Bacillus subtilis. It also include a member from Methanobacterium thermoautotrophicum, in which adenine deaminase activity has been detected. [Purines, pyrimidines, nucleosides, and nucleotides, Salvage of nucleosides and nucleotides]


Pssm-ID: 130246 [Multi-domain]  Cd Length: 552  Bit Score: 45.92  E-value: 2.84e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 518383840   26 NILIAGDKVAAIGRNltipqgYCVEEIDLSGHTLMPGFIDSHVHM 70
Cdd:TIGR01178  21 DIAIANGHIAGVGKY------NGVKVIDALGEYAVPGFIDAHIHI 59
guan_deamin TIGR02967
guanine deaminase; This model describes guanine deaminase, which hydrolyzes guanine to ...
 49-367 3.36e-05

guanine deaminase; This model describes guanine deaminase, which hydrolyzes guanine to xanthine and ammonia. Xanthine can then be converted to urate by xanthine dehydrogenase, and urate subsequently degraded. In some bacteria, the guanine deaminase gene is found near the xdhABC genes for xanthine dehydrogenase. Non-homologous forms of guanine deaminase also exist, as well as distantly related forms outside the scope of this model. [Purines, pyrimidines, nucleosides, and nucleotides, Other]


Pssm-ID: 132012 [Multi-domain]  Cd Length: 401  Bit Score: 45.71  E-value: 3.36e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518383840   49 VEEIDLSGHTLMPGFIDSHVH-----MIGGGGE-------------------GGYATRTPEIVLSKVTTAGVTT-LVGCl 103
Cdd:TIGR02967  33 VEIDDYRGHLIMPGFIDTHIHypqteMIASYGEqllewlekytfptearfadPDHAEEVAEFFLDELLRNGTTTaLVFA- 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518383840  104 gtdgvTRHVESLLAKARGLEAEGLStyiytgayeiptpTITGSVrkdiiiidkiigagelaMADHRSAQPTKDEYQKIAA 183
Cdd:TIGR02967 112 -----TVHPESVDALFEAALKRGMR-------------MIAGKV-----------------LMDRNAPDYLRDTAESSYD 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518383840  184 EarvggmlsAKAGIIDMHmgdGKDgmKLLFEIT-------------ANGEIPKSQ---FLPTHVNRNKElfaqSIEWAK- 246
Cdd:TIGR02967 157 E--------SKALIERWH---GKG--RLLYAVTprfaptsspeqlaAAGELAKEYpdvYVQTHLSENKD----EIAWVKe 219

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518383840  247 ----QGGMMDITSG---VSPASGSVKAIKPSQAVKKAL---DAGV---PLSQITMSSdgnGSMPIFDQQGNTIGVGVAS- 312
Cdd:TIGR02967 220 lfpeAKDYLDVYDHyglLGRRSVFAHCIHLSDEECQRLaetGAAIahcPTSNLFLGS---GLFNLKKALEHGVRVGLGTd 296

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 518383840  313 -----QFSMLEEFRDMV---QLEGIEIS--DAVQIITTNVAKILKIWPQKGSIQVGSDADFTIID 367
Cdd:TIGR02967 297 vgggtSFSMLQTLREAYkvsQLQGARLSpfEAFYLATLGGARALDLDDRIGNFEPGKEADFVVLD 361
PRK08203 PRK08203
hydroxydechloroatrazine ethylaminohydrolase; Reviewed
 9-70 4.40e-05

hydroxydechloroatrazine ethylaminohydrolase; Reviewed


Pssm-ID: 236184 [Multi-domain]  Cd Length: 451  Bit Score: 45.23  E-value: 4.40e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 518383840   9 TLLRN-VKIVAPNDLGCQN----ILIAGDKVAAIGRNLTIPQGyCVEEIDLSGHTLMPGFIDSHVHM 70
Cdd:PRK08203   3 LWIKNpLAIVTMDAARREIadggLVVEGGRIVEVGPGGALPQP-ADEVFDARGHVVTPGLVNTHHHF 68
PRK15446 PRK15446
phosphonate metabolism protein PhnM; Provisional
 9-67 5.24e-05

phosphonate metabolism protein PhnM; Provisional


Pssm-ID: 237967 [Multi-domain]  Cd Length: 383  Bit Score: 44.78  E-value: 5.24e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 518383840   9 TLLRNVKIVAPNDLGCQNILIAGDKVAAIGRNltipQGYCVEEIDLSGHTLMPGFIDSH 67
Cdd:PRK15446   4 MILSNARLVLPDEVVDGSLLIEDGRIAAIDPG----ASALPGAIDAEGDYLLPGLVDLH 58
Imidazolone-5PH cd01296
Imidazolonepropionase/imidazolone-5-propionate hydrolase (Imidazolone-5PH) catalyzes the third ...
 27-71 8.08e-05

Imidazolonepropionase/imidazolone-5-propionate hydrolase (Imidazolone-5PH) catalyzes the third step in the histidine degradation pathway, the hydrolysis of (S)-3-(5-oxo-4,5-dihydro-3H-imidazol-4-yl)propanoate to N-formimidoyl-L-glutamate. In bacteria, the enzyme is part of histidine utilization (hut) operon.


Pssm-ID: 238621 [Multi-domain]  Cd Length: 371  Bit Score: 44.17  E-value: 8.08e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 518383840  27 ILIAGDKVAAIGRNLTIPQ--GYCVEEIDLSGHTLMPGFIDSHVHMI 71
Cdd:cd01296    1 IAIRDGRIAAVGPAASLPApgPAAAEEIDAGGRAVTPGLVDCHTHLV 47
PRK07228 PRK07228
5'-deoxyadenosine deaminase;
9-69 1.16e-04

5'-deoxyadenosine deaminase;


Pssm-ID: 180895 [Multi-domain]  Cd Length: 445  Bit Score: 43.83  E-value: 1.16e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 518383840   9 TLLRNVKIVAPN---DLGCQNILIAGDKVAAIGRNLtIPQGYcVEEIDLSGHTLMPGFIDSHVH 69
Cdd:PRK07228   3 ILIKNAGIVTMNakrEIVDGDVLIEDDRIAAVGDRL-DLEDY-DDHIDATGKVVIPGLIQGHIH 64
Met_dep_hydrolase_C cd01309
Metallo-dependent hydrolases, subgroup C is part of the superfamily of metallo-dependent ...
 33-69 1.68e-04

Metallo-dependent hydrolases, subgroup C is part of the superfamily of metallo-dependent hydrolases, a large group of proteins that show conservation in their 3-dimensional fold (TIM barrel) and in details of their active site. The vast majority of the members have a conserved metal binding site, involving four histidines and one aspartic acid residue. In the common reaction mechanism, the metal ion (or ions) deprotonate a water molecule for a nucleophilic attack on the substrate. The function of this subgroup is unknown.


Pssm-ID: 238634 [Multi-domain]  Cd Length: 359  Bit Score: 43.45  E-value: 1.68e-04
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 518383840  33 KVAAIGRNLTIPQGYCVeeIDLSGHTLMPGFIDSHVH 69
Cdd:cd01309    3 KIVAVGAEITTPADAEV--IDAKGKHVTPGLIDAHSH 37
PRK06687 PRK06687
TRZ/ATZ family protein;
282-366 2.01e-04

TRZ/ATZ family protein;


Pssm-ID: 180657 [Multi-domain]  Cd Length: 419  Bit Score: 43.07  E-value: 2.01e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518383840 282 PLSQITMSSdgnGSMPIFDQQGNTIGVGVAS-------QFSMLEEFRDMVQLEGIEISDAVQ--------IITTNVAKIL 346
Cdd:PRK06687 275 PISNLKLAS---GIAPIIQLQKAGVAVGIATdsvasnnNLDMFEEGRTAALLQKMKSGDASQfpietalkVLTIEGAKAL 351

                         90       100
                 ....*....|....*....|
gi 518383840 347 KIWPQKGSIQVGSDADFTII 366
Cdd:PRK06687 352 GMENQIGSLEVGKQADFLVI 371
AdeC COG1001
Adenine deaminase [Nucleotide transport and metabolism];
327-390 2.94e-04

Adenine deaminase [Nucleotide transport and metabolism];


Pssm-ID: 440625 [Multi-domain]  Cd Length: 559  Bit Score: 42.78  E-value: 2.94e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 518383840 327 EGIEISDAVQIITTNVAKILKIwPQKGSIQVGSDADFTIIDD--EFVLQHVWAKGQHMVNAGKAVV 390
Cdd:COG1001  282 LGLDPVTAIQMATLNAAEHFGL-KDLGAIAPGRRADIVLLDDleDFKVEKVYADGKLVAEDGKLLV 346
pyrC_multi TIGR00857
dihydroorotase, multifunctional complex type; In contrast to the homodimeric type of ...
 27-69 3.65e-04

dihydroorotase, multifunctional complex type; In contrast to the homodimeric type of dihydroorotase found in E. coli, this class tends to appear in a large, multifunctional complex with aspartate transcarbamoylase. Homologous domains appear in multifunctional proteins of higher eukaryotes. In some species, including Pseudomonas putida and P. aeruginosa, this protein is inactive but is required as a non-catalytic subunit of aspartate transcarbamoylase (ATCase). In these species, a second, active dihydroorotase is also present. The seed for this model does not include any example of the dihydroorotase domain of eukaryotic multidomain pyrimidine synthesis proteins. All proteins described by this model should represent active and inactive dihydroorotase per se and functionally equivalent domains of multifunctional proteins from higher eukaryotes, but exclude related proteins such as allantoinase. [Purines, pyrimidines, nucleosides, and nucleotides, Pyrimidine ribonucleotide biosynthesis]


Pssm-ID: 273302 [Multi-domain]  Cd Length: 411  Bit Score: 42.43  E-value: 3.65e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 518383840   27 ILIAGDKVAAIGRnLTIPQGycVEEIDLSGHTLMPGFIDSHVH 69
Cdd:TIGR00857   8 ILVEGGRIKKIGK-LRIPPD--AEVIDAKGLLVLPGFIDLHVH 47
PRK07203 PRK07203
putative aminohydrolase SsnA;
27-69 7.76e-04

putative aminohydrolase SsnA;


Pssm-ID: 235963 [Multi-domain]  Cd Length: 442  Bit Score: 41.46  E-value: 7.76e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 518383840  27 ILIAGDKVAAIGRNLTIPQGYCVEE-IDLSGHTLMPGFIDSHVH 69
Cdd:PRK07203  24 IAIEGNVIVEIGTTDELKAKYPDAEfIDAKGKLIMPGLINSHNH 67
Met_dep_hydrolase_C cd01309
Metallo-dependent hydrolases, subgroup C is part of the superfamily of metallo-dependent ...
 327-369 8.12e-04

Metallo-dependent hydrolases, subgroup C is part of the superfamily of metallo-dependent hydrolases, a large group of proteins that show conservation in their 3-dimensional fold (TIM barrel) and in details of their active site. The vast majority of the members have a conserved metal binding site, involving four histidines and one aspartic acid residue. In the common reaction mechanism, the metal ion (or ions) deprotonate a water molecule for a nucleophilic attack on the substrate. The function of this subgroup is unknown.


Pssm-ID: 238634 [Multi-domain]  Cd Length: 359  Bit Score: 41.14  E-value: 8.12e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 518383840 327 EGIEISDAVQIITTNVAKILKIWPQKGSIQVGSDADFTIIDDE 369
Cdd:cd01309  298 YGLSYEEALKAITINPAKILGIEDRVGSLEPGKDADLVVWNGD 340
PRK08393 PRK08393
N-ethylammeline chlorohydrolase; Provisional
 10-69 1.27e-03

N-ethylammeline chlorohydrolase; Provisional


Pssm-ID: 181411 [Multi-domain]  Cd Length: 424  Bit Score: 40.55  E-value: 1.27e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 518383840  10 LLRNVKIVAPNDLGC--QNILIAGDKVAAIGRNLTIPQGycvEEIDLSGHTLMPGFIDSHVH 69
Cdd:PRK08393   4 LIKNGYVIYGENLKVirADVLIEGNKIVEVKRNINKPAD---TVIDASGSVVSPGFINAHTH 62
AdeC cd01295
Adenine deaminase (AdeC) directly deaminates adenine to form hypoxanthine. This reaction is ...
 312-379 2.89e-03

Adenine deaminase (AdeC) directly deaminates adenine to form hypoxanthine. This reaction is part of one of the adenine salvage pathways, as well as the degradation pathway. It is important for adenine utilization as a purine, as well as a nitrogen source in bacteria and archea.


Pssm-ID: 238620 [Multi-domain]  Cd Length: 422  Bit Score: 39.51  E-value: 2.89e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518383840 312 SQFSMLEEFRDMVQlEGIEISDAVQIITTNVAKILKIwPQKGSIQVGSDADFTIIDD--EFVLQHVWAKG 379
Cdd:cd01295  219 SEGHLDYIVRRAIE-AGIPPEDAIQMATINPAECYGL-HDLGAIAPGRIADIVILDDleNFNITTVLAKG 286
PRK09061 PRK09061
D-glutamate deacylase; Validated
 26-69 2.97e-03

D-glutamate deacylase; Validated


Pssm-ID: 236369 [Multi-domain]  Cd Length: 509  Bit Score: 39.68  E-value: 2.97e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 518383840  26 NILIAGDKVAAIGRNLTIPQgycvEEIDLSGHTLMPGFIDSHVH 69
Cdd:PRK09061  40 DVGIKGGKIAAVGTAAIEGD----RTIDATGLVVAPGFIDLHAH 79
Imidazolone-5PH cd01296
Imidazolonepropionase/imidazolone-5-propionate hydrolase (Imidazolone-5PH) catalyzes the third ...
 273-367 3.34e-03

Imidazolonepropionase/imidazolone-5-propionate hydrolase (Imidazolone-5PH) catalyzes the third step in the histidine degradation pathway, the hydrolysis of (S)-3-(5-oxo-4,5-dihydro-3H-imidazol-4-yl)propanoate to N-formimidoyl-L-glutamate. In bacteria, the enzyme is part of histidine utilization (hut) operon.


Pssm-ID: 238621 [Multi-domain]  Cd Length: 371  Bit Score: 39.16  E-value: 3.34e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518383840 273 VKKALDAGVPlsqITMSSDGN-GSMPIFDQQgntigvgvasqFSMLEEFRDMvqleGIEISDAVQIITTNVAKILKIWPQ 351
Cdd:cd01296  271 ARKLIDAGVP---VALGTDFNpGSSPTSSMP-----------LVMHLACRLM----RMTPEEALTAATINAAAALGLGET 332

                         90
                 ....*....|....*.
gi 518383840 352 KGSIQVGSDADFTIID 367
Cdd:cd01296  333 VGSLEVGKQADLVILD 348
PRK08044 PRK08044
allantoinase AllB;
7-70 3.94e-03

allantoinase AllB;


Pssm-ID: 169193 [Multi-domain]  Cd Length: 449  Bit Score: 39.07  E-value: 3.94e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 518383840   7 FFTLLRNVKIVAPNDLGCQNILIAGDKVAAIGRNLTIPQgycvEEIDLSGHTLMPGFIDSHVHM 70
Cdd:PRK08044   3 FDLIIKNGTVILENEARVVDIAVKGGKIAAIGQDLGDAK----EVMDASGLVVSPGMVDAHTHI 62
nagA PRK11170
N-acetylglucosamine-6-phosphate deacetylase; Provisional
 27-65 8.04e-03

N-acetylglucosamine-6-phosphate deacetylase; Provisional


Pssm-ID: 183010  Cd Length: 382  Bit Score: 38.03  E-value: 8.04e-03
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 518383840  27 ILIAGDKVAAIGRNLTIPQGycVEEIDLSGHTLMPGFID 65
Cdd:PRK11170  21 VVIADGLIEAVCPVAELPPG--IEQRDLNGAILSPGFID 57
PRK07583 PRK07583
cytosine deaminase;
26-70 9.56e-03

cytosine deaminase;


Pssm-ID: 236062  Cd Length: 438  Bit Score: 38.04  E-value: 9.56e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 518383840  26 NILIAGDKVAAIGRNLTIPQGYcvEEIDLSGHTLMPGFIDSHVHM 70
Cdd:PRK07583  42 DIEIADGKIAAILPAGGAPDEL--PAVDLKGRMVWPCFVDMHTHL 84
PRK08044 PRK08044
allantoinase AllB;
320-373 9.79e-03

allantoinase AllB;


Pssm-ID: 169193 [Multi-domain]  Cd Length: 449  Bit Score: 37.91  E-value: 9.79e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 518383840 320 FRDMVQLEGIEISDAVQIITTNVAKILKIwPQKGSIQVGSDADFTII--DDEFVLQ 373
Cdd:PRK08044 346 FDEAVQKRGMSLPMFGKLMATNAADIFGL-QQKGRIAPGKDADFVFIqpNSSYVLK 400
PRK06380 PRK06380
metal-dependent hydrolase; Provisional
 9-70 9.99e-03

metal-dependent hydrolase; Provisional


Pssm-ID: 180548 [Multi-domain]  Cd Length: 418  Bit Score: 37.94  E-value: 9.99e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 518383840   9 TLLRNVKIVAPND---LGCQNILIAGDKVAAIGRNltipQGYCVEEIDLSGHTLMPGFIDSHVHM 70
Cdd:PRK06380   3 ILIKNAWIVTQNEkreILQGNVYIEGNKIVYVGDV----NEEADYIIDATGKVVMPGLINTHAHV 63
YtcJ COG1574
Predicted amidohydrolase YtcJ [General function prediction only];
272-368 1.00e-02

Predicted amidohydrolase YtcJ [General function prediction only];


Pssm-ID: 441182 [Multi-domain]  Cd Length: 535  Bit Score: 37.86  E-value: 1.00e-02
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518383840 272 AVKKALDAGVPLsqiTMSSDGngsmPIfdqqgntigvgvaSQFSMLEEFRDMV-----------QLEGIEISDAVQIITT 340
Cdd:COG1574  419 PFRSLLDAGAPL---AFGSDA----PV-------------EPLDPLLGIYAAVtrrtpsgrglgPEERLTVEEALRAYTI 478

                         90       100
                 ....*....|....*....|....*...
gi 518383840 341 NVAKILKIWPQKGSIQVGSDADFTIIDD 368
Cdd:COG1574  479 GAAYAAFEEDEKGSLEPGKLADFVVLDR 506
 
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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