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Conserved domains on  [gi|446426163|ref|WP_000504018|]
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MULTISPECIES: amidohydrolase [Bacillus]

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];
4-521 0e+00

Predicted amidohydrolase YtcJ [General function prediction only];


:

Pssm-ID: 441182 [Multi-domain]  Cd Length: 535  Bit Score: 586.38  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446426163   4 IWYGGTIYTVREENEKVDAVYIENGTIVDVGSKEELENQY-AAVTLHDLKGKTMIPGLVDSHMHLIGHGERLLRLDLSNC 82
Cdd:COG1574   11 LLTNGRIYTMDPAQPVAEAVAVRDGRIVAVGSDAEVRALAgPATEVIDLGGKTVLPGFIDAHVHLLGGGLALLGVDLSGA 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446426163  83 TSYGEVLTLVQKRVEEAPKGSWIIGEGWNENNFTDTKDVHARDLDEISKEHPILLKRVCRHVTWVNAYILQEANITAATE 162
Cdd:COG1574   91 RSLDELLARLRAAAAELPPGEWILGRGWDESLWPEGRFPTRADLDAVSPDRPVVLTRVDGHAAWVNSAALELAGITADTP 170

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446426163 163 DPKGGKIGRDSSNKLTGLLYEQGQELIKHVQPEIDEAYLQRALQTAIKDCWKYGLVGGHTEDLNyyggfRKTYNAFSHVI 242
Cdd:COG1574  171 DPEGGEIERDADGEPTGVLREAAMDLVRAAIPPPTPEELRAALRAALRELASLGITSVHDAGLG-----PDDLAAYRELA 245

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446426163 243 KE--MPFKAHLLVHHEVAH--------ERKEYENEHcIEFGAMKIFSDGSFGGRTALLSEPYEDAKETNGVAIFSREELA 312
Cdd:COG1574  246 AAgeLPLRVVLYLGADDEDleellalgLRTGYGDDR-LRVGGVKLFADGSLGSRTAALLEPYADDPGNRGLLLLDPEELR 324

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446426163 313 ELVKKARDLHMPVAIHTIGDLSLEYVIDALELYP---PAEGVRDRIIHCQLAREELIERMKNLQAIIDIQPVFLSSDFPS 389
Cdd:COG1574  325 ELVRAADAAGLQVAVHAIGDAAVDEVLDAYEAARaanGRRDRRHRIEHAQLVDPDDLARFAELGVIASMQPTHATSDGDW 404

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446426163 390 VIEKLGEHRLRYAYAWKTLLEAGLHCNGGSDAPIEQVNPFLGIYSAVTRRSfIDGICYMPEERLTVYEAVSLFTTGSAYA 469
Cdd:COG1574  405 AEDRLGPERAARAYPFRSLLDAGAPLAFGSDAPVEPLDPLLGIYAAVTRRT-PSGRGLGPEERLTVEEALRAYTIGAAYA 483

                        490       500       510       520       530
                 ....*....|....*....|....*....|....*....|....*....|..
gi 446426163 470 IGKEAKRGQIAKGYEADFTILDRNIFEIEAEEIKEVQAEMTVIDGQVVYRKD 521
Cdd:COG1574  484 AFEEDEKGSLEPGKLADFVVLDRDPLTVPPEEIKDIKVLLTVVGGRVVYEAE 535
 
Name Accession Description Interval E-value
YtcJ COG1574
Predicted amidohydrolase YtcJ [General function prediction only];
4-521 0e+00

Predicted amidohydrolase YtcJ [General function prediction only];


Pssm-ID: 441182 [Multi-domain]  Cd Length: 535  Bit Score: 586.38  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446426163   4 IWYGGTIYTVREENEKVDAVYIENGTIVDVGSKEELENQY-AAVTLHDLKGKTMIPGLVDSHMHLIGHGERLLRLDLSNC 82
Cdd:COG1574   11 LLTNGRIYTMDPAQPVAEAVAVRDGRIVAVGSDAEVRALAgPATEVIDLGGKTVLPGFIDAHVHLLGGGLALLGVDLSGA 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446426163  83 TSYGEVLTLVQKRVEEAPKGSWIIGEGWNENNFTDTKDVHARDLDEISKEHPILLKRVCRHVTWVNAYILQEANITAATE 162
Cdd:COG1574   91 RSLDELLARLRAAAAELPPGEWILGRGWDESLWPEGRFPTRADLDAVSPDRPVVLTRVDGHAAWVNSAALELAGITADTP 170

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446426163 163 DPKGGKIGRDSSNKLTGLLYEQGQELIKHVQPEIDEAYLQRALQTAIKDCWKYGLVGGHTEDLNyyggfRKTYNAFSHVI 242
Cdd:COG1574  171 DPEGGEIERDADGEPTGVLREAAMDLVRAAIPPPTPEELRAALRAALRELASLGITSVHDAGLG-----PDDLAAYRELA 245

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446426163 243 KE--MPFKAHLLVHHEVAH--------ERKEYENEHcIEFGAMKIFSDGSFGGRTALLSEPYEDAKETNGVAIFSREELA 312
Cdd:COG1574  246 AAgeLPLRVVLYLGADDEDleellalgLRTGYGDDR-LRVGGVKLFADGSLGSRTAALLEPYADDPGNRGLLLLDPEELR 324

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446426163 313 ELVKKARDLHMPVAIHTIGDLSLEYVIDALELYP---PAEGVRDRIIHCQLAREELIERMKNLQAIIDIQPVFLSSDFPS 389
Cdd:COG1574  325 ELVRAADAAGLQVAVHAIGDAAVDEVLDAYEAARaanGRRDRRHRIEHAQLVDPDDLARFAELGVIASMQPTHATSDGDW 404

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446426163 390 VIEKLGEHRLRYAYAWKTLLEAGLHCNGGSDAPIEQVNPFLGIYSAVTRRSfIDGICYMPEERLTVYEAVSLFTTGSAYA 469
Cdd:COG1574  405 AEDRLGPERAARAYPFRSLLDAGAPLAFGSDAPVEPLDPLLGIYAAVTRRT-PSGRGLGPEERLTVEEALRAYTIGAAYA 483

                        490       500       510       520       530
                 ....*....|....*....|....*....|....*....|....*....|..
gi 446426163 470 IGKEAKRGQIAKGYEADFTILDRNIFEIEAEEIKEVQAEMTVIDGQVVYRKD 521
Cdd:COG1574  484 AFEEDEKGSLEPGKLADFVVLDRDPLTVPPEEIKDIKVLLTVVGGRVVYEAE 535
YtcJ_like cd01300
YtcJ_like metal dependent amidohydrolases. YtcJ is a Bacillus subtilis ORF of unknown function. ...
 22-489 1.52e-162

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: 469.87  E-value: 1.52e-162
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446426163  22 AVYIENGTIVDVGSKEELE-NQYAAVTLHDLKGKTMIPGLVDSHMHLIGHGERLLRLDLSNCTSYGEVLTLVQKRVEEAP 100
Cdd:cd01300    1 AVAVRDGRIVAVGSDAEAKaLKGPATEVIDLKGKTVLPGFIDSHSHLLLGGLSLLWLDLSGVTSKEEALARIREDAAAAP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446426163 101 KGSWIIGEGWNENNFTDTKDVHARDLDEISKEHPILLKRVCRHVTWVNAYILQEANITAATEDPKGGKIGRDSSNKLTGL 180
Cdd:cd01300   81 PGEWILGFGWDESLLGEGRYPTRAELDAVSPDRPVLLLRRDGHSAWVNSAALRLAGITRDTPDPPGGEIVRDADGEPTGV 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446426163 181 LYEQGQELIKHVQPEIDEAYLQRALQTAIKDCWKYGLVGGHTEDLNYYGGFrKTYNAFSH-VIKEMPFKAHLLVHHEV-- 257
Cdd:cd01300  161 LVEAAAALVLEAVPPPTPEERRAALRAAARELASLGVTTVHDAGGGAADDI-EAYRRLAAaGELTLRVRVALYVSPLAed 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446426163 258 ----AHERKEYENEHCIEFGAMKIFSDGSFGGRTALLSEPYEDAKETNGVAIFSREELAELVKKARDLHMPVAIHTIGDL 333
Cdd:cd01300  240 lleeLGARKNGAGDDRLRLGGVKLFADGSLGSRTAALSEPYLDSPGTGGLLLISPEELEELVRAADEAGLQVAIHAIGDR 319

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446426163 334 SLEYVIDALE-LYP--PAEGVRDRIIHCQLAREELIERMKNLQAIIDIQPVFLSSDFPSVIEK-LGEHRLRYAYAWKTLL 409
Cdd:cd01300  320 AVDTVLDALEaALKdnPRADHRHRIEHAQLVSPDDIPRFAKLGVIASVQPNHLYSDGDAAEDRrLGEERAKRSYPFRSLL 399

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446426163 410 EAGLHCNGGSDAPIEQVNPFLGIYSAVTRRSFIDGICYMPEERLTVYEAVSLFTTGSAYAIGKEAKRGQIAKGYEADFTI 489
Cdd:cd01300  400 DAGVPVALGSDAPVAPPDPLLGIWAAVTRKTPGGGVLGNPEERLSLEEALRAYTIGAAYAIGEEDEKGSLEPGKLADFVV 479
Amidohydro_3 pfam07969
Amidohydrolase family;
50-518 4.14e-148

Amidohydrolase family;


Pssm-ID: 400360 [Multi-domain]  Cd Length: 464  Bit Score: 432.73  E-value: 4.14e-148
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446426163   50 DLKGKTMIPGLVDSHMHLIGHGERLLRLDLSNCTsygeVLTLVQKRVEEAPKGSWIIGEGWNENNFTDTKDVHAR-DLDE 128
Cdd:pfam07969   4 DAKGRLVLPGFVDPHTHLDGGGLNLRELRLPDVL----PNAVVKGQAGRTPKGRWLVGEGWDEAQFAETRFPYALaDLDE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446426163  129 ISKEHPILLKRVCRHVTWVNAYILQEANITAATEDPKGGKIGRDSSNK-LTGLLYEQGQELIkhvqPEIDEAYLQRALQT 207
Cdd:pfam07969  80 VAPDGPVLLRALHTHAAVANSAALDLAGITKATEDPPGGEIARDANGEgLTGLLREGAYALP----PLLAREAEAAAVAA 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446426163  208 AIKDCWKYGLVGGhtEDLNYYGGFRKTYNAFSHVIKEMpfkahllVHHEVAHERKEYENEHCIE---FGAMKIFSDGSFG 284
Cdd:pfam07969 156 ALAALPGFGITSV--DGGGGNVHSLDDYEPLRELTAAE-------KLKELLDAPERLGLPHSIYelrIGAMKLFADGVLG 226

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446426163  285 GRTALLSEPYEDAKETnGVAIFSREELAELVKKARDLHMPVAIHTIGDLSLEYVIDALELYPPAEGVRD--RIIHCQ--- 359
Cdd:pfam07969 227 SRTAALTEPYFDAPGT-GWPDFEDEALAELVAAARERGLDVAIHAIGDATIDTALDAFEAVAEKLGNQGrvRIEHAQgvv 305

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446426163  360 LAREELIERMKNLQAIIDIQPVFLSSDFPSVIEKLGEHRLRYAYAWKTLLEAGLHCNGGSDAPIEQVNPFLGIYSAVTRR 439
Cdd:pfam07969 306 PYTYSQIERVAALGGAAGVQPVFDPLWGDWLQDRLGAERARGLTPVKELLNAGVKVALGSDAPVGPFDPWPRIGAAVMRQ 385

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446426163  440 SFIDGICYMPEERLTVYEAVSLFTTGSAYAIGKEAKRGQIAKGYEADFTILDRNIFEIEAEEIKEVQAEMTVIDGQVVY 518
Cdd:pfam07969 386 TAGGGEVLGPDEELSLEEALALYTSGPAKALGLEDRKGTLGVGKDADLVVLDDDPLTVDPPAIADIRVRLTVVDGRVVY 464
PRK07203 PRK07203
putative aminohydrolase SsnA;
22-90 1.57e-08

putative aminohydrolase SsnA;


Pssm-ID: 235963 [Multi-domain]  Cd Length: 442  Bit Score: 56.87  E-value: 1.57e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446426163  22 AVYIENGTIVDVGSKEELENQYAAVTLHDLKGKTMIPGLVDSHMHLIGHGERLLRLDLSNCTSYGEVLT 90
Cdd:PRK07203  23 AIAIEGNVIVEIGTTDELKAKYPDAEFIDAKGKLIMPGLINSHNHIYSGLARGMMANIPPPPDFISILK 91
 
Name Accession Description Interval E-value
YtcJ COG1574
Predicted amidohydrolase YtcJ [General function prediction only];
4-521 0e+00

Predicted amidohydrolase YtcJ [General function prediction only];


Pssm-ID: 441182 [Multi-domain]  Cd Length: 535  Bit Score: 586.38  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446426163   4 IWYGGTIYTVREENEKVDAVYIENGTIVDVGSKEELENQY-AAVTLHDLKGKTMIPGLVDSHMHLIGHGERLLRLDLSNC 82
Cdd:COG1574   11 LLTNGRIYTMDPAQPVAEAVAVRDGRIVAVGSDAEVRALAgPATEVIDLGGKTVLPGFIDAHVHLLGGGLALLGVDLSGA 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446426163  83 TSYGEVLTLVQKRVEEAPKGSWIIGEGWNENNFTDTKDVHARDLDEISKEHPILLKRVCRHVTWVNAYILQEANITAATE 162
Cdd:COG1574   91 RSLDELLARLRAAAAELPPGEWILGRGWDESLWPEGRFPTRADLDAVSPDRPVVLTRVDGHAAWVNSAALELAGITADTP 170

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446426163 163 DPKGGKIGRDSSNKLTGLLYEQGQELIKHVQPEIDEAYLQRALQTAIKDCWKYGLVGGHTEDLNyyggfRKTYNAFSHVI 242
Cdd:COG1574  171 DPEGGEIERDADGEPTGVLREAAMDLVRAAIPPPTPEELRAALRAALRELASLGITSVHDAGLG-----PDDLAAYRELA 245

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446426163 243 KE--MPFKAHLLVHHEVAH--------ERKEYENEHcIEFGAMKIFSDGSFGGRTALLSEPYEDAKETNGVAIFSREELA 312
Cdd:COG1574  246 AAgeLPLRVVLYLGADDEDleellalgLRTGYGDDR-LRVGGVKLFADGSLGSRTAALLEPYADDPGNRGLLLLDPEELR 324

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446426163 313 ELVKKARDLHMPVAIHTIGDLSLEYVIDALELYP---PAEGVRDRIIHCQLAREELIERMKNLQAIIDIQPVFLSSDFPS 389
Cdd:COG1574  325 ELVRAADAAGLQVAVHAIGDAAVDEVLDAYEAARaanGRRDRRHRIEHAQLVDPDDLARFAELGVIASMQPTHATSDGDW 404

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446426163 390 VIEKLGEHRLRYAYAWKTLLEAGLHCNGGSDAPIEQVNPFLGIYSAVTRRSfIDGICYMPEERLTVYEAVSLFTTGSAYA 469
Cdd:COG1574  405 AEDRLGPERAARAYPFRSLLDAGAPLAFGSDAPVEPLDPLLGIYAAVTRRT-PSGRGLGPEERLTVEEALRAYTIGAAYA 483

                        490       500       510       520       530
                 ....*....|....*....|....*....|....*....|....*....|..
gi 446426163 470 IGKEAKRGQIAKGYEADFTILDRNIFEIEAEEIKEVQAEMTVIDGQVVYRKD 521
Cdd:COG1574  484 AFEEDEKGSLEPGKLADFVVLDRDPLTVPPEEIKDIKVLLTVVGGRVVYEAE 535
YtcJ_like cd01300
YtcJ_like metal dependent amidohydrolases. YtcJ is a Bacillus subtilis ORF of unknown function. ...
 22-489 1.52e-162

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: 469.87  E-value: 1.52e-162
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446426163  22 AVYIENGTIVDVGSKEELE-NQYAAVTLHDLKGKTMIPGLVDSHMHLIGHGERLLRLDLSNCTSYGEVLTLVQKRVEEAP 100
Cdd:cd01300    1 AVAVRDGRIVAVGSDAEAKaLKGPATEVIDLKGKTVLPGFIDSHSHLLLGGLSLLWLDLSGVTSKEEALARIREDAAAAP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446426163 101 KGSWIIGEGWNENNFTDTKDVHARDLDEISKEHPILLKRVCRHVTWVNAYILQEANITAATEDPKGGKIGRDSSNKLTGL 180
Cdd:cd01300   81 PGEWILGFGWDESLLGEGRYPTRAELDAVSPDRPVLLLRRDGHSAWVNSAALRLAGITRDTPDPPGGEIVRDADGEPTGV 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446426163 181 LYEQGQELIKHVQPEIDEAYLQRALQTAIKDCWKYGLVGGHTEDLNYYGGFrKTYNAFSH-VIKEMPFKAHLLVHHEV-- 257
Cdd:cd01300  161 LVEAAAALVLEAVPPPTPEERRAALRAAARELASLGVTTVHDAGGGAADDI-EAYRRLAAaGELTLRVRVALYVSPLAed 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446426163 258 ----AHERKEYENEHCIEFGAMKIFSDGSFGGRTALLSEPYEDAKETNGVAIFSREELAELVKKARDLHMPVAIHTIGDL 333
Cdd:cd01300  240 lleeLGARKNGAGDDRLRLGGVKLFADGSLGSRTAALSEPYLDSPGTGGLLLISPEELEELVRAADEAGLQVAIHAIGDR 319

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446426163 334 SLEYVIDALE-LYP--PAEGVRDRIIHCQLAREELIERMKNLQAIIDIQPVFLSSDFPSVIEK-LGEHRLRYAYAWKTLL 409
Cdd:cd01300  320 AVDTVLDALEaALKdnPRADHRHRIEHAQLVSPDDIPRFAKLGVIASVQPNHLYSDGDAAEDRrLGEERAKRSYPFRSLL 399

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446426163 410 EAGLHCNGGSDAPIEQVNPFLGIYSAVTRRSFIDGICYMPEERLTVYEAVSLFTTGSAYAIGKEAKRGQIAKGYEADFTI 489
Cdd:cd01300  400 DAGVPVALGSDAPVAPPDPLLGIWAAVTRKTPGGGVLGNPEERLSLEEALRAYTIGAAYAIGEEDEKGSLEPGKLADFVV 479
Amidohydro_3 pfam07969
Amidohydrolase family;
50-518 4.14e-148

Amidohydrolase family;


Pssm-ID: 400360 [Multi-domain]  Cd Length: 464  Bit Score: 432.73  E-value: 4.14e-148
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446426163   50 DLKGKTMIPGLVDSHMHLIGHGERLLRLDLSNCTsygeVLTLVQKRVEEAPKGSWIIGEGWNENNFTDTKDVHAR-DLDE 128
Cdd:pfam07969   4 DAKGRLVLPGFVDPHTHLDGGGLNLRELRLPDVL----PNAVVKGQAGRTPKGRWLVGEGWDEAQFAETRFPYALaDLDE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446426163  129 ISKEHPILLKRVCRHVTWVNAYILQEANITAATEDPKGGKIGRDSSNK-LTGLLYEQGQELIkhvqPEIDEAYLQRALQT 207
Cdd:pfam07969  80 VAPDGPVLLRALHTHAAVANSAALDLAGITKATEDPPGGEIARDANGEgLTGLLREGAYALP----PLLAREAEAAAVAA 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446426163  208 AIKDCWKYGLVGGhtEDLNYYGGFRKTYNAFSHVIKEMpfkahllVHHEVAHERKEYENEHCIE---FGAMKIFSDGSFG 284
Cdd:pfam07969 156 ALAALPGFGITSV--DGGGGNVHSLDDYEPLRELTAAE-------KLKELLDAPERLGLPHSIYelrIGAMKLFADGVLG 226

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446426163  285 GRTALLSEPYEDAKETnGVAIFSREELAELVKKARDLHMPVAIHTIGDLSLEYVIDALELYPPAEGVRD--RIIHCQ--- 359
Cdd:pfam07969 227 SRTAALTEPYFDAPGT-GWPDFEDEALAELVAAARERGLDVAIHAIGDATIDTALDAFEAVAEKLGNQGrvRIEHAQgvv 305

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446426163  360 LAREELIERMKNLQAIIDIQPVFLSSDFPSVIEKLGEHRLRYAYAWKTLLEAGLHCNGGSDAPIEQVNPFLGIYSAVTRR 439
Cdd:pfam07969 306 PYTYSQIERVAALGGAAGVQPVFDPLWGDWLQDRLGAERARGLTPVKELLNAGVKVALGSDAPVGPFDPWPRIGAAVMRQ 385

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446426163  440 SFIDGICYMPEERLTVYEAVSLFTTGSAYAIGKEAKRGQIAKGYEADFTILDRNIFEIEAEEIKEVQAEMTVIDGQVVY 518
Cdd:pfam07969 386 TAGGGEVLGPDEELSLEEALALYTSGPAKALGLEDRKGTLGVGKDADLVVLDDDPLTVDPPAIADIRVRLTVVDGRVVY 464
HutI COG1228
Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport ...
 4-520 2.16e-22

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


Pssm-ID: 440841 [Multi-domain]  Cd Length: 386  Bit Score: 98.88  E-value: 2.16e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446426163   4 IWYGGTIYTVREENEKVDA-VYIENGTIVDVGSKEELENQyAAVTLHDLKGKTMIPGLVDSHMHLIGHGERLlrldlsnc 82
Cdd:COG1228   11 LITNATLVDGTGGGVIENGtVLVEDGKIAAVGPAADLAVP-AGAEVIDATGKTVLPGLIDAHTHLGLGGGRA-------- 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446426163  83 tsygevltlvqkrveeapkgswiiGEGWNENNFTDTKDVHARDLDeiskehpillkrvcrhvtwvNAYILQEANITAAtE 162
Cdd:COG1228   82 ------------------------VEFEAGGGITPTVDLVNPADK--------------------RLRRALAAGVTTV-R 116

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446426163 163 DPKGGKIGrdssnkltgllyeqgqelikhVQPEIDEAYLQRALQTAIkdcwkygLVGGHTedLNYYGGfrktynafshvi 242
Cdd:COG1228  117 DLPGGPLG---------------------LRDAIIAGESKLLPGPRV-------LAAGPA--LSLTGG------------ 154

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446426163 243 kempfkAHLLVHHEVAHE-RKEYENehciefGA--MKIFSDGsfggrtallsepyedaketnGVAIFSREELAELVKKAR 319
Cdd:COG1228  155 ------AHARGPEEARAAlRELLAE------GAdyIKVFAEG--------------------GAPDFSLEELRAILEAAH 202

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446426163 320 DLHMPVAIHTIGDLSLEYVIDAlelyppaeGVrDRIIHCQLAREELIERMKNLQAII-----DIQPVFLSSDFPSVIEKL 394
Cdd:COG1228  203 ALGLPVAAHAHQADDIRLAVEA--------GV-DSIEHGTYLDDEVADLLAEAGTVVlvptlSLFLALLEGAAAPVAAKA 273

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446426163 395 GEHRLRYAYAWKTLLEAGLHCNGGSDAPIEqvnpflgiysAVTRRSFIDGICYMPEERLTVYEAVSLFTTGSAYAIGKEA 474
Cdd:COG1228  274 RKVREAALANARRLHDAGVPVALGTDAGVG----------VPPGRSLHRELALAVEAGLTPEEALRAATINAAKALGLDD 343

                        490       500       510       520
                 ....*....|....*....|....*....|....*....|....*..
gi 446426163 475 KRGQIAKGYEADFTILDRNIFeieaEEIKEVQA-EMTVIDGQVVYRK 520
Cdd:COG1228  344 DVGSLEPGKLADLVLLDGDPL----EDIAYLEDvRAVMKDGRVVDRS 386
SsnA COG0402
Cytosine/adenosine deaminase or related metal-dependent hydrolase [Nucleotide transport and ...
 7-76 7.79e-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: 61.00  E-value: 7.79e-10
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446426163   7 GGTIYTVREENEKVD--AVYIENGTIVDVGSKEELENQYAAVTLHDLKGKTMIPGLVDSHMHLighGERLLR 76
Cdd:COG0402    6 GAWVLTMDPAGGVLEdgAVLVEDGRIAAVGPGAELPARYPAAEVIDAGGKLVLPGLVNTHTHL---PQTLLR 74
Amidohydro_1 pfam01979
Amidohydrolase family; This family of enzymes are a a large metal dependent hydrolase ...
 305-517 5.04e-09

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: 57.90  E-value: 5.04e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446426163  305 IFSREELAELVKKARDLHMPVAIHTIGDLS-LEYVI-------------DALELYPPAEGVRDRIIHCQLAREELIERMK 370
Cdd:pfam01979 123 TFSDDELKAALEEAKKYGLPVAIHALETKGeVEDAIaafgggiehgthlEVAESGGLLDIIKLILAHGVHLSPTEANLLA 202

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446426163  371 NLQAIIDIqpvflsSDFPSVIEKLGEHRLryayAWKTLLEAGLHCNGGSDAPIEQVNPflgiysavtrrSFIDGICYM-- 448
Cdd:pfam01979 203 EHLKGAGV------AHCPFSNSKLRSGRI----ALRKALEDGVKVGLGTDGAGSGNSL-----------NMLEELRLAle 261

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446426163  449 ----PEERLTVYEAVSLFTTGSAYAIGKEAKRGQIAKGYEADFTILDRNIFEIEAEEIKEVQAEMTVIDGQVV 517
Cdd:pfam01979 262 lqfdPEGGLSPLEALRMATINPAKALGLDDKVGSIEVGKDADLVVVDLDPLAAFFGLKPDGNVKKVIVKGKIV 334
PRK07203 PRK07203
putative aminohydrolase SsnA;
22-90 1.57e-08

putative aminohydrolase SsnA;


Pssm-ID: 235963 [Multi-domain]  Cd Length: 442  Bit Score: 56.87  E-value: 1.57e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446426163  22 AVYIENGTIVDVGSKEELENQYAAVTLHDLKGKTMIPGLVDSHMHLIGHGERLLRLDLSNCTSYGEVLT 90
Cdd:PRK07203  23 AIAIEGNVIVEIGTTDELKAKYPDAEFIDAKGKLIMPGLINSHNHIYSGLARGMMANIPPPPDFISILK 91
Imidazolone-5PH cd01296
Imidazolonepropionase/imidazolone-5-propionate hydrolase (Imidazolone-5PH) catalyzes the third ...
 23-89 5.01e-08

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: 54.96  E-value: 5.01e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446426163  23 VYIENGTIVDVGSKEELEN-QYAAVTLHDLKGKTMIPGLVDSHMHLIGHGERL----LRLdlsNCTSYGEVL 89
Cdd:cd01296    1 IAIRDGRIAAVGPAASLPApGPAAAEEIDAGGRAVTPGLVDCHTHLVFAGDRVdefaARL---AGASYEEIL 69
ATZ_TRZ_like cd01298
TRZ/ATZ family contains enzymes from the atrazine degradation pathway and related hydrolases. ...
 7-67 7.85e-08

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: 54.52  E-value: 7.85e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446426163   7 GGTIYTVREENEKVD-AVYIENGTIVDVGSKEELENQYAAVTLhDLKGKTMIPGLVDSHMHL 67
Cdd:cd01298    5 NGTIVTTDPRRVLEDgDVLVEDGRIVAVGPALPLPAYPADEVI-DAKGKVVMPGLVNTHTHL 65
PRK09228 PRK09228
guanine deaminase; Provisional
 22-75 2.60e-07

guanine deaminase; Provisional


Pssm-ID: 236419 [Multi-domain]  Cd Length: 433  Bit Score: 52.89  E-value: 2.60e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446426163  22 AVYIENGTIVDVGSKEELENQYAA-VTLHDLKGKTMIPGLVDSHMHL-----IG-HGERLL 75
Cdd:PRK09228  33 LLLVEDGRIVAAGPYAELRAQLPAdAEVTDYRGKLILPGFIDTHIHYpqtdmIAsYGEQLL 93
AllB COG0044
Dihydroorotase or related cyclic amidohydrolase [Nucleotide transport and metabolism]; ...
 7-67 7.59e-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: 51.63  E-value: 7.59e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446426163   7 GGTIYTvrEENEKVDAVYIENGTIVDVGSKEELEnqyAAVTLHDLKGKTMIPGLVDSHMHL 67
Cdd:COG0044    4 NGRVVD--PGGLERADVLIEDGRIAAIGPDLAAP---EAAEVIDATGLLVLPGLIDLHVHL 59
PRK15493 PRK15493
bifunctional S-methyl-5'-thioadenosine deaminase/S-adenosylhomocysteine deaminase;
1-68 2.01e-05

bifunctional S-methyl-5'-thioadenosine deaminase/S-adenosylhomocysteine deaminase;


Pssm-ID: 185390 [Multi-domain]  Cd Length: 435  Bit Score: 46.97  E-value: 2.01e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446426163   1 MGEIWYGGTIYTVREENEKVDAVYI--ENGTIVDVGSKEeLENQYAAVTLHDLKGKTMIPGLVDSHMHLI 68
Cdd:PRK15493   1 MKTTYVNATIVTMNEQNEVIENGYIivENDQIIDVNSGE-FASDFEVDEVIDMKGKWVLPGLVNTHTHVV 69
PRK07228 PRK07228
5'-deoxyadenosine deaminase;
7-67 2.11e-05

5'-deoxyadenosine deaminase;


Pssm-ID: 180895 [Multi-domain]  Cd Length: 445  Bit Score: 46.92  E-value: 2.11e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446426163   7 GGTIYTVREENEKVD-AVYIENGTIVDVGSKEELENqYAAVTlhDLKGKTMIPGLVDSHMHL 67
Cdd:PRK07228   7 NAGIVTMNAKREIVDgDVLIEDDRIAAVGDRLDLED-YDDHI--DATGKVVIPGLIQGHIHL 65
AdeC COG1001
Adenine deaminase [Nucleotide transport and metabolism];
17-66 3.43e-05

Adenine deaminase [Nucleotide transport and metabolism];


Pssm-ID: 440625 [Multi-domain]  Cd Length: 559  Bit Score: 46.63  E-value: 3.43e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446426163  17 NEKVDAVyIENGTIVDVGSKEELENQYA---------------AVTLHDLKGKTMIPGLVDSHMH 66
Cdd:COG1001    2 REPADLV-IKNGRLVNVFTGEILEGDIAiaggriagvgdyigeATEVIDAAGRYLVPGFIDGHVH 65
NagA cd00854
N-acetylglucosamine-6-phosphate deacetylase, NagA, catalyzes the hydrolysis of the N-acetyl ...
 13-66 3.77e-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: 46.03  E-value: 3.77e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 446426163  13 VREENEKVDAVYIENGTIVDVGSKEELENQYAAVtlhDLKGKTMIPGLVDSHMH 66
Cdd:cd00854    9 LTPGGLEDGAVLVEDGKIVAIGPEDELEEADEII---DLKGQYLVPGFIDIHIH 59
NagA COG1820
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism];
7-66 1.12e-04

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


Pssm-ID: 441425 [Multi-domain]  Cd Length: 373  Bit Score: 44.32  E-value: 1.12e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446426163   7 GGTIYTvreENEKVD--AVYIENGTIVDVGSKEElenqyAAVTLHDLKGKTMIPGLVDSHMH 66
Cdd:COG1820    4 NARIFT---GDGVLEdgALLIEDGRIAAIGPGAE-----PDAEVIDLGGGYLAPGFIDLHVH 57
Isoaspartyl-dipeptidase cd01308
Isoaspartyl dipeptidase hydrolyzes the beta-L-isoaspartyl linkages in dipeptides, as part of ...
 19-92 1.21e-04

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: 44.30  E-value: 1.21e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446426163  19 KVDaVYIENGTIVDVGSKEELeNQYAAVTLHDLKGKTMIPGLVDSHMHLIGHG------ERLLRLDLSNCTSYGeVLTLV 92
Cdd:cd01308   17 KKD-ILIAGGKILAIEDQLNL-PGYENVTVVDLHGKILVPGFIDQHVHIIGGGgeggpsTRTPEVTLSDLTTAG-VTTVV 93
pyrC PRK09357
dihydroorotase; Validated
 7-67 1.24e-04

dihydroorotase; Validated


Pssm-ID: 236479 [Multi-domain]  Cd Length: 423  Bit Score: 44.42  E-value: 1.24e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446426163   7 GGTIYTVREENEKVDaVYIENGTIVDVGSKEELENQyaavTLHDLKGKTMIPGLVDSHMHL 67
Cdd:PRK09357   7 NGRVIDPKGLDEVAD-VLIDDGKIAAIGENIEAEGA----EVIDATGLVVAPGLVDLHVHL 62
PRK08204 PRK08204
hypothetical protein; Provisional
 7-67 1.67e-04

hypothetical protein; Provisional


Pssm-ID: 181288 [Multi-domain]  Cd Length: 449  Bit Score: 44.22  E-value: 1.67e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446426163   7 GGTIYTVREEN---EKVDaVYIENGTIVDVGskEELENQYAAVTlhDLKGKTMIPGLVDSHMHL 67
Cdd:PRK08204   8 GGTVLTMDPAIgdlPRGD-ILIEGDRIAAVA--PSIEAPDAEVV--DARGMIVMPGLVDTHRHT 66
PRK06038 PRK06038
N-ethylammeline chlorohydrolase; Provisional
 7-67 2.44e-04

N-ethylammeline chlorohydrolase; Provisional


Pssm-ID: 180363 [Multi-domain]  Cd Length: 430  Bit Score: 43.59  E-value: 2.44e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446426163   7 GGTIYTVREENEKVDAVYIENGTIVDVGSKEELEnqyaAVTLHDLKGKTMIPGLVDSHMHL 67
Cdd:PRK06038   8 NAYVLTMDAGDLKKGSVVIEDGTITEVSESTPGD----ADTVIDAKGSVVMPGLVNTHTHA 64
D-HYD cd01314
D-hydantoinases (D-HYD) also called dihydropyrimidases (DHPase) and related proteins; DHPases ...
 7-67 3.32e-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: 42.97  E-value: 3.32e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446426163   7 GGTIYTVrEENEKVDaVYIENGTIVDVGskEELENQYAAVTLhDLKGKTMIPGLVDSHMHL 67
Cdd:cd01314    5 NGTIVTA-DGSFKAD-ILIEDGKIVAIG--PNLEAPGGVEVI-DATGKYVLPGGIDPHTHL 60
metallo-dependent_hydrolases cd01292
Superfamily of metallo-dependent hydrolases (also called amidohydrolase superfamily) is a ...
 301-422 5.05e-04

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: 41.94  E-value: 5.05e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446426163 301 NGVAIFSREELAELVKKARDLHMPVAIHTIGDLSLEYVI-DALELYPPaeGVRDRIIHCQLAREELIERMKNLQAIIDIQ 379
Cdd:cd01292  125 YTATGLSDESLRRVLEEARKLGLPVVIHAGELPDPTRALeDLVALLRL--GGRVVIGHVSHLDPELLELLKEAGVSLEVC 202

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 446426163 380 PvflSSDFPSVIEKLGEHRLRYayawktLLEAGLHCNGGSDAP 422
Cdd:cd01292  203 P---LSNYLLGRDGEGAEALRR------LLELGIRVTLGTDGP 236
PRK09045 PRK09045
TRZ/ATZ family hydrolase;
22-66 1.41e-03

TRZ/ATZ family hydrolase;


Pssm-ID: 236366 [Multi-domain]  Cd Length: 443  Bit Score: 41.05  E-value: 1.41e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 446426163  22 AVYIENGTIVDVGSKEELENQYAAVTLHDLKGKTMIPGLVDSHMH 66
Cdd:PRK09045  30 AVAIRDGRIVAILPRAEARARYAAAETVELPDHVLIPGLINAHTH 74
PRK08203 PRK08203
hydroxydechloroatrazine ethylaminohydrolase; Reviewed
 22-67 1.56e-03

hydroxydechloroatrazine ethylaminohydrolase; Reviewed


Pssm-ID: 236184 [Multi-domain]  Cd Length: 451  Bit Score: 40.99  E-value: 1.56e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 446426163  22 AVYIENGTIVDVGSKEELENQYAAVtlHDLKGKTMIPGLVDSHMHL 67
Cdd:PRK08203  25 GLVVEGGRIVEVGPGGALPQPADEV--FDARGHVVTPGLVNTHHHF 68
NagA COG1820
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism];
453-515 1.77e-03

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


Pssm-ID: 441425 [Multi-domain]  Cd Length: 373  Bit Score: 40.85  E-value: 1.77e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446426163 453 LTVYEAVSLFTTGSAYAIGKEAKRGQIAKGYEADFTILDRNIfeieaeeikEVQAemTVIDGQ 515
Cdd:COG1820  322 LPLEEAVRMASLNPARALGLDDRKGSIAPGKDADLVVLDDDL---------NVRA--TWVGGE 373
GDEase cd01303
Guanine deaminase (GDEase). Guanine deaminase is an aminohydrolase responsible for the ...
 6-75 3.23e-03

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


Pssm-ID: 238628 [Multi-domain]  Cd Length: 429  Bit Score: 39.95  E-value: 3.23e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446426163   6 YGGTIYTVR-EENEKVDA--VYIENGTIV-------DVGSKEELENQYAAVTL-HDLKGKTMIPGLVDSHMHL------- 67
Cdd:cd01303    2 RGTFIHTKSlPELELVEDalRVVEDGLIVvvdgniiAAGAAETLKRAAKPGARvIDSPNQFILPGFIDTHIHApqyanig 81


                 ....*...
gi 446426163  68 IGHGERLL 75
Cdd:cd01303   82 SGLGEPLL 89
PRK08323 PRK08323
phenylhydantoinase; Validated
 7-67 3.42e-03

phenylhydantoinase; Validated


Pssm-ID: 236240 [Multi-domain]  Cd Length: 459  Bit Score: 39.77  E-value: 3.42e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446426163   7 GGTIYTVREEnEKVDaVYIENGTIVDVGSKEelenqyaAVTLHDLKGKTMIPGLVDSHMHL 67
Cdd:PRK08323   7 NGTVVTADDT-YKAD-VLIEDGKIAAIGANL-------GDEVIDATGKYVMPGGIDPHTHM 58
COG3964 COG3964
Predicted amidohydrolase [General function prediction only];
17-66 3.55e-03

Predicted amidohydrolase [General function prediction only];


Pssm-ID: 443164 [Multi-domain]  Cd Length: 376  Bit Score: 39.77  E-value: 3.55e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 446426163  17 NEKVDaVYIENGTIVDVGskeELENQYAAVTLHDLKGKTMIPGLVDSHMH 66
Cdd:COG3964   17 DGVMD-IAIKDGKIAAVA---KDIDAAEAKKVIDASGLYVTPGLIDLHTH 62
PLN02942 PLN02942
dihydropyrimidinase
 7-67 3.71e-03

dihydropyrimidinase


Pssm-ID: 178530  Cd Length: 486  Bit Score: 39.83  E-value: 3.71e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446426163   7 GGTIytVREENEKVDAVYIENGTIVDVGSKEELENQyaaVTLHDLKGKTMIPGLVDSHMHL 67
Cdd:PLN02942  11 GGTV--VNAHHQELADVYVEDGIIVAVAPNLKVPDD---VRVIDATGKFVMPGGIDPHTHL 66
PRK05985 PRK05985
cytosine deaminase; Provisional
 23-67 3.79e-03

cytosine deaminase; Provisional


Pssm-ID: 180337 [Multi-domain]  Cd Length: 391  Bit Score: 39.53  E-value: 3.79e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 446426163  23 VYIENGTIVDVGSKEELEnqyAAVTLHDLKGKTMIPGLVDSHMHL 67
Cdd:PRK05985  19 ILIRDGRIAAIGPALAAP---PGAEVEDGGGALALPGLVDGHIHL 60
Bact_CD cd01293
Bacterial cytosine deaminase and related metal-dependent hydrolases. Cytosine deaminases (CDs) ...
 25-67 5.08e-03

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


Pssm-ID: 238618 [Multi-domain]  Cd Length: 398  Bit Score: 39.15  E-value: 5.08e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 446426163  25 IENGTIVDVGSKEELENQYAAVtlhDLKGKTMIPGLVDSHMHL 67
Cdd:cd01293   19 IEDGRIAAIGPALAVPPDAEEV---DAKGRLVLPAFVDPHIHL 58
L-HYD_ALN cd01315
L-Hydantoinases (L-HYDs) and Allantoinase (ALN); L-Hydantoinases are a member of the ...
 25-68 6.22e-03

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: 39.19  E-value: 6.22e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 446426163  25 IENGTIVDVGSKEElenQYAAVTLHDLKGKTMIPGLVDSHMHLI 68
Cdd:cd01315   22 VKGGKIAAIGPDIA---NTEAEEVIDAGGLVVMPGLIDTHVHIN 62
PRK15446 PRK15446
phosphonate metabolism protein PhnM; Provisional
 1-64 7.03e-03

phosphonate metabolism protein PhnM; Provisional


Pssm-ID: 237967 [Multi-domain]  Cd Length: 383  Bit Score: 38.62  E-value: 7.03e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446426163   1 MGEIWY-GGTIYTvreENEKVDA-VYIENGTIVDVGskeelENQYAAVTLHDLKGKTMIPGLVDSH 64
Cdd:PRK15446   1 MMEMILsNARLVL---PDEVVDGsLLIEDGRIAAID-----PGASALPGAIDAEGDYLLPGLVDLH 58
NagA cd00854
N-acetylglucosamine-6-phosphate deacetylase, NagA, catalyzes the hydrolysis of the N-acetyl ...
 453-499 8.16e-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: 38.71  E-value: 8.16e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 446426163 453 LTVYEAVSLFTTGSAYAIGKEAKRGQIAKGYEADFTILDRNiFEIEA 499
Cdd:cd00854  324 CPLEEAVRMASLNPAKLLGLDDRKGSLKPGKDADLVVLDDD-LNVKA 369
 
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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