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Conserved domains on  [gi|2784223663|ref|WP_369350168|]
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amidohydrolase [Stenotrophomonas sp. JAG2]

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

 Zoom to residue level

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List of domain hits

Name Accession Description Interval E-value
YtcJ COG1574
Predicted amidohydrolase YtcJ [General function prediction only];
17-556 0e+00

Predicted amidohydrolase YtcJ [General function prediction only];


:

Pssm-ID: 441182 [Multi-domain]  Cd Length: 535  Bit Score: 635.69  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784223663  17 TAQADVRMLTAATIHTGDPDAPAATALAwdTDTGRVLAVGDRQAMLTLYPLAALT-DVGQATVIPGLIDAHAHLMFLGGT 95
Cdd:COG1574     4 AAAAADLLLTNGRIYTMDPAQPVAEAVA--VRDGRIVAVGSDAEVRALAGPATEViDLGGKTVLPGFIDAHVHLLGGGLA 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784223663  96 LMQADLTGATSSRDIVARLQRFAADNPEG-WLLGSGWDQNRWPDKQFPTVADLDAAFPDRPVWLGRIDGHAGWGNSAALR 174
Cdd:COG1574    82 LLGVDLSGARSLDELLARLRAAAAELPPGeWILGRGWDESLWPEGRFPTRADLDAVSPDRPVVLTRVDGHAAWVNSAALE 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784223663 175 AVarqpgqRALKGSWQPAGGRIVRDAKGQPSGVFVDEAMSLVQAAIPAPSEAAREQMLARALDKAVSQGLTGVHDMGVSR 254
Cdd:COG1574   162 LA------GITADTPDPEGGEIERDADGEPTGVLREAAMDLVRAAIPPPTPEELRAALRAALRELASLGITSVHDAGLGP 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784223663 255 ADLALMRRFADAGKLPLRIDAYADGNGDALADICAQGAYQHAGG-RLEMRGVKLFMDGALGSRGAALLADYSDDPHNRGL 333
Cdd:COG1574   236 DDLAAYRELAAAGELPLRVVLYLGADDEDLEELLALGLRTGYGDdRLRVGGVKLFADGSLGSRTAALLEPYADDPGNRGL 315
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784223663 334 LVTSPDDFETAVRKADTCHVQVATHAIGDRGNRIALDTYQKVLGERRATDHRWRIEHAQVVALEDIPRFAQLGVIASMQP 413
Cdd:COG1574   316 LLLDPEELRELVRAADAAGLQVAVHAIGDAAVDEVLDAYEAARAANGRRDRRHRIEHAQLVDPDDLARFAELGVIASMQP 395
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784223663 414 THATSDMGWAQDRVGPERILGAYAWRRMLASGARLALGSDFPVEQVDPRLGLYAAVTRQDRAGQppgGWQPDQRLTAAEA 493
Cdd:COG1574   396 THATSDGDWAEDRLGPERAARAYPFRSLLDAGAPLAFGSDAPVEPLDPLLGIYAAVTRRTPSGR---GLGPEERLTVEEA 472
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2784223663 494 LRGFTADAAWAGHDEAQVGRLQPGLRADFVVLDRDPLSVPPAGLADLQVRSTWVDGAPVYEAA 556
Cdd:COG1574   473 LRAYTIGAAYAAFEEDEKGSLEPGKLADFVVLDRDPLTVPPEEIKDIKVLLTVVGGRVVYEAE 535
 
Name Accession Description Interval E-value
YtcJ COG1574
Predicted amidohydrolase YtcJ [General function prediction only];
17-556 0e+00

Predicted amidohydrolase YtcJ [General function prediction only];


Pssm-ID: 441182 [Multi-domain]  Cd Length: 535  Bit Score: 635.69  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784223663  17 TAQADVRMLTAATIHTGDPDAPAATALAwdTDTGRVLAVGDRQAMLTLYPLAALT-DVGQATVIPGLIDAHAHLMFLGGT 95
Cdd:COG1574     4 AAAAADLLLTNGRIYTMDPAQPVAEAVA--VRDGRIVAVGSDAEVRALAGPATEViDLGGKTVLPGFIDAHVHLLGGGLA 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784223663  96 LMQADLTGATSSRDIVARLQRFAADNPEG-WLLGSGWDQNRWPDKQFPTVADLDAAFPDRPVWLGRIDGHAGWGNSAALR 174
Cdd:COG1574    82 LLGVDLSGARSLDELLARLRAAAAELPPGeWILGRGWDESLWPEGRFPTRADLDAVSPDRPVVLTRVDGHAAWVNSAALE 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784223663 175 AVarqpgqRALKGSWQPAGGRIVRDAKGQPSGVFVDEAMSLVQAAIPAPSEAAREQMLARALDKAVSQGLTGVHDMGVSR 254
Cdd:COG1574   162 LA------GITADTPDPEGGEIERDADGEPTGVLREAAMDLVRAAIPPPTPEELRAALRAALRELASLGITSVHDAGLGP 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784223663 255 ADLALMRRFADAGKLPLRIDAYADGNGDALADICAQGAYQHAGG-RLEMRGVKLFMDGALGSRGAALLADYSDDPHNRGL 333
Cdd:COG1574   236 DDLAAYRELAAAGELPLRVVLYLGADDEDLEELLALGLRTGYGDdRLRVGGVKLFADGSLGSRTAALLEPYADDPGNRGL 315
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784223663 334 LVTSPDDFETAVRKADTCHVQVATHAIGDRGNRIALDTYQKVLGERRATDHRWRIEHAQVVALEDIPRFAQLGVIASMQP 413
Cdd:COG1574   316 LLLDPEELRELVRAADAAGLQVAVHAIGDAAVDEVLDAYEAARAANGRRDRRHRIEHAQLVDPDDLARFAELGVIASMQP 395
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784223663 414 THATSDMGWAQDRVGPERILGAYAWRRMLASGARLALGSDFPVEQVDPRLGLYAAVTRQDRAGQppgGWQPDQRLTAAEA 493
Cdd:COG1574   396 THATSDGDWAEDRLGPERAARAYPFRSLLDAGAPLAFGSDAPVEPLDPLLGIYAAVTRRTPSGR---GLGPEERLTVEEA 472
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2784223663 494 LRGFTADAAWAGHDEAQVGRLQPGLRADFVVLDRDPLSVPPAGLADLQVRSTWVDGAPVYEAA 556
Cdd:COG1574   473 LRAYTIGAAYAAFEEDEKGSLEPGKLADFVVLDRDPLTVPPEEIKDIKVLLTVVGGRVVYEAE 535
YtcJ_like cd01300
YtcJ_like metal dependent amidohydrolases. YtcJ is a Bacillus subtilis ORF of unknown function. ...
50-524 2.33e-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: 471.02  E-value: 2.33e-162
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784223663  50 GRVLAVGDRQAMLTLYPLAALT-DVGQATVIPGLIDAHAHLMFLGGTLMQADLTGATSSRDIVARLQRFAADNPEG-WLL 127
Cdd:cd01300     7 GRIVAVGSDAEAKALKGPATEViDLKGKTVLPGFIDSHSHLLLGGLSLLWLDLSGVTSKEEALARIREDAAAAPPGeWIL 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784223663 128 GSGWDQNRWPDKQFPTVADLDAAFPDRPVWLGRIDGHAGWGNSAALRAVArqpgqrALKGSWQPAGGRIVRDAKGQPSGV 207
Cdd:cd01300    87 GFGWDESLLGEGRYPTRAELDAVSPDRPVLLLRRDGHSAWVNSAALRLAG------ITRDTPDPPGGEIVRDADGEPTGV 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784223663 208 FVDEAMSLVQAAIPAPSEAAREQMLARALDKAVSQGLTGVHDMGVSRAD-LALMRRFADAGKLPLRIDA--YADGNGDAL 284
Cdd:cd01300   161 LVEAAAALVLEAVPPPTPEERRAALRAAARELASLGVTTVHDAGGGAADdIEAYRRLAAAGELTLRVRValYVSPLAEDL 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784223663 285 ADICAQGAYQHAGGRLEMRGVKLFMDGALGSRGAALLADYSDDPHNRGLLVTSPDDFETAVRKADTCHVQVATHAIGDRG 364
Cdd:cd01300   241 LEELGARKNGAGDDRLRLGGVKLFADGSLGSRTAALSEPYLDSPGTGGLLLISPEELEELVRAADEAGLQVAIHAIGDRA 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784223663 365 NRIALDTYQKVLGERRATDHRWRIEHAQVVALEDIPRFAQLGVIASMQPTHATSDMGWAQDR-VGPERILGAYAWRRMLA 443
Cdd:cd01300   321 VDTVLDALEAALKDNPRADHRHRIEHAQLVSPDDIPRFAKLGVIASVQPNHLYSDGDAAEDRrLGEERAKRSYPFRSLLD 400
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784223663 444 SGARLALGSDFPVEQVDPRLGLYAAVTRQDRAGQPPGGwqPDQRLTAAEALRGFTADAAWAGHDEAQVGRLQPGLRADFV 523
Cdd:cd01300   401 AGVPVALGSDAPVAPPDPLLGIWAAVTRKTPGGGVLGN--PEERLSLEEALRAYTIGAAYAIGEEDEKGSLEPGKLADFV 478

                  .
gi 2784223663 524 V 524
Cdd:cd01300   479 V 479
Amidohydro_3 pfam07969
Amidohydrolase family;
72-553 4.95e-82

Amidohydrolase family;


Pssm-ID: 400360 [Multi-domain]  Cd Length: 464  Bit Score: 264.01  E-value: 4.95e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784223663  72 DVGQATVIPGLIDAHAHLMFLGGTLMQADLTGATSSRDIVARLQRFAADnpeGWLLGSGWDQNRWPDKQFP-TVADLDAA 150
Cdd:pfam07969   4 DAKGRLVLPGFVDPHTHLDGGGLNLRELRLPDVLPNAVVKGQAGRTPKG---RWLVGEGWDEAQFAETRFPyALADLDEV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784223663 151 FPDRPVWLGRIDGHAGWGNSAALRAVARQPGQRAlkgswqPAGGRIVRDAKG-QPSGVFVDEAmslvQAAIPAPSEAARE 229
Cdd:pfam07969  81 APDGPVLLRALHTHAAVANSAALDLAGITKATED------PPGGEIARDANGeGLTGLLREGA----YALPPLLAREAEA 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784223663 230 QMLARALDKAVSQGLTGVHDMGV---SRADLALMRRFADAGKLPlridayadgngdALADICAQGAYQHAGGRLEMRGVK 306
Cdd:pfam07969 151 AAVAAALAALPGFGITSVDGGGGnvhSLDDYEPLRELTAAEKLK------------ELLDAPERLGLPHSIYELRIGAMK 218
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784223663 307 LFMDGALGSRGAALLADYSDDPhNRGLLVTSPDDFETAVRKADTCHVQVATHAIGDRGNRIALDTYQKVlGERRATDHRW 386
Cdd:pfam07969 219 LFADGVLGSRTAALTEPYFDAP-GTGWPDFEDEALAELVAAARERGLDVAIHAIGDATIDTALDAFEAV-AEKLGNQGRV 296
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784223663 387 RIEHAQVVAL---EDIPRFAQLGVIASMQPTHATSDMGWAQDRVGPERILGAYAWRRMLASGARLALGSDFPVEQVDPRL 463
Cdd:pfam07969 297 RIEHAQGVVPytySQIERVAALGGAAGVQPVFDPLWGDWLQDRLGAERARGLTPVKELLNAGVKVALGSDAPVGPFDPWP 376
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784223663 464 GLYAAVTRQDRAGQppGGWQPDQRLTAAEALRGFTADAAWAGHDEAQVGRLQPGLRADFVVLDRDPLSVPPAGLADLQVR 543
Cdd:pfam07969 377 RIGAAVMRQTAGGG--EVLGPDEELSLEEALALYTSGPAKALGLEDRKGTLGVGKDADLVVLDDDPLTVDPPAIADIRVR 454
                         490
                  ....*....|
gi 2784223663 544 STWVDGAPVY 553
Cdd:pfam07969 455 LTVVDGRVVY 464
PRK09229 PRK09229
N-formimino-L-glutamate deiminase; Validated
376-557 3.48e-06

N-formimino-L-glutamate deiminase; Validated


Pssm-ID: 236420 [Multi-domain]  Cd Length: 456  Bit Score: 49.46  E-value: 3.48e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784223663 376 LGERRATDHRWRIEHAQVVALEDIPRFAQLGVIASMQPThatsdmgwaqdrvgPERIL--GAYAWRRMLASGARLALGSD 453
Cdd:PRK09229  257 LLDHAPVDARWCLVHATHLTDAETARLARSGAVAGLCPT--------------TEANLgdGIFPAVDYLAAGGRFGIGSD 322
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784223663 454 FPVEqVDPRLGL----YAA--VTRQDRAGQPPGGWQPDQRLTAAeALRGFTADAAWAghdeaqVGRLQPGLRADFVVLDR 527
Cdd:PRK09229  323 SHVS-IDLVEELrlleYGQrlRDRRRNVLAAAAQPSVGRRLFDA-ALAGGAQALGRA------IGGLAVGARADLVVLDL 394
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 2784223663 528 DPLS---VPPAGLAD--------LQVRSTWVDGAPVYEAAR 557
Cdd:PRK09229  395 DHPAlagREGDALLDrwvfaggdAAVRDVWVAGRWVVRDGR 435
 
Name Accession Description Interval E-value
YtcJ COG1574
Predicted amidohydrolase YtcJ [General function prediction only];
17-556 0e+00

Predicted amidohydrolase YtcJ [General function prediction only];


Pssm-ID: 441182 [Multi-domain]  Cd Length: 535  Bit Score: 635.69  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784223663  17 TAQADVRMLTAATIHTGDPDAPAATALAwdTDTGRVLAVGDRQAMLTLYPLAALT-DVGQATVIPGLIDAHAHLMFLGGT 95
Cdd:COG1574     4 AAAAADLLLTNGRIYTMDPAQPVAEAVA--VRDGRIVAVGSDAEVRALAGPATEViDLGGKTVLPGFIDAHVHLLGGGLA 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784223663  96 LMQADLTGATSSRDIVARLQRFAADNPEG-WLLGSGWDQNRWPDKQFPTVADLDAAFPDRPVWLGRIDGHAGWGNSAALR 174
Cdd:COG1574    82 LLGVDLSGARSLDELLARLRAAAAELPPGeWILGRGWDESLWPEGRFPTRADLDAVSPDRPVVLTRVDGHAAWVNSAALE 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784223663 175 AVarqpgqRALKGSWQPAGGRIVRDAKGQPSGVFVDEAMSLVQAAIPAPSEAAREQMLARALDKAVSQGLTGVHDMGVSR 254
Cdd:COG1574   162 LA------GITADTPDPEGGEIERDADGEPTGVLREAAMDLVRAAIPPPTPEELRAALRAALRELASLGITSVHDAGLGP 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784223663 255 ADLALMRRFADAGKLPLRIDAYADGNGDALADICAQGAYQHAGG-RLEMRGVKLFMDGALGSRGAALLADYSDDPHNRGL 333
Cdd:COG1574   236 DDLAAYRELAAAGELPLRVVLYLGADDEDLEELLALGLRTGYGDdRLRVGGVKLFADGSLGSRTAALLEPYADDPGNRGL 315
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784223663 334 LVTSPDDFETAVRKADTCHVQVATHAIGDRGNRIALDTYQKVLGERRATDHRWRIEHAQVVALEDIPRFAQLGVIASMQP 413
Cdd:COG1574   316 LLLDPEELRELVRAADAAGLQVAVHAIGDAAVDEVLDAYEAARAANGRRDRRHRIEHAQLVDPDDLARFAELGVIASMQP 395
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784223663 414 THATSDMGWAQDRVGPERILGAYAWRRMLASGARLALGSDFPVEQVDPRLGLYAAVTRQDRAGQppgGWQPDQRLTAAEA 493
Cdd:COG1574   396 THATSDGDWAEDRLGPERAARAYPFRSLLDAGAPLAFGSDAPVEPLDPLLGIYAAVTRRTPSGR---GLGPEERLTVEEA 472
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2784223663 494 LRGFTADAAWAGHDEAQVGRLQPGLRADFVVLDRDPLSVPPAGLADLQVRSTWVDGAPVYEAA 556
Cdd:COG1574   473 LRAYTIGAAYAAFEEDEKGSLEPGKLADFVVLDRDPLTVPPEEIKDIKVLLTVVGGRVVYEAE 535
YtcJ_like cd01300
YtcJ_like metal dependent amidohydrolases. YtcJ is a Bacillus subtilis ORF of unknown function. ...
50-524 2.33e-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: 471.02  E-value: 2.33e-162
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784223663  50 GRVLAVGDRQAMLTLYPLAALT-DVGQATVIPGLIDAHAHLMFLGGTLMQADLTGATSSRDIVARLQRFAADNPEG-WLL 127
Cdd:cd01300     7 GRIVAVGSDAEAKALKGPATEViDLKGKTVLPGFIDSHSHLLLGGLSLLWLDLSGVTSKEEALARIREDAAAAPPGeWIL 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784223663 128 GSGWDQNRWPDKQFPTVADLDAAFPDRPVWLGRIDGHAGWGNSAALRAVArqpgqrALKGSWQPAGGRIVRDAKGQPSGV 207
Cdd:cd01300    87 GFGWDESLLGEGRYPTRAELDAVSPDRPVLLLRRDGHSAWVNSAALRLAG------ITRDTPDPPGGEIVRDADGEPTGV 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784223663 208 FVDEAMSLVQAAIPAPSEAAREQMLARALDKAVSQGLTGVHDMGVSRAD-LALMRRFADAGKLPLRIDA--YADGNGDAL 284
Cdd:cd01300   161 LVEAAAALVLEAVPPPTPEERRAALRAAARELASLGVTTVHDAGGGAADdIEAYRRLAAAGELTLRVRValYVSPLAEDL 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784223663 285 ADICAQGAYQHAGGRLEMRGVKLFMDGALGSRGAALLADYSDDPHNRGLLVTSPDDFETAVRKADTCHVQVATHAIGDRG 364
Cdd:cd01300   241 LEELGARKNGAGDDRLRLGGVKLFADGSLGSRTAALSEPYLDSPGTGGLLLISPEELEELVRAADEAGLQVAIHAIGDRA 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784223663 365 NRIALDTYQKVLGERRATDHRWRIEHAQVVALEDIPRFAQLGVIASMQPTHATSDMGWAQDR-VGPERILGAYAWRRMLA 443
Cdd:cd01300   321 VDTVLDALEAALKDNPRADHRHRIEHAQLVSPDDIPRFAKLGVIASVQPNHLYSDGDAAEDRrLGEERAKRSYPFRSLLD 400
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784223663 444 SGARLALGSDFPVEQVDPRLGLYAAVTRQDRAGQPPGGwqPDQRLTAAEALRGFTADAAWAGHDEAQVGRLQPGLRADFV 523
Cdd:cd01300   401 AGVPVALGSDAPVAPPDPLLGIWAAVTRKTPGGGVLGN--PEERLSLEEALRAYTIGAAYAIGEEDEKGSLEPGKLADFV 478

                  .
gi 2784223663 524 V 524
Cdd:cd01300   479 V 479
Amidohydro_3 pfam07969
Amidohydrolase family;
72-553 4.95e-82

Amidohydrolase family;


Pssm-ID: 400360 [Multi-domain]  Cd Length: 464  Bit Score: 264.01  E-value: 4.95e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784223663  72 DVGQATVIPGLIDAHAHLMFLGGTLMQADLTGATSSRDIVARLQRFAADnpeGWLLGSGWDQNRWPDKQFP-TVADLDAA 150
Cdd:pfam07969   4 DAKGRLVLPGFVDPHTHLDGGGLNLRELRLPDVLPNAVVKGQAGRTPKG---RWLVGEGWDEAQFAETRFPyALADLDEV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784223663 151 FPDRPVWLGRIDGHAGWGNSAALRAVARQPGQRAlkgswqPAGGRIVRDAKG-QPSGVFVDEAmslvQAAIPAPSEAARE 229
Cdd:pfam07969  81 APDGPVLLRALHTHAAVANSAALDLAGITKATED------PPGGEIARDANGeGLTGLLREGA----YALPPLLAREAEA 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784223663 230 QMLARALDKAVSQGLTGVHDMGV---SRADLALMRRFADAGKLPlridayadgngdALADICAQGAYQHAGGRLEMRGVK 306
Cdd:pfam07969 151 AAVAAALAALPGFGITSVDGGGGnvhSLDDYEPLRELTAAEKLK------------ELLDAPERLGLPHSIYELRIGAMK 218
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784223663 307 LFMDGALGSRGAALLADYSDDPhNRGLLVTSPDDFETAVRKADTCHVQVATHAIGDRGNRIALDTYQKVlGERRATDHRW 386
Cdd:pfam07969 219 LFADGVLGSRTAALTEPYFDAP-GTGWPDFEDEALAELVAAARERGLDVAIHAIGDATIDTALDAFEAV-AEKLGNQGRV 296
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784223663 387 RIEHAQVVAL---EDIPRFAQLGVIASMQPTHATSDMGWAQDRVGPERILGAYAWRRMLASGARLALGSDFPVEQVDPRL 463
Cdd:pfam07969 297 RIEHAQGVVPytySQIERVAALGGAAGVQPVFDPLWGDWLQDRLGAERARGLTPVKELLNAGVKVALGSDAPVGPFDPWP 376
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784223663 464 GLYAAVTRQDRAGQppGGWQPDQRLTAAEALRGFTADAAWAGHDEAQVGRLQPGLRADFVVLDRDPLSVPPAGLADLQVR 543
Cdd:pfam07969 377 RIGAAVMRQTAGGG--EVLGPDEELSLEEALALYTSGPAKALGLEDRKGTLGVGKDADLVVLDDDPLTVDPPAIADIRVR 454
                         490
                  ....*....|
gi 2784223663 544 STWVDGAPVY 553
Cdd:pfam07969 455 LTVVDGRVVY 464
HutI COG1228
Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport ...
191-555 2.48e-18

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


Pssm-ID: 440841 [Multi-domain]  Cd Length: 386  Bit Score: 86.94  E-value: 2.48e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784223663 191 PAGGRIVrDAKGQ---PSgvFVDEAMSLVQAAIPAPSEAARE---------QMLARALDKAVSQGLTGVHDMgvSRADLA 258
Cdd:COG1228    50 PAGAEVI-DATGKtvlPG--LIDAHTHLGLGGGRAVEFEAGGgitptvdlvNPADKRLRRALAAGVTTVRDL--PGGPLG 124
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784223663 259 LmRRFADAGKLPLRIDAYADGNGDALAdiCAQGAyqHAGGRLEMRGV--KLFMDGAlgsrgaallaDYSDDPHNRGLLVT 336
Cdd:COG1228   125 L-RDAIIAGESKLLPGPRVLAAGPALS--LTGGA--HARGPEEARAAlrELLAEGA----------DYIKVFAEGGAPDF 189
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784223663 337 SPDDFETAVRKADTCHVQVATHAIGDRGNRIALDTYQKVlgerratdhrwrIEHAQVVALEDIPRFAQLGVIAsMQPTHA 416
Cdd:COG1228   190 SLEELRAILEAAHALGLPVAAHAHQADDIRLAVEAGVDS------------IEHGTYLDDEVADLLAEAGTVV-LVPTLS 256
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784223663 417 TSDMG------WAQDRVGPERILGAYAWRRMLASGARLALGSDFPVEqVDPRLGLYAAVTRQDRAGqppggwqpdqrLTA 490
Cdd:COG1228   257 LFLALlegaaaPVAAKARKVREAALANARRLHDAGVPVALGTDAGVG-VPPGRSLHRELALAVEAG-----------LTP 324
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2784223663 491 AEALRGFTADAAWAGHDEAQVGRLQPGLRADFVVLDRDPLSVppagLADLQ-VRSTWVDGAPVYEA 555
Cdd:COG1228   325 EEALRAATINAAKALGLDDDVGSLEPGKLADLVLLDGDPLED----IAYLEdVRAVMKDGRVVDRS 386
SsnA COG0402
Cytosine/adenosine deaminase or related metal-dependent hydrolase [Nucleotide transport and ...
434-554 2.14e-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: 62.92  E-value: 2.14e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784223663 434 GAYAWRRMLASGARLALGSDFPVEQVDP------RLGLYAAvtrQDRAGQPPggwqpdqRLTAAEALRGFTADAAWAGHD 507
Cdd:COG0402   290 GIAPVPRLLAAGVRVGLGTDGAASNNSLdmfeemRLAALLQ---RLRGGDPT-------ALSAREALEMATLGGARALGL 359
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2784223663 508 EAQVGRLQPGLRADFVVLDRDplSVPPAGLADL-----------QVRSTWVDGAPVYE 554
Cdd:COG0402   360 DDEIGSLEPGKRADLVVLDLD--APHLAPLHDPlsalvyaadgrDVRTVWVAGRVVVR 415
Met_dep_hydrolase_A cd01299
Metallo-dependent hydrolases, subgroup A is part of the superfamily of metallo-dependent ...
233-530 1.49e-09

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


Pssm-ID: 238624 [Multi-domain]  Cd Length: 342  Bit Score: 59.61  E-value: 1.49e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784223663 233 ARALDKAVSQGLTGVHDMGvsRADLALMRRFADAGKLPL-RI----------DAYADGNGDALADICAQGAYQhAGGRLE 301
Cdd:cd01299    45 TRQARAALRAGFTTVRDAG--GADYGLLRDAIDAGLIPGpRVfasgralsqtGGHGDPRGLSGLFPAGGLAAV-VDGVEE 121
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784223663 302 MRG------------VKLFMDGALGSRGaalladysDDPHNRGLlvtSPDDFETAVRKADTCHVQVATHAIGDRGNRIAL 369
Cdd:cd01299   122 VRAavreqlrrgadqIKIMATGGVLSPG--------DPPPDTQF---SEEELRAIVDEAHKAGLYVAAHAYGAEAIRRAI 190
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784223663 370 ----DTyqkvlgerratdhrwrIEHAQVVALEDIPRFAQLGVIASMQPT---------HATSDMGWAQDRVGPERILGAY 436
Cdd:cd01299   191 ragvDT----------------IEHGFLIDDETIELMKEKGIFLVPTLAtyealaaegAAPGLPADSAEKVALVLEAGRD 254
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784223663 437 AWRRMLASGARLALGSD--FPVeqvdprlglyaavtrqdragqPPGGWQPDQ-------RLTAAEALRGFTADAAWAGHD 507
Cdd:cd01299   255 ALRRAHKAGVKIAFGTDagFPV---------------------PPHGWNARElellvkaGGTPAEALRAATANAAELLGL 313
                         330       340
                  ....*....|....*....|...
gi 2784223663 508 EAQVGRLQPGLRADFVVLDRDPL 530
Cdd:cd01299   314 SDELGVIEAGKLADLLVVDGDPL 336
Amidohydro_1 pfam01979
Amidohydrolase family; This family of enzymes are a a large metal dependent hydrolase ...
220-552 1.97e-08

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: 56.36  E-value: 1.97e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784223663 220 IPAPSEAAREqMLARALDKAVSQGLTGVHDMGVSRAD-LALMRRFADAGKLPLRIDA-----YADGNGDALADICAQGAY 293
Cdd:pfam01979  21 IPVPPEFAYE-ALRLGITTMLKSGTTTVLDMGATTSTgIEALLEAAEELPLGLRFLGpgcslDTDGELEGRKALREKLKA 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784223663 294 qhaggrlEMRGVKLFMDGALGSRGAalladysddPHnrGLLVTSPDDFETAVRKADTCHVQVATHAIGDRGnrialDTYQ 373
Cdd:pfam01979 100 -------GAEFIKGMADGVVFVGLA---------PH--GAPTFSDDELKAALEEAKKYGLPVAIHALETKG-----EVED 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784223663 374 KVLGERRATDHRWRIEHAQVVALEDIPRFA-QLGV---IASMQPTHATSDMGWAQDRVGPERIL--GAYAWRRMLASGAR 447
Cdd:pfam01979 157 AIAAFGGGIEHGTHLEVAESGGLLDIIKLIlAHGVhlsPTEANLLAEHLKGAGVAHCPFSNSKLrsGRIALRKALEDGVK 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784223663 448 LALGSDFPVEQVDPRL---GLYAAVTRQDragqppggwqPDQRLTAAEALRGFTADAAWAGHDEAQVGRLQPGLRADFVV 524
Cdd:pfam01979 237 VGLGTDGAGSGNSLNMleeLRLALELQFD----------PEGGLSPLEALRMATINPAKALGLDDKVGSIEVGKDADLVV 306
                         330       340
                  ....*....|....*....|....*...
gi 2784223663 525 LDRDPLSVPPAGLADLQVRSTWVDGAPV 552
Cdd:pfam01979 307 VDLDPLAAFFGLKPDGNVKKVIVKGKIV 334
PRK09229 PRK09229
N-formimino-L-glutamate deiminase; Validated
376-557 3.48e-06

N-formimino-L-glutamate deiminase; Validated


Pssm-ID: 236420 [Multi-domain]  Cd Length: 456  Bit Score: 49.46  E-value: 3.48e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784223663 376 LGERRATDHRWRIEHAQVVALEDIPRFAQLGVIASMQPThatsdmgwaqdrvgPERIL--GAYAWRRMLASGARLALGSD 453
Cdd:PRK09229  257 LLDHAPVDARWCLVHATHLTDAETARLARSGAVAGLCPT--------------TEANLgdGIFPAVDYLAAGGRFGIGSD 322
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784223663 454 FPVEqVDPRLGL----YAA--VTRQDRAGQPPGGWQPDQRLTAAeALRGFTADAAWAghdeaqVGRLQPGLRADFVVLDR 527
Cdd:PRK09229  323 SHVS-IDLVEELrlleYGQrlRDRRRNVLAAAAQPSVGRRLFDA-ALAGGAQALGRA------IGGLAVGARADLVVLDL 394
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 2784223663 528 DPLS---VPPAGLAD--------LQVRSTWVDGAPVYEAAR 557
Cdd:PRK09229  395 DHPAlagREGDALLDrwvfaggdAAVRDVWVAGRWVVRDGR 435
metallo-dependent_hydrolases cd01292
Superfamily of metallo-dependent hydrolases (also called amidohydrolase superfamily) is a ...
218-502 1.03e-05

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: 47.33  E-value: 1.03e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784223663 218 AAIPAPSEAAREQMLARALDKAVSQGLTGVHDMGVSRADlalmrrfadaGKLPLRIDAYADGNGDA--LADICAQGAYQH 295
Cdd:cd01292    23 KEAEELSPEDLYEDTLRALEALLAGGVTTVVDMGSTPPP----------TTTKAAIEAVAEAARASagIRVVLGLGIPGV 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784223663 296 AGGRLEMRGV----KLFMDGALGSRGAALLADYSDDPHNrgllvtsPDDFETAVRKADTCHVQVATHAIGDRGNRIALDT 371
Cdd:cd01292    93 PAAVDEDAEAllleLLRRGLELGAVGLKLAGPYTATGLS-------DESLRRVLEEARKLGLPVVIHAGELPDPTRALED 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784223663 372 YQKVLGErratDHRWRIEHAQVVALEDIPRFAQLGVIASMQPTHATSDMGWAQDRvgperilgaYAWRRMLASGARLALG 451
Cdd:cd01292   166 LVALLRL----GGRVVIGHVSHLDPELLELLKEAGVSLEVCPLSNYLLGRDGEGA---------EALRRLLELGIRVTLG 232
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2784223663 452 SDFPVEQVDPRLGLYAAVTRQDRAGQppggwqpdqrLTAAEALRGFTADAA 502
Cdd:cd01292   233 TDGPPHPLGTDLLALLRLLLKVLRLG----------LSLEEALRLATINPA 273
Met_dep_hydrolase_C cd01309
Metallo-dependent hydrolases, subgroup C is part of the superfamily of metallo-dependent ...
441-553 1.33e-05

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


Pssm-ID: 238634 [Multi-domain]  Cd Length: 359  Bit Score: 47.31  E-value: 1.33e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784223663 441 MLASGARLALGSDFPVEQVDpRLGLYAAVTRqdRAGqppggwqpdqrLTAAEALRGFTADAAWAGHDEAQVGRLQPGLRA 520
Cdd:cd01309   267 LKKGGVAFAISSDHPVLNIR-NLNLEAAKAV--KYG-----------LSYEEALKAITINPAKILGIEDRVGSLEPGKDA 332
                          90       100       110
                  ....*....|....*....|....*....|...
gi 2784223663 521 DFVVLDRDPLSVppaglaDLQVRSTWVDGAPVY 553
Cdd:cd01309   333 DLVVWNGDPLEP------TSKPEQVYIDGRLVY 359
D-aminoacylase cd01297
D-aminoacylases (N-acyl-D-Amino acid amidohydrolases) catalyze the hydrolysis of ...
486-554 7.97e-05

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


Pssm-ID: 238622 [Multi-domain]  Cd Length: 415  Bit Score: 45.37  E-value: 7.97e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2784223663 486 QRLTAAEALRGFTAD-AAWAGHDEAqvGRLQPGLRADFVVLDRDPLSVPPAGLADLQ----VRSTWVDGAPVYE 554
Cdd:cd01297   333 KLLSLEEAVRKMTGLpARVFGLADR--GRIAPGYRADIVVFDPDTLADRATFTRPNQpaegIEAVLVNGVPVVR 404
ATZ_TRZ_like cd01298
TRZ/ATZ family contains enzymes from the atrazine degradation pathway and related hydrolases. ...
337-554 1.97e-04

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


Pssm-ID: 238623 [Multi-domain]  Cd Length: 411  Bit Score: 44.12  E-value: 1.97e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784223663 337 SPDDFETAVRKADTCHVQVATH-AIGDRGNRIALDTYQK----VLGERRATDHRWRIEHAQVVALEDIPRFAQLGVIASM 411
Cdd:cd01298   192 SDELLREVAELAREYGVPLHIHlAETEDEVEESLEKYGKrpveYLEELGLLGPDVVLAHCVWLTDEEIELLAETGTGVAH 271
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784223663 412 QPThatSDMGWAqdrVGPERIlgayawRRMLASGARLALGSDFP--------VEQVdpRLglyAAVTRQDRAGQPPGgwq 483
Cdd:cd01298   272 NPA---SNMKLA---SGIAPV------PEMLEAGVNVGLGTDGAasnnnldmFEEM--RL---AALLQKLAHGDPTA--- 331
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784223663 484 pdqrLTAAEALRGFTADAAWA-GHDEaqVGRLQPGLRADFVVLD-RDPLSVPPAGLADL--------QVRSTWVDGAPVY 553
Cdd:cd01298   332 ----LPAEEALEMATIGGAKAlGLDE--IGSLEVGKKADLILIDlDGPHLLPVHDPISHlvysanggDVDTVIVNGRVVM 405

                  .
gi 2784223663 554 E 554
Cdd:cd01298   406 E 406
Met_dep_hydrolase_E cd01313
Metallo-dependent hydrolases, subgroup D is part of the superfamily of metallo-dependent ...
376-549 2.06e-04

Metallo-dependent hydrolases, subgroup D 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: 238638 [Multi-domain]  Cd Length: 418  Bit Score: 43.98  E-value: 2.06e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784223663 376 LGERRATDHRWRIEHAQVVALEDIPRFAQLGVIASMQPThatsdmgwaqdrvgPERIL--GAYAWRRMLASGARLALGSD 453
Cdd:cd01313   248 LLDHGHLDARWCLVHATHLTDNETLLLGRSGAVVGLCPT--------------TEANLgdGIFPAAALLAAGGRIGIGSD 313
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784223663 454 FPVeQVDPRLGLYAAVTRQDRAGQPPGGWQPDQRLTAAEALRGFTADAAWAGhdEAQVGRLQPGLRADFVVLDRDPLSVP 533
Cdd:cd01313   314 SNA-RIDLLEELRQLEYSQRLRDRARNVLATAGGSSARALLDAALAGGAQAL--GLATGALEAGARADLLSLDLDHPSLA 390
                         170       180
                  ....*....|....*....|....*..
gi 2784223663 534 ---PAGLAD--------LQVRSTWVDG 549
Cdd:cd01313   391 galPDTLLDawvfaagdREVRDVVVGG 417
PRK09228 PRK09228
guanine deaminase; Provisional
486-556 2.18e-04

guanine deaminase; Provisional


Pssm-ID: 236419 [Multi-domain]  Cd Length: 433  Bit Score: 43.64  E-value: 2.18e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784223663 486 QRLTAAEALRGFTADAAWAGHDEAQVGRLQPGLRADFVVLDrdplsvPPAG------------LADL-----------QV 542
Cdd:PRK09228  346 YRLSPFQAFYLATLGGARALGLDDRIGNLAPGKEADFVVLD------PAATpllalrtaraesLEELlfalmtlgddrAV 419
                          90
                  ....*....|....
gi 2784223663 543 RSTWVDGAPVYEAA 556
Cdd:PRK09228  420 AETYVAGRPVYRRL 433
Imidazolone-5PH cd01296
Imidazolonepropionase/imidazolone-5-propionate hydrolase (Imidazolone-5PH) catalyzes the third ...
50-113 2.19e-04

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: 43.79  E-value: 2.19e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2784223663  50 GRVLAVGDRQAMLTLYPLAALT-DVGQATVIPGLIDAHAHLMFLGGTL--MQADLTGATSSrDIVAR 113
Cdd:cd01296     6 GRIAAVGPAASLPAPGPAAAEEiDAGGRAVTPGLVDCHTHLVFAGDRVdeFAARLAGASYE-EILAA 71
NagA cd00854
N-acetylglucosamine-6-phosphate deacetylase, NagA, catalyzes the hydrolysis of the N-acetyl ...
488-549 2.39e-04

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


Pssm-ID: 238434 [Multi-domain]  Cd Length: 374  Bit Score: 43.72  E-value: 2.39e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2784223663 488 LTAAEALRGFTADAAWAGHDEAQVGRLQPGLRADFVVLDRdplsvppaglaDLQVRSTWVDG 549
Cdd:cd00854   324 CPLEEAVRMASLNPAKLLGLDDRKGSLKPGKDADLVVLDD-----------DLNVKATWING 374
NagA COG1820
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism];
488-549 1.08e-03

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


Pssm-ID: 441425 [Multi-domain]  Cd Length: 373  Bit Score: 41.62  E-value: 1.08e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2784223663 488 LTAAEALRGFTADAAWAGHDEAQVGRLQPGLRADFVVLDRdplsvppaglaDLQVRSTWVDG 549
Cdd:COG1820   322 LPLEEAVRMASLNPARALGLDDRKGSIAPGKDADLVVLDD-----------DLNVRATWVGG 372
Imidazolone-5PH cd01296
Imidazolonepropionase/imidazolone-5-propionate hydrolase (Imidazolone-5PH) catalyzes the third ...
439-526 1.13e-03

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


Pssm-ID: 238621 [Multi-domain]  Cd Length: 371  Bit Score: 41.47  E-value: 1.13e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784223663 439 RRMLASGARLALGSDF-PVEQVDPRLGLYA--AVTrqdragqppggwqpDQRLTAAEALRGFTADAAWAGHDEAQVGRLQ 515
Cdd:cd01296   272 RKLIDAGVPVALGTDFnPGSSPTSSMPLVMhlACR--------------LMRMTPEEALTAATINAAAALGLGETVGSLE 337
                          90
                  ....*....|.
gi 2784223663 516 PGLRADFVVLD 526
Cdd:cd01296   338 VGKQADLVILD 348
PRK15446 PRK15446
phosphonate metabolism protein PhnM; Provisional
512-556 2.74e-03

phosphonate metabolism protein PhnM; Provisional


Pssm-ID: 237967 [Multi-domain]  Cd Length: 383  Bit Score: 40.16  E-value: 2.74e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 2784223663 512 GRLQPGLRADFVVLDRDPlSVPpagladlQVRSTWVDGAPVYEAA 556
Cdd:PRK15446  347 GEIAPGKRADLVRVRRAG-GLP-------VVRAVWRGGRRVFLAG 383
PRK08204 PRK08204
hypothetical protein; Provisional
440-552 3.47e-03

hypothetical protein; Provisional


Pssm-ID: 181288 [Multi-domain]  Cd Length: 449  Bit Score: 39.99  E-value: 3.47e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2784223663 440 RMLASGARLALGSDfpVEQVDP-------RLGLYAAVTRQDRAGQPPGGWQPDQ-RLTAAEALRGFTADAAWAGHDEAQV 511
Cdd:PRK08204  288 RLLAHGVRPSLGVD--VVTSTGgdmftqmRFALQAERARDNAVHLREGGMPPPRlTLTARQVLEWATIEGARALGLEDRI 365
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2784223663 512 GRLQPGLRADFVVLDRDPLSVPP-----------AGLADlqVRSTWVDGAPV 552
Cdd:PRK08204  366 GSLTPGKQADLVLIDATDLNLAPvhdpvgavvqsAHPGN--VDSVMVAGRAV 415
PRK09228 PRK09228
guanine deaminase; Provisional
20-88 3.91e-03

guanine deaminase; Provisional


Pssm-ID: 236419 [Multi-domain]  Cd Length: 433  Bit Score: 39.79  E-value: 3.91e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2784223663  20 ADVRMLTAATIH-TGDPDAPAAT-ALAWDTD------TGRVLAVGDRQAMLTLYP-LAALTDVGQATVIPGLIDAHAH 88
Cdd:PRK09228    1 MTTKAYRGRLLHfTADPAEVDDEdALRYIEDglllveDGRIVAAGPYAELRAQLPaDAEVTDYRGKLILPGFIDTHIH 78
 
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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