|
Name |
Accession |
Description |
Interval |
E-value |
| NagA |
COG1820 |
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism]; |
4-379 |
8.26e-165 |
|
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism];
Pssm-ID: 441425 [Multi-domain] Cd Length: 373 Bit Score: 466.11 E-value: 8.26e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309388644 4 YIKSKKIYKEDEIILDHALKIEGEKISGFVKSSELssNDIVVDCGNKIIIPALIDLHIHGAVGKDVMDGDYESLNDISKY 83
Cdd:COG1820 1 AITNARIFTGDGVLEDGALLIEDGRIAAIGPGAEP--DAEVIDLGGGYLAPGFIDLHVHGGGGVDFMDGTPEALRTIARA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309388644 84 LASIGVSRFLATTLTAPISKIENALKNIRESQKRGlAGAKIIGTYLEGPYLSKEKKGAHPEEYLKEPNIKEIKKMIDISG 163
Cdd:COG1820 79 HARHGTTSFLPTTITAPPEDLLRALAAIAEAIEQG-GGAGILGIHLEGPFLSPEKKGAHPPEYIRPPDPEELDRLLEAAG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309388644 164 NNIKILALAPEKNESQKVIKFLCDKGIIAALAHTNADYSVIEESVKNGAFLATHTFNGMKGLHHRNPGAIGGIMAFDEIY 243
Cdd:COG1820 158 GLIKLVTLAPELPGALEFIRYLVEAGVVVSLGHTDATYEQARAAFEAGATHVTHLFNAMSPLHHREPGVVGAALDDDDVY 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309388644 244 SELIADKIHVHPAVMKILYKVKGLEKIALISDCMRAGGIEDGEYKLGEIDVNVKNATARTRSGSLAGSTLKIKDALLNIK 323
Cdd:COG1820 238 AELIADGIHVHPAAVRLALRAKGPDRLILVTDAMAAAGLPDGEYELGGLEVTVKDGVARLADGTLAGSTLTMDDAVRNLV 317
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 309388644 324 EAVDIELFEAVKMASLVPAKILGLDSELGSIKKFKKADITVIDSEMNIYLTAVDGK 379
Cdd:COG1820 318 EWTGLPLEEAVRMASLNPARALGLDDRKGSIAPGKDADLVVLDDDLNVRATWVGGE 373
|
|
| NagA |
cd00854 |
N-acetylglucosamine-6-phosphate deacetylase, NagA, catalyzes the hydrolysis of the N-acetyl ... |
3-378 |
1.12e-153 |
|
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: 438.17 E-value: 1.12e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309388644 3 YYIKSKKIYKEDEIIlDHALKIEGEKISGFVKSSELSSNDIVVDCGNKIIIPALIDLHIHGAVGKDVMDGDYESLNDISK 82
Cdd:cd00854 1 LIIKNARILTPGGLE-DGAVLVEDGKIVAIGPEDELEEADEIIDLKGQYLVPGFIDIHIHGGGGADFMDGTAEALKTIAE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309388644 83 YLASIGVSRFLATTLTAPISKIENALKNIRESQKRGLaGAKIIGTYLEGPYLSKEKKGAHPEEYLKEPNIKEIKKMIDIS 162
Cdd:cd00854 80 ALAKHGTTSFLPTTVTAPPEEIAKALAAIAEAIAEGQ-GAEILGIHLEGPFISPEKKGAHPPEYLRAPDPEELKKWLEAA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309388644 163 GNNIKILALAPEKNESQKVIKFLCDKGIIAALAHTNADYSVIEESVKNGAFLATHTFNGMKGLHHRNPGAIGGIMAFDEI 242
Cdd:cd00854 159 GGLIKLVTLAPELDGALELIRYLVERGIIVSIGHSDATYEQAVAAFEAGATHVTHLFNAMSPLHHREPGVVGAALSDDDV 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309388644 243 YSELIADKIHVHPAVMKILYKVKGLEKIALISDCMRAGGIEDGEYKLGEIDVNVKNATARTRSGSLAGSTLKIKDALLNI 322
Cdd:cd00854 239 YAELIADGIHVHPAAVRLAYRAKGADKIVLVTDAMAAAGLPDGEYELGGQTVTVKDGVARLADGTLAGSTLTMDQAVRNM 318
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 309388644 323 KEAVDIELFEAVKMASLVPAKILGLDSELGSIKKFKKADITVIDSEMNIYLTAVDG 378
Cdd:cd00854 319 VKWGGCPLEEAVRMASLNPAKLLGLDDRKGSLKPGKDADLVVLDDDLNVKATWING 374
|
|
| nagA |
TIGR00221 |
N-acetylglucosamine-6-phosphate deacetylase; [Central intermediary metabolism, Amino sugars] |
1-379 |
4.01e-104 |
|
N-acetylglucosamine-6-phosphate deacetylase; [Central intermediary metabolism, Amino sugars]
Pssm-ID: 272968 Cd Length: 380 Bit Score: 312.15 E-value: 4.01e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309388644 1 MSYYIKSKKIYKEDEIILDHALKIEGEKISGFVKSSELSSNDIVVDCGNKIIIPALIDLHIHGAVGKDVMDGDYESLNDI 80
Cdd:TIGR00221 3 ESYLLKDIAIVTGNEVIDNGAVGINDGKISTVSTEAELEPEIKEIDLPGNVLTPGFIDIHIHGCGGVDTNDASFETLEIM 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309388644 81 SKYLASIGVSRFLATTLTAPISKIENALKNIRESQKRGlAGAKIIGTYLEGPYLSKEKKGAHPEEYLKEPNIKEIKKMID 160
Cdd:TIGR00221 83 SERLPKSGCTSFLPTLITQPDENIKQAVKNMREYLAKE-KNAQALGLHLEGPFLSPEKKGAHPPEYIREPDVELFKKFLC 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309388644 161 ISGNNIKILALAPEKNESQKVIKFLCDKGIIAALAHTNADYSVIEESVKNGAFLATHTFNGMKGLHHRNPGAIGGIMAFD 240
Cdd:TIGR00221 162 EAGGVITKVTLAPEEDQHFELIRHLKDAGIIVSAGHTNATYELAKAAFKAGATHATHLYNAMSPIHHREPGVIGAVLDHD 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309388644 241 EIYSELIADKIHVHPAVMKILYKVKGLEKIALISDCMRAGGIEDGEYKLGEIDVNVKNATARTRSGSLAGSTLKIKDALL 320
Cdd:TIGR00221 242 DVYTEIIADGIHIHPLNIRLAKKLKGDSKLCLVTDSMAAAGAKDGVFIFGGKTVYIREGTCLDSNGTLAGSSLTMIEGAR 321
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 309388644 321 NIKEAVDIELFEAVKMASLVPAKILGLDSELGSIKKFKKADITVIDSEMNIYLTAVDGK 379
Cdd:TIGR00221 322 NLVEFTNISLTDAARMSSLNPARALGIDDRLGSVTVGKDANLVVFTPDFEVILTIVNGN 380
|
|
| nagA |
PRK11170 |
N-acetylglucosamine-6-phosphate deacetylase; Provisional |
9-381 |
1.08e-68 |
|
N-acetylglucosamine-6-phosphate deacetylase; Provisional
Pssm-ID: 183010 Cd Length: 382 Bit Score: 221.39 E-value: 1.08e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309388644 9 KIYKEDEIILDHALKIEGEKISGFVKSSELSSNDIVVDCGNKIIIPALIDLHIHGAVGkdVMDGDyeSLNDISKYLASI- 87
Cdd:PRK11170 8 RIYTGHEVLDDHAVVIADGLIEAVCPVAELPPGIEQRDLNGAILSPGFIDLQLNGCGG--VQFND--TAEAISVETLEIm 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309388644 88 -------GVSRFLATTLTAPISKIENALKNIRESQKRGLAGAkiIGTYLEGPYLSKEKKGAHPEEYLKEPNikeiKKMID 160
Cdd:PRK11170 84 qkaneksGCTSFLPTLITSSDELMKQAVRVMREYLAKHPNQA--LGLHLEGPYLNLVKKGTHNPEFIRKPD----AEMVD 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309388644 161 ISGNN---IKILALAPEKNEsQKVIKFLCDKGIIAALAHTNADYSVIEESVKNGAFLATHTFNGMKGLHHRNPGAIGGIM 237
Cdd:PRK11170 158 FLCENadvITKVTLAPEMVD-AEVIRKLVEAGIVVSAGHSNATYEEAKAGFRAGITFATHLYNAMPYITGREPGLVGAIL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309388644 238 AFDEIYSELIADKIHVHPAVMKILYKVKGlEKIALISDCMRAGGIEDGEYKLGEIDVNVKNATARTRSGSLAGSTLKIKD 317
Cdd:PRK11170 237 DEPDVYCGIIADGLHVDYANIRNAKRLKG-DKLCLVTDATAPAGANIEQFIFAGKTIYYRDGLCVDENGTLSGSALTMIE 315
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 309388644 318 ALLNIKEAVDIELFEAVKMASLVPAKILGLDSELGSIKKFKKADITVIDSEMNIYLTAVDGKIV 381
Cdd:PRK11170 316 AVRNLVEHVGIALDEALRMATLYPARAIGVDKRLGSIEAGKVANLTAFTRDFKITKTIVNGNEV 379
|
|
| Amidohydro_1 |
pfam01979 |
Amidohydrolase family; This family of enzymes are a a large metal dependent hydrolase ... |
51-381 |
1.29e-17 |
|
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: 82.93 E-value: 1.29e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309388644 51 IIIPALIDLHIHGAVGkdVMDGDYESLnDISKYLASIGVSRFLA--TTLTAPISKIEN-ALKNIRESqkrglAGAKIIGT 127
Cdd:pfam01979 1 IVLPGLIDAHVHLEMG--LLRGIPVPP-EFAYEALRLGITTMLKsgTTTVLDMGATTStGIEALLEA-----AEELPLGL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309388644 128 YLEGPYLSKEKKG-AHPEEYLKEPNIKEIKKMIDISGNNIKI-LALAPEKNESQKVIKFL------CDKGIIAALAHTNA 199
Cdd:pfam01979 73 RFLGPGCSLDTDGeLEGRKALREKLKAGAEFIKGMADGVVFVgLAPHGAPTFSDDELKAAleeakkYGLPVAIHALETKG 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309388644 200 DYSVIEESVKNGAFLATHTFNGMKGlhhrnpgaiggimAFDEIYSELIADKIHVHPAVMKILYKVKGLEKIALI--SDCM 277
Cdd:pfam01979 153 EVEDAIAAFGGGIEHGTHLEVAESG-------------GLLDIIKLILAHGVHLSPTEANLLAEHLKGAGVAHCpfSNSK 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309388644 278 RAGGIEDGEyKLGEIDVNVKNATARTRSGSLAGSTLKIKDALLNIKEA-VDIELFEAVKMASLVPAKILGLDSELGSIKK 356
Cdd:pfam01979 220 LRSGRIALR-KALEDGVKVGLGTDGAGSGNSLNMLEELRLALELQFDPeGGLSPLEALRMATINPAKALGLDDKVGSIEV 298
|
330 340 350
....*....|....*....|....*....|....*.
gi 309388644 357 FKKADITVID-----------SEMNIYLTAVDGKIV 381
Cdd:pfam01979 299 GKDADLVVVDldplaaffglkPDGNVKKVIVKGKIV 334
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| NagA |
COG1820 |
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism]; |
4-379 |
8.26e-165 |
|
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism];
Pssm-ID: 441425 [Multi-domain] Cd Length: 373 Bit Score: 466.11 E-value: 8.26e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309388644 4 YIKSKKIYKEDEIILDHALKIEGEKISGFVKSSELssNDIVVDCGNKIIIPALIDLHIHGAVGKDVMDGDYESLNDISKY 83
Cdd:COG1820 1 AITNARIFTGDGVLEDGALLIEDGRIAAIGPGAEP--DAEVIDLGGGYLAPGFIDLHVHGGGGVDFMDGTPEALRTIARA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309388644 84 LASIGVSRFLATTLTAPISKIENALKNIRESQKRGlAGAKIIGTYLEGPYLSKEKKGAHPEEYLKEPNIKEIKKMIDISG 163
Cdd:COG1820 79 HARHGTTSFLPTTITAPPEDLLRALAAIAEAIEQG-GGAGILGIHLEGPFLSPEKKGAHPPEYIRPPDPEELDRLLEAAG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309388644 164 NNIKILALAPEKNESQKVIKFLCDKGIIAALAHTNADYSVIEESVKNGAFLATHTFNGMKGLHHRNPGAIGGIMAFDEIY 243
Cdd:COG1820 158 GLIKLVTLAPELPGALEFIRYLVEAGVVVSLGHTDATYEQARAAFEAGATHVTHLFNAMSPLHHREPGVVGAALDDDDVY 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309388644 244 SELIADKIHVHPAVMKILYKVKGLEKIALISDCMRAGGIEDGEYKLGEIDVNVKNATARTRSGSLAGSTLKIKDALLNIK 323
Cdd:COG1820 238 AELIADGIHVHPAAVRLALRAKGPDRLILVTDAMAAAGLPDGEYELGGLEVTVKDGVARLADGTLAGSTLTMDDAVRNLV 317
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 309388644 324 EAVDIELFEAVKMASLVPAKILGLDSELGSIKKFKKADITVIDSEMNIYLTAVDGK 379
Cdd:COG1820 318 EWTGLPLEEAVRMASLNPARALGLDDRKGSIAPGKDADLVVLDDDLNVRATWVGGE 373
|
|
| NagA |
cd00854 |
N-acetylglucosamine-6-phosphate deacetylase, NagA, catalyzes the hydrolysis of the N-acetyl ... |
3-378 |
1.12e-153 |
|
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: 438.17 E-value: 1.12e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309388644 3 YYIKSKKIYKEDEIIlDHALKIEGEKISGFVKSSELSSNDIVVDCGNKIIIPALIDLHIHGAVGKDVMDGDYESLNDISK 82
Cdd:cd00854 1 LIIKNARILTPGGLE-DGAVLVEDGKIVAIGPEDELEEADEIIDLKGQYLVPGFIDIHIHGGGGADFMDGTAEALKTIAE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309388644 83 YLASIGVSRFLATTLTAPISKIENALKNIRESQKRGLaGAKIIGTYLEGPYLSKEKKGAHPEEYLKEPNIKEIKKMIDIS 162
Cdd:cd00854 80 ALAKHGTTSFLPTTVTAPPEEIAKALAAIAEAIAEGQ-GAEILGIHLEGPFISPEKKGAHPPEYLRAPDPEELKKWLEAA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309388644 163 GNNIKILALAPEKNESQKVIKFLCDKGIIAALAHTNADYSVIEESVKNGAFLATHTFNGMKGLHHRNPGAIGGIMAFDEI 242
Cdd:cd00854 159 GGLIKLVTLAPELDGALELIRYLVERGIIVSIGHSDATYEQAVAAFEAGATHVTHLFNAMSPLHHREPGVVGAALSDDDV 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309388644 243 YSELIADKIHVHPAVMKILYKVKGLEKIALISDCMRAGGIEDGEYKLGEIDVNVKNATARTRSGSLAGSTLKIKDALLNI 322
Cdd:cd00854 239 YAELIADGIHVHPAAVRLAYRAKGADKIVLVTDAMAAAGLPDGEYELGGQTVTVKDGVARLADGTLAGSTLTMDQAVRNM 318
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 309388644 323 KEAVDIELFEAVKMASLVPAKILGLDSELGSIKKFKKADITVIDSEMNIYLTAVDG 378
Cdd:cd00854 319 VKWGGCPLEEAVRMASLNPAKLLGLDDRKGSLKPGKDADLVVLDDDLNVKATWING 374
|
|
| nagA |
TIGR00221 |
N-acetylglucosamine-6-phosphate deacetylase; [Central intermediary metabolism, Amino sugars] |
1-379 |
4.01e-104 |
|
N-acetylglucosamine-6-phosphate deacetylase; [Central intermediary metabolism, Amino sugars]
Pssm-ID: 272968 Cd Length: 380 Bit Score: 312.15 E-value: 4.01e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309388644 1 MSYYIKSKKIYKEDEIILDHALKIEGEKISGFVKSSELSSNDIVVDCGNKIIIPALIDLHIHGAVGKDVMDGDYESLNDI 80
Cdd:TIGR00221 3 ESYLLKDIAIVTGNEVIDNGAVGINDGKISTVSTEAELEPEIKEIDLPGNVLTPGFIDIHIHGCGGVDTNDASFETLEIM 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309388644 81 SKYLASIGVSRFLATTLTAPISKIENALKNIRESQKRGlAGAKIIGTYLEGPYLSKEKKGAHPEEYLKEPNIKEIKKMID 160
Cdd:TIGR00221 83 SERLPKSGCTSFLPTLITQPDENIKQAVKNMREYLAKE-KNAQALGLHLEGPFLSPEKKGAHPPEYIREPDVELFKKFLC 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309388644 161 ISGNNIKILALAPEKNESQKVIKFLCDKGIIAALAHTNADYSVIEESVKNGAFLATHTFNGMKGLHHRNPGAIGGIMAFD 240
Cdd:TIGR00221 162 EAGGVITKVTLAPEEDQHFELIRHLKDAGIIVSAGHTNATYELAKAAFKAGATHATHLYNAMSPIHHREPGVIGAVLDHD 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309388644 241 EIYSELIADKIHVHPAVMKILYKVKGLEKIALISDCMRAGGIEDGEYKLGEIDVNVKNATARTRSGSLAGSTLKIKDALL 320
Cdd:TIGR00221 242 DVYTEIIADGIHIHPLNIRLAKKLKGDSKLCLVTDSMAAAGAKDGVFIFGGKTVYIREGTCLDSNGTLAGSSLTMIEGAR 321
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 309388644 321 NIKEAVDIELFEAVKMASLVPAKILGLDSELGSIKKFKKADITVIDSEMNIYLTAVDGK 379
Cdd:TIGR00221 322 NLVEFTNISLTDAARMSSLNPARALGIDDRLGSVTVGKDANLVVFTPDFEVILTIVNGN 380
|
|
| nagA |
PRK11170 |
N-acetylglucosamine-6-phosphate deacetylase; Provisional |
9-381 |
1.08e-68 |
|
N-acetylglucosamine-6-phosphate deacetylase; Provisional
Pssm-ID: 183010 Cd Length: 382 Bit Score: 221.39 E-value: 1.08e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309388644 9 KIYKEDEIILDHALKIEGEKISGFVKSSELSSNDIVVDCGNKIIIPALIDLHIHGAVGkdVMDGDyeSLNDISKYLASI- 87
Cdd:PRK11170 8 RIYTGHEVLDDHAVVIADGLIEAVCPVAELPPGIEQRDLNGAILSPGFIDLQLNGCGG--VQFND--TAEAISVETLEIm 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309388644 88 -------GVSRFLATTLTAPISKIENALKNIRESQKRGLAGAkiIGTYLEGPYLSKEKKGAHPEEYLKEPNikeiKKMID 160
Cdd:PRK11170 84 qkaneksGCTSFLPTLITSSDELMKQAVRVMREYLAKHPNQA--LGLHLEGPYLNLVKKGTHNPEFIRKPD----AEMVD 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309388644 161 ISGNN---IKILALAPEKNEsQKVIKFLCDKGIIAALAHTNADYSVIEESVKNGAFLATHTFNGMKGLHHRNPGAIGGIM 237
Cdd:PRK11170 158 FLCENadvITKVTLAPEMVD-AEVIRKLVEAGIVVSAGHSNATYEEAKAGFRAGITFATHLYNAMPYITGREPGLVGAIL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309388644 238 AFDEIYSELIADKIHVHPAVMKILYKVKGlEKIALISDCMRAGGIEDGEYKLGEIDVNVKNATARTRSGSLAGSTLKIKD 317
Cdd:PRK11170 237 DEPDVYCGIIADGLHVDYANIRNAKRLKG-DKLCLVTDATAPAGANIEQFIFAGKTIYYRDGLCVDENGTLSGSALTMIE 315
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 309388644 318 ALLNIKEAVDIELFEAVKMASLVPAKILGLDSELGSIKKFKKADITVIDSEMNIYLTAVDGKIV 381
Cdd:PRK11170 316 AVRNLVEHVGIALDEALRMATLYPARAIGVDKRLGSIEAGKVANLTAFTRDFKITKTIVNGNEV 379
|
|
| Amidohydro_1 |
pfam01979 |
Amidohydrolase family; This family of enzymes are a a large metal dependent hydrolase ... |
51-381 |
1.29e-17 |
|
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: 82.93 E-value: 1.29e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309388644 51 IIIPALIDLHIHGAVGkdVMDGDYESLnDISKYLASIGVSRFLA--TTLTAPISKIEN-ALKNIRESqkrglAGAKIIGT 127
Cdd:pfam01979 1 IVLPGLIDAHVHLEMG--LLRGIPVPP-EFAYEALRLGITTMLKsgTTTVLDMGATTStGIEALLEA-----AEELPLGL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309388644 128 YLEGPYLSKEKKG-AHPEEYLKEPNIKEIKKMIDISGNNIKI-LALAPEKNESQKVIKFL------CDKGIIAALAHTNA 199
Cdd:pfam01979 73 RFLGPGCSLDTDGeLEGRKALREKLKAGAEFIKGMADGVVFVgLAPHGAPTFSDDELKAAleeakkYGLPVAIHALETKG 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309388644 200 DYSVIEESVKNGAFLATHTFNGMKGlhhrnpgaiggimAFDEIYSELIADKIHVHPAVMKILYKVKGLEKIALI--SDCM 277
Cdd:pfam01979 153 EVEDAIAAFGGGIEHGTHLEVAESG-------------GLLDIIKLILAHGVHLSPTEANLLAEHLKGAGVAHCpfSNSK 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309388644 278 RAGGIEDGEyKLGEIDVNVKNATARTRSGSLAGSTLKIKDALLNIKEA-VDIELFEAVKMASLVPAKILGLDSELGSIKK 356
Cdd:pfam01979 220 LRSGRIALR-KALEDGVKVGLGTDGAGSGNSLNMLEELRLALELQFDPeGGLSPLEALRMATINPAKALGLDDKVGSIEV 298
|
330 340 350
....*....|....*....|....*....|....*.
gi 309388644 357 FKKADITVID-----------SEMNIYLTAVDGKIV 381
Cdd:pfam01979 299 GKDADLVVVDldplaaffglkPDGNVKKVIVKGKIV 334
|
|
| HutI |
COG1228 |
Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport ... |
12-384 |
6.46e-12 |
|
Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440841 [Multi-domain] Cd Length: 386 Bit Score: 66.52 E-value: 6.46e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309388644 12 KEDEIILDHALKIEGEKISGFVKSSELS--SNDIVVDCGNKIIIPALIDLHIHGAVGKDVMDGDYESLNDIS----KYLA 85
Cdd:COG1228 21 TGGGVIENGTVLVEDGKIAAVGPAADLAvpAGAEVIDATGKTVLPGLIDAHTHLGLGGGRAVEFEAGGGITPtvdlVNPA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309388644 86 SIGVSRFLA----TTLTAPISKIENAlKNIRESQKRGLAGAKIIGTyleGPYLSkEKKGAH---PEEylkepNIKEIKKM 158
Cdd:COG1228 101 DKRLRRALAagvtTVRDLPGGPLGLR-DAIIAGESKLLPGPRVLAA---GPALS-LTGGAHargPEE-----ARAALREL 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309388644 159 IDISGNNIKILALAPEKNESQKVIKFLCDKGIIAAL---AHTNADYSvIEESVKNGAFLATH----TFNGMKGLHHRNPG 231
Cdd:COG1228 171 LAEGADYIKVFAEGGAPDFSLEELRAILEAAHALGLpvaAHAHQADD-IRLAVEAGVDSIEHgtylDDEVADLLAEAGTV 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309388644 232 AIG-GIMAFDEIY-------SELIADKIHVHPAVMKILYKvKGLeKIALISDCMraggiedgeyklgeidvnvknatart 303
Cdd:COG1228 250 VLVpTLSLFLALLegaaapvAAKARKVREAALANARRLHD-AGV-PVALGTDAG-------------------------- 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309388644 304 rSGSLAGSTLkikdaLLNIKEAVDIEL--FEAVKMASLVPAKILGLDSELGSIKKFKKADITVIDSE--------MNIYL 373
Cdd:COG1228 302 -VGVPPGRSL-----HRELALAVEAGLtpEEALRAATINAAKALGLDDDVGSLEPGKLADLVLLDGDplediaylEDVRA 375
|
410
....*....|.
gi 309388644 374 TAVDGKIVYKN 384
Cdd:COG1228 376 VMKDGRVVDRS 386
|
|
| Amidohydro_3 |
pfam07969 |
Amidohydrolase family; |
318-382 |
6.24e-08 |
|
Amidohydrolase family;
Pssm-ID: 400360 [Multi-domain] Cd Length: 464 Bit Score: 54.46 E-value: 6.24e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 309388644 318 ALLNIKEAVDIElfEAVKMASLVPAKILGLDSELGSIKKFKKADITVIDSE------MNIY-----LTAVDGKIVY 382
Cdd:pfam07969 391 EVLGPDEELSLE--EALALYTSGPAKALGLEDRKGTLGVGKDADLVVLDDDpltvdpPAIAdirvrLTVVDGRVVY 464
|
|
| Met_dep_hydrolase_C |
cd01309 |
Metallo-dependent hydrolases, subgroup C is part of the superfamily of metallo-dependent ... |
322-382 |
4.08e-06 |
|
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: 48.46 E-value: 4.08e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 309388644 322 IKEAVDIElfEAVKMASLVPAKILGLDSELGSIKKFKKADITVIDSE-MNIY----LTAVDGKIVY 382
Cdd:cd01309 296 VKYGLSYE--EALKAITINPAKILGIEDRVGSLEPGKDADLVVWNGDpLEPTskpeQVYIDGRLVY 359
|
|
| SsnA |
COG0402 |
Cytosine/adenosine deaminase or related metal-dependent hydrolase [Nucleotide transport and ... |
13-62 |
6.10e-06 |
|
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: 47.90 E-value: 6.10e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 309388644 13 EDEIILDHALKIEGEKISGFVKSSELSS---NDIVVDCGNKIIIPALIDLHIH 62
Cdd:COG0402 15 AGGVLEDGAVLVEDGRIAAVGPGAELPArypAAEVIDAGGKLVLPGLVNTHTH 67
|
|
| SsnA |
COG0402 |
Cytosine/adenosine deaminase or related metal-dependent hydrolase [Nucleotide transport and ... |
332-384 |
8.76e-06 |
|
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: 47.51 E-value: 8.76e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 309388644 332 EAVKMASLVPAKILGLDSELGSIKKFKKADITVID--------------------SEMNIYLTAVDGKIVYKN 384
Cdd:COG0402 344 EALEMATLGGARALGLDDEIGSLEPGKRADLVVLDldaphlaplhdplsalvyaaDGRDVRTVWVAGRVVVRD 416
|
|
| AllB |
COG0044 |
Dihydroorotase or related cyclic amidohydrolase [Nucleotide transport and metabolism]; ... |
24-62 |
3.60e-05 |
|
Dihydroorotase or related cyclic amidohydrolase [Nucleotide transport and metabolism]; Dihydroorotase or related cyclic amidohydrolase is part of the Pathway/BioSystem: Pyrimidine biosynthesis
Pssm-ID: 439814 [Multi-domain] Cd Length: 439 Bit Score: 45.47 E-value: 3.60e-05
10 20 30
....*....|....*....|....*....|....*....
gi 309388644 24 IEGEKISGFVKSSELSSNDIVVDCGNKIIIPALIDLHIH 62
Cdd:COG0044 20 IEDGRIAAIGPDLAAPEAAEVIDATGLLVLPGLIDLHVH 58
|
|
| PRK07228 |
PRK07228 |
5'-deoxyadenosine deaminase; |
335-384 |
1.00e-04 |
|
5'-deoxyadenosine deaminase;
Pssm-ID: 180895 [Multi-domain] Cd Length: 445 Bit Score: 44.22 E-value: 1.00e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 309388644 335 KMASLVPAKILGLDSELGSIKKFKKADITVIDS---------EMNIY-------------LTAVDGKIVYKN 384
Cdd:PRK07228 344 EMATLGGAKAAGFEDEIGSLEEGKKADLAILDLdglhatpshGVDVLshlvyaahgsdveTTMVDGKIVMED 415
|
|
| Bact_CD |
cd01293 |
Bacterial cytosine deaminase and related metal-dependent hydrolases. Cytosine deaminases (CDs) ... |
4-118 |
1.07e-04 |
|
Bacterial cytosine deaminase and related metal-dependent hydrolases. Cytosine deaminases (CDs) catalyze the deamination of cytosine, producing uracil and ammonia. They play an important role in pyrimidine salvage. CDs are present in prokaryotes and fungi, but not mammalian cells. The bacterial enzymes, but not the fungal enzymes, are related to the adenosine deaminases (ADA). The bacterial enzymes are iron dependent and hexameric.
Pssm-ID: 238618 [Multi-domain] Cd Length: 398 Bit Score: 44.16 E-value: 1.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309388644 4 YIKSKKIYKEDEIILDhaLKIEGEKISGFVKSSELSSNDIVVDCGNKIIIPALIDLHIHgavgkdvMD----GDYESLND 79
Cdd:cd01293 1 LLRNARLADGGTALVD--IAIEDGRIAAIGPALAVPPDAEEVDAKGRLVLPAFVDPHIH-------LDktftGGRWPNNS 71
|
90 100 110
....*....|....*....|....*....|....*....
gi 309388644 80 ISKYLASIGVSRFLATTLTAPISKiENALKNIRESQKRG 118
Cdd:cd01293 72 GGTLLEAIIAWEERKLLLTAEDVK-ERAERALELAIAHG 109
|
|
| Met_dep_hydrolase_A |
cd01299 |
Metallo-dependent hydrolases, subgroup A is part of the superfamily of metallo-dependent ... |
42-366 |
1.08e-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: 43.82 E-value: 1.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309388644 42 DIVVDCGNKIIIPALIDLHIHgaVGKDVMDGDYEslNDISKYLASIGVSRFLATTLTAPISKIENA----LKNIRESQKR 117
Cdd:cd01299 1 AQVIDLGGKTLMPGLIDAHTH--LGSDPGDLPLD--LALPVEYRTIRATRQARAALRAGFTTVRDAggadYGLLRDAIDA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309388644 118 GL-AGAKIIGTyleGPYLSKekKGAHPEEYLKEPN----------------IKEIKKMIDISGNNIKILA---------L 171
Cdd:cd01299 77 GLiPGPRVFAS---GRALSQ--TGGHGDPRGLSGLfpagglaavvdgveevRAAVREQLRRGADQIKIMAtggvlspgdP 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309388644 172 APEKNESQKVIKFLCD----KGI-IAALAHTNA-------------------DYSVIEESVKNGAFLaTHTFNGMKGLHh 227
Cdd:cd01299 152 PPDTQFSEEELRAIVDeahkAGLyVAAHAYGAEairrairagvdtiehgfliDDETIELMKEKGIFL-VPTLATYEALA- 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309388644 228 rNPGAIGGIMafdEIYSELIADKIHVHPAVMKILYKVkGLeKIALISDcmrAG-GIEDGEYKLGEIDVNVKnatartrsg 306
Cdd:cd01299 230 -AEGAAPGLP---ADSAEKVALVLEAGRDALRRAHKA-GV-KIAFGTD---AGfPVPPHGWNARELELLVK--------- 291
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 309388644 307 sLAGSTLkikdallnikeavdielfEAVKMASLVPAKILGLDSELGSIKKFKKADITVID 366
Cdd:cd01299 292 -AGGTPA------------------EALRAATANAAELLGLSDELGVIEAGKLADLLVVD 332
|
|
| YtcJ |
COG1574 |
Predicted amidohydrolase YtcJ [General function prediction only]; |
320-383 |
1.21e-04 |
|
Predicted amidohydrolase YtcJ [General function prediction only];
Pssm-ID: 441182 [Multi-domain] Cd Length: 535 Bit Score: 44.02 E-value: 1.21e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 309388644 320 LNIKEAVDIElfEAVKMASLVPAKILGLDSELGSIKKFKKADITVID-----------SEMNIYLTAVDGKIVYK 383
Cdd:COG1574 461 LGPEERLTVE--EALRAYTIGAAYAAFEEDEKGSLEPGKLADFVVLDrdpltvppeeiKDIKVLLTVVGGRVVYE 533
|
|
| PRK09045 |
PRK09045 |
TRZ/ATZ family hydrolase; |
332-366 |
1.22e-04 |
|
TRZ/ATZ family hydrolase;
Pssm-ID: 236366 [Multi-domain] Cd Length: 443 Bit Score: 43.75 E-value: 1.22e-04
10 20 30
....*....|....*....|....*....|....*
gi 309388644 332 EAVKMASLVPAKILGLDSELGSIKKFKKADITVID 366
Cdd:PRK09045 344 TALRMATLNGARALGLDDEIGSLEPGKQADLVAVD 378
|
|
| PLN02795 |
PLN02795 |
allantoinase |
2-62 |
1.57e-04 |
|
allantoinase
Pssm-ID: 178392 [Multi-domain] Cd Length: 505 Bit Score: 43.61 E-value: 1.57e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 309388644 2 SYYIKSKKIYKEDEIIlDHALKIEGEKISGFVKSSELSSNDI---VVDCGNKIIIPALIDLHIH 62
Cdd:PLN02795 45 HFVLYSKRVVTPAGVI-PGAVEVEGGRIVSVTKEEEAPKSQKkphVLDYGNAVVMPGLIDVHVH 107
|
|
| PRK02382 |
PRK02382 |
dihydroorotase; Provisional |
5-62 |
3.52e-04 |
|
dihydroorotase; Provisional
Pssm-ID: 179417 [Multi-domain] Cd Length: 443 Bit Score: 42.33 E-value: 3.52e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 309388644 5 IKSKKIYKeDEIILDHALKIEGEKISGFVKSSELSSNDIVVDCGNKIIIPALIDLHIH 62
Cdd:PRK02382 6 LKDGRVYY-NNSLQPRDVRIDGGKITAVGKDLDGSSSEEVIDARGMLLLPGGIDVHVH 62
|
|
| pyrC |
PRK09357 |
dihydroorotase; Validated |
1-62 |
3.75e-04 |
|
dihydroorotase; Validated
Pssm-ID: 236479 [Multi-domain] Cd Length: 423 Bit Score: 42.49 E-value: 3.75e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 309388644 1 MSYYIKSKKIYKEDEIILDHALKIEGEKISGFVKSSELSsNDIVVDCGNKIIIPALIDLHIH 62
Cdd:PRK09357 1 MMILIKNGRVIDPKGLDEVADVLIDDGKIAAIGENIEAE-GAEVIDATGLVVAPGLVDLHVH 61
|
|
| PRK07228 |
PRK07228 |
5'-deoxyadenosine deaminase; |
13-62 |
8.11e-04 |
|
5'-deoxyadenosine deaminase;
Pssm-ID: 180895 [Multi-domain] Cd Length: 445 Bit Score: 41.14 E-value: 8.11e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 309388644 13 EDEIILDHALKIEGEKISGFVKSSELSSNDIVVDCGNKIIIPALIDLHIH 62
Cdd:PRK07228 15 AKREIVDGDVLIEDDRIAAVGDRLDLEDYDDHIDATGKVVIPGLIQGHIH 64
|
|
| ATZ_TRZ_like |
cd01298 |
TRZ/ATZ family contains enzymes from the atrazine degradation pathway and related hydrolases. ... |
331-385 |
9.47e-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: 9.47e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 309388644 331 FEAVKMASLVPAKILGLDsELGSIKKFKKADITVID--------------------SEMNIYLTAVDGKIVYKNK 385
Cdd:cd01298 335 EEALEMATIGGAKALGLD-EIGSLEVGKKADLILIDldgphllpvhdpishlvysaNGGDVDTVIVNGRVVMEDG 408
|
|
| AdeC |
cd01295 |
Adenine deaminase (AdeC) directly deaminates adenine to form hypoxanthine. This reaction is ... |
321-381 |
1.96e-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: 1.96e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 309388644 321 NIKEAVD--IELFEAVKMASLVPAKILGLDsELGSIKKFKKADITVIDS--EMNIYLTAVDGKIV 381
Cdd:cd01295 226 IVRRAIEagIPPEDAIQMATINPAECYGLH-DLGAIAPGRIADIVILDDleNFNITTVLAKGIAV 289
|
|
| PhnM |
cd01306 |
PhnM is believed to be a subunit of the membrane associated C-P lyase complex. C-P lyase is ... |
317-366 |
3.04e-03 |
|
PhnM is believed to be a subunit of the membrane associated C-P lyase complex. C-P lyase is thought to catalyze the direct cleavage of inactivated C-P bonds to yield inorganic phosphate and the corresponding hydrocarbons. It is responsible for cleavage of alkylphosphonates, which are utilized as sole phosphorus sources by many bacteria.
Pssm-ID: 238631 Cd Length: 325 Bit Score: 39.19 E-value: 3.04e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 309388644 317 DALLNIKEAVDIELFEAVKMASLVPAKILGLDsELGSIKKFKKADITVID 366
Cdd:cd01306 262 HAAFRLADLGGWSLPEAVALVSANPARAVGLT-DRGSIAPGKRADLILVD 310
|
|
| PRK05985 |
PRK05985 |
cytosine deaminase; Provisional |
20-62 |
7.60e-03 |
|
cytosine deaminase; Provisional
Pssm-ID: 180337 [Multi-domain] Cd Length: 391 Bit Score: 37.99 E-value: 7.60e-03
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 309388644 20 HALKIEGEKISGFVKSSELSSNDIVVDCGNKIIIPALIDLHIH 62
Cdd:PRK05985 17 VDILIRDGRIAAIGPALAAPPGAEVEDGGGALALPGLVDGHIH 59
|
|
| YtcJ_like |
cd01300 |
YtcJ_like metal dependent amidohydrolases. YtcJ is a Bacillus subtilis ORF of unknown function. ... |
255-364 |
8.13e-03 |
|
YtcJ_like metal dependent amidohydrolases. YtcJ is a Bacillus subtilis ORF of unknown function. The Arabidopsis homolog LAF3 has been identified as a factor required for phytochrome A signalling.
Pssm-ID: 238625 [Multi-domain] Cd Length: 479 Bit Score: 38.06 E-value: 8.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309388644 255 PAVMKILYKVKGLEK----IALISDCMRAGgiedgeyklgeID--VNVKNA-TARTRSGSLAGstlkikdallNIKEAVD 327
Cdd:cd01300 386 EERAKRSYPFRSLLDagvpVALGSDAPVAP-----------PDplLGIWAAvTRKTPGGGVLG----------NPEERLS 444
|
90 100 110
....*....|....*....|....*....|....*..
gi 309388644 328 IElfEAVKMASLVPAKILGLDSELGSIKKFKKADITV 364
Cdd:cd01300 445 LE--EALRAYTIGAAYAIGEEDEKGSLEPGKLADFVV 479
|
|
| |
