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Conserved domains on  [gi|1601837630|gb|QBQ42420|]
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amidohydrolase [Sphingobacterium psychroaquaticum]

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];
17-544 0e+00

Predicted amidohydrolase YtcJ [General function prediction only];


:

Pssm-ID: 441182 [Multi-domain]  Cd Length: 535  Bit Score: 658.03  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601837630  17 MScTTNKQVDLIVFNAKVYTVDSSFSNAEAFAVKNGIFIDIGTNAEMQKKYTAR-EVIDAQGMPIYPGFYDAHAHFLMLA 95
Cdd:COG1574     1 MK-LAAAAADLLLTNGRIYTMDPAQPVAEAVAVRDGRIVAVGSDAEVRALAGPAtEVIDLGGKTVLPGFIDAHVHLLGGG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601837630  96 ELMEQVDLSGSKSFDEVVNRLKAYQKINPNKKWIVGGGWDQNLWPDKAFPTKDSLDKYFSETPIFLSRVDYHAAVANSAA 175
Cdd:COG1574    80 LALLGVDLSGARSLDELLARLRAAAAELPPGEWILGRGWDESLWPEGRFPTRADLDAVSPDRPVVLTRVDGHAAWVNSAA 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601837630 176 LKIAKIDSAVH-VEGGVIGVGPDGKPNGLFIDNAMQLVSKYIPEPKEEELLARLQKAQDSLFSVGLTSIVDAGLSTEQLE 254
Cdd:COG1574   160 LELAGITADTPdPEGGEIERDADGEPTGVLREAAMDLVRAAIPPPTPEELRAALRAALRELASLGITSVHDAGLGPDDLA 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601837630 255 DLKKFYQKNELKIRDYAMIAGNPHSIEKYIKDGI---FESDRLTIRAVKLMADGALGSRGACLLDHYHDAP-TRGFLLHS 330
Cdd:COG1574   240 AYRELAAAGELPLRVVLYLGADDEDLEELLALGLrtgYGDDRLRVGGVKLFADGSLGSRTAALLEPYADDPgNRGLLLLD 319

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601837630 331 PAEFDQVIKKLANTEFQVNTHAIGDSANRLILDTYGKYLKD--GKQRRWRIEHAQIIAPTDFPKFAQFHIIPSVQPTHAT 408
Cdd:COG1574   320 PEELRELVRAADAAGLQVAVHAIGDAAVDEVLDAYEAARAAngRRDRRHRIEHAQLVDPDDLARFAELGVIASMQPTHAT 399

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601837630 409 SDMYWAEERLGAERMKGAYAYKRLLEQYGMLALGSDFPVEHFNPLYGFHAAVARVDKAGFpqgGFQMEDAISRQDALRGM 488
Cdd:COG1574   400 SDGDWAEDRLGPERAARAYPFRSLLDAGAPLAFGSDAPVEPLDPLLGIYAAVTRRTPSGR---GLGPEERLTVEEALRAY 476

                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1601837630 489 TIWAAYASFQEKKRGSIERGKDADFVILQADIMTAPFEELRQIKTMRTVVAGETVF 544
Cdd:COG1574   477 TIGAAYAAFEEDEKGSLEPGKLADFVVLDRDPLTVPPEEIKDIKVLLTVVGGRVVY 532
 
Name Accession Description Interval E-value
YtcJ COG1574
Predicted amidohydrolase YtcJ [General function prediction only];
17-544 0e+00

Predicted amidohydrolase YtcJ [General function prediction only];


Pssm-ID: 441182 [Multi-domain]  Cd Length: 535  Bit Score: 658.03  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601837630  17 MScTTNKQVDLIVFNAKVYTVDSSFSNAEAFAVKNGIFIDIGTNAEMQKKYTAR-EVIDAQGMPIYPGFYDAHAHFLMLA 95
Cdd:COG1574     1 MK-LAAAAADLLLTNGRIYTMDPAQPVAEAVAVRDGRIVAVGSDAEVRALAGPAtEVIDLGGKTVLPGFIDAHVHLLGGG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601837630  96 ELMEQVDLSGSKSFDEVVNRLKAYQKINPNKKWIVGGGWDQNLWPDKAFPTKDSLDKYFSETPIFLSRVDYHAAVANSAA 175
Cdd:COG1574    80 LALLGVDLSGARSLDELLARLRAAAAELPPGEWILGRGWDESLWPEGRFPTRADLDAVSPDRPVVLTRVDGHAAWVNSAA 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601837630 176 LKIAKIDSAVH-VEGGVIGVGPDGKPNGLFIDNAMQLVSKYIPEPKEEELLARLQKAQDSLFSVGLTSIVDAGLSTEQLE 254
Cdd:COG1574   160 LELAGITADTPdPEGGEIERDADGEPTGVLREAAMDLVRAAIPPPTPEELRAALRAALRELASLGITSVHDAGLGPDDLA 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601837630 255 DLKKFYQKNELKIRDYAMIAGNPHSIEKYIKDGI---FESDRLTIRAVKLMADGALGSRGACLLDHYHDAP-TRGFLLHS 330
Cdd:COG1574   240 AYRELAAAGELPLRVVLYLGADDEDLEELLALGLrtgYGDDRLRVGGVKLFADGSLGSRTAALLEPYADDPgNRGLLLLD 319

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601837630 331 PAEFDQVIKKLANTEFQVNTHAIGDSANRLILDTYGKYLKD--GKQRRWRIEHAQIIAPTDFPKFAQFHIIPSVQPTHAT 408
Cdd:COG1574   320 PEELRELVRAADAAGLQVAVHAIGDAAVDEVLDAYEAARAAngRRDRRHRIEHAQLVDPDDLARFAELGVIASMQPTHAT 399

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601837630 409 SDMYWAEERLGAERMKGAYAYKRLLEQYGMLALGSDFPVEHFNPLYGFHAAVARVDKAGFpqgGFQMEDAISRQDALRGM 488
Cdd:COG1574   400 SDGDWAEDRLGPERAARAYPFRSLLDAGAPLAFGSDAPVEPLDPLLGIYAAVTRRTPSGR---GLGPEERLTVEEALRAY 476

                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1601837630 489 TIWAAYASFQEKKRGSIERGKDADFVILQADIMTAPFEELRQIKTMRTVVAGETVF 544
Cdd:COG1574   477 TIGAAYAAFEEDEKGSLEPGKLADFVVLDRDPLTVPPEEIKDIKVLLTVVGGRVVY 532
YtcJ_like cd01300
YtcJ_like metal dependent amidohydrolases. YtcJ is a Bacillus subtilis ORF of unknown function. ...
 46-515 6.19e-158

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: 459.08  E-value: 6.19e-158
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601837630  46 AFAVKNGIFIDIGTNAE-MQKKYTAREVIDAQGMPIYPGFYDAHAHFLMLAELMEQVDLSGSKSFDEVVNRLKAYQKINP 124
Cdd:cd01300     1 AVAVRDGRIVAVGSDAEaKALKGPATEVIDLKGKTVLPGFIDSHSHLLLGGLSLLWLDLSGVTSKEEALARIREDAAAAP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601837630 125 NKKWIVGGGWDQNLWPDKAFPTKDSLDKYFSETPIFLSRVDYHAAVANSAALKIAKID-SAVHVEGGVIGVGPDGKPNGL 203
Cdd:cd01300    81 PGEWILGFGWDESLLGEGRYPTRAELDAVSPDRPVLLLRRDGHSAWVNSAALRLAGITrDTPDPPGGEIVRDADGEPTGV 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601837630 204 FIDNAMQLVSKYIPEPKEEELLARLQKAQDSLFSVGLTSIVDAGLSTEQ-LEDLKKFYQKNELKIRDYAMIAGNPHSIEK 282
Cdd:cd01300   161 LVEAAAALVLEAVPPPTPEERRAALRAAARELASLGVTTVHDAGGGAADdIEAYRRLAAAGELTLRVRVALYVSPLAEDL 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601837630 283 -----YIKDGiFESDRLTIRAVKLMADGALGSRGACLLDHYHDAP-TRGFLLHSPAEFDQVIKKLANTEFQVNTHAIGDS 356
Cdd:cd01300   241 leelgARKNG-AGDDRLRLGGVKLFADGSLGSRTAALSEPYLDSPgTGGLLLISPEELEELVRAADEAGLQVAIHAIGDR 319

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601837630 357 ANRLILDTYGKYLKDGKQ--RRWRIEHAQIIAPTDFPKFAQFHIIPSVQPTHATSDMYWAEER-LGAERMKGAYAYKRLL 433
Cdd:cd01300   320 AVDTVLDALEAALKDNPRadHRHRIEHAQLVSPDDIPRFAKLGVIASVQPNHLYSDGDAAEDRrLGEERAKRSYPFRSLL 399

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601837630 434 EQYGMLALGSDFPVEHFNPLYGFHAAVARVDKAGFPQGGfqMEDAISRQDALRGMTIWAAYASFQEKKRGSIERGKDADF 513
Cdd:cd01300   400 DAGVPVALGSDAPVAPPDPLLGIWAAVTRKTPGGGVLGN--PEERLSLEEALRAYTIGAAYAIGEEDEKGSLEPGKLADF 477


                  ..
gi 1601837630 514 VI 515
Cdd:cd01300   478 VV 479
Amidohydro_3 pfam07969
Amidohydrolase family;
71-544 5.75e-93

Amidohydrolase family;


Pssm-ID: 400360 [Multi-domain]  Cd Length: 464  Bit Score: 292.13  E-value: 5.75e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601837630  71 EVIDAQGMPIYPGFYDAHAHFLMLAELMEQVDLSGsksfDEVVNRLKAYQKINPNKKWIVGGGWDQNLWPDKAFP-TKDS 149
Cdd:pfam07969   1 EVIDAKGRLVLPGFVDPHTHLDGGGLNLRELRLPD----VLPNAVVKGQAGRTPKGRWLVGEGWDEAQFAETRFPyALAD 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601837630 150 LDKYFSETPIFLSRVDYHAAVANSAALKIAKIDSAVHV-EGGVIGVGPDGK-PNGLFIDNAMQLVSKYIPEpKEEELLAR 227
Cdd:pfam07969  77 LDEVAPDGPVLLRALHTHAAVANSAALDLAGITKATEDpPGGEIARDANGEgLTGLLREGAYALPPLLARE-AEAAAVAA 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601837630 228 LQKAQDSLfsvGLTSIVDAGLSTEQLEDLKKFYqknelKIRDYAMIAGNPHSIEKYIKDGifESDRLTIRAVKLMADGAL 307
Cdd:pfam07969 156 ALAALPGF---GITSVDGGGGNVHSLDDYEPLR-----ELTAAEKLKELLDAPERLGLPH--SIYELRIGAMKLFADGVL 225

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601837630 308 GSRGACLLDHYHDAPTRGFLLHSPAEFDQVIKKLANTEFQVNTHAIGDSANRLILDTYGKY-LKDGKQRRWRIEHAQIIA 386
Cdd:pfam07969 226 GSRTAALTEPYFDAPGTGWPDFEDEALAELVAAARERGLDVAIHAIGDATIDTALDAFEAVaEKLGNQGRVRIEHAQGVV 305

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601837630 387 PTDFPKFAQFH---IIPSVQPTHATSDMYWAEERLGAERMKGAYAYKRLLEQYGMLALGSDFPVEHFNPLYGFHAAVARv 463
Cdd:pfam07969 306 PYTYSQIERVAalgGAAGVQPVFDPLWGDWLQDRLGAERARGLTPVKELLNAGVKVALGSDAPVGPFDPWPRIGAAVMR- 384

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601837630 464 dKAGFPQGGFQMEDAISRQDALRGMTIWAAYASFQEKKRGSIERGKDADFVILQADIMTAPFEELRQIKTMRTVVAGETV 543
Cdd:pfam07969 385 -QTAGGGEVLGPDEELSLEEALALYTSGPAKALGLEDRKGTLGVGKDADLVVLDDDPLTVDPPAIADIRVRLTVVDGRVV 463


                  .
gi 1601837630 544 F 544
Cdd:pfam07969 464 Y 464
PRK07203 PRK07203
putative aminohydrolase SsnA;
27-91 3.74e-09

putative aminohydrolase SsnA;


Pssm-ID: 235963 [Multi-domain]  Cd Length: 442  Bit Score: 58.79  E-value: 3.74e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1601837630  27 LIVFNAKVYTVDSSFSNAE--AFAVKNGIFIDIGTNAEMQKKYTAREVIDAQGMPIYPGFYDAHAHF 91
Cdd:PRK07203    2 LLIGNGTAITRDPAKPVIEdgAIAIEGNVIVEIGTTDELKAKYPDAEFIDAKGKLIMPGLINSHNHI 68
 
Name Accession Description Interval E-value
YtcJ COG1574
Predicted amidohydrolase YtcJ [General function prediction only];
17-544 0e+00

Predicted amidohydrolase YtcJ [General function prediction only];


Pssm-ID: 441182 [Multi-domain]  Cd Length: 535  Bit Score: 658.03  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601837630  17 MScTTNKQVDLIVFNAKVYTVDSSFSNAEAFAVKNGIFIDIGTNAEMQKKYTAR-EVIDAQGMPIYPGFYDAHAHFLMLA 95
Cdd:COG1574     1 MK-LAAAAADLLLTNGRIYTMDPAQPVAEAVAVRDGRIVAVGSDAEVRALAGPAtEVIDLGGKTVLPGFIDAHVHLLGGG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601837630  96 ELMEQVDLSGSKSFDEVVNRLKAYQKINPNKKWIVGGGWDQNLWPDKAFPTKDSLDKYFSETPIFLSRVDYHAAVANSAA 175
Cdd:COG1574    80 LALLGVDLSGARSLDELLARLRAAAAELPPGEWILGRGWDESLWPEGRFPTRADLDAVSPDRPVVLTRVDGHAAWVNSAA 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601837630 176 LKIAKIDSAVH-VEGGVIGVGPDGKPNGLFIDNAMQLVSKYIPEPKEEELLARLQKAQDSLFSVGLTSIVDAGLSTEQLE 254
Cdd:COG1574   160 LELAGITADTPdPEGGEIERDADGEPTGVLREAAMDLVRAAIPPPTPEELRAALRAALRELASLGITSVHDAGLGPDDLA 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601837630 255 DLKKFYQKNELKIRDYAMIAGNPHSIEKYIKDGI---FESDRLTIRAVKLMADGALGSRGACLLDHYHDAP-TRGFLLHS 330
Cdd:COG1574   240 AYRELAAAGELPLRVVLYLGADDEDLEELLALGLrtgYGDDRLRVGGVKLFADGSLGSRTAALLEPYADDPgNRGLLLLD 319

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601837630 331 PAEFDQVIKKLANTEFQVNTHAIGDSANRLILDTYGKYLKD--GKQRRWRIEHAQIIAPTDFPKFAQFHIIPSVQPTHAT 408
Cdd:COG1574   320 PEELRELVRAADAAGLQVAVHAIGDAAVDEVLDAYEAARAAngRRDRRHRIEHAQLVDPDDLARFAELGVIASMQPTHAT 399

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601837630 409 SDMYWAEERLGAERMKGAYAYKRLLEQYGMLALGSDFPVEHFNPLYGFHAAVARVDKAGFpqgGFQMEDAISRQDALRGM 488
Cdd:COG1574   400 SDGDWAEDRLGPERAARAYPFRSLLDAGAPLAFGSDAPVEPLDPLLGIYAAVTRRTPSGR---GLGPEERLTVEEALRAY 476

                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1601837630 489 TIWAAYASFQEKKRGSIERGKDADFVILQADIMTAPFEELRQIKTMRTVVAGETVF 544
Cdd:COG1574   477 TIGAAYAAFEEDEKGSLEPGKLADFVVLDRDPLTVPPEEIKDIKVLLTVVGGRVVY 532
YtcJ_like cd01300
YtcJ_like metal dependent amidohydrolases. YtcJ is a Bacillus subtilis ORF of unknown function. ...
 46-515 6.19e-158

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: 459.08  E-value: 6.19e-158
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601837630  46 AFAVKNGIFIDIGTNAE-MQKKYTAREVIDAQGMPIYPGFYDAHAHFLMLAELMEQVDLSGSKSFDEVVNRLKAYQKINP 124
Cdd:cd01300     1 AVAVRDGRIVAVGSDAEaKALKGPATEVIDLKGKTVLPGFIDSHSHLLLGGLSLLWLDLSGVTSKEEALARIREDAAAAP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601837630 125 NKKWIVGGGWDQNLWPDKAFPTKDSLDKYFSETPIFLSRVDYHAAVANSAALKIAKID-SAVHVEGGVIGVGPDGKPNGL 203
Cdd:cd01300    81 PGEWILGFGWDESLLGEGRYPTRAELDAVSPDRPVLLLRRDGHSAWVNSAALRLAGITrDTPDPPGGEIVRDADGEPTGV 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601837630 204 FIDNAMQLVSKYIPEPKEEELLARLQKAQDSLFSVGLTSIVDAGLSTEQ-LEDLKKFYQKNELKIRDYAMIAGNPHSIEK 282
Cdd:cd01300   161 LVEAAAALVLEAVPPPTPEERRAALRAAARELASLGVTTVHDAGGGAADdIEAYRRLAAAGELTLRVRVALYVSPLAEDL 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601837630 283 -----YIKDGiFESDRLTIRAVKLMADGALGSRGACLLDHYHDAP-TRGFLLHSPAEFDQVIKKLANTEFQVNTHAIGDS 356
Cdd:cd01300   241 leelgARKNG-AGDDRLRLGGVKLFADGSLGSRTAALSEPYLDSPgTGGLLLISPEELEELVRAADEAGLQVAIHAIGDR 319

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601837630 357 ANRLILDTYGKYLKDGKQ--RRWRIEHAQIIAPTDFPKFAQFHIIPSVQPTHATSDMYWAEER-LGAERMKGAYAYKRLL 433
Cdd:cd01300   320 AVDTVLDALEAALKDNPRadHRHRIEHAQLVSPDDIPRFAKLGVIASVQPNHLYSDGDAAEDRrLGEERAKRSYPFRSLL 399

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601837630 434 EQYGMLALGSDFPVEHFNPLYGFHAAVARVDKAGFPQGGfqMEDAISRQDALRGMTIWAAYASFQEKKRGSIERGKDADF 513
Cdd:cd01300   400 DAGVPVALGSDAPVAPPDPLLGIWAAVTRKTPGGGVLGN--PEERLSLEEALRAYTIGAAYAIGEEDEKGSLEPGKLADF 477


                  ..
gi 1601837630 514 VI 515
Cdd:cd01300   478 VV 479
Amidohydro_3 pfam07969
Amidohydrolase family;
71-544 5.75e-93

Amidohydrolase family;


Pssm-ID: 400360 [Multi-domain]  Cd Length: 464  Bit Score: 292.13  E-value: 5.75e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601837630  71 EVIDAQGMPIYPGFYDAHAHFLMLAELMEQVDLSGsksfDEVVNRLKAYQKINPNKKWIVGGGWDQNLWPDKAFP-TKDS 149
Cdd:pfam07969   1 EVIDAKGRLVLPGFVDPHTHLDGGGLNLRELRLPD----VLPNAVVKGQAGRTPKGRWLVGEGWDEAQFAETRFPyALAD 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601837630 150 LDKYFSETPIFLSRVDYHAAVANSAALKIAKIDSAVHV-EGGVIGVGPDGK-PNGLFIDNAMQLVSKYIPEpKEEELLAR 227
Cdd:pfam07969  77 LDEVAPDGPVLLRALHTHAAVANSAALDLAGITKATEDpPGGEIARDANGEgLTGLLREGAYALPPLLARE-AEAAAVAA 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601837630 228 LQKAQDSLfsvGLTSIVDAGLSTEQLEDLKKFYqknelKIRDYAMIAGNPHSIEKYIKDGifESDRLTIRAVKLMADGAL 307
Cdd:pfam07969 156 ALAALPGF---GITSVDGGGGNVHSLDDYEPLR-----ELTAAEKLKELLDAPERLGLPH--SIYELRIGAMKLFADGVL 225

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601837630 308 GSRGACLLDHYHDAPTRGFLLHSPAEFDQVIKKLANTEFQVNTHAIGDSANRLILDTYGKY-LKDGKQRRWRIEHAQIIA 386
Cdd:pfam07969 226 GSRTAALTEPYFDAPGTGWPDFEDEALAELVAAARERGLDVAIHAIGDATIDTALDAFEAVaEKLGNQGRVRIEHAQGVV 305

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601837630 387 PTDFPKFAQFH---IIPSVQPTHATSDMYWAEERLGAERMKGAYAYKRLLEQYGMLALGSDFPVEHFNPLYGFHAAVARv 463
Cdd:pfam07969 306 PYTYSQIERVAalgGAAGVQPVFDPLWGDWLQDRLGAERARGLTPVKELLNAGVKVALGSDAPVGPFDPWPRIGAAVMR- 384

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601837630 464 dKAGFPQGGFQMEDAISRQDALRGMTIWAAYASFQEKKRGSIERGKDADFVILQADIMTAPFEELRQIKTMRTVVAGETV 543
Cdd:pfam07969 385 -QTAGGGEVLGPDEELSLEEALALYTSGPAKALGLEDRKGTLGVGKDADLVVLDDDPLTVDPPAIADIRVRLTVVDGRVV 463


                  .
gi 1601837630 544 F 544
Cdd:pfam07969 464 Y 464
HutI COG1228
Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport ...
 20-540 1.46e-13

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


Pssm-ID: 440841 [Multi-domain]  Cd Length: 386  Bit Score: 72.30  E-value: 1.46e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601837630  20 TTNKQVDLIVF-NAKVYTVDSS--FSNAeAFAVKNGIFIDIGTNAEMQKKYTArEVIDAQGMPIYPGFYDAHAHflmlae 96
Cdd:COG1228     2 KAPAQAGTLLItNATLVDGTGGgvIENG-TVLVEDGKIAAVGPAADLAVPAGA-EVIDATGKTVLPGLIDAHTH------ 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601837630  97 lmeqvdlsgsksfdevvnrlkayqkinpnkkwIVGGGWDQNlwpdkafptkdsldkYFSETPIFLSRVDYHAAVANSAal 176
Cdd:COG1228    74 --------------------------------LGLGGGRAV---------------EFEAGGGITPTVDLVNPADKRL-- 104

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601837630 177 kiakidsavhveggvigvgpdgkpnglfidnamqlvskyipepkeEELLARlqkaqdslfsvGLTSIVDAGLSTEQLedl 256
Cdd:COG1228   105 ---------------------------------------------RRALAA-----------GVTTVRDLPGGPLGL--- 125

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601837630 257 KKFYQKNELKIRDYAMIAGNPHSIekYIKDGIFESDRLTIRA-VKLMADgalgsRGACLLDHYHDAPTRGFllhSPAEFD 335
Cdd:COG1228   126 RDAIIAGESKLLPGPRVLAAGPAL--SLTGGAHARGPEEARAaLRELLA-----EGADYIKVFAEGGAPDF---SLEELR 195

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601837630 336 QVIKKLANTEFQVNTHAIGDSANRLIL----DTygkylkdgkqrrwrIEHAQIIAPTDFPKFAQFHIIpSVQPTHATSDm 411
Cdd:COG1228   196 AILEAAHALGLPVAAHAHQADDIRLAVeagvDS--------------IEHGTYLDDEVADLLAEAGTV-VLVPTLSLFL- 259

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601837630 412 YWAEERLGAERMKGAYAYKRLLEQYGML-------ALGSDFPVEHfNPLYGFHAAVARVDKAGFpqggfqmedaiSRQDA 484
Cdd:COG1228   260 ALLEGAAAPVAAKARKVREAALANARRLhdagvpvALGTDAGVGV-PPGRSLHRELALAVEAGL-----------TPEEA 327

                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1601837630 485 LRGMTIWAAYASFQEKKRGSIERGKDADFVILQADimtaPFEELRQIKTMRTVVAG 540
Cdd:COG1228   328 LRAATINAAKALGLDDDVGSLEPGKLADLVLLDGD----PLEDIAYLEDVRAVMKD 379
SsnA COG0402
Cytosine/adenosine deaminase or related metal-dependent hydrolase [Nucleotide transport and ...
 26-91 5.51e-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: 61.38  E-value: 5.51e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1601837630  26 DLIVFNAKVYTVDSSFSNAE--AFAVKNGIFIDIGTNAEMQKKYTAREVIDAQGMPIYPGFYDAHAHF 91
Cdd:COG0402     1 DLLIRGAWVLTMDPAGGVLEdgAVLVEDGRIAAVGPGAELPARYPAAEVIDAGGKLVLPGLVNTHTHL 68
PRK07203 PRK07203
putative aminohydrolase SsnA;
27-91 3.74e-09

putative aminohydrolase SsnA;


Pssm-ID: 235963 [Multi-domain]  Cd Length: 442  Bit Score: 58.79  E-value: 3.74e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1601837630  27 LIVFNAKVYTVDSSFSNAE--AFAVKNGIFIDIGTNAEMQKKYTAREVIDAQGMPIYPGFYDAHAHF 91
Cdd:PRK07203    2 LLIGNGTAITRDPAKPVIEdgAIAIEGNVIVEIGTTDELKAKYPDAEFIDAKGKLIMPGLINSHNHI 68
Imidazolone-5PH cd01296
Imidazolonepropionase/imidazolone-5-propionate hydrolase (Imidazolone-5PH) catalyzes the third ...
 426-519 4.11e-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: 58.42  E-value: 4.11e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601837630 426 AYAYKRLLEQYGM-LALGSDFpvehfNPLYGFHAAVARVdkAGFPQGGFQMedaiSRQDALRGMTIWAAYASFQEKKRGS 504
Cdd:cd01296   267 TYPPARKLIDAGVpVALGTDF-----NPGSSPTSSMPLV--MHLACRLMRM----TPEEALTAATINAAAALGLGETVGS 335

                          90
                  ....*....|....*
gi 1601837630 505 IERGKDADFVILQAD 519
Cdd:cd01296   336 LEVGKQADLVILDAP 350
Met_dep_hydrolase_C cd01309
Metallo-dependent hydrolases, subgroup C is part of the superfamily of metallo-dependent ...
 428-544 4.32e-06

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: 48.85  E-value: 4.32e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601837630 428 AYKRLLEQYGM-LALGSDFPVEHFNPLYgFHAAVArvdkagfpqggfqMEDAISRQDALRGMTIWAAYASFQEKKRGSIE 506
Cdd:cd01309   262 TNAYLLKKGGVaFAISSDHPVLNIRNLN-LEAAKA-------------VKYGLSYEEALKAITINPAKILGIEDRVGSLE 327

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1601837630 507 RGKDADFVILQADimtaPFEELRqiKTMRTVVAGETVF 544
Cdd:cd01309   328 PGKDADLVVWNGD----PLEPTS--KPEQVYIDGRLVY 359
Imidazolone-5PH cd01296
Imidazolonepropionase/imidazolone-5-propionate hydrolase (Imidazolone-5PH) catalyzes the third ...
 48-92 4.60e-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: 45.71  E-value: 4.60e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1601837630  48 AVKNGIFIDIGTNAEMQK-KYTAREVIDAQGMPIYPGFYDAHAHFL 92
Cdd:cd01296     2 AIRDGRIAAVGPAASLPApGPAAAEEIDAGGRAVTPGLVDCHTHLV 47
COG3653 COG3653
N-acyl-D-aspartate/D-glutamate deacylase [Secondary metabolites biosynthesis, transport and ...
 24-90 5.46e-05

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


Pssm-ID: 442870 [Multi-domain]  Cd Length: 528  Bit Score: 45.93  E-value: 5.46e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1601837630  24 QVDLIVFNAKVytVDSSfsNAEAF----AVKNGIFIDIGTNAEmqkkYTAREVIDAQGMPIYPGFYDAHAH 90
Cdd:COG3653     1 MFDLLIRGGTV--VDGT--GAPPFradvAIKGGRIVAVGDLAA----AEAARVIDATGLVVAPGFIDIHTH 63
ATZ_TRZ_like cd01298
TRZ/ATZ family contains enzymes from the atrazine degradation pathway and related hydrolases. ...
 46-93 6.27e-05

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: 45.66  E-value: 6.27e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1601837630  46 AFAVKNGIFIDIGTNAEmQKKYTAREVIDAQGMPIYPGFYDAHAHFLM 93
Cdd:cd01298    21 DVLVEDGRIVAVGPALP-LPAYPADEVIDAKGKVVMPGLVNTHTHLAM 67
AllB COG0044
Dihydroorotase or related cyclic amidohydrolase [Nucleotide transport and metabolism]; ...
 48-91 6.27e-05

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: 45.47  E-value: 6.27e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1601837630  48 AVKNGIFIDIGTNAEMQkkyTAREVIDAQGMPIYPGFYDAHAHF 91
Cdd:COG0044    19 LIEDGRIAAIGPDLAAP---EAAEVIDATGLLVLPGLIDLHVHL 59
D-aminoacylase cd01297
D-aminoacylases (N-acyl-D-Amino acid amidohydrolases) catalyze the hydrolysis of ...
 26-90 9.38e-05

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: 44.98  E-value: 9.38e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1601837630  26 DLIVFNAKVytVDSSfsNAEAF----AVKNGIFIDIGTNAEMQkkytAREVIDAQGMPIYPGFYDAHAH 90
Cdd:cd01297     1 DLVIRNGTV--VDGT--GAPPFtadvGIRDGRIAAIGPILSTS----AREVIDAAGLVVAPGFIDVHTH 61
D-HYD cd01314
D-hydantoinases (D-HYD) also called dihydropyrimidases (DHPase) and related proteins; DHPases ...
 27-108 1.48e-04

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: 44.52  E-value: 1.48e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601837630  27 LIVFNAKVYTVDSSFsnaEA-FAVKNGIFIDIGTNAEMQKKYtarEVIDAQGMPIYPGFYDAHAHFLMLAELMEQVD--L 103
Cdd:cd01314     1 LIIKNGTIVTADGSF---KAdILIEDGKIVAIGPNLEAPGGV---EVIDATGKYVLPGGIDPHTHLELPFMGTVTADdfE 74


                  ....*
gi 1601837630 104 SGSKS 108
Cdd:cd01314    75 SGTRA 79
PRK09061 PRK09061
D-glutamate deacylase; Validated
 9-128 2.73e-04

D-glutamate deacylase; Validated


Pssm-ID: 236369 [Multi-domain]  Cd Length: 509  Bit Score: 43.53  E-value: 2.73e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601837630   9 ICSIIFFLMSCTTNKQV-DLIVFNAKVYTVDSSFSNAEAFAVKNGIFIDIGTNAemqkkYTAREVIDAQGMPIYPGFYDA 87
Cdd:PRK09061    2 AKVAVLSLLLMPASMAPyDLVIRNGRVVDPETGLDAVRDVGIKGGKIAAVGTAA-----IEGDRTIDATGLVVAPGFIDL 76

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1601837630  88 HAHFLMLAElmeqvdlSGSKSFDEVVNRLKAYQKINPNKKW 128
Cdd:PRK09061   77 HAHGQSVAA-------YRMQAFDGVTTALELEAGVLPVARW 110
PRK06189 PRK06189
allantoinase; Provisional
 26-91 4.12e-04

allantoinase; Provisional


Pssm-ID: 235732 [Multi-domain]  Cd Length: 451  Bit Score: 42.77  E-value: 4.12e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1601837630  26 DLIVFNAKVYTVDSSfsnAEA-FAVKNGIFIDIGTNAEMqkkyTAREVIDAQGMPIYPGFYDAHAHF 91
Cdd:PRK06189    4 DLIIRGGKVVTPEGV---YRAdIGIKNGKIAEIAPEISS----PAREIIDADGLYVFPGMIDVHVHF 63
COG3964 COG3964
Predicted amidohydrolase [General function prediction only];
26-90 6.17e-04

Predicted amidohydrolase [General function prediction only];


Pssm-ID: 443164 [Multi-domain]  Cd Length: 376  Bit Score: 42.08  E-value: 6.17e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1601837630  26 DLIVFNAKVytVDSSFSNAEAF--AVKNGIFIDIGTNAEmqkKYTAREVIDAQGMPIYPGFYDAHAH 90
Cdd:COG3964     1 DLLIKGGRV--IDPANGIDGVMdiAIKDGKIAAVAKDID---AAEAKKVIDASGLYVTPGLIDLHTH 62
L-HYD_ALN cd01315
L-Hydantoinases (L-HYDs) and Allantoinase (ALN); L-Hydantoinases are a member of the ...
 26-91 6.40e-04

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: 42.28  E-value: 6.40e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1601837630  26 DLIVFNAKVYTVDSSFSNAeaFAVKNGIFIDIGTNAEmqkKYTAREVIDAQGMPIYPGFYDAHAHF 91
Cdd:cd01315     1 DLVIKNGRVVTPDGVREAD--IAVKGGKIAAIGPDIA---NTEAEEVIDAGGLVVMPGLIDTHVHI 61
Amidohydro_1 pfam01979
Amidohydrolase family; This family of enzymes are a a large metal dependent hydrolase ...
 483-543 7.05e-04

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: 42.10  E-value: 7.05e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1601837630 483 DALRGMTIWAAYASFQEKKRGSIERGKDADFVILQADIMTAPFEELRQIKTMRTVVAGETV 543
Cdd:pfam01979 274 EALRMATINPAKALGLDDKVGSIEVGKDADLVVVDLDPLAAFFGLKPDGNVKKVIVKGKIV 334
pyrC PRK09357
dihydroorotase; Validated
 49-91 1.45e-03

dihydroorotase; Validated


Pssm-ID: 236479 [Multi-domain]  Cd Length: 423  Bit Score: 41.33  E-value: 1.45e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1601837630  49 VKNGIFIDIGTNAEmqkkYTAREVIDAQGMPIYPGFYDAHAHF 91
Cdd:PRK09357   24 IDDGKIAAIGENIE----AEGAEVIDATGLVVAPGLVDLHVHL 62
AdeC COG1001
Adenine deaminase [Nucleotide transport and metabolism];
29-91 1.69e-03

Adenine deaminase [Nucleotide transport and metabolism];


Pssm-ID: 440625 [Multi-domain]  Cd Length: 559  Bit Score: 41.24  E-value: 1.69e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1601837630  29 VFNAKVYTVDssfsnaeaFAVKNGIFIDIGtnaemqkKYT--AREVIDAQGMPIYPGFYDAHAHF 91
Cdd:COG1001    17 VFTGEILEGD--------IAIAGGRIAGVG-------DYIgeATEVIDAAGRYLVPGFIDGHVHI 66
PRK09045 PRK09045
TRZ/ATZ family hydrolase;
46-93 2.71e-03

TRZ/ATZ family hydrolase;


Pssm-ID: 236366 [Multi-domain]  Cd Length: 443  Bit Score: 40.28  E-value: 2.71e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1601837630  46 AFAVKNGIFIDIGTNAEMQKKYTAREVIDAQGMPIYPGFYDAHAHFLM 93
Cdd:PRK09045   30 AVAIRDGRIVAILPRAEARARYAAAETVELPDHVLIPGLINAHTHAAM 77
PRK12394 PRK12394
metallo-dependent hydrolase;
26-90 3.76e-03

metallo-dependent hydrolase;


Pssm-ID: 183497 [Multi-domain]  Cd Length: 379  Bit Score: 39.74  E-value: 3.76e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1601837630  26 DLIVFNAKVYTVDSSFSNAEAFAVKNGIFIDIGTNAEMQkkytAREVIDAQGMPIYPGFYDAHAH 90
Cdd:PRK12394    4 DILITNGHIIDPARNINEINNLRIINDIIVDADKYPVAS----ETRIIHADGCIVTPGLIDYHAH 64
NagA cd00854
N-acetylglucosamine-6-phosphate deacetylase, NagA, catalyzes the hydrolysis of the N-acetyl ...
 31-90 5.45e-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: 39.10  E-value: 5.45e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601837630  31 NAKVYTVDSSFSNAeaFAVKNGIFIDIGTNAEmqkKYTAREVIDAQGMPIYPGFYDAHAH 90
Cdd:cd00854     5 NARILTPGGLEDGA--VLVEDGKIVAIGPEDE---LEEADEIIDLKGQYLVPGFIDIHIH 59
PRK09060 PRK09060
dihydroorotase; Validated
 26-91 6.25e-03

dihydroorotase; Validated


Pssm-ID: 181632 [Multi-domain]  Cd Length: 444  Bit Score: 39.13  E-value: 6.25e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1601837630  26 DLIVFNAKVYTVDSSfsnAEA-FAVKNGIFIDIGTNAemqkKYTAREVIDAQGMPIYPGFYDAHAHF 91
Cdd:PRK09060    6 DLILKGGTVVNPDGE---GRAdIGIRDGRIAAIGDLS----GASAGEVIDCRGLHVLPGVIDSQVHF 65
PRK13404 PRK13404
dihydropyrimidinase; Provisional
 23-91 7.80e-03

dihydropyrimidinase; Provisional


Pssm-ID: 184033 [Multi-domain]  Cd Length: 477  Bit Score: 38.91  E-value: 7.80e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1601837630  23 KQVDLIVFNAKVYTVDSSFsnAEAFAVKNGIFIDIGTNAEmqkkyTAREVIDAQGMPIYPGFYDAHAHF 91
Cdd:PRK13404    2 MAFDLVIRGGTVVTATDTF--QADIGIRGGRIAALGEGLG-----PGAREIDATGRLVLPGGVDSHCHI 63
metallo-dependent_hydrolases cd01292
Superfamily of metallo-dependent hydrolases (also called amidohydrolase superfamily) is a ...
 180-495 8.10e-03

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: 38.47  E-value: 8.10e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601837630 180 KIDSAVHVEGGVigvgpDGKPNGLFIDNAMQLVSKYIPEPKEEELLARLQKAqdslfsvGLTSIVDAG------LSTEQL 253
Cdd:cd01292     1 FIDTHVHLDGSA-----LRGTRLNLELKEAEELSPEDLYEDTLRALEALLAG-------GVTTVVDMGstppptTTKAAI 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601837630 254 EDLKKFYQKNElKIRDYaMIAGNPHSIEKYIKDGIFESDRLTIRAVKLMADGaLGSRGAClldhyhdaptrGFLLHSPAE 333
Cdd:cd01292    69 EAVAEAARASA-GIRVV-LGLGIPGVPAAVDEDAEALLLELLRRGLELGAVG-LKLAGPY-----------TATGLSDES 134

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601837630 334 FDQVIKKLANTEFQVNTHAI-GDSANRLILDTYgkyLKDGKQRRWRIEHAQIIAPTDFPKFAQFHIIPSVQPTHATSDMY 412
Cdd:cd01292   135 LRRVLEEARKLGLPVVIHAGeLPDPTRALEDLV---ALLRLGGRVVIGHVSHLDPELLELLKEAGVSLEVCPLSNYLLGR 211

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1601837630 413 WAEerlgaermkGAYAYKRLLEQYGMLALGSDFPV--EHFNPLYGFHAAVArvdkagfpQGGFQMedaiSRQDALRGMTI 490
Cdd:cd01292   212 DGE---------GAEALRRLLELGIRVTLGTDGPPhpLGTDLLALLRLLLK--------VLRLGL----SLEEALRLATI 270


                  ....*
gi 1601837630 491 WAAYA 495
Cdd:cd01292   271 NPARA 275
 
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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