|
Name |
Accession |
Description |
Interval |
E-value |
| NagA |
COG1820 |
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism]; |
22-411 |
1.98e-138 |
|
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism];
Pssm-ID: 441425 [Multi-domain] Cd Length: 373 Bit Score: 400.24 E-value: 1.98e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136213 22 AIRDARKVDARGIEEHAWIVADaNGAIAARGTSDDDfeaacrangigTDAVIDASGKIMTPGYVDIHSHGAWEKSFDDG- 100
Cdd:COG1820 1 AITNARIFTGDGVLEDGALLIE-DGRIAAIGPGAEP-----------DAEVIDLGGGYLAPGFIDLHVHGGGGVDFMDGt 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136213 101 PDGIDVARAGHAMHGTTRQVCSLITNPIDVQCENLRNVRAKMDQR--PDILGAHLEGPFLALSRKGAHDPECLKDPVPEI 178
Cdd:COG1820 69 PEALRTIARAHARHGTTSFLPTTITAPPEDLLRALAAIAEAIEQGggAGILGIHLEGPFLSPEKKGAHPPEYIRPPDPEE 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136213 179 VDRMLEAADGCLRQITIAPELPHGLQAIRSFATAGTVPAVGHCDADYETARRAFDEGAGLMTHMFNAMNGLHHRKPGPIP 258
Cdd:COG1820 149 LDRLLEAAGGLIKLVTLAPELPGALEFIRYLVEAGVVVSLGHTDATYEQARAAFEAGATHVTHLFNAMSPLHHREPGVVG 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136213 259 AAVEDPRVTIELICDGFHVQDPMLRLGLG-FAPHRIAFVTDAMAATDCPDGAYKLGALDVDVVDGHARLKsNGAIAGSTL 337
Cdd:COG1820 229 AALDDDDVYAELIADGIHVHPAAVRLALRaKGPDRLILVTDAMAAAGLPDGEYELGGLEVTVKDGVARLA-DGTLAGSTL 307
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 585136213 338 TLEHAVQRAVLELGMSPVEAIEAATLTPARAFGFDRpypvtgaPLGLLAPGYAADVLLTDPaDWSVQHAWCAGR 411
Cdd:COG1820 308 TMDDAVRNLVEWTGLPLEEAVRMASLNPARALGLDD-------RKGSIAPGKDADLVVLDD-DLNVRATWVGGE 373
|
|
| NagA |
cd00854 |
N-acetylglucosamine-6-phosphate deacetylase, NagA, catalyzes the hydrolysis of the N-acetyl ... |
22-410 |
1.96e-137 |
|
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: 397.72 E-value: 1.96e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136213 22 AIRDARKVDARGIEEHAWIVADanGAIAARGTSDDDFEaacrangigTDAVIDASGKIMTPGYVDIHSHGAWEKSFDDG- 100
Cdd:cd00854 2 IIKNARILTPGGLEDGAVLVED--GKIVAIGPEDELEE---------ADEIIDLKGQYLVPGFIDIHIHGGGGADFMDGt 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136213 101 PDGIDVARAGHAMHGTTRQVCSLITNPIDVQCENLRNVRAKMDQ--RPDILGAHLEGPFLALSRKGAHDPECLKDPVPEI 178
Cdd:cd00854 71 AEALKTIAEALAKHGTTSFLPTTVTAPPEEIAKALAAIAEAIAEgqGAEILGIHLEGPFISPEKKGAHPPEYLRAPDPEE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136213 179 VDRMLEAADGCLRQITIAPELPHGLQAIRSFATAGTVPAVGHCDADYETARRAFDEGAGLMTHMFNAMNGLHHRKPGPIP 258
Cdd:cd00854 151 LKKWLEAAGGLIKLVTLAPELDGALELIRYLVERGIIVSIGHSDATYEQAVAAFEAGATHVTHLFNAMSPLHHREPGVVG 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136213 259 AAVEDPRVTIELICDGFHVQDPMLRLGLGFAP-HRIAFVTDAMAATDCPDGAYKLGALDVDVVDGHARLkSNGAIAGSTL 337
Cdd:cd00854 231 AALSDDDVYAELIADGIHVHPAAVRLAYRAKGaDKIVLVTDAMAAAGLPDGEYELGGQTVTVKDGVARL-ADGTLAGSTL 309
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 585136213 338 TLEHAVQRAVLELGMSPVEAIEAATLTPARAFGFDRpypvtgaPLGLLAPGYAADVLLTDPaDWSVQHAWCAG 410
Cdd:cd00854 310 TMDQAVRNMVKWGGCPLEEAVRMASLNPAKLLGLDD-------RKGSLKPGKDADLVVLDD-DLNVKATWING 374
|
|
| nagA |
TIGR00221 |
N-acetylglucosamine-6-phosphate deacetylase; [Central intermediary metabolism, Amino sugars] |
73-411 |
3.23e-64 |
|
N-acetylglucosamine-6-phosphate deacetylase; [Central intermediary metabolism, Amino sugars]
Pssm-ID: 272968 Cd Length: 380 Bit Score: 210.46 E-value: 3.23e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136213 73 IDASGKIMTPGYVDIHSHGAWEKSFDDGP-DGIDVARAGHAMHGTTRQVCSLITNPIDVQCENLRNVRAKMDQRP--DIL 149
Cdd:TIGR00221 47 IDLPGNVLTPGFIDIHIHGCGGVDTNDASfETLEIMSERLPKSGCTSFLPTLITQPDENIKQAVKNMREYLAKEKnaQAL 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136213 150 GAHLEGPFLALSRKGAHDPECLKDPVPEIVDRMLEAADGCLRQITIAPELPHGLQAIRSFATAGTVPAVGHCDADYETAR 229
Cdd:TIGR00221 127 GLHLEGPFLSPEKKGAHPPEYIREPDVELFKKFLCEAGGVITKVTLAPEEDQHFELIRHLKDAGIIVSAGHTNATYELAK 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136213 230 RAFDEGAGLMTHMFNAMNGLHHRKPGPIPAAVEDPRVTIELICDGFHVqDP----MLRLGLGFAphRIAFVTDAMAATDC 305
Cdd:TIGR00221 207 AAFKAGATHATHLYNAMSPIHHREPGVIGAVLDHDDVYTEIIADGIHI-HPlnirLAKKLKGDS--KLCLVTDSMAAAGA 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136213 306 PDGAYKLGALDVDVVDGHArLKSNGAIAGSTLTLEHAVQRAVLELGMSPVEAIEAATLTPARAFG-FDRpypvtgapLGL 384
Cdd:TIGR00221 284 KDGVFIFGGKTVYIREGTC-LDSNGTLAGSSLTMIEGARNLVEFTNISLTDAARMSSLNPARALGiDDR--------LGS 354
|
330 340
....*....|....*....|....*..
gi 585136213 385 LAPGYAADVLLTDPaDWSVQHAWCAGR 411
Cdd:TIGR00221 355 VTVGKDANLVVFTP-DFEVILTIVNGN 380
|
|
| nagA |
PRK11170 |
N-acetylglucosamine-6-phosphate deacetylase; Provisional |
34-391 |
1.71e-54 |
|
N-acetylglucosamine-6-phosphate deacetylase; Provisional
Pssm-ID: 183010 Cd Length: 382 Bit Score: 185.18 E-value: 1.71e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136213 34 IEEHAWIVAdaNGAIaargtsdddfEAACRANGIGTD-AVIDASGKIMTPGYVDIHSHGAWEKSFDDGPDGIDVaRAGHA 112
Cdd:PRK11170 16 LDDHAVVIA--DGLI----------EAVCPVAELPPGiEQRDLNGAILSPGFIDLQLNGCGGVQFNDTAEAISV-ETLEI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136213 113 MH------GTTRQVCSLITNPIDVQCENLRNVRAKMDQRPD-ILGAHLEGPFLALSRKGAHDPECLKDPVPEIVDRMLEA 185
Cdd:PRK11170 83 MQkaneksGCTSFLPTLITSSDELMKQAVRVMREYLAKHPNqALGLHLEGPYLNLVKKGTHNPEFIRKPDAEMVDFLCEN 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136213 186 ADgCLRQITIAPELPhGLQAIRSFATAGTVPAVGHCDADYETARRAFDEGAGLMTHMFNAMNGLHHRKPGPIPAAVEDPR 265
Cdd:PRK11170 163 AD-VITKVTLAPEMV-DAEVIRKLVEAGIVVSAGHSNATYEEAKAGFRAGITFATHLYNAMPYITGREPGLVGAILDEPD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136213 266 VTIELICDGFHVQDPMLRLGLGFAPHRIAFVTDAMAatdcPDGA-------------YKLGaLDVDvvdgharlkSNGAI 332
Cdd:PRK11170 241 VYCGIIADGLHVDYANIRNAKRLKGDKLCLVTDATA----PAGAnieqfifagktiyYRDG-LCVD---------ENGTL 306
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 585136213 333 AGSTLTLEHAVQRAVLELGMSPVEAIEAATLTPARAFGFDrpypvtgAPLGLLAPGYAA 391
Cdd:PRK11170 307 SGSALTMIEAVRNLVEHVGIALDEALRMATLYPARAIGVD-------KRLGSIEAGKVA 358
|
|
| Amidohydro_1 |
pfam01979 |
Amidohydrolase family; This family of enzymes are a a large metal dependent hydrolase ... |
79-398 |
3.74e-14 |
|
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: 72.92 E-value: 3.74e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136213 79 IMTPGYVDIHSHGAWEKSFDDGPDGIDVARAghAMHGTTRQVCSLITNPID---VQCENLRNVRAKMDQRPDILGAHLEG 155
Cdd:pfam01979 1 IVLPGLIDAHVHLEMGLLRGIPVPPEFAYEA--LRLGITTMLKSGTTTVLDmgaTTSTGIEALLEAAEELPLGLRFLGPG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136213 156 PFLALSRKGAHDPECLKDPVPEIVDRMLEAADGCLRQITIAPEL---PHGLQAIRSFATAGTVPAVGHC---DADYETAR 229
Cdd:pfam01979 79 CSLDTDGELEGRKALREKLKAGAEFIKGMADGVVFVGLAPHGAPtfsDDELKAALEEAKKYGLPVAIHAletKGEVEDAI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136213 230 RAFDEGAGLMTHMFNAMNGLHHRKPGPIPAA-----VEDPRVTIELICDGF--HVQDPMLRLGLGFAPHR--------IA 294
Cdd:pfam01979 159 AAFGGGIEHGTHLEVAESGGLLDIIKLILAHgvhlsPTEANLLAEHLKGAGvaHCPFSNSKLRSGRIALRkaledgvkVG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136213 295 FVTDAMAATDCPdgayklgaldvdvvdgharlksNGAIAGSTLTLEHAVQRAvlelGMSPVEAIEAATLTPARAFGFDRp 374
Cdd:pfam01979 239 LGTDGAGSGNSL----------------------NMLEELRLALELQFDPEG----GLSPLEALRMATINPAKALGLDD- 291
|
330 340
....*....|....*....|....
gi 585136213 375 ypvtgaPLGLLAPGYAADVLLTDP 398
Cdd:pfam01979 292 ------KVGSIEVGKDADLVVVDL 309
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| NagA |
COG1820 |
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism]; |
22-411 |
1.98e-138 |
|
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism];
Pssm-ID: 441425 [Multi-domain] Cd Length: 373 Bit Score: 400.24 E-value: 1.98e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136213 22 AIRDARKVDARGIEEHAWIVADaNGAIAARGTSDDDfeaacrangigTDAVIDASGKIMTPGYVDIHSHGAWEKSFDDG- 100
Cdd:COG1820 1 AITNARIFTGDGVLEDGALLIE-DGRIAAIGPGAEP-----------DAEVIDLGGGYLAPGFIDLHVHGGGGVDFMDGt 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136213 101 PDGIDVARAGHAMHGTTRQVCSLITNPIDVQCENLRNVRAKMDQR--PDILGAHLEGPFLALSRKGAHDPECLKDPVPEI 178
Cdd:COG1820 69 PEALRTIARAHARHGTTSFLPTTITAPPEDLLRALAAIAEAIEQGggAGILGIHLEGPFLSPEKKGAHPPEYIRPPDPEE 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136213 179 VDRMLEAADGCLRQITIAPELPHGLQAIRSFATAGTVPAVGHCDADYETARRAFDEGAGLMTHMFNAMNGLHHRKPGPIP 258
Cdd:COG1820 149 LDRLLEAAGGLIKLVTLAPELPGALEFIRYLVEAGVVVSLGHTDATYEQARAAFEAGATHVTHLFNAMSPLHHREPGVVG 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136213 259 AAVEDPRVTIELICDGFHVQDPMLRLGLG-FAPHRIAFVTDAMAATDCPDGAYKLGALDVDVVDGHARLKsNGAIAGSTL 337
Cdd:COG1820 229 AALDDDDVYAELIADGIHVHPAAVRLALRaKGPDRLILVTDAMAAAGLPDGEYELGGLEVTVKDGVARLA-DGTLAGSTL 307
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 585136213 338 TLEHAVQRAVLELGMSPVEAIEAATLTPARAFGFDRpypvtgaPLGLLAPGYAADVLLTDPaDWSVQHAWCAGR 411
Cdd:COG1820 308 TMDDAVRNLVEWTGLPLEEAVRMASLNPARALGLDD-------RKGSIAPGKDADLVVLDD-DLNVRATWVGGE 373
|
|
| NagA |
cd00854 |
N-acetylglucosamine-6-phosphate deacetylase, NagA, catalyzes the hydrolysis of the N-acetyl ... |
22-410 |
1.96e-137 |
|
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: 397.72 E-value: 1.96e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136213 22 AIRDARKVDARGIEEHAWIVADanGAIAARGTSDDDFEaacrangigTDAVIDASGKIMTPGYVDIHSHGAWEKSFDDG- 100
Cdd:cd00854 2 IIKNARILTPGGLEDGAVLVED--GKIVAIGPEDELEE---------ADEIIDLKGQYLVPGFIDIHIHGGGGADFMDGt 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136213 101 PDGIDVARAGHAMHGTTRQVCSLITNPIDVQCENLRNVRAKMDQ--RPDILGAHLEGPFLALSRKGAHDPECLKDPVPEI 178
Cdd:cd00854 71 AEALKTIAEALAKHGTTSFLPTTVTAPPEEIAKALAAIAEAIAEgqGAEILGIHLEGPFISPEKKGAHPPEYLRAPDPEE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136213 179 VDRMLEAADGCLRQITIAPELPHGLQAIRSFATAGTVPAVGHCDADYETARRAFDEGAGLMTHMFNAMNGLHHRKPGPIP 258
Cdd:cd00854 151 LKKWLEAAGGLIKLVTLAPELDGALELIRYLVERGIIVSIGHSDATYEQAVAAFEAGATHVTHLFNAMSPLHHREPGVVG 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136213 259 AAVEDPRVTIELICDGFHVQDPMLRLGLGFAP-HRIAFVTDAMAATDCPDGAYKLGALDVDVVDGHARLkSNGAIAGSTL 337
Cdd:cd00854 231 AALSDDDVYAELIADGIHVHPAAVRLAYRAKGaDKIVLVTDAMAAAGLPDGEYELGGQTVTVKDGVARL-ADGTLAGSTL 309
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 585136213 338 TLEHAVQRAVLELGMSPVEAIEAATLTPARAFGFDRpypvtgaPLGLLAPGYAADVLLTDPaDWSVQHAWCAG 410
Cdd:cd00854 310 TMDQAVRNMVKWGGCPLEEAVRMASLNPAKLLGLDD-------RKGSLKPGKDADLVVLDD-DLNVKATWING 374
|
|
| nagA |
TIGR00221 |
N-acetylglucosamine-6-phosphate deacetylase; [Central intermediary metabolism, Amino sugars] |
73-411 |
3.23e-64 |
|
N-acetylglucosamine-6-phosphate deacetylase; [Central intermediary metabolism, Amino sugars]
Pssm-ID: 272968 Cd Length: 380 Bit Score: 210.46 E-value: 3.23e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136213 73 IDASGKIMTPGYVDIHSHGAWEKSFDDGP-DGIDVARAGHAMHGTTRQVCSLITNPIDVQCENLRNVRAKMDQRP--DIL 149
Cdd:TIGR00221 47 IDLPGNVLTPGFIDIHIHGCGGVDTNDASfETLEIMSERLPKSGCTSFLPTLITQPDENIKQAVKNMREYLAKEKnaQAL 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136213 150 GAHLEGPFLALSRKGAHDPECLKDPVPEIVDRMLEAADGCLRQITIAPELPHGLQAIRSFATAGTVPAVGHCDADYETAR 229
Cdd:TIGR00221 127 GLHLEGPFLSPEKKGAHPPEYIREPDVELFKKFLCEAGGVITKVTLAPEEDQHFELIRHLKDAGIIVSAGHTNATYELAK 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136213 230 RAFDEGAGLMTHMFNAMNGLHHRKPGPIPAAVEDPRVTIELICDGFHVqDP----MLRLGLGFAphRIAFVTDAMAATDC 305
Cdd:TIGR00221 207 AAFKAGATHATHLYNAMSPIHHREPGVIGAVLDHDDVYTEIIADGIHI-HPlnirLAKKLKGDS--KLCLVTDSMAAAGA 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136213 306 PDGAYKLGALDVDVVDGHArLKSNGAIAGSTLTLEHAVQRAVLELGMSPVEAIEAATLTPARAFG-FDRpypvtgapLGL 384
Cdd:TIGR00221 284 KDGVFIFGGKTVYIREGTC-LDSNGTLAGSSLTMIEGARNLVEFTNISLTDAARMSSLNPARALGiDDR--------LGS 354
|
330 340
....*....|....*....|....*..
gi 585136213 385 LAPGYAADVLLTDPaDWSVQHAWCAGR 411
Cdd:TIGR00221 355 VTVGKDANLVVFTP-DFEVILTIVNGN 380
|
|
| nagA |
PRK11170 |
N-acetylglucosamine-6-phosphate deacetylase; Provisional |
34-391 |
1.71e-54 |
|
N-acetylglucosamine-6-phosphate deacetylase; Provisional
Pssm-ID: 183010 Cd Length: 382 Bit Score: 185.18 E-value: 1.71e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136213 34 IEEHAWIVAdaNGAIaargtsdddfEAACRANGIGTD-AVIDASGKIMTPGYVDIHSHGAWEKSFDDGPDGIDVaRAGHA 112
Cdd:PRK11170 16 LDDHAVVIA--DGLI----------EAVCPVAELPPGiEQRDLNGAILSPGFIDLQLNGCGGVQFNDTAEAISV-ETLEI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136213 113 MH------GTTRQVCSLITNPIDVQCENLRNVRAKMDQRPD-ILGAHLEGPFLALSRKGAHDPECLKDPVPEIVDRMLEA 185
Cdd:PRK11170 83 MQkaneksGCTSFLPTLITSSDELMKQAVRVMREYLAKHPNqALGLHLEGPYLNLVKKGTHNPEFIRKPDAEMVDFLCEN 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136213 186 ADgCLRQITIAPELPhGLQAIRSFATAGTVPAVGHCDADYETARRAFDEGAGLMTHMFNAMNGLHHRKPGPIPAAVEDPR 265
Cdd:PRK11170 163 AD-VITKVTLAPEMV-DAEVIRKLVEAGIVVSAGHSNATYEEAKAGFRAGITFATHLYNAMPYITGREPGLVGAILDEPD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136213 266 VTIELICDGFHVQDPMLRLGLGFAPHRIAFVTDAMAatdcPDGA-------------YKLGaLDVDvvdgharlkSNGAI 332
Cdd:PRK11170 241 VYCGIIADGLHVDYANIRNAKRLKGDKLCLVTDATA----PAGAnieqfifagktiyYRDG-LCVD---------ENGTL 306
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 585136213 333 AGSTLTLEHAVQRAVLELGMSPVEAIEAATLTPARAFGFDrpypvtgAPLGLLAPGYAA 391
Cdd:PRK11170 307 SGSALTMIEAVRNLVEHVGIALDEALRMATLYPARAIGVD-------KRLGSIEAGKVA 358
|
|
| Amidohydro_1 |
pfam01979 |
Amidohydrolase family; This family of enzymes are a a large metal dependent hydrolase ... |
79-398 |
3.74e-14 |
|
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: 72.92 E-value: 3.74e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136213 79 IMTPGYVDIHSHGAWEKSFDDGPDGIDVARAghAMHGTTRQVCSLITNPID---VQCENLRNVRAKMDQRPDILGAHLEG 155
Cdd:pfam01979 1 IVLPGLIDAHVHLEMGLLRGIPVPPEFAYEA--LRLGITTMLKSGTTTVLDmgaTTSTGIEALLEAAEELPLGLRFLGPG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136213 156 PFLALSRKGAHDPECLKDPVPEIVDRMLEAADGCLRQITIAPEL---PHGLQAIRSFATAGTVPAVGHC---DADYETAR 229
Cdd:pfam01979 79 CSLDTDGELEGRKALREKLKAGAEFIKGMADGVVFVGLAPHGAPtfsDDELKAALEEAKKYGLPVAIHAletKGEVEDAI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136213 230 RAFDEGAGLMTHMFNAMNGLHHRKPGPIPAA-----VEDPRVTIELICDGF--HVQDPMLRLGLGFAPHR--------IA 294
Cdd:pfam01979 159 AAFGGGIEHGTHLEVAESGGLLDIIKLILAHgvhlsPTEANLLAEHLKGAGvaHCPFSNSKLRSGRIALRkaledgvkVG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136213 295 FVTDAMAATDCPdgayklgaldvdvvdgharlksNGAIAGSTLTLEHAVQRAvlelGMSPVEAIEAATLTPARAFGFDRp 374
Cdd:pfam01979 239 LGTDGAGSGNSL----------------------NMLEELRLALELQFDPEG----GLSPLEALRMATINPAKALGLDD- 291
|
330 340
....*....|....*....|....
gi 585136213 375 ypvtgaPLGLLAPGYAADVLLTDP 398
Cdd:pfam01979 292 ------KVGSIEVGKDADLVVVDL 309
|
|
| AdeC |
COG1001 |
Adenine deaminase [Nucleotide transport and metabolism]; |
290-413 |
6.71e-14 |
|
Adenine deaminase [Nucleotide transport and metabolism];
Pssm-ID: 440625 [Multi-domain] Cd Length: 559 Bit Score: 73.21 E-value: 6.71e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136213 290 PHRIAFVTDamaatdcpdgayklgalDVDVVDgharLKSNGAIagstltlEHAVQRAVlELGMSPVEAIEAATLTPARAF 369
Cdd:COG1001 251 SRRCALCTD-----------------DRHPDD----LLEEGHI-------DHVVRRAI-ELGLDPVTAIQMATLNAAEHF 301
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 585136213 370 GFDRpypvtgapLGLLAPGYAAD-VLLTDPADWSVQHAWCAGRRI 413
Cdd:COG1001 302 GLKD--------LGAIAPGRRADiVLLDDLEDFKVEKVYADGKLV 338
|
|
| HutI |
COG1228 |
Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport ... |
17-397 |
4.13e-11 |
|
Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440841 [Multi-domain] Cd Length: 386 Bit Score: 64.21 E-value: 4.13e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136213 17 APSAFAIRDARKVDARG--IEEHAWIVADaNGAIAARGTSDDDFEAAcrangigTDAVIDASGKIMTPGYVDIHSH---- 90
Cdd:COG1228 6 QAGTLLITNATLVDGTGggVIENGTVLVE-DGKIAAVGPAADLAVPA-------GAEVIDATGKTVLPGLIDAHTHlglg 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136213 91 ----GAWEKSFDDGPDGIDVARAGHA-----MHGTTRqVCSLITNPIDVQCENLRNvRAKMDQRPDILGAhleGPFLALS 161
Cdd:COG1228 78 ggraVEFEAGGGITPTVDLVNPADKRlrralAAGVTT-VRDLPGGPLGLRDAIIAG-ESKLLPGPRVLAA---GPALSLT 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136213 162 rKGAHD---PECLKdpvpeIVDRMLEA--------ADGCLRQITIAPelphgLQAIRSFATAGTVPAVGHCDADyETARR 230
Cdd:COG1228 153 -GGAHArgpEEARA-----ALRELLAEgadyikvfAEGGAPDFSLEE-----LRAILEAAHALGLPVAAHAHQA-DDIRL 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136213 231 AFDEGAGLMTHmfnamnglhhrkpgpIPAAVEDprvTIELICD-GFHVQDPMLRLGLGFAPHRIAFVTDAMAATDC--PD 307
Cdd:COG1228 221 AVEAGVDSIEH---------------GTYLDDE---VADLLAEaGTVVLVPTLSLFLALLEGAAAPVAAKARKVREaaLA 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136213 308 GAYKLGALDVDVV---DGharlkSNGAIAGSTLTLEhaVQRAVlELGMSPVEAIEAATLTPARAFGFDrpypvtgAPLGL 384
Cdd:COG1228 283 NARRLHDAGVPVAlgtDA-----GVGVPPGRSLHRE--LALAV-EAGLTPEEALRAATINAAKALGLD-------DDVGS 347
|
410
....*....|...
gi 585136213 385 LAPGYAADVLLTD 397
Cdd:COG1228 348 LEPGKLADLVLLD 360
|
|
| D-aminoacylase |
cd01297 |
D-aminoacylases (N-acyl-D-Amino acid amidohydrolases) catalyze the hydrolysis of ... |
23-400 |
1.34e-08 |
|
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: 56.54 E-value: 1.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136213 23 IRDARKVDARGieeHAWIVAD---ANGAIAARGTSDddfeaacranGIGTDAVIDASGKIMTPGYVDIHSHgaweksfDD 99
Cdd:cd01297 4 IRNGTVVDGTG---APPFTADvgiRDGRIAAIGPIL----------STSAREVIDAAGLVVAPGFIDVHTH-------YD 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136213 100 GPDGIDVARAGHAMHGTTRQV---CSLITNPIDVQcenlrnVRAKMDQRPDILGAHLEG---------PFLALSRKGAHD 167
Cdd:cd01297 64 GQVFWDPDLRPSSRQGVTTVVlgnCGVSPAPANPD------DLARLIMLMEGLVALGEGlpwgwatfaEYLDALEARPPA 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136213 168 PE--CL---------------KDPVPEIVDRMLEAADGCLRQ----ITIAPELPHGLQA----IRSFATagtvpAVGHCD 222
Cdd:cd01297 138 VNvaALvghaalrravmgldaREATEEELAKMRELLREALEAgalgISTGLAYAPRLYAgtaeLVALAR-----VAARYG 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136213 223 ADYETARR--------AFDE--------GAGLMTHMFNAMNGLHHRKPGPIPAAVEDPRVtielicDGFHVQDPMLRLGL 286
Cdd:cd01297 213 GVYQTHVRyegdsileALDEllrlgretGRPVHISHLKSAGAPNWGKIDRLLALIEAARA------EGLQVTADVYPYGA 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136213 287 GFAPHRIAFVTDAmAATDCPDGayklGALDVdvvdGHARLksngaIAGSTLTLEHAV-QRAVLelgmSPVEAIEAATLTP 365
Cdd:cd01297 287 GSEDDVRRIMAHP-VVMGGSDG----GALGK----PHPRS-----YGDFTRVLGHYVrERKLL----SLEEAVRKMTGLP 348
|
410 420 430
....*....|....*....|....*....|....*.
gi 585136213 366 ARAFG-FDRpypvtgaplGLLAPGYAADVLLTDPAD 400
Cdd:cd01297 349 ARVFGlADR---------GRIAPGYRADIVVFDPDT 375
|
|
| AdeC |
cd01295 |
Adenine deaminase (AdeC) directly deaminates adenine to form hypoxanthine. This reaction is ... |
282-405 |
1.62e-08 |
|
Adenine deaminase (AdeC) directly deaminates adenine to form hypoxanthine. This reaction is part of one of the adenine salvage pathways, as well as the degradation pathway. It is important for adenine utilization as a purine, as well as a nitrogen source in bacteria and archea.
Pssm-ID: 238620 [Multi-domain] Cd Length: 422 Bit Score: 56.08 E-value: 1.62e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136213 282 LRLGLGFAPHRIAFVTDamaatdcpdgayklgalDVDVVDgharLKSNGAIagstltlEHAVQRAVlELGMSPVEAIEAA 361
Cdd:cd01295 194 LPAITEKNFRRFMFCTD-----------------DVHPDD----LLSEGHL-------DYIVRRAI-EAGIPPEDAIQMA 244
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 585136213 362 TLTPARAFGFDrpypvtgaPLGLLAPGYAAD-VLLTDPADWSVQH 405
Cdd:cd01295 245 TINPAECYGLH--------DLGAIAPGRIADiVILDDLENFNITT 281
|
|
| Met_dep_hydrolase_A |
cd01299 |
Metallo-dependent hydrolases, subgroup A is part of the superfamily of metallo-dependent ... |
72-397 |
1.36e-06 |
|
Metallo-dependent hydrolases, subgroup A is part of the superfamily of metallo-dependent hydrolases, a large group of proteins that show conservation in their 3-dimensional fold (TIM barrel) and in details of their active site. The vast majority of the members have a conserved metal binding site, involving four histidines and one aspartic acid residue. In the common reaction mechanism, the metal ion (or ions) deprotonate a water molecule for a nucleophilic attack on the substrate. The function of this subgroup is unknown.
Pssm-ID: 238624 [Multi-domain] Cd Length: 342 Bit Score: 49.98 E-value: 1.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136213 72 VIDASGKIMTPGYVDIHSHGAWEKS----FDDGPDGIDVARAGHAMHGTTRqvcSLITNPIDVQCENLRNVRaKMDQRPD 147
Cdd:cd01299 3 VIDLGGKTLMPGLIDAHTHLGSDPGdlplDLALPVEYRTIRATRQARAALR---AGFTTVRDAGGADYGLLR-DAIDAGL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136213 148 ILGAHLEGPFLALSRKGAHDPEcLKDPVPEIVDRMLEAADG---CLRQitIAPELPHGLQAIRSFATAGTV---PAVGHC 221
Cdd:cd01299 79 IPGPRVFASGRALSQTGGHGDP-RGLSGLFPAGGLAAVVDGveeVRAA--VREQLRRGADQIKIMATGGVLspgDPPPDT 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136213 222 DADYETARRAFDEgaglmTHMFNAMNGLHHRKPGPIPAAVEDPRVTIElicDGFHVQDP----MLRLGLGFAPHRI---A 294
Cdd:cd01299 156 QFSEEELRAIVDE-----AHKAGLYVAAHAYGAEAIRRAIRAGVDTIE---HGFLIDDEtielMKEKGIFLVPTLAtyeA 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136213 295 FVTDAMAATDCPDGAYKLGALDVDVVDGHARLKSNGA--IAGS---TLTLEHAVQRAVLEL----GMSPVEAIEAATLTP 365
Cdd:cd01299 228 LAAEGAAPGLPADSAEKVALVLEAGRDALRRAHKAGVkiAFGTdagFPVPPHGWNARELELlvkaGGTPAEALRAATANA 307
|
330 340 350
....*....|....*....|....*....|..
gi 585136213 366 ARAFGFDrpypvtgAPLGLLAPGYAADVLLTD 397
Cdd:cd01299 308 AELLGLS-------DELGVIEAGKLADLLVVD 332
|
|
| pyrC |
PRK09357 |
dihydroorotase; Validated |
23-90 |
3.07e-05 |
|
dihydroorotase; Validated
Pssm-ID: 236479 [Multi-domain] Cd Length: 423 Bit Score: 45.96 E-value: 3.07e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 585136213 23 IRDARKVDARGIEEHAWIVADaNGAIAARGTsDDDFEAacrangigtDAVIDASGKIMTPGYVDIHSH 90
Cdd:PRK09357 5 IKNGRVIDPKGLDEVADVLID-DGKIAAIGE-NIEAEG---------AEVIDATGLVVAPGLVDLHVH 61
|
|
| COG3653 |
COG3653 |
N-acyl-D-aspartate/D-glutamate deacylase [Secondary metabolites biosynthesis, transport and ... |
23-90 |
4.22e-05 |
|
N-acyl-D-aspartate/D-glutamate deacylase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442870 [Multi-domain] Cd Length: 528 Bit Score: 45.55 E-value: 4.22e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 585136213 23 IRDARKVDARGieeHAWIVAD---ANGAIAARGTSDDdfEAACRangigtdaVIDASGKIMTPGYVDIHSH 90
Cdd:COG3653 6 IRGGTVVDGTG---APPFRADvaiKGGRIVAVGDLAA--AEAAR--------VIDATGLVVAPGFIDIHTH 63
|
|
| Imidazolone-5PH |
cd01296 |
Imidazolonepropionase/imidazolone-5-propionate hydrolase (Imidazolone-5PH) catalyzes the third ... |
41-118 |
7.44e-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: 44.56 E-value: 7.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136213 41 VADANGAIAARGTSDDDfeaacRANGIGTDAVIDASGKIMTPGYVDIHSHGAWEKSFDD-------GPDGIDVARAGHAM 113
Cdd:cd01296 1 IAIRDGRIAAVGPAASL-----PAPGPAAAEEIDAGGRAVTPGLVDCHTHLVFAGDRVDefaarlaGASYEEILAAGGGI 75
|
....*
gi 585136213 114 HGTTR 118
Cdd:cd01296 76 LSTVR 80
|
|
| PRK09061 |
PRK09061 |
D-glutamate deacylase; Validated |
14-91 |
7.84e-05 |
|
D-glutamate deacylase; Validated
Pssm-ID: 236369 [Multi-domain] Cd Length: 509 Bit Score: 44.69 E-value: 7.84e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 585136213 14 MEGAPSAFAIRDARKVD-ARGIEEHAwIVADANGAIAARGTsdddfeaacraNGIGTDAVIDASGKIMTPGYVDIHSHG 91
Cdd:PRK09061 14 ASMAPYDLVIRNGRVVDpETGLDAVR-DVGIKGGKIAAVGT-----------AAIEGDRTIDATGLVVAPGFIDLHAHG 80
|
|
| AllB |
COG0044 |
Dihydroorotase or related cyclic amidohydrolase [Nucleotide transport and metabolism]; ... |
23-90 |
9.42e-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: 44.31 E-value: 9.42e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 585136213 23 IRDARKVDARGIEEhAWIVADaNGAIAARGTSDDDFEAacrangigtDAVIDASGKIMTPGYVDIHSH 90
Cdd:COG0044 2 IKNGRVVDPGGLER-ADVLIE-DGRIAAIGPDLAAPEA---------AEVIDATGLLVLPGLIDLHVH 58
|
|
| COG3964 |
COG3964 |
Predicted amidohydrolase [General function prediction only]; |
23-108 |
1.17e-04 |
|
Predicted amidohydrolase [General function prediction only];
Pssm-ID: 443164 [Multi-domain] Cd Length: 376 Bit Score: 44.00 E-value: 1.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136213 23 IRDARKVD-ARGIEEHAwIVADANGAIAARGTSDDDFEAAcrangigtdAVIDASGKIMTPGYVDIHSHgAWEKSFDDG- 100
Cdd:COG3964 4 IKGGRVIDpANGIDGVM-DIAIKDGKIAAVAKDIDAAEAK---------KVIDASGLYVTPGLIDLHTH-VFPGGTDYGv 72
|
....*....
gi 585136213 101 -PDGIDVAR 108
Cdd:COG3964 73 dPDGVGVRS 81
|
|
| PRK09237 |
PRK09237 |
amidohydrolase/deacetylase family metallohydrolase; |
23-108 |
1.52e-04 |
|
amidohydrolase/deacetylase family metallohydrolase;
Pssm-ID: 236423 [Multi-domain] Cd Length: 380 Bit Score: 43.69 E-value: 1.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136213 23 IRDARKVDARGIEEHAWIVADANGAIAARGTSDDDFEAAcrangigtdAVIDASGKIMTPGYVDIHSHgAWEKSFDDG-- 100
Cdd:PRK09237 3 LRGGRVIDPANGIDGVIDIAIEDGKIAAVAGDIDGSQAK---------KVIDLSGLYVSPGWIDLHVH-VYPGSTPYGde 72
|
....*...
gi 585136213 101 PDGIDVAR 108
Cdd:PRK09237 73 PDEVGVRS 80
|
|
| COG3964 |
COG3964 |
Predicted amidohydrolase [General function prediction only]; |
348-393 |
1.67e-04 |
|
Predicted amidohydrolase [General function prediction only];
Pssm-ID: 443164 [Multi-domain] Cd Length: 376 Bit Score: 43.62 E-value: 1.67e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 585136213 348 LELGMSPVEAIEAATLTPARAFGFDRpypvtgapLGLLAPGYAADV 393
Cdd:COG3964 292 LALGMPLEEVIAAVTWNPARAIGLPE--------LGTLSVGADADI 329
|
|
| SsnA |
COG0402 |
Cytosine/adenosine deaminase or related metal-dependent hydrolase [Nucleotide transport and ... |
352-414 |
1.78e-03 |
|
Cytosine/adenosine deaminase or related metal-dependent hydrolase [Nucleotide transport and metabolism, General function prediction only]; Cytosine/adenosine deaminase or related metal-dependent hydrolase is part of the Pathway/BioSystem: Pyrimidine salvage
Pssm-ID: 440171 [Multi-domain] Cd Length: 416 Bit Score: 40.20 E-value: 1.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136213 352 MSPVEAIEAATLTPARAFGFDrpypvtgAPLGLLAPGYAADVLLTDPADWS-------------------VQHAWCAGRR 412
Cdd:COG0402 340 LSAREALEMATLGGARALGLD-------DEIGSLEPGKRADLVVLDLDAPHlaplhdplsalvyaadgrdVRTVWVAGRV 412
|
..
gi 585136213 413 IK 414
Cdd:COG0402 413 VV 414
|
|
| SsnA |
COG0402 |
Cytosine/adenosine deaminase or related metal-dependent hydrolase [Nucleotide transport and ... |
30-90 |
1.86e-03 |
|
Cytosine/adenosine deaminase or related metal-dependent hydrolase [Nucleotide transport and metabolism, General function prediction only]; Cytosine/adenosine deaminase or related metal-dependent hydrolase is part of the Pathway/BioSystem: Pyrimidine salvage
Pssm-ID: 440171 [Multi-domain] Cd Length: 416 Bit Score: 40.20 E-value: 1.86e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 585136213 30 DARGIEEHAWIVADaNGAIAARGTSDDDFEAAcrangiGTDAVIDASGKIMTPGYVDIHSH 90
Cdd:COG0402 14 PAGGVLEDGAVLVE-DGRIAAVGPGAELPARY------PAAEVIDAGGKLVLPGLVNTHTH 67
|
|
| Met_dep_hydrolase_C |
cd01309 |
Metallo-dependent hydrolases, subgroup C is part of the superfamily of metallo-dependent ... |
72-413 |
2.18e-03 |
|
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: 39.99 E-value: 2.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136213 72 VIDASGKIMTPGYVDIHSH-----GAWEKSFDDGPDGIDV----ARAGHAM----HGTTRQVCSLIT---------NPID 129
Cdd:cd01309 19 VIDAKGKHVTPGLIDAHSHlgldeEGGVRETSDANEETDPvtphVRAIDGInpddEAFKRARAGGVTtvqvlpgsaNLIG 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136213 130 VQCENLRNVRAKMDQrpDILGAHLeGPFLALsrkGAHDPECLKDPVPEIVDRMLEAADgcLRQITI-APELPHGLQAIRS 208
Cdd:cd01309 99 GQGVVIKTDGGTIED--MFIKAPA-GLKMAL---GENPKRVYGGKGKEPATRMGVAAL--LRDAFIkAQEYGRKYDLGKN 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136213 209 FATAGTVPavghcDADYETARRAFDEGAGLMTHMfnamnglhHRkPGPIPAAV-----EDPRVTIELICDGFHVQDPMLR 283
Cdd:cd01309 171 AKKDPPER-----DLKLEALLPVLKGEIPVRIHA--------HR-ADDILTAIriakeFGIKITIEHGAEGYKLADELAK 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136213 284 LGlgfaphriafvtdAMAATDCPDGAYKLGALDVDVVDGHARLKSNGAIAGStLTLEHAV---QRAVLEL------GMSP 354
Cdd:cd01309 237 HG-------------IPVIYGPTLTLPKKVEEVNDAIDTNAYLLKKGGVAFA-ISSDHPVlniRNLNLEAakavkyGLSY 302
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 585136213 355 VEAIEAATLTPARAFGFDRpypvtgaPLGLLAPGYAADVLL--TDP--ADWSVQHAWCAGRRI 413
Cdd:cd01309 303 EEALKAITINPAKILGIED-------RVGSLEPGKDADLVVwnGDPlePTSKPEQVYIDGRLV 358
|
|
| Met_dep_hydrolase_B |
cd01307 |
Metallo-dependent hydrolases, subgroup B is part of the superfamily of metallo-dependent ... |
40-393 |
2.45e-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: 39.62 E-value: 2.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136213 40 IVADANGAIAARGtSDDDFEAACRangigtdaVIDASGKIMTPGYVDIHSHGAWE-KSFDDGPDGIDVARAghamhgttr 118
Cdd:cd01307 1 DVAIENGKIAAVG-AALAAPAATQ--------IVDAGGCYVSPGWIDLHVHVYQGgTRYGDRPDMIGVKSG--------- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136213 119 qvcslITNPIDV---QCENLRNVRAKM--DQRPDILGahlegpFLALSRKGAHdpECLKDPVPEIVDrmleaADGCLRQI 193
Cdd:cd01307 63 -----VTTVVDAgsaGADNIDGFRYTVieRSATRVYA------FLNISRVGLV--AQDELPDPDNID-----EDAVVAAA 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136213 194 TIAPELPHGLQA---IRSFATAGTVPA-----------------VGHCDADYETARRAFDEGaGLMTHMFNamnglhhRK 253
Cdd:cd01307 125 REYPDVIVGLKArasKSVVGEWGIKPLelakkiakeadlplmvhIGSPPPILDEVVPLLRRG-DVLTHCFN-------GK 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585136213 254 PGPIPAAVEDPRVTIE------LICD--------GFHVQDPMLRLGLgfAPHRIAfvtdamaatdcpdgayklgaldvdv 319
Cdd:cd01307 197 PNGIVDEEGEVLPLVRrarergVIFDvghgtasfSFRVARAAIAAGL--LPDTIS------------------------- 249
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 585136213 320 VDGHARLKSNGAIAGSTLTLEhavqrAVLELGMSPVEAIEAATLTPARAFGFDRpypvtgapLGLLAPGYAADV 393
Cdd:cd01307 250 SDIHGRNRTNGPVYALATTLS-----KLLALGMPLEEVIEAVTANPARMLGLAE--------IGTLAVGYDADL 310
|
|
| PRK15446 |
PRK15446 |
phosphonate metabolism protein PhnM; Provisional |
341-413 |
4.73e-03 |
|
phosphonate metabolism protein PhnM; Provisional
Pssm-ID: 237967 [Multi-domain] Cd Length: 383 Bit Score: 39.01 E-value: 4.73e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 585136213 341 HAVQRAVLELGMSPVEAIEAATLTPARAFGF-DRpypvtgaplGLLAPGYAADVLLTDPADWS--VQHAWCAGRRI 413
Cdd:PRK15446 313 DAAFRLADDGGLDLPQAVALVTANPARAAGLdDR---------GEIAPGKRADLVRVRRAGGLpvVRAVWRGGRRV 379
|
|
| FwdA |
COG1229 |
Formylmethanofuran dehydrogenase subunit A [Energy production and conversion]; |
70-90 |
4.94e-03 |
|
Formylmethanofuran dehydrogenase subunit A [Energy production and conversion];
Pssm-ID: 440842 Cd Length: 554 Bit Score: 39.02 E-value: 4.94e-03
|
|