NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|505168603|ref|WP_015355705|]
View 

amidohydrolase [Mycobacterium liflandii]

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

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
YtcJ COG1574
Predicted amidohydrolase YtcJ [General function prediction only];
6-533 3.61e-121

Predicted amidohydrolase YtcJ [General function prediction only];


:

Pssm-ID: 441182 [Multi-domain]  Cd Length: 535  Bit Score: 366.43  E-value: 3.61e-121
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505168603   6 TKLLVNGRVY--SPTHPDATAMAVRGDTVAWLGSDEVGRNQF-PDAQVEDLDGGLVAPGFVDSHIHLTATGLTISGLDLR 82
Cdd:COG1574    9 DLLLTNGRIYtmDPAQPVAEAVAVRDGRIVAVGSDAEVRALAgPATEVIDLGGKTVLPGFIDAHVHLLGGGLALLGVDLS 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505168603  83 PASSLGGCLQLAADHAAAHP-GQPLWGHGWDESAWPQHIAPSTAQLDAVLGERPAYLARVDVHSALASS-GLrrlvphls 160
Cdd:COG1574   89 GARSLDELLARLRAAAAELPpGEWILGRGWDESLWPEGRFPTRADLDAVSPDRPVVLTRVDGHAAWVNSaAL-------- 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505168603 161 EAAGFTEQ------------------GPLTGEAHHLVRARARDLlTQPQLAEARTAALGSLAAAGIVAVHECGGPEiGGL 222
Cdd:COG1574  161 ELAGITADtpdpeggeierdadgeptGVLREAAMDLVRAAIPPP-TPEELRAALRAALRELASLGITSVHDAGLGP-DDL 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505168603 223 DDWLQLSA---LPhgVEVIGYWGEAVTTAAQARTLMAETGARG----LAG-DLFVDGALGSRTAWLHEPYADQPGCVGTC 294
Cdd:COG1574  239 AAYRELAAageLP--LRVVLYLGADDEDLEELLALGLRTGYGDdrlrVGGvKLFADGSLGSRTAALLEPYADDPGNRGLL 316

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505168603 295 HLDGPAVEAHARACTEAEVTAGFHVIGDAAVATVVDAFERVVADLGvvaVARCGHRLEHAEMVTAEQAAKLGAWGIIASV 374
Cdd:COG1574  317 LLDPEELRELVRAADAAGLQVAVHAIGDAAVDEVLDAYEAARAANG---RRDRRHRIEHAQLVDPDDLARFAELGVIASM 393

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505168603 375 QPNFDALWGgaeGMYARRLGPKRARLLNPLALLASQGVPLAFGSDAPVTGFDPWASVRAAVNHHTAGSAVSARAAF---- 450
Cdd:COG1574  394 QPTHATSDG---DWAEDRLGPERAARAYPFRSLLDAGAPLAFGSDAPVEPLDPLLGIYAAVTRRTPSGRGLGPEERltve 470

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505168603 451 ---AAATRGGWRAAGvRDGKTGTLVPGAPASYAVWDAGALTVSAPRdavqrwstdprsrvpaLPRLdpadplpRCRQTVH 527
Cdd:COG1574  471 ealRAYTIGAAYAAF-EEDEKGSLEPGKLADFVVLDRDPLTVPPEE----------------IKDI-------KVLLTVV 526


                 ....*.
gi 505168603 528 RGAVIY 533
Cdd:COG1574  527 GGRVVY 532
 
Name Accession Description Interval E-value
YtcJ COG1574
Predicted amidohydrolase YtcJ [General function prediction only];
6-533 3.61e-121

Predicted amidohydrolase YtcJ [General function prediction only];


Pssm-ID: 441182 [Multi-domain]  Cd Length: 535  Bit Score: 366.43  E-value: 3.61e-121
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505168603   6 TKLLVNGRVY--SPTHPDATAMAVRGDTVAWLGSDEVGRNQF-PDAQVEDLDGGLVAPGFVDSHIHLTATGLTISGLDLR 82
Cdd:COG1574    9 DLLLTNGRIYtmDPAQPVAEAVAVRDGRIVAVGSDAEVRALAgPATEVIDLGGKTVLPGFIDAHVHLLGGGLALLGVDLS 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505168603  83 PASSLGGCLQLAADHAAAHP-GQPLWGHGWDESAWPQHIAPSTAQLDAVLGERPAYLARVDVHSALASS-GLrrlvphls 160
Cdd:COG1574   89 GARSLDELLARLRAAAAELPpGEWILGRGWDESLWPEGRFPTRADLDAVSPDRPVVLTRVDGHAAWVNSaAL-------- 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505168603 161 EAAGFTEQ------------------GPLTGEAHHLVRARARDLlTQPQLAEARTAALGSLAAAGIVAVHECGGPEiGGL 222
Cdd:COG1574  161 ELAGITADtpdpeggeierdadgeptGVLREAAMDLVRAAIPPP-TPEELRAALRAALRELASLGITSVHDAGLGP-DDL 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505168603 223 DDWLQLSA---LPhgVEVIGYWGEAVTTAAQARTLMAETGARG----LAG-DLFVDGALGSRTAWLHEPYADQPGCVGTC 294
Cdd:COG1574  239 AAYRELAAageLP--LRVVLYLGADDEDLEELLALGLRTGYGDdrlrVGGvKLFADGSLGSRTAALLEPYADDPGNRGLL 316

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505168603 295 HLDGPAVEAHARACTEAEVTAGFHVIGDAAVATVVDAFERVVADLGvvaVARCGHRLEHAEMVTAEQAAKLGAWGIIASV 374
Cdd:COG1574  317 LLDPEELRELVRAADAAGLQVAVHAIGDAAVDEVLDAYEAARAANG---RRDRRHRIEHAQLVDPDDLARFAELGVIASM 393

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505168603 375 QPNFDALWGgaeGMYARRLGPKRARLLNPLALLASQGVPLAFGSDAPVTGFDPWASVRAAVNHHTAGSAVSARAAF---- 450
Cdd:COG1574  394 QPTHATSDG---DWAEDRLGPERAARAYPFRSLLDAGAPLAFGSDAPVEPLDPLLGIYAAVTRRTPSGRGLGPEERltve 470

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505168603 451 ---AAATRGGWRAAGvRDGKTGTLVPGAPASYAVWDAGALTVSAPRdavqrwstdprsrvpaLPRLdpadplpRCRQTVH 527
Cdd:COG1574  471 ealRAYTIGAAYAAF-EEDEKGSLEPGKLADFVVLDRDPLTVPPEE----------------IKDI-------KVLLTVV 526


                 ....*.
gi 505168603 528 RGAVIY 533
Cdd:COG1574  527 GGRVVY 532
YtcJ_like cd01300
YtcJ_like metal dependent amidohydrolases. YtcJ is a Bacillus subtilis ORF of unknown function. ...
 24-481 8.53e-100

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: 309.62  E-value: 8.53e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505168603  24 AMAVRGDTVAWLGSD-EVGRNQFPDAQVEDLDGGLVAPGFVDSHIHLTATGLTISGLDLRPASSLG-GCLQLAADHAAAH 101
Cdd:cd01300    1 AVAVRDGRIVAVGSDaEAKALKGPATEVIDLKGKTVLPGFIDSHSHLLLGGLSLLWLDLSGVTSKEeALARIREDAAAAP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505168603 102 PGQPLWGHGWDESAWPQHIAPSTAQLDAVLGERPAYLARVDVHSALASS-GLRRL-VPHLSE-----AAGFTEQGPLTG- 173
Cdd:cd01300   81 PGEWILGFGWDESLLGEGRYPTRAELDAVSPDRPVLLLRRDGHSAWVNSaALRLAgITRDTPdppggEIVRDADGEPTGv 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505168603 174 --EAHHLVRARARDLLTQPQLAEARTAALGSLAAAGIVAVHECGGPEIGGLDDWLQLSALP-------HGVEVIGYWGEA 244
Cdd:cd01300  161 lvEAAAALVLEAVPPPTPEERRAALRAAARELASLGVTTVHDAGGGAADDIEAYRRLAAAGeltlrvrVALYVSPLAEDL 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505168603 245 VTTAAQARTLMAETGARGLAGDLFVDGALGSRTAWLHEPYADQPGCVGTCHLDGPAVEAHARACTEAEVTAGFHVIGDAA 324
Cdd:cd01300  241 LEELGARKNGAGDDRLRLGGVKLFADGSLGSRTAALSEPYLDSPGTGGLLLISPEELEELVRAADEAGLQVAIHAIGDRA 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505168603 325 VATVVDAFERVVADLGvvaVARCGHRLEHAEMVTAEQAAKLGAWGIIASVQPNFDALWGGAEGMYarRLGPKRARLLNPL 404
Cdd:cd01300  321 VDTVLDALEAALKDNP---RADHRHRIEHAQLVSPDDIPRFAKLGVIASVQPNHLYSDGDAAEDR--RLGEERAKRSYPF 395

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505168603 405 ALLASQGVPLAFGSDAPVTGFDPWASVRAAVNHHTAGSAVSARAAFA--------AATRGGWRAAGvRDGKTGTLVPGAP 476
Cdd:cd01300  396 RSLLDAGVPVALGSDAPVAPPDPLLGIWAAVTRKTPGGGVLGNPEERlsleealrAYTIGAAYAIG-EEDEKGSLEPGKL 474


                 ....*
gi 505168603 477 ASYAV 481
Cdd:cd01300  475 ADFVV 479
Amidohydro_3 pfam07969
Amidohydrolase family;
49-498 3.90e-70

Amidohydrolase family;


Pssm-ID: 400360 [Multi-domain]  Cd Length: 464  Bit Score: 232.04  E-value: 3.90e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505168603   49 QVEDLDGGLVAPGFVDSHIHLTATGLTISGLDLRPASslggCLQLAADHAAAHP-GQPLWGHGWDESAWPQHIAPST-AQ 126
Cdd:pfam07969   1 EVIDAKGRLVLPGFVDPHTHLDGGGLNLRELRLPDVL----PNAVVKGQAGRTPkGRWLVGEGWDEAQFAETRFPYAlAD 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505168603  127 LDAVLGERPAYLARVDVHSALASSGLRRLVPHLSEAA------------GFTEQGPLTGEAHHLVRARARDlltqpQLAE 194
Cdd:pfam07969  77 LDEVAPDGPVLLRALHTHAAVANSAALDLAGITKATEdppggeiardanGEGLTGLLREGAYALPPLLARE-----AEAA 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505168603  195 ARTAALGSLAAAGIVAVhECGGPEIGGLDDWLQLSALPHgvEVIGYWGEAVTTAAQARTLMAETGARglAGDLFVDGALG 274
Cdd:pfam07969 152 AVAAALAALPGFGITSV-DGGGGNVHSLDDYEPLRELTA--AEKLKELLDAPERLGLPHSIYELRIG--AMKLFADGVLG 226

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505168603  275 SRTAWLHEPYADQPGCvGTCHLDGPAVEAHARACTEAEVTAGFHVIGDAAVATVVDAFERVVADLGVVAVarcgHRLEHA 354
Cdd:pfam07969 227 SRTAALTEPYFDAPGT-GWPDFEDEALAELVAAARERGLDVAIHAIGDATIDTALDAFEAVAEKLGNQGR----VRIEHA 301

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505168603  355 EMV---TAEQAAKLGAWGIIASVQPNFDALWGGAEGMyarRLGPKRARLLNPLALLASQGVPLAFGSDAPVTGFDPWASV 431
Cdd:pfam07969 302 QGVvpyTYSQIERVAALGGAAGVQPVFDPLWGDWLQD---RLGAERARGLTPVKELLNAGVKVALGSDAPVGPFDPWPRI 378

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 505168603  432 RAAVNHHTAGSAVSARAAFAA--------ATRGGWRAAGVRDgKTGTLVPGAPASYAVWDAGALTVSAPRDAVQR 498
Cdd:pfam07969 379 GAAVMRQTAGGGEVLGPDEELsleealalYTSGPAKALGLED-RKGTLGVGKDADLVVLDDDPLTVDPPAIADIR 452
PRK09228 PRK09228
guanine deaminase; Provisional
 24-68 1.98e-06

guanine deaminase; Provisional


Pssm-ID: 236419 [Multi-domain]  Cd Length: 433  Bit Score: 50.19  E-value: 1.98e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 505168603  24 AMAVRGDTVAWLGSDEVGRNQFP-DAQVEDLDGGLVAPGFVDSHIH 68
Cdd:PRK09228  33 LLLVEDGRIVAAGPYAELRAQLPaDAEVTDYRGKLILPGFIDTHIH 78
guan_deamin TIGR02967
guanine deaminase; This model describes guanine deaminase, which hydrolyzes guanine to ...
 19-68 3.24e-04

guanine deaminase; This model describes guanine deaminase, which hydrolyzes guanine to xanthine and ammonia. Xanthine can then be converted to urate by xanthine dehydrogenase, and urate subsequently degraded. In some bacteria, the guanine deaminase gene is found near the xdhABC genes for xanthine dehydrogenase. Non-homologous forms of guanine deaminase also exist, as well as distantly related forms outside the scope of this model. [Purines, pyrimidines, nucleosides, and nucleotides, Other]


Pssm-ID: 132012 [Multi-domain]  Cd Length: 401  Bit Score: 43.01  E-value: 3.24e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 505168603   19 HPDAtAMAVRGDTVAWLGS-DEVGRNQFPDAQVEDLDGGLVAPGFVDSHIH 68
Cdd:TIGR02967   4 FEDG-LLVVENGRIVAVGDyAELKETLPAGVEIDDYRGHLIMPGFIDTHIH 53
 
Name Accession Description Interval E-value
YtcJ COG1574
Predicted amidohydrolase YtcJ [General function prediction only];
6-533 3.61e-121

Predicted amidohydrolase YtcJ [General function prediction only];


Pssm-ID: 441182 [Multi-domain]  Cd Length: 535  Bit Score: 366.43  E-value: 3.61e-121
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505168603   6 TKLLVNGRVY--SPTHPDATAMAVRGDTVAWLGSDEVGRNQF-PDAQVEDLDGGLVAPGFVDSHIHLTATGLTISGLDLR 82
Cdd:COG1574    9 DLLLTNGRIYtmDPAQPVAEAVAVRDGRIVAVGSDAEVRALAgPATEVIDLGGKTVLPGFIDAHVHLLGGGLALLGVDLS 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505168603  83 PASSLGGCLQLAADHAAAHP-GQPLWGHGWDESAWPQHIAPSTAQLDAVLGERPAYLARVDVHSALASS-GLrrlvphls 160
Cdd:COG1574   89 GARSLDELLARLRAAAAELPpGEWILGRGWDESLWPEGRFPTRADLDAVSPDRPVVLTRVDGHAAWVNSaAL-------- 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505168603 161 EAAGFTEQ------------------GPLTGEAHHLVRARARDLlTQPQLAEARTAALGSLAAAGIVAVHECGGPEiGGL 222
Cdd:COG1574  161 ELAGITADtpdpeggeierdadgeptGVLREAAMDLVRAAIPPP-TPEELRAALRAALRELASLGITSVHDAGLGP-DDL 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505168603 223 DDWLQLSA---LPhgVEVIGYWGEAVTTAAQARTLMAETGARG----LAG-DLFVDGALGSRTAWLHEPYADQPGCVGTC 294
Cdd:COG1574  239 AAYRELAAageLP--LRVVLYLGADDEDLEELLALGLRTGYGDdrlrVGGvKLFADGSLGSRTAALLEPYADDPGNRGLL 316

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505168603 295 HLDGPAVEAHARACTEAEVTAGFHVIGDAAVATVVDAFERVVADLGvvaVARCGHRLEHAEMVTAEQAAKLGAWGIIASV 374
Cdd:COG1574  317 LLDPEELRELVRAADAAGLQVAVHAIGDAAVDEVLDAYEAARAANG---RRDRRHRIEHAQLVDPDDLARFAELGVIASM 393

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505168603 375 QPNFDALWGgaeGMYARRLGPKRARLLNPLALLASQGVPLAFGSDAPVTGFDPWASVRAAVNHHTAGSAVSARAAF---- 450
Cdd:COG1574  394 QPTHATSDG---DWAEDRLGPERAARAYPFRSLLDAGAPLAFGSDAPVEPLDPLLGIYAAVTRRTPSGRGLGPEERltve 470

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505168603 451 ---AAATRGGWRAAGvRDGKTGTLVPGAPASYAVWDAGALTVSAPRdavqrwstdprsrvpaLPRLdpadplpRCRQTVH 527
Cdd:COG1574  471 ealRAYTIGAAYAAF-EEDEKGSLEPGKLADFVVLDRDPLTVPPEE----------------IKDI-------KVLLTVV 526


                 ....*.
gi 505168603 528 RGAVIY 533
Cdd:COG1574  527 GGRVVY 532
YtcJ_like cd01300
YtcJ_like metal dependent amidohydrolases. YtcJ is a Bacillus subtilis ORF of unknown function. ...
 24-481 8.53e-100

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: 309.62  E-value: 8.53e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505168603  24 AMAVRGDTVAWLGSD-EVGRNQFPDAQVEDLDGGLVAPGFVDSHIHLTATGLTISGLDLRPASSLG-GCLQLAADHAAAH 101
Cdd:cd01300    1 AVAVRDGRIVAVGSDaEAKALKGPATEVIDLKGKTVLPGFIDSHSHLLLGGLSLLWLDLSGVTSKEeALARIREDAAAAP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505168603 102 PGQPLWGHGWDESAWPQHIAPSTAQLDAVLGERPAYLARVDVHSALASS-GLRRL-VPHLSE-----AAGFTEQGPLTG- 173
Cdd:cd01300   81 PGEWILGFGWDESLLGEGRYPTRAELDAVSPDRPVLLLRRDGHSAWVNSaALRLAgITRDTPdppggEIVRDADGEPTGv 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505168603 174 --EAHHLVRARARDLLTQPQLAEARTAALGSLAAAGIVAVHECGGPEIGGLDDWLQLSALP-------HGVEVIGYWGEA 244
Cdd:cd01300  161 lvEAAAALVLEAVPPPTPEERRAALRAAARELASLGVTTVHDAGGGAADDIEAYRRLAAAGeltlrvrVALYVSPLAEDL 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505168603 245 VTTAAQARTLMAETGARGLAGDLFVDGALGSRTAWLHEPYADQPGCVGTCHLDGPAVEAHARACTEAEVTAGFHVIGDAA 324
Cdd:cd01300  241 LEELGARKNGAGDDRLRLGGVKLFADGSLGSRTAALSEPYLDSPGTGGLLLISPEELEELVRAADEAGLQVAIHAIGDRA 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505168603 325 VATVVDAFERVVADLGvvaVARCGHRLEHAEMVTAEQAAKLGAWGIIASVQPNFDALWGGAEGMYarRLGPKRARLLNPL 404
Cdd:cd01300  321 VDTVLDALEAALKDNP---RADHRHRIEHAQLVSPDDIPRFAKLGVIASVQPNHLYSDGDAAEDR--RLGEERAKRSYPF 395

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505168603 405 ALLASQGVPLAFGSDAPVTGFDPWASVRAAVNHHTAGSAVSARAAFA--------AATRGGWRAAGvRDGKTGTLVPGAP 476
Cdd:cd01300  396 RSLLDAGVPVALGSDAPVAPPDPLLGIWAAVTRKTPGGGVLGNPEERlsleealrAYTIGAAYAIG-EEDEKGSLEPGKL 474


                 ....*
gi 505168603 477 ASYAV 481
Cdd:cd01300  475 ADFVV 479
Amidohydro_3 pfam07969
Amidohydrolase family;
49-498 3.90e-70

Amidohydrolase family;


Pssm-ID: 400360 [Multi-domain]  Cd Length: 464  Bit Score: 232.04  E-value: 3.90e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505168603   49 QVEDLDGGLVAPGFVDSHIHLTATGLTISGLDLRPASslggCLQLAADHAAAHP-GQPLWGHGWDESAWPQHIAPST-AQ 126
Cdd:pfam07969   1 EVIDAKGRLVLPGFVDPHTHLDGGGLNLRELRLPDVL----PNAVVKGQAGRTPkGRWLVGEGWDEAQFAETRFPYAlAD 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505168603  127 LDAVLGERPAYLARVDVHSALASSGLRRLVPHLSEAA------------GFTEQGPLTGEAHHLVRARARDlltqpQLAE 194
Cdd:pfam07969  77 LDEVAPDGPVLLRALHTHAAVANSAALDLAGITKATEdppggeiardanGEGLTGLLREGAYALPPLLARE-----AEAA 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505168603  195 ARTAALGSLAAAGIVAVhECGGPEIGGLDDWLQLSALPHgvEVIGYWGEAVTTAAQARTLMAETGARglAGDLFVDGALG 274
Cdd:pfam07969 152 AVAAALAALPGFGITSV-DGGGGNVHSLDDYEPLRELTA--AEKLKELLDAPERLGLPHSIYELRIG--AMKLFADGVLG 226

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505168603  275 SRTAWLHEPYADQPGCvGTCHLDGPAVEAHARACTEAEVTAGFHVIGDAAVATVVDAFERVVADLGVVAVarcgHRLEHA 354
Cdd:pfam07969 227 SRTAALTEPYFDAPGT-GWPDFEDEALAELVAAARERGLDVAIHAIGDATIDTALDAFEAVAEKLGNQGR----VRIEHA 301

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505168603  355 EMV---TAEQAAKLGAWGIIASVQPNFDALWGGAEGMyarRLGPKRARLLNPLALLASQGVPLAFGSDAPVTGFDPWASV 431
Cdd:pfam07969 302 QGVvpyTYSQIERVAALGGAAGVQPVFDPLWGDWLQD---RLGAERARGLTPVKELLNAGVKVALGSDAPVGPFDPWPRI 378

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 505168603  432 RAAVNHHTAGSAVSARAAFAA--------ATRGGWRAAGVRDgKTGTLVPGAPASYAVWDAGALTVSAPRDAVQR 498
Cdd:pfam07969 379 GAAVMRQTAGGGEVLGPDEELsleealalYTSGPAKALGLED-RKGTLGVGKDADLVVLDDDPLTVDPPAIADIR 452
SsnA COG0402
Cytosine/adenosine deaminase or related metal-dependent hydrolase [Nucleotide transport and ...
 24-69 4.50e-07

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: 52.14  E-value: 4.50e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 505168603  24 AMAVRGDTVAWLGSDEVGRNQFPDAQVEDLDGGLVAPGFVDSHIHL 69
Cdd:COG0402   23 AVLVEDGRIAAVGPGAELPARYPAAEVIDAGGKLVLPGLVNTHTHL 68
Isoaspartyl-dipeptidase cd01308
Isoaspartyl dipeptidase hydrolyzes the beta-L-isoaspartyl linkages in dipeptides, as part of ...
 7-73 8.77e-07

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: 51.24  E-value: 8.77e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 505168603   7 KLLVNGRVYSPTHPDATAMAVRGDTVAWLGsDEVGRNQFPDAQVEDLDGGLVAPGFVDSHIHLTATG 73
Cdd:cd01308    2 TLIKNAEVYAPEYLGKKDILIAGGKILAIE-DQLNLPGYENVTVVDLHGKILVPGFIDQHVHIIGGG 67
PRK09228 PRK09228
guanine deaminase; Provisional
 24-68 1.98e-06

guanine deaminase; Provisional


Pssm-ID: 236419 [Multi-domain]  Cd Length: 433  Bit Score: 50.19  E-value: 1.98e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 505168603  24 AMAVRGDTVAWLGSDEVGRNQFP-DAQVEDLDGGLVAPGFVDSHIH 68
Cdd:PRK09228  33 LLLVEDGRIVAAGPYAELRAQLPaDAEVTDYRGKLILPGFIDTHIH 78
NagA COG1820
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism];
8-68 3.25e-06

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


Pssm-ID: 441425 [Multi-domain]  Cd Length: 373  Bit Score: 49.33  E-value: 3.25e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 505168603   8 LLVNGRVYSPTHP-DATAMAVRGDTVAwlgsdEVGRNQFPDAQVEDLDGGLVAPGFVDSHIH 68
Cdd:COG1820    1 AITNARIFTGDGVlEDGALLIEDGRIA-----AIGPGAEPDAEVIDLGGGYLAPGFIDLHVH 57
PRK07203 PRK07203
putative aminohydrolase SsnA;
8-78 9.18e-06

putative aminohydrolase SsnA;


Pssm-ID: 235963 [Multi-domain]  Cd Length: 442  Bit Score: 48.01  E-value: 9.18e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 505168603   8 LLVNGRVYS--PTHP--DATAMAVRGDTVAWLGSDEVGRNQFPDAQVEDLDGGLVAPGFVDSHIHLTAT---GLTISG 78
Cdd:PRK07203   3 LIGNGTAITrdPAKPviEDGAIAIEGNVIVEIGTTDELKAKYPDAEFIDAKGKLIMPGLINSHNHIYSGlarGMMANI 80
HutI COG1228
Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport ...
 340-499 1.01e-05

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


Pssm-ID: 440841 [Multi-domain]  Cd Length: 386  Bit Score: 48.03  E-value: 1.01e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505168603 340 GVVAVARCGHR-LEHAEMVTAEQAAKLGAWGIIASV--QPNFDALWGGAEGMYARRLGPKRARLLNPLALLASQGVPLAF 416
Cdd:COG1228  217 DIRLAVEAGVDsIEHGTYLDDEVADLLAEAGTVVLVptLSLFLALLEGAAAPVAAKARKVREAALANARRLHDAGVPVAL 296

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505168603 417 GSDAPVT-----------------GFDPWASVRAAvnhhtagsavsaraafaaaTRGGWRAAGvRDGKTGTLVPGAPASY 479
Cdd:COG1228  297 GTDAGVGvppgrslhrelalaveaGLTPEEALRAA-------------------TINAAKALG-LDDDVGSLEPGKLADL 356

                        170       180
                 ....*....|....*....|.
gi 505168603 480 AVWDAGALT-VSAPRDAVQRW 499
Cdd:COG1228  357 VLLDGDPLEdIAYLEDVRAVM 377
D-HYD cd01314
D-hydantoinases (D-HYD) also called dihydropyrimidases (DHPase) and related proteins; DHPases ...
 7-106 2.31e-05

D-hydantoinases (D-HYD) also called dihydropyrimidases (DHPase) and related proteins; DHPases are a family of enzymes that catalyze the reversible hydrolytic ring opening of the amide bond in five- or six-membered cyclic diamides, like dihydropyrimidine or hydantoin. The hydrolysis of dihydropyrimidines is the second step of reductive catabolism of pyrimidines in human. The hydrolysis of 5-substituted hydantoins in microorganisms leads to enantiomerically pure N-carbamyl amino acids, which are used for the production of antibiotics, peptide hormones, pyrethroids, and pesticides. HYDs are classified depending on their stereoselectivity. This family also includes collapsin response regulators (CRMPs), cytosolic proteins involved in neuronal differentiation and axonal guidance which have strong homology to DHPases, but lack most of the active site residues.


Pssm-ID: 238639 [Multi-domain]  Cd Length: 447  Bit Score: 46.83  E-value: 2.31e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505168603   7 KLLVNGRVYSPTHPDATAMAVRGDTVAWLGSDEVGRnqfPDAQVEDLDGGLVAPGFVDSHIHL-TATGLTISGLDLRPA- 84
Cdd:cd01314    1 LIIKNGTIVTADGSFKADILIEDGKIVAIGPNLEAP---GGVEVIDATGKYVLPGGIDPHTHLeLPFMGTVTADDFESGt 77

                         90       100
                 ....*....|....*....|...
gi 505168603  85 -SSLGGCLQLAADHAAAHPGQPL 106
Cdd:cd01314   78 rAAAAGGTTTIIDFAIPNKGQSL 100
pyrC PRK09357
dihydroorotase; Validated
 5-69 3.13e-05

dihydroorotase; Validated


Pssm-ID: 236479 [Multi-domain]  Cd Length: 423  Bit Score: 46.34  E-value: 3.13e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 505168603   5 STKLLVNGRVYSPTHPDATA-MAVRGDTVAWLGSDEVgrnqFPDAQVEDLDGGLVAPGFVDSHIHL 69
Cdd:PRK09357   1 MMILIKNGRVIDPKGLDEVAdVLIDDGKIAAIGENIE----AEGAEVIDATGLVVAPGLVDLHVHL 62
AllB COG0044
Dihydroorotase or related cyclic amidohydrolase [Nucleotide transport and metabolism]; ...
 8-69 3.57e-05

Dihydroorotase or related cyclic amidohydrolase [Nucleotide transport and metabolism]; Dihydroorotase or related cyclic amidohydrolase is part of the Pathway/BioSystem: Pyrimidine biosynthesis


Pssm-ID: 439814 [Multi-domain]  Cd Length: 439  Bit Score: 46.24  E-value: 3.57e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 505168603   8 LLVNGRVYSPTHPDATAMAVRGDTVAWLGSDEVGrnqFPDAQVEDLDGGLVAPGFVDSHIHL 69
Cdd:COG0044    1 LIKNGRVVDPGGLERADVLIEDGRIAAIGPDLAA---PEAAEVIDATGLLVLPGLIDLHVHL 59
Imidazolone-5PH cd01296
Imidazolonepropionase/imidazolone-5-propionate hydrolase (Imidazolone-5PH) catalyzes the third ...
 26-69 4.95e-05

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


Pssm-ID: 238621 [Multi-domain]  Cd Length: 371  Bit Score: 45.71  E-value: 4.95e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 505168603  26 AVRGDTVAWLG-SDEVGRNQFPDAQVEDLDGGLVAPGFVDSHIHL 69
Cdd:cd01296    2 AIRDGRIAAVGpAASLPAPGPAAAEEIDAGGRAVTPGLVDCHTHL 46
SsnA COG0402
Cytosine/adenosine deaminase or related metal-dependent hydrolase [Nucleotide transport and ...
 403-499 1.89e-04

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: 44.05  E-value: 1.89e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505168603 403 PLALLASQGVPLAFGSD--APVTGFDPWASVRAAVNHHTAGSAVSARAAFAA----ATRGGWRAAGvRDGKTGTLVPGAP 476
Cdd:COG0402  293 PVPRLLAAGVRVGLGTDgaASNNSLDMFEEMRLAALLQRLRGGDPTALSAREalemATLGGARALG-LDDEIGSLEPGKR 371

                         90       100
                 ....*....|....*....|...
gi 505168603 477 ASYAVWDAGALTVSAPRDAVQRW 499
Cdd:COG0402  372 ADLVVLDLDAPHLAPLHDPLSAL 394
guan_deamin TIGR02967
guanine deaminase; This model describes guanine deaminase, which hydrolyzes guanine to ...
 19-68 3.24e-04

guanine deaminase; This model describes guanine deaminase, which hydrolyzes guanine to xanthine and ammonia. Xanthine can then be converted to urate by xanthine dehydrogenase, and urate subsequently degraded. In some bacteria, the guanine deaminase gene is found near the xdhABC genes for xanthine dehydrogenase. Non-homologous forms of guanine deaminase also exist, as well as distantly related forms outside the scope of this model. [Purines, pyrimidines, nucleosides, and nucleotides, Other]


Pssm-ID: 132012 [Multi-domain]  Cd Length: 401  Bit Score: 43.01  E-value: 3.24e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 505168603   19 HPDAtAMAVRGDTVAWLGS-DEVGRNQFPDAQVEDLDGGLVAPGFVDSHIH 68
Cdd:TIGR02967   4 FEDG-LLVVENGRIVAVGDyAELKETLPAGVEIDDYRGHLIMPGFIDTHIH 53
AdeC COG1001
Adenine deaminase [Nucleotide transport and metabolism];
26-68 4.71e-04

Adenine deaminase [Nucleotide transport and metabolism];


Pssm-ID: 440625 [Multi-domain]  Cd Length: 559  Bit Score: 42.78  E-value: 4.71e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 505168603  26 AVRGDTVAWlgsdeVGRNQFPDAQVEDLDGGLVAPGFVDSHIH 68
Cdd:COG1001   28 AIAGGRIAG-----VGDYIGEATEVIDAAGRYLVPGFIDGHVH 65
ATZ_TRZ_like cd01298
TRZ/ATZ family contains enzymes from the atrazine degradation pathway and related hydrolases. ...
 24-74 1.03e-03

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


Pssm-ID: 238623 [Multi-domain]  Cd Length: 411  Bit Score: 41.42  E-value: 1.03e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 505168603  24 AMAVRGDTVAWLGSDEVgRNQFPDAQVEDLDGGLVAPGFVDSHIHLTATGL 74
Cdd:cd01298   21 DVLVEDGRIVAVGPALP-LPAYPADEVIDAKGKVVMPGLVNTHTHLAMTLL 70
isoAsp_dipep TIGR01975
isoaspartyl dipeptidase IadA; The L-isoaspartyl derivative of Asp arises non-enzymatically ...
 7-73 1.09e-03

isoaspartyl dipeptidase IadA; The L-isoaspartyl derivative of Asp arises non-enzymatically over time as a form of protein damage. In this isomerization, the connectivity of the polypeptide changes to pass through the beta-carboxyl of the side chain. Much but not all of this damage can be repaired by protein-L-isoaspartate (D-aspartate) O-methyltransferase. This model describes the isoaspartyl dipeptidase IadA, apparently one of two such enzymes in E. coli, an enzyme that degrades isoaspartyl dipeptides and may unblock degradation of proteins that cannot be repaired. This model also describes closely related proteins from other species (e.g. Clostridium perfringens, Thermoanaerobacter tengcongensis) that we assume to be equivalent in function. This family shows homology to dihydroorotases. [Protein fate, Degradation of proteins, peptides, and glycopeptides]


Pssm-ID: 131030  Cd Length: 389  Bit Score: 41.31  E-value: 1.09e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 505168603    7 KLLVNGRVYSPTHPDATAMAVRGDTVAWLGSD-EVGRNQFPDAQVEDLDGGLVAPGFVDSHIHLTATG 73
Cdd:TIGR01975   2 TLLKGAEVYAPEYIGKKDILIANDKIIAIADEiPSTKDFVPNCVVVGLEGMIAVPGFIDQHVHIIGGG 69
PRK05985 PRK05985
cytosine deaminase; Provisional
 8-72 1.46e-03

cytosine deaminase; Provisional


Pssm-ID: 180337 [Multi-domain]  Cd Length: 391  Bit Score: 41.07  E-value: 1.46e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 505168603   8 LLVNGRvysPTHPDATAMAVRGDTVAWLGSDevgRNQFPDAQVEDLDGGLVAPGFVDSHIHLTAT 72
Cdd:PRK05985   5 LFRNVR---PAGGAAVDILIRDGRIAAIGPA---LAAPPGAEVEDGGGALALPGLVDGHIHLDKT 63
D-aminoacylase cd01297
D-aminoacylases (N-acyl-D-Amino acid amidohydrolases) catalyze the hydrolysis of ...
 8-88 2.63e-03

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: 40.36  E-value: 2.63e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505168603   8 LLVNGRVYSPT-HPDATA-MAVRGDTVAwlgsdEVGRNQFPDAQ-VEDLDGGLVAPGFVDSHIHLTATGLTISglDLRPA 84
Cdd:cd01297    3 VIRNGTVVDGTgAPPFTAdVGIRDGRIA-----AIGPILSTSAReVIDAAGLVVAPGFIDVHTHYDGQVFWDP--DLRPS 75


                 ....
gi 505168603  85 SSLG 88
Cdd:cd01297   76 SRQG 79
Bact_CD cd01293
Bacterial cytosine deaminase and related metal-dependent hydrolases. Cytosine deaminases (CDs) ...
 46-72 3.83e-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: 39.54  E-value: 3.83e-03
                         10        20
                 ....*....|....*....|....*..
gi 505168603  46 PDAQVEDLDGGLVAPGFVDSHIHLTAT 72
Cdd:cd01293   35 PDAEEVDAKGRLVLPAFVDPHIHLDKT 61
PRK08418 PRK08418
metal-dependent hydrolase;
35-69 5.63e-03

metal-dependent hydrolase;


Pssm-ID: 181419 [Multi-domain]  Cd Length: 408  Bit Score: 39.18  E-value: 5.63e-03
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 505168603  35 LGSDEVGRNQFPDAQVEDLDGGLVAPGFVDSHIHL 69
Cdd:PRK08418  33 IGDYENLKKKYPNAKIQFFKNSVLLPAFINPHTHL 67
NagA cd00854
N-acetylglucosamine-6-phosphate deacetylase, NagA, catalyzes the hydrolysis of the N-acetyl ...
 45-68 5.63e-03

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


Pssm-ID: 238434 [Multi-domain]  Cd Length: 374  Bit Score: 39.10  E-value: 5.63e-03
                         10        20
                 ....*....|....*....|....
gi 505168603  45 FPDAQVEDLDGGLVAPGFVDSHIH 68
Cdd:cd00854   36 EEADEIIDLKGQYLVPGFIDIHIH 59
GDEase cd01303
Guanine deaminase (GDEase). Guanine deaminase is an aminohydrolase responsible for the ...
 24-81 6.63e-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: 39.18  E-value: 6.63e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 505168603  24 AMAVRGDTVAWLGSDEVGRNQF-PDAQVEDLDGGLVAPGFVDSHIHLTATGLTISGLDL 81
Cdd:cd01303   28 LIVVVDGNIIAAGAAETLKRAAkPGARVIDSPNQFILPGFIDTHIHAPQYANIGSGLGE 86
PRK08204 PRK08204
hypothetical protein; Provisional
 8-74 8.97e-03

hypothetical protein; Provisional


Pssm-ID: 181288 [Multi-domain]  Cd Length: 449  Bit Score: 38.44  E-value: 8.97e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 505168603   8 LLVNGRVYS--PTHPDATA--MAVRGDTVAwlgsdEVGRN-QFPDAQVEDLDGGLVAPGFVDSHIHLTATGL 74
Cdd:PRK08204   5 LIRGGTVLTmdPAIGDLPRgdILIEGDRIA-----AVAPSiEAPDAEVVDARGMIVMPGLVDTHRHTWQSVL 71
PRK07228 PRK07228
5'-deoxyadenosine deaminase;
24-72 9.18e-03

5'-deoxyadenosine deaminase;


Pssm-ID: 180895 [Multi-domain]  Cd Length: 445  Bit Score: 38.44  E-value: 9.18e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 505168603  24 AMAVRGDTVAWLGSDEVGRNqfpDAQVEDLDGGLVAPGFVDSHIHLTAT 72
Cdd:PRK07228  23 DVLIEDDRIAAVGDRLDLED---YDDHIDATGKVVIPGLIQGHIHLCQT 68
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH