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Conserved domains on  [gi|186511115|ref|NP_567027|]
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Amidohydrolase family [Arabidopsis thaliana]

Protein Classification

amidohydrolase( domain architecture ID 11446324)

metal-dependent amidohydrolase similar to Bacillus subtilis YtcJ and Arthrobacter pascens N-substituted formamide deformylase, which catalyzes the hydrolysis of N-substituted formamides

CATH:  3.20.20.140
EC:  3.5.-.-
Gene Ontology:  GO:0046872|GO:0016810
PubMed:  9144792
SCOP:  3000176

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
YtcJ COG1574
Predicted amidohydrolase YtcJ [General function prediction only];
42-575 0e+00

Predicted amidohydrolase YtcJ [General function prediction only];


:

Pssm-ID: 441182 [Multi-domain]  Cd Length: 535  Bit Score: 559.03  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186511115  42 ADLLVTNGTIFTSDSSLPFADSMAIRNGRILKVGSFATLKGFIGDGTMEVNLEGKIVVPGLIDSHVHLISGGLQMAQVGL 121
Cdd:COG1574    8 ADLLLTNGRIYTMDPAQPVAEAVAVRDGRIVAVGSDAEVRALAGPATEVIDLGGKTVLPGFIDAHVHLLGGGLALLGVDL 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186511115 122 RGVSQKDEFCKMVKDAVQNAKEGSWILGGGWNNDFWG-GELPSASWIDEISPRNPVWLIRMDGHMALANSLALKIAGVIS 200
Cdd:COG1574   88 SGARSLDELLARLRAAAAELPPGEWILGRGWDESLWPeGRFPTRADLDAVSPDRPVVLTRVDGHAAWVNSAALELAGITA 167

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186511115 201 LTEDPVGGTIMRMPSGEPTGLLIDAAMELVTPWVKEISVDERREALFRASKYALTRGVTTVIDLGryfpgttdeLSWKDF 280
Cdd:COG1574  168 DTPDPEGGEIERDADGEPTGVLREAAMDLVRAAIPPPTPEELRAALRAALRELASLGITSVHDAG---------LGPDDL 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186511115 281 qDVYLYADSSKKMMIRTCLFFPITT--WSRLLDLKLQKGSVlSEWLYLGGVKAFIDGSLGSNSALFYEEYIDTPNNYGLE 358
Cdd:COG1574  239 -AAYRELAAAGELPLRVVLYLGADDedLEELLALGLRTGYG-DDRLRVGGVKLFADGSLGSRTAALLEPYADDPGNRGLL 316

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186511115 359 VMDPEKLSNFTMAADKSGLQVAIHAIGDKANDMILDMYESVAAANGDRDRRFRIEHAQHLAPGSANRFGQLHIVASVQPD 438
Cdd:COG1574  317 LLDPEELRELVRAADAAGLQVAVHAIGDAAVDEVLDAYEAARAANGRRDRRHRIEHAQLVDPDDLARFAELGVIASMQPT 396

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186511115 439 HLLDDADSVAKKLGSERAvKESYLFQSLLNGNALLALGSDWPVADINPLHSIRTAVKRIPPKwDHAWIPSERISFTDALI 518
Cdd:COG1574  397 HATSDGDWAEDRLGPERA-ARAYPFRSLLDAGAPLAFGSDAPVEPLDPLLGIYAAVTRRTPS-GRGLGPEERLTVEEALR 474

                        490       500       510       520       530       540
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 186511115 519 AQTISAARAAFLDHHLGSLSPGKLADFVILSTnswDEFSKDVSA----SVLATYVGGKQLY 575
Cdd:COG1574  475 AYTIGAAYAAFEEDEKGSLEPGKLADFVVLDR---DPLTVPPEEikdiKVLLTVVGGRVVY 532
 
Name Accession Description Interval E-value
YtcJ COG1574
Predicted amidohydrolase YtcJ [General function prediction only];
42-575 0e+00

Predicted amidohydrolase YtcJ [General function prediction only];


Pssm-ID: 441182 [Multi-domain]  Cd Length: 535  Bit Score: 559.03  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186511115  42 ADLLVTNGTIFTSDSSLPFADSMAIRNGRILKVGSFATLKGFIGDGTMEVNLEGKIVVPGLIDSHVHLISGGLQMAQVGL 121
Cdd:COG1574    8 ADLLLTNGRIYTMDPAQPVAEAVAVRDGRIVAVGSDAEVRALAGPATEVIDLGGKTVLPGFIDAHVHLLGGGLALLGVDL 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186511115 122 RGVSQKDEFCKMVKDAVQNAKEGSWILGGGWNNDFWG-GELPSASWIDEISPRNPVWLIRMDGHMALANSLALKIAGVIS 200
Cdd:COG1574   88 SGARSLDELLARLRAAAAELPPGEWILGRGWDESLWPeGRFPTRADLDAVSPDRPVVLTRVDGHAAWVNSAALELAGITA 167

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186511115 201 LTEDPVGGTIMRMPSGEPTGLLIDAAMELVTPWVKEISVDERREALFRASKYALTRGVTTVIDLGryfpgttdeLSWKDF 280
Cdd:COG1574  168 DTPDPEGGEIERDADGEPTGVLREAAMDLVRAAIPPPTPEELRAALRAALRELASLGITSVHDAG---------LGPDDL 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186511115 281 qDVYLYADSSKKMMIRTCLFFPITT--WSRLLDLKLQKGSVlSEWLYLGGVKAFIDGSLGSNSALFYEEYIDTPNNYGLE 358
Cdd:COG1574  239 -AAYRELAAAGELPLRVVLYLGADDedLEELLALGLRTGYG-DDRLRVGGVKLFADGSLGSRTAALLEPYADDPGNRGLL 316

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186511115 359 VMDPEKLSNFTMAADKSGLQVAIHAIGDKANDMILDMYESVAAANGDRDRRFRIEHAQHLAPGSANRFGQLHIVASVQPD 438
Cdd:COG1574  317 LLDPEELRELVRAADAAGLQVAVHAIGDAAVDEVLDAYEAARAANGRRDRRHRIEHAQLVDPDDLARFAELGVIASMQPT 396

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186511115 439 HLLDDADSVAKKLGSERAvKESYLFQSLLNGNALLALGSDWPVADINPLHSIRTAVKRIPPKwDHAWIPSERISFTDALI 518
Cdd:COG1574  397 HATSDGDWAEDRLGPERA-ARAYPFRSLLDAGAPLAFGSDAPVEPLDPLLGIYAAVTRRTPS-GRGLGPEERLTVEEALR 474

                        490       500       510       520       530       540
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 186511115 519 AQTISAARAAFLDHHLGSLSPGKLADFVILSTnswDEFSKDVSA----SVLATYVGGKQLY 575
Cdd:COG1574  475 AYTIGAAYAAFEEDEKGSLEPGKLADFVVLDR---DPLTVPPEEikdiKVLLTVVGGRVVY 532
YtcJ_like cd01300
YtcJ_like metal dependent amidohydrolases. YtcJ is a Bacillus subtilis ORF of unknown function. ...
 64-547 0e+00

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: 536.89  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186511115  64 MAIRNGRILKVGSFATLKGFIGDGTMEVNLEGKIVVPGLIDSHVHLISGGLQMAQVGLRGVSQKDEFCKMVKDAVQNAKE 143
Cdd:cd01300    2 VAVRDGRIVAVGSDAEAKALKGPATEVIDLKGKTVLPGFIDSHSHLLLGGLSLLWLDLSGVTSKEEALARIREDAAAAPP 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186511115 144 GSWILGGGWNNDFWGG-ELPSASWIDEISPRNPVWLIRMDGHMALANSLALKIAGVISLTEDPVGGTIMRMPSGEPTGLL 222
Cdd:cd01300   82 GEWILGFGWDESLLGEgRYPTRAELDAVSPDRPVLLLRRDGHSAWVNSAALRLAGITRDTPDPPGGEIVRDADGEPTGVL 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186511115 223 IDAAMELVTPWVKEISVDERREALFRASKYALTRGVTTVIDLGRYFPGttdelswkDFQDVYLYADSSK-KMMIRTCLFF 301
Cdd:cd01300  162 VEAAAALVLEAVPPPTPEERRAALRAAARELASLGVTTVHDAGGGAAD--------DIEAYRRLAAAGElTLRVRVALYV 233

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186511115 302 PITTWSRLLDLKLQKGSVLSEWLYLGGVKAFIDGSLGSNSALFYEEYIDTPNNYGLEVMDPEKLSNFTMAADKSGLQVAI 381
Cdd:cd01300  234 SPLAEDLLEELGARKNGAGDDRLRLGGVKLFADGSLGSRTAALSEPYLDSPGTGGLLLISPEELEELVRAADEAGLQVAI 313

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186511115 382 HAIGDKANDMILDMYESVAAANGDRDRRFRIEHAQHLAPGSANRFGQLHIVASVQPDHLLDDADSVAKKLGSERAVKESY 461
Cdd:cd01300  314 HAIGDRAVDTVLDALEAALKDNPRADHRHRIEHAQLVSPDDIPRFAKLGVIASVQPNHLYSDGDAAEDRRLGEERAKRSY 393

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186511115 462 LFQSLLNGNALLALGSDWPVADINPLHSIRTAVKRIPPKWDHAWIPSERISFTDALIAQTISAARAAFLDHHLGSLSPGK 541
Cdd:cd01300  394 PFRSLLDAGVPVALGSDAPVAPPDPLLGIWAAVTRKTPGGGVLGNPEERLSLEEALRAYTIGAAYAIGEEDEKGSLEPGK 473


                 ....*.
gi 186511115 542 LADFVI 547
Cdd:cd01300  474 LADFVV 479
Amidohydro_3 pfam07969
Amidohydrolase family;
90-575 6.79e-83

Amidohydrolase family;


Pssm-ID: 400360 [Multi-domain]  Cd Length: 464  Bit Score: 266.70  E-value: 6.79e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186511115   90 EVNLEGKIVVPGLIDSHVHLISGGLQMAQVGLRGVSQKDEfckmVKDAVQNAKEGSWILGGGWN--NDFWGGELPSASWI 167
Cdd:pfam07969   2 VIDAKGRLVLPGFVDPHTHLDGGGLNLRELRLPDVLPNAV----VKGQAGRTPKGRWLVGEGWDeaQFAETRFPYALADL 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186511115  168 DEISPRNPVWLIRMDGHMALANSLALKIAGVISLTEDPVGGTIMRMPSGE-PTGLLIDAAMELVTPWVKEisvdERREAL 246
Cdd:pfam07969  78 DEVAPDGPVLLRALHTHAAVANSAALDLAGITKATEDPPGGEIARDANGEgLTGLLREGAYALPPLLARE----AEAAAV 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186511115  247 FRASKYALTRGVTTVIDLGRYfpgttdelsWKDFQDVYLYADSSKKMMIrtclffpittwSRLLDLKLQKGSVLS-EWLY 325
Cdd:pfam07969 154 AAALAALPGFGITSVDGGGGN---------VHSLDDYEPLRELTAAEKL-----------KELLDAPERLGLPHSiYELR 213

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186511115  326 LGGVKAFIDGSLGSNSALFYEEYIDTPNNyGLEVMDPEKLSNFTMAADKSGLQVAIHAIGDKANDMILDMYESVAAANGD 405
Cdd:pfam07969 214 IGAMKLFADGVLGSRTAALTEPYFDAPGT-GWPDFEDEALAELVAAARERGLDVAIHAIGDATIDTALDAFEAVAEKLGN 292

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186511115  406 RDRRfRIEHAQHLAPGS---ANRFGQLHIVASVQPDHLLDDADSVAKKLGSERAvKESYLFQSLLNGNALLALGSDWPVA 482
Cdd:pfam07969 293 QGRV-RIEHAQGVVPYTysqIERVAALGGAAGVQPVFDPLWGDWLQDRLGAERA-RGLTPVKELLNAGVKVALGSDAPVG 370

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186511115  483 DINPLHSIRTAVKRIPPKWDHAWIPSERISFTDALIAQTISAARAAFLDHHLGSLSPGKLADFVILSTNSWD-EFSKDVS 561
Cdd:pfam07969 371 PFDPWPRIGAAVMRQTAGGGEVLGPDEELSLEEALALYTSGPAKALGLEDRKGTLGVGKDADLVVLDDDPLTvDPPAIAD 450

                         490
                  ....*....|....
gi 186511115  562 ASVLATYVGGKQLY 575
Cdd:pfam07969 451 IRVRLTVVDGRVVY 464
PRK09228 PRK09228
guanine deaminase; Provisional
 64-108 9.30e-09

guanine deaminase; Provisional


Pssm-ID: 236419 [Multi-domain]  Cd Length: 433  Bit Score: 57.89  E-value: 9.30e-09
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 186511115  64 MAIRNGRILKVGSFATLKGFIGDGTMEVNLEGKIVVPGLIDSHVH 108
Cdd:PRK09228  34 LLVEDGRIVAAGPYAELRAQLPADAEVTDYRGKLILPGFIDTHIH 78
isoAsp_dipep TIGR01975
isoaspartyl dipeptidase IadA; The L-isoaspartyl derivative of Asp arises non-enzymatically ...
 64-113 8.41e-08

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: 54.79  E-value: 8.41e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 186511115   64 MAIRNGRILKVGSFATLKGFIGDGTMEVNLEGKIVVPGLIDSHVHLISGG 113
Cdd:TIGR01975  20 ILIANDKIIAIADEIPSTKDFVPNCVVVGLEGMIAVPGFIDQHVHIIGGG 69
 
Name Accession Description Interval E-value
YtcJ COG1574
Predicted amidohydrolase YtcJ [General function prediction only];
42-575 0e+00

Predicted amidohydrolase YtcJ [General function prediction only];


Pssm-ID: 441182 [Multi-domain]  Cd Length: 535  Bit Score: 559.03  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186511115  42 ADLLVTNGTIFTSDSSLPFADSMAIRNGRILKVGSFATLKGFIGDGTMEVNLEGKIVVPGLIDSHVHLISGGLQMAQVGL 121
Cdd:COG1574    8 ADLLLTNGRIYTMDPAQPVAEAVAVRDGRIVAVGSDAEVRALAGPATEVIDLGGKTVLPGFIDAHVHLLGGGLALLGVDL 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186511115 122 RGVSQKDEFCKMVKDAVQNAKEGSWILGGGWNNDFWG-GELPSASWIDEISPRNPVWLIRMDGHMALANSLALKIAGVIS 200
Cdd:COG1574   88 SGARSLDELLARLRAAAAELPPGEWILGRGWDESLWPeGRFPTRADLDAVSPDRPVVLTRVDGHAAWVNSAALELAGITA 167

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186511115 201 LTEDPVGGTIMRMPSGEPTGLLIDAAMELVTPWVKEISVDERREALFRASKYALTRGVTTVIDLGryfpgttdeLSWKDF 280
Cdd:COG1574  168 DTPDPEGGEIERDADGEPTGVLREAAMDLVRAAIPPPTPEELRAALRAALRELASLGITSVHDAG---------LGPDDL 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186511115 281 qDVYLYADSSKKMMIRTCLFFPITT--WSRLLDLKLQKGSVlSEWLYLGGVKAFIDGSLGSNSALFYEEYIDTPNNYGLE 358
Cdd:COG1574  239 -AAYRELAAAGELPLRVVLYLGADDedLEELLALGLRTGYG-DDRLRVGGVKLFADGSLGSRTAALLEPYADDPGNRGLL 316

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186511115 359 VMDPEKLSNFTMAADKSGLQVAIHAIGDKANDMILDMYESVAAANGDRDRRFRIEHAQHLAPGSANRFGQLHIVASVQPD 438
Cdd:COG1574  317 LLDPEELRELVRAADAAGLQVAVHAIGDAAVDEVLDAYEAARAANGRRDRRHRIEHAQLVDPDDLARFAELGVIASMQPT 396

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186511115 439 HLLDDADSVAKKLGSERAvKESYLFQSLLNGNALLALGSDWPVADINPLHSIRTAVKRIPPKwDHAWIPSERISFTDALI 518
Cdd:COG1574  397 HATSDGDWAEDRLGPERA-ARAYPFRSLLDAGAPLAFGSDAPVEPLDPLLGIYAAVTRRTPS-GRGLGPEERLTVEEALR 474

                        490       500       510       520       530       540
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 186511115 519 AQTISAARAAFLDHHLGSLSPGKLADFVILSTnswDEFSKDVSA----SVLATYVGGKQLY 575
Cdd:COG1574  475 AYTIGAAYAAFEEDEKGSLEPGKLADFVVLDR---DPLTVPPEEikdiKVLLTVVGGRVVY 532
YtcJ_like cd01300
YtcJ_like metal dependent amidohydrolases. YtcJ is a Bacillus subtilis ORF of unknown function. ...
 64-547 0e+00

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: 536.89  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186511115  64 MAIRNGRILKVGSFATLKGFIGDGTMEVNLEGKIVVPGLIDSHVHLISGGLQMAQVGLRGVSQKDEFCKMVKDAVQNAKE 143
Cdd:cd01300    2 VAVRDGRIVAVGSDAEAKALKGPATEVIDLKGKTVLPGFIDSHSHLLLGGLSLLWLDLSGVTSKEEALARIREDAAAAPP 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186511115 144 GSWILGGGWNNDFWGG-ELPSASWIDEISPRNPVWLIRMDGHMALANSLALKIAGVISLTEDPVGGTIMRMPSGEPTGLL 222
Cdd:cd01300   82 GEWILGFGWDESLLGEgRYPTRAELDAVSPDRPVLLLRRDGHSAWVNSAALRLAGITRDTPDPPGGEIVRDADGEPTGVL 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186511115 223 IDAAMELVTPWVKEISVDERREALFRASKYALTRGVTTVIDLGRYFPGttdelswkDFQDVYLYADSSK-KMMIRTCLFF 301
Cdd:cd01300  162 VEAAAALVLEAVPPPTPEERRAALRAAARELASLGVTTVHDAGGGAAD--------DIEAYRRLAAAGElTLRVRVALYV 233

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186511115 302 PITTWSRLLDLKLQKGSVLSEWLYLGGVKAFIDGSLGSNSALFYEEYIDTPNNYGLEVMDPEKLSNFTMAADKSGLQVAI 381
Cdd:cd01300  234 SPLAEDLLEELGARKNGAGDDRLRLGGVKLFADGSLGSRTAALSEPYLDSPGTGGLLLISPEELEELVRAADEAGLQVAI 313

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186511115 382 HAIGDKANDMILDMYESVAAANGDRDRRFRIEHAQHLAPGSANRFGQLHIVASVQPDHLLDDADSVAKKLGSERAVKESY 461
Cdd:cd01300  314 HAIGDRAVDTVLDALEAALKDNPRADHRHRIEHAQLVSPDDIPRFAKLGVIASVQPNHLYSDGDAAEDRRLGEERAKRSY 393

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186511115 462 LFQSLLNGNALLALGSDWPVADINPLHSIRTAVKRIPPKWDHAWIPSERISFTDALIAQTISAARAAFLDHHLGSLSPGK 541
Cdd:cd01300  394 PFRSLLDAGVPVALGSDAPVAPPDPLLGIWAAVTRKTPGGGVLGNPEERLSLEEALRAYTIGAAYAIGEEDEKGSLEPGK 473


                 ....*.
gi 186511115 542 LADFVI 547
Cdd:cd01300  474 LADFVV 479
Amidohydro_3 pfam07969
Amidohydrolase family;
90-575 6.79e-83

Amidohydrolase family;


Pssm-ID: 400360 [Multi-domain]  Cd Length: 464  Bit Score: 266.70  E-value: 6.79e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186511115   90 EVNLEGKIVVPGLIDSHVHLISGGLQMAQVGLRGVSQKDEfckmVKDAVQNAKEGSWILGGGWN--NDFWGGELPSASWI 167
Cdd:pfam07969   2 VIDAKGRLVLPGFVDPHTHLDGGGLNLRELRLPDVLPNAV----VKGQAGRTPKGRWLVGEGWDeaQFAETRFPYALADL 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186511115  168 DEISPRNPVWLIRMDGHMALANSLALKIAGVISLTEDPVGGTIMRMPSGE-PTGLLIDAAMELVTPWVKEisvdERREAL 246
Cdd:pfam07969  78 DEVAPDGPVLLRALHTHAAVANSAALDLAGITKATEDPPGGEIARDANGEgLTGLLREGAYALPPLLARE----AEAAAV 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186511115  247 FRASKYALTRGVTTVIDLGRYfpgttdelsWKDFQDVYLYADSSKKMMIrtclffpittwSRLLDLKLQKGSVLS-EWLY 325
Cdd:pfam07969 154 AAALAALPGFGITSVDGGGGN---------VHSLDDYEPLRELTAAEKL-----------KELLDAPERLGLPHSiYELR 213

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186511115  326 LGGVKAFIDGSLGSNSALFYEEYIDTPNNyGLEVMDPEKLSNFTMAADKSGLQVAIHAIGDKANDMILDMYESVAAANGD 405
Cdd:pfam07969 214 IGAMKLFADGVLGSRTAALTEPYFDAPGT-GWPDFEDEALAELVAAARERGLDVAIHAIGDATIDTALDAFEAVAEKLGN 292

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186511115  406 RDRRfRIEHAQHLAPGS---ANRFGQLHIVASVQPDHLLDDADSVAKKLGSERAvKESYLFQSLLNGNALLALGSDWPVA 482
Cdd:pfam07969 293 QGRV-RIEHAQGVVPYTysqIERVAALGGAAGVQPVFDPLWGDWLQDRLGAERA-RGLTPVKELLNAGVKVALGSDAPVG 370

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186511115  483 DINPLHSIRTAVKRIPPKWDHAWIPSERISFTDALIAQTISAARAAFLDHHLGSLSPGKLADFVILSTNSWD-EFSKDVS 561
Cdd:pfam07969 371 PFDPWPRIGAAVMRQTAGGGEVLGPDEELSLEEALALYTSGPAKALGLEDRKGTLGVGKDADLVVLDDDPLTvDPPAIAD 450

                         490
                  ....*....|....
gi 186511115  562 ASVLATYVGGKQLY 575
Cdd:pfam07969 451 IRVRLTVVDGRVVY 464
HutI COG1228
Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport ...
 43-575 4.70e-13

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


Pssm-ID: 440841 [Multi-domain]  Cd Length: 386  Bit Score: 71.15  E-value: 4.70e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186511115  43 DLLVTNGTIFTSDSSLPFAD-SMAIRNGRILKVGSFATLKgfIGDGTMEVNLEGKIVVPGLIDSHVHLIsgglqmaqvgl 121
Cdd:COG1228    9 TLLITNATLVDGTGGGVIENgTVLVEDGKIAAVGPAADLA--VPAGAEVIDATGKTVLPGLIDAHTHLG----------- 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186511115 122 rgvsqkdefckmvkdavqnakegswilgggwnndFWGGELPSASWIDEISPRNPVwLIRMDGHMALAnsLAlkiAGVisl 201
Cdd:COG1228   76 ----------------------------------LGGGRAVEFEAGGGITPTVDL-VNPADKRLRRA--LA---AGV--- 112

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186511115 202 tedpvggTIMRMPSGEPTGLlidaamelvtpwvkeisvderrealfrasKYALTRGVTTVIDLGRYFPGTTdelswkdFQ 281
Cdd:COG1228  113 -------TTVRDLPGGPLGL-----------------------------RDAIIAGESKLLPGPRVLAAGP-------AL 149

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186511115 282 DVYLYADSSKKMMIRtclffpittwsRLLDLKLQKGSvlsewlylggvkafidgslgsnsalfyeEYIDTPNNYGLEVMD 361
Cdd:COG1228  150 SLTGGAHARGPEEAR-----------AALRELLAEGA----------------------------DYIKVFAEGGAPDFS 190

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186511115 362 PEKLSNFTMAADKSGLQVAIHAIGDKANDMildmyesvAAANGdrdrrFR-IEHAQHLAPGSANRFGQLHIVAsVQPDHL 440
Cdd:COG1228  191 LEELRAILEAAHALGLPVAAHAHQADDIRL--------AVEAG-----VDsIEHGTYLDDEVADLLAEAGTVV-LVPTLS 256

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186511115 441 LDDADSVAKKLGSERAVKESY-----------------LFQSllngnallalgsDWPVADI---NPLHSIRTAVKrippk 500
Cdd:COG1228  257 LFLALLEGAAAPVAAKARKVReaalanarrlhdagvpvALGT------------DAGVGVPpgrSLHRELALAVE----- 319

                        490       500       510       520       530       540       550
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 186511115 501 wdhawipsERISFTDALIAQTISAARAAFLDHHLGSLSPGKLADFVILSTNSWDEFSkdVSASVLATYVGGKQLY 575
Cdd:COG1228  320 --------AGLTPEEALRAATINAAKALGLDDDVGSLEPGKLADLVLLDGDPLEDIA--YLEDVRAVMKDGRVVD 384
SsnA COG0402
Cytosine/adenosine deaminase or related metal-dependent hydrolase [Nucleotide transport and ...
 43-130 1.15e-10

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: 63.69  E-value: 1.15e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186511115  43 DLLVTNGTIFTSDSSLPFAD--SMAIRNGRILKVGSFATLKGFIgDGTMEVNLEGKIVVPGLIDSHVHLisgglqmAQVG 120
Cdd:COG0402    1 DLLIRGAWVLTMDPAGGVLEdgAVLVEDGRIAAVGPGAELPARY-PAAEVIDAGGKLVLPGLVNTHTHL-------PQTL 72

                         90
                 ....*....|
gi 186511115 121 LRGVSQKDEF 130
Cdd:COG0402   73 LRGLADDLPL 82
AdeC COG1001
Adenine deaminase [Nucleotide transport and metabolism];
42-108 2.45e-10

Adenine deaminase [Nucleotide transport and metabolism];


Pssm-ID: 440625 [Multi-domain]  Cd Length: 559  Bit Score: 63.20  E-value: 2.45e-10
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 186511115  42 ADLLVTNGTIFTSDSSLPFADSMAIRNGRILKVGSFatlkgfIGDGTMEVNLEGKIVVPGLIDSHVH 108
Cdd:COG1001    5 ADLVIKNGRLVNVFTGEILEGDIAIAGGRIAGVGDY------IGEATEVIDAAGRYLVPGFIDGHVH 65
D-aminoacylase cd01297
D-aminoacylases (N-acyl-D-Amino acid amidohydrolases) catalyze the hydrolysis of ...
 43-108 8.63e-10

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: 60.77  E-value: 8.63e-10
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 186511115  43 DLLVTNGTIFTSDSSLPFADSMAIRNGRILKVGsfatlKGFIGDGTMEVNLEGKIVVPGLIDSHVH 108
Cdd:cd01297    1 DLVIRNGTVVDGTGAPPFTADVGIRDGRIAAIG-----PILSTSAREVIDAAGLVVAPGFIDVHTH 61
AllB COG0044
Dihydroorotase or related cyclic amidohydrolase [Nucleotide transport and metabolism]; ...
 45-109 2.18e-09

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: 59.72  E-value: 2.18e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 186511115  45 LVTNGTIFTSDSSLPfADsMAIRNGRILKVGSFATLkgfiGDGTMEVNLEGKIVVPGLIDSHVHL 109
Cdd:COG0044    1 LIKNGRVVDPGGLER-AD-VLIEDGRIAAIGPDLAA----PEAAEVIDATGLLVLPGLIDLHVHL 59
metallo-dependent_hydrolases cd01292
Superfamily of metallo-dependent hydrolases (also called amidohydrolase superfamily) is a ...
 233-527 5.94e-09

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: 57.34  E-value: 5.94e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186511115 233 WVKEISVDERREALFRASKYALTRGVTTVIDLGRYFPGTTDelsWKDFQDVYLYADSSKKMMIRTCLFFPITTWsrlldl 312
Cdd:cd01292   24 EAEELSPEDLYEDTLRALEALLAGGVTTVVDMGSTPPPTTT---KAAIEAVAEAARASAGIRVVLGLGIPGVPA------ 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186511115 313 klqkgSVLSEWLYLGGVKAFIDGSLGSNSALFYEEYIDTPNNyglevmdPEKLSNFTMAADKSGLQVAIHAIGDKANDMi 392
Cdd:cd01292   95 -----AVDEDAEALLLELLRRGLELGAVGLKLAGPYTATGLS-------DESLRRVLEEARKLGLPVVIHAGELPDPTR- 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186511115 393 ldMYESVAAANGDrDRRFRIEHAQHLAPGSANRFGQL--HIVASVQPDHLLDDADSVAKKLGSERAVKESYLFqsllngn 470
Cdd:cd01292  162 --ALEDLVALLRL-GGRVVIGHVSHLDPELLELLKEAgvSLEVCPLSNYLLGRDGEGAEALRRLLELGIRVTL------- 231

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 186511115 471 allalGSDWPVA--DINPLHSIRTAVKRIPPKWDHAwipserisftDALIAQTISAARA 527
Cdd:cd01292  232 -----GTDGPPHplGTDLLALLRLLLKVLRLGLSLE----------EALRLATINPARA 275
Imidazolone-5PH cd01296
Imidazolonepropionase/imidazolone-5-propionate hydrolase (Imidazolone-5PH) catalyzes the third ...
 65-113 5.99e-09

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: 58.04  E-value: 5.99e-09
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 186511115  65 AIRNGRILKVGSFATLKGFIGDGTMEVNLEGKIVVPGLIDSHVHLISGG 113
Cdd:cd01296    2 AIRDGRIAAVGPAASLPAPGPAAAEEIDAGGRAVTPGLVDCHTHLVFAG 50
D-HYD cd01314
D-hydantoinases (D-HYD) also called dihydropyrimidases (DHPase) and related proteins; DHPases ...
 44-117 7.71e-09

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: 58.00  E-value: 7.71e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 186511115  44 LLVTNGTIFTSDSSlpFADSMAIRNGRILKVGsfATLKGfiGDGTMEVNLEGKIVVPGLIDSHVHL--ISGGLQMA 117
Cdd:cd01314    1 LIIKNGTIVTADGS--FKADILIEDGKIVAIG--PNLEA--PGGVEVIDATGKYVLPGGIDPHTHLelPFMGTVTA 70
PRK09228 PRK09228
guanine deaminase; Provisional
 64-108 9.30e-09

guanine deaminase; Provisional


Pssm-ID: 236419 [Multi-domain]  Cd Length: 433  Bit Score: 57.89  E-value: 9.30e-09
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 186511115  64 MAIRNGRILKVGSFATLKGFIGDGTMEVNLEGKIVVPGLIDSHVH 108
Cdd:PRK09228  34 LLVEDGRIVAAGPYAELRAQLPADAEVTDYRGKLILPGFIDTHIH 78
COG3964 COG3964
Predicted amidohydrolase [General function prediction only];
43-108 1.70e-08

Predicted amidohydrolase [General function prediction only];


Pssm-ID: 443164 [Multi-domain]  Cd Length: 376  Bit Score: 56.71  E-value: 1.70e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 186511115  43 DLLVTNGTIFTSDSSLPFADSMAIRNGRILKVGSFATlkgfIGDGTMEVNLEGKIVVPGLIDSHVH 108
Cdd:COG3964    1 DLLIKGGRVIDPANGIDGVMDIAIKDGKIAAVAKDID----AAEAKKVIDASGLYVTPGLIDLHTH 62
Isoaspartyl-dipeptidase cd01308
Isoaspartyl dipeptidase hydrolyzes the beta-L-isoaspartyl linkages in dipeptides, as part of ...
 64-113 3.37e-08

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: 55.86  E-value: 3.37e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 186511115  64 MAIRNGRILKVGSfaTLKGFIGDGTMEVNLEGKIVVPGLIDSHVHLISGG 113
Cdd:cd01308   20 ILIAGGKILAIED--QLNLPGYENVTVVDLHGKILVPGFIDQHVHIIGGG 67
PRK08323 PRK08323
phenylhydantoinase; Validated
 43-117 5.17e-08

phenylhydantoinase; Validated


Pssm-ID: 236240 [Multi-domain]  Cd Length: 459  Bit Score: 55.56  E-value: 5.17e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 186511115  43 DLLVTNGTIFTSDSSLPfADsMAIRNGRILKVGSfatlkgfiGDGTMEVNLEGKIVVPGLIDSHVHL--ISGGLQMA 117
Cdd:PRK08323   2 STLIKNGTVVTADDTYK-AD-VLIEDGKIAAIGA--------NLGDEVIDATGKYVMPGGIDPHTHMemPFGGTVSS 68
isoAsp_dipep TIGR01975
isoaspartyl dipeptidase IadA; The L-isoaspartyl derivative of Asp arises non-enzymatically ...
 64-113 8.41e-08

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: 54.79  E-value: 8.41e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 186511115   64 MAIRNGRILKVGSFATLKGFIGDGTMEVNLEGKIVVPGLIDSHVHLISGG 113
Cdd:TIGR01975  20 ILIANDKIIAIADEIPSTKDFVPNCVVVGLEGMIAVPGFIDQHVHIIGGG 69
PRK07203 PRK07203
putative aminohydrolase SsnA;
44-140 1.28e-07

putative aminohydrolase SsnA;


Pssm-ID: 235963 [Multi-domain]  Cd Length: 442  Bit Score: 54.17  E-value: 1.28e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186511115  44 LLVTNGTIFTSDSSLPFADSM--AIRNGRILKVGSFATLKGFIGDGTMeVNLEGKIVVPGLIDSHVHLISGglqMAqvgl 121
Cdd:PRK07203   2 LLIGNGTAITRDPAKPVIEDGaiAIEGNVIVEIGTTDELKAKYPDAEF-IDAKGKLIMPGLINSHNHIYSG---LA---- 73

                         90
                 ....*....|....*....
gi 186511115 122 RGVSQKDEFCKMVKDAVQN 140
Cdd:PRK07203  74 RGMMANIPPPPDFISILKN 92
PRK13404 PRK13404
dihydropyrimidinase; Provisional
 43-117 1.64e-07

dihydropyrimidinase; Provisional


Pssm-ID: 184033 [Multi-domain]  Cd Length: 477  Bit Score: 53.93  E-value: 1.64e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 186511115  43 DLLVTNGTIFTSDSSlpFADSMAIRNGRIlkvgsfATLKGFIGDGTMEVNLEGKIVVPGLIDSHVHL---ISGGLQMA 117
Cdd:PRK13404   5 DLVIRGGTVVTATDT--FQADIGIRGGRI------AALGEGLGPGAREIDATGRLVLPGGVDSHCHIdqpSGDGIMMA 74
Amidohydro_1 pfam01979
Amidohydrolase family; This family of enzymes are a a large metal dependent hydrolase ...
 371-574 1.73e-07

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: 53.27  E-value: 1.73e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186511115  371 AADKSGLQVAIHAIGDKA----------NDMILDMYESVAAANGD-RDRRFRIEHAQHLAPGSANRFGQLHIVASVqpDH 439
Cdd:pfam01979 135 EAKKYGLPVAIHALETKGevedaiaafgGGIEHGTHLEVAESGGLlDIIKLILAHGVHLSPTEANLLAEHLKGAGV--AH 212

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186511115  440 LLDDADSVAKKLGSERAVKESYLFQSLLngnallalgSDWPVADINP--LHSIRTAVKRippkwdhAWIPSERISFTDAL 517
Cdd:pfam01979 213 CPFSNSKLRSGRIALRKALEDGVKVGLG---------TDGAGSGNSLnmLEELRLALEL-------QFDPEGGLSPLEAL 276

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 186511115  518 IAQTISAARAAFLDHHLGSLSPGKLADFVILSTNSWDEFSKD-VSASVLATYVGGKQL 574
Cdd:pfam01979 277 RMATINPAKALGLDDKVGSIEVGKDADLVVVDLDPLAAFFGLkPDGNVKKVIVKGKIV 334
ATZ_TRZ_like cd01298
TRZ/ATZ family contains enzymes from the atrazine degradation pathway and related hydrolases. ...
 44-124 2.34e-07

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: 53.36  E-value: 2.34e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186511115  44 LLVTNGTIFTSDSSLPFADS-MAIRNGRILKVGSFATLKGFIGDgtMEVNLEGKIVVPGLIDSHVHLisgglqmAQVGLR 122
Cdd:cd01298    1 ILIRNGTIVTTDPRRVLEDGdVLVEDGRIVAVGPALPLPAYPAD--EVIDAKGKVVMPGLVNTHTHL-------AMTLLR 71


                 ..
gi 186511115 123 GV 124
Cdd:cd01298   72 GL 73
ureC PRK13308
urease subunit alpha; Reviewed
 33-114 6.58e-07

urease subunit alpha; Reviewed


Pssm-ID: 183965 [Multi-domain]  Cd Length: 569  Bit Score: 52.02  E-value: 6.58e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186511115  33 SLTPPAGIVaDLLVTNGTIFTSDSSLPFADsMAIRNGRIL---KVGSFATLKG-----FIGDGTMEVNLEGKIVVPGLID 104
Cdd:PRK13308  60 GVTSADGAL-DFVLCNVTVIDPVLGIVKGD-IGIRDGRIVgigKAGNPDIMDGvdprlVVGPGTDVRPAEGLIATPGAID 137

                         90
                 ....*....|
gi 186511115 105 SHVHLISGGL 114
Cdd:PRK13308 138 VHVHFDSAQL 147
PRK09237 PRK09237
amidohydrolase/deacetylase family metallohydrolase;
65-108 4.61e-06

amidohydrolase/deacetylase family metallohydrolase;


Pssm-ID: 236423 [Multi-domain]  Cd Length: 380  Bit Score: 49.08  E-value: 4.61e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 186511115  65 AIRNGRILKVGsfATLKGfiGDGTMEVNLEGKIVVPGLIDSHVH 108
Cdd:PRK09237  22 AIEDGKIAAVA--GDIDG--SQAKKVIDLSGLYVSPGWIDLHVH 61
PRK02382 PRK02382
dihydroorotase; Provisional
 43-108 4.90e-06

dihydroorotase; Provisional


Pssm-ID: 179417 [Multi-domain]  Cd Length: 443  Bit Score: 49.27  E-value: 4.90e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 186511115  43 DLLVTNGTIFTSDSSLPfaDSMAIRNGRILKVGsfATLKGFIGDgtMEVNLEGKIVVPGLIDSHVH 108
Cdd:PRK02382   3 DALLKDGRVYYNNSLQP--RDVRIDGGKITAVG--KDLDGSSSE--EVIDARGMLLLPGGIDVHVH 62
NagA COG1820
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism];
45-108 6.71e-06

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


Pssm-ID: 441425 [Multi-domain]  Cd Length: 373  Bit Score: 48.56  E-value: 6.71e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 186511115  45 LVTNGTIFTSDSSLPFADsMAIRNGRILKVGSFATLkgfigdGTMEVNLEGKIVVPGLIDSHVH 108
Cdd:COG1820    1 AITNARIFTGDGVLEDGA-LLIEDGRIAAIGPGAEP------DAEVIDLGGGYLAPGFIDLHVH 57
ureC PRK13207
urease subunit alpha; Reviewed
 41-111 8.07e-06

urease subunit alpha; Reviewed


Pssm-ID: 237305 [Multi-domain]  Cd Length: 568  Bit Score: 48.63  E-value: 8.07e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 186511115  41 VADLLVTNGTIFtsDSSLPFADSMAIRNGRILKVGSfA----TLKGF---IGDGTMEVNLEGKIVVPGLIDSHVHLIS 111
Cdd:PRK13207  66 AVDTVITNALIL--DHWGIVKADIGIKDGRIVAIGK-AgnpdIQDGVdiiIGPGTEVIAGEGLIVTAGGIDTHIHFIC 140
Met_dep_hydrolase_C cd01309
Metallo-dependent hydrolases, subgroup C is part of the superfamily of metallo-dependent ...
 512-575 1.00e-05

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: 48.08  E-value: 1.00e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 186511115 512 SFTDALIAQTISAARAAFLDHHLGSLSPGKLADFVIlstnsWDEFSKDVSASVLATYVGGKQLY 575
Cdd:cd01309  301 SYEEALKAITINPAKILGIEDRVGSLEPGKDADLVV-----WNGDPLEPTSKPEQVYIDGRLVY 359
NagA COG1820
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism];
511-572 1.83e-05

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


Pssm-ID: 441425 [Multi-domain]  Cd Length: 373  Bit Score: 47.02  E-value: 1.83e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 186511115 511 ISFTDALIAQTISAARAAFLDHHLGSLSPGKLADFVILStnswDEFskdvsaSVLATYVGGK 572
Cdd:COG1820  322 LPLEEAVRMASLNPARALGLDDRKGSIAPGKDADLVVLD----DDL------NVRATWVGGE 373
PRK06189 PRK06189
allantoinase; Provisional
 43-109 2.00e-05

allantoinase; Provisional


Pssm-ID: 235732 [Multi-domain]  Cd Length: 451  Bit Score: 47.39  E-value: 2.00e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 186511115  43 DLLVTNGTIFTSDSSLPfADsMAIRNGRILKVGSfatlkGFIGDGTMEVNLEGKIVVPGLIDSHVHL 109
Cdd:PRK06189   4 DLIIRGGKVVTPEGVYR-AD-IGIKNGKIAEIAP-----EISSPAREIIDADGLYVFPGMIDVHVHF 63
PRK08204 PRK08204
hypothetical protein; Provisional
 501-552 2.30e-05

hypothetical protein; Provisional


Pssm-ID: 181288 [Multi-domain]  Cd Length: 449  Bit Score: 46.92  E-value: 2.30e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 186511115 501 WDHAWIPSERISFT--DALIAQTISAARAAFLDHHLGSLSPGKLADFVILSTNS 552
Cdd:PRK08204 330 LREGGMPPPRLTLTarQVLEWATIEGARALGLEDRIGSLTPGKQADLVLIDATD 383
L-HYD_ALN cd01315
L-Hydantoinases (L-HYDs) and Allantoinase (ALN); L-Hydantoinases are a member of the ...
 43-113 3.69e-05

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: 46.51  E-value: 3.69e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 186511115  43 DLLVTNGTIFTSDSSLPfADsMAIRNGRILKVGSFATlkgfIGDGTMEVNLEGKIVVPGLIDSHVHLISGG 113
Cdd:cd01315    1 DLVIKNGRVVTPDGVRE-AD-IAVKGGKIAAIGPDIA----NTEAEEVIDAGGLVVMPGLIDTHVHINEPG 65
Urease_alpha cd00375
Urease alpha-subunit; Urease is a nickel-dependent metalloenzyme that catalyzes the hydrolysis ...
 41-111 5.28e-05

Urease alpha-subunit; Urease is a nickel-dependent metalloenzyme that catalyzes the hydrolysis of urea to form ammonia and carbon dioxide. Nickel-dependent ureases are found in bacteria, fungi and plants. Their primary role is to allow the use of external and internally generated urea as a nitrogen source. The enzyme consists of 3 subunits, alpha, beta and gamma, which can be fused and present on a single protein chain and which in turn forms multimers, mainly trimers. The large alpha subunit is the catalytic domain containing an active site with a bi-nickel center complexed by a carbamylated lysine. The beta and gamma subunits play a role in subunit association to form the higher order trimers.


Pssm-ID: 238221 [Multi-domain]  Cd Length: 567  Bit Score: 46.17  E-value: 5.28e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 186511115  41 VADLLVTNGTIFtsDSSLPFADSMAIRNGRIL---KVGSFATLKG-----FIGDGTMEVNLEGKIVVPGLIDSHVHLIS 111
Cdd:cd00375   64 VLDLVITNALII--DYTGIYKADIGIKDGRIVaigKAGNPDIMDGvtpnmIVGPSTEVIAGEGKIVTAGGIDTHVHFIC 140
PRK08204 PRK08204
hypothetical protein; Provisional
 45-124 7.06e-05

hypothetical protein; Provisional


Pssm-ID: 181288 [Multi-domain]  Cd Length: 449  Bit Score: 45.38  E-value: 7.06e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186511115  45 LVTNGTIFTSDSSLPFADS--MAIRNGRILKVGSFATlkgfiGDGTMEVNLEGKIVVPGLIDSHVHLisgglqmAQVGLR 122
Cdd:PRK08204   5 LIRGGTVLTMDPAIGDLPRgdILIEGDRIAAVAPSIE-----APDAEVVDARGMIVMPGLVDTHRHT-------WQSVLR 72


                 ..
gi 186511115 123 GV 124
Cdd:PRK08204  73 GI 74
ureC PRK13308
urease subunit alpha; Reviewed
 506-547 7.68e-05

urease subunit alpha; Reviewed


Pssm-ID: 183965 [Multi-domain]  Cd Length: 569  Bit Score: 45.47  E-value: 7.68e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 186511115 506 IPSERISFTDAL-----IAQ-TISAARAAFLDHHLGSLSPGKLADFVI 547
Cdd:PRK13308 389 LPEDRGTFADNArikryIAKyTINPAITFGIDDHIGSLEPGKLADIVL 436
PRK06038 PRK06038
N-ethylammeline chlorohydrolase; Provisional
 42-109 8.35e-05

N-ethylammeline chlorohydrolase; Provisional


Pssm-ID: 180363 [Multi-domain]  Cd Length: 430  Bit Score: 45.13  E-value: 8.35e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 186511115  42 ADLLVTNGTIFTSDSSLPFADSMAIRNGRILKVGSFATlkgfiGDGTMEVNLEGKIVVPGLIDSHVHL 109
Cdd:PRK06038   2 ADIIIKNAYVLTMDAGDLKKGSVVIEDGTITEVSESTP-----GDADTVIDAKGSVVMPGLVNTHTHA 64
PRK09061 PRK09061
D-glutamate deacylase; Validated
 33-108 1.22e-04

D-glutamate deacylase; Validated


Pssm-ID: 236369 [Multi-domain]  Cd Length: 509  Bit Score: 44.69  E-value: 1.22e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 186511115  33 SLTPPAGIVADLLVTNGTIFTSDSSLPFADSMAIRNGRILKVGSFAtlkgfiGDGTMEVNLEGKIVVPGLIDSHVH 108
Cdd:PRK09061  10 LLMPASMAPYDLVIRNGRVVDPETGLDAVRDVGIKGGKIAAVGTAA------IEGDRTIDATGLVVAPGFIDLHAH 79
PRK09060 PRK09060
dihydroorotase; Validated
 43-114 1.28e-04

dihydroorotase; Validated


Pssm-ID: 181632 [Multi-domain]  Cd Length: 444  Bit Score: 44.53  E-value: 1.28e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 186511115  43 DLLVTNGTIFTSDSSlPFADsMAIRNGRILKVGSFAtlkgfiGDGTMEV-NLEGKIVVPGLIDSHVHLISGGL 114
Cdd:PRK09060   6 DLILKGGTVVNPDGE-GRAD-IGIRDGRIAAIGDLS------GASAGEViDCRGLHVLPGVIDSQVHFREPGL 70
pyrC PRK09357
dihydroorotase; Validated
 44-109 1.89e-04

dihydroorotase; Validated


Pssm-ID: 236479 [Multi-domain]  Cd Length: 423  Bit Score: 44.03  E-value: 1.89e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 186511115  44 LLVTNGTIFTSDSSLPFADsMAIRNGRILKVGSFAtlkgfIGDGTMEVNLEGKIVVPGLIDSHVHL 109
Cdd:PRK09357   3 ILIKNGRVIDPKGLDEVAD-VLIDDGKIAAIGENI-----EAEGAEVIDATGLVVAPGLVDLHVHL 62
PRK09045 PRK09045
TRZ/ATZ family hydrolase;
516-575 2.52e-04

TRZ/ATZ family hydrolase;


Pssm-ID: 236366 [Multi-domain]  Cd Length: 443  Bit Score: 43.75  E-value: 2.52e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186511115 516 ALIAQTISAARAAFLDHHLGSLSPGKLADFVILSTNS------WDEFSKDVSAS----VLATYVGGKQLY 575
Cdd:PRK09045 345 ALRMATLNGARALGLDDEIGSLEPGKQADLVAVDLSGletqpvYDPVSQLVYAAgreqVSHVWVAGKQLL 414
PRK07228 PRK07228
5'-deoxyadenosine deaminase;
43-109 3.28e-04

5'-deoxyadenosine deaminase;


Pssm-ID: 180895 [Multi-domain]  Cd Length: 445  Bit Score: 43.45  E-value: 3.28e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 186511115  43 DLLVTNGTIFTSDSS--LPFADsMAIRNGRILKVGSFATLKGFigdgTMEVNLEGKIVVPGLIDSHVHL 109
Cdd:PRK07228   2 TILIKNAGIVTMNAKreIVDGD-VLIEDDRIAAVGDRLDLEDY----DDHIDATGKVVIPGLIQGHIHL 65
PRK07228 PRK07228
5'-deoxyadenosine deaminase;
521-575 3.45e-04

5'-deoxyadenosine deaminase;


Pssm-ID: 180895 [Multi-domain]  Cd Length: 445  Bit Score: 43.45  E-value: 3.45e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 186511115 521 TISAARAAFLDHHLGSLSPGKLADFVILSTN--------SWDEFSKDVSAS----VLATYVGGKQLY 575
Cdd:PRK07228 347 TLGGAKAAGFEDEIGSLEEGKKADLAILDLDglhatpshGVDVLSHLVYAAhgsdVETTMVDGKIVM 413
pyrC_multi TIGR00857
dihydroorotase, multifunctional complex type; In contrast to the homodimeric type of ...
 62-109 3.47e-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: 43.20  E-value: 3.47e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 186511115   62 DSMAIRNGRILKVGsfatlkGFIGDGTMEV-NLEGKIVVPGLIDSHVHL 109
Cdd:TIGR00857   6 VDILVEGGRIKKIG------KLRIPPDAEViDAKGLLVLPGFIDLHVHL 48
AdeC COG1001
Adenine deaminase [Nucleotide transport and metabolism];
483-573 4.04e-04

Adenine deaminase [Nucleotide transport and metabolism];


Pssm-ID: 440625 [Multi-domain]  Cd Length: 559  Bit Score: 43.17  E-value: 4.04e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186511115 483 DINPL---------HSIRTAVKR-IPPkwdhawipserisfTDALIAQTISAARAAFLDHhLGSLSPGKLADFVILStnS 552
Cdd:COG1001  260 DRHPDdlleeghidHVVRRAIELgLDP--------------VTAIQMATLNAAEHFGLKD-LGAIAPGRRADIVLLD--D 322

                         90       100
                 ....*....|....*....|.
gi 186511115 553 WDEFskdvsaSVLATYVGGKQ 573
Cdd:COG1001  323 LEDF------KVEKVYADGKL 337
ATZ_TRZ_like cd01298
TRZ/ATZ family contains enzymes from the atrazine degradation pathway and related hydrolases. ...
 501-575 4.40e-04

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: 42.96  E-value: 4.40e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186511115 501 WDHAWIPSErisftDALIAQTISAARAAFLDHhLGSLSPGKLADFVILSTNSWDEFSKD----------VSASVLATYVG 570
Cdd:cd01298  327 GDPTALPAE-----EALEMATIGGAKALGLDE-IGSLEVGKKADLILIDLDGPHLLPVHdpishlvysaNGGDVDTVIVN 400


                 ....*
gi 186511115 571 GKQLY 575
Cdd:cd01298  401 GRVVM 405
PRK09059 PRK09059
dihydroorotase; Validated
 44-109 6.06e-04

dihydroorotase; Validated


Pssm-ID: 181631 [Multi-domain]  Cd Length: 429  Bit Score: 42.33  E-value: 6.06e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 186511115  44 LLVTNGTIFTSDSSLPFADSMAIRNGRILKVGSFATLKGfIGDGTMEVNLEGKIVVPGLIDSHVHL 109
Cdd:PRK09059   5 ILLANARIIDPSRGLDEIGTVLIEDGVIVAAGKGAGNQG-APEGAEIVDCAGKAVAPGLVDARVFV 69
NagA cd00854
N-acetylglucosamine-6-phosphate deacetylase, NagA, catalyzes the hydrolysis of the N-acetyl ...
 44-108 7.20e-04

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: 42.18  E-value: 7.20e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 186511115  44 LLVTNGTIFTSDSSLPFAdsMAIRNGRILKVGSFATLKGfigdGTMEVNLEGKIVVPGLIDSHVH 108
Cdd:cd00854    1 LIIKNARILTPGGLEDGA--VLVEDGKIVAIGPEDELEE----ADEIIDLKGQYLVPGFIDIHIH 59
NagA cd00854
N-acetylglucosamine-6-phosphate deacetylase, NagA, catalyzes the hydrolysis of the N-acetyl ...
 511-571 1.39e-03

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: 41.03  E-value: 1.39e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 186511115 511 ISFTDALIAQTISAARAAFLDHHLGSLSPGKLADFVILStNSWDefskdvsasVLATYVGG 571
Cdd:cd00854  324 CPLEEAVRMASLNPAKLLGLDDRKGSLKPGKDADLVVLD-DDLN---------VKATWING 374
ureC PRK13206
urease subunit alpha; Reviewed
 61-111 1.88e-03

urease subunit alpha; Reviewed


Pssm-ID: 237304 [Multi-domain]  Cd Length: 573  Bit Score: 41.23  E-value: 1.88e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 186511115  61 ADsMAIRNGRIL---KVGSFATLKGF-----IGDGTMEVNLEGKIVVPGLIDSHVHLIS 111
Cdd:PRK13206  89 AD-VGIRDGRIVaigKAGNPDIMDGVhpdlvIGPSTEIIAGNGRILTAGAIDCHVHFIC 146
PRK04250 PRK04250
dihydroorotase; Provisional
 63-109 2.74e-03

dihydroorotase; Provisional


Pssm-ID: 235265 [Multi-domain]  Cd Length: 398  Bit Score: 40.52  E-value: 2.74e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 186511115  63 SMAIRNGRILKVGsfatLKGFIGDGTMEVnlEGKIVVPGLIDSHVHL 109
Cdd:PRK04250  16 GIGIENGRISKIS----LRDLKGKEVIKV--KGGIILPGLIDVHVHL 56
PRK09228 PRK09228
guanine deaminase; Provisional
 521-575 2.91e-03

guanine deaminase; Provisional


Pssm-ID: 236419 [Multi-domain]  Cd Length: 433  Bit Score: 40.17  E-value: 2.91e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 186511115 521 TISAARAAFLDHHLGSLSPGKLADFVILSTNS------WDEFSKDVS------------ASVLATYVGGKQLY 575
Cdd:PRK09228 358 TLGGARALGLDDRIGNLAPGKEADFVVLDPAAtpllalRTARAESLEellfalmtlgddRAVAETYVAGRPVY 430
Bact_CD cd01293
Bacterial cytosine deaminase and related metal-dependent hydrolases. Cytosine deaminases (CDs) ...
 64-109 2.91e-03

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: 40.31  E-value: 2.91e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 186511115  64 MAIRNGRILKVGsfatLKGFIGDGTMEVNLEGKIVVPGLIDSHVHL 109
Cdd:cd01293   17 IAIEDGRIAAIG----PALAVPPDAEEVDAKGRLVLPAFVDPHIHL 58
ureC PRK13309
urease subunit alpha; Reviewed
 34-111 3.52e-03

urease subunit alpha; Reviewed


Pssm-ID: 183966 [Multi-domain]  Cd Length: 572  Bit Score: 40.24  E-value: 3.52e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186511115  34 LTPPAGIVaDLLVTNGTIFTSDSSLPFADsMAIRNGRIL---KVGSFATLKGF-----IGDGTMEVNLEGKIVVPGLIDS 105
Cdd:PRK13309  61 LTRDNGVL-DLVITNVTIVDARLGVIKAD-VGIRDGKIVgigKSGNPSTMDGVtqgmvVGVSTDAISGEHLILTAAGIDT 138


                 ....*.
gi 186511115 106 HVHLIS 111
Cdd:PRK13309 139 HIHLIS 144
AdeC cd01295
Adenine deaminase (AdeC) directly deaminates adenine to form hypoxanthine. This reaction is ...
 488-549 4.00e-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: 39.90  E-value: 4.00e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 186511115 488 HSIRTAVKrippkwdhawipsERISFTDALIAQTISAARAAFLdHHLGSLSPGKLADFVILS 549
Cdd:cd01295  225 YIVRRAIE-------------AGIPPEDAIQMATINPAECYGL-HDLGAIAPGRIADIVILD 272
GDEase cd01303
Guanine deaminase (GDEase). Guanine deaminase is an aminohydrolase responsible for the ...
 64-123 4.47e-03

Guanine deaminase (GDEase). Guanine deaminase is an aminohydrolase responsible for the conversion of guanine to xanthine and ammonia, the first step to utilize guanine as a nitrogen source. This reaction also removes the guanine base from the pool and therefore can play a role in the regulation of cellular GTP and the guanylate nucleotide pool.


Pssm-ID: 238628 [Multi-domain]  Cd Length: 429  Bit Score: 39.57  E-value: 4.47e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 186511115  64 MAIRNGRILKVGSFATLKGFIGDGTMEVNLEGKIVVPGLIDSHVHLIsgglQMAQVGLRG 123
Cdd:cd01303   29 IVVVDGNIIAAGAAETLKRAAKPGARVIDSPNQFILPGFIDTHIHAP----QYANIGSGL 84
PRK12394 PRK12394
metallo-dependent hydrolase;
43-113 4.97e-03

metallo-dependent hydrolase;


Pssm-ID: 183497 [Multi-domain]  Cd Length: 379  Bit Score: 39.36  E-value: 4.97e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 186511115  43 DLLVTNGTIFTSDSSLPFADSMAIRNGRILKVGSFATLKGfigdgTMEVNLEGKIVVPGLIDSHVHLISGG 113
Cdd:PRK12394   4 DILITNGHIIDPARNINEINNLRIINDIIVDADKYPVASE-----TRIIHADGCIVTPGLIDYHAHVFYDG 69
Met_dep_hydrolase_A cd01299
Metallo-dependent hydrolases, subgroup A is part of the superfamily of metallo-dependent ...
 89-113 5.15e-03

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: 39.20  E-value: 5.15e-03
                         10        20
                 ....*....|....*....|....*
gi 186511115  89 MEVNLEGKIVVPGLIDSHVHLISGG 113
Cdd:cd01299    2 QVIDLGGKTLMPGLIDAHTHLGSDP 26
PRK08044 PRK08044
allantoinase AllB;
42-113 8.47e-03

allantoinase AllB;


Pssm-ID: 169193 [Multi-domain]  Cd Length: 449  Bit Score: 38.68  E-value: 8.47e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 186511115  42 ADLLVTNGTIFTSDSSlpFADSMAIRNGRILKVGSFatlkgfIGDGTMEVNLEGKIVVPGLIDSHVHLISGG 113
Cdd:PRK08044   3 FDLIIKNGTVILENEA--RVVDIAVKGGKIAAIGQD------LGDAKEVMDASGLVVSPGMVDAHTHISEPG 66
 
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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