NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|446193314|ref|WP_000271169|]
View 

MULTISPECIES: N-acetylglucosamine-6-phosphate deacetylase [Shigella]

Protein Classification

N-acetylglucosamine-6-phosphate deacetylase( domain architecture ID 10793546)

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
nagA PRK11170
N-acetylglucosamine-6-phosphate deacetylase; Provisional
 1-382 0e+00

N-acetylglucosamine-6-phosphate deacetylase; Provisional


:

Pssm-ID: 183010  Cd Length: 382  Bit Score: 806.89  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446193314   1 MYALTQGRIFTGHEFLDDHAVVIADGLIKSVCPVAELPPEIEQRSLNGAILSPGFIDVQLNGCGGVQFNDTAEAVSVETL 80
Cdd:PRK11170   1 MYALTNGRIYTGHEVLDDHAVVIADGLIEAVCPVAELPPGIEQRDLNGAILSPGFIDLQLNGCGGVQFNDTAEAISVETL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446193314  81 EIMQKANEKSGCTNYLPTLITTSDELMKQGVRVMREYLARHPNQALGLHLEGPWLNLVKKGTHNPNFVRKPDAALVDFLC 160
Cdd:PRK11170  81 EIMQKANEKSGCTSFLPTLITSSDELMKQAVRVMREYLAKHPNQALGLHLEGPYLNLVKKGTHNPEFIRKPDAEMVDFLC 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446193314 161 ENADVITKVTLAPEMVPAEVISKLANAGIVVSAGHSNATLKEAKAGFRAGITFATHLYNAMPYITGREPGLAGAILDEAD 240
Cdd:PRK11170 161 ENADVITKVTLAPEMVDAEVIRKLVEAGIVVSAGHSNATYEEAKAGFRAGITFATHLYNAMPYITGREPGLVGAILDEPD 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446193314 241 IYCGIIADGLHVDYANIRNAKRLKGDKLCLVTDATAPAGANIEQFIFAGKTIYYRNGLCVDENGTLSGSSLTMIEGVRNL 320
Cdd:PRK11170 241 VYCGIIADGLHVDYANIRNAKRLKGDKLCLVTDATAPAGANIEQFIFAGKTIYYRDGLCVDENGTLSGSALTMIEAVRNL 320

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446193314 321 VEHCGIALDEVLRMATLYPARAIGVEKRLGTLAAGKVANLTSFTPDFKITKTIVNGNEVVTQ 382
Cdd:PRK11170 321 VEHVGIALDEALRMATLYPARAIGVDKRLGSIEAGKVANLTAFTRDFKITKTIVNGNEVVTQ 382
 
Name Accession Description Interval E-value
nagA PRK11170
N-acetylglucosamine-6-phosphate deacetylase; Provisional
 1-382 0e+00

N-acetylglucosamine-6-phosphate deacetylase; Provisional


Pssm-ID: 183010  Cd Length: 382  Bit Score: 806.89  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446193314   1 MYALTQGRIFTGHEFLDDHAVVIADGLIKSVCPVAELPPEIEQRSLNGAILSPGFIDVQLNGCGGVQFNDTAEAVSVETL 80
Cdd:PRK11170   1 MYALTNGRIYTGHEVLDDHAVVIADGLIEAVCPVAELPPGIEQRDLNGAILSPGFIDLQLNGCGGVQFNDTAEAISVETL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446193314  81 EIMQKANEKSGCTNYLPTLITTSDELMKQGVRVMREYLARHPNQALGLHLEGPWLNLVKKGTHNPNFVRKPDAALVDFLC 160
Cdd:PRK11170  81 EIMQKANEKSGCTSFLPTLITSSDELMKQAVRVMREYLAKHPNQALGLHLEGPYLNLVKKGTHNPEFIRKPDAEMVDFLC 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446193314 161 ENADVITKVTLAPEMVPAEVISKLANAGIVVSAGHSNATLKEAKAGFRAGITFATHLYNAMPYITGREPGLAGAILDEAD 240
Cdd:PRK11170 161 ENADVITKVTLAPEMVDAEVIRKLVEAGIVVSAGHSNATYEEAKAGFRAGITFATHLYNAMPYITGREPGLVGAILDEPD 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446193314 241 IYCGIIADGLHVDYANIRNAKRLKGDKLCLVTDATAPAGANIEQFIFAGKTIYYRNGLCVDENGTLSGSSLTMIEGVRNL 320
Cdd:PRK11170 241 VYCGIIADGLHVDYANIRNAKRLKGDKLCLVTDATAPAGANIEQFIFAGKTIYYRDGLCVDENGTLSGSALTMIEAVRNL 320

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446193314 321 VEHCGIALDEVLRMATLYPARAIGVEKRLGTLAAGKVANLTSFTPDFKITKTIVNGNEVVTQ 382
Cdd:PRK11170 321 VEHVGIALDEALRMATLYPARAIGVDKRLGSIEAGKVANLTAFTRDFKITKTIVNGNEVVTQ 382
nagA TIGR00221
N-acetylglucosamine-6-phosphate deacetylase; [Central intermediary metabolism, Amino sugars]
 1-377 0e+00

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


Pssm-ID: 272968  Cd Length: 380  Bit Score: 612.22  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446193314    1 MYALTQGRIFTGHEFLDDHAVVIADGLIKSVCPVAELPPEIEQRSLNGAILSPGFIDVQLNGCGGVQFNDTaeavSVETL 80
Cdd:TIGR00221   4 SYLLKDIAIVTGNEVIDNGAVGINDGKISTVSTEAELEPEIKEIDLPGNVLTPGFIDIHIHGCGGVDTNDA----SFETL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446193314   81 EIMQKANEKSGCTNYLPTLITTSDELMKQGVRVMREYLARHPN-QALGLHLEGPWLNLVKKGTHNPNFVRKPDAAL-VDF 158
Cdd:TIGR00221  80 EIMSERLPKSGCTSFLPTLITQPDENIKQAVKNMREYLAKEKNaQALGLHLEGPFLSPEKKGAHPPEYIREPDVELfKKF 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446193314  159 LCENADVITKVTLAP-EMVPAEVISKLANAGIVVSAGHSNATLKEAKAGFRAGITFATHLYNAMPYITGREPGLAGAILD 237
Cdd:TIGR00221 160 LCEAGGVITKVTLAPeEDQHFELIRHLKDAGIIVSAGHTNATYELAKAAFKAGATHATHLYNAMSPIHHREPGVIGAVLD 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446193314  238 EADIYCGIIADGLHVDYANIRNAKRLKGD-KLCLVTDATAPAGANIEQFIFAGKTIYYRNGLCVDENGTLSGSSLTMIEG 316
Cdd:TIGR00221 240 HDDVYTEIIADGIHIHPLNIRLAKKLKGDsKLCLVTDSMAAAGAKDGVFIFGGKTVYIREGTCLDSNGTLAGSSLTMIEG 319

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446193314  317 VRNLVEHCGIALDEVLRMATLYPARAIGVEKRLGTLAAGKVANLTSFTPDFKITKTIVNGN 377
Cdd:TIGR00221 320 ARNLVEFTNISLTDAARMSSLNPARALGIDDRLGSVTVGKDANLVVFTPDFEVILTIVNGN 380
NagA COG1820
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism];
3-377 4.41e-178

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


Pssm-ID: 441425 [Multi-domain]  Cd Length: 373  Bit Score: 499.63  E-value: 4.41e-178
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446193314   3 ALTQGRIFTGHEFLDDHAVVIADGLIKSVCPVAELPPEIEQrsLNGAILSPGFIDVQLNGCGGVQFNDTaeavSVETLEI 82
Cdd:COG1820    1 AITNARIFTGDGVLEDGALLIEDGRIAAIGPGAEPDAEVID--LGGGYLAPGFIDLHVHGGGGVDFMDG----TPEALRT 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446193314  83 MQKANEKSGCTNYLPTLITTSDELMKQGVRVMREYLARHP-NQALGLHLEGPWLNLVKKGTHNPNFVRKPDAALVDFLCE 161
Cdd:COG1820   75 IARAHARHGTTSFLPTTITAPPEDLLRALAAIAEAIEQGGgAGILGIHLEGPFLSPEKKGAHPPEYIRPPDPEELDRLLE 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446193314 162 NA-DVITKVTLAPEMVPA-EVISKLANAGIVVSAGHSNATLKEAKAGFRAGITFATHLYNAMPYITGREPGLAGAILDEA 239
Cdd:COG1820  155 AAgGLIKLVTLAPELPGAlEFIRYLVEAGVVVSLGHTDATYEQARAAFEAGATHVTHLFNAMSPLHHREPGVVGAALDDD 234

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446193314 240 DIYCGIIADGLHVDYANIRNAKRLKG-DKLCLVTDATAPAGANIEQFIFAGKTIYYRNGLCVDENGTLSGSSLTMIEGVR 318
Cdd:COG1820  235 DVYAELIADGIHVHPAAVRLALRAKGpDRLILVTDAMAAAGLPDGEYELGGLEVTVKDGVARLADGTLAGSTLTMDDAVR 314

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 446193314 319 NLVEHCGIALDEVLRMATLYPARAIGVEKRLGTLAAGKVANLTSFTPDFKITKTIVNGN 377
Cdd:COG1820  315 NLVEWTGLPLEEAVRMASLNPARALGLDDRKGSIAPGKDADLVVLDDDLNVRATWVGGE 373
NagA cd00854
N-acetylglucosamine-6-phosphate deacetylase, NagA, catalyzes the hydrolysis of the N-acetyl ...
 2-376 2.09e-140

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: 404.27  E-value: 2.09e-140
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446193314   2 YALTQGRIFTGhEFLDDHAVVIADGLIKSVCPVAELPPEIEQRSLNGAILSPGFIDVQLNGCGGVQFNDTaeavSVETLE 81
Cdd:cd00854    1 LIIKNARILTP-GGLEDGAVLVEDGKIVAIGPEDELEEADEIIDLKGQYLVPGFIDIHIHGGGGADFMDG----TAEALK 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446193314  82 IMQKANEKSGCTNYLPTLITTSDELMKQGVRVMREYLARHP-NQALGLHLEGPWLNLVKKGTHNPNFVRKPDAALV-DFL 159
Cdd:cd00854   76 TIAEALAKHGTTSFLPTTVTAPPEEIAKALAAIAEAIAEGQgAEILGIHLEGPFISPEKKGAHPPEYLRAPDPEELkKWL 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446193314 160 CENADVITKVTLAPEMVPA-EVISKLANAGIVVSAGHSNATLKEAKAGFRAGITFATHLYNAMPYITGREPGLAGAILDE 238
Cdd:cd00854  156 EAAGGLIKLVTLAPELDGAlELIRYLVERGIIVSIGHSDATYEQAVAAFEAGATHVTHLFNAMSPLHHREPGVVGAALSD 235

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446193314 239 ADIYCGIIADGLHVDYANIRNAKRLKG-DKLCLVTDATAPAGANIEQFIFAGKTIYYRNGLCVDENGTLSGSSLTMIEGV 317
Cdd:cd00854  236 DDVYAELIADGIHVHPAAVRLAYRAKGaDKIVLVTDAMAAAGLPDGEYELGGQTVTVKDGVARLADGTLAGSTLTMDQAV 315

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 446193314 318 RNLVEHCGIALDEVLRMATLYPARAIGVEKRLGTLAAGKVANLTSFTPDFKITKTIVNG 376
Cdd:cd00854  316 RNMVKWGGCPLEEAVRMASLNPAKLLGLDDRKGSLKPGKDADLVVLDDDLNVKATWING 374
Amidohydro_1 pfam01979
Amidohydrolase family; This family of enzymes are a a large metal dependent hydrolase ...
 50-379 4.38e-45

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: 158.05  E-value: 4.38e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446193314   50 ILSPGFIDVQLNGCGGVQFNDTA-EAVSVETLEIMQKANEKSGCTNYLPTLITTS--DELMKQGVRvmreylarhpNQAL 126
Cdd:pfam01979   1 IVLPGLIDAHVHLEMGLLRGIPVpPEFAYEALRLGITTMLKSGTTTVLDMGATTStgIEALLEAAE----------ELPL 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446193314  127 GLHLEGPWLNLVKKGTHNPNF-VRKPDAALVDFLCENADVITKVTLAPEMVPA---EVISKLA------NAGIVVSAGHS 196
Cdd:pfam01979  71 GLRFLGPGCSLDTDGELEGRKaLREKLKAGAEFIKGMADGVVFVGLAPHGAPTfsdDELKAALeeakkyGLPVAIHALET 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446193314  197 NATLKEAKAGFRAGITFATHLYNAMPYitgrepglagailDEADIYCGIIADGLHVDYANI-RNAKRLKGDKLCLVTDAT 275
Cdd:pfam01979 151 KGEVEDAIAAFGGGIEHGTHLEVAESG-------------GLLDIIKLILAHGVHLSPTEAnLLAEHLKGAGVAHCPFSN 217

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446193314  276 APAGANIEQF---IFAGKTIyyrnGLCVDenGTLSGSSLTMIEGVRNLVE-----HCGIALDEVLRMATLYPARAIGVEK 347
Cdd:pfam01979 218 SKLRSGRIALrkaLEDGVKV----GLGTD--GAGSGNSLNMLEELRLALElqfdpEGGLSPLEALRMATINPAKALGLDD 291

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|...
gi 446193314  348 RLGTLAAGKVANLTSF-----------TPDFKITKTIVNGNEV 379
Cdd:pfam01979 292 KVGSIEVGKDADLVVVdldplaaffglKPDGNVKKVIVKGKIV 334
 
Name Accession Description Interval E-value
nagA PRK11170
N-acetylglucosamine-6-phosphate deacetylase; Provisional
 1-382 0e+00

N-acetylglucosamine-6-phosphate deacetylase; Provisional


Pssm-ID: 183010  Cd Length: 382  Bit Score: 806.89  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446193314   1 MYALTQGRIFTGHEFLDDHAVVIADGLIKSVCPVAELPPEIEQRSLNGAILSPGFIDVQLNGCGGVQFNDTAEAVSVETL 80
Cdd:PRK11170   1 MYALTNGRIYTGHEVLDDHAVVIADGLIEAVCPVAELPPGIEQRDLNGAILSPGFIDLQLNGCGGVQFNDTAEAISVETL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446193314  81 EIMQKANEKSGCTNYLPTLITTSDELMKQGVRVMREYLARHPNQALGLHLEGPWLNLVKKGTHNPNFVRKPDAALVDFLC 160
Cdd:PRK11170  81 EIMQKANEKSGCTSFLPTLITSSDELMKQAVRVMREYLAKHPNQALGLHLEGPYLNLVKKGTHNPEFIRKPDAEMVDFLC 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446193314 161 ENADVITKVTLAPEMVPAEVISKLANAGIVVSAGHSNATLKEAKAGFRAGITFATHLYNAMPYITGREPGLAGAILDEAD 240
Cdd:PRK11170 161 ENADVITKVTLAPEMVDAEVIRKLVEAGIVVSAGHSNATYEEAKAGFRAGITFATHLYNAMPYITGREPGLVGAILDEPD 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446193314 241 IYCGIIADGLHVDYANIRNAKRLKGDKLCLVTDATAPAGANIEQFIFAGKTIYYRNGLCVDENGTLSGSSLTMIEGVRNL 320
Cdd:PRK11170 241 VYCGIIADGLHVDYANIRNAKRLKGDKLCLVTDATAPAGANIEQFIFAGKTIYYRDGLCVDENGTLSGSALTMIEAVRNL 320

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446193314 321 VEHCGIALDEVLRMATLYPARAIGVEKRLGTLAAGKVANLTSFTPDFKITKTIVNGNEVVTQ 382
Cdd:PRK11170 321 VEHVGIALDEALRMATLYPARAIGVDKRLGSIEAGKVANLTAFTRDFKITKTIVNGNEVVTQ 382
nagA TIGR00221
N-acetylglucosamine-6-phosphate deacetylase; [Central intermediary metabolism, Amino sugars]
 1-377 0e+00

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


Pssm-ID: 272968  Cd Length: 380  Bit Score: 612.22  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446193314    1 MYALTQGRIFTGHEFLDDHAVVIADGLIKSVCPVAELPPEIEQRSLNGAILSPGFIDVQLNGCGGVQFNDTaeavSVETL 80
Cdd:TIGR00221   4 SYLLKDIAIVTGNEVIDNGAVGINDGKISTVSTEAELEPEIKEIDLPGNVLTPGFIDIHIHGCGGVDTNDA----SFETL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446193314   81 EIMQKANEKSGCTNYLPTLITTSDELMKQGVRVMREYLARHPN-QALGLHLEGPWLNLVKKGTHNPNFVRKPDAAL-VDF 158
Cdd:TIGR00221  80 EIMSERLPKSGCTSFLPTLITQPDENIKQAVKNMREYLAKEKNaQALGLHLEGPFLSPEKKGAHPPEYIREPDVELfKKF 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446193314  159 LCENADVITKVTLAP-EMVPAEVISKLANAGIVVSAGHSNATLKEAKAGFRAGITFATHLYNAMPYITGREPGLAGAILD 237
Cdd:TIGR00221 160 LCEAGGVITKVTLAPeEDQHFELIRHLKDAGIIVSAGHTNATYELAKAAFKAGATHATHLYNAMSPIHHREPGVIGAVLD 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446193314  238 EADIYCGIIADGLHVDYANIRNAKRLKGD-KLCLVTDATAPAGANIEQFIFAGKTIYYRNGLCVDENGTLSGSSLTMIEG 316
Cdd:TIGR00221 240 HDDVYTEIIADGIHIHPLNIRLAKKLKGDsKLCLVTDSMAAAGAKDGVFIFGGKTVYIREGTCLDSNGTLAGSSLTMIEG 319

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446193314  317 VRNLVEHCGIALDEVLRMATLYPARAIGVEKRLGTLAAGKVANLTSFTPDFKITKTIVNGN 377
Cdd:TIGR00221 320 ARNLVEFTNISLTDAARMSSLNPARALGIDDRLGSVTVGKDANLVVFTPDFEVILTIVNGN 380
NagA COG1820
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism];
3-377 4.41e-178

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


Pssm-ID: 441425 [Multi-domain]  Cd Length: 373  Bit Score: 499.63  E-value: 4.41e-178
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446193314   3 ALTQGRIFTGHEFLDDHAVVIADGLIKSVCPVAELPPEIEQrsLNGAILSPGFIDVQLNGCGGVQFNDTaeavSVETLEI 82
Cdd:COG1820    1 AITNARIFTGDGVLEDGALLIEDGRIAAIGPGAEPDAEVID--LGGGYLAPGFIDLHVHGGGGVDFMDG----TPEALRT 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446193314  83 MQKANEKSGCTNYLPTLITTSDELMKQGVRVMREYLARHP-NQALGLHLEGPWLNLVKKGTHNPNFVRKPDAALVDFLCE 161
Cdd:COG1820   75 IARAHARHGTTSFLPTTITAPPEDLLRALAAIAEAIEQGGgAGILGIHLEGPFLSPEKKGAHPPEYIRPPDPEELDRLLE 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446193314 162 NA-DVITKVTLAPEMVPA-EVISKLANAGIVVSAGHSNATLKEAKAGFRAGITFATHLYNAMPYITGREPGLAGAILDEA 239
Cdd:COG1820  155 AAgGLIKLVTLAPELPGAlEFIRYLVEAGVVVSLGHTDATYEQARAAFEAGATHVTHLFNAMSPLHHREPGVVGAALDDD 234

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446193314 240 DIYCGIIADGLHVDYANIRNAKRLKG-DKLCLVTDATAPAGANIEQFIFAGKTIYYRNGLCVDENGTLSGSSLTMIEGVR 318
Cdd:COG1820  235 DVYAELIADGIHVHPAAVRLALRAKGpDRLILVTDAMAAAGLPDGEYELGGLEVTVKDGVARLADGTLAGSTLTMDDAVR 314

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 446193314 319 NLVEHCGIALDEVLRMATLYPARAIGVEKRLGTLAAGKVANLTSFTPDFKITKTIVNGN 377
Cdd:COG1820  315 NLVEWTGLPLEEAVRMASLNPARALGLDDRKGSIAPGKDADLVVLDDDLNVRATWVGGE 373
NagA cd00854
N-acetylglucosamine-6-phosphate deacetylase, NagA, catalyzes the hydrolysis of the N-acetyl ...
 2-376 2.09e-140

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: 404.27  E-value: 2.09e-140
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446193314   2 YALTQGRIFTGhEFLDDHAVVIADGLIKSVCPVAELPPEIEQRSLNGAILSPGFIDVQLNGCGGVQFNDTaeavSVETLE 81
Cdd:cd00854    1 LIIKNARILTP-GGLEDGAVLVEDGKIVAIGPEDELEEADEIIDLKGQYLVPGFIDIHIHGGGGADFMDG----TAEALK 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446193314  82 IMQKANEKSGCTNYLPTLITTSDELMKQGVRVMREYLARHP-NQALGLHLEGPWLNLVKKGTHNPNFVRKPDAALV-DFL 159
Cdd:cd00854   76 TIAEALAKHGTTSFLPTTVTAPPEEIAKALAAIAEAIAEGQgAEILGIHLEGPFISPEKKGAHPPEYLRAPDPEELkKWL 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446193314 160 CENADVITKVTLAPEMVPA-EVISKLANAGIVVSAGHSNATLKEAKAGFRAGITFATHLYNAMPYITGREPGLAGAILDE 238
Cdd:cd00854  156 EAAGGLIKLVTLAPELDGAlELIRYLVERGIIVSIGHSDATYEQAVAAFEAGATHVTHLFNAMSPLHHREPGVVGAALSD 235

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446193314 239 ADIYCGIIADGLHVDYANIRNAKRLKG-DKLCLVTDATAPAGANIEQFIFAGKTIYYRNGLCVDENGTLSGSSLTMIEGV 317
Cdd:cd00854  236 DDVYAELIADGIHVHPAAVRLAYRAKGaDKIVLVTDAMAAAGLPDGEYELGGQTVTVKDGVARLADGTLAGSTLTMDQAV 315

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 446193314 318 RNLVEHCGIALDEVLRMATLYPARAIGVEKRLGTLAAGKVANLTSFTPDFKITKTIVNG 376
Cdd:cd00854  316 RNMVKWGGCPLEEAVRMASLNPAKLLGLDDRKGSLKPGKDADLVVLDDDLNVKATWING 374
Amidohydro_1 pfam01979
Amidohydrolase family; This family of enzymes are a a large metal dependent hydrolase ...
 50-379 4.38e-45

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: 158.05  E-value: 4.38e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446193314   50 ILSPGFIDVQLNGCGGVQFNDTA-EAVSVETLEIMQKANEKSGCTNYLPTLITTS--DELMKQGVRvmreylarhpNQAL 126
Cdd:pfam01979   1 IVLPGLIDAHVHLEMGLLRGIPVpPEFAYEALRLGITTMLKSGTTTVLDMGATTStgIEALLEAAE----------ELPL 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446193314  127 GLHLEGPWLNLVKKGTHNPNF-VRKPDAALVDFLCENADVITKVTLAPEMVPA---EVISKLA------NAGIVVSAGHS 196
Cdd:pfam01979  71 GLRFLGPGCSLDTDGELEGRKaLREKLKAGAEFIKGMADGVVFVGLAPHGAPTfsdDELKAALeeakkyGLPVAIHALET 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446193314  197 NATLKEAKAGFRAGITFATHLYNAMPYitgrepglagailDEADIYCGIIADGLHVDYANI-RNAKRLKGDKLCLVTDAT 275
Cdd:pfam01979 151 KGEVEDAIAAFGGGIEHGTHLEVAESG-------------GLLDIIKLILAHGVHLSPTEAnLLAEHLKGAGVAHCPFSN 217

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446193314  276 APAGANIEQF---IFAGKTIyyrnGLCVDenGTLSGSSLTMIEGVRNLVE-----HCGIALDEVLRMATLYPARAIGVEK 347
Cdd:pfam01979 218 SKLRSGRIALrkaLEDGVKV----GLGTD--GAGSGNSLNMLEELRLALElqfdpEGGLSPLEALRMATINPAKALGLDD 291

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|...
gi 446193314  348 RLGTLAAGKVANLTSF-----------TPDFKITKTIVNGNEV 379
Cdd:pfam01979 292 KVGSIEVGKDADLVVVdldplaaffglKPDGNVKKVIVKGKIV 334
HutI COG1228
Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport ...
 1-360 5.27e-14

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


Pssm-ID: 440841 [Multi-domain]  Cd Length: 386  Bit Score: 72.69  E-value: 5.27e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446193314   1 MYALTQGRIFTGH--EFLDDHAVVIADGLIKSVCPVAEL--PPEIEQRSLNGAILSPGFID----VQLNGCGGVQF---- 68
Cdd:COG1228    9 TLLITNATLVDGTggGVIENGTVLVEDGKIAAVGPAADLavPAGAEVIDATGKTVLPGLIDahthLGLGGGRAVEFeagg 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446193314  69 NDTAEAVSVETLEIMQKANEKSGctnylptlITTsdelmkqgVRVMREY---LARHPNQALGLHLEGPwlNLVKKGT--- 142
Cdd:COG1228   89 GITPTVDLVNPADKRLRRALAAG--------VTT--------VRDLPGGplgLRDAIIAGESKLLPGP--RVLAAGPals 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446193314 143 -HNPNFVRKPD---AALVDFLCENADVItKVTLAPEMV--PAEVISKLANA----GIVVsAGHSNaTLKEAKAGFRAGIT 212
Cdd:COG1228  151 lTGGAHARGPEearAALRELLAEGADYI-KVFAEGGAPdfSLEELRAILEAahalGLPV-AAHAH-QADDIRLAVEAGVD 227

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446193314 213 FATHLYNAMP------------YITgrePGLAGAILDEADIYCGIIADGLHVDYANIRNAKRLK--GDKLCLVTDAtapa 278
Cdd:COG1228  228 SIEHGTYLDDevadllaeagtvVLV---PTLSLFLALLEGAAAPVAAKARKVREAALANARRLHdaGVPVALGTDA---- 300

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446193314 279 ganieqfifagktiyyrnglcvdENGTLSGSSLTMIegVRNLVEHcGIALDEVLRMATLYPARAIGVEKRLGTLAAGKVA 358
Cdd:COG1228  301 -----------------------GVGVPPGRSLHRE--LALAVEA-GLTPEEALRAATINAAKALGLDDDVGSLEPGKLA 354


                 ..
gi 446193314 359 NL 360
Cdd:COG1228  355 DL 356
Met_dep_hydrolase_C cd01309
Metallo-dependent hydrolases, subgroup C is part of the superfamily of metallo-dependent ...
 260-379 5.27e-08

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: 54.24  E-value: 5.27e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446193314 260 AKRLKGDKLCLVTDATAPAGANIEQF---IFAGKTIYYRNGLCVdenGTLSGSSLTMIegvRNLVEHCGIA------LDE 330
Cdd:cd01309  231 ADELAKHGIPVIYGPTLTLPKKVEEVndaIDTNAYLLKKGGVAF---AISSDHPVLNI---RNLNLEAAKAvkyglsYEE 304

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 446193314 331 VLRMATLYPARAIGVEKRLGTLAAGKVANLT-----SFTPDFKITKTIVNGNEV 379
Cdd:cd01309  305 ALKAITINPAKILGIEDRVGSLEPGKDADLVvwngdPLEPTSKPEQVYIDGRLV 358
Amidohydro_3 pfam07969
Amidohydrolase family;
328-380 2.89e-06

Amidohydrolase family;


Pssm-ID: 400360 [Multi-domain]  Cd Length: 464  Bit Score: 49.07  E-value: 2.89e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446193314  328 LDEVLRMATLYPARAIGVEKRLGTLAAGKVANLTSFTPDF-----------KITKTIVNGNEVV 380
Cdd:pfam07969 401 LEEALALYTSGPAKALGLEDRKGTLGVGKDADLVVLDDDPltvdppaiadiRVRLTVVDGRVVY 464
YtcJ COG1574
Predicted amidohydrolase YtcJ [General function prediction only];
328-379 9.07e-06

Predicted amidohydrolase YtcJ [General function prediction only];


Pssm-ID: 441182 [Multi-domain]  Cd Length: 535  Bit Score: 47.49  E-value: 9.07e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446193314 328 LDEVLRMATLYPARAIGVEKRLGTLAAGKVANLT-----SFT------PDFKITKTIVNGNEV 379
Cdd:COG1574  469 VEEALRAYTIGAAYAAFEEDEKGSLEPGKLADFVvldrdPLTvppeeiKDIKVLLTVVGGRVV 531
AdeC COG1001
Adenine deaminase [Nucleotide transport and metabolism];
317-380 1.24e-05

Adenine deaminase [Nucleotide transport and metabolism];


Pssm-ID: 440625 [Multi-domain]  Cd Length: 559  Bit Score: 47.02  E-value: 1.24e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446193314 317 VRNLVEHcGIALDEVLRMATLYPARAIGVeKRLGTLAAGKVAN--LTSFTPDFKITKTIVNGNEVV 380
Cdd:COG1001  276 VRRAIEL-GLDPVTAIQMATLNAAEHFGL-KDLGAIAPGRRADivLLDDLEDFKVEKVYADGKLVA 339
PRK09045 PRK09045
TRZ/ATZ family hydrolase;
327-363 1.56e-05

TRZ/ATZ family hydrolase;


Pssm-ID: 236366 [Multi-domain]  Cd Length: 443  Bit Score: 46.83  E-value: 1.56e-05
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 446193314 327 ALD--EVLRMATLYPARAIGVEKRLGTLAAGKVANLTSF 363
Cdd:PRK09045 339 ALPahTALRMATLNGARALGLDDEIGSLEPGKQADLVAV 377
YtcJ_like cd01300
YtcJ_like metal dependent amidohydrolases. YtcJ is a Bacillus subtilis ORF of unknown function. ...
 312-361 1.88e-05

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: 46.53  E-value: 1.88e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 446193314 312 TMIEGVRNLVEHCGIALDEVLRMATLYPARAIGVEKRLGTLAAGKVANLT 361
Cdd:cd01300  429 KTPGGGVLGNPEERLSLEEALRAYTIGAAYAIGEEDEKGSLEPGKLADFV 478
SsnA COG0402
Cytosine/adenosine deaminase or related metal-dependent hydrolase [Nucleotide transport and ...
 297-366 4.06e-05

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: 45.20  E-value: 4.06e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446193314 297 GLCVDenGTLSGSSLTMIEGVR------NLVEHCGIALD--EVLRMATLYPARAIGVEKRLGTLAAGKVANLTSFTPD 366
Cdd:COG0402  305 GLGTD--GAASNNSLDMFEEMRlaallqRLRGGDPTALSarEALEMATLGGARALGLDDEIGSLEPGKRADLVVLDLD 380
SsnA COG0402
Cytosine/adenosine deaminase or related metal-dependent hydrolase [Nucleotide transport and ...
 2-57 5.73e-05

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: 44.82  E-value: 5.73e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446193314   2 YALTQGRIFTG---HEFLDDHAVVIADGLIKSVCPVAELP---PEIEQRSLNGAILSPGFID 57
Cdd:COG0402    2 LLIRGAWVLTMdpaGGVLEDGAVLVEDGRIAAVGPGAELParyPAAEVIDAGGKLVLPGLVN 63
Isoaspartyl-dipeptidase cd01308
Isoaspartyl dipeptidase hydrolyzes the beta-L-isoaspartyl linkages in dipeptides, as part of ...
 301-380 1.07e-04

Isoaspartyl dipeptidase hydrolyzes the beta-L-isoaspartyl linkages in dipeptides, as part of the degradative pathway to eliminate proteins with beta-L-isoaspartyl peptide bonds, bonds whereby the beta-group of an aspartate forms the peptide link with the amino group of the following amino acid. Formation of this bond is a spontaneous nonenzymatic reaction in nature and can profoundly effect the function of the protein. Isoaspartyl dipeptidase is an octameric enzyme that contains a binuclear zinc center in the active site of each subunit and shows a strong preference of hydrolyzing Asp-Leu dipeptides.


Pssm-ID: 238633 [Multi-domain]  Cd Length: 387  Bit Score: 43.92  E-value: 1.07e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446193314 301 DENGTLSG----SSLTMIEGVRNLVEHCGIALDEVLRMATLYPARAIGVEKRlGTLAAGKVANLTSFTPDFKITKTIVNG 376
Cdd:cd01308  293 DENGNLVGlgvgSVDTLLREVREAVKCGDIPLEVALRVITSNVARILKLRKK-GEIQPGFDADLVILDKDLDINSVIAKG 371


                 ....
gi 446193314 377 NEVV 380
Cdd:cd01308  372 QIMV 375
PRK09237 PRK09237
amidohydrolase/deacetylase family metallohydrolase;
325-364 5.28e-04

amidohydrolase/deacetylase family metallohydrolase;


Pssm-ID: 236423 [Multi-domain]  Cd Length: 380  Bit Score: 41.76  E-value: 5.28e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 446193314 325 GIALDEVLRMATLYPARAIGVEkRLGTLAAGKVANLTSFT 364
Cdd:PRK09237 295 GMPLEEVIAAVTKNAADALRLP-ELGRLQVGSDADLTLFT 333
Imidazolone-5PH cd01296
Imidazolonepropionase/imidazolone-5-propionate hydrolase (Imidazolone-5PH) catalyzes the third ...
 303-360 6.43e-04

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


Pssm-ID: 238621 [Multi-domain]  Cd Length: 371  Bit Score: 41.47  E-value: 6.43e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 446193314 303 NGTLSGSSLTMIEGVRNLvehcGIALDEVLRMATLYPARAIGVEKRLGTLAAGKVANL 360
Cdd:cd01296  291 SSPTSSMPLVMHLACRLM----RMTPEEALTAATINAAAALGLGETVGSLEVGKQADL 344
Met_dep_hydrolase_A cd01299
Metallo-dependent hydrolases, subgroup A is part of the superfamily of metallo-dependent ...
 320-360 6.49e-04

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


Pssm-ID: 238624 [Multi-domain]  Cd Length: 342  Bit Score: 41.51  E-value: 6.49e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 446193314 320 LVEHCGIALdEVLRMATLYPARAIGVEKRLGTLAAGKVANL 360
Cdd:cd01299  289 LVKAGGTPA-EALRAATANAAELLGLSDELGVIEAGKLADL 328
PRK07228 PRK07228
5'-deoxyadenosine deaminase;
330-361 6.94e-04

5'-deoxyadenosine deaminase;


Pssm-ID: 180895 [Multi-domain]  Cd Length: 445  Bit Score: 41.52  E-value: 6.94e-04
                         10        20        30
                 ....*....|....*....|....*....|..
gi 446193314 330 EVLRMATLYPARAIGVEKRLGTLAAGKVANLT 361
Cdd:PRK07228 341 TVFEMATLGGAKAAGFEDEIGSLEEGKKADLA 372
ATZ_TRZ_like cd01298
TRZ/ATZ family contains enzymes from the atrazine degradation pathway and related hydrolases. ...
 297-380 8.93e-04

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


Pssm-ID: 238623 [Multi-domain]  Cd Length: 411  Bit Score: 41.03  E-value: 8.93e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446193314 297 GLCVDenGTLSGSSLTMIEGVRN-LVEHCGIALD-------EVLRMATLYPARAIGVEKrLGTLAAGKVANLTSFTPDFK 368
Cdd:cd01298  297 GLGTD--GAASNNNLDMFEEMRLaALLQKLAHGDptalpaeEALEMATIGGAKALGLDE-IGSLEVGKKADLILIDLDGP 373

                         90       100       110
                 ....*....|....*....|....*....|..
gi 446193314 369 --------------------ITKTIVNGNEVV 380
Cdd:cd01298  374 hllpvhdpishlvysanggdVDTVIVNGRVVM 405
PRK09228 PRK09228
guanine deaminase; Provisional
 13-57 1.35e-03

guanine deaminase; Provisional


Pssm-ID: 236419 [Multi-domain]  Cd Length: 433  Bit Score: 40.56  E-value: 1.35e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 446193314  13 HEFLDDHAVVIADGLIKSVCPVAEL----PPEIEQRSLNGAILSPGFID 57
Cdd:PRK09228  26 LRYIEDGLLLVEDGRIVAAGPYAELraqlPADAEVTDYRGKLILPGFID 74
Met_dep_hydrolase_D cd01312
Metallo-dependent hydrolases, subgroup D is part of the superfamily of metallo-dependent ...
 307-363 1.75e-03

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


Pssm-ID: 238637 [Multi-domain]  Cd Length: 381  Bit Score: 40.13  E-value: 1.75e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446193314 307 SGSSLTMIEGVR-NLVEHCGIALD----EVLRMATLYPARAIGVEkrLGTLAAGKVANLTSF 363
Cdd:cd01312  292 SNISLSLLDELRaLLDLHPEEDLLelasELLLMATLGGARALGLN--NGEIEAGKRADFAVF 351
AdeC cd01295
Adenine deaminase (AdeC) directly deaminates adenine to form hypoxanthine. This reaction is ...
 317-380 1.98e-03

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: 39.90  E-value: 1.98e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446193314 317 VRNLVEHcGIALDEVLRMATLYPARAIGVEKrLGTLAAGKVANLTSFTP--DFKITKTIVNGNEVV 380
Cdd:cd01295  227 VRRAIEA-GIPPEDAIQMATINPAECYGLHD-LGAIAPGRIADIVILDDleNFNITTVLAKGIAVV 290
PRK12394 PRK12394
metallo-dependent hydrolase;
325-363 2.53e-03

metallo-dependent hydrolase;


Pssm-ID: 183497 [Multi-domain]  Cd Length: 379  Bit Score: 39.74  E-value: 2.53e-03
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 446193314 325 GIALDEVLRMATLYPARAIGVEKRLGTLAAGKVANLTSF 363
Cdd:PRK12394 300 GMALEDVINACTHTPAVLMGMAAEIGTLAPGAFADIAIF 338
PRK09045 PRK09045
TRZ/ATZ family hydrolase;
16-56 3.02e-03

TRZ/ATZ family hydrolase;


Pssm-ID: 236366 [Multi-domain]  Cd Length: 443  Bit Score: 39.51  E-value: 3.02e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 446193314  16 LDDHAVVIADGLIKSVCPVAE----LPPEiEQRSLNGAILSPGFI 56
Cdd:PRK09045  26 LEDHAVAIRDGRIVAILPRAEararYAAA-ETVELPDHVLIPGLI 69
Met_dep_hydrolase_B cd01307
Metallo-dependent hydrolases, subgroup B is part of the superfamily of metallo-dependent ...
 325-364 3.53e-03

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: 39.23  E-value: 3.53e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 446193314 325 GIALDEVLRMATLYPARAIGVeKRLGTLAAGKVANLTSFT 364
Cdd:cd01307  276 GMPLEEVIEAVTANPARMLGL-AEIGTLAVGYDADLTVFD 314
PRK08204 PRK08204
hypothetical protein; Provisional
 325-361 5.31e-03

hypothetical protein; Provisional


Pssm-ID: 181288 [Multi-domain]  Cd Length: 449  Bit Score: 38.83  E-value: 5.31e-03
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 446193314 325 GIALDEVLRMATLYPARAIGVEKRLGTLAAGKVANLT 361
Cdd:PRK08204 341 TLTARQVLEWATIEGARALGLEDRIGSLTPGKQADLV 377
PRK15446 PRK15446
phosphonate metabolism protein PhnM; Provisional
 320-381 7.22e-03

phosphonate metabolism protein PhnM; Provisional


Pssm-ID: 237967 [Multi-domain]  Cd Length: 383  Bit Score: 38.24  E-value: 7.22e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446193314 320 LVEHCGIALDEVLRMATLYPARAIGVEKRlGTLAAGKVANLTSFTPD---FKITKTIVNGNEVVT 381
Cdd:PRK15446 318 LADDGGLDLPQAVALVTANPARAAGLDDR-GEIAPGKRADLVRVRRAgglPVVRAVWRGGRRVFL 381
PRK08418 PRK08418
metal-dependent hydrolase;
307-382 8.97e-03

metal-dependent hydrolase;


Pssm-ID: 181419 [Multi-domain]  Cd Length: 408  Bit Score: 38.03  E-value: 8.97e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446193314 307 SGSSLTMIEGVR-NLVEHCGIALDE----VLRMATLYPARAIGVEkrLGTLAAGKVANLTSFTPDFKITktivNGNEVVT 381
Cdd:PRK08418 315 SNISLSLLDELRaALLTHANMPLLElakiLLLSATRYGAKALGLN--NGEIKEGKDADLSVFELPEECT----KKEQLPL 388


                 .
gi 446193314 382 Q 382
Cdd:PRK08418 389 Q 389
 
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