|
Name |
Accession |
Description |
Interval |
E-value |
| NagA |
cd00854 |
N-acetylglucosamine-6-phosphate deacetylase, NagA, catalyzes the hydrolysis of the N-acetyl ... |
13-428 |
3.73e-163 |
|
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: 464.36 E-value: 3.73e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361513 13 LQFTNCRILRGGKLLREDLWVRGGRILDPEKLFFEERRvaDERRDCGGRILAPGFIDVQINGGFGVDFSQATEDvgsGVA 92
Cdd:cd00854 1 LIIKNARILTPGGLEDGAVLVEDGKIVAIGPEDELEEA--DEIIDLKGQYLVPGFIDIHIHGGGGADFMDGTAE---ALK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361513 93 LVARRILSHGVTSFCPTLVTSPPEVYHKVVPQIPVKSGGPHGAGVLGLHLEGPFISREKRGAHPEAHLRSFEADAFQDLL 172
Cdd:cd00854 76 TIAEALAKHGTTSFLPTTVTAPPEEIAKALAAIAEAIAEGQGAEILGIHLEGPFISPEKKGAHPPEYLRAPDPEELKKWL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361513 173 ATYGplDNVRIVTLAPELGRSHEVIRALTARGICVSLGHSVADLRAAEDAVWSGATFITHLFNAMLPFHHRDPGIVGLLT 252
Cdd:cd00854 156 EAAG--GLIKLVTLAPELDGALELIRYLVERGIIVSIGHSDATYEQAVAAFEAGATHVTHLFNAMSPLHHREPGVVGAAL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361513 253 SDrlpagRCIFYGMIADGTHTNPAALRIAHRAHP-QGLVLVTDAIPALGLGNGRHTLGQQEVEVDGLTAYVAgerpdplg 331
Cdd:cd00854 234 SD-----DDVYAELIADGIHVHPAAVRLAYRAKGaDKIVLVTDAMAAAGLPDGEYELGGQTVTVKDGVARLA-------- 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361513 332 prsqpacqvahdppracplcsqgTKTLSGSIAPMDVCVRHFLQATGCSMESALEAASLHPAQLLGLEKSKGTLDFGADAD 411
Cdd:cd00854 301 -----------------------DGTLAGSTLTMDQAVRNMVKWGGCPLEEAVRMASLNPAKLLGLDDRKGSLKPGKDAD 357
|
410
....*....|....*..
gi 21361513 412 FVVLDDSLHVQATYISG 428
Cdd:cd00854 358 LVVLDDDLNVKATWING 374
|
|
| NagA |
COG1820 |
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism]; |
15-429 |
6.87e-136 |
|
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism];
Pssm-ID: 441425 [Multi-domain] Cd Length: 373 Bit Score: 394.85 E-value: 6.87e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361513 15 FTNCRILRGGKLLRE-DLWVRGGRILDpeklFFEERRVADERRDCGGRILAPGFIDVQINGGFGVDFSQATEDvgsGVAL 93
Cdd:COG1820 2 ITNARIFTGDGVLEDgALLIEDGRIAA----IGPGAEPDAEVIDLGGGYLAPGFIDLHVHGGGGVDFMDGTPE---ALRT 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361513 94 VARRILSHGVTSFCPTLVTSPPEVYHKVVPQIPVKSGGPHGAGVLGLHLEGPFISREKRGAHPEAHLRSFEADAFQDLLA 173
Cdd:COG1820 75 IARAHARHGTTSFLPTTITAPPEDLLRALAAIAEAIEQGGGAGILGIHLEGPFLSPEKKGAHPPEYIRPPDPEELDRLLE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361513 174 TYGplDNVRIVTLAPELGRSHEVIRALTARGICVSLGHSVADLRAAEDAVWSGATFITHLFNAMLPFHHRDPGIVG-LLT 252
Cdd:COG1820 155 AAG--GLIKLVTLAPELPGALEFIRYLVEAGVVVSLGHTDATYEQARAAFEAGATHVTHLFNAMSPLHHREPGVVGaALD 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361513 253 SDRLPAgrcifyGMIADGTHTNPAALRIAHRA-HPQGLVLVTDAIPALGLGNGRHTLGQQEVEVDGLTAYVAgerpdplg 331
Cdd:COG1820 233 DDDVYA------ELIADGIHVHPAAVRLALRAkGPDRLILVTDAMAAAGLPDGEYELGGLEVTVKDGVARLA-------- 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361513 332 prsqpacqvahdppracplcsqgTKTLSGSIAPMDVCVRHFLQATGCSMESALEAASLHPAQLLGLEKSKGTLDFGADAD 411
Cdd:COG1820 299 -----------------------DGTLAGSTLTMDDAVRNLVEWTGLPLEEAVRMASLNPARALGLDDRKGSIAPGKDAD 355
|
410
....*....|....*...
gi 21361513 412 FVVLDDSLHVQATYISGE 429
Cdd:COG1820 356 LVVLDDDLNVRATWVGGE 373
|
|
| nagA |
TIGR00221 |
N-acetylglucosamine-6-phosphate deacetylase; [Central intermediary metabolism, Amino sugars] |
15-428 |
8.18e-81 |
|
N-acetylglucosamine-6-phosphate deacetylase; [Central intermediary metabolism, Amino sugars]
Pssm-ID: 272968 Cd Length: 380 Bit Score: 254.37 E-value: 8.18e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361513 15 FTNCRILRGGKLLRED-LWVRGGRILD--PEKlffeERRVADERRDCGGRILAPGFIDVQINGGFGVDFSQATEdvgSGV 91
Cdd:TIGR00221 7 LKDIAIVTGNEVIDNGaVGINDGKISTvsTEA----ELEPEIKEIDLPGNVLTPGFIDIHIHGCGGVDTNDASF---ETL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361513 92 ALVARRILSHGVTSFCPTLVTSPPEVYHKVVPQIPVKSGGPHGAGVLGLHLEGPFISREKRGAHPEAHLRSFEADAFQDL 171
Cdd:TIGR00221 80 EIMSERLPKSGCTSFLPTLITQPDENIKQAVKNMREYLAKEKNAQALGLHLEGPFLSPEKKGAHPPEYIREPDVELFKKF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361513 172 LATYGplDNVRIVTLAPELGRSHEVIRALTARGICVSLGHSVADLRAAEDAVWSGATFITHLFNAMLPFHHRDPGIVG-L 250
Cdd:TIGR00221 160 LCEAG--GVITKVTLAPEEDQHFELIRHLKDAGIIVSAGHTNATYELAKAAFKAGATHATHLYNAMSPIHHREPGVIGaV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361513 251 LTSDRlpagrcIFYGMIADGTHTNPAALRIAHRAHPQG-LVLVTDAIPALGLGNGRHTLGQQEVevdgltaYVAGERpdp 329
Cdd:TIGR00221 238 LDHDD------VYTEIIADGIHIHPLNIRLAKKLKGDSkLCLVTDSMAAAGAKDGVFIFGGKTV-------YIREGT--- 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361513 330 lgprsqpacqvahdppracplCSQGTKTLSGSIAPMDVCVRHFLQATGCSMESALEAASLHPAQLLGLEKSKGTLDFGAD 409
Cdd:TIGR00221 302 ---------------------CLDSNGTLAGSSLTMIEGARNLVEFTNISLTDAARMSSLNPARALGIDDRLGSVTVGKD 360
|
410
....*....|....*....
gi 21361513 410 ADFVVLDDSLHVQATYISG 428
Cdd:TIGR00221 361 ANLVVFTPDFEVILTIVNG 379
|
|
| nagA |
PRK11170 |
N-acetylglucosamine-6-phosphate deacetylase; Provisional |
15-432 |
7.43e-66 |
|
N-acetylglucosamine-6-phosphate deacetylase; Provisional
Pssm-ID: 183010 Cd Length: 382 Bit Score: 215.61 E-value: 7.43e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361513 15 FTNCRILRGGKLLRED-LWVRGGRIldpEKLFFEERRVAD-ERRDCGGRILAPGFIDVQINGGFGVDFSQATEDVG-SGV 91
Cdd:PRK11170 4 LTNGRIYTGHEVLDDHaVVIADGLI---EAVCPVAELPPGiEQRDLNGAILSPGFIDLQLNGCGGVQFNDTAEAISvETL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361513 92 ALVARRILSHGVTSFCPTLVTSPPEVYHKVVpQIPVKSGGPHGAGVLGLHLEGPFISREKRGAHPEAHLRSFEADAFQDL 171
Cdd:PRK11170 81 EIMQKANEKSGCTSFLPTLITSSDELMKQAV-RVMREYLAKHPNQALGLHLEGPYLNLVKKGTHNPEFIRKPDAEMVDFL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361513 172 LATygpLDNVRIVTLAPELGRShEVIRALTARGICVSLGHSVADLRAAEDAVWSGATFITHLFNAMLPFHHRDPGIVGLL 251
Cdd:PRK11170 160 CEN---ADVITKVTLAPEMVDA-EVIRKLVEAGIVVSAGHSNATYEEAKAGFRAGITFATHLYNAMPYITGREPGLVGAI 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361513 252 --TSDrlpagrcIFYGMIADGTHTNPAALRIAHRAHPQGLVLVTDAIPALGLGNGRHTLGqqevevdGLTAYVagerpdp 329
Cdd:PRK11170 236 ldEPD-------VYCGIIADGLHVDYANIRNAKRLKGDKLCLVTDATAPAGANIEQFIFA-------GKTIYY------- 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361513 330 lgprsqpacqvaHDppracPLCSQGTKTLSGSIAPMDVCVRHFLQATGCSMESALEAASLHPAQLLGLEKSKGTLDFGAD 409
Cdd:PRK11170 295 ------------RD-----GLCVDENGTLSGSALTMIEAVRNLVEHVGIALDEALRMATLYPARAIGVDKRLGSIEAGKV 357
|
410 420
....*....|....*....|...
gi 21361513 410 ADFVVLDDSLHVQATYISGELVW 432
Cdd:PRK11170 358 ANLTAFTRDFKITKTIVNGNEVV 380
|
|
| Amidohydro_1 |
pfam01979 |
Amidohydrolase family; This family of enzymes are a a large metal dependent hydrolase ... |
62-431 |
1.20e-10 |
|
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: 62.52 E-value: 1.20e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361513 62 ILAPGFIDVQINGGFGVDFSQAT--EDVGSGVALVARRILSHGVTSFCPTLVTSPP------EVYHKVVPQIPVksGGPH 133
Cdd:pfam01979 1 IVLPGLIDAHVHLEMGLLRGIPVppEFAYEALRLGITTMLKSGTTTVLDMGATTSTgieallEAAEELPLGLRF--LGPG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361513 134 GAGVLGLHLEGPFISREKrgAHPEAHLRSFEAD-AFQDLLATYGPldnvriVTLAPELGRshEVIRALTARG--ICVSLG 210
Cdd:pfam01979 79 CSLDTDGELEGRKALREK--LKAGAEFIKGMADgVVFVGLAPHGA------PTFSDDELK--AALEEAKKYGlpVAIHAL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361513 211 HSVADLRAAEDAVWSGATFITHLFNAMLPFHHRdpgivglltsdrlpagrcIFYGMIADGTHTNPA-ALRIAHRAHPQGL 289
Cdd:pfam01979 149 ETKGEVEDAIAAFGGGIEHGTHLEVAESGGLLD------------------IIKLILAHGVHLSPTeANLLAEHLKGAGV 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361513 290 VLVTDAIPALGLG-NGRHTLGQQEVEVdgltayvagerpdPLGPRSQpacqvahdppracplcsqgtktLSGSIAPMDVC 368
Cdd:pfam01979 211 AHCPFSNSKLRSGrIALRKALEDGVKV-------------GLGTDGA----------------------GSGNSLNMLEE 255
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 21361513 369 VR-----HFLQATGCSMESALEAASLHPAQLLGLEKSKGTLDFGADADFVVLD-----------DSLHVQATYISGELV 431
Cdd:pfam01979 256 LRlalelQFDPEGGLSPLEALRMATINPAKALGLDDKVGSIEVGKDADLVVVDldplaaffglkPDGNVKKVIVKGKIV 334
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| NagA |
cd00854 |
N-acetylglucosamine-6-phosphate deacetylase, NagA, catalyzes the hydrolysis of the N-acetyl ... |
13-428 |
3.73e-163 |
|
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: 464.36 E-value: 3.73e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361513 13 LQFTNCRILRGGKLLREDLWVRGGRILDPEKLFFEERRvaDERRDCGGRILAPGFIDVQINGGFGVDFSQATEDvgsGVA 92
Cdd:cd00854 1 LIIKNARILTPGGLEDGAVLVEDGKIVAIGPEDELEEA--DEIIDLKGQYLVPGFIDIHIHGGGGADFMDGTAE---ALK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361513 93 LVARRILSHGVTSFCPTLVTSPPEVYHKVVPQIPVKSGGPHGAGVLGLHLEGPFISREKRGAHPEAHLRSFEADAFQDLL 172
Cdd:cd00854 76 TIAEALAKHGTTSFLPTTVTAPPEEIAKALAAIAEAIAEGQGAEILGIHLEGPFISPEKKGAHPPEYLRAPDPEELKKWL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361513 173 ATYGplDNVRIVTLAPELGRSHEVIRALTARGICVSLGHSVADLRAAEDAVWSGATFITHLFNAMLPFHHRDPGIVGLLT 252
Cdd:cd00854 156 EAAG--GLIKLVTLAPELDGALELIRYLVERGIIVSIGHSDATYEQAVAAFEAGATHVTHLFNAMSPLHHREPGVVGAAL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361513 253 SDrlpagRCIFYGMIADGTHTNPAALRIAHRAHP-QGLVLVTDAIPALGLGNGRHTLGQQEVEVDGLTAYVAgerpdplg 331
Cdd:cd00854 234 SD-----DDVYAELIADGIHVHPAAVRLAYRAKGaDKIVLVTDAMAAAGLPDGEYELGGQTVTVKDGVARLA-------- 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361513 332 prsqpacqvahdppracplcsqgTKTLSGSIAPMDVCVRHFLQATGCSMESALEAASLHPAQLLGLEKSKGTLDFGADAD 411
Cdd:cd00854 301 -----------------------DGTLAGSTLTMDQAVRNMVKWGGCPLEEAVRMASLNPAKLLGLDDRKGSLKPGKDAD 357
|
410
....*....|....*..
gi 21361513 412 FVVLDDSLHVQATYISG 428
Cdd:cd00854 358 LVVLDDDLNVKATWING 374
|
|
| NagA |
COG1820 |
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism]; |
15-429 |
6.87e-136 |
|
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism];
Pssm-ID: 441425 [Multi-domain] Cd Length: 373 Bit Score: 394.85 E-value: 6.87e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361513 15 FTNCRILRGGKLLRE-DLWVRGGRILDpeklFFEERRVADERRDCGGRILAPGFIDVQINGGFGVDFSQATEDvgsGVAL 93
Cdd:COG1820 2 ITNARIFTGDGVLEDgALLIEDGRIAA----IGPGAEPDAEVIDLGGGYLAPGFIDLHVHGGGGVDFMDGTPE---ALRT 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361513 94 VARRILSHGVTSFCPTLVTSPPEVYHKVVPQIPVKSGGPHGAGVLGLHLEGPFISREKRGAHPEAHLRSFEADAFQDLLA 173
Cdd:COG1820 75 IARAHARHGTTSFLPTTITAPPEDLLRALAAIAEAIEQGGGAGILGIHLEGPFLSPEKKGAHPPEYIRPPDPEELDRLLE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361513 174 TYGplDNVRIVTLAPELGRSHEVIRALTARGICVSLGHSVADLRAAEDAVWSGATFITHLFNAMLPFHHRDPGIVG-LLT 252
Cdd:COG1820 155 AAG--GLIKLVTLAPELPGALEFIRYLVEAGVVVSLGHTDATYEQARAAFEAGATHVTHLFNAMSPLHHREPGVVGaALD 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361513 253 SDRLPAgrcifyGMIADGTHTNPAALRIAHRA-HPQGLVLVTDAIPALGLGNGRHTLGQQEVEVDGLTAYVAgerpdplg 331
Cdd:COG1820 233 DDDVYA------ELIADGIHVHPAAVRLALRAkGPDRLILVTDAMAAAGLPDGEYELGGLEVTVKDGVARLA-------- 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361513 332 prsqpacqvahdppracplcsqgTKTLSGSIAPMDVCVRHFLQATGCSMESALEAASLHPAQLLGLEKSKGTLDFGADAD 411
Cdd:COG1820 299 -----------------------DGTLAGSTLTMDDAVRNLVEWTGLPLEEAVRMASLNPARALGLDDRKGSIAPGKDAD 355
|
410
....*....|....*...
gi 21361513 412 FVVLDDSLHVQATYISGE 429
Cdd:COG1820 356 LVVLDDDLNVRATWVGGE 373
|
|
| nagA |
TIGR00221 |
N-acetylglucosamine-6-phosphate deacetylase; [Central intermediary metabolism, Amino sugars] |
15-428 |
8.18e-81 |
|
N-acetylglucosamine-6-phosphate deacetylase; [Central intermediary metabolism, Amino sugars]
Pssm-ID: 272968 Cd Length: 380 Bit Score: 254.37 E-value: 8.18e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361513 15 FTNCRILRGGKLLRED-LWVRGGRILD--PEKlffeERRVADERRDCGGRILAPGFIDVQINGGFGVDFSQATEdvgSGV 91
Cdd:TIGR00221 7 LKDIAIVTGNEVIDNGaVGINDGKISTvsTEA----ELEPEIKEIDLPGNVLTPGFIDIHIHGCGGVDTNDASF---ETL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361513 92 ALVARRILSHGVTSFCPTLVTSPPEVYHKVVPQIPVKSGGPHGAGVLGLHLEGPFISREKRGAHPEAHLRSFEADAFQDL 171
Cdd:TIGR00221 80 EIMSERLPKSGCTSFLPTLITQPDENIKQAVKNMREYLAKEKNAQALGLHLEGPFLSPEKKGAHPPEYIREPDVELFKKF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361513 172 LATYGplDNVRIVTLAPELGRSHEVIRALTARGICVSLGHSVADLRAAEDAVWSGATFITHLFNAMLPFHHRDPGIVG-L 250
Cdd:TIGR00221 160 LCEAG--GVITKVTLAPEEDQHFELIRHLKDAGIIVSAGHTNATYELAKAAFKAGATHATHLYNAMSPIHHREPGVIGaV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361513 251 LTSDRlpagrcIFYGMIADGTHTNPAALRIAHRAHPQG-LVLVTDAIPALGLGNGRHTLGQQEVevdgltaYVAGERpdp 329
Cdd:TIGR00221 238 LDHDD------VYTEIIADGIHIHPLNIRLAKKLKGDSkLCLVTDSMAAAGAKDGVFIFGGKTV-------YIREGT--- 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361513 330 lgprsqpacqvahdppracplCSQGTKTLSGSIAPMDVCVRHFLQATGCSMESALEAASLHPAQLLGLEKSKGTLDFGAD 409
Cdd:TIGR00221 302 ---------------------CLDSNGTLAGSSLTMIEGARNLVEFTNISLTDAARMSSLNPARALGIDDRLGSVTVGKD 360
|
410
....*....|....*....
gi 21361513 410 ADFVVLDDSLHVQATYISG 428
Cdd:TIGR00221 361 ANLVVFTPDFEVILTIVNG 379
|
|
| nagA |
PRK11170 |
N-acetylglucosamine-6-phosphate deacetylase; Provisional |
15-432 |
7.43e-66 |
|
N-acetylglucosamine-6-phosphate deacetylase; Provisional
Pssm-ID: 183010 Cd Length: 382 Bit Score: 215.61 E-value: 7.43e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361513 15 FTNCRILRGGKLLRED-LWVRGGRIldpEKLFFEERRVAD-ERRDCGGRILAPGFIDVQINGGFGVDFSQATEDVG-SGV 91
Cdd:PRK11170 4 LTNGRIYTGHEVLDDHaVVIADGLI---EAVCPVAELPPGiEQRDLNGAILSPGFIDLQLNGCGGVQFNDTAEAISvETL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361513 92 ALVARRILSHGVTSFCPTLVTSPPEVYHKVVpQIPVKSGGPHGAGVLGLHLEGPFISREKRGAHPEAHLRSFEADAFQDL 171
Cdd:PRK11170 81 EIMQKANEKSGCTSFLPTLITSSDELMKQAV-RVMREYLAKHPNQALGLHLEGPYLNLVKKGTHNPEFIRKPDAEMVDFL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361513 172 LATygpLDNVRIVTLAPELGRShEVIRALTARGICVSLGHSVADLRAAEDAVWSGATFITHLFNAMLPFHHRDPGIVGLL 251
Cdd:PRK11170 160 CEN---ADVITKVTLAPEMVDA-EVIRKLVEAGIVVSAGHSNATYEEAKAGFRAGITFATHLYNAMPYITGREPGLVGAI 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361513 252 --TSDrlpagrcIFYGMIADGTHTNPAALRIAHRAHPQGLVLVTDAIPALGLGNGRHTLGqqevevdGLTAYVagerpdp 329
Cdd:PRK11170 236 ldEPD-------VYCGIIADGLHVDYANIRNAKRLKGDKLCLVTDATAPAGANIEQFIFA-------GKTIYY------- 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361513 330 lgprsqpacqvaHDppracPLCSQGTKTLSGSIAPMDVCVRHFLQATGCSMESALEAASLHPAQLLGLEKSKGTLDFGAD 409
Cdd:PRK11170 295 ------------RD-----GLCVDENGTLSGSALTMIEAVRNLVEHVGIALDEALRMATLYPARAIGVDKRLGSIEAGKV 357
|
410 420
....*....|....*....|...
gi 21361513 410 ADFVVLDDSLHVQATYISGELVW 432
Cdd:PRK11170 358 ANLTAFTRDFKITKTIVNGNEVV 380
|
|
| Amidohydro_1 |
pfam01979 |
Amidohydrolase family; This family of enzymes are a a large metal dependent hydrolase ... |
62-431 |
1.20e-10 |
|
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: 62.52 E-value: 1.20e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361513 62 ILAPGFIDVQINGGFGVDFSQAT--EDVGSGVALVARRILSHGVTSFCPTLVTSPP------EVYHKVVPQIPVksGGPH 133
Cdd:pfam01979 1 IVLPGLIDAHVHLEMGLLRGIPVppEFAYEALRLGITTMLKSGTTTVLDMGATTSTgieallEAAEELPLGLRF--LGPG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361513 134 GAGVLGLHLEGPFISREKrgAHPEAHLRSFEAD-AFQDLLATYGPldnvriVTLAPELGRshEVIRALTARG--ICVSLG 210
Cdd:pfam01979 79 CSLDTDGELEGRKALREK--LKAGAEFIKGMADgVVFVGLAPHGA------PTFSDDELK--AALEEAKKYGlpVAIHAL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361513 211 HSVADLRAAEDAVWSGATFITHLFNAMLPFHHRdpgivglltsdrlpagrcIFYGMIADGTHTNPA-ALRIAHRAHPQGL 289
Cdd:pfam01979 149 ETKGEVEDAIAAFGGGIEHGTHLEVAESGGLLD------------------IIKLILAHGVHLSPTeANLLAEHLKGAGV 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361513 290 VLVTDAIPALGLG-NGRHTLGQQEVEVdgltayvagerpdPLGPRSQpacqvahdppracplcsqgtktLSGSIAPMDVC 368
Cdd:pfam01979 211 AHCPFSNSKLRSGrIALRKALEDGVKV-------------GLGTDGA----------------------GSGNSLNMLEE 255
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 21361513 369 VR-----HFLQATGCSMESALEAASLHPAQLLGLEKSKGTLDFGADADFVVLD-----------DSLHVQATYISGELV 431
Cdd:pfam01979 256 LRlalelQFDPEGGLSPLEALRMATINPAKALGLDDKVGSIEVGKDADLVVVDldplaaffglkPDGNVKKVIVKGKIV 334
|
|
| YtcJ |
COG1574 |
Predicted amidohydrolase YtcJ [General function prediction only]; |
379-435 |
2.74e-07 |
|
Predicted amidohydrolase YtcJ [General function prediction only];
Pssm-ID: 441182 [Multi-domain] Cd Length: 535 Bit Score: 52.88 E-value: 2.74e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 21361513 379 SMESALEAASLHPAQLLGLEKSKGTLDFGADADFVVLDDSL-----------HVQATYISGELVWQAD 435
Cdd:COG1574 468 TVEEALRAYTIGAAYAAFEEDEKGSLEPGKLADFVVLDRDPltvppeeikdiKVLLTVVGGRVVYEAE 535
|
|
| HutI |
COG1228 |
Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport ... |
7-434 |
1.87e-06 |
|
Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440841 [Multi-domain] Cd Length: 386 Bit Score: 49.57 E-value: 1.87e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361513 7 AAGARVLQFTNCRIL--RGGKLLRE-DLWVRGGRILDPEKLFFEERRVADERRDCGGRILAPGFIDV---QINGGFGVDF 80
Cdd:COG1228 4 PAQAGTLLITNATLVdgTGGGVIENgTVLVEDGKIAAVGPAADLAVPAGAEVIDATGKTVLPGLIDAhthLGLGGGRAVE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361513 81 SQATEDVGSGVALV------ARRILSHGVTSfcptlvtsppevyhkVVpqipVKSGGPHG----------AGVLGLHL-- 142
Cdd:COG1228 84 FEAGGGITPTVDLVnpadkrLRRALAAGVTT---------------VR----DLPGGPLGlrdaiiagesKLLPGPRVla 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361513 143 EGPFISREKrGAH---PE---AHLRS-FEADA-FQDLLATYGPLDnvrivtlapelgRSHEVIRALTARGICVSL---GH 211
Cdd:COG1228 145 AGPALSLTG-GAHargPEearAALRElLAEGAdYIKVFAEGGAPD------------FSLEELRAILEAAHALGLpvaAH 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361513 212 sVADLRAAEDAVWSGATFITHL-------FNAMLpfhHRDPGIVGLLTSDRLPAGRCIFYGMIADGTHTNPAALRIAHRA 284
Cdd:COG1228 212 -AHQADDIRLAVEAGVDSIEHGtylddevADLLA---EAGTVVLVPTLSLFLALLEGAAAPVAAKARKVREAALANARRL 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361513 285 HPQGlVLVtdaipALGlgngrhTlgqqevevDGLTAYVAGerpdplgpRSQPACqvahdppracplcsqgtktlsgsiap 364
Cdd:COG1228 288 HDAG-VPV-----ALG------T--------DAGVGVPPG--------RSLHRE-------------------------- 313
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 21361513 365 MDVCVRHflqatGCSMESALEAASLHPAQLLGLEKSKGTLDFGADADFVVLD-DSL-------HVQATYISGELVWQA 434
Cdd:COG1228 314 LALAVEA-----GLTPEEALRAATINAAKALGLDDDVGSLEPGKLADLVLLDgDPLediayleDVRAVMKDGRVVDRS 386
|
|
| AdeC |
COG1001 |
Adenine deaminase [Nucleotide transport and metabolism]; |
365-431 |
2.24e-06 |
|
Adenine deaminase [Nucleotide transport and metabolism];
Pssm-ID: 440625 [Multi-domain] Cd Length: 559 Bit Score: 49.71 E-value: 2.24e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 21361513 365 MDVCVRHFLQAtGCSMESALEAASLHPAQLLGLeKSKGTLDFGADADFVVLDD--SLHVQATYISGELV 431
Cdd:COG1001 272 IDHVVRRAIEL-GLDPVTAIQMATLNAAEHFGL-KDLGAIAPGRRADIVLLDDleDFKVEKVYADGKLV 338
|
|
| AdeC |
cd01295 |
Adenine deaminase (AdeC) directly deaminates adenine to form hypoxanthine. This reaction is ... |
365-431 |
3.48e-06 |
|
Adenine deaminase (AdeC) directly deaminates adenine to form hypoxanthine. This reaction is part of one of the adenine salvage pathways, as well as the degradation pathway. It is important for adenine utilization as a purine, as well as a nitrogen source in bacteria and archea.
Pssm-ID: 238620 [Multi-domain] Cd Length: 422 Bit Score: 49.14 E-value: 3.48e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 21361513 365 MDVCVRHFLQAtGCSMESALEAASLHPAQLLGLEKsKGTLDFGADADFVVLDD--SLHVQATYISGELV 431
Cdd:cd01295 223 LDYIVRRAIEA-GIPPEDAIQMATINPAECYGLHD-LGAIAPGRIADIVILDDleNFNITTVLAKGIAV 289
|
|
| Met_dep_hydrolase_C |
cd01309 |
Metallo-dependent hydrolases, subgroup C is part of the superfamily of metallo-dependent ... |
367-431 |
7.11e-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: 47.69 E-value: 7.11e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361513 367 VCVRHflqatGCSMESALEAASLHPAQLLGLEKSKGTLDFGADADFVVLD-DSLH----VQATYISGELV 431
Cdd:cd01309 294 KAVKY-----GLSYEEALKAITINPAKILGIEDRVGSLEPGKDADLVVWNgDPLEptskPEQVYIDGRLV 358
|
|
| AllB |
COG0044 |
Dihydroorotase or related cyclic amidohydrolase [Nucleotide transport and metabolism]; ... |
377-436 |
1.72e-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: 47.01 E-value: 1.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361513 377 GCSMESALEAASLHPAQLLGLEKsKGTLDFGADADFVVLD---------DSLH----------------VQATYISGELV 431
Cdd:COG0044 344 RLSLERLVELLSTNPARIFGLPR-KGRIAVGADADLVLFDpdaewtvtaEDLHskskntpfegreltgrVVATIVRGRVV 422
|
....*
gi 21361513 432 WQADA 436
Cdd:COG0044 423 YEDGE 427
|
|
| Imidazolone-5PH |
cd01296 |
Imidazolonepropionase/imidazolone-5-propionate hydrolase (Imidazolone-5PH) catalyzes the third ... |
351-416 |
1.94e-05 |
|
Imidazolonepropionase/imidazolone-5-propionate hydrolase (Imidazolone-5PH) catalyzes the third step in the histidine degradation pathway, the hydrolysis of (S)-3-(5-oxo-4,5-dihydro-3H-imidazol-4-yl)propanoate to N-formimidoyl-L-glutamate. In bacteria, the enzyme is part of histidine utilization (hut) operon.
Pssm-ID: 238621 [Multi-domain] Cd Length: 371 Bit Score: 46.48 E-value: 1.94e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 21361513 351 CSQGTKTLSGSIAPMDVCVRHFlqatGCSMESALEAASLHPAQLLGLEKSKGTLDFGADADFVVLD 416
Cdd:cd01296 287 FNPGSSPTSSMPLVMHLACRLM----RMTPEEALTAATINAAAALGLGETVGSLEVGKQADLVILD 348
|
|
| Amidohydro_3 |
pfam07969 |
Amidohydrolase family; |
379-433 |
2.95e-05 |
|
Amidohydrolase family;
Pssm-ID: 400360 [Multi-domain] Cd Length: 464 Bit Score: 45.99 E-value: 2.95e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 21361513 379 SMESALEAASLHPAQLLGLEKSKGTLDFGADADFVVLD-DSLHVQATYISGELVWQ 433
Cdd:pfam07969 400 SLEEALALYTSGPAKALGLEDRKGTLGVGKDADLVVLDdDPLTVDPPAIADIRVRL 455
|
|
| AllB |
COG0044 |
Dihydroorotase or related cyclic amidohydrolase [Nucleotide transport and metabolism]; ... |
15-125 |
3.46e-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: 45.85 E-value: 3.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361513 15 FTNCRILRGGKLLREDLWVRGGRILDPEKLFFEERrvADERRDCGGRILAPGFIDVQINggFGVDFSQATEDVGSG-VAL 93
Cdd:COG0044 2 IKNGRVVDPGGLERADVLIEDGRIAAIGPDLAAPE--AAEVIDATGLLVLPGLIDLHVH--LREPGLEHKEDIETGtRAA 77
|
90 100 110
....*....|....*....|....*....|..
gi 21361513 94 VArrilsHGVTSFCPTLVTSPPEVYHKVVPQI 125
Cdd:COG0044 78 AA-----GGVTTVVDMPNTNPVTDTPEALEFK 104
|
|
| L-HYD_ALN |
cd01315 |
L-Hydantoinases (L-HYDs) and Allantoinase (ALN); L-Hydantoinases are a member of the ... |
388-417 |
4.71e-04 |
|
L-Hydantoinases (L-HYDs) and Allantoinase (ALN); L-Hydantoinases are a member of the dihydropyrimidinase family, which catalyzes the reversible hydrolytic ring opening of dihydropyrimidines and hydantoins (five-membered cyclic diamides used in biotechnology). But L-HYDs differ by having an L-enantio specificity and by lacking activity on possible natural substrates such as dihydropyrimidines. Allantoinase catalyzes the hydrolytic cleavage of the five-member ring of allantoin (5-ureidohydantoin) to form allantoic acid.
Pssm-ID: 238640 [Multi-domain] Cd Length: 447 Bit Score: 42.28 E-value: 4.71e-04
10 20 30
....*....|....*....|....*....|
gi 21361513 388 SLHPAQLLGLEKSKGTLDFGADADFVVLDD 417
Cdd:cd01315 363 CENPAKLFGLSHQKGRIAVGYDADFVVWDP 392
|
|
| SsnA |
COG0402 |
Cytosine/adenosine deaminase or related metal-dependent hydrolase [Nucleotide transport and ... |
383-433 |
8.16e-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: 41.35 E-value: 8.16e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 21361513 383 ALEAASLHPAQLLGLEKSKGTLDFGADADFVVLD--------------------DSLHVQATYISGELVWQ 433
Cdd:COG0402 345 ALEMATLGGARALGLDDEIGSLEPGKRADLVVLDldaphlaplhdplsalvyaaDGRDVRTVWVAGRVVVR 415
|
|
| Met_dep_hydrolase_B |
cd01307 |
Metallo-dependent hydrolases, subgroup B is part of the superfamily of metallo-dependent ... |
365-417 |
2.40e-03 |
|
Metallo-dependent hydrolases, subgroup B is part of the superfamily of metallo-dependent hydrolases, a large group of proteins that show conservation in their 3-dimensional fold (TIM barrel) and in details of their active site. The vast majority of the members have a conserved metal binding site, involving four histidines and one aspartic acid residue. In the common reaction mechanism, the metal ion (or ions) deprotonate a water molecule for a nucleophilic attack on the substrate. The function of this subgroup is unknown.
Pssm-ID: 238632 [Multi-domain] Cd Length: 338 Bit Score: 40.00 E-value: 2.40e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 21361513 365 MDVCVRHFLqATGCSMESALEAASLHPAQLLGLeKSKGTLDFGADADFVVLDD 417
Cdd:cd01307 265 LATTLSKLL-ALGMPLEEVIEAVTANPARMLGL-AEIGTLAVGYDADLTVFDL 315
|
|
| Isoaspartyl-dipeptidase |
cd01308 |
Isoaspartyl dipeptidase hydrolyzes the beta-L-isoaspartyl linkages in dipeptides, as part of ... |
360-433 |
2.51e-03 |
|
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: 40.07 E-value: 2.51e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 21361513 360 GSIAPMDVCVRHFLQATGCSMESALEAASLHPAQLLGLEKsKGTLDFGADADFVVLDDSLHVQATYISGELVWQ 433
Cdd:cd01308 304 GSVDTLLREVREAVKCGDIPLEVALRVITSNVARILKLRK-KGEIQPGFDADLVILDKDLDINSVIAKGQIMVR 376
|
|
| PRK09228 |
PRK09228 |
guanine deaminase; Provisional |
384-435 |
2.98e-03 |
|
guanine deaminase; Provisional
Pssm-ID: 236419 [Multi-domain] Cd Length: 433 Bit Score: 39.79 E-value: 2.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361513 384 LEAASLHPAQL-----------LGLEKSKGTLDFGADADFVVLD--------------DSLH--------------VQAT 424
Cdd:PRK09228 343 LQGYRLSPFQAfylatlggaraLGLDDRIGNLAPGKEADFVVLDpaatpllalrtaraESLEellfalmtlgddraVAET 422
|
90
....*....|.
gi 21361513 425 YISGELVWQAD 435
Cdd:PRK09228 423 YVAGRPVYRRL 433
|
|
| PRK06189 |
PRK06189 |
allantoinase; Provisional |
374-433 |
4.97e-03 |
|
allantoinase; Provisional
Pssm-ID: 235732 [Multi-domain] Cd Length: 451 Bit Score: 38.91 E-value: 4.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361513 374 QATGCSMESALEAASLHPAQLLGLEKsKGTLDFGADADFVVLD---------DSLH----------------VQATYISG 428
Cdd:PRK06189 349 IERGIPLETIARLLATNPAKRFGLPQ-KGRLEVGADADFVLVDldetytltkEDLFyrhkqspyegrtfpgrVVATYLRG 427
|
....*
gi 21361513 429 ELVWQ 433
Cdd:PRK06189 428 QCVYQ 432
|
|
| Met_dep_hydrolase_A |
cd01299 |
Metallo-dependent hydrolases, subgroup A is part of the superfamily of metallo-dependent ... |
354-416 |
5.06e-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: 38.81 E-value: 5.06e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 21361513 354 GTKTLSGSIAPMDVcVRHFLQAT---------GCSMEsALEAASLHPAQLLGLEKSKGTLDFGADADFVVLD 416
Cdd:cd01299 263 GVKIAFGTDAGFPV-PPHGWNARelellvkagGTPAE-ALRAATANAAELLGLSDELGVIEAGKLADLLVVD 332
|
|
| D-HYD |
cd01314 |
D-hydantoinases (D-HYD) also called dihydropyrimidases (DHPase) and related proteins; DHPases ... |
379-416 |
6.16e-03 |
|
D-hydantoinases (D-HYD) also called dihydropyrimidases (DHPase) and related proteins; DHPases are a family of enzymes that catalyze the reversible hydrolytic ring opening of the amide bond in five- or six-membered cyclic diamides, like dihydropyrimidine or hydantoin. The hydrolysis of dihydropyrimidines is the second step of reductive catabolism of pyrimidines in human. The hydrolysis of 5-substituted hydantoins in microorganisms leads to enantiomerically pure N-carbamyl amino acids, which are used for the production of antibiotics, peptide hormones, pyrethroids, and pesticides. HYDs are classified depending on their stereoselectivity. This family also includes collapsin response regulators (CRMPs), cytosolic proteins involved in neuronal differentiation and axonal guidance which have strong homology to DHPases, but lack most of the active site residues.
Pssm-ID: 238639 [Multi-domain] Cd Length: 447 Bit Score: 38.74 E-value: 6.16e-03
10 20 30
....*....|....*....|....*....|....*...
gi 21361513 379 SMESALEAASLHPAQLLGLEKSKGTLDFGADADFVVLD 416
Cdd:cd01314 357 TLEKFVELTSTNPAKIFGLYPRKGTIAVGSDADLVIWD 394
|
|
| PLN02795 |
PLN02795 |
allantoinase |
373-416 |
6.81e-03 |
|
allantoinase
Pssm-ID: 178392 [Multi-domain] Cd Length: 505 Bit Score: 38.60 E-value: 6.81e-03
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 21361513 373 LQATGCSMESALEAASLHPAQLLGLeKSKGTLDFGADADFVVLD 416
Cdd:PLN02795 403 GRAYGLTLEQLARWWSERPAKLAGL-DSKGAIAPGKDADIVVWD 445
|
|
| PRK15446 |
PRK15446 |
phosphonate metabolism protein PhnM; Provisional |
15-70 |
8.05e-03 |
|
phosphonate metabolism protein PhnM; Provisional
Pssm-ID: 237967 [Multi-domain] Cd Length: 383 Bit Score: 38.24 E-value: 8.05e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 21361513 15 FTNCRILRGGKLLREDLWVRGGRILDPEklffEERRVADERRDCGGRILAPGFIDV 70
Cdd:PRK15446 6 LSNARLVLPDEVVDGSLLIEDGRIAAID----PGASALPGAIDAEGDYLLPGLVDL 57
|
|
| |
