|
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: 815.36 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994419 1 MYALTQGRIYTGHEILDDHAIVIANGLIERICPQTELPTGIEQRSVDGAILAPGFIDVQLNGCGGVQFNDTADAVTVETL 80
Cdd:PRK11170 1 MYALTNGRIYTGHEVLDDHAVVIADGLIEAVCPVAELPPGIEQRDLNGAILSPGFIDLQLNGCGGVQFNDTAEAISVETL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994419 81 EIMQKANERSGCTSYLPTLITSSDDLMKQGVRVMREYLQKHPNQALGLHLEGPWLNIVKKGTHNPDYVRKPDAALVDFLC 160
Cdd:PRK11170 81 EIMQKANEKSGCTSFLPTLITSSDELMKQAVRVMREYLAKHPNQALGLHLEGPYLNLVKKGTHNPEFIRKPDAEMVDFLC 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994419 161 ENADVITKITLAPERVEPEVIRKLVAAGIIVSAGHSNATLKEAKIGFRAGITFATHLFNAMPYITGREPGLAGAIFDEPD 240
Cdd:PRK11170 161 ENADVITKVTLAPEMVDAEVIRKLVEAGIVVSAGHSNATYEEAKAGFRAGITFATHLYNAMPYITGREPGLVGAILDEPD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994419 241 VYCGIIVDGMHVDFANVRLAKRLKGDKLCLVTDATAPAGANIEQFIFAGKTIYYRNGLCVDENGTLSGSSLTMIEGVRNL 320
Cdd:PRK11170 241 VYCGIIADGLHVDYANIRNAKRLKGDKLCLVTDATAPAGANIEQFIFAGKTIYYRDGLCVDENGTLSGSALTMIEAVRNL 320
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 503994419 321 VEHCGIALDEVLRMATLYPSRAIGVDKQLGSIAPGMVANLTAFTRDYKITKTIVNGNEVVTE 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: 570.62 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994419 1 MYALTQGRIYTGHEILDDHAIVIANGLIERICPQTELPTGIEQRSVDGAILAPGFIDVQLNGCGGVQFNDTadavTVETL 80
Cdd:TIGR00221 4 SYLLKDIAIVTGNEVIDNGAVGINDGKISTVSTEAELEPEIKEIDLPGNVLTPGFIDIHIHGCGGVDTNDA----SFETL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994419 81 EIMQKANERSGCTSYLPTLITSSDDLMKQGVRVMREYLQKHPN-QALGLHLEGPWLNIVKKGTHNPDYVRKPDAAL-VDF 158
Cdd:TIGR00221 80 EIMSERLPKSGCTSFLPTLITQPDENIKQAVKNMREYLAKEKNaQALGLHLEGPFLSPEKKGAHPPEYIREPDVELfKKF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994419 159 LCENADVITKITLAPERVEP-EVIRKLVAAGIIVSAGHSNATLKEAKIGFRAGITFATHLFNAMPYITGREPGLAGAIFD 237
Cdd:TIGR00221 160 LCEAGGVITKVTLAPEEDQHfELIRHLKDAGIIVSAGHTNATYELAKAAFKAGATHATHLYNAMSPIHHREPGVIGAVLD 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994419 238 EPDVYCGIIVDGMHVDFANVRLAKRLKGD-KLCLVTDATAPAGANIEQFIFAGKTIYYRNGLCVDENGTLSGSSLTMIEG 316
Cdd:TIGR00221 240 HDDVYTEIIADGIHIHPLNIRLAKKLKGDsKLCLVTDSMAAAGAKDGVFIFGGKTVYIREGTCLDSNGTLAGSSLTMIEG 319
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 503994419 317 VRNLVEHCGIALDEVLRMATLYPSRAIGVDKQLGSIAPGMVANLTAFTRDYKITKTIVNGN 377
Cdd:TIGR00221 320 ARNLVEFTNISLTDAARMSSLNPARALGIDDRLGSVTVGKDANLVVFTPDFEVILTIVNGN 380
|
|
| NagA |
COG1820 |
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism]; |
3-377 |
1.49e-180 |
|
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism];
Pssm-ID: 441425 [Multi-domain] Cd Length: 373 Bit Score: 505.79 E-value: 1.49e-180
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994419 3 ALTQGRIYTGHEILDDHAIVIANGLIERICPQTELptGIEQRSVDGAILAPGFIDVQLNGCGGVQFNDTadavTVETLEI 82
Cdd:COG1820 1 AITNARIFTGDGVLEDGALLIEDGRIAAIGPGAEP--DAEVIDLGGGYLAPGFIDLHVHGGGGVDFMDG----TPEALRT 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994419 83 MQKANERSGCTSYLPTLITSSDDLMKQGVRVMREYLQKHP-NQALGLHLEGPWLNIVKKGTHNPDYVRKPDAALVDFLCE 161
Cdd:COG1820 75 IARAHARHGTTSFLPTTITAPPEDLLRALAAIAEAIEQGGgAGILGIHLEGPFLSPEKKGAHPPEYIRPPDPEELDRLLE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994419 162 NA-DVITKITLAPERVEP-EVIRKLVAAGIIVSAGHSNATLKEAKIGFRAGITFATHLFNAMPYITGREPGLAGAIFDEP 239
Cdd:COG1820 155 AAgGLIKLVTLAPELPGAlEFIRYLVEAGVVVSLGHTDATYEQARAAFEAGATHVTHLFNAMSPLHHREPGVVGAALDDD 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994419 240 DVYCGIIVDGMHVDFANVRLAKRLKG-DKLCLVTDATAPAGANIEQFIFAGKTIYYRNGLCVDENGTLSGSSLTMIEGVR 318
Cdd:COG1820 235 DVYAELIADGIHVHPAAVRLALRAKGpDRLILVTDAMAAAGLPDGEYELGGLEVTVKDGVARLADGTLAGSTLTMDDAVR 314
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 503994419 319 NLVEHCGIALDEVLRMATLYPSRAIGVDKQLGSIAPGMVANLTAFTRDYKITKTIVNGN 377
Cdd:COG1820 315 NLVEWTGLPLEEAVRMASLNPARALGLDDRKGSIAPGKDADLVVLDDDLNVRATWVGGE 373
|
|
| NagA |
cd00854 |
N-acetylglucosamine-6-phosphate deacetylase, NagA, catalyzes the hydrolysis of the N-acetyl ... |
2-376 |
2.07e-143 |
|
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: 411.59 E-value: 2.07e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994419 2 YALTQGRIYTGHEIlDDHAIVIANGLIERICPQTELPTGIEQRSVDGAILAPGFIDVQLNGCGGVQFNDTadavTVETLE 81
Cdd:cd00854 1 LIIKNARILTPGGL-EDGAVLVEDGKIVAIGPEDELEEADEIIDLKGQYLVPGFIDIHIHGGGGADFMDG----TAEALK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994419 82 IMQKANERSGCTSYLPTLITSSDDLMKQGVRVMREYLQKHP-NQALGLHLEGPWLNIVKKGTHNPDYVRKPDAALV-DFL 159
Cdd:cd00854 76 TIAEALAKHGTTSFLPTTVTAPPEEIAKALAAIAEAIAEGQgAEILGIHLEGPFISPEKKGAHPPEYLRAPDPEELkKWL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994419 160 CENADVITKITLAPERVE-PEVIRKLVAAGIIVSAGHSNATLKEAKIGFRAGITFATHLFNAMPYITGREPGLAGAIFDE 238
Cdd:cd00854 156 EAAGGLIKLVTLAPELDGaLELIRYLVERGIIVSIGHSDATYEQAVAAFEAGATHVTHLFNAMSPLHHREPGVVGAALSD 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994419 239 PDVYCGIIVDGMHVDFANVRLAKRLKG-DKLCLVTDATAPAGANIEQFIFAGKTIYYRNGLCVDENGTLSGSSLTMIEGV 317
Cdd:cd00854 236 DDVYAELIADGIHVHPAAVRLAYRAKGaDKIVLVTDAMAAAGLPDGEYELGGQTVTVKDGVARLADGTLAGSTLTMDQAV 315
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 503994419 318 RNLVEHCGIALDEVLRMATLYPSRAIGVDKQLGSIAPGMVANLTAFTRDYKITKTIVNG 376
Cdd:cd00854 316 RNMVKWGGCPLEEAVRMASLNPAKLLGLDDRKGSLKPGKDADLVVLDDDLNVKATWING 374
|
|
| Amidohydro_1 |
pfam01979 |
Amidohydrolase family; This family of enzymes are a a large metal dependent hydrolase ... |
50-379 |
3.31e-42 |
|
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: 150.34 E-value: 3.31e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994419 50 ILAPGFIDVQLNGCGGVQFNDTADAVTV-ETLEIMQKANERSGCTSYLPTLIT--SSDDLMKQGVRvmreylqkhpNQAL 126
Cdd:pfam01979 1 IVLPGLIDAHVHLEMGLLRGIPVPPEFAyEALRLGITTMLKSGTTTVLDMGATtsTGIEALLEAAE----------ELPL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994419 127 GLHLEGPWLNIVKKGTHNPDY-VRKPDAALVDFLCENADVITKITLAPER---VEPEVIRKLVAA------GIIVSAGHS 196
Cdd:pfam01979 71 GLRFLGPGCSLDTDGELEGRKaLREKLKAGAEFIKGMADGVVFVGLAPHGaptFSDDELKAALEEakkyglPVAIHALET 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994419 197 NATLKEAKIGFRAGITFATHLFNAMPYitgrepglagaifDEPDVYCGIIVDGMHVDFANV-RLAKRLKGDKLCLVTDAT 275
Cdd:pfam01979 151 KGEVEDAIAAFGGGIEHGTHLEVAESG-------------GLLDIIKLILAHGVHLSPTEAnLLAEHLKGAGVAHCPFSN 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994419 276 APAGANIEQF---IFAGKTIyyrnGLCVDenGTLSGSSLTMIEGVRNLVE-----HCGIALDEVLRMATLYPSRAIGVDK 347
Cdd:pfam01979 218 SKLRSGRIALrkaLEDGVKV----GLGTD--GAGSGNSLNMLEELRLALElqfdpEGGLSPLEALRMATINPAKALGLDD 291
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 503994419 348 QLGSIAPGMVANLTAF-----------TRDYKITKTIVNGNEV 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: 815.36 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994419 1 MYALTQGRIYTGHEILDDHAIVIANGLIERICPQTELPTGIEQRSVDGAILAPGFIDVQLNGCGGVQFNDTADAVTVETL 80
Cdd:PRK11170 1 MYALTNGRIYTGHEVLDDHAVVIADGLIEAVCPVAELPPGIEQRDLNGAILSPGFIDLQLNGCGGVQFNDTAEAISVETL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994419 81 EIMQKANERSGCTSYLPTLITSSDDLMKQGVRVMREYLQKHPNQALGLHLEGPWLNIVKKGTHNPDYVRKPDAALVDFLC 160
Cdd:PRK11170 81 EIMQKANEKSGCTSFLPTLITSSDELMKQAVRVMREYLAKHPNQALGLHLEGPYLNLVKKGTHNPEFIRKPDAEMVDFLC 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994419 161 ENADVITKITLAPERVEPEVIRKLVAAGIIVSAGHSNATLKEAKIGFRAGITFATHLFNAMPYITGREPGLAGAIFDEPD 240
Cdd:PRK11170 161 ENADVITKVTLAPEMVDAEVIRKLVEAGIVVSAGHSNATYEEAKAGFRAGITFATHLYNAMPYITGREPGLVGAILDEPD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994419 241 VYCGIIVDGMHVDFANVRLAKRLKGDKLCLVTDATAPAGANIEQFIFAGKTIYYRNGLCVDENGTLSGSSLTMIEGVRNL 320
Cdd:PRK11170 241 VYCGIIADGLHVDYANIRNAKRLKGDKLCLVTDATAPAGANIEQFIFAGKTIYYRDGLCVDENGTLSGSALTMIEAVRNL 320
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 503994419 321 VEHCGIALDEVLRMATLYPSRAIGVDKQLGSIAPGMVANLTAFTRDYKITKTIVNGNEVVTE 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: 570.62 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994419 1 MYALTQGRIYTGHEILDDHAIVIANGLIERICPQTELPTGIEQRSVDGAILAPGFIDVQLNGCGGVQFNDTadavTVETL 80
Cdd:TIGR00221 4 SYLLKDIAIVTGNEVIDNGAVGINDGKISTVSTEAELEPEIKEIDLPGNVLTPGFIDIHIHGCGGVDTNDA----SFETL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994419 81 EIMQKANERSGCTSYLPTLITSSDDLMKQGVRVMREYLQKHPN-QALGLHLEGPWLNIVKKGTHNPDYVRKPDAAL-VDF 158
Cdd:TIGR00221 80 EIMSERLPKSGCTSFLPTLITQPDENIKQAVKNMREYLAKEKNaQALGLHLEGPFLSPEKKGAHPPEYIREPDVELfKKF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994419 159 LCENADVITKITLAPERVEP-EVIRKLVAAGIIVSAGHSNATLKEAKIGFRAGITFATHLFNAMPYITGREPGLAGAIFD 237
Cdd:TIGR00221 160 LCEAGGVITKVTLAPEEDQHfELIRHLKDAGIIVSAGHTNATYELAKAAFKAGATHATHLYNAMSPIHHREPGVIGAVLD 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994419 238 EPDVYCGIIVDGMHVDFANVRLAKRLKGD-KLCLVTDATAPAGANIEQFIFAGKTIYYRNGLCVDENGTLSGSSLTMIEG 316
Cdd:TIGR00221 240 HDDVYTEIIADGIHIHPLNIRLAKKLKGDsKLCLVTDSMAAAGAKDGVFIFGGKTVYIREGTCLDSNGTLAGSSLTMIEG 319
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 503994419 317 VRNLVEHCGIALDEVLRMATLYPSRAIGVDKQLGSIAPGMVANLTAFTRDYKITKTIVNGN 377
Cdd:TIGR00221 320 ARNLVEFTNISLTDAARMSSLNPARALGIDDRLGSVTVGKDANLVVFTPDFEVILTIVNGN 380
|
|
| NagA |
COG1820 |
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism]; |
3-377 |
1.49e-180 |
|
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism];
Pssm-ID: 441425 [Multi-domain] Cd Length: 373 Bit Score: 505.79 E-value: 1.49e-180
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994419 3 ALTQGRIYTGHEILDDHAIVIANGLIERICPQTELptGIEQRSVDGAILAPGFIDVQLNGCGGVQFNDTadavTVETLEI 82
Cdd:COG1820 1 AITNARIFTGDGVLEDGALLIEDGRIAAIGPGAEP--DAEVIDLGGGYLAPGFIDLHVHGGGGVDFMDG----TPEALRT 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994419 83 MQKANERSGCTSYLPTLITSSDDLMKQGVRVMREYLQKHP-NQALGLHLEGPWLNIVKKGTHNPDYVRKPDAALVDFLCE 161
Cdd:COG1820 75 IARAHARHGTTSFLPTTITAPPEDLLRALAAIAEAIEQGGgAGILGIHLEGPFLSPEKKGAHPPEYIRPPDPEELDRLLE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994419 162 NA-DVITKITLAPERVEP-EVIRKLVAAGIIVSAGHSNATLKEAKIGFRAGITFATHLFNAMPYITGREPGLAGAIFDEP 239
Cdd:COG1820 155 AAgGLIKLVTLAPELPGAlEFIRYLVEAGVVVSLGHTDATYEQARAAFEAGATHVTHLFNAMSPLHHREPGVVGAALDDD 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994419 240 DVYCGIIVDGMHVDFANVRLAKRLKG-DKLCLVTDATAPAGANIEQFIFAGKTIYYRNGLCVDENGTLSGSSLTMIEGVR 318
Cdd:COG1820 235 DVYAELIADGIHVHPAAVRLALRAKGpDRLILVTDAMAAAGLPDGEYELGGLEVTVKDGVARLADGTLAGSTLTMDDAVR 314
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 503994419 319 NLVEHCGIALDEVLRMATLYPSRAIGVDKQLGSIAPGMVANLTAFTRDYKITKTIVNGN 377
Cdd:COG1820 315 NLVEWTGLPLEEAVRMASLNPARALGLDDRKGSIAPGKDADLVVLDDDLNVRATWVGGE 373
|
|
| NagA |
cd00854 |
N-acetylglucosamine-6-phosphate deacetylase, NagA, catalyzes the hydrolysis of the N-acetyl ... |
2-376 |
2.07e-143 |
|
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: 411.59 E-value: 2.07e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994419 2 YALTQGRIYTGHEIlDDHAIVIANGLIERICPQTELPTGIEQRSVDGAILAPGFIDVQLNGCGGVQFNDTadavTVETLE 81
Cdd:cd00854 1 LIIKNARILTPGGL-EDGAVLVEDGKIVAIGPEDELEEADEIIDLKGQYLVPGFIDIHIHGGGGADFMDG----TAEALK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994419 82 IMQKANERSGCTSYLPTLITSSDDLMKQGVRVMREYLQKHP-NQALGLHLEGPWLNIVKKGTHNPDYVRKPDAALV-DFL 159
Cdd:cd00854 76 TIAEALAKHGTTSFLPTTVTAPPEEIAKALAAIAEAIAEGQgAEILGIHLEGPFISPEKKGAHPPEYLRAPDPEELkKWL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994419 160 CENADVITKITLAPERVE-PEVIRKLVAAGIIVSAGHSNATLKEAKIGFRAGITFATHLFNAMPYITGREPGLAGAIFDE 238
Cdd:cd00854 156 EAAGGLIKLVTLAPELDGaLELIRYLVERGIIVSIGHSDATYEQAVAAFEAGATHVTHLFNAMSPLHHREPGVVGAALSD 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994419 239 PDVYCGIIVDGMHVDFANVRLAKRLKG-DKLCLVTDATAPAGANIEQFIFAGKTIYYRNGLCVDENGTLSGSSLTMIEGV 317
Cdd:cd00854 236 DDVYAELIADGIHVHPAAVRLAYRAKGaDKIVLVTDAMAAAGLPDGEYELGGQTVTVKDGVARLADGTLAGSTLTMDQAV 315
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 503994419 318 RNLVEHCGIALDEVLRMATLYPSRAIGVDKQLGSIAPGMVANLTAFTRDYKITKTIVNG 376
Cdd:cd00854 316 RNMVKWGGCPLEEAVRMASLNPAKLLGLDDRKGSLKPGKDADLVVLDDDLNVKATWING 374
|
|
| Amidohydro_1 |
pfam01979 |
Amidohydrolase family; This family of enzymes are a a large metal dependent hydrolase ... |
50-379 |
3.31e-42 |
|
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: 150.34 E-value: 3.31e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994419 50 ILAPGFIDVQLNGCGGVQFNDTADAVTV-ETLEIMQKANERSGCTSYLPTLIT--SSDDLMKQGVRvmreylqkhpNQAL 126
Cdd:pfam01979 1 IVLPGLIDAHVHLEMGLLRGIPVPPEFAyEALRLGITTMLKSGTTTVLDMGATtsTGIEALLEAAE----------ELPL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994419 127 GLHLEGPWLNIVKKGTHNPDY-VRKPDAALVDFLCENADVITKITLAPER---VEPEVIRKLVAA------GIIVSAGHS 196
Cdd:pfam01979 71 GLRFLGPGCSLDTDGELEGRKaLREKLKAGAEFIKGMADGVVFVGLAPHGaptFSDDELKAALEEakkyglPVAIHALET 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994419 197 NATLKEAKIGFRAGITFATHLFNAMPYitgrepglagaifDEPDVYCGIIVDGMHVDFANV-RLAKRLKGDKLCLVTDAT 275
Cdd:pfam01979 151 KGEVEDAIAAFGGGIEHGTHLEVAESG-------------GLLDIIKLILAHGVHLSPTEAnLLAEHLKGAGVAHCPFSN 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994419 276 APAGANIEQF---IFAGKTIyyrnGLCVDenGTLSGSSLTMIEGVRNLVE-----HCGIALDEVLRMATLYPSRAIGVDK 347
Cdd:pfam01979 218 SKLRSGRIALrkaLEDGVKV----GLGTD--GAGSGNSLNMLEELRLALElqfdpEGGLSPLEALRMATINPAKALGLDD 291
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 503994419 348 QLGSIAPGMVANLTAF-----------TRDYKITKTIVNGNEV 379
Cdd:pfam01979 292 KVGSIEVGKDADLVVVdldplaaffglKPDGNVKKVIVKGKIV 334
|
|
| HutI |
COG1228 |
Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport ... |
1-382 |
2.11e-14 |
|
Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440841 [Multi-domain] Cd Length: 386 Bit Score: 73.84 E-value: 2.11e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994419 1 MYALTQGRIYTGH--EILDDHAIVIANGLIERICPQTEL--PTGIEQRSVDGAILAPGFID--VQLNGCGGVQFNDTADA 74
Cdd:COG1228 9 TLLITNATLVDGTggGVIENGTVLVEDGKIAAVGPAADLavPAGAEVIDATGKTVLPGLIDahTHLGLGGGRAVEFEAGG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994419 75 VTVETLEIMQKANERSgctsylptlitssDDLMKQG---VRVMREY---LQKHPNQALGLHLEGPwlNIVKKGT----HN 144
Cdd:COG1228 89 GITPTVDLVNPADKRL-------------RRALAAGvttVRDLPGGplgLRDAIIAGESKLLPGP--RVLAAGPalslTG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994419 145 PDYVRKPD---AALVDFLCENADVItKITLAPERVE--PEVIRKLVAA----GIIVsAGHSNaTLKEAKIGFRAGITFAT 215
Cdd:COG1228 154 GAHARGPEearAALRELLAEGADYI-KVFAEGGAPDfsLEELRAILEAahalGLPV-AAHAH-QADDIRLAVEAGVDSIE 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994419 216 HLFNAMP------------YITgrePGLAGAIFDEPDVYCGIIVDGMHVDFANVRLAKRLK--GDKLCLVTDAtapagan 281
Cdd:COG1228 231 HGTYLDDevadllaeagtvVLV---PTLSLFLALLEGAAAPVAAKARKVREAALANARRLHdaGVPVALGTDA------- 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994419 282 ieqfifagktiyyrnglcvdENGTLSGSSLTMIegVRNLVEHcGIALDEVLRMATLYPSRAIGVDKQLGSIAPGMVANLT 361
Cdd:COG1228 301 --------------------GVGVPPGRSLHRE--LALAVEA-GLTPEEALRAATINAAKALGLDDDVGSLEPGKLADLV 357
|
410 420
....*....|....*....|....*....
gi 503994419 362 AFTRD--------YKITKTIVNGNEVVTE 382
Cdd:COG1228 358 LLDGDplediaylEDVRAVMKDGRVVDRS 386
|
|
| Met_dep_hydrolase_C |
cd01309 |
Metallo-dependent hydrolases, subgroup C is part of the superfamily of metallo-dependent ... |
258-379 |
8.20e-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: 8.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994419 258 RLAKRLKGDKLCLVTDATAPAGANIEQF---IFAGKTIYYRNGLCVdenGTLSGSSLTMIegvRNLVEHCGIA------L 328
Cdd:cd01309 229 KLADELAKHGIPVIYGPTLTLPKKVEEVndaIDTNAYLLKKGGVAF---AISSDHPVLNI---RNLNLEAAKAvkyglsY 302
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 503994419 329 DEVLRMATLYPSRAIGVDKQLGSIAPGMVANLTAFTRD-----YKITKTIVNGNEV 379
Cdd:cd01309 303 EEALKAITINPAKILGIEDRVGSLEPGKDADLVVWNGDpleptSKPEQVYIDGRLV 358
|
|
| YtcJ |
COG1574 |
Predicted amidohydrolase YtcJ [General function prediction only]; |
328-379 |
4.23e-06 |
|
Predicted amidohydrolase YtcJ [General function prediction only];
Pssm-ID: 441182 [Multi-domain] Cd Length: 535 Bit Score: 48.64 E-value: 4.23e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 503994419 328 LDEVLRMATLYPSRAIGVDKQLGSIAPGMVANLTAFTRDY-----------KITKTIVNGNEV 379
Cdd:COG1574 469 VEEALRAYTIGAAYAAFEEDEKGSLEPGKLADFVVLDRDPltvppeeikdiKVLLTVVGGRVV 531
|
|
| PRK09045 |
PRK09045 |
TRZ/ATZ family hydrolase; |
327-363 |
8.58e-06 |
|
TRZ/ATZ family hydrolase;
Pssm-ID: 236366 [Multi-domain] Cd Length: 443 Bit Score: 47.60 E-value: 8.58e-06
10 20 30
....*....|....*....|....*....|....*....
gi 503994419 327 ALD--EVLRMATLYPSRAIGVDKQLGSIAPGMVANLTAF 363
Cdd:PRK09045 339 ALPahTALRMATLNGARALGLDDEIGSLEPGKQADLVAV 377
|
|
| AdeC |
COG1001 |
Adenine deaminase [Nucleotide transport and metabolism]; |
317-380 |
1.75e-05 |
|
Adenine deaminase [Nucleotide transport and metabolism];
Pssm-ID: 440625 [Multi-domain] Cd Length: 559 Bit Score: 46.63 E-value: 1.75e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 503994419 317 VRNLVEHcGIALDEVLRMATLYPSRAIGVdKQLGSIAPGMVANLTAFT--RDYKITKTIVNGNEVV 380
Cdd:COG1001 276 VRRAIEL-GLDPVTAIQMATLNAAEHFGL-KDLGAIAPGRRADIVLLDdlEDFKVEKVYADGKLVA 339
|
|
| Isoaspartyl-dipeptidase |
cd01308 |
Isoaspartyl dipeptidase hydrolyzes the beta-L-isoaspartyl linkages in dipeptides, as part of ... |
21-382 |
9.45e-05 |
|
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: 9.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994419 21 IVIANGLIERICPQTELPTGIEQRSVD--GAILAPGFIDVQLNGCGGvqfnDTADAVTVETLEIMQKANERSGCTSYLPT 98
Cdd:cd01308 20 ILIAGGKILAIEDQLNLPGYENVTVVDlhGKILVPGFIDQHVHIIGG----GGEGGPSTRTPEVTLSDLTTAGVTTVVGC 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994419 99 LITSSDDlmkqgvRVMREYLQKhpnqALGLHLEGpwlniVKKGTHNPDYvRKPDAALVDflcenaDVITKITLapervep 178
Cdd:cd01308 96 LGTDGIS------RSMEDLLAK----ARALEEEG-----ITCFVYTGSY-EVPTRTITG------SIRKDLLL------- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994419 179 evIRKLVAAGIIVSAGHSNA---------TLKEAKIGF----RAGITfATHLFNA---------------------MPYI 224
Cdd:cd01308 147 --IDKVIGVGEIAISDHRSSqptveelarIAAEARVGGllggKAGIV-HIHLGDGkralspifelieeteipitqfLPTH 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994419 225 TGREPGL--AGAIFDEP----DVYCGIIVDgmHVDFANVRLAKRLKgdklclvtdATAPAGANIEQFIFA----GKTIYY 294
Cdd:cd01308 224 INRTAPLfeQGVEFAKMggtiDLTSSIDPQ--FRKEGEVRPSEALK---------RLLEQGVPLERITFSsdgnGSLPKF 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994419 295 rnglcvDENGTLSG----SSLTMIEGVRNLVEHCGIALDEVLRMATLYPSRAIGVDKQlGSIAPGMVANLTAFTRDYKIT 370
Cdd:cd01308 293 ------DENGNLVGlgvgSVDTLLREVREAVKCGDIPLEVALRVITSNVARILKLRKK-GEIQPGFDADLVILDKDLDIN 365
|
410
....*....|..
gi 503994419 371 KTIVNGNEVVTE 382
Cdd:cd01308 366 SVIAKGQIMVRN 377
|
|
| Amidohydro_3 |
pfam07969 |
Amidohydrolase family; |
328-380 |
1.03e-04 |
|
Amidohydrolase family;
Pssm-ID: 400360 [Multi-domain] Cd Length: 464 Bit Score: 44.06 E-value: 1.03e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 503994419 328 LDEVLRMATLYPSRAIGVDKQLGSIAPGMVANLTAFTRDY-----------KITKTIVNGNEVV 380
Cdd:pfam07969 401 LEEALALYTSGPAKALGLEDRKGTLGVGKDADLVVLDDDPltvdppaiadiRVRLTVVDGRVVY 464
|
|
| SsnA |
COG0402 |
Cytosine/adenosine deaminase or related metal-dependent hydrolase [Nucleotide transport and ... |
297-363 |
2.21e-04 |
|
Cytosine/adenosine deaminase or related metal-dependent hydrolase [Nucleotide transport and metabolism, General function prediction only]; Cytosine/adenosine deaminase or related metal-dependent hydrolase is part of the Pathway/BioSystem: Pyrimidine salvage
Pssm-ID: 440171 [Multi-domain] Cd Length: 416 Bit Score: 42.89 E-value: 2.21e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 503994419 297 GLCVDenGTLSGSSLTMIEGVR------NLVEHCGIALD--EVLRMATLYPSRAIGVDKQLGSIAPGMVANLTAF 363
Cdd:COG0402 305 GLGTD--GAASNNSLDMFEEMRlaallqRLRGGDPTALSarEALEMATLGGARALGLDDEIGSLEPGKRADLVVL 377
|
|
| YtcJ_like |
cd01300 |
YtcJ_like metal dependent amidohydrolases. YtcJ is a Bacillus subtilis ORF of unknown function. ... |
312-361 |
2.57e-04 |
|
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: 43.07 E-value: 2.57e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 503994419 312 TMIEGVRNLVEHCGIALDEVLRMATLYPSRAIGVDKQLGSIAPGMVANLT 361
Cdd:cd01300 429 KTPGGGVLGNPEERLSLEEALRAYTIGAAYAIGEEDEKGSLEPGKLADFV 478
|
|
| ATZ_TRZ_like |
cd01298 |
TRZ/ATZ family contains enzymes from the atrazine degradation pathway and related hydrolases. ... |
297-363 |
3.74e-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: 42.19 E-value: 3.74e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 503994419 297 GLCVDenGTLSGSSLTMIEGVRN-LVEHCGIALD-------EVLRMATLYPSRAIGVDkQLGSIAPGMVANLTAF 363
Cdd:cd01298 297 GLGTD--GAASNNNLDMFEEMRLaALLQKLAHGDptalpaeEALEMATIGGAKALGLD-EIGSLEVGKKADLILI 368
|
|
| AllB |
COG0044 |
Dihydroorotase or related cyclic amidohydrolase [Nucleotide transport and metabolism]; ... |
4-59 |
9.30e-04 |
|
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: 41.23 E-value: 9.30e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 503994419 4 LTQGRIYT--GHEILDdhaIVIANGLIERICPQTELPTGIEQRSVDGAILAPGFIDVQ 59
Cdd:COG0044 2 IKNGRVVDpgGLERAD---VLIEDGRIAAIGPDLAAPEAAEVIDATGLLVLPGLIDLH 56
|
|
| Met_dep_hydrolase_A |
cd01299 |
Metallo-dependent hydrolases, subgroup A is part of the superfamily of metallo-dependent ... |
178-360 |
1.16e-03 |
|
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: 40.74 E-value: 1.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994419 178 PEVIRKLVAAGI-IVSAGH--SNATLKEAKigfRAGITFA-THLFNAMPYITGREPGLAgaifDEPDVYCGIIVDGMhvd 253
Cdd:cd01299 183 AEAIRRAIRAGVdTIEHGFliDDETIELMK---EKGIFLVpTLATYEALAAEGAAPGLP----ADSAEKVALVLEAG--- 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503994419 254 FANVRLAKRlKGDKLCLVTDA---TAPAGANIEQFIFagktiyyrnglcvdengtlsgssltmiegvrnLVEHCGIALdE 330
Cdd:cd01299 253 RDALRRAHK-AGVKIAFGTDAgfpVPPHGWNARELEL--------------------------------LVKAGGTPA-E 298
|
170 180 190
....*....|....*....|....*....|
gi 503994419 331 VLRMATLYPSRAIGVDKQLGSIAPGMVANL 360
Cdd:cd01299 299 ALRAATANAAELLGLSDELGVIEAGKLADL 328
|
|
| AdeC |
cd01295 |
Adenine deaminase (AdeC) directly deaminates adenine to form hypoxanthine. This reaction is ... |
317-380 |
1.23e-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: 40.67 E-value: 1.23e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 503994419 317 VRNLVEHcGIALDEVLRMATLYPSRAIGVDKqLGSIAPGMVANLTAFT--RDYKITKTIVNGNEVV 380
Cdd:cd01295 227 VRRAIEA-GIPPEDAIQMATINPAECYGLHD-LGAIAPGRIADIVILDdlENFNITTVLAKGIAVV 290
|
|
| SsnA |
COG0402 |
Cytosine/adenosine deaminase or related metal-dependent hydrolase [Nucleotide transport and ... |
2-57 |
4.12e-03 |
|
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: 39.04 E-value: 4.12e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 503994419 2 YALTQGRIYTG---HEILDDHAIVIANGLIERICPQTELP---TGIEQRSVDGAILAPGFID 57
Cdd:COG0402 2 LLIRGAWVLTMdpaGGVLEDGAVLVEDGRIAAVGPGAELParyPAAEVIDAGGKLVLPGLVN 63
|
|
| PRK08203 |
PRK08203 |
hydroxydechloroatrazine ethylaminohydrolase; Reviewed |
297-366 |
7.95e-03 |
|
hydroxydechloroatrazine ethylaminohydrolase; Reviewed
Pssm-ID: 236184 [Multi-domain] Cd Length: 451 Bit Score: 38.29 E-value: 7.95e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 503994419 297 GLCVDenGTLSGSSLTMIEGVRN--LVEHCG-----IALDEVLRMATLYPSRAIGVDkQLGSIAPGMVANLTAFTRD 366
Cdd:PRK08203 317 GLGVD--GSASNDGSNLIGEARQalLLQRLRygpdaMTAREALEWATLGGARVLGRD-DIGSLAPGKLADLALFDLD 390
|
|
| PRK07228 |
PRK07228 |
5'-deoxyadenosine deaminase; |
330-361 |
9.45e-03 |
|
5'-deoxyadenosine deaminase;
Pssm-ID: 180895 [Multi-domain] Cd Length: 445 Bit Score: 38.06 E-value: 9.45e-03
10 20 30
....*....|....*....|....*....|..
gi 503994419 330 EVLRMATLYPSRAIGVDKQLGSIAPGMVANLT 361
Cdd:PRK07228 341 TVFEMATLGGAKAAGFEDEIGSLEEGKKADLA 372
|
|
| |
