|
Name |
Accession |
Description |
Interval |
E-value |
| NagA |
cd00854 |
N-acetylglucosamine-6-phosphate deacetylase, NagA, catalyzes the hydrolysis of the N-acetyl ... |
13-398 |
9.41e-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: 462.05 E-value: 9.41e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982133 13 LQFTNCRILRGGTLLREDLWVRGGRILDPEKLFFEERRvaDEQRDCGGRILAPGFIDVQINGGFGVDFSKATEDvgsGVA 92
Cdd:cd00854 1 LIIKNARILTPGGLEDGAVLVEDGKIVAIGPEDELEEA--DEIIDLKGQYLVPGFIDIHIHGGGGADFMDGTAE---ALK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982133 93 LVARRLLSHGVTSFCPTLVTSPPEVYHKVLPQIPVKSGGPHGAGVLGVHLEGPFISREKRGAHPEAYLRSFEANAFHDVL 172
Cdd:cd00854 76 TIAEALAKHGTTSFLPTTVTAPPEEIAKALAAIAEAIAEGQGAEILGIHLEGPFISPEKKGAHPPEYLRAPDPEELKKWL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982133 173 ATYGplDNVCIVTLAPELDRSHEVIQALTAQGIRVSLGHSVADLRAAEVAVQSGATFITHLFNAMLPFHHRDPGIVGLLT 252
Cdd:cd00854 156 EAAG--GLIKLVTLAPELDGALELIRYLVERGIIVSIGHSDATYEQAVAAFEAGATHVTHLFNAMSPLHHREPGVVGAAL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982133 253 SDQlppghCIFYGMIADGIHTNPAALRIAHRAHP-QGLVLVTDAVPALGLGNGRHTLGQQEVEVDGLIAYIAgTKTLGGS 331
Cdd:cd00854 234 SDD-----DVYAELIADGIHVHPAAVRLAYRAKGaDKIVLVTDAMAAAGLPDGEYELGGQTVTVKDGVARLA-DGTLAGS 307
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 31982133 332 IAPMDVCVRHFLQATGCSVESALEAASLHPAQMLGLEKTKGSLDFGADADFVVLDDTLHVQATYISG 398
Cdd:cd00854 308 TLTMDQAVRNMVKWGGCPLEEAVRMASLNPAKLLGLDDRKGSLKPGKDADLVVLDDDLNVKATWING 374
|
|
| NagA |
COG1820 |
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism]; |
15-399 |
3.45e-140 |
|
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism];
Pssm-ID: 441425 [Multi-domain] Cd Length: 373 Bit Score: 404.48 E-value: 3.45e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982133 15 FTNCRILRGGTLLRE-DLWVRGGRILDpeklFFEERRVADEQRDCGGRILAPGFIDVQINGGFGVDFSKATEDvgsGVAL 93
Cdd:COG1820 2 ITNARIFTGDGVLEDgALLIEDGRIAA----IGPGAEPDAEVIDLGGGYLAPGFIDLHVHGGGGVDFMDGTPE---ALRT 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982133 94 VARRLLSHGVTSFCPTLVTSPPEVYHKVLPQIPVKSGGPHGAGVLGVHLEGPFISREKRGAHPEAYLRSFEANAFHDVLA 173
Cdd:COG1820 75 IARAHARHGTTSFLPTTITAPPEDLLRALAAIAEAIEQGGGAGILGIHLEGPFLSPEKKGAHPPEYIRPPDPEELDRLLE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982133 174 TYGplDNVCIVTLAPELDRSHEVIQALTAQGIRVSLGHSVADLRAAEVAVQSGATFITHLFNAMLPFHHRDPGIVG-LLT 252
Cdd:COG1820 155 AAG--GLIKLVTLAPELPGALEFIRYLVEAGVVVSLGHTDATYEQARAAFEAGATHVTHLFNAMSPLHHREPGVVGaALD 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982133 253 SDQLppgHCifyGMIADGIHTNPAALRIAHRA-HPQGLVLVTDAVPALGLGNGRHTLGQQEVEVDGLIAYIAgTKTLGGS 331
Cdd:COG1820 233 DDDV---YA---ELIADGIHVHPAAVRLALRAkGPDRLILVTDAMAAAGLPDGEYELGGLEVTVKDGVARLA-DGTLAGS 305
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 31982133 332 IAPMDVCVRHFLQATGCSVESALEAASLHPAQMLGLEKTKGSLDFGADADFVVLDDTLHVQATYISGE 399
Cdd:COG1820 306 TLTMDDAVRNLVEWTGLPLEEAVRMASLNPARALGLDDRKGSIAPGKDADLVVLDDDLNVRATWVGGE 373
|
|
| nagA |
TIGR00221 |
N-acetylglucosamine-6-phosphate deacetylase; [Central intermediary metabolism, Amino sugars] |
15-398 |
1.34e-82 |
|
N-acetylglucosamine-6-phosphate deacetylase; [Central intermediary metabolism, Amino sugars]
Pssm-ID: 272968 Cd Length: 380 Bit Score: 257.84 E-value: 1.34e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982133 15 FTNCRILRGGTLLRED-LWVRGGRILD--PEKlffeERRVADEQRDCGGRILAPGFIDVQINGGFGVDFSKATEdvgSGV 91
Cdd:TIGR00221 7 LKDIAIVTGNEVIDNGaVGINDGKISTvsTEA----ELEPEIKEIDLPGNVLTPGFIDIHIHGCGGVDTNDASF---ETL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982133 92 ALVARRLLSHGVTSFCPTLVTSPPEVYHKVLPQIPVKSGGPHGAGVLGVHLEGPFISREKRGAHPEAYLRSFEANAFHDV 171
Cdd:TIGR00221 80 EIMSERLPKSGCTSFLPTLITQPDENIKQAVKNMREYLAKEKNAQALGLHLEGPFLSPEKKGAHPPEYIREPDVELFKKF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982133 172 LATYGplDNVCIVTLAPELDRSHEVIQALTAQGIRVSLGHSVADLRAAEVAVQSGATFITHLFNAMLPFHHRDPGIVG-L 250
Cdd:TIGR00221 160 LCEAG--GVITKVTLAPEEDQHFELIRHLKDAGIIVSAGHTNATYELAKAAFKAGATHATHLYNAMSPIHHREPGVIGaV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982133 251 LTSDQlppghcIFYGMIADGIHTNPAALRIAHRAHPQG-LVLVTDAVPALGLGNGRHTLGQQEVEVDGLIAYIAgTKTLG 329
Cdd:TIGR00221 238 LDHDD------VYTEIIADGIHIHPLNIRLAKKLKGDSkLCLVTDSMAAAGAKDGVFIFGGKTVYIREGTCLDS-NGTLA 310
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 31982133 330 GSIAPMDVCVRHFLQATGCSVESALEAASLHPAQMLGLEKTKGSLDFGADADFVVLDDTLHVQATYISG 398
Cdd:TIGR00221 311 GSSLTMIEGARNLVEFTNISLTDAARMSSLNPARALGIDDRLGSVTVGKDANLVVFTPDFEVILTIVNG 379
|
|
| nagA |
PRK11170 |
N-acetylglucosamine-6-phosphate deacetylase; Provisional |
15-402 |
1.28e-67 |
|
N-acetylglucosamine-6-phosphate deacetylase; Provisional
Pssm-ID: 183010 Cd Length: 382 Bit Score: 219.08 E-value: 1.28e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982133 15 FTNCRILRGGTLLRED-LWVRGGRIldpEKLFFEERRVAD-EQRDCGGRILAPGFIDVQINGGFGVDFSKATEDVG-SGV 91
Cdd:PRK11170 4 LTNGRIYTGHEVLDDHaVVIADGLI---EAVCPVAELPPGiEQRDLNGAILSPGFIDLQLNGCGGVQFNDTAEAISvETL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982133 92 ALVARRLLSHGVTSFCPTLVTSPPE-------VYHKVLPQipvksggpHGAGVLGVHLEGPFISREKRGAHPEAYLRSFE 164
Cdd:PRK11170 81 EIMQKANEKSGCTSFLPTLITSSDElmkqavrVMREYLAK--------HPNQALGLHLEGPYLNLVKKGTHNPEFIRKPD 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982133 165 --------ANAfhDVLAtygpldnvcIVTLAPELDRShEVIQALTAQGIRVSLGHSVADLRAAEVAVQSGATFITHLFNA 236
Cdd:PRK11170 153 aemvdflcENA--DVIT---------KVTLAPEMVDA-EVIRKLVEAGIVVSAGHSNATYEEAKAGFRAGITFATHLYNA 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982133 237 MLPFHHRDPGIVGLL--TSDqlppghcIFYGMIADGIHTNPAALRIAHRAHPQGLVLVTDAVPALGLGNGRHTLGQQEVE 314
Cdd:PRK11170 221 MPYITGREPGLVGAIldEPD-------VYCGIIADGLHVDYANIRNAKRLKGDKLCLVTDATAPAGANIEQFIFAGKTIY 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982133 315 V-DGLIayIAGTKTLGGSIAPMDVCVRHFLQATGCSVESALEAASLHPAQMLGLEKTKGSLDFGADADFVVLDDTLHVQA 393
Cdd:PRK11170 294 YrDGLC--VDENGTLSGSALTMIEAVRNLVEHVGIALDEALRMATLYPARAIGVDKRLGSIEAGKVANLTAFTRDFKITK 371
|
....*....
gi 31982133 394 TYISGELVW 402
Cdd:PRK11170 372 TIVNGNEVV 380
|
|
| Amidohydro_1 |
pfam01979 |
Amidohydrolase family; This family of enzymes are a a large metal dependent hydrolase ... |
62-401 |
9.26e-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: 77.93 E-value: 9.26e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982133 62 ILAPGFIDVQINGGFGVDFSKAT--EDVGSGVALVARRLLSHGVTSFCPTLVTSPP------EVYHKVlpqipvksggph 133
Cdd:pfam01979 1 IVLPGLIDAHVHLEMGLLRGIPVppEFAYEALRLGITTMLKSGTTTVLDMGATTSTgieallEAAEEL------------ 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982133 134 gagVLGVHLEGPF--ISREKRGAHPEAYLRSF--EANAFHdvlatyGPLDNVCIVTLAPELDRS------HEVIQALTAQ 203
Cdd:pfam01979 69 ---PLGLRFLGPGcsLDTDGELEGRKALREKLkaGAEFIK------GMADGVVFVGLAPHGAPTfsddelKAALEEAKKY 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982133 204 GIRVS--LGHSVADLRAAEVAVQSGATFITHLFNAMLPFHHRDpgivglltsdqlppghciFYGMIADGIHTNPA-ALRI 280
Cdd:pfam01979 140 GLPVAihALETKGEVEDAIAAFGGGIEHGTHLEVAESGGLLDI------------------IKLILAHGVHLSPTeANLL 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982133 281 AHRAHPQGLVLVTDAVPALGlgngRHTLGQQEVEVDGLIAYIaGTKTLG-GSIAPMDVCVR-----HFLQATGCSVESAL 354
Cdd:pfam01979 202 AEHLKGAGVAHCPFSNSKLR----SGRIALRKALEDGVKVGL-GTDGAGsGNSLNMLEELRlalelQFDPEGGLSPLEAL 276
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 31982133 355 EAASLHPAQMLGLEKTKGSLDFGADADFVVLDDTLH-----------VQATYISGELV 401
Cdd:pfam01979 277 RMATINPAKALGLDDKVGSIEVGKDADLVVVDLDPLaaffglkpdgnVKKVIVKGKIV 334
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| NagA |
cd00854 |
N-acetylglucosamine-6-phosphate deacetylase, NagA, catalyzes the hydrolysis of the N-acetyl ... |
13-398 |
9.41e-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: 462.05 E-value: 9.41e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982133 13 LQFTNCRILRGGTLLREDLWVRGGRILDPEKLFFEERRvaDEQRDCGGRILAPGFIDVQINGGFGVDFSKATEDvgsGVA 92
Cdd:cd00854 1 LIIKNARILTPGGLEDGAVLVEDGKIVAIGPEDELEEA--DEIIDLKGQYLVPGFIDIHIHGGGGADFMDGTAE---ALK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982133 93 LVARRLLSHGVTSFCPTLVTSPPEVYHKVLPQIPVKSGGPHGAGVLGVHLEGPFISREKRGAHPEAYLRSFEANAFHDVL 172
Cdd:cd00854 76 TIAEALAKHGTTSFLPTTVTAPPEEIAKALAAIAEAIAEGQGAEILGIHLEGPFISPEKKGAHPPEYLRAPDPEELKKWL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982133 173 ATYGplDNVCIVTLAPELDRSHEVIQALTAQGIRVSLGHSVADLRAAEVAVQSGATFITHLFNAMLPFHHRDPGIVGLLT 252
Cdd:cd00854 156 EAAG--GLIKLVTLAPELDGALELIRYLVERGIIVSIGHSDATYEQAVAAFEAGATHVTHLFNAMSPLHHREPGVVGAAL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982133 253 SDQlppghCIFYGMIADGIHTNPAALRIAHRAHP-QGLVLVTDAVPALGLGNGRHTLGQQEVEVDGLIAYIAgTKTLGGS 331
Cdd:cd00854 234 SDD-----DVYAELIADGIHVHPAAVRLAYRAKGaDKIVLVTDAMAAAGLPDGEYELGGQTVTVKDGVARLA-DGTLAGS 307
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 31982133 332 IAPMDVCVRHFLQATGCSVESALEAASLHPAQMLGLEKTKGSLDFGADADFVVLDDTLHVQATYISG 398
Cdd:cd00854 308 TLTMDQAVRNMVKWGGCPLEEAVRMASLNPAKLLGLDDRKGSLKPGKDADLVVLDDDLNVKATWING 374
|
|
| NagA |
COG1820 |
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism]; |
15-399 |
3.45e-140 |
|
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism];
Pssm-ID: 441425 [Multi-domain] Cd Length: 373 Bit Score: 404.48 E-value: 3.45e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982133 15 FTNCRILRGGTLLRE-DLWVRGGRILDpeklFFEERRVADEQRDCGGRILAPGFIDVQINGGFGVDFSKATEDvgsGVAL 93
Cdd:COG1820 2 ITNARIFTGDGVLEDgALLIEDGRIAA----IGPGAEPDAEVIDLGGGYLAPGFIDLHVHGGGGVDFMDGTPE---ALRT 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982133 94 VARRLLSHGVTSFCPTLVTSPPEVYHKVLPQIPVKSGGPHGAGVLGVHLEGPFISREKRGAHPEAYLRSFEANAFHDVLA 173
Cdd:COG1820 75 IARAHARHGTTSFLPTTITAPPEDLLRALAAIAEAIEQGGGAGILGIHLEGPFLSPEKKGAHPPEYIRPPDPEELDRLLE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982133 174 TYGplDNVCIVTLAPELDRSHEVIQALTAQGIRVSLGHSVADLRAAEVAVQSGATFITHLFNAMLPFHHRDPGIVG-LLT 252
Cdd:COG1820 155 AAG--GLIKLVTLAPELPGALEFIRYLVEAGVVVSLGHTDATYEQARAAFEAGATHVTHLFNAMSPLHHREPGVVGaALD 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982133 253 SDQLppgHCifyGMIADGIHTNPAALRIAHRA-HPQGLVLVTDAVPALGLGNGRHTLGQQEVEVDGLIAYIAgTKTLGGS 331
Cdd:COG1820 233 DDDV---YA---ELIADGIHVHPAAVRLALRAkGPDRLILVTDAMAAAGLPDGEYELGGLEVTVKDGVARLA-DGTLAGS 305
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 31982133 332 IAPMDVCVRHFLQATGCSVESALEAASLHPAQMLGLEKTKGSLDFGADADFVVLDDTLHVQATYISGE 399
Cdd:COG1820 306 TLTMDDAVRNLVEWTGLPLEEAVRMASLNPARALGLDDRKGSIAPGKDADLVVLDDDLNVRATWVGGE 373
|
|
| nagA |
TIGR00221 |
N-acetylglucosamine-6-phosphate deacetylase; [Central intermediary metabolism, Amino sugars] |
15-398 |
1.34e-82 |
|
N-acetylglucosamine-6-phosphate deacetylase; [Central intermediary metabolism, Amino sugars]
Pssm-ID: 272968 Cd Length: 380 Bit Score: 257.84 E-value: 1.34e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982133 15 FTNCRILRGGTLLRED-LWVRGGRILD--PEKlffeERRVADEQRDCGGRILAPGFIDVQINGGFGVDFSKATEdvgSGV 91
Cdd:TIGR00221 7 LKDIAIVTGNEVIDNGaVGINDGKISTvsTEA----ELEPEIKEIDLPGNVLTPGFIDIHIHGCGGVDTNDASF---ETL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982133 92 ALVARRLLSHGVTSFCPTLVTSPPEVYHKVLPQIPVKSGGPHGAGVLGVHLEGPFISREKRGAHPEAYLRSFEANAFHDV 171
Cdd:TIGR00221 80 EIMSERLPKSGCTSFLPTLITQPDENIKQAVKNMREYLAKEKNAQALGLHLEGPFLSPEKKGAHPPEYIREPDVELFKKF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982133 172 LATYGplDNVCIVTLAPELDRSHEVIQALTAQGIRVSLGHSVADLRAAEVAVQSGATFITHLFNAMLPFHHRDPGIVG-L 250
Cdd:TIGR00221 160 LCEAG--GVITKVTLAPEEDQHFELIRHLKDAGIIVSAGHTNATYELAKAAFKAGATHATHLYNAMSPIHHREPGVIGaV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982133 251 LTSDQlppghcIFYGMIADGIHTNPAALRIAHRAHPQG-LVLVTDAVPALGLGNGRHTLGQQEVEVDGLIAYIAgTKTLG 329
Cdd:TIGR00221 238 LDHDD------VYTEIIADGIHIHPLNIRLAKKLKGDSkLCLVTDSMAAAGAKDGVFIFGGKTVYIREGTCLDS-NGTLA 310
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 31982133 330 GSIAPMDVCVRHFLQATGCSVESALEAASLHPAQMLGLEKTKGSLDFGADADFVVLDDTLHVQATYISG 398
Cdd:TIGR00221 311 GSSLTMIEGARNLVEFTNISLTDAARMSSLNPARALGIDDRLGSVTVGKDANLVVFTPDFEVILTIVNG 379
|
|
| nagA |
PRK11170 |
N-acetylglucosamine-6-phosphate deacetylase; Provisional |
15-402 |
1.28e-67 |
|
N-acetylglucosamine-6-phosphate deacetylase; Provisional
Pssm-ID: 183010 Cd Length: 382 Bit Score: 219.08 E-value: 1.28e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982133 15 FTNCRILRGGTLLRED-LWVRGGRIldpEKLFFEERRVAD-EQRDCGGRILAPGFIDVQINGGFGVDFSKATEDVG-SGV 91
Cdd:PRK11170 4 LTNGRIYTGHEVLDDHaVVIADGLI---EAVCPVAELPPGiEQRDLNGAILSPGFIDLQLNGCGGVQFNDTAEAISvETL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982133 92 ALVARRLLSHGVTSFCPTLVTSPPE-------VYHKVLPQipvksggpHGAGVLGVHLEGPFISREKRGAHPEAYLRSFE 164
Cdd:PRK11170 81 EIMQKANEKSGCTSFLPTLITSSDElmkqavrVMREYLAK--------HPNQALGLHLEGPYLNLVKKGTHNPEFIRKPD 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982133 165 --------ANAfhDVLAtygpldnvcIVTLAPELDRShEVIQALTAQGIRVSLGHSVADLRAAEVAVQSGATFITHLFNA 236
Cdd:PRK11170 153 aemvdflcENA--DVIT---------KVTLAPEMVDA-EVIRKLVEAGIVVSAGHSNATYEEAKAGFRAGITFATHLYNA 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982133 237 MLPFHHRDPGIVGLL--TSDqlppghcIFYGMIADGIHTNPAALRIAHRAHPQGLVLVTDAVPALGLGNGRHTLGQQEVE 314
Cdd:PRK11170 221 MPYITGREPGLVGAIldEPD-------VYCGIIADGLHVDYANIRNAKRLKGDKLCLVTDATAPAGANIEQFIFAGKTIY 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982133 315 V-DGLIayIAGTKTLGGSIAPMDVCVRHFLQATGCSVESALEAASLHPAQMLGLEKTKGSLDFGADADFVVLDDTLHVQA 393
Cdd:PRK11170 294 YrDGLC--VDENGTLSGSALTMIEAVRNLVEHVGIALDEALRMATLYPARAIGVDKRLGSIEAGKVANLTAFTRDFKITK 371
|
....*....
gi 31982133 394 TYISGELVW 402
Cdd:PRK11170 372 TIVNGNEVV 380
|
|
| Amidohydro_1 |
pfam01979 |
Amidohydrolase family; This family of enzymes are a a large metal dependent hydrolase ... |
62-401 |
9.26e-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: 77.93 E-value: 9.26e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982133 62 ILAPGFIDVQINGGFGVDFSKAT--EDVGSGVALVARRLLSHGVTSFCPTLVTSPP------EVYHKVlpqipvksggph 133
Cdd:pfam01979 1 IVLPGLIDAHVHLEMGLLRGIPVppEFAYEALRLGITTMLKSGTTTVLDMGATTSTgieallEAAEEL------------ 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982133 134 gagVLGVHLEGPF--ISREKRGAHPEAYLRSF--EANAFHdvlatyGPLDNVCIVTLAPELDRS------HEVIQALTAQ 203
Cdd:pfam01979 69 ---PLGLRFLGPGcsLDTDGELEGRKALREKLkaGAEFIK------GMADGVVFVGLAPHGAPTfsddelKAALEEAKKY 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982133 204 GIRVS--LGHSVADLRAAEVAVQSGATFITHLFNAMLPFHHRDpgivglltsdqlppghciFYGMIADGIHTNPA-ALRI 280
Cdd:pfam01979 140 GLPVAihALETKGEVEDAIAAFGGGIEHGTHLEVAESGGLLDI------------------IKLILAHGVHLSPTeANLL 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982133 281 AHRAHPQGLVLVTDAVPALGlgngRHTLGQQEVEVDGLIAYIaGTKTLG-GSIAPMDVCVR-----HFLQATGCSVESAL 354
Cdd:pfam01979 202 AEHLKGAGVAHCPFSNSKLR----SGRIALRKALEDGVKVGL-GTDGAGsGNSLNMLEELRlalelQFDPEGGLSPLEAL 276
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 31982133 355 EAASLHPAQMLGLEKTKGSLDFGADADFVVLDDTLH-----------VQATYISGELV 401
Cdd:pfam01979 277 RMATINPAKALGLDDKVGSIEVGKDADLVVVDLDPLaaffglkpdgnVKKVIVKGKIV 334
|
|
| HutI |
COG1228 |
Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport ... |
15-404 |
9.89e-14 |
|
Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440841 [Multi-domain] Cd Length: 386 Bit Score: 71.92 E-value: 9.89e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982133 15 FTNCRIL--RGGTLLRE-DLWVRGGRILDPEKLFFEERRVADEQRDCGGRILAPGFIDV---QINGGFGVDFSKATEDVG 88
Cdd:COG1228 12 ITNATLVdgTGGGVIENgTVLVEDGKIAAVGPAADLAVPAGAEVIDATGKTVLPGLIDAhthLGLGGGRAVEFEAGGGIT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982133 89 SGVALV------ARRLLSHGVTSFCptlvtsppevyhkvlpqipVKSGGPHG----------AGVLGVHL--EGPFISRE 150
Cdd:COG1228 92 PTVDLVnpadkrLRRALAAGVTTVR-------------------DLPGGPLGlrdaiiagesKLLPGPRVlaAGPALSLT 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982133 151 KrGAH---PE---AYLRS-FEANA-FHDVLATYGPLDnvcivtlaPELDRSHEVIQALTAQGIRVSlGHsVADLRAAEVA 222
Cdd:COG1228 153 G-GAHargPEearAALRElLAEGAdYIKVFAEGGAPD--------FSLEELRAILEAAHALGLPVA-AH-AHQADDIRLA 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982133 223 VQSGATFITHLFnamlpfhHRDPGIVGLL-----TSdqLPPGHCIFYGMIADGIHTNPAALRIAHRAHPQGLVLVTDA-V 296
Cdd:COG1228 222 VEAGVDSIEHGT-------YLDDEVADLLaeagtVV--LVPTLSLFLALLEGAAAPVAAKARKVREAALANARRLHDAgV 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982133 297 PaLGLGNgrhtlgqqevevDGLIAYIAGTKTLggsiapmdVCVRHFLQAtGCSVESALEAASLHPAQMLGLEKTKGSLDF 376
Cdd:COG1228 293 P-VALGT------------DAGVGVPPGRSLH--------RELALAVEA-GLTPEEALRAATINAAKALGLDDDVGSLEP 350
|
410 420 430
....*....|....*....|....*....|....*.
gi 31982133 377 GADADFVVLD--------DTLHVQATYISGELVWQA 404
Cdd:COG1228 351 GKLADLVLLDgdplediaYLEDVRAVMKDGRVVDRS 386
|
|
| YtcJ |
COG1574 |
Predicted amidohydrolase YtcJ [General function prediction only]; |
349-405 |
2.41e-08 |
|
Predicted amidohydrolase YtcJ [General function prediction only];
Pssm-ID: 441182 [Multi-domain] Cd Length: 535 Bit Score: 55.96 E-value: 2.41e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 31982133 349 SVESALEAASLHPAQMLGLEKTKGSLDFGADADFVVLDD-----------TLHVQATYISGELVWQAE 405
Cdd:COG1574 468 TVEEALRAYTIGAAYAAFEEDEKGSLEPGKLADFVVLDRdpltvppeeikDIKVLLTVVGGRVVYEAE 535
|
|
| AdeC |
COG1001 |
Adenine deaminase [Nucleotide transport and metabolism]; |
335-401 |
1.18e-07 |
|
Adenine deaminase [Nucleotide transport and metabolism];
Pssm-ID: 440625 [Multi-domain] Cd Length: 559 Bit Score: 53.57 E-value: 1.18e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 31982133 335 MDVCVRHFLQAtGCSVESALEAASLHPAQMLGLEKtKGSLDFGADADFVVLDD--TLHVQATYISGELV 401
Cdd:COG1001 272 IDHVVRRAIEL-GLDPVTAIQMATLNAAEHFGLKD-LGAIAPGRRADIVLLDDleDFKVEKVYADGKLV 338
|
|
| AllB |
COG0044 |
Dihydroorotase or related cyclic amidohydrolase [Nucleotide transport and metabolism]; ... |
15-406 |
2.22e-07 |
|
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: 52.79 E-value: 2.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982133 15 FTNCRILRGGTLLREDLWVRGGRILDPEKLFFEERrvADEQRDCGGRILAPGFIDVQINggFGVDFSKATEDVGSG-VAL 93
Cdd:COG0044 2 IKNGRVVDPGGLERADVLIEDGRIAAIGPDLAAPE--AAEVIDATGLLVLPGLIDLHVH--LREPGLEHKEDIETGtRAA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982133 94 VArrllsHGVTSFCPTLVTSPPEVYHKVLpqipvksggphgagvlgvhlegpfisrekrgahpEAYLRSFEANAFHDvla 173
Cdd:COG0044 78 AA-----GGVTTVVDMPNTNPVTDTPEAL----------------------------------EFKLARAEEKALVD--- 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982133 174 tYGPldnvcIVTLAPELDRSHEVIQALTAQGIRV-------SLGHSVADLRAAEVAVQSGATFithlfNAMLPFHHRDPG 246
Cdd:COG0044 116 -VGP-----HGALTKGLGENLAELGALAEAGAVAfkvfmgsDDGNPVLDDGLLRRALEYAAEF-----GALVAVHAEDPD 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982133 247 IV--GLLTSDQLPPghcifygmiADGIHTNPA---------ALRIAH----RAH-------------------------- 285
Cdd:COG0044 185 LIrgGVMNEGKTSP---------RLGLKGRPAeaeeeavarDIALAEetgaRLHivhvstaeavelireakarglpvtae 255
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982133 286 --PQGLVLVTDAVPALGlgngrhTLGQ------QEVEVDGLIAYIA-GT---------------KTLGGSIAP------- 334
Cdd:COG0044 256 vcPHHLTLTDEDLERYG------TNFKvnpplrTEEDREALWEGLAdGTidviatdhaphtleeKELPFAEAPngipgle 329
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982133 335 --MDVCVRHFLQATGCSVESALEAASLHPAQMLGLEKtKGSLDFGADADFVVLD---------DTLH------------- 390
Cdd:COG0044 330 taLPLLLTELVHKGRLSLERLVELLSTNPARIFGLPR-KGRIAVGADADLVLFDpdaewtvtaEDLHskskntpfegrel 408
|
490
....*....|....*....
gi 31982133 391 ---VQATYISGELVWQAEE 406
Cdd:COG0044 409 tgrVVATIVRGRVVYEDGE 427
|
|
| AdeC |
cd01295 |
Adenine deaminase (AdeC) directly deaminates adenine to form hypoxanthine. This reaction is ... |
335-401 |
1.10e-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: 50.30 E-value: 1.10e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 31982133 335 MDVCVRHFLQAtGCSVESALEAASLHPAQMLGLEKtKGSLDFGADADFVVLDD--TLHVQATYISGELV 401
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 ... |
337-401 |
5.94e-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: 48.08 E-value: 5.94e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982133 337 VCVRHflqatGCSVESALEAASLHPAQMLGLEKTKGSLDFGADADFVV-----LDDTLHVQATYISGELV 401
Cdd:cd01309 294 KAVKY-----GLSYEEALKAITINPAKILGIEDRVGSLEPGKDADLVVwngdpLEPTSKPEQVYIDGRLV 358
|
|
| Amidohydro_3 |
pfam07969 |
Amidohydrolase family; |
349-403 |
1.04e-05 |
|
Amidohydrolase family;
Pssm-ID: 400360 [Multi-domain] Cd Length: 464 Bit Score: 47.53 E-value: 1.04e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 31982133 349 SVESALEAASLHPAQMLGLEKTKGSLDFGADADFVVLD-DTLHVQATYISGELVWQ 403
Cdd:pfam07969 400 SLEEALALYTSGPAKALGLEDRKGTLGVGKDADLVVLDdDPLTVDPPAIADIRVRL 455
|
|
| Imidazolone-5PH |
cd01296 |
Imidazolonepropionase/imidazolone-5-propionate hydrolase (Imidazolone-5PH) catalyzes the third ... |
349-386 |
1.45e-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: 46.87 E-value: 1.45e-05
10 20 30
....*....|....*....|....*....|....*...
gi 31982133 349 SVESALEAASLHPAQMLGLEKTKGSLDFGADADFVVLD 386
Cdd:cd01296 311 TPEEALTAATINAAAALGLGETVGSLEVGKQADLVILD 348
|
|
| SsnA |
COG0402 |
Cytosine/adenosine deaminase or related metal-dependent hydrolase [Nucleotide transport and ... |
343-403 |
1.36e-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: 43.66 E-value: 1.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982133 343 LQATGCSVESALEAASLHPAQMLGLEKTKGSLDFGADADFVVLD-DTLH-------------------VQATYISGELVW 402
Cdd:COG0402 335 GDPTALSAREALEMATLGGARALGLDDEIGSLEPGKRADLVVLDlDAPHlaplhdplsalvyaadgrdVRTVWVAGRVVV 414
|
.
gi 31982133 403 Q 403
Cdd:COG0402 415 R 415
|
|
| PRK06189 |
PRK06189 |
allantoinase; Provisional |
344-409 |
4.11e-04 |
|
allantoinase; Provisional
Pssm-ID: 235732 [Multi-domain] Cd Length: 451 Bit Score: 42.38 E-value: 4.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982133 344 QATGCSVESALEAASLHPAQMLGLEKtKGSLDFGADADFVVLD---------DTLH----------------VQATYISG 398
Cdd:PRK06189 349 IERGIPLETIARLLATNPAKRFGLPQ-KGRLEVGADADFVLVDldetytltkEDLFyrhkqspyegrtfpgrVVATYLRG 427
|
90
....*....|.
gi 31982133 399 ELVWQAEEAGP 409
Cdd:PRK06189 428 QCVYQDGEVFP 438
|
|
| Met_dep_hydrolase_A |
cd01299 |
Metallo-dependent hydrolases, subgroup A is part of the superfamily of metallo-dependent ... |
319-386 |
5.06e-04 |
|
Metallo-dependent hydrolases, subgroup A is part of the superfamily of metallo-dependent hydrolases, a large group of proteins that show conservation in their 3-dimensional fold (TIM barrel) and in details of their active site. The vast majority of the members have a conserved metal binding site, involving four histidines and one aspartic acid residue. In the common reaction mechanism, the metal ion (or ions) deprotonate a water molecule for a nucleophilic attack on the substrate. The function of this subgroup is unknown.
Pssm-ID: 238624 [Multi-domain] Cd Length: 342 Bit Score: 41.90 E-value: 5.06e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 31982133 319 IAYIAGTKTLGGSIAPMDVcVRHFLQAT--------GCSVESALEAASLHPAQMLGLEKTKGSLDFGADADFVVLD 386
Cdd:cd01299 258 RAHKAGVKIAFGTDAGFPV-PPHGWNARelellvkaGGTPAEALRAATANAAELLGLSDELGVIEAGKLADLLVVD 332
|
|
| D-aminoacylase |
cd01297 |
D-aminoacylases (N-acyl-D-Amino acid amidohydrolases) catalyze the hydrolysis of ... |
23-402 |
5.63e-04 |
|
D-aminoacylases (N-acyl-D-Amino acid amidohydrolases) catalyze the hydrolysis of N-acyl-D-amino acids to produce the corresponding D-amino acids, which are used as intermediates in the synthesis of pesticides, bioactive peptides, and antibiotics.
Pssm-ID: 238622 [Multi-domain] Cd Length: 415 Bit Score: 41.90 E-value: 5.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982133 23 GGTLLREDLWVRGGRI------LDPEklffeerrvADEQRDCGGRILAPGFIDVQINGGfgvdfSKATEDVGsgvalvAR 96
Cdd:cd01297 14 GAPPFTADVGIRDGRIaaigpiLSTS---------AREVIDAAGLVVAPGFIDVHTHYD-----GQVFWDPD------LR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982133 97 RLLSHGVTSF----CPTLVTSPPEVYHKVLPQIpvksggphGAGVLGVHLEGPFisrekRGAHPEAYLRSFEAN------ 166
Cdd:cd01297 74 PSSRQGVTTVvlgnCGVSPAPANPDDLARLIML--------MEGLVALGEGLPW-----GWATFAEYLDALEARppavnv 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982133 167 ---AFHDVLATYGPLDNVCIVTlAPELDRSHEVI-QALTAQGIRVS--------LGHSVADLRA-AEVAVQSGATFITHL 233
Cdd:cd01297 141 aalVGHAALRRAVMGLDAREAT-EEELAKMRELLrEALEAGALGIStglayaprLYAGTAELVAlARVAARYGGVYQTHV 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982133 234 FNamlPFHHRDPGIVGLLTSD---QLPPGHCIFYGMIADGIHTNPAALRIAHRAHPQGLVLVTDAVP--ALGLGNGRHTL 308
Cdd:cd01297 220 RY---EGDSILEALDELLRLGretGRPVHISHLKSAGAPNWGKIDRLLALIEAARAEGLQVTADVYPygAGSEDDVRRIM 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982133 309 GQQEVEV--DGLIAYIAGTKTLGGSIAPMDVCVRhflQATGCSVESALEAASLHPAQMLGLeKTKGSLDFGADADFVVLD 386
Cdd:cd01297 297 AHPVVMGgsDGGALGKPHPRSYGDFTRVLGHYVR---ERKLLSLEEAVRKMTGLPARVFGL-ADRGRIAPGYRADIVVFD 372
|
410 420 430
....*....|....*....|....*....|.
gi 31982133 387 -DTLH--------------VQATYISGELVW 402
Cdd:cd01297 373 pDTLAdratftrpnqpaegIEAVLVNGVPVV 403
|
|
| PRK09228 |
PRK09228 |
guanine deaminase; Provisional |
354-403 |
1.29e-03 |
|
guanine deaminase; Provisional
Pssm-ID: 236419 [Multi-domain] Cd Length: 433 Bit Score: 40.56 E-value: 1.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982133 354 LEAASLHPAQM-----------LGLEKTKGSLDFGADADFVVLD--------------DTLH--------------VQAT 394
Cdd:PRK09228 343 LQGYRLSPFQAfylatlggaraLGLDDRIGNLAPGKEADFVVLDpaatpllalrtaraESLEellfalmtlgddraVAET 422
|
....*....
gi 31982133 395 YISGELVWQ 403
Cdd:PRK09228 423 YVAGRPVYR 431
|
|
| PRK15446 |
PRK15446 |
phosphonate metabolism protein PhnM; Provisional |
15-104 |
1.95e-03 |
|
phosphonate metabolism protein PhnM; Provisional
Pssm-ID: 237967 [Multi-domain] Cd Length: 383 Bit Score: 40.16 E-value: 1.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982133 15 FTNCRILRGGTLLREDLWVRGGRILDPEklffEERRVADEQRDCGGRILAPGFIDV---QINGGF----GVDFskateDV 87
Cdd:PRK15446 6 LSNARLVLPDEVVDGSLLIEDGRIAAID----PGASALPGAIDAEGDYLLPGLVDLhtdNLEKHLaprpGVDW-----PA 76
|
90
....*....|....*..
gi 31982133 88 GSGVALVARRLLSHGVT 104
Cdd:PRK15446 77 DAALAAHDAQLAAAGIT 93
|
|
| PRK06687 |
PRK06687 |
TRZ/ATZ family protein; |
345-385 |
2.82e-03 |
|
TRZ/ATZ family protein;
Pssm-ID: 180657 [Multi-domain] Cd Length: 419 Bit Score: 39.60 E-value: 2.82e-03
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 31982133 345 ATGCSVESALEAASLHPAQMLGLEKTKGSLDFGADADFVVL 385
Cdd:PRK06687 331 ASQFPIETALKVLTIEGAKALGMENQIGSLEVGKQADFLVI 371
|
|
| PRK07575 |
PRK07575 |
dihydroorotase; Provisional |
17-115 |
3.59e-03 |
|
dihydroorotase; Provisional
Pssm-ID: 236055 [Multi-domain] Cd Length: 438 Bit Score: 39.27 E-value: 3.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31982133 17 NCRI-LRGGTLLREDLWVRGGRIL--DPEklffEERRVADEQRDCGGRILAPGFIDVQinggfgVDFSKA----TEDVGS 89
Cdd:PRK07575 9 NARIlLPSGELLLGDVLVEDGKIVaiAPE----ISATAVDTVIDAEGLTLLPGVIDPQ------VHFREPglehKEDLFT 78
|
90 100
....*....|....*....|....*.
gi 31982133 90 GVALVARrllsHGVTSFCPTLVTSPP 115
Cdd:PRK07575 79 ASRACAK----GGVTSFLEMPNTKPL 100
|
|
| YtcJ_like |
cd01300 |
YtcJ_like metal dependent amidohydrolases. YtcJ is a Bacillus subtilis ORF of unknown function. ... |
349-384 |
5.50e-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: 38.83 E-value: 5.50e-03
10 20 30
....*....|....*....|....*....|....*.
gi 31982133 349 SVESALEAASLHPAQMLGLEKTKGSLDFGADADFVV 384
Cdd:cd01300 444 SLEEALRAYTIGAAYAIGEEDEKGSLEPGKLADFVV 479
|
|
| PRK09237 |
PRK09237 |
amidohydrolase/deacetylase family metallohydrolase; |
327-387 |
5.68e-03 |
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amidohydrolase/deacetylase family metallohydrolase;
Pssm-ID: 236423 [Multi-domain] Cd Length: 380 Bit Score: 38.68 E-value: 5.68e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 31982133 327 TLGGSIAPMDVCVRHFLqATGCSVESALEAASLHPAQMLGLEkTKGSLDFGADADFVVLDD 387
Cdd:PRK09237 276 RINGPVYSLATVMSKFL-ALGMPLEEVIAAVTKNAADALRLP-ELGRLQVGSDADLTLFTL 334
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