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Conserved domains on  [gi|948188955|ref|WP_056846866|]
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MULTISPECIES: amidohydrolase [Pseudomonas]

Protein Classification

amidohydrolase( domain architecture ID 10101347)

metal-dependent amidohydrolase similar to Bacillus subtilis YtcJ and Arthrobacter pascens N-substituted formamide deformylase that catalyzes the hydrolysis of N-benzylformamide (an N-substituted formamide) to benzylamine and formate

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

Graphical summary

 Zoom to residue level

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List of domain hits

 Name Accession Description Interval E-value
YtcJ_like cd01300
YtcJ_like metal dependent amidohydrolases. YtcJ is a Bacillus subtilis ORF of unknown function. ...
 24-502 1.20e-163

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: 476.03  E-value: 1.20e-163
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948188955  24 AVAIRDGRFVAVGTDGEAMALRGSGTQVIDLKGRTVIPGLNDSHLHLIRGGLnYNLELRWEGVPSLADALRMLKDQADRT 103
Cdd:cd01300    1 AVAVRDGRIVAVGSDAEAKALKGPATEVIDLKGKTVLPGFIDSHSHLLLGGL-SLLWLDLSGVTSKEEALARIREDAAAA 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948188955 104 PTPQWVRvVGGWNEFQFAEKRMPTLEELNQAAPDTPVFVLHL-YDRALLNRAALRVAGYTKDTPNPPGGEIVRDSHGNPT 182
Cdd:cd01300   80 PPGEWIL-GFGWDESLLGEGRYPTRAELDAVSPDRPVLLLRRdGHSAWVNSAALRLAGITRDTPDPPGGEIVRDADGEPT 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948188955 183 GMLVARPNAMILYSTlakgPKLPLEYQVNSTRQFMRELNRLGLTSAIDAGGGfqnYPDDYAVIEQLAKDQQLTVRIAYNL 262
Cdd:cd01300  159 GVLVEAAAALVLEAV----PPPTPEERRAALRAAARELASLGVTTVHDAGGG---AADDIEAYRRLAAAGELTLRVRVAL 231

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948188955 263 FTQKPKEELSDF----KNWTGSVTLHQGDDYLRHNGAGEmlVFSAADFEDFLEPRPD--LPLTMEQELEPVVRHLVEQRW 336
Cdd:cd01300  232 YVSPLAEDLLEElgarKNGAGDDRLRLGGVKLFADGSLG--SRTAALSEPYLDSPGTggLLLISPEELEELVRAADEAGL 309

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948188955 337 PFRLHATYDESISRMLDVFEKVNRDIPFNGLPWFFDHAETITPKNIERVRALGGGIAIQDRMAFQGEYFVERY--GAKAA 414
Cdd:cd01300  310 QVAIHAIGDRAVDTVLDALEAALKDNPRADHRHRIEHAQLVSPDDIPRFAKLGVIASVQPNHLYSDGDAAEDRrlGEERA 389

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948188955 415 EATPPIKRMLAEGVPVGAGTDATrVSSYNPWTSLYWMVSGRTVGGLELH--AEGLPRLTALELFTHGSAWFSSEQGKKGQ 492
Cdd:cd01300  390 KRSYPFRSLLDAGVPVALGSDAP-VAPPDPLLGIWAAVTRKTPGGGVLGnpEERLSLEEALRAYTIGAAYAIGEEDEKGS 468

                        490
                 ....*....|
gi 948188955 493 IKVGQLADVA 502
Cdd:cd01300  469 LEPGKLADFV 478
 
Name Accession Description Interval E-value
YtcJ_like cd01300
YtcJ_like metal dependent amidohydrolases. YtcJ is a Bacillus subtilis ORF of unknown function. ...
 24-502 1.20e-163

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: 476.03  E-value: 1.20e-163
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948188955  24 AVAIRDGRFVAVGTDGEAMALRGSGTQVIDLKGRTVIPGLNDSHLHLIRGGLnYNLELRWEGVPSLADALRMLKDQADRT 103
Cdd:cd01300    1 AVAVRDGRIVAVGSDAEAKALKGPATEVIDLKGKTVLPGFIDSHSHLLLGGL-SLLWLDLSGVTSKEEALARIREDAAAA 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948188955 104 PTPQWVRvVGGWNEFQFAEKRMPTLEELNQAAPDTPVFVLHL-YDRALLNRAALRVAGYTKDTPNPPGGEIVRDSHGNPT 182
Cdd:cd01300   80 PPGEWIL-GFGWDESLLGEGRYPTRAELDAVSPDRPVLLLRRdGHSAWVNSAALRLAGITRDTPDPPGGEIVRDADGEPT 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948188955 183 GMLVARPNAMILYSTlakgPKLPLEYQVNSTRQFMRELNRLGLTSAIDAGGGfqnYPDDYAVIEQLAKDQQLTVRIAYNL 262
Cdd:cd01300  159 GVLVEAAAALVLEAV----PPPTPEERRAALRAAARELASLGVTTVHDAGGG---AADDIEAYRRLAAAGELTLRVRVAL 231

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948188955 263 FTQKPKEELSDF----KNWTGSVTLHQGDDYLRHNGAGEmlVFSAADFEDFLEPRPD--LPLTMEQELEPVVRHLVEQRW 336
Cdd:cd01300  232 YVSPLAEDLLEElgarKNGAGDDRLRLGGVKLFADGSLG--SRTAALSEPYLDSPGTggLLLISPEELEELVRAADEAGL 309

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948188955 337 PFRLHATYDESISRMLDVFEKVNRDIPFNGLPWFFDHAETITPKNIERVRALGGGIAIQDRMAFQGEYFVERY--GAKAA 414
Cdd:cd01300  310 QVAIHAIGDRAVDTVLDALEAALKDNPRADHRHRIEHAQLVSPDDIPRFAKLGVIASVQPNHLYSDGDAAEDRrlGEERA 389

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948188955 415 EATPPIKRMLAEGVPVGAGTDATrVSSYNPWTSLYWMVSGRTVGGLELH--AEGLPRLTALELFTHGSAWFSSEQGKKGQ 492
Cdd:cd01300  390 KRSYPFRSLLDAGVPVALGSDAP-VAPPDPLLGIWAAVTRKTPGGGVLGnpEERLSLEEALRAYTIGAAYAIGEEDEKGS 468

                        490
                 ....*....|
gi 948188955 493 IKVGQLADVA 502
Cdd:cd01300  469 LEPGKLADFV 478
YtcJ COG1574
Predicted amidohydrolase YtcJ [General function prediction only];
3-535 3.98e-152

Predicted amidohydrolase YtcJ [General function prediction only];


Pssm-ID: 441182 [Multi-domain]  Cd Length: 535  Bit Score: 448.86  E-value: 3.98e-152
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948188955   3 ADLILFNGQFHTVDRENPRATAVAIRDGRFVAVGTDGEAMALRGSGTQVIDLKGRTVIPGLNDSHLHLIRGGLNyNLELR 82
Cdd:COG1574    8 ADLLLTNGRIYTMDPAQPVAEAVAVRDGRIVAVGSDAEVRALAGPATEVIDLGGKTVLPGFIDAHVHLLGGGLA-LLGVD 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948188955  83 WEGVPSLADALRMLKDQADRTPTPQWVrVVGGWNEFQFAEKRMPTLEELNQAAPDTPVFVLHlYDR--ALLNRAALRVAG 160
Cdd:COG1574   87 LSGARSLDELLARLRAAAAELPPGEWI-LGRGWDESLWPEGRFPTRADLDAVSPDRPVVLTR-VDGhaAWVNSAALELAG 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948188955 161 YTKDTPNPPGGEIVRDSHGNPTGMLVArpNAMILYSTLAkgPKLPLEYQVNSTRQFMRELNRLGLTSAIDAGGGfqnyPD 240
Cdd:COG1574  165 ITADTPDPEGGEIERDADGEPTGVLRE--AAMDLVRAAI--PPPTPEELRAALRAALRELASLGITSVHDAGLG----PD 236

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948188955 241 DYAVIEQLAKDQQLTVRIAYNLFTQkpKEELSDFKNWtgSVTLHQGDDYLRHNGA-----GEMLVFSAAdfedFLEPRPD 315
Cdd:COG1574  237 DLAAYRELAAAGELPLRVVLYLGAD--DEDLEELLAL--GLRTGYGDDRLRVGGVklfadGSLGSRTAA----LLEPYAD 308

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948188955 316 LP-----LTMEQE-LEPVVRHLVEQRWPFRLHATYDESISRMLDVFEKVNRDIPFNGLPWFFDHAETITPKNIERVRALG 389
Cdd:COG1574  309 DPgnrglLLLDPEeLRELVRAADAAGLQVAVHAIGDAAVDEVLDAYEAARAANGRRDRRHRIEHAQLVDPDDLARFAELG 388

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948188955 390 GGIAIQDR-MAFQGEYFVERYGAKAAEATPPIKRMLAEGVPVGAGTDATrVSSYNPWTSLYWMVSGRTVGGLELHA-EGL 467
Cdd:COG1574  389 VIASMQPThATSDGDWAEDRLGPERAARAYPFRSLLDAGAPLAFGSDAP-VEPLDPLLGIYAAVTRRTPSGRGLGPeERL 467

                        490       500       510       520       530       540
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 948188955 468 PRLTALELFTHGSAWFSSEQGKKGQIKVGQLADVAALSADFFSVDEEAIKWIESVLTVVGGKVVYGAG 535
Cdd:COG1574  468 TVEEALRAYTIGAAYAAFEEDEKGSLEPGKLADFVVLDRDPLTVPPEEIKDIKVLLTVVGGRVVYEAE 535
Amidohydro_3 pfam07969
Amidohydrolase family;
50-532 2.31e-122

Amidohydrolase family;


Pssm-ID: 400360 [Multi-domain]  Cd Length: 464  Bit Score: 369.94  E-value: 2.31e-122
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948188955   50 QVIDLKGRTVIPGLNDSHLHLIRGGLNYNlELRWEGVPSLADalrmLKDQADRTPTPQWvRVVGGWNEFQFAEKRMP-TL 128
Cdd:pfam07969   1 EVIDAKGRLVLPGFVDPHTHLDGGGLNLR-ELRLPDVLPNAV----VKGQAGRTPKGRW-LVGEGWDEAQFAETRFPyAL 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948188955  129 EELNQAAPDTPVFVLHL-YDRALLNRAALRVAGYTKDTPNPPGGEIVRDSHGN-PTGMLVARPNAMilystlakGPKLPL 206
Cdd:pfam07969  75 ADLDEVAPDGPVLLRALhTHAAVANSAALDLAGITKATEDPPGGEIARDANGEgLTGLLREGAYAL--------PPLLAR 146

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948188955  207 EYQVNSTRQFMRELNRLGLTSaIDAGGGFQNYPDDYAVIEQLAKdqqltvriaynlfTQKPKEELSDFKNWTGSVTLHQ- 285
Cdd:pfam07969 147 EAEAAAVAAALAALPGFGITS-VDGGGGNVHSLDDYEPLRELTA-------------AEKLKELLDAPERLGLPHSIYEl 212

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948188955  286 GDDYLRHNGAGEMLVFSAADFEDFLEPRPDLPLTMEQE-LEPVVRHLVEQRWPFRLHATYDESISRMLDVFEKVNRDIPF 364
Cdd:pfam07969 213 RIGAMKLFADGVLGSRTAALTEPYFDAPGTGWPDFEDEaLAELVAAARERGLDVAIHAIGDATIDTALDAFEAVAEKLGN 292

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948188955  365 NGLPwFFDHAETI---TPKNIERVRALGGGIAIQDRMAFQGEYFV-ERYGAKAAEATPPIKRMLAEGVPVGAGTDAtRVS 440
Cdd:pfam07969 293 QGRV-RIEHAQGVvpyTYSQIERVAALGGAAGVQPVFDPLWGDWLqDRLGAERARGLTPVKELLNAGVKVALGSDA-PVG 370

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948188955  441 SYNPWTSLYWMVSGRTVGGLELH--AEGLPRLTALELFTHGSAWFSSEQGKKGQIKVGQLADVAALSADFFSVDEEAIKW 518
Cdd:pfam07969 371 PFDPWPRIGAAVMRQTAGGGEVLgpDEELSLEEALALYTSGPAKALGLEDRKGTLGVGKDADLVVLDDDPLTVDPPAIAD 450

                         490
                  ....*....|....
gi 948188955  519 IESVLTVVGGKVVY 532
Cdd:pfam07969 451 IRVRLTVVDGRVVY 464
PRK09237 PRK09237
amidohydrolase/deacetylase family metallohydrolase;
5-69 2.36e-08

amidohydrolase/deacetylase family metallohydrolase;


Pssm-ID: 236423 [Multi-domain]  Cd Length: 380  Bit Score: 56.40  E-value: 2.36e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 948188955   5 LILFNGqfHTVDRENP--RATAVAIRDGRFVAVGTDGEAmalrGSGTQVIDLKGRTVIPGLNDSHLH 69
Cdd:PRK09237   1 LLLRGG--RVIDPANGidGVIDIAIEDGKIAAVAGDIDG----SQAKKVIDLSGLYVSPGWIDLHVH 61
 
Name Accession Description Interval E-value
YtcJ_like cd01300
YtcJ_like metal dependent amidohydrolases. YtcJ is a Bacillus subtilis ORF of unknown function. ...
 24-502 1.20e-163

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: 476.03  E-value: 1.20e-163
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948188955  24 AVAIRDGRFVAVGTDGEAMALRGSGTQVIDLKGRTVIPGLNDSHLHLIRGGLnYNLELRWEGVPSLADALRMLKDQADRT 103
Cdd:cd01300    1 AVAVRDGRIVAVGSDAEAKALKGPATEVIDLKGKTVLPGFIDSHSHLLLGGL-SLLWLDLSGVTSKEEALARIREDAAAA 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948188955 104 PTPQWVRvVGGWNEFQFAEKRMPTLEELNQAAPDTPVFVLHL-YDRALLNRAALRVAGYTKDTPNPPGGEIVRDSHGNPT 182
Cdd:cd01300   80 PPGEWIL-GFGWDESLLGEGRYPTRAELDAVSPDRPVLLLRRdGHSAWVNSAALRLAGITRDTPDPPGGEIVRDADGEPT 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948188955 183 GMLVARPNAMILYSTlakgPKLPLEYQVNSTRQFMRELNRLGLTSAIDAGGGfqnYPDDYAVIEQLAKDQQLTVRIAYNL 262
Cdd:cd01300  159 GVLVEAAAALVLEAV----PPPTPEERRAALRAAARELASLGVTTVHDAGGG---AADDIEAYRRLAAAGELTLRVRVAL 231

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948188955 263 FTQKPKEELSDF----KNWTGSVTLHQGDDYLRHNGAGEmlVFSAADFEDFLEPRPD--LPLTMEQELEPVVRHLVEQRW 336
Cdd:cd01300  232 YVSPLAEDLLEElgarKNGAGDDRLRLGGVKLFADGSLG--SRTAALSEPYLDSPGTggLLLISPEELEELVRAADEAGL 309

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948188955 337 PFRLHATYDESISRMLDVFEKVNRDIPFNGLPWFFDHAETITPKNIERVRALGGGIAIQDRMAFQGEYFVERY--GAKAA 414
Cdd:cd01300  310 QVAIHAIGDRAVDTVLDALEAALKDNPRADHRHRIEHAQLVSPDDIPRFAKLGVIASVQPNHLYSDGDAAEDRrlGEERA 389

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948188955 415 EATPPIKRMLAEGVPVGAGTDATrVSSYNPWTSLYWMVSGRTVGGLELH--AEGLPRLTALELFTHGSAWFSSEQGKKGQ 492
Cdd:cd01300  390 KRSYPFRSLLDAGVPVALGSDAP-VAPPDPLLGIWAAVTRKTPGGGVLGnpEERLSLEEALRAYTIGAAYAIGEEDEKGS 468

                        490
                 ....*....|
gi 948188955 493 IKVGQLADVA 502
Cdd:cd01300  469 LEPGKLADFV 478
YtcJ COG1574
Predicted amidohydrolase YtcJ [General function prediction only];
3-535 3.98e-152

Predicted amidohydrolase YtcJ [General function prediction only];


Pssm-ID: 441182 [Multi-domain]  Cd Length: 535  Bit Score: 448.86  E-value: 3.98e-152
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948188955   3 ADLILFNGQFHTVDRENPRATAVAIRDGRFVAVGTDGEAMALRGSGTQVIDLKGRTVIPGLNDSHLHLIRGGLNyNLELR 82
Cdd:COG1574    8 ADLLLTNGRIYTMDPAQPVAEAVAVRDGRIVAVGSDAEVRALAGPATEVIDLGGKTVLPGFIDAHVHLLGGGLA-LLGVD 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948188955  83 WEGVPSLADALRMLKDQADRTPTPQWVrVVGGWNEFQFAEKRMPTLEELNQAAPDTPVFVLHlYDR--ALLNRAALRVAG 160
Cdd:COG1574   87 LSGARSLDELLARLRAAAAELPPGEWI-LGRGWDESLWPEGRFPTRADLDAVSPDRPVVLTR-VDGhaAWVNSAALELAG 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948188955 161 YTKDTPNPPGGEIVRDSHGNPTGMLVArpNAMILYSTLAkgPKLPLEYQVNSTRQFMRELNRLGLTSAIDAGGGfqnyPD 240
Cdd:COG1574  165 ITADTPDPEGGEIERDADGEPTGVLRE--AAMDLVRAAI--PPPTPEELRAALRAALRELASLGITSVHDAGLG----PD 236

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948188955 241 DYAVIEQLAKDQQLTVRIAYNLFTQkpKEELSDFKNWtgSVTLHQGDDYLRHNGA-----GEMLVFSAAdfedFLEPRPD 315
Cdd:COG1574  237 DLAAYRELAAAGELPLRVVLYLGAD--DEDLEELLAL--GLRTGYGDDRLRVGGVklfadGSLGSRTAA----LLEPYAD 308

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948188955 316 LP-----LTMEQE-LEPVVRHLVEQRWPFRLHATYDESISRMLDVFEKVNRDIPFNGLPWFFDHAETITPKNIERVRALG 389
Cdd:COG1574  309 DPgnrglLLLDPEeLRELVRAADAAGLQVAVHAIGDAAVDEVLDAYEAARAANGRRDRRHRIEHAQLVDPDDLARFAELG 388

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948188955 390 GGIAIQDR-MAFQGEYFVERYGAKAAEATPPIKRMLAEGVPVGAGTDATrVSSYNPWTSLYWMVSGRTVGGLELHA-EGL 467
Cdd:COG1574  389 VIASMQPThATSDGDWAEDRLGPERAARAYPFRSLLDAGAPLAFGSDAP-VEPLDPLLGIYAAVTRRTPSGRGLGPeERL 467

                        490       500       510       520       530       540
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 948188955 468 PRLTALELFTHGSAWFSSEQGKKGQIKVGQLADVAALSADFFSVDEEAIKWIESVLTVVGGKVVYGAG 535
Cdd:COG1574  468 TVEEALRAYTIGAAYAAFEEDEKGSLEPGKLADFVVLDRDPLTVPPEEIKDIKVLLTVVGGRVVYEAE 535
Amidohydro_3 pfam07969
Amidohydrolase family;
50-532 2.31e-122

Amidohydrolase family;


Pssm-ID: 400360 [Multi-domain]  Cd Length: 464  Bit Score: 369.94  E-value: 2.31e-122
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948188955   50 QVIDLKGRTVIPGLNDSHLHLIRGGLNYNlELRWEGVPSLADalrmLKDQADRTPTPQWvRVVGGWNEFQFAEKRMP-TL 128
Cdd:pfam07969   1 EVIDAKGRLVLPGFVDPHTHLDGGGLNLR-ELRLPDVLPNAV----VKGQAGRTPKGRW-LVGEGWDEAQFAETRFPyAL 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948188955  129 EELNQAAPDTPVFVLHL-YDRALLNRAALRVAGYTKDTPNPPGGEIVRDSHGN-PTGMLVARPNAMilystlakGPKLPL 206
Cdd:pfam07969  75 ADLDEVAPDGPVLLRALhTHAAVANSAALDLAGITKATEDPPGGEIARDANGEgLTGLLREGAYAL--------PPLLAR 146

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948188955  207 EYQVNSTRQFMRELNRLGLTSaIDAGGGFQNYPDDYAVIEQLAKdqqltvriaynlfTQKPKEELSDFKNWTGSVTLHQ- 285
Cdd:pfam07969 147 EAEAAAVAAALAALPGFGITS-VDGGGGNVHSLDDYEPLRELTA-------------AEKLKELLDAPERLGLPHSIYEl 212

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948188955  286 GDDYLRHNGAGEMLVFSAADFEDFLEPRPDLPLTMEQE-LEPVVRHLVEQRWPFRLHATYDESISRMLDVFEKVNRDIPF 364
Cdd:pfam07969 213 RIGAMKLFADGVLGSRTAALTEPYFDAPGTGWPDFEDEaLAELVAAARERGLDVAIHAIGDATIDTALDAFEAVAEKLGN 292

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948188955  365 NGLPwFFDHAETI---TPKNIERVRALGGGIAIQDRMAFQGEYFV-ERYGAKAAEATPPIKRMLAEGVPVGAGTDAtRVS 440
Cdd:pfam07969 293 QGRV-RIEHAQGVvpyTYSQIERVAALGGAAGVQPVFDPLWGDWLqDRLGAERARGLTPVKELLNAGVKVALGSDA-PVG 370

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948188955  441 SYNPWTSLYWMVSGRTVGGLELH--AEGLPRLTALELFTHGSAWFSSEQGKKGQIKVGQLADVAALSADFFSVDEEAIKW 518
Cdd:pfam07969 371 PFDPWPRIGAAVMRQTAGGGEVLgpDEELSLEEALALYTSGPAKALGLEDRKGTLGVGKDADLVVLDDDPLTVDPPAIAD 450

                         490
                  ....*....|....
gi 948188955  519 IESVLTVVGGKVVY 532
Cdd:pfam07969 451 IRVRLTVVDGRVVY 464
HutI COG1228
Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport ...
 1-534 3.17e-19

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


Pssm-ID: 440841 [Multi-domain]  Cd Length: 386  Bit Score: 90.02  E-value: 3.17e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948188955   1 MNADLILFNGQFHTVDRENPRA-TAVAIRDGRFVAVGTDGEAMAlrGSGTQVIDLKGRTVIPGLNDSHLHLirgglnynl 79
Cdd:COG1228    6 QAGTLLITNATLVDGTGGGVIEnGTVLVEDGKIAAVGPAADLAV--PAGAEVIDATGKTVLPGLIDAHTHL--------- 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948188955  80 elrwegvpsladalrmlkdqadrtptpqwvrVVGGWNEFQFAEKrmptleelnqaapDTPVFVLHLYDRALLNRAALRVA 159
Cdd:COG1228   75 -------------------------------GLGGGRAVEFEAG-------------GGITPTVDLVNPADKRLRRALAA 110

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948188955 160 GYTkdtpnppggeIVRDSHGNPTGMLVArpnamilystlakgpklpleyqVNSTRQFMRELNRLgLTS--AIDAGGGFQN 237
Cdd:COG1228  111 GVT----------TVRDLPGGPLGLRDA----------------------IIAGESKLLPGPRV-LAAgpALSLTGGAHA 157

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948188955 238 -YPDDyavIEQLAKDQqltvriaynlftqkpkeelsdfknwtgsvtLHQGDDYLRHNGAGEMLVFSAAdfedfleprpdl 316
Cdd:COG1228  158 rGPEE---ARAALREL------------------------------LAEGADYIKVFAEGGAPDFSLE------------ 192

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948188955 317 pltmeqELEPVVRHLVEQRWPFRLHATYDESISRML----DVFEkvnrdipfnglpwffdHAETITPKNIERVRA----- 387
Cdd:COG1228  193 ------ELRAILEAAHALGLPVAAHAHQADDIRLAVeagvDSIE----------------HGTYLDDEVADLLAEagtvv 250

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948188955 388 LGGGIAIQDRMAFQGEYFVERYGAKAAEAT-PPIKRMLAEGVPVGAGTDATRVssYNPWTSLYWMVSgrtvgglELHAEG 466
Cdd:COG1228  251 LVPTLSLFLALLEGAAAPVAAKARKVREAAlANARRLHDAGVPVALGTDAGVG--VPPGRSLHRELA-------LAVEAG 321

                        490       500       510       520       530       540
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 948188955 467 LPRLTALELFTHGSAWFSSEQGKKGQIKVGQLADVAALSADFFSvDEEAIKWIESVltVVGGKVVYGA 534
Cdd:COG1228  322 LTPEEALRAATINAAKALGLDDDVGSLEPGKLADLVLLDGDPLE-DIAYLEDVRAV--MKDGRVVDRS 386
Imidazolone-5PH cd01296
Imidazolonepropionase/imidazolone-5-propionate hydrolase (Imidazolone-5PH) catalyzes the third ...
 25-87 2.93e-10

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: 62.28  E-value: 2.93e-10
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 948188955  25 VAIRDGRFVAVGTDGEAMALRGSGTQVIDLKGRTVIPGLNDSHLHLIRGGLNYN-LELRWEGVP 87
Cdd:cd01296    1 IAIRDGRIAAVGPAASLPAPGPAAAEEIDAGGRAVTPGLVDCHTHLVFAGDRVDeFAARLAGAS 64
COG3964 COG3964
Predicted amidohydrolase [General function prediction only];
4-92 6.69e-10

Predicted amidohydrolase [General function prediction only];


Pssm-ID: 443164 [Multi-domain]  Cd Length: 376  Bit Score: 61.34  E-value: 6.69e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948188955   4 DLILFNGqfHTVDREN--PRATAVAIRDGRFVAVGTDGEAmalrGSGTQVIDLKGRTVIPGLNDSHLHLIRGGLNYNLEL 81
Cdd:COG3964    1 DLLIKGG--RVIDPANgiDGVMDIAIKDGKIAAVAKDIDA----AEAKKVIDASGLYVTPGLIDLHTHVFPGGTDYGVDP 74

                         90
                 ....*....|....*
gi 948188955  82 RWEGVPS----LADA 92
Cdd:COG3964   75 DGVGVRSgvttVVDA 89
AdeC COG1001
Adenine deaminase [Nucleotide transport and metabolism];
3-69 2.34e-09

Adenine deaminase [Nucleotide transport and metabolism];


Pssm-ID: 440625 [Multi-domain]  Cd Length: 559  Bit Score: 60.11  E-value: 2.34e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 948188955   3 ADLILFNGQFHTVDRENPRATAVAIRDGRFVAVGTdgeamaLRGSGTQVIDLKGRTVIPGLNDSHLH 69
Cdd:COG1001    5 ADLVIKNGRLVNVFTGEILEGDIAIAGGRIAGVGD------YIGEATEVIDAAGRYLVPGFIDGHVH 65
SsnA COG0402
Cytosine/adenosine deaminase or related metal-dependent hydrolase [Nucleotide transport and ...
 4-73 5.83e-09

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


Pssm-ID: 440171 [Multi-domain]  Cd Length: 416  Bit Score: 58.30  E-value: 5.83e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 948188955   4 DLILFNGQFHTVDRENP--RATAVAIRDGRFVAVGTDGEAMAlRGSGTQVIDLKGRTVIPGLNDSHLH----LIRG 73
Cdd:COG0402    1 DLLIRGAWVLTMDPAGGvlEDGAVLVEDGRIAAVGPGAELPA-RYPAAEVIDAGGKLVLPGLVNTHTHlpqtLLRG 75
PRK09237 PRK09237
amidohydrolase/deacetylase family metallohydrolase;
5-69 2.36e-08

amidohydrolase/deacetylase family metallohydrolase;


Pssm-ID: 236423 [Multi-domain]  Cd Length: 380  Bit Score: 56.40  E-value: 2.36e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 948188955   5 LILFNGqfHTVDRENP--RATAVAIRDGRFVAVGTDGEAmalrGSGTQVIDLKGRTVIPGLNDSHLH 69
Cdd:PRK09237   1 LLLRGG--RVIDPANGidGVIDIAIEDGKIAAVAGDIDG----SQAKKVIDLSGLYVSPGWIDLHVH 61
AllB COG0044
Dihydroorotase or related cyclic amidohydrolase [Nucleotide transport and metabolism]; ...
 15-70 1.33e-07

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: 54.33  E-value: 1.33e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 948188955  15 VDRENPRATAVAIRDGRFVAVGTDGEAmalrGSGTQVIDLKGRTVIPGLNDSHLHL 70
Cdd:COG0044    8 VDPGGLERADVLIEDGRIAAIGPDLAA----PEAAEVIDATGLLVLPGLIDLHVHL 59
PRK08044 PRK08044
allantoinase AllB;
1-85 1.52e-07

allantoinase AllB;


Pssm-ID: 169193 [Multi-domain]  Cd Length: 449  Bit Score: 54.09  E-value: 1.52e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948188955   1 MNADLILFNGqfhTVDREN-PRATAVAIRDGRFVAVGTDgeamalRGSGTQVIDLKGRTVIPGLNDSHLHLIRGGLNYnl 79
Cdd:PRK08044   1 MSFDLIIKNG---TVILENeARVVDIAVKGGKIAAIGQD------LGDAKEVMDASGLVVSPGMVDAHTHISEPGRSH-- 69


                 ....*.
gi 948188955  80 elrWEG 85
Cdd:PRK08044  70 ---WEG 72
ATZ_TRZ_like cd01298
TRZ/ATZ family contains enzymes from the atrazine degradation pathway and related hydrolases. ...
 24-70 7.07e-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: 51.82  E-value: 7.07e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 948188955  24 AVAIRDGRFVAVGTDGEAMAlrGSGTQVIDLKGRTVIPGLNDSHLHL 70
Cdd:cd01298   21 DVLVEDGRIVAVGPALPLPA--YPADEVIDAKGKVVMPGLVNTHTHL 65
PRK05985 PRK05985
cytosine deaminase; Provisional
 21-70 7.68e-07

cytosine deaminase; Provisional


Pssm-ID: 180337 [Multi-domain]  Cd Length: 391  Bit Score: 51.86  E-value: 7.68e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 948188955  21 RATAVAIRDGRFVAVGTDGEAMAlrgsGTQVIDLKGRTVIPGLNDSHLHL 70
Cdd:PRK05985  15 AAVDILIRDGRIAAIGPALAAPP----GAEVEDGGGALALPGLVDGHIHL 60
L-HYD_ALN cd01315
L-Hydantoinases (L-HYDs) and Allantoinase (ALN); L-Hydantoinases are a member of the ...
 4-85 8.16e-07

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: 51.91  E-value: 8.16e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948188955   4 DLILFNGQFHTVDREnpRATAVAIRDGRFVAVGTDGEamalRGSGTQVIDLKGRTVIPGLNDSHLHLIRGGLNynlelRW 83
Cdd:cd01315    1 DLVIKNGRVVTPDGV--READIAVKGGKIAAIGPDIA----NTEAEEVIDAGGLVVMPGLIDTHVHINEPGRT-----EW 69


                 ..
gi 948188955  84 EG 85
Cdd:cd01315   70 EG 71
PRK06038 PRK06038
N-ethylammeline chlorohydrolase; Provisional
 2-73 9.64e-07

N-ethylammeline chlorohydrolase; Provisional


Pssm-ID: 180363 [Multi-domain]  Cd Length: 430  Bit Score: 51.67  E-value: 9.64e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 948188955   2 NADLILFNGQFHTVDRENPRATAVAIRDGRFVAVGTDGEamalrGSGTQVIDLKGRTVIPGLNDSHLH----LIRG 73
Cdd:PRK06038   1 MADIIIKNAYVLTMDAGDLKKGSVVIEDGTITEVSESTP-----GDADTVIDAKGSVVMPGLVNTHTHaamtLFRG 71
D-aminoacylase cd01297
D-aminoacylases (N-acyl-D-Amino acid amidohydrolases) catalyze the hydrolysis of ...
 4-84 1.32e-06

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: 51.14  E-value: 1.32e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948188955   4 DLILFNGqfHTVDRE-NPRATA-VAIRDGRFVAVGTDgeamaLRGSGTQVIDLKGRTVIPGLNDSHLHlirgglnYNLEL 81
Cdd:cd01297    1 DLVIRNG--TVVDGTgAPPFTAdVGIRDGRIAAIGPI-----LSTSAREVIDAAGLVVAPGFIDVHTH-------YDGQV 66


                 ...
gi 948188955  82 RWE 84
Cdd:cd01297   67 FWD 69
PRK09060 PRK09060
dihydroorotase; Validated
 1-75 2.17e-06

dihydroorotase; Validated


Pssm-ID: 181632 [Multi-domain]  Cd Length: 444  Bit Score: 50.30  E-value: 2.17e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 948188955   1 MNADLILFNGQFHTVDRENPRAtaVAIRDGRFVAVGTDGEAMALRgsgtqVIDLKGRTVIPGLNDSHLHLIRGGL 75
Cdd:PRK09060   3 QTFDLILKGGTVVNPDGEGRAD--IGIRDGRIAAIGDLSGASAGE-----VIDCRGLHVLPGVIDSQVHFREPGL 70
PRK12394 PRK12394
metallo-dependent hydrolase;
1-92 8.69e-06

metallo-dependent hydrolase;


Pssm-ID: 183497 [Multi-domain]  Cd Length: 379  Bit Score: 48.22  E-value: 8.69e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948188955   1 MNADLILFNGQFHTVDRENPRATAVAIRDGRFVAVGTDGEAMAlrgsgTQVIDLKGRTVIPGLNDSHLHLIRGG----LN 76
Cdd:PRK12394   1 MKNDILITNGHIIDPARNINEINNLRIINDIIVDADKYPVASE-----TRIIHADGCIVTPGLIDYHAHVFYDGteggVR 75

                         90
                 ....*....|....*.
gi 948188955  77 YNLELRWEGVPSLADA 92
Cdd:PRK12394  76 PDMYMPPNGVTTVVDA 91
D-HYD cd01314
D-hydantoinases (D-HYD) also called dihydropyrimidases (DHPase) and related proteins; DHPases ...
 5-70 2.62e-05

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: 46.83  E-value: 2.62e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 948188955   5 LILFNGQFHTVDreNPRATAVAIRDGRFVAVGTDGEAmalrGSGTQVIDLKGRTVIPGLNDSHLHL 70
Cdd:cd01314    1 LIIKNGTIVTAD--GSFKADILIEDGKIVAIGPNLEA----PGGVEVIDATGKYVLPGGIDPHTHL 60
NagA cd00854
N-acetylglucosamine-6-phosphate deacetylase, NagA, catalyzes the hydrolysis of the N-acetyl ...
 24-94 3.27e-05

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: 46.42  E-value: 3.27e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 948188955  24 AVAIRDGRFVAVGTDGEAMAlrgsGTQVIDLKGRTVIPGLNDSHLHlirGGLNYNL-ELRWEGVPSLADALR 94
Cdd:cd00854   18 AVLVEDGKIVAIGPEDELEE----ADEIIDLKGQYLVPGFIDIHIH---GGGGADFmDGTAEALKTIAEALA 82
PRK13404 PRK13404
dihydropyrimidinase; Provisional
 11-70 3.70e-05

dihydropyrimidinase; Provisional


Pssm-ID: 184033 [Multi-domain]  Cd Length: 477  Bit Score: 46.61  E-value: 3.70e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 948188955  11 QFHTVDRENPRATA-------VAIRDGRFVAVGTDgeamalRGSGTQVIDLKGRTVIPGLNDSHLHL 70
Cdd:PRK13404   3 AFDLVIRGGTVVTAtdtfqadIGIRGGRIAALGEG------LGPGAREIDATGRLVLPGGVDSHCHI 63
NagA COG1820
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism];
6-94 4.49e-05

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


Pssm-ID: 441425 [Multi-domain]  Cd Length: 373  Bit Score: 45.86  E-value: 4.49e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948188955   6 ILFNGQFHTVDRENPRAtAVAIRDGRFVAVGTDGEAmalrgsGTQVIDLKGRTVIPGLNDSHLHlirGGLNYNL-ELRWE 84
Cdd:COG1820    1 AITNARIFTGDGVLEDG-ALLIEDGRIAAIGPGAEP------DAEVIDLGGGYLAPGFIDLHVH---GGGGVDFmDGTPE 70

                         90
                 ....*....|
gi 948188955  85 GVPSLADALR 94
Cdd:COG1820   71 ALRTIARAHA 80
PRK08204 PRK08204
hypothetical protein; Provisional
 25-73 4.77e-05

hypothetical protein; Provisional


Pssm-ID: 181288 [Multi-domain]  Cd Length: 449  Bit Score: 46.15  E-value: 4.77e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 948188955  25 VAIRDGRFVAVGTdgeamALRGSGTQVIDLKGRTVIPGLNDSHLHL----IRG 73
Cdd:PRK08204  26 ILIEGDRIAAVAP-----SIEAPDAEVVDARGMIVMPGLVDTHRHTwqsvLRG 73
PRK08323 PRK08323
phenylhydantoinase; Validated
 25-70 8.08e-05

phenylhydantoinase; Validated


Pssm-ID: 236240 [Multi-domain]  Cd Length: 459  Bit Score: 45.55  E-value: 8.08e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 948188955  25 VAIRDGRFVAVGTDgeamalrgSGTQVIDLKGRTVIPGLNDSHLHL 70
Cdd:PRK08323  21 VLIEDGKIAAIGAN--------LGDEVIDATGKYVMPGGIDPHTHM 58
PRK09228 PRK09228
guanine deaminase; Provisional
 24-69 1.13e-04

guanine deaminase; Provisional


Pssm-ID: 236419 [Multi-domain]  Cd Length: 433  Bit Score: 44.80  E-value: 1.13e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 948188955  24 AVAIRDGRFVAVGTDGEAMALRGSGTQVIDLKGRTVIPGLNDSHLH 69
Cdd:PRK09228  33 LLLVEDGRIVAAGPYAELRAQLPADAEVTDYRGKLILPGFIDTHIH 78
Met_dep_hydrolase_B cd01307
Metallo-dependent hydrolases, subgroup B is part of the superfamily of metallo-dependent ...
 24-88 1.99e-04

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


Pssm-ID: 238632 [Multi-domain]  Cd Length: 338  Bit Score: 43.86  E-value: 1.99e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 948188955  24 AVAIRDGRFVAVGTDGEAmalrGSGTQVIDLKGRTVIPGLNDSHLHLIRGGLNYNLELRWEGVPS 88
Cdd:cd01307    1 DVAIENGKIAAVGAALAA----PAATQIVDAGGCYVSPGWIDLHVHVYQGGTRYGDRPDMIGVKS 61
PRK07203 PRK07203
putative aminohydrolase SsnA;
5-73 3.25e-04

putative aminohydrolase SsnA;


Pssm-ID: 235963 [Multi-domain]  Cd Length: 442  Bit Score: 43.39  E-value: 3.25e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 948188955   5 LILFNGQFHTVDRENP--RATAVAIRDGRFVAVGTDGEaMALRGSGTQVIDLKGRTVIPGLNDSHLH----LIRG 73
Cdd:PRK07203   2 LLIGNGTAITRDPAKPviEDGAIAIEGNVIVEIGTTDE-LKAKYPDAEFIDAKGKLIMPGLINSHNHiysgLARG 75
Bact_CD cd01293
Bacterial cytosine deaminase and related metal-dependent hydrolases. Cytosine deaminases (CDs) ...
 25-70 3.40e-04

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: 43.39  E-value: 3.40e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 948188955  25 VAIRDGRFVAVGTDGEAmalrGSGTQVIDLKGRTVIPGLNDSHLHL 70
Cdd:cd01293   17 IAIEDGRIAAIGPALAV----PPDAEEVDAKGRLVLPAFVDPHIHL 58
pyrC PRK09357
dihydroorotase; Validated
 1-70 3.74e-04

dihydroorotase; Validated


Pssm-ID: 236479 [Multi-domain]  Cd Length: 423  Bit Score: 43.26  E-value: 3.74e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948188955   1 MNADLILFNGQFHTVDrenprataVAIRDGRFVAVGTDGEamalrGSGTQVIDLKGRTVIPGLNDSHLHL 70
Cdd:PRK09357   6 KNGRVIDPKGLDEVAD--------VLIDDGKIAAIGENIE-----AEGAEVIDATGLVVAPGLVDLHVHL 62
PRK09045 PRK09045
TRZ/ATZ family hydrolase;
24-73 5.43e-04

TRZ/ATZ family hydrolase;


Pssm-ID: 236366 [Multi-domain]  Cd Length: 443  Bit Score: 42.59  E-value: 5.43e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 948188955  24 AVAIRDGRFVAVGTDGEAMAlRGSGTQVIDLKGRTVIPGLNDSHLH----LIRG 73
Cdd:PRK09045  30 AVAIRDGRIVAILPRAEARA-RYAAAETVELPDHVLIPGLINAHTHaamsLLRG 82
PRK08203 PRK08203
hydroxydechloroatrazine ethylaminohydrolase; Reviewed
 14-70 6.73e-04

hydroxydechloroatrazine ethylaminohydrolase; Reviewed


Pssm-ID: 236184 [Multi-domain]  Cd Length: 451  Bit Score: 42.53  E-value: 6.73e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 948188955  14 TVD---RENPRAtAVAIRDGRFVAVGTDGeamALRGSGTQVIDLKGRTVIPGLNDSHLHL 70
Cdd:PRK08203  13 TMDaarREIADG-GLVVEGGRIVEVGPGG---ALPQPADEVFDARGHVVTPGLVNTHHHF 68
PRK09061 PRK09061
D-glutamate deacylase; Validated
 4-69 7.44e-04

D-glutamate deacylase; Validated


Pssm-ID: 236369 [Multi-domain]  Cd Length: 509  Bit Score: 42.37  E-value: 7.44e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 948188955   4 DLILFNGQfhTVDRE-NPRATA-VAIRDGRFVAVGTDGeamalrGSGTQVIDLKGRTVIPGLNDSHLH 69
Cdd:PRK09061  20 DLVIRNGR--VVDPEtGLDAVRdVGIKGGKIAAVGTAA------IEGDRTIDATGLVVAPGFIDLHAH 79
PRK06189 PRK06189
allantoinase; Provisional
 1-93 7.68e-04

allantoinase; Provisional


Pssm-ID: 235732 [Multi-domain]  Cd Length: 451  Bit Score: 42.38  E-value: 7.68e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948188955   1 MNADLILFNGQfhTVDRENPRATAVAIRDGRFVAVGTDgeamaLRGSGTQVIDLKGRTVIPGLNDSHLHLIRGGLNYnle 80
Cdd:PRK06189   1 MMYDLIIRGGK--VVTPEGVYRADIGIKNGKIAEIAPE-----ISSPAREIIDADGLYVFPGMIDVHVHFNEPGRTH--- 70

                         90
                 ....*....|...
gi 948188955  81 lrWEGVPSLADAL 93
Cdd:PRK06189  71 --WEGFATGSAAL 81
PLN02795 PLN02795
allantoinase
 21-88 8.92e-04

allantoinase


Pssm-ID: 178392 [Multi-domain]  Cd Length: 505  Bit Score: 42.07  E-value: 8.92e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 948188955  21 RATAVAIRDGRFVAVgTDGEAMALRGSGTQVIDLKGRTVIPGLNDSHLHLIRGGlnynlELRWEGVPS 88
Cdd:PLN02795  60 IPGAVEVEGGRIVSV-TKEEEAPKSQKKPHVLDYGNAVVMPGLIDVHVHLNEPG-----RTEWEGFPT 121
Met_dep_hydrolase_A cd01299
Metallo-dependent hydrolases, subgroup A is part of the superfamily of metallo-dependent ...
 50-94 1.21e-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: 41.51  E-value: 1.21e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 948188955  50 QVIDLKGRTVIPGLNDSHLHL--IRGGLNYNLEL-----RWEGVPSLADALR 94
Cdd:cd01299    2 QVIDLGGKTLMPGLIDAHTHLgsDPGDLPLDLALpveyrTIRATRQARAALR 53
ureC PRK13206
urease subunit alpha; Reviewed
 25-71 2.17e-03

urease subunit alpha; Reviewed


Pssm-ID: 237304 [Multi-domain]  Cd Length: 573  Bit Score: 40.85  E-value: 2.17e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 948188955  25 VAIRDGRFVAVG-------TDGEAMALR-GSGTQVIDLKGRTVIPGLNDSHLHLI 71
Cdd:PRK13206  91 VGIRDGRIVAIGkagnpdiMDGVHPDLViGPSTEIIAGNGRILTAGAIDCHVHFI 145
PRK02382 PRK02382
dihydroorotase; Provisional
 4-69 2.23e-03

dihydroorotase; Provisional


Pssm-ID: 179417 [Multi-domain]  Cd Length: 443  Bit Score: 40.79  E-value: 2.23e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 948188955   4 DLILFNGQFHTVDRENPRAtaVAIRDGRFVAVGTDgeamaLRGS-GTQVIDLKGRTVIPGLNDSHLH 69
Cdd:PRK02382   3 DALLKDGRVYYNNSLQPRD--VRIDGGKITAVGKD-----LDGSsSEEVIDARGMLLLPGGIDVHVH 62
PRK07228 PRK07228
5'-deoxyadenosine deaminase;
1-70 2.61e-03

5'-deoxyadenosine deaminase;


Pssm-ID: 180895 [Multi-domain]  Cd Length: 445  Bit Score: 40.75  E-value: 2.61e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948188955   1 MNADLILFNGqfhtvdrenpratAVAIRDGRFVAVGTDGEAMALRgsgtQVIDLKGRTVIPGLNDSHLHL 70
Cdd:PRK07228  13 MNAKREIVDG-------------DVLIEDDRIAAVGDRLDLEDYD----DHIDATGKVVIPGLIQGHIHL 65
ureC PRK13207
urease subunit alpha; Reviewed
 25-71 2.86e-03

urease subunit alpha; Reviewed


Pssm-ID: 237305 [Multi-domain]  Cd Length: 568  Bit Score: 40.55  E-value: 2.86e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 948188955  25 VAIRDGRFVAVG-------TDGEAMALrGSGTQVIDLKGRTVIPGLNDSHLHLI 71
Cdd:PRK13207  87 IGIKDGRIVAIGkagnpdiQDGVDIII-GPGTEVIAGEGLIVTAGGIDTHIHFI 139
FwdA COG1229
Formylmethanofuran dehydrogenase subunit A [Energy production and conversion];
25-74 3.60e-03

Formylmethanofuran dehydrogenase subunit A [Energy production and conversion];


Pssm-ID: 440842  Cd Length: 554  Bit Score: 40.18  E-value: 3.60e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 948188955  25 VAIRDGRFVAVGTDGEAmalrgsgTQVIDLKGRTVIPGLNDSHLHlIRGG 74
Cdd:COG1229   24 IAIKDGKIVEEPSDPKD-------AKVIDASGKVVMAGGVDIHTH-IAGG 65
ATZ_TRZ_like cd01298
TRZ/ATZ family contains enzymes from the atrazine degradation pathway and related hydrolases. ...
 412-532 5.07e-03

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: 39.49  E-value: 5.07e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948188955 412 KAAEATPPIKRMLAEGVPVGAGTDATrvSSYNpwtSLYWMVSGRTVGGLELHAEG----LPRLTALELFTHGSA-WFSSE 486
Cdd:cd01298  278 KLASGIAPVPEMLEAGVNVGLGTDGA--ASNN---NLDMFEEMRLAALLQKLAHGdptaLPAEEALEMATIGGAkALGLD 352

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 948188955 487 QGkkGQIKVGQLADVAALSAD---FFSVDEEAIKWIESV------LTVVGGKVVY 532
Cdd:cd01298  353 EI--GSLEVGKKADLILIDLDgphLLPVHDPISHLVYSAnggdvdTVIVNGRVVM 405
Met_dep_hydrolase_A cd01299
Metallo-dependent hydrolases, subgroup A is part of the superfamily of metallo-dependent ...
 420-507 5.28e-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: 39.58  E-value: 5.28e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 948188955 420 IKRMLAEGVPVGAGTDAtrvssynpwtSLYWMVSGRTVGGLELHAE-GLPRLTALELFTHGSAWFSSEQGKKGQIKVGQL 498
Cdd:cd01299  256 LRRAHKAGVKIAFGTDA----------GFPVPPHGWNARELELLVKaGGTPAEALRAATANAAELLGLSDELGVIEAGKL 325


                 ....*....
gi 948188955 499 ADVAALSAD 507
Cdd:cd01299  326 ADLLVVDGD 334
PRK07572 PRK07572
cytosine deaminase; Validated
 4-70 5.64e-03

cytosine deaminase; Validated


Pssm-ID: 181039  Cd Length: 426  Bit Score: 39.62  E-value: 5.64e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 948188955   4 DLILFNGQFHtvdrENPRATAVAIRDGRFVAVGTdgeamALRGSGTQVIDLKGRTVIPGLNDSHLHL 70
Cdd:PRK07572   3 DLIVRNANLP----DGRTGIDIGIAGGRIAAVEP-----GLQAEAAEEIDAAGRLVSPPFVDPHFHM 60
Isoaspartyl-dipeptidase cd01308
Isoaspartyl dipeptidase hydrolyzes the beta-L-isoaspartyl linkages in dipeptides, as part of ...
 50-74 8.48e-03

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: 38.91  E-value: 8.48e-03
                         10        20
                 ....*....|....*....|....*
gi 948188955  50 QVIDLKGRTVIPGLNDSHLHLIRGG 74
Cdd:cd01308   43 TVVDLHGKILVPGFIDQHVHIIGGG 67
 
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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