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Conserved domains on  [gi|1755663628|gb|QEY35650|]
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N-acetylglucosamine-6-phosphate deacetylase [Caproiciproducens galactitolivorans]

Protein Classification

N-acetylglucosamine-6-phosphate deacetylase( domain architecture ID 10788057)

N-acetylglucosamine-6-phosphate deacetylase catalyzes the hydrolysis of the N-acetyl group of N-acetyl-glucosamine-6-phosphate (GlcNAc-6-P) to glucosamine 6-phosphate and acetate, which is the first committed step in the biosynthetic pathway to amino-sugar

CATH:  3.20.20.140|2.30.40.10
EC:  3.5.1.25
Gene Ontology:  GO:0008448|GO:0046872|GO:0005975|GO:0046349
PubMed:  17567048|17567047|9144792
SCOP:  4002805|4002851

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
NagA COG1820
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism];
2-372 6.46e-173

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


:

Pssm-ID: 441425 [Multi-domain]  Cd Length: 373  Bit Score: 486.53  E-value: 6.46e-173
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755663628   2 ILKNAKIVDDSFRFADADVAVEEDKISEIAPGLAGGEE-IDLSGCVLVPGFVDIHIHACVGADTCDADADGLAKMCAHLV 80
Cdd:COG1820     1 AITNARIFTGDGVLEDGALLIEDGRIAAIGPGAEPDAEvIDLGGGYLAPGFIDLHVHGGGGVDFMDGTPEALRTIARAHA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755663628  81 TKGVTSFCPTTMTVSHKGILRALETVKSCMDHPPkGAAIAGVNMEGPYISIHKKGAQKGEFVKNSDFKEFQEFYDTCGGI 160
Cdd:COG1820    81 RHGTTSFLPTTITAPPEDLLRALAAIAEAIEQGG-GAGILGIHLEGPFLSPEKKGAHPPEYIRPPDPEELDRLLEAAGGL 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755663628 161 IKLVDIAPECPGAEEFIPQASRL-CTVSIAHTEADYACAKHAFELGITHATHLYNAMPGMKHREPGVIGAVLDDPRVRAE 239
Cdd:COG1820   160 IKLVTLAPELPGALEFIRYLVEAgVVVSLGHTDATYEQARAAFEAGATHVTHLFNAMSPLHHREPGVVGAALDDDDVYAE 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755663628 240 LICDGFHIHPAVLRITFEALGKDRVVIVSDSMRAAGAPDGVSELGGQTVYVKDGQARLKDGTIAGSTTNLHQEIKNLVGW 319
Cdd:COG1820   240 LIADGIHVHPAAVRLALRAKGPDRLILVTDAMAAAGLPDGEYELGGLEVTVKDGVARLADGTLAGSTLTMDDAVRNLVEW 319

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1755663628 320 -GVPFLTAIQAATLNPARAIHEDERIGSIKVGKYADMVALDSDLNIRMVVARGK 372
Cdd:COG1820   320 tGLPLEEAVRMASLNPARALGLDDRKGSIAPGKDADLVVLDDDLNVRATWVGGE 373
 
Name Accession Description Interval E-value
NagA COG1820
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism];
2-372 6.46e-173

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


Pssm-ID: 441425 [Multi-domain]  Cd Length: 373  Bit Score: 486.53  E-value: 6.46e-173
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755663628   2 ILKNAKIVDDSFRFADADVAVEEDKISEIAPGLAGGEE-IDLSGCVLVPGFVDIHIHACVGADTCDADADGLAKMCAHLV 80
Cdd:COG1820     1 AITNARIFTGDGVLEDGALLIEDGRIAAIGPGAEPDAEvIDLGGGYLAPGFIDLHVHGGGGVDFMDGTPEALRTIARAHA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755663628  81 TKGVTSFCPTTMTVSHKGILRALETVKSCMDHPPkGAAIAGVNMEGPYISIHKKGAQKGEFVKNSDFKEFQEFYDTCGGI 160
Cdd:COG1820    81 RHGTTSFLPTTITAPPEDLLRALAAIAEAIEQGG-GAGILGIHLEGPFLSPEKKGAHPPEYIRPPDPEELDRLLEAAGGL 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755663628 161 IKLVDIAPECPGAEEFIPQASRL-CTVSIAHTEADYACAKHAFELGITHATHLYNAMPGMKHREPGVIGAVLDDPRVRAE 239
Cdd:COG1820   160 IKLVTLAPELPGALEFIRYLVEAgVVVSLGHTDATYEQARAAFEAGATHVTHLFNAMSPLHHREPGVVGAALDDDDVYAE 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755663628 240 LICDGFHIHPAVLRITFEALGKDRVVIVSDSMRAAGAPDGVSELGGQTVYVKDGQARLKDGTIAGSTTNLHQEIKNLVGW 319
Cdd:COG1820   240 LIADGIHVHPAAVRLALRAKGPDRLILVTDAMAAAGLPDGEYELGGLEVTVKDGVARLADGTLAGSTLTMDDAVRNLVEW 319

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1755663628 320 -GVPFLTAIQAATLNPARAIHEDERIGSIKVGKYADMVALDSDLNIRMVVARGK 372
Cdd:COG1820   320 tGLPLEEAVRMASLNPARALGLDDRKGSIAPGKDADLVVLDDDLNVRATWVGGE 373
NagA cd00854
N-acetylglucosamine-6-phosphate deacetylase, NagA, catalyzes the hydrolysis of the N-acetyl ...
 1-371 1.91e-151

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: 432.00  E-value: 1.91e-151
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755663628   1 MILKNAKIVDDSFRFaDADVAVEEDKISEIAPGL---AGGEEIDLSGCVLVPGFVDIHIHACVGADTCDADADGLAKMCA 77
Cdd:cd00854     1 LIIKNARILTPGGLE-DGAVLVEDGKIVAIGPEDeleEADEIIDLKGQYLVPGFIDIHIHGGGGADFMDGTAEALKTIAE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755663628  78 HLVTKGVTSFCPTTMTVSHKGILRALETVKSCMDHPpKGAAIAGVNMEGPYISIHKKGAQKGEFVKNSDFKEFQEFYDTC 157
Cdd:cd00854    80 ALAKHGTTSFLPTTVTAPPEEIAKALAAIAEAIAEG-QGAEILGIHLEGPFISPEKKGAHPPEYLRAPDPEELKKWLEAA 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755663628 158 GGIIKLVDIAPECPGAEEFIPQ-ASRLCTVSIAHTEADYACAKHAFELGITHATHLYNAMPGMKHREPGVIGAVLDDPRV 236
Cdd:cd00854   159 GGLIKLVTLAPELDGALELIRYlVERGIIVSIGHSDATYEQAVAAFEAGATHVTHLFNAMSPLHHREPGVVGAALSDDDV 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755663628 237 RAELICDGFHIHPAVLRITFEALGKDRVVIVSDSMRAAGAPDGVSELGGQTVYVKDGQARLKDGTIAGSTTNLHQEIKNL 316
Cdd:cd00854   239 YAELIADGIHVHPAAVRLAYRAKGADKIVLVTDAMAAAGLPDGEYELGGQTVTVKDGVARLADGTLAGSTLTMDQAVRNM 318

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1755663628 317 VGW-GVPFLTAIQAATLNPARAIHEDERIGSIKVGKYADMVALDSDLNIRMVVARG 371
Cdd:cd00854   319 VKWgGCPLEEAVRMASLNPAKLLGLDDRKGSLKPGKDADLVVLDDDLNVKATWING 374
nagA TIGR00221
N-acetylglucosamine-6-phosphate deacetylase; [Central intermediary metabolism, Amino sugars]
 3-372 3.85e-104

N-acetylglucosamine-6-phosphate deacetylase; [Central intermediary metabolism, Amino sugars]


Pssm-ID: 272968  Cd Length: 380  Bit Score: 312.15  E-value: 3.85e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755663628   3 LKNAKIVDDSFRFADADVAVEEDKISEI---APGLAGGEEIDLSGCVLVPGFVDIHIHACVGADTCDADADGLAKMCAHL 79
Cdd:TIGR00221   7 LKDIAIVTGNEVIDNGAVGINDGKISTVsteAELEPEIKEIDLPGNVLTPGFIDIHIHGCGGVDTNDASFETLEIMSERL 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755663628  80 VTKGVTSFCPTTMTVSHKGILRALETVKSCMDHPpKGAAIAGVNMEGPYISIHKKGAQKGEFVKNSDFKEFQEFYDTCGG 159
Cdd:TIGR00221  87 PKSGCTSFLPTLITQPDENIKQAVKNMREYLAKE-KNAQALGLHLEGPFLSPEKKGAHPPEYIREPDVELFKKFLCEAGG 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755663628 160 IIKLVDIAPECPGAEEFIPQ-ASRLCTVSIAHTEADYACAKHAFELGITHATHLYNAMPGMKHREPGVIGAVLDDPRVRA 238
Cdd:TIGR00221 166 VITKVTLAPEEDQHFELIRHlKDAGIIVSAGHTNATYELAKAAFKAGATHATHLYNAMSPIHHREPGVIGAVLDHDDVYT 245

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755663628 239 ELICDGFHIHPAVLRITFEALGKDRVVIVSDSMRAAGAPDGVSELGGQTVYVKDGQARLKDGTIAGSTTNLHQEIKNLVG 318
Cdd:TIGR00221 246 EIIADGIHIHPLNIRLAKKLKGDSKLCLVTDSMAAAGAKDGVFIFGGKTVYIREGTCLDSNGTLAGSSLTMIEGARNLVE 325

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1755663628 319 WG-VPFLTAIQAATLNPARAIHEDERIGSIKVGKYADMVALDSDLNIRMVVARGK 372
Cdd:TIGR00221 326 FTnISLTDAARMSSLNPARALGIDDRLGSVTVGKDANLVVFTPDFEVILTIVNGN 380
nagA PRK11170
N-acetylglucosamine-6-phosphate deacetylase; Provisional
 3-377 1.05e-78

N-acetylglucosamine-6-phosphate deacetylase; Provisional


Pssm-ID: 183010  Cd Length: 382  Bit Score: 246.81  E-value: 1.05e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755663628   3 LKNAKIVDDSFRFADADVAVEEDKISEIAPGL---AGGEEIDLSGCVLVPGFVDIHIHACVGA---DTCDA-DADGLAKM 75
Cdd:PRK11170    4 LTNGRIYTGHEVLDDHAVVIADGLIEAVCPVAelpPGIEQRDLNGAILSPGFIDLQLNGCGGVqfnDTAEAiSVETLEIM 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755663628  76 CAHLVTKGVTSFCPTTMTVSHKGILRALETVKSCMDHPPKGAAiaGVNMEGPYISIHKKGAQKGEFVKNSDfKEFQEFYD 155
Cdd:PRK11170   84 QKANEKSGCTSFLPTLITSSDELMKQAVRVMREYLAKHPNQAL--GLHLEGPYLNLVKKGTHNPEFIRKPD-AEMVDFLC 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755663628 156 TCGGIIKLVDIAPECPGAEeFIPQASRL-CTVSIAHTEADYACAKHAFELGITHATHLYNAMPGMKHREPGVIGAVLDDP 234
Cdd:PRK11170  161 ENADVITKVTLAPEMVDAE-VIRKLVEAgIVVSAGHSNATYEEAKAGFRAGITFATHLYNAMPYITGREPGLVGAILDEP 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755663628 235 RVRAELICDGFHIHPAVLRITFEALGkDRVVIVSDSMRAAGAPDGVSELGGQTVYVKDGQARLKDGTIAGSTTNLHQEIK 314
Cdd:PRK11170  240 DVYCGIIADGLHVDYANIRNAKRLKG-DKLCLVTDATAPAGANIEQFIFAGKTIYYRDGLCVDENGTLSGSALTMIEAVR 318

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1755663628 315 NLVGW-GVPFLTAIQAATLNPARAIHEDERIGSIKVGKYADMVALDSDLNIRMVVARGKIAVNN 377
Cdd:PRK11170  319 NLVEHvGIALDEALRMATLYPARAIGVDKRLGSIEAGKVANLTAFTRDFKITKTIVNGNEVVTQ 382
Amidohydro_1 pfam01979
Amidohydrolase family; This family of enzymes are a a large metal dependent hydrolase ...
 46-373 5.82e-24

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: 101.04  E-value: 5.82e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755663628  46 VLVPGFVDIHIHAC----VGADTCDADA-DGLAKMCAHLVTKGVTSFCPTTmTVSHKGILRALETVKscmdhppkgAAIA 120
Cdd:pfam01979   1 IVLPGLIDAHVHLEmgllRGIPVPPEFAyEALRLGITTMLKSGTTTVLDMG-ATTSTGIEALLEAAE---------ELPL 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755663628 121 GVNMEGPYISIHKKGAQKGEFVKNSDFKEFQEFYDTCGGIIKLVDIAPECPGA--EEFIPQASRLC-------TVSIAHT 191
Cdd:pfam01979  71 GLRFLGPGCSLDTDGELEGRKALREKLKAGAEFIKGMADGVVFVGLAPHGAPTfsDDELKAALEEAkkyglpvAIHALET 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755663628 192 EADYACAKHAFELGITHATHLYNAMPGMKHREPGVIGAvlddprvraelicDGFHIHPAVLRITFEALGKDRVV------ 265
Cdd:pfam01979 151 KGEVEDAIAAFGGGIEHGTHLEVAESGGLLDIIKLILA-------------HGVHLSPTEANLLAEHLKGAGVAhcpfsn 217

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755663628 266 --IVSDSMRAAGA-PDGVSelggQTVYVkdgqarlkDGTIAGSTTNLHQEIKNLVGW------GVPFLTAIQAATLNPAR 336
Cdd:pfam01979 218 skLRSGRIALRKAlEDGVK----VGLGT--------DGAGSGNSLNMLEELRLALELqfdpegGLSPLEALRMATINPAK 285

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*...
gi 1755663628 337 AIHEDERIGSIKVGKYADMVALDSDL-----------NIRMVVARGKI 373
Cdd:pfam01979 286 ALGLDDKVGSIEVGKDADLVVVDLDPlaaffglkpdgNVKKVIVKGKI 333
 
Name Accession Description Interval E-value
NagA COG1820
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism];
2-372 6.46e-173

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


Pssm-ID: 441425 [Multi-domain]  Cd Length: 373  Bit Score: 486.53  E-value: 6.46e-173
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755663628   2 ILKNAKIVDDSFRFADADVAVEEDKISEIAPGLAGGEE-IDLSGCVLVPGFVDIHIHACVGADTCDADADGLAKMCAHLV 80
Cdd:COG1820     1 AITNARIFTGDGVLEDGALLIEDGRIAAIGPGAEPDAEvIDLGGGYLAPGFIDLHVHGGGGVDFMDGTPEALRTIARAHA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755663628  81 TKGVTSFCPTTMTVSHKGILRALETVKSCMDHPPkGAAIAGVNMEGPYISIHKKGAQKGEFVKNSDFKEFQEFYDTCGGI 160
Cdd:COG1820    81 RHGTTSFLPTTITAPPEDLLRALAAIAEAIEQGG-GAGILGIHLEGPFLSPEKKGAHPPEYIRPPDPEELDRLLEAAGGL 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755663628 161 IKLVDIAPECPGAEEFIPQASRL-CTVSIAHTEADYACAKHAFELGITHATHLYNAMPGMKHREPGVIGAVLDDPRVRAE 239
Cdd:COG1820   160 IKLVTLAPELPGALEFIRYLVEAgVVVSLGHTDATYEQARAAFEAGATHVTHLFNAMSPLHHREPGVVGAALDDDDVYAE 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755663628 240 LICDGFHIHPAVLRITFEALGKDRVVIVSDSMRAAGAPDGVSELGGQTVYVKDGQARLKDGTIAGSTTNLHQEIKNLVGW 319
Cdd:COG1820   240 LIADGIHVHPAAVRLALRAKGPDRLILVTDAMAAAGLPDGEYELGGLEVTVKDGVARLADGTLAGSTLTMDDAVRNLVEW 319

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1755663628 320 -GVPFLTAIQAATLNPARAIHEDERIGSIKVGKYADMVALDSDLNIRMVVARGK 372
Cdd:COG1820   320 tGLPLEEAVRMASLNPARALGLDDRKGSIAPGKDADLVVLDDDLNVRATWVGGE 373
NagA cd00854
N-acetylglucosamine-6-phosphate deacetylase, NagA, catalyzes the hydrolysis of the N-acetyl ...
 1-371 1.91e-151

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: 432.00  E-value: 1.91e-151
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755663628   1 MILKNAKIVDDSFRFaDADVAVEEDKISEIAPGL---AGGEEIDLSGCVLVPGFVDIHIHACVGADTCDADADGLAKMCA 77
Cdd:cd00854     1 LIIKNARILTPGGLE-DGAVLVEDGKIVAIGPEDeleEADEIIDLKGQYLVPGFIDIHIHGGGGADFMDGTAEALKTIAE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755663628  78 HLVTKGVTSFCPTTMTVSHKGILRALETVKSCMDHPpKGAAIAGVNMEGPYISIHKKGAQKGEFVKNSDFKEFQEFYDTC 157
Cdd:cd00854    80 ALAKHGTTSFLPTTVTAPPEEIAKALAAIAEAIAEG-QGAEILGIHLEGPFISPEKKGAHPPEYLRAPDPEELKKWLEAA 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755663628 158 GGIIKLVDIAPECPGAEEFIPQ-ASRLCTVSIAHTEADYACAKHAFELGITHATHLYNAMPGMKHREPGVIGAVLDDPRV 236
Cdd:cd00854   159 GGLIKLVTLAPELDGALELIRYlVERGIIVSIGHSDATYEQAVAAFEAGATHVTHLFNAMSPLHHREPGVVGAALSDDDV 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755663628 237 RAELICDGFHIHPAVLRITFEALGKDRVVIVSDSMRAAGAPDGVSELGGQTVYVKDGQARLKDGTIAGSTTNLHQEIKNL 316
Cdd:cd00854   239 YAELIADGIHVHPAAVRLAYRAKGADKIVLVTDAMAAAGLPDGEYELGGQTVTVKDGVARLADGTLAGSTLTMDQAVRNM 318

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1755663628 317 VGW-GVPFLTAIQAATLNPARAIHEDERIGSIKVGKYADMVALDSDLNIRMVVARG 371
Cdd:cd00854   319 VKWgGCPLEEAVRMASLNPAKLLGLDDRKGSLKPGKDADLVVLDDDLNVKATWING 374
nagA TIGR00221
N-acetylglucosamine-6-phosphate deacetylase; [Central intermediary metabolism, Amino sugars]
 3-372 3.85e-104

N-acetylglucosamine-6-phosphate deacetylase; [Central intermediary metabolism, Amino sugars]


Pssm-ID: 272968  Cd Length: 380  Bit Score: 312.15  E-value: 3.85e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755663628   3 LKNAKIVDDSFRFADADVAVEEDKISEI---APGLAGGEEIDLSGCVLVPGFVDIHIHACVGADTCDADADGLAKMCAHL 79
Cdd:TIGR00221   7 LKDIAIVTGNEVIDNGAVGINDGKISTVsteAELEPEIKEIDLPGNVLTPGFIDIHIHGCGGVDTNDASFETLEIMSERL 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755663628  80 VTKGVTSFCPTTMTVSHKGILRALETVKSCMDHPpKGAAIAGVNMEGPYISIHKKGAQKGEFVKNSDFKEFQEFYDTCGG 159
Cdd:TIGR00221  87 PKSGCTSFLPTLITQPDENIKQAVKNMREYLAKE-KNAQALGLHLEGPFLSPEKKGAHPPEYIREPDVELFKKFLCEAGG 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755663628 160 IIKLVDIAPECPGAEEFIPQ-ASRLCTVSIAHTEADYACAKHAFELGITHATHLYNAMPGMKHREPGVIGAVLDDPRVRA 238
Cdd:TIGR00221 166 VITKVTLAPEEDQHFELIRHlKDAGIIVSAGHTNATYELAKAAFKAGATHATHLYNAMSPIHHREPGVIGAVLDHDDVYT 245

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755663628 239 ELICDGFHIHPAVLRITFEALGKDRVVIVSDSMRAAGAPDGVSELGGQTVYVKDGQARLKDGTIAGSTTNLHQEIKNLVG 318
Cdd:TIGR00221 246 EIIADGIHIHPLNIRLAKKLKGDSKLCLVTDSMAAAGAKDGVFIFGGKTVYIREGTCLDSNGTLAGSSLTMIEGARNLVE 325

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1755663628 319 WG-VPFLTAIQAATLNPARAIHEDERIGSIKVGKYADMVALDSDLNIRMVVARGK 372
Cdd:TIGR00221 326 FTnISLTDAARMSSLNPARALGIDDRLGSVTVGKDANLVVFTPDFEVILTIVNGN 380
nagA PRK11170
N-acetylglucosamine-6-phosphate deacetylase; Provisional
 3-377 1.05e-78

N-acetylglucosamine-6-phosphate deacetylase; Provisional


Pssm-ID: 183010  Cd Length: 382  Bit Score: 246.81  E-value: 1.05e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755663628   3 LKNAKIVDDSFRFADADVAVEEDKISEIAPGL---AGGEEIDLSGCVLVPGFVDIHIHACVGA---DTCDA-DADGLAKM 75
Cdd:PRK11170    4 LTNGRIYTGHEVLDDHAVVIADGLIEAVCPVAelpPGIEQRDLNGAILSPGFIDLQLNGCGGVqfnDTAEAiSVETLEIM 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755663628  76 CAHLVTKGVTSFCPTTMTVSHKGILRALETVKSCMDHPPKGAAiaGVNMEGPYISIHKKGAQKGEFVKNSDfKEFQEFYD 155
Cdd:PRK11170   84 QKANEKSGCTSFLPTLITSSDELMKQAVRVMREYLAKHPNQAL--GLHLEGPYLNLVKKGTHNPEFIRKPD-AEMVDFLC 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755663628 156 TCGGIIKLVDIAPECPGAEeFIPQASRL-CTVSIAHTEADYACAKHAFELGITHATHLYNAMPGMKHREPGVIGAVLDDP 234
Cdd:PRK11170  161 ENADVITKVTLAPEMVDAE-VIRKLVEAgIVVSAGHSNATYEEAKAGFRAGITFATHLYNAMPYITGREPGLVGAILDEP 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755663628 235 RVRAELICDGFHIHPAVLRITFEALGkDRVVIVSDSMRAAGAPDGVSELGGQTVYVKDGQARLKDGTIAGSTTNLHQEIK 314
Cdd:PRK11170  240 DVYCGIIADGLHVDYANIRNAKRLKG-DKLCLVTDATAPAGANIEQFIFAGKTIYYRDGLCVDENGTLSGSALTMIEAVR 318

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1755663628 315 NLVGW-GVPFLTAIQAATLNPARAIHEDERIGSIKVGKYADMVALDSDLNIRMVVARGKIAVNN 377
Cdd:PRK11170  319 NLVEHvGIALDEALRMATLYPARAIGVDKRLGSIEAGKVANLTAFTRDFKITKTIVNGNEVVTQ 382
Amidohydro_1 pfam01979
Amidohydrolase family; This family of enzymes are a a large metal dependent hydrolase ...
 46-373 5.82e-24

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: 101.04  E-value: 5.82e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755663628  46 VLVPGFVDIHIHAC----VGADTCDADA-DGLAKMCAHLVTKGVTSFCPTTmTVSHKGILRALETVKscmdhppkgAAIA 120
Cdd:pfam01979   1 IVLPGLIDAHVHLEmgllRGIPVPPEFAyEALRLGITTMLKSGTTTVLDMG-ATTSTGIEALLEAAE---------ELPL 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755663628 121 GVNMEGPYISIHKKGAQKGEFVKNSDFKEFQEFYDTCGGIIKLVDIAPECPGA--EEFIPQASRLC-------TVSIAHT 191
Cdd:pfam01979  71 GLRFLGPGCSLDTDGELEGRKALREKLKAGAEFIKGMADGVVFVGLAPHGAPTfsDDELKAALEEAkkyglpvAIHALET 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755663628 192 EADYACAKHAFELGITHATHLYNAMPGMKHREPGVIGAvlddprvraelicDGFHIHPAVLRITFEALGKDRVV------ 265
Cdd:pfam01979 151 KGEVEDAIAAFGGGIEHGTHLEVAESGGLLDIIKLILA-------------HGVHLSPTEANLLAEHLKGAGVAhcpfsn 217

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755663628 266 --IVSDSMRAAGA-PDGVSelggQTVYVkdgqarlkDGTIAGSTTNLHQEIKNLVGW------GVPFLTAIQAATLNPAR 336
Cdd:pfam01979 218 skLRSGRIALRKAlEDGVK----VGLGT--------DGAGSGNSLNMLEELRLALELqfdpegGLSPLEALRMATINPAK 285

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*...
gi 1755663628 337 AIHEDERIGSIKVGKYADMVALDSDL-----------NIRMVVARGKI 373
Cdd:pfam01979 286 ALGLDDKVGSIEVGKDADLVVVDLDPlaaffglkpdgNVKKVIVKGKI 333
HutI COG1228
Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport ...
 1-377 8.41e-24

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


Pssm-ID: 440841 [Multi-domain]  Cd Length: 386  Bit Score: 101.19  E-value: 8.41e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755663628   1 MILKNAKIVD--DSFRFADADVAVEEDKISEIAPGL-----AGGEEIDLSGCVLVPGFVDIHIHACVGADTCDADADG-- 71
Cdd:COG1228    10 LLITNATLVDgtGGGVIENGTVLVEDGKIAAVGPAAdlavpAGAEVIDATGKTVLPGLIDAHTHLGLGGGRAVEFEAGgg 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755663628  72 ----------LAKMCAHLVTKGVTSFCptTMTVSHKGILRALETVKSCMDHPPK----GAAIA---GVNMEGP------Y 128
Cdd:COG1228    90 itptvdlvnpADKRLRRALAAGVTTVR--DLPGGPLGLRDAIIAGESKLLPGPRvlaaGPALSltgGAHARGPeearaaL 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755663628 129 ISIHKKGAQkgeFVKnsdfkefqeFYDTcGGIIKLvdiapecpGAEEFIP---QASRLCTVSIAHTEADYAcAKHAFELG 205
Cdd:COG1228   168 RELLAEGAD---YIK---------VFAE-GGAPDF--------SLEELRAileAAHALGLPVAAHAHQADD-IRLAVEAG 225

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755663628 206 ---ITHATHLYNA-MPGMKHREPGVIGAVLDDPRVRAELIC-DGFHIHPAVLRITFEALGKdrvvivsdsMRAAGAPdgV 280
Cdd:COG1228   226 vdsIEHGTYLDDEvADLLAEAGTVVLVPTLSLFLALLEGAAaPVAAKARKVREAALANARR---------LHDAGVP--V 294

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755663628 281 SeLGGqtvyvkDGQARLKDGTiagsttNLHQEIKNLVGWGVPFLTAIQAATLNPARAIHEDERIGSIKVGKYADMVALDS 360
Cdd:COG1228   295 A-LGT------DAGVGVPPGR------SLHRELALAVEAGLTPEEALRAATINAAKALGLDDDVGSLEPGKLADLVLLDG 361

                         410       420
                  ....*....|....*....|....*
gi 1755663628 361 D--------LNIRMVVARGKIAVNN 377
Cdd:COG1228   362 DplediaylEDVRAVMKDGRVVDRS 386
AllB COG0044
Dihydroorotase or related cyclic amidohydrolase [Nucleotide transport and metabolism]; ...
 2-57 7.21e-13

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: 69.35  E-value: 7.21e-13
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1755663628   2 ILKNAKIVDDSfRFADADVAVEEDKISEIAPGLA---GGEEIDLSGCVLVPGFVDIHIH 57
Cdd:COG0044     1 LIKNGRVVDPG-GLERADVLIEDGRIAAIGPDLAapeAAEVIDATGLLVLPGLIDLHVH 58
SsnA COG0402
Cytosine/adenosine deaminase or related metal-dependent hydrolase [Nucleotide transport and ...
 2-377 6.16e-12

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: 66.39  E-value: 6.16e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755663628   2 ILKNAKIV--DDSFRF-ADADVAVEEDKISEIAPGLA------GGEEIDLSGCVLVPGFVDIHIHACVGADTCDADADGL 72
Cdd:COG0402     3 LIRGAWVLtmDPAGGVlEDGAVLVEDGRIAAVGPGAElparypAAEVIDAGGKLVLPGLVNTHTHLPQTLLRGLADDLPL 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755663628  73 ------------AKM------------CAHLVTKGVTSFCP--TTMTVSHKGILRALETV-------KSCMDHppkGAAI 119
Cdd:COG0402    83 ldwleeyiwpleARLdpedvyagallaLAEMLRSGTTTVADfyYVHPESADALAEAAAEAgiravlgRGLMDR---GFPD 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755663628 120 AGVNMEGPYIsihkkgaqkgefvknSDFKEFQE-FYDTCGGIIKLVdIAPECPGA--EEFIPQASRL-----CTVSI--A 189
Cdd:COG0402   160 GLREDADEGL---------------ADSERLIErWHGAADGRIRVA-LAPHAPYTvsPELLRAAAALarelgLPLHThlA 223

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755663628 190 HTEADYACAKHAF---------ELGIT-------HATHlynampgmkhrepgvigavLDDprvrAELicdgfhihpavlr 253
Cdd:COG0402   224 ETRDEVEWVLELYgkrpveyldELGLLgprtllaHCVH-------------------LTD----EEI------------- 267

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755663628 254 itfEALGKDRVVIVS---------------DSMRAAGAPdgVSeLGgqTvyvkdgqarlkDGTIAGSTTNLHQEIKNL-- 316
Cdd:COG0402   268 ---ALLAETGASVAHcptsnlklgsgiapvPRLLAAGVR--VG-LG--T-----------DGAASNNSLDMFEEMRLAal 328

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755663628 317 ---VGWG----VPFLTAIQAATLNPARAIHEDERIGSIKVGKYADMVALD--------------------SDLNIRMVVA 369
Cdd:COG0402   329 lqrLRGGdptaLSAREALEMATLGGARALGLDDEIGSLEPGKRADLVVLDldaphlaplhdplsalvyaaDGRDVRTVWV 408


                  ....*...
gi 1755663628 370 RGKIAVNN 377
Cdd:COG0402   409 AGRVVVRD 416
AdeC COG1001
Adenine deaminase [Nucleotide transport and metabolism];
313-377 1.65e-11

Adenine deaminase [Nucleotide transport and metabolism];


Pssm-ID: 440625 [Multi-domain]  Cd Length: 559  Bit Score: 65.51  E-value: 1.65e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1755663628 313 IKNLVGWGVPFLTAIQAATLNPARAIHEDeRIGSIKVGKYADMVALDS--DLNIRMVVARGKIAVNN 377
Cdd:COG1001   276 VRRAIELGLDPVTAIQMATLNAAEHFGLK-DLGAIAPGRRADIVLLDDleDFKVEKVYADGKLVAED 341
pyrC PRK09357
dihydroorotase; Validated
 1-57 2.27e-11

dihydroorotase; Validated


Pssm-ID: 236479 [Multi-domain]  Cd Length: 423  Bit Score: 64.83  E-value: 2.27e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1755663628   1 MILKNAKIVDDSFRFADADVAVEEDKISEIAPGLA--GGEEIDLSGCVLVPGFVDIHIH 57
Cdd:PRK09357    3 ILIKNGRVIDPKGLDEVADVLIDDGKIAAIGENIEaeGAEVIDATGLVVAPGLVDLHVH 61
D-HYD cd01314
D-hydantoinases (D-HYD) also called dihydropyrimidases (DHPase) and related proteins; DHPases ...
 1-64 4.95e-11

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: 63.78  E-value: 4.95e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1755663628   1 MILKNAKIV--DDSFRfadADVAVEEDKISEIAPGLAGG---EEIDLSGCVLVPGFVDIHIH------ACVGADT 64
Cdd:cd01314     1 LIIKNGTIVtaDGSFK---ADILIEDGKIVAIGPNLEAPggvEVIDATGKYVLPGGIDPHTHlelpfmGTVTADD 72
COG3653 COG3653
N-acyl-D-aspartate/D-glutamate deacylase [Secondary metabolites biosynthesis, transport and ...
 1-58 2.07e-10

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


Pssm-ID: 442870 [Multi-domain]  Cd Length: 528  Bit Score: 62.11  E-value: 2.07e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1755663628   1 MILKNAKIVD----DSFRfadADVAVEEDKISEIA--PGLAGGEEIDLSGCVLVPGFVDIHIHA 58
Cdd:COG3653     4 LLIRGGTVVDgtgaPPFR---ADVAIKGGRIVAVGdlAAAEAARVIDATGLVVAPGFIDIHTHY 64
D-aminoacylase cd01297
D-aminoacylases (N-acyl-D-Amino acid amidohydrolases) catalyze the hydrolysis of ...
 2-57 2.77e-10

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: 61.54  E-value: 2.77e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755663628   2 ILKNAKIVDDS--FRFAdADVAVEEDKISEIAPGLAGG--EEIDLSGCVLVPGFVDIHIH 57
Cdd:cd01297     3 VIRNGTVVDGTgaPPFT-ADVGIRDGRIAAIGPILSTSarEVIDAAGLVVAPGFIDVHTH 61
YtcJ COG1574
Predicted amidohydrolase YtcJ [General function prediction only];
325-362 1.10e-09

Predicted amidohydrolase YtcJ [General function prediction only];


Pssm-ID: 441182 [Multi-domain]  Cd Length: 535  Bit Score: 59.81  E-value: 1.10e-09
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1755663628 325 TAIQAATLNPARAIHEDERIGSIKVGKYADMVALDSDL 362
Cdd:COG1574   471 EALRAYTIGAAYAAFEEDEKGSLEPGKLADFVVLDRDP 508
Isoaspartyl-dipeptidase cd01308
Isoaspartyl dipeptidase hydrolyzes the beta-L-isoaspartyl linkages in dipeptides, as part of ...
 2-377 1.57e-09

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: 58.94  E-value: 1.57e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755663628   2 ILKNAKIVDDSFRfADADVAVEEDKISEIA-----PGLAGGEEIDLSGCVLVPGFVDIHIH------------------- 57
Cdd:cd01308     3 LIKNAEVYAPEYL-GKKDILIAGGKILAIEdqlnlPGYENVTVVDLHGKILVPGFIDQHVHiiggggeggpstrtpevtl 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755663628  58 ------------ACVGADTCDADADGLAKMCAHLVTKGVTSFCPT--------TMTVSHKGILRALETV-----KSCMDH 112
Cdd:cd01308    82 sdlttagvttvvGCLGTDGISRSMEDLLAKARALEEEGITCFVYTgsyevptrTITGSIRKDLLLIDKVigvgeIAISDH 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755663628 113 ----PPK------------GAAIAGvnmEGPYISIHKKGAQKGefvknsdfkeFQEFYDtcggIIKLVDIApecpgAEEF 176
Cdd:cd01308   162 rssqPTVeelariaaearvGGLLGG---KAGIVHIHLGDGKRA----------LSPIFE----LIEETEIP-----ITQF 219

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755663628 177 IPqasrlctVSIAHTEadyacakHAFELGITHAthlynampgmkhREPGVIGAVLD-DPRVRAELicdgfHIHP--AVLR 253
Cdd:cd01308   220 LP-------THINRTA-------PLFEQGVEFA------------KMGGTIDLTSSiDPQFRKEG-----EVRPseALKR 268

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755663628 254 ITFEALGKDRVVIVSDSMRAAGAPDGVSELGGQTVyvkdgqarlkdgtiaGSTTNLHQEIKNLV-GWGVPFLTAIQAATL 332
Cdd:cd01308   269 LLEQGVPLERITFSSDGNGSLPKFDENGNLVGLGV---------------GSVDTLLREVREAVkCGDIPLEVALRVITS 333

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*
gi 1755663628 333 NPARAIHEDERiGSIKVGKYADMVALDSDLNIRMVVARGKIAVNN 377
Cdd:cd01308   334 NVARILKLRKK-GEIQPGFDADLVILDKDLDINSVIAKGQIMVRN 377
ATZ_TRZ_like cd01298
TRZ/ATZ family contains enzymes from the atrazine degradation pathway and related hydrolases. ...
 1-58 2.98e-09

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: 58.37  E-value: 2.98e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1755663628   1 MILKNAKIV--DDSFRFADADVAVEEDKISEIAPGL-----AGGEEIDLSGCVLVPGFVDIHIHA 58
Cdd:cd01298     1 ILIRNGTIVttDPRRVLEDGDVLVEDGRIVAVGPALplpayPADEVIDAKGKVVMPGLVNTHTHL 65
Amidohydro_3 pfam07969
Amidohydrolase family;
321-375 7.29e-09

Amidohydrolase family;


Pssm-ID: 400360 [Multi-domain]  Cd Length: 464  Bit Score: 57.16  E-value: 7.29e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1755663628 321 VPFLTAIQAATLNPARAIHEDERIGSIKVGKYADMVALDSDL-----------NIRMVVARGKIAV 375
Cdd:pfam07969 399 LSLEEALALYTSGPAKALGLEDRKGTLGVGKDADLVVLDDDPltvdppaiadiRVRLTVVDGRVVY 464
PRK09237 PRK09237
amidohydrolase/deacetylase family metallohydrolase;
1-85 1.16e-08

amidohydrolase/deacetylase family metallohydrolase;


Pssm-ID: 236423 [Multi-domain]  Cd Length: 380  Bit Score: 56.40  E-value: 1.16e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755663628   1 MILKNAKIVDDSFRF-ADADVAVEEDKISEIAPGLAGG---EEIDLSGCVLVPGFVDIHIHACVGADTCDADADGLAkmc 76
Cdd:PRK09237    1 LLLRGGRVIDPANGIdGVIDIAIEDGKIAAVAGDIDGSqakKVIDLSGLYVSPGWIDLHVHVYPGSTPYGDEPDEVG--- 77


                  ....*....
gi 1755663628  77 ahlVTKGVT 85
Cdd:PRK09237   78 ---VRSGVT 83
YtcJ COG1574
Predicted amidohydrolase YtcJ [General function prediction only];
1-57 1.20e-08

Predicted amidohydrolase YtcJ [General function prediction only];


Pssm-ID: 441182 [Multi-domain]  Cd Length: 535  Bit Score: 56.73  E-value: 1.20e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1755663628   1 MILKNAKI--VDDSFRFADAdVAVEEDKI-----SEIAPGLAGG--EEIDLSGCVLVPGFVDIHIH 57
Cdd:COG1574    10 LLLTNGRIytMDPAQPVAEA-VAVRDGRIvavgsDAEVRALAGPatEVIDLGGKTVLPGFIDAHVH 74
PRK09045 PRK09045
TRZ/ATZ family hydrolase;
321-365 1.35e-08

TRZ/ATZ family hydrolase;


Pssm-ID: 236366 [Multi-domain]  Cd Length: 443  Bit Score: 56.07  E-value: 1.35e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1755663628 321 VPFLTAIQAATLNPARAIHEDERIGSIKVGKYADMVALD-SDLNIR 365
Cdd:PRK09045  340 LPAHTALRMATLNGARALGLDDEIGSLEPGKQADLVAVDlSGLETQ 385
Met_dep_hydrolase_A cd01299
Metallo-dependent hydrolases, subgroup A is part of the superfamily of metallo-dependent ...
 300-361 1.93e-08

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: 55.38  E-value: 1.93e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1755663628 300 GTIAGSTTNLH----QEIKNLVGWGVPFLTAIQAATLNPARAIHEDERIGSIKVGKYADMVALDSD 361
Cdd:cd01299   269 GTDAGFPVPPHgwnaRELELLVKAGGTPAEALRAATANAAELLGLSDELGVIEAGKLADLLVVDGD 334
PRK08323 PRK08323
phenylhydantoinase; Validated
 1-57 2.28e-08

phenylhydantoinase; Validated


Pssm-ID: 236240 [Multi-domain]  Cd Length: 459  Bit Score: 55.56  E-value: 2.28e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1755663628   1 MILKNAKIV--DDSFRfadADVAVEEDKISEIAPGlAGGEEIDLSGCVLVPGFVDIHIH 57
Cdd:PRK08323    3 TLIKNGTVVtaDDTYK---ADVLIEDGKIAAIGAN-LGDEVIDATGKYVMPGGIDPHTH 57
Bact_CD cd01293
Bacterial cytosine deaminase and related metal-dependent hydrolases. Cytosine deaminases (CDs) ...
 2-57 1.07e-07

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: 53.40  E-value: 1.07e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1755663628   2 ILKNAKIVDDsfRFADADVAVEEDKISEIAPGLA---GGEEIDLSGCVLVPGFVDIHIH 57
Cdd:cd01293     1 LLRNARLADG--GTALVDIAIEDGRIAAIGPALAvppDAEEVDAKGRLVLPAFVDPHIH 57
YtcJ_like cd01300
YtcJ_like metal dependent amidohydrolases. YtcJ is a Bacillus subtilis ORF of unknown function. ...
 318-356 1.08e-07

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: 53.47  E-value: 1.08e-07
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1755663628 318 GWGVPFLTAIQAATLNPARAIHEDERIGSIKVGKYADMV 356
Cdd:cd01300   440 EERLSLEEALRAYTIGAAYAIGEEDEKGSLEPGKLADFV 478
PRK06189 PRK06189
allantoinase; Provisional
 1-111 1.51e-07

allantoinase; Provisional


Pssm-ID: 235732 [Multi-domain]  Cd Length: 451  Bit Score: 53.17  E-value: 1.51e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755663628   1 MILKNAKIV--DDSFRfadADVAVEEDKISEIAPGLAG--GEEIDLSGCVLVPGFVDIHIHAcvgADTCDADADGLAKMC 76
Cdd:PRK06189    5 LIIRGGKVVtpEGVYR---ADIGIKNGKIAEIAPEISSpaREIIDADGLYVFPGMIDVHVHF---NEPGRTHWEGFATGS 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1755663628  77 AHLVTKGVTSFC-------PTTMTVSHKGILRALETVKSCMD 111
Cdd:PRK06189   79 AALAAGGCTTYFdmplnsiPPTVTREALDAKAELARQKSAVD 120
PRK15446 PRK15446
phosphonate metabolism protein PhnM; Provisional
 1-55 2.17e-07

phosphonate metabolism protein PhnM; Provisional


Pssm-ID: 237967 [Multi-domain]  Cd Length: 383  Bit Score: 52.49  E-value: 2.17e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1755663628   1 MILKNAKIVDDSfRFADADVAVEEDKISEIAPGLAG-GEEIDLSGCVLVPGFVDIH 55
Cdd:PRK15446    4 MILSNARLVLPD-EVVDGSLLIEDGRIAAIDPGASAlPGAIDAEGDYLLPGLVDLH 58
PRK09236 PRK09236
dihydroorotase; Reviewed
 2-57 3.49e-07

dihydroorotase; Reviewed


Pssm-ID: 181716  Cd Length: 444  Bit Score: 51.79  E-value: 3.49e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1755663628   2 ILKNAKIVDDSFRFaDADVAVEEDKISEIAPGLA---GGEEIDLSGCVLVPGFVDIHIH 57
Cdd:PRK09236    5 LIKNARIVNEGKIF-EGDVLIENGRIAKIASSISaksADTVIDAAGRYLLPGMIDDQVH 62
Met_dep_hydrolase_C cd01309
Metallo-dependent hydrolases, subgroup C is part of the superfamily of metallo-dependent ...
 189-361 7.66e-07

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: 50.39  E-value: 7.66e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755663628 189 AHTEADYACA-----KHAFELGITHATHLYNAMPGM-KHREPGVIGAVLDDPRvRAELICDGFHIhPAVLRitfeALGKD 262
Cdd:cd01309   199 AHRADDILTAiriakEFGIKITIEHGAEGYKLADELaKHGIPVIYGPTLTLPK-KVEEVNDAIDT-NAYLL----KKGGV 272

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755663628 263 RVVIVSDSmraagapdgvSELGGQTVYVKDGQArlkdgtiagsttnlhqeiknlVGWGVPFLTAIQAATLNPARAIHEDE 342
Cdd:cd01309   273 AFAISSDH----------PVLNIRNLNLEAAKA---------------------VKYGLSYEEALKAITINPAKILGIED 321

                         170
                  ....*....|....*....
gi 1755663628 343 RIGSIKVGKYADMVALDSD 361
Cdd:cd01309   322 RVGSLEPGKDADLVVWNGD 340
PRK07572 PRK07572
cytosine deaminase; Validated
 1-57 2.05e-06

cytosine deaminase; Validated


Pssm-ID: 181039  Cd Length: 426  Bit Score: 49.25  E-value: 2.05e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1755663628   1 MILKNAKIVDDSfrfADADVAVEEDKISEIAPGLAG--GEEIDLSGCVLVPGFVDIHIH 57
Cdd:PRK07572    4 LIVRNANLPDGR---TGIDIGIAGGRIAAVEPGLQAeaAEEIDAAGRLVSPPFVDPHFH 59
AdeC cd01295
Adenine deaminase (AdeC) directly deaminates adenine to form hypoxanthine. This reaction is ...
 313-375 3.04e-06

Adenine deaminase (AdeC) directly deaminates adenine to form hypoxanthine. This reaction is part of one of the adenine salvage pathways, as well as the degradation pathway. It is important for adenine utilization as a purine, as well as a nitrogen source in bacteria and archea.


Pssm-ID: 238620 [Multi-domain]  Cd Length: 422  Bit Score: 48.76  E-value: 3.04e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1755663628 313 IKNLVGWGVPFLTAIQAATLNPARA--IHEderIGSIKVGKYADMVALDS--DLNIRMVVARGkIAV 375
Cdd:cd01295   227 VRRAIEAGIPPEDAIQMATINPAECygLHD---LGAIAPGRIADIVILDDleNFNITTVLAKG-IAV 289
PRK07228 PRK07228
5'-deoxyadenosine deaminase;
1-59 3.22e-06

5'-deoxyadenosine deaminase;


Pssm-ID: 180895 [Multi-domain]  Cd Length: 445  Bit Score: 48.84  E-value: 3.22e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1755663628   1 MILKNAKIV--DDSFRFADADVAVEEDKISEIAPGLAGGE---EIDLSGCVLVPGFVDIHIHAC 59
Cdd:PRK07228    3 ILIKNAGIVtmNAKREIVDGDVLIEDDRIAAVGDRLDLEDyddHIDATGKVVIPGLIQGHIHLC 66
PRK08393 PRK08393
N-ethylammeline chlorohydrolase; Provisional
 1-61 1.52e-05

N-ethylammeline chlorohydrolase; Provisional


Pssm-ID: 181411 [Multi-domain]  Cd Length: 424  Bit Score: 46.72  E-value: 1.52e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1755663628   1 MILKNAKIV-DDSFRFADADVAVEEDKISEIAPGL--AGGEEIDLSGCVLVPGFVDIHIHACVG 61
Cdd:PRK08393    3 ILIKNGYVIyGENLKVIRADVLIEGNKIVEVKRNInkPADTVIDASGSVVSPGFINAHTHSPMV 66
PRK08204 PRK08204
hypothetical protein; Provisional
 17-57 1.75e-05

hypothetical protein; Provisional


Pssm-ID: 181288 [Multi-domain]  Cd Length: 449  Bit Score: 46.53  E-value: 1.75e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1755663628  17 DADVAVEEDKISEIAPGL--AGGEEIDLSGCVLVPGFVDIHIH 57
Cdd:PRK08204   23 RGDILIEGDRIAAVAPSIeaPDAEVVDARGMIVMPGLVDTHRH 65
hutI TIGR01224
imidazolonepropionase; This enzyme catalyzes the third step in histidine degradation. [Energy ...
 17-63 1.85e-05

imidazolonepropionase; This enzyme catalyzes the third step in histidine degradation. [Energy metabolism, Amino acids and amines]


Pssm-ID: 273512 [Multi-domain]  Cd Length: 377  Bit Score: 46.25  E-value: 1.85e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1755663628  17 DADVAVEEDKISEI-----APGLAGGEEIDLSGCVLVPGFVDIHIHACVGAD 63
Cdd:TIGR01224   3 DAVILIHGGKIVWIgqlaaLPGEEATEIIDCGGGLVTPGLVDPHTHLVFAGD 54
PRK05985 PRK05985
cytosine deaminase; Provisional
 14-57 2.74e-05

cytosine deaminase; Provisional


Pssm-ID: 180337 [Multi-domain]  Cd Length: 391  Bit Score: 45.69  E-value: 2.74e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1755663628  14 RFADA---DVAVEEDKISEIAPGL---AGGEEIDLSGCVLVPGFVDIHIH 57
Cdd:PRK05985   10 RPAGGaavDILIRDGRIAAIGPALaapPGAEVEDGGGALALPGLVDGHIH 59
Imidazolone-5PH cd01296
Imidazolonepropionase/imidazolone-5-propionate hydrolase (Imidazolone-5PH) catalyzes the third ...
 326-361 2.92e-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: 2.92e-05
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 1755663628 326 AIQAATLNPARAIHEDERIGSIKVGKYADMVALDSD 361
Cdd:cd01296   315 ALTAATINAAAALGLGETVGSLEVGKQADLVILDAP 350
ade TIGR01178
adenine deaminase; The family described by this model includes an experimentally characterized ...
 2-57 3.01e-05

adenine deaminase; The family described by this model includes an experimentally characterized adenine deaminase of Bacillus subtilis. It also include a member from Methanobacterium thermoautotrophicum, in which adenine deaminase activity has been detected. [Purines, pyrimidines, nucleosides, and nucleotides, Salvage of nucleosides and nucleotides]


Pssm-ID: 130246 [Multi-domain]  Cd Length: 552  Bit Score: 45.92  E-value: 3.01e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1755663628   2 ILKNAKIVD-DSFRFADADVAVEEDKISEIApGLAGGEEIDLSGCVLVPGFVDIHIH 57
Cdd:TIGR01178   3 VIKNAKIIDvYNGEIIPGDIAIANGHIAGVG-KYNGVKVIDALGEYAVPGFIDAHIH 58
PRK13404 PRK13404
dihydropyrimidinase; Provisional
 2-57 3.12e-05

dihydropyrimidinase; Provisional


Pssm-ID: 184033 [Multi-domain]  Cd Length: 477  Bit Score: 45.84  E-value: 3.12e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1755663628   2 ILKNAKIV--DDSFRfadADVAVEEDKISEIAPGLAGG-EEIDLSGCVLVPGFVDIHIH 57
Cdd:PRK13404    7 VIRGGTVVtaTDTFQ---ADIGIRGGRIAALGEGLGPGaREIDATGRLVLPGGVDSHCH 62
PRK08203 PRK08203
hydroxydechloroatrazine ethylaminohydrolase; Reviewed
 1-57 3.78e-05

hydroxydechloroatrazine ethylaminohydrolase; Reviewed


Pssm-ID: 236184 [Multi-domain]  Cd Length: 451  Bit Score: 45.61  E-value: 3.78e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1755663628   1 MILKNAKIV---DDSFR-FADADVAVEEDKISEIAPGLA----GGEEIDLSGCVLVPGFVDIHIH 57
Cdd:PRK08203    3 LWIKNPLAIvtmDAARReIADGGLVVEGGRIVEVGPGGAlpqpADEVFDARGHVVTPGLVNTHHH 67
L-HYD_ALN cd01315
L-Hydantoinases (L-HYDs) and Allantoinase (ALN); L-Hydantoinases are a member of the ...
 1-57 3.82e-05

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: 45.36  E-value: 3.82e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1755663628   1 MILKNAKIV-DDSFRfaDADVAVEEDKISEIAPGLAGGEE---IDLSGCVLVPGFVDIHIH 57
Cdd:cd01315     2 LVIKNGRVVtPDGVR--EADIAVKGGKIAAIGPDIANTEAeevIDAGGLVVMPGLIDTHVH 60
PRK09061 PRK09061
D-glutamate deacylase; Validated
 2-63 4.50e-05

D-glutamate deacylase; Validated


Pssm-ID: 236369 [Multi-domain]  Cd Length: 509  Bit Score: 45.46  E-value: 4.50e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1755663628   2 ILKNAKIVDDSFRF-ADADVAVEEDKISEIAPGLAGGE-EIDLSGCVLVPGFVDIHIHA-CVGAD 63
Cdd:PRK09061   22 VIRNGRVVDPETGLdAVRDVGIKGGKIAAVGTAAIEGDrTIDATGLVVAPGFIDLHAHGqSVAAY 86
PRK07575 PRK07575
dihydroorotase; Provisional
 1-95 6.23e-05

dihydroorotase; Provisional


Pssm-ID: 236055 [Multi-domain]  Cd Length: 438  Bit Score: 44.67  E-value: 6.23e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755663628   1 MILKNAKIVDDSFRFADADVAVEEDKISEIAPGL---AGGEEIDLSGCVLVPGFVDIHIHACVGADTCDADADGLAKMCA 77
Cdd:PRK07575    5 LLIRNARILLPSGELLLGDVLVEDGKIVAIAPEIsatAVDTVIDAEGLTLLPGVIDPQVHFREPGLEHKEDLFTASRACA 84

                          90       100
                  ....*....|....*....|....
gi 1755663628  78 HlvtKGVTSFC------PTTMTVS 95
Cdd:PRK07575   85 K---GGVTSFLempntkPLTTTQA 105
PRK06380 PRK06380
metal-dependent hydrolase; Provisional
 1-57 7.27e-05

metal-dependent hydrolase; Provisional


Pssm-ID: 180548 [Multi-domain]  Cd Length: 418  Bit Score: 44.49  E-value: 7.27e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755663628   1 MILKNAKIV--DDSFRFADADVAVEEDKISEIAPGLAGGEE-IDLSGCVLVPGFVDIHIH 57
Cdd:PRK06380    3 ILIKNAWIVtqNEKREILQGNVYIEGNKIVYVGDVNEEADYiIDATGKVVMPGLINTHAH 62
PRK12394 PRK12394
metallo-dependent hydrolase;
1-62 1.16e-04

metallo-dependent hydrolase;


Pssm-ID: 183497 [Multi-domain]  Cd Length: 379  Bit Score: 43.98  E-value: 1.16e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1755663628   1 MILKNAKIVD-DSFRFADADVAVEEDKISEIAPGLAGGEE--IDLSGCVLVPGFVDIHIHACVGA 62
Cdd:PRK12394    5 ILITNGHIIDpARNINEINNLRIINDIIVDADKYPVASETriIHADGCIVTPGLIDYHAHVFYDG 69
pyrC_multi TIGR00857
dihydroorotase, multifunctional complex type; In contrast to the homodimeric type of ...
 17-57 1.39e-04

dihydroorotase, multifunctional complex type; In contrast to the homodimeric type of dihydroorotase found in E. coli, this class tends to appear in a large, multifunctional complex with aspartate transcarbamoylase. Homologous domains appear in multifunctional proteins of higher eukaryotes. In some species, including Pseudomonas putida and P. aeruginosa, this protein is inactive but is required as a non-catalytic subunit of aspartate transcarbamoylase (ATCase). In these species, a second, active dihydroorotase is also present. The seed for this model does not include any example of the dihydroorotase domain of eukaryotic multidomain pyrimidine synthesis proteins. All proteins described by this model should represent active and inactive dihydroorotase per se and functionally equivalent domains of multifunctional proteins from higher eukaryotes, but exclude related proteins such as allantoinase. [Purines, pyrimidines, nucleosides, and nucleotides, Pyrimidine ribonucleotide biosynthesis]


Pssm-ID: 273302 [Multi-domain]  Cd Length: 411  Bit Score: 43.59  E-value: 1.39e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1755663628  17 DADVAVEEDKISEIA--PGLAGGEEIDLSGCVLVPGFVDIHIH 57
Cdd:TIGR00857   5 EVDILVEGGRIKKIGklRIPPDAEVIDAKGLLVLPGFIDLHVH 47
PRK08417 PRK08417
metal-dependent hydrolase;
22-56 1.47e-04

metal-dependent hydrolase;


Pssm-ID: 236262 [Multi-domain]  Cd Length: 386  Bit Score: 43.54  E-value: 1.47e-04
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 1755663628  22 VEEDKISEIAPGLAGGEEIDLSGCVLVPGFVDIHI 56
Cdd:PRK08417    3 IKDGKITEIGSDLKGEEILDAKGKTLLPALVDLNV 37
PRK02382 PRK02382
dihydroorotase; Provisional
 3-57 3.13e-04

dihydroorotase; Provisional


Pssm-ID: 179417 [Multi-domain]  Cd Length: 443  Bit Score: 42.72  E-value: 3.13e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1755663628   3 LKNAKIVDDSfRFADADVAVEEDKISEIAPGLAG---GEEIDLSGCVLVPGFVDIHIH 57
Cdd:PRK02382    6 LKDGRVYYNN-SLQPRDVRIDGGKITAVGKDLDGsssEEVIDARGMLLLPGGIDVHVH 62
Met_dep_hydrolase_B cd01307
Metallo-dependent hydrolases, subgroup B is part of the superfamily of metallo-dependent ...
 19-87 3.67e-04

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


Pssm-ID: 238632 [Multi-domain]  Cd Length: 338  Bit Score: 41.93  E-value: 3.67e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1755663628  19 DVAVEEDKISEIA---PGLAGGEEIDLSGCVLVPGFVDIHIHACVGADTCDADADglakMCAhlVTKGVTSF 87
Cdd:cd01307     1 DVAIENGKIAAVGaalAAPAATQIVDAGGCYVSPGWIDLHVHVYQGGTRYGDRPD----MIG--VKSGVTTV 66
PRK12393 PRK12393
amidohydrolase; Provisional
 1-57 4.27e-04

amidohydrolase; Provisional


Pssm-ID: 237088 [Multi-domain]  Cd Length: 457  Bit Score: 41.98  E-value: 4.27e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1755663628   1 MILKNAKIV-----DDSFRFADADVAVEEDKISEIAP--GLAGGEEIDLSGCVLVPGFVDIHIH 57
Cdd:PRK12393    4 LLIRNAAAImtglpGDAARLGGPDIRIRDGRIAAIGAltPLPGERVIDATDCVVYPGWVNTHHH 67
PRK09228 PRK09228
guanine deaminase; Provisional
 9-57 4.77e-04

guanine deaminase; Provisional


Pssm-ID: 236419 [Multi-domain]  Cd Length: 433  Bit Score: 42.10  E-value: 4.77e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1755663628   9 VDDSFRF-ADADVAVEEDKI------SEIAPGLAGG-EEIDLSGCVLVPGFVDIHIH 57
Cdd:PRK09228   22 DEDALRYiEDGLLLVEDGRIvaagpyAELRAQLPADaEVTDYRGKLILPGFIDTHIH 78
PRK07228 PRK07228
5'-deoxyadenosine deaminase;
325-361 5.60e-04

5'-deoxyadenosine deaminase;


Pssm-ID: 180895 [Multi-domain]  Cd Length: 445  Bit Score: 41.91  E-value: 5.60e-04
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 1755663628 325 TAIQAATLNPARAIHEDERIGSIKVGKYADMVALDSD 361
Cdd:PRK07228  341 TVFEMATLGGAKAAGFEDEIGSLEEGKKADLAILDLD 377
PRK09228 PRK09228
guanine deaminase; Provisional
 324-359 5.99e-04

guanine deaminase; Provisional


Pssm-ID: 236419 [Multi-domain]  Cd Length: 433  Bit Score: 41.71  E-value: 5.99e-04
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1755663628 324 LTAIQA---ATLNPARAIHEDERIGSIKVGKYADMVALD 359
Cdd:PRK09228  348 LSPFQAfylATLGGARALGLDDRIGNLAPGKEADFVVLD 386
guan_deamin TIGR02967
guanine deaminase; This model describes guanine deaminase, which hydrolyzes guanine to ...
 15-58 7.41e-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: 41.47  E-value: 7.41e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1755663628  15 FADADVAVEEDKI------SEIAPGL-AGGEEIDLSGCVLVPGFVDIHIHA 58
Cdd:TIGR02967   4 FEDGLLVVENGRIvavgdyAELKETLpAGVEIDDYRGHLIMPGFIDTHIHY 54
PRK08203 PRK08203
hydroxydechloroatrazine ethylaminohydrolase; Reviewed
 271-361 1.08e-03

hydroxydechloroatrazine ethylaminohydrolase; Reviewed


Pssm-ID: 236184 [Multi-domain]  Cd Length: 451  Bit Score: 40.99  E-value: 1.08e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755663628 271 MRAAGAPDGvseLGgqtvyVkdgqarlkDGTIAGSTTNLHQEIK-----NLVGWGVPFLTAIQA---ATLNPARAIHEDE 342
Cdd:PRK08203  309 LRAAGVPVG---LG-----V--------DGSASNDGSNLIGEARqalllQRLRYGPDAMTAREAlewATLGGARVLGRDD 372

                          90
                  ....*....|....*....
gi 1755663628 343 rIGSIKVGKYADMVALDSD 361
Cdd:PRK08203  373 -IGSLAPGKLADLALFDLD 390
PRK04250 PRK04250
dihydroorotase; Provisional
 14-57 2.27e-03

dihydroorotase; Provisional


Pssm-ID: 235265 [Multi-domain]  Cd Length: 398  Bit Score: 39.75  E-value: 2.27e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1755663628  14 RFADADVAVEEDKISEIAPGLAGGEE-IDLSGCVLVPGFVDIHIH 57
Cdd:PRK04250   11 RIVEGGIGIENGRISKISLRDLKGKEvIKVKGGIILPGLIDVHVH 55
PRK07369 PRK07369
dihydroorotase; Provisional
 18-58 2.44e-03

dihydroorotase; Provisional


Pssm-ID: 236002 [Multi-domain]  Cd Length: 418  Bit Score: 39.58  E-value: 2.44e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1755663628  18 ADVAVEEDKISEIAPGLAG----GEEIDLSGCVLVPGFVDIHIHA 58
Cdd:PRK07369   22 ADVLIEDGKIQAIEPHIDPippdTQIIDASGLILGPGLVDLYSHS 66
PRK07583 PRK07583
cytosine deaminase;
15-57 2.56e-03

cytosine deaminase;


Pssm-ID: 236062  Cd Length: 438  Bit Score: 39.58  E-value: 2.56e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1755663628  15 FADADVAVEEDKISEIAPGLAGGEE---IDLSGCVLVPGFVDIHIH 57
Cdd:PRK07583   38 LVLVDIEIADGKIAAILPAGGAPDElpaVDLKGRMVWPCFVDMHTH 83
PhnM cd01306
PhnM is believed to be a subunit of the membrane associated C-P lyase complex. C-P lyase is ...
 316-369 2.67e-03

PhnM is believed to be a subunit of the membrane associated C-P lyase complex. C-P lyase is thought to catalyze the direct cleavage of inactivated C-P bonds to yield inorganic phosphate and the corresponding hydrocarbons. It is responsible for cleavage of alkylphosphonates, which are utilized as sole phosphorus sources by many bacteria.


Pssm-ID: 238631  Cd Length: 325  Bit Score: 39.19  E-value: 2.67e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1755663628 316 LVGWGVPflTAIQAATLNPARAIHEDERiGSIKVGKYADMVALDSDLNIRMVVA 369
Cdd:cd01306   270 LGGWSLP--EAVALVSANPARAVGLTDR-GSIAPGKRADLILVDDMDGVPVVRT 320
PRK06038 PRK06038
N-ethylammeline chlorohydrolase; Provisional
 1-58 3.36e-03

N-ethylammeline chlorohydrolase; Provisional


Pssm-ID: 180363 [Multi-domain]  Cd Length: 430  Bit Score: 39.35  E-value: 3.36e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1755663628   1 MILKNAKIVD-DSFRFADADVAVEEDKISEIAPGLAGGEE--IDLSGCVLVPGFVDIHIHA 58
Cdd:PRK06038    4 IIIKNAYVLTmDAGDLKKGSVVIEDGTITEVSESTPGDADtvIDAKGSVVMPGLVNTHTHA 64
FMDH_A cd01304
Formylmethanofuran dehydrogenase (FMDH) subunit A; Methanogenic bacteria and archea derive ...
 3-57 3.66e-03

Formylmethanofuran dehydrogenase (FMDH) subunit A; Methanogenic bacteria and archea derive the energy for autotrophic growth from methanogenesis, the reduction of CO2 with molecular hydrogen as the electron donor. FMDH catalyzes the first step in methanogenesis, the formyl-methanofuran synthesis. In this step, CO2 is bound to methanofuran and subsequently reduced to the formyl state with electrons derived from hydrogen.


Pssm-ID: 238629 [Multi-domain]  Cd Length: 541  Bit Score: 39.32  E-value: 3.66e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1755663628   3 LKNAKIVDDSFRFADA--DVAVEEDKISEIAPGLAGGEEIDLSGCVLVPGFVDIHIH 57
Cdd:cd01304     1 IKNGTVYDPLNGINGEkmDIFIRDGKIVESSSGAKPAKVIDASGKVVMAGGVDMHSH 57
PRK06846 PRK06846
putative deaminase; Validated
 19-57 4.13e-03

putative deaminase; Validated


Pssm-ID: 235873 [Multi-domain]  Cd Length: 410  Bit Score: 38.84  E-value: 4.13e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1755663628  19 DVAVEEDKISEIAPG----LAGGEEIDLSGCVLVPGFVDIHIH 57
Cdd:PRK06846   33 TLEIQDGKIVAIRPNkqvpDATLPTYDANGLLMLPAFREMHIH 75
YtcJ_like cd01300
YtcJ_like metal dependent amidohydrolases. YtcJ is a Bacillus subtilis ORF of unknown function. ...
 19-57 4.48e-03

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: 38.83  E-value: 4.48e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1755663628  19 DVAVEEDKI-----SEIAPGLAGG--EEIDLSGCVLVPGFVDIHIH 57
Cdd:cd01300     1 AVAVRDGRIvavgsDAEAKALKGPatEVIDLKGKTVLPGFIDSHSH 46
Imidazolone-5PH cd01296
Imidazolonepropionase/imidazolone-5-propionate hydrolase (Imidazolone-5PH) catalyzes the third ...
 20-58 5.23e-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: 38.39  E-value: 5.23e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1755663628  20 VAVEEDKISEI-------APGLAGGEEIDLSGCVLVPGFVDIHIHA 58
Cdd:cd01296     1 IAIRDGRIAAVgpaaslpAPGPAAAEEIDAGGRAVTPGLVDCHTHL 46
 
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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