|
Name |
Accession |
Description |
Interval |
E-value |
| NagA |
COG1820 |
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism]; |
4-373 |
1.44e-167 |
|
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism];
Pssm-ID: 441425 [Multi-domain] Cd Length: 373 Bit Score: 472.66 E-value: 1.44e-167
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995764522 4 LLRARRLLTGQGWLDDHQLRMDRGVITAIEP-IPAGINTREAD--LLCPAYIDIHVHGGAGVDVMDDAPDVLDRLAMHKA 80
Cdd:COG1820 1 AITNARIFTGDGVLEDGALLIEDGRIAAIGPgAEPDAEVIDLGggYLAPGFIDLHVHGGGGVDFMDGTPEALRTIARAHA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995764522 81 REGVGAFLPTTVTAPLEAIHGALRRIARRCHvGGPGAQVLGSYLEGPYFTPQNKGAHPQELFRELDLAELDDLIAVSQNT 160
Cdd:COG1820 81 RHGTTSFLPTTITAPPEDLLRALAAIAEAIE-QGGGAGILGIHLEGPFLSPEKKGAHPPEYIRPPDPEELDRLLEAAGGL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995764522 161 LRVVALAPEKAEALKAIHHLKQKGIRVMLGHSAATYAQTLAAFDAGAAGLVHCYNGMTGLHHREPGMVGAGLTDPRAWLE 240
Cdd:COG1820 160 IKLVTLAPELPGALEFIRYLVEAGVVVSLGHTDATYEQARAAFEAGATHVTHLFNAMSPLHHREPGVVGAALDDDDVYAE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995764522 241 LIADGHHVHPGAMRLCC-CCAKDRTVLITDAMQAAGMPDGGYTLCGESVEMQGGVVRTASGGLAGSTLALDAAVRNMVEH 319
Cdd:COG1820 240 LIADGIHVHPAAVRLALrAKGPDRLILVTDAMAAAGLPDGEYELGGLEVTVKDGVARLADGTLAGSTLTMDDAVRNLVEW 319
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 1995764522 320 TGVAPEQAIHMASLHPARLLGMDHLLGSLAPGKRANIIALDAGLHLRQIWIQGQ 373
Cdd:COG1820 320 TGLPLEEAVRMASLNPARALGLDDRKGSIAPGKDADLVVLDDDLNVRATWVGGE 373
|
|
| NagA |
cd00854 |
N-acetylglucosamine-6-phosphate deacetylase, NagA, catalyzes the hydrolysis of the N-acetyl ... |
4-372 |
6.27e-161 |
|
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: 455.88 E-value: 6.27e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995764522 4 LLRARRLLTGqGWLDDHQLRMDRGVITAIEPIPAGINTREA-----DLLCPAYIDIHVHGGAGVDVMDDAPDVLDRLAMH 78
Cdd:cd00854 2 IIKNARILTP-GGLEDGAVLVEDGKIVAIGPEDELEEADEIidlkgQYLVPGFIDIHIHGGGGADFMDGTAEALKTIAEA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995764522 79 KAREGVGAFLPTTVTAPLEAIHGALRRIARRCHvGGPGAQVLGSYLEGPYFTPQNKGAHPQELFRELDLAELDDLIAVSQ 158
Cdd:cd00854 81 LAKHGTTSFLPTTVTAPPEEIAKALAAIAEAIA-EGQGAEILGIHLEGPFISPEKKGAHPPEYLRAPDPEELKKWLEAAG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995764522 159 NTLRVVALAPEKAEALKAIHHLKQKGIRVMLGHSAATYAQTLAAFDAGAAGLVHCYNGMTGLHHREPGMVGAGLTDPRAW 238
Cdd:cd00854 160 GLIKLVTLAPELDGALELIRYLVERGIIVSIGHSDATYEQAVAAFEAGATHVTHLFNAMSPLHHREPGVVGAALSDDDVY 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995764522 239 LELIADGHHVHPGAMRLCCCCA-KDRTVLITDAMQAAGMPDGGYTLCGESVEMQGGVVRTASGGLAGSTLALDAAVRNMV 317
Cdd:cd00854 240 AELIADGIHVHPAAVRLAYRAKgADKIVLVTDAMAAAGLPDGEYELGGQTVTVKDGVARLADGTLAGSTLTMDQAVRNMV 319
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 1995764522 318 EHTGVAPEQAIHMASLHPARLLGMDHLLGSLAPGKRANIIALDAGLHLRQIWIQG 372
Cdd:cd00854 320 KWGGCPLEEAVRMASLNPAKLLGLDDRKGSLKPGKDADLVVLDDDLNVKATWING 374
|
|
| nagA |
TIGR00221 |
N-acetylglucosamine-6-phosphate deacetylase; [Central intermediary metabolism, Amino sugars] |
1-373 |
5.83e-93 |
|
N-acetylglucosamine-6-phosphate deacetylase; [Central intermediary metabolism, Amino sugars]
Pssm-ID: 272968 Cd Length: 380 Bit Score: 283.26 E-value: 5.83e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995764522 1 MSQLLRARRLLTGQGWLDDHQLRMDRGVITAI---EPIPAGINTRE--ADLLCPAYIDIHVHGGAGVDVMDDAPDVLDRL 75
Cdd:TIGR00221 3 ESYLLKDIAIVTGNEVIDNGAVGINDGKISTVsteAELEPEIKEIDlpGNVLTPGFIDIHIHGCGGVDTNDASFETLEIM 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995764522 76 AMHKAREGVGAFLPTTVTAPLEAIHGALRrIARRCHVGGPGAQVLGSYLEGPYFTPQNKGAHPQELFRELDLAELDDLIA 155
Cdd:TIGR00221 83 SERLPKSGCTSFLPTLITQPDENIKQAVK-NMREYLAKEKNAQALGLHLEGPFLSPEKKGAHPPEYIREPDVELFKKFLC 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995764522 156 VSQNTLRVVALAPEKAEALKAIHHLKQKGIRVMLGHSAATYAQTLAAFDAGAAGLVHCYNGMTGLHHREPGMVGAGLTDP 235
Cdd:TIGR00221 162 EAGGVITKVTLAPEEDQHFELIRHLKDAGIIVSAGHTNATYELAKAAFKAGATHATHLYNAMSPIHHREPGVIGAVLDHD 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995764522 236 RAWLELIADGHHVHPGAMRLCCCCAKD-RTVLITDAMQAAGMPDGGYTLCGESVEMQGGVVRTASGGLAGSTLALDAAVR 314
Cdd:TIGR00221 242 DVYTEIIADGIHIHPLNIRLAKKLKGDsKLCLVTDSMAAAGAKDGVFIFGGKTVYIREGTCLDSNGTLAGSSLTMIEGAR 321
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 1995764522 315 NMVEHTGVAPEQAIHMASLHPARLLGMDHLLGSLAPGKRANIIALDAGLHLRQIWIQGQ 373
Cdd:TIGR00221 322 NLVEFTNISLTDAARMSSLNPARALGIDDRLGSVTVGKDANLVVFTPDFEVILTIVNGN 380
|
|
| nagA |
PRK11170 |
N-acetylglucosamine-6-phosphate deacetylase; Provisional |
9-360 |
5.14e-82 |
|
N-acetylglucosamine-6-phosphate deacetylase; Provisional
Pssm-ID: 183010 Cd Length: 382 Bit Score: 255.28 E-value: 5.14e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995764522 9 RLLTGQGWLDDHQLRMDRGVITAIEPI---PAGINTREAD--LLCPAYIDIHVHGGAGVDVMDDAPDV-LDRLA-MHKA- 80
Cdd:PRK11170 8 RIYTGHEVLDDHAVVIADGLIEAVCPVaelPPGIEQRDLNgaILSPGFIDLQLNGCGGVQFNDTAEAIsVETLEiMQKAn 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995764522 81 -REGVGAFLPTTVTAPLEAIHGALRrIARRCHVGGPGaQVLGSYLEGPYFTPQNKGAHPQELFRELDlAELDDLIAVSQN 159
Cdd:PRK11170 88 eKSGCTSFLPTLITSSDELMKQAVR-VMREYLAKHPN-QALGLHLEGPYLNLVKKGTHNPEFIRKPD-AEMVDFLCENAD 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995764522 160 TLRVVALAPEKAEAlKAIHHLKQKGIRVMLGHSAATYAQTLAAFDAGAAGLVHCYNGMTGLHHREPGMVGAGLTDPRAWL 239
Cdd:PRK11170 165 VITKVTLAPEMVDA-EVIRKLVEAGIVVSAGHSNATYEEAKAGFRAGITFATHLYNAMPYITGREPGLVGAILDEPDVYC 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995764522 240 ELIADGHHVHPGAMRLCCCCAKDRTVLITDAMQAAGMPDGGYTLCGESVEMQGGVVRTASGGLAGSTLALDAAVRNMVEH 319
Cdd:PRK11170 244 GIIADGLHVDYANIRNAKRLKGDKLCLVTDATAPAGANIEQFIFAGKTIYYRDGLCVDENGTLSGSALTMIEAVRNLVEH 323
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 1995764522 320 TGVAPEQAIHMASLHPARLLGMDHLLGSLAPGKRANIIALD 360
Cdd:PRK11170 324 VGIALDEALRMATLYPARAIGVDKRLGSIEAGKVANLTAFT 364
|
|
| Amidohydro_1 |
pfam01979 |
Amidohydrolase family; This family of enzymes are a a large metal dependent hydrolase ... |
46-360 |
4.00e-16 |
|
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: 78.31 E-value: 4.00e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995764522 46 LLCPAYIDIHVHGGAGVDVMDDAPDvldRLAMHKAREGVGAFLP---TTVTAPLEAIHGALRRIARRCHvggpgAQVLGS 122
Cdd:pfam01979 1 IVLPGLIDAHVHLEMGLLRGIPVPP---EFAYEALRLGITTMLKsgtTTVLDMGATTSTGIEALLEAAE-----ELPLGL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995764522 123 YLEGPYFTPQNKGAHPQELFRELDLAELDDLIAVSQNTLRVVALAPE------KAEALKAIHHLKQKGIRVM--LGHSAA 194
Cdd:pfam01979 73 RFLGPGCSLDTDGELEGRKALREKLKAGAEFIKGMADGVVFVGLAPHgaptfsDDELKAALEEAKKYGLPVAihALETKG 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995764522 195 TYAQTLAAFDAGAaglVHcyngMTGLHHREPGMvgagltDPRAWLELIADGHHVHPGAMRLC---------CCCAKDRTV 265
Cdd:pfam01979 153 EVEDAIAAFGGGI---EH----GTHLEVAESGG------LLDIIKLILAHGVHLSPTEANLLaehlkgagvAHCPFSNSK 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995764522 266 LITDAMQAAGMPDggytlcgesvemQGGVVRTAS-GGLAGSTLALDAAVRNMVE-----HTGVAPEQAIHMASLHPARLL 339
Cdd:pfam01979 220 LRSGRIALRKALE------------DGVKVGLGTdGAGSGNSLNMLEELRLALElqfdpEGGLSPLEALRMATINPAKAL 287
|
330 340
....*....|....*....|.
gi 1995764522 340 GMDHLLGSLAPGKRANIIALD 360
Cdd:pfam01979 288 GLDDKVGSIEVGKDADLVVVD 308
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| NagA |
COG1820 |
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism]; |
4-373 |
1.44e-167 |
|
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism];
Pssm-ID: 441425 [Multi-domain] Cd Length: 373 Bit Score: 472.66 E-value: 1.44e-167
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995764522 4 LLRARRLLTGQGWLDDHQLRMDRGVITAIEP-IPAGINTREAD--LLCPAYIDIHVHGGAGVDVMDDAPDVLDRLAMHKA 80
Cdd:COG1820 1 AITNARIFTGDGVLEDGALLIEDGRIAAIGPgAEPDAEVIDLGggYLAPGFIDLHVHGGGGVDFMDGTPEALRTIARAHA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995764522 81 REGVGAFLPTTVTAPLEAIHGALRRIARRCHvGGPGAQVLGSYLEGPYFTPQNKGAHPQELFRELDLAELDDLIAVSQNT 160
Cdd:COG1820 81 RHGTTSFLPTTITAPPEDLLRALAAIAEAIE-QGGGAGILGIHLEGPFLSPEKKGAHPPEYIRPPDPEELDRLLEAAGGL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995764522 161 LRVVALAPEKAEALKAIHHLKQKGIRVMLGHSAATYAQTLAAFDAGAAGLVHCYNGMTGLHHREPGMVGAGLTDPRAWLE 240
Cdd:COG1820 160 IKLVTLAPELPGALEFIRYLVEAGVVVSLGHTDATYEQARAAFEAGATHVTHLFNAMSPLHHREPGVVGAALDDDDVYAE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995764522 241 LIADGHHVHPGAMRLCC-CCAKDRTVLITDAMQAAGMPDGGYTLCGESVEMQGGVVRTASGGLAGSTLALDAAVRNMVEH 319
Cdd:COG1820 240 LIADGIHVHPAAVRLALrAKGPDRLILVTDAMAAAGLPDGEYELGGLEVTVKDGVARLADGTLAGSTLTMDDAVRNLVEW 319
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 1995764522 320 TGVAPEQAIHMASLHPARLLGMDHLLGSLAPGKRANIIALDAGLHLRQIWIQGQ 373
Cdd:COG1820 320 TGLPLEEAVRMASLNPARALGLDDRKGSIAPGKDADLVVLDDDLNVRATWVGGE 373
|
|
| NagA |
cd00854 |
N-acetylglucosamine-6-phosphate deacetylase, NagA, catalyzes the hydrolysis of the N-acetyl ... |
4-372 |
6.27e-161 |
|
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: 455.88 E-value: 6.27e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995764522 4 LLRARRLLTGqGWLDDHQLRMDRGVITAIEPIPAGINTREA-----DLLCPAYIDIHVHGGAGVDVMDDAPDVLDRLAMH 78
Cdd:cd00854 2 IIKNARILTP-GGLEDGAVLVEDGKIVAIGPEDELEEADEIidlkgQYLVPGFIDIHIHGGGGADFMDGTAEALKTIAEA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995764522 79 KAREGVGAFLPTTVTAPLEAIHGALRRIARRCHvGGPGAQVLGSYLEGPYFTPQNKGAHPQELFRELDLAELDDLIAVSQ 158
Cdd:cd00854 81 LAKHGTTSFLPTTVTAPPEEIAKALAAIAEAIA-EGQGAEILGIHLEGPFISPEKKGAHPPEYLRAPDPEELKKWLEAAG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995764522 159 NTLRVVALAPEKAEALKAIHHLKQKGIRVMLGHSAATYAQTLAAFDAGAAGLVHCYNGMTGLHHREPGMVGAGLTDPRAW 238
Cdd:cd00854 160 GLIKLVTLAPELDGALELIRYLVERGIIVSIGHSDATYEQAVAAFEAGATHVTHLFNAMSPLHHREPGVVGAALSDDDVY 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995764522 239 LELIADGHHVHPGAMRLCCCCA-KDRTVLITDAMQAAGMPDGGYTLCGESVEMQGGVVRTASGGLAGSTLALDAAVRNMV 317
Cdd:cd00854 240 AELIADGIHVHPAAVRLAYRAKgADKIVLVTDAMAAAGLPDGEYELGGQTVTVKDGVARLADGTLAGSTLTMDQAVRNMV 319
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 1995764522 318 EHTGVAPEQAIHMASLHPARLLGMDHLLGSLAPGKRANIIALDAGLHLRQIWIQG 372
Cdd:cd00854 320 KWGGCPLEEAVRMASLNPAKLLGLDDRKGSLKPGKDADLVVLDDDLNVKATWING 374
|
|
| nagA |
TIGR00221 |
N-acetylglucosamine-6-phosphate deacetylase; [Central intermediary metabolism, Amino sugars] |
1-373 |
5.83e-93 |
|
N-acetylglucosamine-6-phosphate deacetylase; [Central intermediary metabolism, Amino sugars]
Pssm-ID: 272968 Cd Length: 380 Bit Score: 283.26 E-value: 5.83e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995764522 1 MSQLLRARRLLTGQGWLDDHQLRMDRGVITAI---EPIPAGINTRE--ADLLCPAYIDIHVHGGAGVDVMDDAPDVLDRL 75
Cdd:TIGR00221 3 ESYLLKDIAIVTGNEVIDNGAVGINDGKISTVsteAELEPEIKEIDlpGNVLTPGFIDIHIHGCGGVDTNDASFETLEIM 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995764522 76 AMHKAREGVGAFLPTTVTAPLEAIHGALRrIARRCHVGGPGAQVLGSYLEGPYFTPQNKGAHPQELFRELDLAELDDLIA 155
Cdd:TIGR00221 83 SERLPKSGCTSFLPTLITQPDENIKQAVK-NMREYLAKEKNAQALGLHLEGPFLSPEKKGAHPPEYIREPDVELFKKFLC 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995764522 156 VSQNTLRVVALAPEKAEALKAIHHLKQKGIRVMLGHSAATYAQTLAAFDAGAAGLVHCYNGMTGLHHREPGMVGAGLTDP 235
Cdd:TIGR00221 162 EAGGVITKVTLAPEEDQHFELIRHLKDAGIIVSAGHTNATYELAKAAFKAGATHATHLYNAMSPIHHREPGVIGAVLDHD 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995764522 236 RAWLELIADGHHVHPGAMRLCCCCAKD-RTVLITDAMQAAGMPDGGYTLCGESVEMQGGVVRTASGGLAGSTLALDAAVR 314
Cdd:TIGR00221 242 DVYTEIIADGIHIHPLNIRLAKKLKGDsKLCLVTDSMAAAGAKDGVFIFGGKTVYIREGTCLDSNGTLAGSSLTMIEGAR 321
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 1995764522 315 NMVEHTGVAPEQAIHMASLHPARLLGMDHLLGSLAPGKRANIIALDAGLHLRQIWIQGQ 373
Cdd:TIGR00221 322 NLVEFTNISLTDAARMSSLNPARALGIDDRLGSVTVGKDANLVVFTPDFEVILTIVNGN 380
|
|
| nagA |
PRK11170 |
N-acetylglucosamine-6-phosphate deacetylase; Provisional |
9-360 |
5.14e-82 |
|
N-acetylglucosamine-6-phosphate deacetylase; Provisional
Pssm-ID: 183010 Cd Length: 382 Bit Score: 255.28 E-value: 5.14e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995764522 9 RLLTGQGWLDDHQLRMDRGVITAIEPI---PAGINTREAD--LLCPAYIDIHVHGGAGVDVMDDAPDV-LDRLA-MHKA- 80
Cdd:PRK11170 8 RIYTGHEVLDDHAVVIADGLIEAVCPVaelPPGIEQRDLNgaILSPGFIDLQLNGCGGVQFNDTAEAIsVETLEiMQKAn 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995764522 81 -REGVGAFLPTTVTAPLEAIHGALRrIARRCHVGGPGaQVLGSYLEGPYFTPQNKGAHPQELFRELDlAELDDLIAVSQN 159
Cdd:PRK11170 88 eKSGCTSFLPTLITSSDELMKQAVR-VMREYLAKHPN-QALGLHLEGPYLNLVKKGTHNPEFIRKPD-AEMVDFLCENAD 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995764522 160 TLRVVALAPEKAEAlKAIHHLKQKGIRVMLGHSAATYAQTLAAFDAGAAGLVHCYNGMTGLHHREPGMVGAGLTDPRAWL 239
Cdd:PRK11170 165 VITKVTLAPEMVDA-EVIRKLVEAGIVVSAGHSNATYEEAKAGFRAGITFATHLYNAMPYITGREPGLVGAILDEPDVYC 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995764522 240 ELIADGHHVHPGAMRLCCCCAKDRTVLITDAMQAAGMPDGGYTLCGESVEMQGGVVRTASGGLAGSTLALDAAVRNMVEH 319
Cdd:PRK11170 244 GIIADGLHVDYANIRNAKRLKGDKLCLVTDATAPAGANIEQFIFAGKTIYYRDGLCVDENGTLSGSALTMIEAVRNLVEH 323
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 1995764522 320 TGVAPEQAIHMASLHPARLLGMDHLLGSLAPGKRANIIALD 360
Cdd:PRK11170 324 VGIALDEALRMATLYPARAIGVDKRLGSIEAGKVANLTAFT 364
|
|
| Amidohydro_1 |
pfam01979 |
Amidohydrolase family; This family of enzymes are a a large metal dependent hydrolase ... |
46-360 |
4.00e-16 |
|
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: 78.31 E-value: 4.00e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995764522 46 LLCPAYIDIHVHGGAGVDVMDDAPDvldRLAMHKAREGVGAFLP---TTVTAPLEAIHGALRRIARRCHvggpgAQVLGS 122
Cdd:pfam01979 1 IVLPGLIDAHVHLEMGLLRGIPVPP---EFAYEALRLGITTMLKsgtTTVLDMGATTSTGIEALLEAAE-----ELPLGL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995764522 123 YLEGPYFTPQNKGAHPQELFRELDLAELDDLIAVSQNTLRVVALAPE------KAEALKAIHHLKQKGIRVM--LGHSAA 194
Cdd:pfam01979 73 RFLGPGCSLDTDGELEGRKALREKLKAGAEFIKGMADGVVFVGLAPHgaptfsDDELKAALEEAKKYGLPVAihALETKG 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995764522 195 TYAQTLAAFDAGAaglVHcyngMTGLHHREPGMvgagltDPRAWLELIADGHHVHPGAMRLC---------CCCAKDRTV 265
Cdd:pfam01979 153 EVEDAIAAFGGGI---EH----GTHLEVAESGG------LLDIIKLILAHGVHLSPTEANLLaehlkgagvAHCPFSNSK 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995764522 266 LITDAMQAAGMPDggytlcgesvemQGGVVRTAS-GGLAGSTLALDAAVRNMVE-----HTGVAPEQAIHMASLHPARLL 339
Cdd:pfam01979 220 LRSGRIALRKALE------------DGVKVGLGTdGAGSGNSLNMLEELRLALElqfdpEGGLSPLEALRMATINPAKAL 287
|
330 340
....*....|....*....|.
gi 1995764522 340 GMDHLLGSLAPGKRANIIALD 360
Cdd:pfam01979 288 GLDDKVGSIEVGKDADLVVVD 308
|
|
| HutI |
COG1228 |
Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport ... |
4-373 |
2.50e-11 |
|
Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440841 [Multi-domain] Cd Length: 386 Bit Score: 64.60 E-value: 2.50e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995764522 4 LLRARRLLTG--QGWLDDHQLRMDRGVITAIEP-----IPAGINTREAD--LLCPAYIDIHVHGGAGVDVMDDA----PD 70
Cdd:COG1228 11 LITNATLVDGtgGGVIENGTVLVEDGKIAAVGPaadlaVPAGAEVIDATgkTVLPGLIDAHTHLGLGGGRAVEFeaggGI 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995764522 71 VLDRLAMHKAREGVGAFLP---TTVTAPLEAIHGALRRIArrchvGGPGAQVLGS--YLEGPYFTpQNKGAH---PQELF 142
Cdd:COG1228 91 TPTVDLVNPADKRLRRALAagvTTVRDLPGGPLGLRDAII-----AGESKLLPGPrvLAAGPALS-LTGGAHargPEEAR 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995764522 143 RELD--LAELDDLIAVsQNTLRVVALAPEkaEALKAIHHLKQKGIRVMlGHsAATYAQTLAAFDAGAAGLVHCY----NG 216
Cdd:COG1228 165 AALRelLAEGADYIKV-FAEGGAPDFSLE--ELRAILEAAHALGLPVA-AH-AHQADDIRLAVEAGVDSIEHGTylddEV 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995764522 217 MTGLHHREPGMVGAGLTDPRAWLEliADGHHVHPGAMRlccccAKDRTVLITDAMQAAGMP-----DGGytlcgesvemq 291
Cdd:COG1228 240 ADLLAEAGTVVLVPTLSLFLALLE--GAAAPVAAKARK-----VREAALANARRLHDAGVPvalgtDAG----------- 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995764522 292 ggvvrtaSGGLAGSTLALDAAvrNMVEHtGVAPEQAIHMASLHPARLLGMDHLLGSLAPGKRANIIALDAG--------L 363
Cdd:COG1228 302 -------VGVPPGRSLHRELA--LAVEA-GLTPEEALRAATINAAKALGLDDDVGSLEPGKLADLVLLDGDplediaylE 371
|
410
....*....|
gi 1995764522 364 HLRQIWIQGQ 373
Cdd:COG1228 372 DVRAVMKDGR 381
|
|
| AdeC |
COG1001 |
Adenine deaminase [Nucleotide transport and metabolism]; |
309-373 |
1.29e-10 |
|
Adenine deaminase [Nucleotide transport and metabolism];
Pssm-ID: 440625 [Multi-domain] Cd Length: 559 Bit Score: 62.81 E-value: 1.29e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1995764522 309 LDAAVRNMVEHtGVAPEQAIHMASLHPARLLGMDHlLGSLAPGKRANIIALD--AGLHLRQIWIQGQ 373
Cdd:COG1001 272 IDHVVRRAIEL-GLDPVTAIQMATLNAAEHFGLKD-LGAIAPGRRADIVLLDdlEDFKVEKVYADGK 336
|
|
| AdeC |
cd01295 |
Adenine deaminase (AdeC) directly deaminates adenine to form hypoxanthine. This reaction is ... |
309-360 |
6.75e-08 |
|
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: 54.15 E-value: 6.75e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 1995764522 309 LDAAVRNMVEHtGVAPEQAIHMASLHPARLLGMDHlLGSLAPGKRANIIALD 360
Cdd:cd01295 223 LDYIVRRAIEA-GIPPEDAIQMATINPAECYGLHD-LGAIAPGRIADIVILD 272
|
|
| SsnA |
COG0402 |
Cytosine/adenosine deaminase or related metal-dependent hydrolase [Nucleotide transport and ... |
320-361 |
5.29e-07 |
|
Cytosine/adenosine deaminase or related metal-dependent hydrolase [Nucleotide transport and metabolism, General function prediction only]; Cytosine/adenosine deaminase or related metal-dependent hydrolase is part of the Pathway/BioSystem: Pyrimidine salvage
Pssm-ID: 440171 [Multi-domain] Cd Length: 416 Bit Score: 51.37 E-value: 5.29e-07
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 1995764522 320 TGVAPEQAIHMASLHPARLLGMDHLLGSLAPGKRANIIALDA 361
Cdd:COG0402 338 TALSAREALEMATLGGARALGLDDEIGSLEPGKRADLVVLDL 379
|
|
| PRK09045 |
PRK09045 |
TRZ/ATZ family hydrolase; |
296-360 |
7.44e-07 |
|
TRZ/ATZ family hydrolase;
Pssm-ID: 236366 [Multi-domain] Cd Length: 443 Bit Score: 50.68 E-value: 7.44e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1995764522 296 RTAS---GGLAGSTLALDAAvrnmvehtgvapeQAIHMASLHPARLLGMDHLLGSLAPGKRANIIALD 360
Cdd:PRK09045 324 RTAAllaKAVAGDATALPAH-------------TALRMATLNGARALGLDDEIGSLEPGKQADLVAVD 378
|
|
| Met_dep_hydrolase_A |
cd01299 |
Metallo-dependent hydrolases, subgroup A is part of the superfamily of metallo-dependent ... |
316-361 |
1.05e-06 |
|
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: 49.98 E-value: 1.05e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 1995764522 316 MVEHtGVAPEQAIHMASLHPARLLGMDHLLGSLAPGKRANIIALDA 361
Cdd:cd01299 289 LVKA-GGTPAEALRAATANAAELLGLSDELGVIEAGKLADLLVVDG 333
|
|
| PRK08204 |
PRK08204 |
hypothetical protein; Provisional |
316-361 |
1.07e-05 |
|
hypothetical protein; Provisional
Pssm-ID: 181288 [Multi-domain] Cd Length: 449 Bit Score: 47.30 E-value: 1.07e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 1995764522 316 MVEHTGVAPEQAIHMASLHPARLLGMDHLLGSLAPGKRANIIALDA 361
Cdd:PRK08204 336 PPPRLTLTARQVLEWATIEGARALGLEDRIGSLTPGKQADLVLIDA 381
|
|
| PRK15446 |
PRK15446 |
phosphonate metabolism protein PhnM; Provisional |
309-373 |
1.24e-05 |
|
phosphonate metabolism protein PhnM; Provisional
Pssm-ID: 237967 [Multi-domain] Cd Length: 383 Bit Score: 46.71 E-value: 1.24e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1995764522 309 LDAAVRnMVEHTGVAPEQAIHMASLHPARLLGMDHlLGSLAPGKRANIIALDAGLHL---RQIWIQGQ 373
Cdd:PRK15446 312 LDAAFR-LADDGGLDLPQAVALVTANPARAAGLDD-RGEIAPGKRADLVRVRRAGGLpvvRAVWRGGR 377
|
|
| YtcJ |
COG1574 |
Predicted amidohydrolase YtcJ [General function prediction only]; |
307-361 |
1.34e-05 |
|
Predicted amidohydrolase YtcJ [General function prediction only];
Pssm-ID: 441182 [Multi-domain] Cd Length: 535 Bit Score: 47.10 E-value: 1.34e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1995764522 307 LALDAAV-RNMVEHTGVAPEQ------AIHMASLHPARLLGMDHLLGSLAPGKRANIIALDA 361
Cdd:COG1574 445 LGIYAAVtRRTPSGRGLGPEErltveeALRAYTIGAAYAAFEEDEKGSLEPGKLADFVVLDR 506
|
|
| PRK07228 |
PRK07228 |
5'-deoxyadenosine deaminase; |
320-364 |
7.41e-05 |
|
5'-deoxyadenosine deaminase;
Pssm-ID: 180895 [Multi-domain] Cd Length: 445 Bit Score: 44.61 E-value: 7.41e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 1995764522 320 TGVAPEQAIHMASLHPARLLGMDHLLGSLAPGKRANIIALDA-GLH 364
Cdd:PRK07228 335 TAMPARTVFEMATLGGAKAAGFEDEIGSLEEGKKADLAILDLdGLH 380
|
|
| ATZ_TRZ_like |
cd01298 |
TRZ/ATZ family contains enzymes from the atrazine degradation pathway and related hydrolases. ... |
320-360 |
1.00e-04 |
|
TRZ/ATZ family contains enzymes from the atrazine degradation pathway and related hydrolases. Atrazine, a chlorinated herbizide, can be catabolized by a variety of different bacteria. The first three steps of the atrazine dehalogenation pathway are catalyzed by atrazine chlorohydrolase (AtzA), hydroxyatrazine ethylaminohydrolase (AtzB), and N-isopropylammelide N-isopropylaminohydrolase (AtzC). All three enzymes belong to the superfamily of metal dependent hydrolases. AtzA and AtzB, beside other related enzymes are represented in this CD.
Pssm-ID: 238623 [Multi-domain] Cd Length: 411 Bit Score: 44.12 E-value: 1.00e-04
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 1995764522 320 TGVAPEQAIHMASLHPARLLGMDHLlGSLAPGKRANIIALD 360
Cdd:cd01298 330 TALPAEEALEMATIGGAKALGLDEI-GSLEVGKKADLILID 369
|
|
| Isoaspartyl-dipeptidase |
cd01308 |
Isoaspartyl dipeptidase hydrolyzes the beta-L-isoaspartyl linkages in dipeptides, as part of ... |
303-375 |
1.02e-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: 1.02e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1995764522 303 AGSTLALDAAVRNMVEHTGVAPEQAIHMASLHPARLLGMDHlLGSLAPGKRANIIALDAGLHLRQIWIQGQAL 375
Cdd:cd01308 303 VGSVDTLLREVREAVKCGDIPLEVALRVITSNVARILKLRK-KGEIQPGFDADLVILDKDLDINSVIAKGQIM 374
|
|
| YtcJ_like |
cd01300 |
YtcJ_like metal dependent amidohydrolases. YtcJ is a Bacillus subtilis ORF of unknown function. ... |
290-357 |
1.61e-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: 43.45 E-value: 1.61e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1995764522 290 MQGGVVRTASGGLAGSTlaldaavrnmvEHTGVAPEQAIHMASLHPARLLGMDHLLGSLAPGKRANII 357
Cdd:cd01300 422 IWAAVTRKTPGGGVLGN-----------PEERLSLEEALRAYTIGAAYAIGEEDEKGSLEPGKLADFV 478
|
|
| Met_dep_hydrolase_C |
cd01309 |
Metallo-dependent hydrolases, subgroup C is part of the superfamily of metallo-dependent ... |
321-372 |
1.63e-04 |
|
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: 43.07 E-value: 1.63e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1995764522 321 GVAPEQAIHMASLHPARLLGMDHLLGSLAPGKRANIIA-----LDAGLHLRQIWIQG 372
Cdd:cd01309 299 GLSYEEALKAITINPAKILGIEDRVGSLEPGKDADLVVwngdpLEPTSKPEQVYIDG 355
|
|
| PRK10027 |
PRK10027 |
cryptic adenine deaminase; Provisional |
309-376 |
1.89e-04 |
|
cryptic adenine deaminase; Provisional
Pssm-ID: 182201 [Multi-domain] Cd Length: 588 Bit Score: 43.28 E-value: 1.89e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995764522 309 LDAAVRNMVEHTGVAPEQAIHMASLHPARLLGMDHLlGSLAPGKRANIIALD--AGLHLRQIWIQGQALS 376
Cdd:PRK10027 297 IDALIRRLIEQHNVPLHVAYRVASWSTARHFGLNHL-GLLAPGKQADIVLLSdaRKVTVQQVLVKGEPID 365
|
|
| PhnM |
cd01306 |
PhnM is believed to be a subunit of the membrane associated C-P lyase complex. C-P lyase is ... |
325-372 |
1.96e-04 |
|
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: 43.04 E-value: 1.96e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 1995764522 325 EQAIHMASLHPARLLGMdHLLGSLAPGKRANIIA--LDAGL-HLRQIWIQG 372
Cdd:cd01306 276 PEAVALVSANPARAVGL-TDRGSIAPGKRADLILvdDMDGVpVVRTVWRGG 325
|
|
| GDEase |
cd01303 |
Guanine deaminase (GDEase). Guanine deaminase is an aminohydrolase responsible for the ... |
299-360 |
3.11e-04 |
|
Guanine deaminase (GDEase). Guanine deaminase is an aminohydrolase responsible for the conversion of guanine to xanthine and ammonia, the first step to utilize guanine as a nitrogen source. This reaction also removes the guanine base from the pool and therefore can play a role in the regulation of cellular GTP and the guanylate nucleotide pool.
Pssm-ID: 238628 [Multi-domain] Cd Length: 429 Bit Score: 42.65 E-value: 3.11e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995764522 299 SGGLAGSTL-ALDAAV-------RNMVEHTGVAPEQAIHMASLHPARLLGMDHLLGSLAPGKRANIIALD 360
Cdd:cd01303 320 GGGTSFSMLdTLRQAYkvsrllgYELGGHAKLSPAEAFYLATLGGAEALGLDDKIGNFEVGKEFDAVVID 389
|
|
| Amidohydro_3 |
pfam07969 |
Amidohydrolase family; |
325-361 |
4.72e-04 |
|
Amidohydrolase family;
Pssm-ID: 400360 [Multi-domain] Cd Length: 464 Bit Score: 42.13 E-value: 4.72e-04
10 20 30
....*....|....*....|....*....|....*..
gi 1995764522 325 EQAIHMASLHPARLLGMDHLLGSLAPGKRANIIALDA 361
Cdd:pfam07969 402 EEALALYTSGPAKALGLEDRKGTLGVGKDADLVVLDD 438
|
|
| PRK09228 |
PRK09228 |
guanine deaminase; Provisional |
324-361 |
6.90e-04 |
|
guanine deaminase; Provisional
Pssm-ID: 236419 [Multi-domain] Cd Length: 433 Bit Score: 41.33 E-value: 6.90e-04
10 20 30
....*....|....*....|....*....|....*...
gi 1995764522 324 PEQAIHMASLHPARLLGMDHLLGSLAPGKRANIIALDA 361
Cdd:PRK09228 350 PFQAFYLATLGGARALGLDDRIGNLAPGKEADFVVLDP 387
|
|
| Imidazolone-5PH |
cd01296 |
Imidazolonepropionase/imidazolone-5-propionate hydrolase (Imidazolone-5PH) catalyzes the third ... |
307-361 |
3.88e-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: 38.78 E-value: 3.88e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1995764522 307 LALDAAVRNMvehtGVAPEQAIHMASLHPARLLGMDHLLGSLAPGKRANIIALDA 361
Cdd:cd01296 299 LVMHLACRLM----RMTPEEALTAATINAAAALGLGETVGSLEVGKQADLVILDA 349
|
|
| |
