|
Name |
Accession |
Description |
Interval |
E-value |
| COG3653 |
COG3653 |
N-acyl-D-aspartate/D-glutamate deacylase [Secondary metabolites biosynthesis, transport and ... |
3-478 |
2.55e-176 |
|
N-acyl-D-aspartate/D-glutamate deacylase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442870 [Multi-domain] Cd Length: 528 Bit Score: 505.48 E-value: 2.55e-176
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224246933 3 YDTLIRNALVIDGSNAPGYAADVALLNGRIERIGDLHDARASEQIDAAGRVLAPGFIDVHTHDDTVVIRQPQMLPKLSQG 82
Cdd:COG3653 2 FDLLIRGGTVVDGTGAPPFRADVAIKGGRIVAVGDLAAAEAARVIDATGLVVAPGFIDIHTHYDLQLLWDPRLEPSLRQG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224246933 83 VTTVIVGNCGISAAPVSlRGDPPDPMNLLGTSAA------FVYPTFRDYREAVEAANTTLNVAALVGHTALRSNHLDDLL 156
Cdd:COG3653 82 VTTVVMGNCGVSFAPVR-PEDRDRLIDLMEGVEGipegldWDWESFGEYLDALERRGLGVNVASLVGHGTLRAYVMGLDD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224246933 157 RSASAEEITAMREQLRESLEAGALGLSTGLAYASAFSASTDEVMQLSEELTAFGAVYTTHLRSEFAPVLEAMDEAFQIGR 236
Cdd:COG3653 161 RPPTPEELARMRALLREAMEAGALGLSTGLIYVPGTYASTDELVALAKVVAEYGGVYQSHMRDEGDGLLEAVDELIRIGR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224246933 237 HAKSPVIISHLKCAGVGNWGRSPQLLAALETA-AQSHPVGCDCYPYAASSSTLD---------------LKQVTDA---- 296
Cdd:COG3653 241 EAGVPVHISHLKAAGKPNWGKADEVLALIEAArAEGLDVTADVYPYPAGSTGLGallppwaaagglderLARLRDPatra 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224246933 297 --------------------HRITITWSTPHPELGGRDLIDIAADWNVPLLDAARRL-----QPAGAVYYGMDEADVRRI 351
Cdd:COG3653 321 riraeieeglpdnllgrggwDNILISDSPPNEPLVGKSLAEIAAERGVDPADAALDLlleedGRVLIVYFIMSEEDVREL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224246933 352 LAHPLSMVGSDGLPEDPfPHPRLWGAFPRVLGHFSRDVGLFPLHTAVHKMTGLSAARFGLKQRGEIRAGHWADLVLFDPL 431
Cdd:COG3653 401 LRHPWVMIGSDGGLGGK-AHPRAYGTFPRVLGHYVRERGVLSLEEAVRKLTSLPADRLGLKDRGLLRPGYRADLVVFDPA 479
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 1224246933 432 TIRDVADFHDPQRAAEGIDGVWINGVLSYVDGKANGRRAGRFLAREG 478
Cdd:COG3653 480 TLADRATFDLPAQRADGIRAVIVNGVVVVEDGKPTGARPGRVLRGGG 526
|
|
| D-aminoacylase |
cd01297 |
D-aminoacylases (N-acyl-D-Amino acid amidohydrolases) catalyze the hydrolysis of ... |
4-472 |
1.18e-172 |
|
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: 491.81 E-value: 1.18e-172
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224246933 4 DTLIRNALVIDGSNAPGYAADVALLNGRIERIGDLHDARASEQIDAAGRVLAPGFIDVHTHDDTVVIRQPQMLPKLSQGV 83
Cdd:cd01297 1 DLVIRNGTVVDGTGAPPFTADVGIRDGRIAAIGPILSTSAREVIDAAGLVVAPGFIDVHTHYDGQVFWDPDLRPSSRQGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224246933 84 TTVIVGNCGISAAPVSLRGDPPDPMNLLGTSA-----AFVYPTFRDYREAVEAANTTLNVAALVGHTALRSNHLDDLLRS 158
Cdd:cd01297 81 TTVVLGNCGVSPAPANPDDLARLIMLMEGLVAlgeglPWGWATFAEYLDALEARPPAVNVAALVGHAALRRAVMGLDARE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224246933 159 ASAEEITAMREQLRESLEAGALGLSTGLAYASAFSASTDEVMQLSEELTAFGAVYTTHLRSEFAPVLEAMDEAFQIGRHA 238
Cdd:cd01297 161 ATEEELAKMRELLREALEAGALGISTGLAYAPRLYAGTAELVALARVAARYGGVYQTHVRYEGDSILEALDELLRLGRET 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224246933 239 KSPVIISHLKCAGVGNWGRSPQLLAALETA-AQSHPVGCDCYPYAASSstldlkqvtdahrititwstphpelggrdlid 317
Cdd:cd01297 241 GRPVHISHLKSAGAPNWGKIDRLLALIEAArAEGLQVTADVYPYGAGS-------------------------------- 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224246933 318 iaadwnvplldaarrlqpagavyygmdEADVRRILAHPLSMVGSDGLPEdPFPHPRLWGAFPRVLGHFSRDVGLFPLHTA 397
Cdd:cd01297 289 ---------------------------EDDVRRIMAHPVVMGGSDGGAL-GKPHPRSYGDFTRVLGHYVRERKLLSLEEA 340
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1224246933 398 VHKMTGLSAARFGLKQRGEIRAGHWADLVLFDPLTIRDVADFHDPQRAAEGIDGVWINGVLSYVDGKANGRRAGR 472
Cdd:cd01297 341 VRKMTGLPARVFGLADRGRIAPGYRADIVVFDPDTLADRATFTRPNQPAEGIEAVLVNGVPVVRDGAFTGARPGR 415
|
|
| PRK09061 |
PRK09061 |
D-glutamate deacylase; Validated |
3-477 |
2.72e-43 |
|
D-glutamate deacylase; Validated
Pssm-ID: 236369 [Multi-domain] Cd Length: 509 Bit Score: 159.86 E-value: 2.72e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224246933 3 YDTLIRNALVIDGSNAPGYAADVALLNGRIERIGdlHDARASEQ-IDAAGRVLAPGFIDVHTHDDTVVIRQPQMLpklsQ 81
Cdd:PRK09061 19 YDLVIRNGRVVDPETGLDAVRDVGIKGGKIAAVG--TAAIEGDRtIDATGLVVAPGFIDLHAHGQSVAAYRMQAF----D 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224246933 82 GVTTVIVGNCGisaapvslrgdppdpmnllgtsaafVYPTFRDYREAvEAANTTLNVAALVGHTALR---------SNHL 152
Cdd:PRK09061 93 GVTTALELEAG-------------------------VLPVARWYAEQ-AGEGRPLNYGASVGWTPARiavltgpqaEGTI 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224246933 153 DDLL----------RSASAEEITAMREQLRESLEAGALGLSTGLAYASAFSAStdEVMQLSEELTAFGAVYTTHLR---- 218
Cdd:PRK09061 147 ADFGkalgdprwqeRAATPAELAEILELLEQGLDEGALGIGIGAGYAPGTGHK--EYLELARLAARAGVPTYTHVRylsn 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224246933 219 ----SEFAPVLEAMDEAFQIGRHakspVIISHLKCAGVGNwgrSPQLLAALETA-AQSHPVGCDCYPYAASSSTL----- 288
Cdd:PRK09061 225 vdprSSVDAYQELIAAAAETGAH----MHICHVNSTSLRD---IDRCLALVEKAqAQGLDVTTEAYPYGAGSTVVgaaff 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224246933 289 --DLKQVTDAHRITITWSTPHPELGGRDLidiaadwnvplLDAARRLQPAGAVYYGM-------DEADVRRILAHPLSMV 359
Cdd:PRK09061 298 dpGWLERMGLGYGSLQWVETGERLLTREE-----------LAKLRANDPGGLVLIHFldednprDRALLDRSVLFPGAAI 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224246933 360 GSDG-----------------LPEDPFPHPRLWGAFPRVLGHFSRDVGLFPLHTAVHKMTGLSAARFG-----LKQRGEI 417
Cdd:PRK09061 367 ASDAmpwtwsdgtvyegdawpLPEDAVSHPRSAGTFARFLREYVRERKALSLLEAIRKCTLMPAQILEdsvpaMRRKGRL 446
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1224246933 418 RAGHWADLVLFDPLTIRDVADFHDPQRAAEGIDGVWINGVLSYVDGKAN-GRRAGRFLARE 477
Cdd:PRK09061 447 QAGADADIVVFDPETITDRATFEDPNRPSEGVRHVLVNGVPVVSNGELVrDARPGRPVRRP 507
|
|
| Amidohydro_3 |
pfam07969 |
Amidohydrolase family; |
47-460 |
2.02e-39 |
|
Amidohydrolase family;
Pssm-ID: 400360 [Multi-domain] Cd Length: 464 Bit Score: 148.45 E-value: 2.02e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224246933 47 IDAAGRVLAPGFIDVHTHDDT-----VVIRQPQMLPKlsqgvtTVIVGNCGISAAPVSLRGDPPDpmnllgtSAAFVYPT 121
Cdd:pfam07969 3 IDAKGRLVLPGFVDPHTHLDGgglnlRELRLPDVLPN------AVVKGQAGRTPKGRWLVGEGWD-------EAQFAETR 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224246933 122 FRDYREAVEAA--NTTLNVAALVGHTALRSNHLDDLLRSASAEEITAMREQLRESLEAGALGLSTGLAYASAFSASTDE- 198
Cdd:pfam07969 70 FPYALADLDEVapDGPVLLRALHTHAAVANSAALDLAGITKATEDPPGGEIARDANGEGLTGLLREGAYALPPLLAREAe 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224246933 199 ---VMQLSEELTAFG------AVYTTHLRSEFAPVLEAMDEAF----------QIGRHAKSPVIISHLKCAGVGNWGRSP 259
Cdd:pfam07969 150 aaaVAAALAALPGFGitsvdgGGGNVHSLDDYEPLRELTAAEKlkelldaperLGLPHSIYELRIGAMKLFADGVLGSRT 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224246933 260 QLL------------------AALETAAQSHPVGCDCYPYAASSSTLDLKQVTDAhRITITWStphpeLGGRDLID---I 318
Cdd:pfam07969 230 AALtepyfdapgtgwpdfedeALAELVAAARERGLDVAIHAIGDATIDTALDAFE-AVAEKLG-----NQGRVRIEhaqG 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224246933 319 AADWNVPLLDAARRLQPAGAVYYGMDEAD------------------VRRILAHPLSMV-GSDGLPEDPFPHPRLWGAFP 379
Cdd:pfam07969 304 VVPYTYSQIERVAALGGAAGVQPVFDPLWgdwlqdrlgaerargltpVKELLNAGVKVAlGSDAPVGPFDPWPRIGAAVM 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224246933 380 R---VLGHFSRDVGLFPLHTAVHKMTGLSAARFGLKQR-GEIRAGHWADLVLFDpltiRDVADFHDPQRAAEGIDGVWIN 455
Cdd:pfam07969 384 RqtaGGGEVLGPDEELSLEEALALYTSGPAKALGLEDRkGTLGVGKDADLVVLD----DDPLTVDPPAIADIRVRLTVVD 459
|
....*
gi 1224246933 456 GVLSY 460
Cdd:pfam07969 460 GRVVY 464
|
|
| AllB |
COG0044 |
Dihydroorotase or related cyclic amidohydrolase [Nucleotide transport and metabolism]; ... |
6-476 |
1.82e-20 |
|
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: 93.62 E-value: 1.82e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224246933 6 LIRNALVIDGSNApgYAADVALLNGRIERIG-DLHDARASEQIDAAGRVLAPGFIDVHTHddtvvIRQPQMLPK------ 78
Cdd:COG0044 1 LIKNGRVVDPGGL--ERADVLIEDGRIAAIGpDLAAPEAAEVIDATGLLVLPGLIDLHVH-----LREPGLEHKedietg 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224246933 79 ----LSQGVTTVIvgncgisaapvslrgDPPDPMNLLGTSAAfvyptFRDYREAVEAANTTlNVAALVGHTALRSNHLDd 154
Cdd:COG0044 74 traaAAGGVTTVV---------------DMPNTNPVTDTPEA-----LEFKLARAEEKALV-DVGPHGALTKGLGENLA- 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224246933 155 llrsasaeEITAMReqlreslEAGALGLSTGLAYASAFSASTDEVMQLS-EELTAFGAVYTTH----------LRSE--F 221
Cdd:COG0044 132 --------ELGALA-------EAGAVAFKVFMGSDDGNPVLDDGLLRRAlEYAAEFGALVAVHaedpdlirggVMNEgkT 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224246933 222 APVL-----------EAMDEAFQIGRHAKSPVIISHLKCAGVgnwgrspqlLAALETA-AQSHPVGCDCypyaassstld 289
Cdd:COG0044 197 SPRLglkgrpaeaeeEAVARDIALAEETGARLHIVHVSTAEA---------VELIREAkARGLPVTAEV----------- 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224246933 290 lkqvtdahrititwsTPH---------PELGGRdlidiaADWNVPLldaaRrlqpagavyygmDEADVRRILAH----PL 356
Cdd:COG0044 257 ---------------CPHhltltdedlERYGTN------FKVNPPL----R------------TEEDREALWEGladgTI 299
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224246933 357 SMVGSDGLP------EDPFPH-----PRLWGAFPRVLGHFSRDvGLFPLHTAVHKMTGLSAARFGLKQRGEIRAGHWADL 425
Cdd:COG0044 300 DVIATDHAPhtleekELPFAEapngiPGLETALPLLLTELVHK-GRLSLERLVELLSTNPARIFGLPRKGRIAVGADADL 378
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1224246933 426 VLFDP---LTIrDVADFHDPQR--AAEG------IDGVWINGVLSYVDGKANGRRAGRFLAR 476
Cdd:COG0044 379 VLFDPdaeWTV-TAEDLHSKSKntPFEGreltgrVVATIVRGRVVYEDGEVVGEPRGRFLRR 439
|
|
| COG3964 |
COG3964 |
Predicted amidohydrolase [General function prediction only]; |
4-92 |
1.84e-14 |
|
Predicted amidohydrolase [General function prediction only];
Pssm-ID: 443164 [Multi-domain] Cd Length: 376 Bit Score: 74.82 E-value: 1.84e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224246933 4 DTLIRNALVIDGSNAPGYAADVALLNGRIERIG-DLHDARASEQIDAAGRVLAPGFIDVHTH-----------DDTVVIR 71
Cdd:COG3964 1 DLLIKGGRVIDPANGIDGVMDIAIKDGKIAAVAkDIDAAEAKKVIDASGLYVTPGLIDLHTHvfpggtdygvdPDGVGVR 80
|
90 100
....*....|....*....|..
gi 1224246933 72 qpqmlpklsQGVTTVI-VGNCG 92
Cdd:COG3964 81 ---------SGVTTVVdAGSAG 93
|
|
| PRK09237 |
PRK09237 |
amidohydrolase/deacetylase family metallohydrolase; |
6-92 |
2.08e-12 |
|
amidohydrolase/deacetylase family metallohydrolase;
Pssm-ID: 236423 [Multi-domain] Cd Length: 380 Bit Score: 68.34 E-value: 2.08e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224246933 6 LIRNALVIDGSNAPGYAADVALLNGRIERIG-DLHDARASEQIDAAGRVLAPGFIDVHTH-----------DDTVVIRqp 73
Cdd:PRK09237 2 LLRGGRVIDPANGIDGVIDIAIEDGKIAAVAgDIDGSQAKKVIDLSGLYVSPGWIDLHVHvypgstpygdePDEVGVR-- 79
|
90 100
....*....|....*....|
gi 1224246933 74 qmlpklsQGVTTVI-VGNCG 92
Cdd:PRK09237 80 -------SGVTTVVdAGSAG 92
|
|
| PRK02382 |
PRK02382 |
dihydroorotase; Provisional |
7-481 |
6.40e-12 |
|
dihydroorotase; Provisional
Pssm-ID: 179417 [Multi-domain] Cd Length: 443 Bit Score: 67.37 E-value: 6.40e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224246933 7 IRNALVIDG---SNAPGYAADVALLNGRIERIGDLHDARASEQ-IDAAGRVLAPGFIDVHTHddtvvIRQPQMLPK---- 78
Cdd:PRK02382 1 MRDALLKDGrvyYNNSLQPRDVRIDGGKITAVGKDLDGSSSEEvIDARGMLLLPGGIDVHVH-----FREPGYTHKetwy 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224246933 79 ------LSQGVTTVIvgncgisaapvslrgDPP--DPmnllgtsaafvyPTF--RDYREAVE-AANTTLNVAALVGHTAL 147
Cdd:PRK02382 76 tgsrsaAAGGVTTVV---------------DQPntDP------------PTVdgESFDEKAElAARKSIVDFGINGGVTG 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224246933 148 RSNHLDDLLRsasaEEITAMREQ-LRESleAGALGLStglayASAFSASTDEVMQLseeltafGAVYTTHLRSEfapvlE 226
Cdd:PRK02382 129 NWDPLESLWE----RGVFALGEIfMADS--TGGMGID-----EELFEEALAEAARL-------GVLATVHAEDE-----D 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224246933 227 AMDEAFQIGRHAKSPVIISHLKCAGvgnwGRSPQLLAALETAAQShpvgcDCYPYAASSSTLDLKQVTDAHRITiTWSTP 306
Cdd:PRK02382 186 LFDELAKLLKGDADADAWSAYRPAA----AEAAAVERALEVASET-----GARIHIAHISTPEGVDAARREGIT-CEVTP 255
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224246933 307 HPELGGRDlidiaaDW---------NVPLLDAARRlqpagavyygmdEADVRRILAHPLSMVGSDGLPEDPF-PHPRLWG 376
Cdd:PRK02382 256 HHLFLSRR------DWerlgtfgkmNPPLRSEKRR------------EALWERLNDGTIDVVASDHAPHTREeKDADIWD 317
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224246933 377 A----------FPRVLGHFSRdvGLFPLHTAVHKMTGLSAARFGLKQRGEIRAGHWADLVLFDPLTIR--DVADFHdpQR 444
Cdd:PRK02382 318 ApsgvpgvetmLPLLLAAVRK--NRLPLERVRDVTAANPARIFGLDGKGRIAEGYDADLVLVDPDAAReiRGDDLH--SK 393
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 1224246933 445 AA----EGIDGVW-----INGVLSYVDGKANGRR-AGRFLAREGDLR 481
Cdd:PRK02382 394 AGwtpfEGMEGVFpeltmVRGTVVWDGDDINAKRgRGEFLRGRGYER 440
|
|
| PRK06189 |
PRK06189 |
allantoinase; Provisional |
1-477 |
9.27e-12 |
|
allantoinase; Provisional
Pssm-ID: 235732 [Multi-domain] Cd Length: 451 Bit Score: 67.03 E-value: 9.27e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224246933 1 MLYDTLIRNALVI--DGSnapgYAADVALLNGRIERIGDLHDARASEQIDAAGRVLAPGFIDVHTHDDTvvirqpqmlPK 78
Cdd:PRK06189 1 MMYDLIIRGGKVVtpEGV----YRADIGIKNGKIAEIAPEISSPAREIIDADGLYVFPGMIDVHVHFNE---------PG 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224246933 79 LS--QGVTTvivGNCGISAAPVSLRGDppdpMNLLGTSAAFVYPTFRDYREAVEAANTTlnVAALVGhtALRSNHLDdll 156
Cdd:PRK06189 68 RThwEGFAT---GSAALAAGGCTTYFD----MPLNSIPPTVTREALDAKAELARQKSAV--DFALWG--GLVPGNLE--- 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224246933 157 rsasaeeitamreQLRESLEAGALGLStglAYASafSASTDEvMQLSEELTafgavytthlrsefapVLEAMDEAFQIGR 236
Cdd:PRK06189 134 -------------HLRELAEAGVIGFK---AFMS--NSGTDE-FRSSDDLT----------------LYEGMKEIAALGK 178
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224246933 237 ----HAKSPVIISHL-------KCAGVGNWGRS-PQ----------LLAALETAAQSHPVgcdcypYAASSSTLDLKQVT 294
Cdd:PRK06189 179 ilalHAESDALTRHLttqarqqGKTDVRDYLESrPVvaeleavqraLLYAQETGCPLHFV------HISSGKAVALIAEA 252
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224246933 295 DAHRITITWST-PHPEL-GGRDLIDI--AADWNVPLLDAARRlqpagavyygmdEADVRRILAHPLSMVGSDGLP----- 365
Cdd:PRK06189 253 KKRGVDVSVETcPHYLLfTEEDFERIgaVAKCAPPLRSRSQK------------EELWRGLLAGEIDMISSDHSPcppel 320
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224246933 366 ---EDPFphpRLWGAFPRV---------LGHFSRDVglfPLHTAVHKMTGLSAARFGLKQRGEIRAGHWADLVLFDP--- 430
Cdd:PRK06189 321 kegDDFF---LVWGGISGGqstllvmltEGYIERGI---PLETIARLLATNPAKRFGLPQKGRLEVGADADFVLVDLdet 394
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 1224246933 431 --LTIRDVADFHdPQRAAEG------IDGVWINGVLSYVDGKANGRRAGRFLARE 477
Cdd:PRK06189 395 ytLTKEDLFYRH-KQSPYEGrtfpgrVVATYLRGQCVYQDGEVFPPPRGQLLRPS 448
|
|
| pyrC |
PRK09357 |
dihydroorotase; Validated |
5-64 |
1.34e-11 |
|
dihydroorotase; Validated
Pssm-ID: 236479 [Multi-domain] Cd Length: 423 Bit Score: 66.37 E-value: 1.34e-11
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224246933 5 TLIRNALVIDGSNApGYAADVALLNGRIERIGDLHDARASEQIDAAGRVLAPGFIDVHTH 64
Cdd:PRK09357 3 ILIKNGRVIDPKGL-DEVADVLIDDGKIAAIGENIEAEGAEVIDATGLVVAPGLVDLHVH 61
|
|
| SsnA |
COG0402 |
Cytosine/adenosine deaminase or related metal-dependent hydrolase [Nucleotide transport and ... |
4-64 |
2.71e-10 |
|
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: 62.15 E-value: 2.71e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1224246933 4 DTLIRNALVIDGSNAPGYAADVALL--NGRIERIGDLHDARAS----EQIDAAGRVLAPGFIDVHTH 64
Cdd:COG0402 1 DLLIRGAWVLTMDPAGGVLEDGAVLveDGRIAAVGPGAELPARypaaEVIDAGGKLVLPGLVNTHTH 67
|
|
| PRK08323 |
PRK08323 |
phenylhydantoinase; Validated |
3-64 |
3.38e-10 |
|
phenylhydantoinase; Validated
Pssm-ID: 236240 [Multi-domain] Cd Length: 459 Bit Score: 62.11 E-value: 3.38e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1224246933 3 YDTLIRNALVIDGSNApgYAADVALLNGRIERIGDlhdARASEQIDAAGRVLAPGFIDVHTH 64
Cdd:PRK08323 1 MSTLIKNGTVVTADDT--YKADVLIEDGKIAAIGA---NLGDEVIDATGKYVMPGGIDPHTH 57
|
|
| AdeC |
COG1001 |
Adenine deaminase [Nucleotide transport and metabolism]; |
4-87 |
9.29e-10 |
|
Adenine deaminase [Nucleotide transport and metabolism];
Pssm-ID: 440625 [Multi-domain] Cd Length: 559 Bit Score: 60.88 E-value: 9.29e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224246933 4 DTLIRNALVIDGSNAPGYAADVALLNGRIERIGDlHDARASEQIDAAGRVLAPGFIDVHTHddtvvIRQPQMLPK----- 78
Cdd:COG1001 6 DLVIKNGRLVNVFTGEILEGDIAIAGGRIAGVGD-YIGEATEVIDAAGRYLVPGFIDGHVH-----IESSMVTPAefara 79
|
90
....*....|
gi 1224246933 79 -LSQGVTTVI 87
Cdd:COG1001 80 vLPHGTTTVI 89
|
|
| D-HYD |
cd01314 |
D-hydantoinases (D-HYD) also called dihydropyrimidases (DHPase) and related proteins; DHPases ... |
5-64 |
1.35e-09 |
|
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: 59.92 E-value: 1.35e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1224246933 5 TLIRNALVIDGSNApgYAADVALLNGRIERIG-DLHDARASEQIDAAGRVLAPGFIDVHTH 64
Cdd:cd01314 1 LIIKNGTIVTADGS--FKADILIEDGKIVAIGpNLEAPGGVEVIDATGKYVLPGGIDPHTH 59
|
|
| YtcJ |
COG1574 |
Predicted amidohydrolase YtcJ [General function prediction only]; |
4-64 |
1.44e-09 |
|
Predicted amidohydrolase YtcJ [General function prediction only];
Pssm-ID: 441182 [Multi-domain] Cd Length: 535 Bit Score: 60.20 E-value: 1.44e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1224246933 4 DTLIRNALVIDGSNAPGYAADVALLNGRIERIGDLHDARA-----SEQIDAAGRVLAPGFIDVHTH 64
Cdd:COG1574 9 DLLLTNGRIYTMDPAQPVAEAVAVRDGRIVAVGSDAEVRAlagpaTEVIDLGGKTVLPGFIDAHVH 74
|
|
| HutI |
COG1228 |
Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport ... |
4-86 |
2.07e-09 |
|
Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440841 [Multi-domain] Cd Length: 386 Bit Score: 59.20 E-value: 2.07e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224246933 4 DTLIRNALVIDGSNAPGYA-ADVALLNGRIERIGDLHDARAS---EQIDAAGRVLAPGFIDVHTH--------------- 64
Cdd:COG1228 9 TLLITNATLVDGTGGGVIEnGTVLVEDGKIAAVGPAADLAVPagaEVIDATGKTVLPGLIDAHTHlglgggravefeagg 88
|
90 100
....*....|....*....|....*..
gi 1224246933 65 ----DDTVVIRQPQMLPK-LSQGVTTV 86
Cdd:COG1228 89 gitpTVDLVNPADKRLRRaLAAGVTTV 115
|
|
| L-HYD_ALN |
cd01315 |
L-Hydantoinases (L-HYDs) and Allantoinase (ALN); L-Hydantoinases are a member of the ... |
4-430 |
4.70e-09 |
|
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: 58.45 E-value: 4.70e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224246933 4 DTLIRNALVIDGSNApgYAADVALLNGRIERIG-DLHDARASEQIDAAGRVLAPGFIDVHTHddtvvIRQP--------- 73
Cdd:cd01315 1 DLVIKNGRVVTPDGV--READIAVKGGKIAAIGpDIANTEAEEVIDAGGLVVMPGLIDTHVH-----INEPgrtewegfe 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224246933 74 ---QMLPKlsQGVTTVIvgncgisaaPVSLRGDPPDpmnllgTSAAFvyptFRDYREAVEaANTTLNVAALVGhtaLRSN 150
Cdd:cd01315 74 tgtKAAAA--GGITTII---------DMPLNSIPPT------TTVEN----LEAKLEAAQ-GKLHVDVGFWGG---LVPG 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224246933 151 HLDdllrsasaeeitamreQLRESLEAGALGLSTGLAYASA--FSASTDE-VMQLSEELTAFGAV--------------- 212
Cdd:cd01315 129 NLD----------------QLRPLDEAGVVGFKCFLCPSGVdeFPAVDDEqLEEAMKELAKTGSVlavhaenpeitealq 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224246933 213 ----------YTTHLRSEfaPV---LEAMDEAFQIGRHAKSPVIISHLKCAgvgnwgrspqllAALETAAQshpvgcdcy 279
Cdd:cd01315 193 eqakakgkrdYRDYLASR--PVfteVEAIQRILLLAKETGCRLHIVHLSSA------------EAVPLIRE--------- 249
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224246933 280 pyaASSSTLDLKQVTDAHRITITwstphpelgGRDLIDIAADWNV--PLLDAARRLQPAGAVYYGMdeadvrrilahpLS 357
Cdd:cd01315 250 ---ARAEGVDVTVETCPHYLTFT---------AEDVPDGGTEFKCapPIRDAANQEQLWEALENGD------------ID 305
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224246933 358 MVGSDGLPEDP----FPHPRLWGAFPRVLG-HFSRDV--------GLFPLHTAVHKMTGLSAARFGLK-QRGEIRAGHWA 423
Cdd:cd01315 306 MVVSDHSPCTPelklLGKGDFFKAWGGISGlQLGLPVmlteavnkRGLSLEDIARLMCENPAKLFGLShQKGRIAVGYDA 385
|
....*..
gi 1224246933 424 DLVLFDP 430
Cdd:cd01315 386 DFVVWDP 392
|
|
| ureB |
PRK13985 |
urease subunit alpha; |
4-182 |
7.79e-09 |
|
urease subunit alpha;
Pssm-ID: 184438 [Multi-domain] Cd Length: 568 Bit Score: 57.98 E-value: 7.79e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224246933 4 DTLIRNALVIDGSNApgYAADVALLNGRIERIG-----DLHDA--------RASEQIDAAGRVLAPGFIDVHTHddtvvI 70
Cdd:PRK13985 66 DLIITNALIIDYTGI--YKADIGIKDGKIAGIGkggnkDMQDGvknnlsvgPATEALAGEGLIVTAGGIDTHIH-----F 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224246933 71 RQPQMLPK-LSQGVTTVIVGNCGisaapvslrgdPPDpmnllGTSAAFVYPTFRDYREAVEAANT-TLNVAALvghtalr 148
Cdd:PRK13985 139 ISPQQIPTaFASGVTTMIGGGTG-----------PAD-----GTNATTITPGRRNLKWMLRAAEEySMNLGFL------- 195
|
170 180 190
....*....|....*....|....*....|....
gi 1224246933 149 snhlddllrsasAEEITAMREQLRESLEAGALGL 182
Cdd:PRK13985 196 ------------GKGNSSNDASLADQIEAGAIGF 217
|
|
| PRK12394 |
PRK12394 |
metallo-dependent hydrolase; |
1-87 |
1.03e-08 |
|
metallo-dependent hydrolase;
Pssm-ID: 183497 [Multi-domain] Cd Length: 379 Bit Score: 57.08 E-value: 1.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224246933 1 MLYDTLIRNALVIDGSNAPGYAADVALLNGRIERIGDLHDARASEQIDAAGRVLAPGFIDVHTH---DDTVVIRQPQMLp 77
Cdd:PRK12394 1 MKNDILITNGHIIDPARNINEINNLRIINDIIVDADKYPVASETRIIHADGCIVTPGLIDYHAHvfyDGTEGGVRPDMY- 79
|
90
....*....|
gi 1224246933 78 KLSQGVTTVI 87
Cdd:PRK12394 80 MPPNGVTTVV 89
|
|
| PRK09060 |
PRK09060 |
dihydroorotase; Validated |
1-64 |
1.12e-08 |
|
dihydroorotase; Validated
Pssm-ID: 181632 [Multi-domain] Cd Length: 444 Bit Score: 57.24 E-value: 1.12e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1224246933 1 MLYDTLIRNALVI--DGSNApgyaADVALLNGRIERIGDLHDARASEQIDAAGRVLAPGFIDVHTH 64
Cdd:PRK09060 3 QTFDLILKGGTVVnpDGEGR----ADIGIRDGRIAAIGDLSGASAGEVIDCRGLHVLPGVIDSQVH 64
|
|
| PRK08393 |
PRK08393 |
N-ethylammeline chlorohydrolase; Provisional |
6-71 |
1.40e-08 |
|
N-ethylammeline chlorohydrolase; Provisional
Pssm-ID: 181411 [Multi-domain] Cd Length: 424 Bit Score: 56.73 E-value: 1.40e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1224246933 6 LIRNALVIDGSNAPGYAADVALLNGRIERIGDLHDARASEQIDAAGRVLAPGFIDVHTHDDTVVIR 71
Cdd:PRK08393 4 LIKNGYVIYGENLKVIRADVLIEGNKIVEVKRNINKPADTVIDASGSVVSPGFINAHTHSPMVLLR 69
|
|
| Urease_alpha |
cd00375 |
Urease alpha-subunit; Urease is a nickel-dependent metalloenzyme that catalyzes the hydrolysis ... |
4-182 |
1.43e-08 |
|
Urease alpha-subunit; Urease is a nickel-dependent metalloenzyme that catalyzes the hydrolysis of urea to form ammonia and carbon dioxide. Nickel-dependent ureases are found in bacteria, fungi and plants. Their primary role is to allow the use of external and internally generated urea as a nitrogen source. The enzyme consists of 3 subunits, alpha, beta and gamma, which can be fused and present on a single protein chain and which in turn forms multimers, mainly trimers. The large alpha subunit is the catalytic domain containing an active site with a bi-nickel center complexed by a carbamylated lysine. The beta and gamma subunits play a role in subunit association to form the higher order trimers.
Pssm-ID: 238221 [Multi-domain] Cd Length: 567 Bit Score: 56.95 E-value: 1.43e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224246933 4 DTLIRNALVIDgsnAPG-YAADVALLNGRIERIG-----DLHD--------ARASEQIDAAGRVLAPGFIDVHTHddtvV 69
Cdd:cd00375 66 DLVITNALIID---YTGiYKADIGIKDGRIVAIGkagnpDIMDgvtpnmivGPSTEVIAGEGKIVTAGGIDTHVH----F 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224246933 70 IRQPQMLPKLSQGVTTVIVGNCGISAapvslrgdppdpmnllGTSAAFVYPTFRDYREAVEAANT-TLNVAalvghtalr 148
Cdd:cd00375 139 ICPQQIEEALASGITTMIGGGTGPAA----------------GTKATTCTPGPWNIKRMLQAADGlPVNIG--------- 193
|
170 180 190
....*....|....*....|....*....|....
gi 1224246933 149 snhlddLLRSASAEEITAMREQlresLEAGALGL 182
Cdd:cd00375 194 ------FLGKGNGSSPDALAEQ----IEAGACGL 217
|
|
| Isoaspartyl-dipeptidase |
cd01308 |
Isoaspartyl dipeptidase hydrolyzes the beta-L-isoaspartyl linkages in dipeptides, as part of ... |
5-100 |
2.48e-08 |
|
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: 55.86 E-value: 2.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224246933 5 TLIRNALVIdgsnAPGYAA--DVALLNGRIERIGD---LHDARASEQIDAAGRVLAPGFIDVHTH------DDTVVIRQP 73
Cdd:cd01308 2 TLIKNAEVY----APEYLGkkDILIAGGKILAIEDqlnLPGYENVTVVDLHGKILVPGFIDQHVHiiggggEGGPSTRTP 77
|
90 100 110
....*....|....*....|....*....|...
gi 1224246933 74 QMlpKLSQ----GVTTVI--VGNCGISAAPVSL 100
Cdd:cd01308 78 EV--TLSDlttaGVTTVVgcLGTDGISRSMEDL 108
|
|
| PRK09236 |
PRK09236 |
dihydroorotase; Reviewed |
377-474 |
3.03e-08 |
|
dihydroorotase; Reviewed
Pssm-ID: 181716 Cd Length: 444 Bit Score: 55.65 E-value: 3.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224246933 377 AFPRVLGHFSRdvGLFPLHTAVHKMTGLSAARFGLKQRGEIRAGHWADLVLFDPLTIRDVAD----------------FH 440
Cdd:PRK09236 335 ALPALLELVHE--GKLSLEKVVEKTSHAPAILFDIKERGFIREGYWADLVLVDLNSPWTVTKenilykcgwspfegrtFR 412
|
90 100 110
....*....|....*....|....*....|....
gi 1224246933 441 dpqraaEGIDGVWINGVLSYVDGKANGRRAGRFL 474
Cdd:PRK09236 413 ------SRVATTFVNGQLVYHNGQLVESCRGQRL 440
|
|
| PRK09236 |
PRK09236 |
dihydroorotase; Reviewed |
5-64 |
1.54e-07 |
|
dihydroorotase; Reviewed
Pssm-ID: 181716 Cd Length: 444 Bit Score: 53.72 E-value: 1.54e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1224246933 5 TLIRNALVI-DGSNapgYAADVALLNGRIERIG-DLHDARASEQIDAAGRVLAPGFIDVHTH 64
Cdd:PRK09236 4 ILIKNARIVnEGKI---FEGDVLIENGRIAKIAsSISAKSADTVIDAAGRYLLPGMIDDQVH 62
|
|
| PRK07572 |
PRK07572 |
cytosine deaminase; Validated |
2-66 |
1.56e-07 |
|
cytosine deaminase; Validated
Pssm-ID: 181039 Cd Length: 426 Bit Score: 53.48 E-value: 1.56e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1224246933 2 LYDTLIRNALVIDGSNApgyaADVALLNGRIERIGDLHDARASEQIDAAGRVLAPGFIDVHTHDD 66
Cdd:PRK07572 1 MFDLIVRNANLPDGRTG----IDIGIAGGRIAAVEPGLQAEAAEEIDAAGRLVSPPFVDPHFHMD 61
|
|
| NagA |
COG1820 |
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism]; |
6-64 |
2.23e-07 |
|
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism];
Pssm-ID: 441425 [Multi-domain] Cd Length: 373 Bit Score: 52.79 E-value: 2.23e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1224246933 6 LIRNALVIDGsNAPGYAADVALLNGRIERIGDLHDARAsEQIDAAGRVLAPGFIDVHTH 64
Cdd:COG1820 1 AITNARIFTG-DGVLEDGALLIEDGRIAAIGPGAEPDA-EVIDLGGGYLAPGFIDLHVH 57
|
|
| PRK05985 |
PRK05985 |
cytosine deaminase; Provisional |
4-73 |
2.65e-07 |
|
cytosine deaminase; Provisional
Pssm-ID: 180337 [Multi-domain] Cd Length: 391 Bit Score: 52.63 E-value: 2.65e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1224246933 4 DTLIRNALVIDGSnapgyAADVALLNGRIERIG-DLHDARASEQIDAAGRVLAPGFIDVHTHDDTVVIRQP 73
Cdd:PRK05985 3 DLLFRNVRPAGGA-----AVDILIRDGRIAAIGpALAAPPGAEVEDGGGALALPGLVDGHIHLDKTFWGDP 68
|
|
| ade |
TIGR01178 |
adenine deaminase; The family described by this model includes an experimentally characterized ... |
4-87 |
4.32e-07 |
|
adenine deaminase; The family described by this model includes an experimentally characterized adenine deaminase of Bacillus subtilis. It also include a member from Methanobacterium thermoautotrophicum, in which adenine deaminase activity has been detected. [Purines, pyrimidines, nucleosides, and nucleotides, Salvage of nucleosides and nucleotides]
Pssm-ID: 130246 [Multi-domain] Cd Length: 552 Bit Score: 52.47 E-value: 4.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224246933 4 DTLIRNALVIDGSNAPGYAADVALLNGRIERIGDLHDArasEQIDAAGRVLAPGFIDVHTHddtvvIRQPQMLPK----- 78
Cdd:TIGR01178 1 DIVIKNAKIIDVYNGEIIPGDIAIANGHIAGVGKYNGV---KVIDALGEYAVPGFIDAHIH-----IESSMLTPSefakl 72
|
90
....*....|
gi 1224246933 79 -LSQGVTTVI 87
Cdd:TIGR01178 73 vLPHGVTTVV 82
|
|
| PRK13404 |
PRK13404 |
dihydropyrimidinase; Provisional |
1-73 |
6.06e-07 |
|
dihydropyrimidinase; Provisional
Pssm-ID: 184033 [Multi-domain] Cd Length: 477 Bit Score: 51.62 E-value: 6.06e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1224246933 1 MLYDTLIRNALVIDGSNApgYAADVALLNGRIERIGDLHDArASEQIDAAGRVLAPGFIDVHTHddtvvIRQP 73
Cdd:PRK13404 2 MAFDLVIRGGTVVTATDT--FQADIGIRGGRIAALGEGLGP-GAREIDATGRLVLPGGVDSHCH-----IDQP 66
|
|
| ureC |
PRK13207 |
urease subunit alpha; Reviewed |
4-182 |
8.01e-07 |
|
urease subunit alpha; Reviewed
Pssm-ID: 237305 [Multi-domain] Cd Length: 568 Bit Score: 51.33 E-value: 8.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224246933 4 DTLIRNALVIDgsnAPG-YAADVALLNGRIERIG-----DLHD------ARASEQIDAAGRVLAPGFIDVHTHddtvVIR 71
Cdd:PRK13207 68 DTVITNALILD---HWGiVKADIGIKDGRIVAIGkagnpDIQDgvdiiiGPGTEVIAGEGLIVTAGGIDTHIH----FIC 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224246933 72 QPQMLPKLSQGVTTVIVGNCGISAapvslrgdppdpmnllGTSAAFVYPTFRDYREAVEAANTT-LNVAalvghtalrsn 150
Cdd:PRK13207 141 PQQIEEALASGVTTMIGGGTGPAT----------------GTNATTCTPGPWHIHRMLQAADAFpMNIG----------- 193
|
170 180 190
....*....|....*....|....*....|..
gi 1224246933 151 hlddLLRSASAEEITAMREQlresLEAGALGL 182
Cdd:PRK13207 194 ----FLGKGNASLPEALEEQ----IEAGAIGL 217
|
|
| PRK08044 |
PRK08044 |
allantoinase AllB; |
1-64 |
1.29e-06 |
|
allantoinase AllB;
Pssm-ID: 169193 [Multi-domain] Cd Length: 449 Bit Score: 50.62 E-value: 1.29e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1224246933 1 MLYDTLIRNALVIDGSNApgYAADVALLNGRIERIGDlHDARASEQIDAAGRVLAPGFIDVHTH 64
Cdd:PRK08044 1 MSFDLIIKNGTVILENEA--RVVDIAVKGGKIAAIGQ-DLGDAKEVMDASGLVVSPGMVDAHTH 61
|
|
| FwdA |
COG1229 |
Formylmethanofuran dehydrogenase subunit A [Energy production and conversion]; |
5-64 |
1.34e-06 |
|
Formylmethanofuran dehydrogenase subunit A [Energy production and conversion];
Pssm-ID: 440842 Cd Length: 554 Bit Score: 50.96 E-value: 1.34e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1224246933 5 TLIRNALVIDGSNAP-GYAADVALLNGRIerIGDLHDARASEQIDAAGRVLAPGFIDVHTH 64
Cdd:COG1229 3 LIIKNGRVYDPANGIdGEVMDIAIKDGKI--VEEPSDPKDAKVIDASGKVVMAGGVDIHTH 61
|
|
| NagA |
cd00854 |
N-acetylglucosamine-6-phosphate deacetylase, NagA, catalyzes the hydrolysis of the N-acetyl ... |
5-64 |
2.22e-06 |
|
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: 49.88 E-value: 2.22e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1224246933 5 TLIRNALVIDGSNAPGyaADVALLNGRIERIGD-LHDARASEQIDAAGRVLAPGFIDVHTH 64
Cdd:cd00854 1 LIIKNARILTPGGLED--GAVLVEDGKIVAIGPeDELEEADEIIDLKGQYLVPGFIDIHIH 59
|
|
| ATZ_TRZ_like |
cd01298 |
TRZ/ATZ family contains enzymes from the atrazine degradation pathway and related hydrolases. ... |
5-64 |
6.53e-06 |
|
TRZ/ATZ family contains enzymes from the atrazine degradation pathway and related hydrolases. Atrazine, a chlorinated herbizide, can be catabolized by a variety of different bacteria. The first three steps of the atrazine dehalogenation pathway are catalyzed by atrazine chlorohydrolase (AtzA), hydroxyatrazine ethylaminohydrolase (AtzB), and N-isopropylammelide N-isopropylaminohydrolase (AtzC). All three enzymes belong to the superfamily of metal dependent hydrolases. AtzA and AtzB, beside other related enzymes are represented in this CD.
Pssm-ID: 238623 [Multi-domain] Cd Length: 411 Bit Score: 48.35 E-value: 6.53e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1224246933 5 TLIRNALVIDGSNAPGYA-ADVALLNGRIERIGDLHDAR---ASEQIDAAGRVLAPGFIDVHTH 64
Cdd:cd01298 1 ILIRNGTIVTTDPRRVLEdGDVLVEDGRIVAVGPALPLPaypADEVIDAKGKVVMPGLVNTHTH 64
|
|
| pyrC_multi |
TIGR00857 |
dihydroorotase, multifunctional complex type; In contrast to the homodimeric type of ... |
23-64 |
7.85e-06 |
|
dihydroorotase, multifunctional complex type; In contrast to the homodimeric type of dihydroorotase found in E. coli, this class tends to appear in a large, multifunctional complex with aspartate transcarbamoylase. Homologous domains appear in multifunctional proteins of higher eukaryotes. In some species, including Pseudomonas putida and P. aeruginosa, this protein is inactive but is required as a non-catalytic subunit of aspartate transcarbamoylase (ATCase). In these species, a second, active dihydroorotase is also present. The seed for this model does not include any example of the dihydroorotase domain of eukaryotic multidomain pyrimidine synthesis proteins. All proteins described by this model should represent active and inactive dihydroorotase per se and functionally equivalent domains of multifunctional proteins from higher eukaryotes, but exclude related proteins such as allantoinase. [Purines, pyrimidines, nucleosides, and nucleotides, Pyrimidine ribonucleotide biosynthesis]
Pssm-ID: 273302 [Multi-domain] Cd Length: 411 Bit Score: 48.21 E-value: 7.85e-06
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 1224246933 23 ADVALLNGRIERIGDLHDARASEQIDAAGRVLAPGFIDVHTH 64
Cdd:TIGR00857 6 VDILVEGGRIKKIGKLRIPPDAEVIDAKGLLVLPGFIDLHVH 47
|
|
| PRK06038 |
PRK06038 |
N-ethylammeline chlorohydrolase; Provisional |
4-64 |
9.83e-06 |
|
N-ethylammeline chlorohydrolase; Provisional
Pssm-ID: 180363 [Multi-domain] Cd Length: 430 Bit Score: 47.82 E-value: 9.83e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1224246933 4 DTLIRNALVIDGSNAPGYAADVALLNGRIERIGDLHDARASEQIDAAGRVLAPGFIDVHTH 64
Cdd:PRK06038 3 DIIIKNAYVLTMDAGDLKKGSVVIEDGTITEVSESTPGDADTVIDAKGSVVMPGLVNTHTH 63
|
|
| Bact_CD |
cd01293 |
Bacterial cytosine deaminase and related metal-dependent hydrolases. Cytosine deaminases (CDs) ... |
6-68 |
1.10e-05 |
|
Bacterial cytosine deaminase and related metal-dependent hydrolases. Cytosine deaminases (CDs) catalyze the deamination of cytosine, producing uracil and ammonia. They play an important role in pyrimidine salvage. CDs are present in prokaryotes and fungi, but not mammalian cells. The bacterial enzymes, but not the fungal enzymes, are related to the adenosine deaminases (ADA). The bacterial enzymes are iron dependent and hexameric.
Pssm-ID: 238618 [Multi-domain] Cd Length: 398 Bit Score: 47.63 E-value: 1.10e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1224246933 6 LIRNALVIDGSNAPgyaADVALLNGRIERIGD-LHDARASEQIDAAGRVLAPGFIDVHTHDDTV 68
Cdd:cd01293 1 LLRNARLADGGTAL---VDIAIEDGRIAAIGPaLAVPPDAEEVDAKGRLVLPAFVDPHIHLDKT 61
|
|
| PRK08204 |
PRK08204 |
hypothetical protein; Provisional |
5-71 |
1.76e-05 |
|
hypothetical protein; Provisional
Pssm-ID: 181288 [Multi-domain] Cd Length: 449 Bit Score: 46.92 E-value: 1.76e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1224246933 5 TLIRNALVIDGSNAPGYA--ADVALLNGRIERIGDLHDARASEQIDAAGRVLAPGFIDVHTHDDTVVIR 71
Cdd:PRK08204 4 TLIRGGTVLTMDPAIGDLprGDILIEGDRIAAVAPSIEAPDAEVVDARGMIVMPGLVDTHRHTWQSVLR 72
|
|
| YtcJ_like |
cd01300 |
YtcJ_like metal dependent amidohydrolases. YtcJ is a Bacillus subtilis ORF of unknown function. ... |
24-64 |
3.71e-05 |
|
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: 46.15 E-value: 3.71e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 1224246933 24 DVALLNGRIERIGDLHDARA-----SEQIDAAGRVLAPGFIDVHTH 64
Cdd:cd01300 1 AVAVRDGRIVAVGSDAEAKAlkgpaTEVIDLKGKTVLPGFIDSHSH 46
|
|
| AdeC |
COG1001 |
Adenine deaminase [Nucleotide transport and metabolism]; |
393-465 |
4.07e-05 |
|
Adenine deaminase [Nucleotide transport and metabolism];
Pssm-ID: 440625 [Multi-domain] Cd Length: 559 Bit Score: 45.86 E-value: 4.07e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1224246933 393 PLHTAVhKMTGLSAAR-FGLKQRGEIRAGHWADLVLFDpltirDVADFHdpqraaegIDGVWINGVLSYVDGKA 465
Cdd:COG1001 285 DPVTAI-QMATLNAAEhFGLKDLGAIAPGRRADIVLLD-----DLEDFK--------VEKVYADGKLVAEDGKL 344
|
|
| PRK06380 |
PRK06380 |
metal-dependent hydrolase; Provisional |
5-64 |
4.14e-05 |
|
metal-dependent hydrolase; Provisional
Pssm-ID: 180548 [Multi-domain] Cd Length: 418 Bit Score: 45.64 E-value: 4.14e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1224246933 5 TLIRNALVI-DGSNAPGYAADVALLNGRIERIGDLHDArASEQIDAAGRVLAPGFIDVHTH 64
Cdd:PRK06380 3 ILIKNAWIVtQNEKREILQGNVYIEGNKIVYVGDVNEE-ADYIIDATGKVVMPGLINTHAH 62
|
|
| DHOase_IIa |
cd01317 |
Dihydroorotase (DHOase), subgroup IIa; DHOases catalyze the reversible interconversion of ... |
43-441 |
4.70e-05 |
|
Dihydroorotase (DHOase), subgroup IIa; DHOases catalyze the reversible interconversion of carbamoyl aspartate to dihydroorotate, a key reaction in pyrimidine biosynthesis. This subgroup also contains proteins that lack the active site, like unc-33, a C.elegans protein involved in axon growth.
Pssm-ID: 238642 [Multi-domain] Cd Length: 374 Bit Score: 45.69 E-value: 4.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224246933 43 ASEQIDAAGRVLAPGFIDVHTHddtvvIRQPQMLPK--LSQGVTTVIVGncgisaapvslrgdppdpmnllGTSAAFVYP 120
Cdd:cd01317 1 DAEVIDAEGKILAPGLVDLHVH-----LREPGFEYKetLESGAKAAAAG----------------------GFTTVVCMP 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224246933 121 TFRDYREAVEAANTTLNVAALVGhtalrsNHLDDLLRSAS----AEEITAMREQlresLEAGALGLSTG----------- 185
Cdd:cd01317 54 NTNPVIDNPAVVELLKNRAKDVG------IVRVLPIGALTkglkGEELTEIGEL----LEAGAVGFSDDgkpiqdaellr 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224246933 186 --LAYASAFSAStdeVMQLSEE--LTAFGAVytthLRSEFA-----PVLEAMDEAFQIGR------HAKSPVIISHLKCA 250
Cdd:cd01317 124 raLEYAAMLDLP---IIVHPEDpsLAGGGVM----NEGKVAsrlglPGIPPEAETIMVARdlelaeATGARVHFQHLSTA 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224246933 251 gvgnwgRSpqlLAALETA-AQSHPVGCDCYPYAASSSTLDLKQVTDAHRItitwstpHPELGGRD------------LID 317
Cdd:cd01317 197 ------RS---LELIRKAkAKGLPVTAEVTPHHLLLDDEALESYDTNAKV-------NPPLRSEEdrealiealkdgTID 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224246933 318 IAADWNVPLLDAARRLqpagavyyGMDEAdvrrilahplsMVGSDGLPEdpfphprlwgAFPRVLGHFsRDVGLFPLHTA 397
Cdd:cd01317 261 AIASDHAPHTDEEKDL--------PFAEA-----------PPGIIGLET----------ALPLLWTLL-VKGGLLTLPDL 310
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 1224246933 398 VHKMTGLSAARFGLKQrGEIRAGHWADLVLFDPLT--IRDVADFHD 441
Cdd:cd01317 311 IRALSTNPAKILGLPP-GRLEVGAPADLVLFDPDAewIVDEETFRS 355
|
|
| Imidazolone-5PH |
cd01296 |
Imidazolonepropionase/imidazolone-5-propionate hydrolase (Imidazolone-5PH) catalyzes the third ... |
25-64 |
4.93e-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: 45.33 E-value: 4.93e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 1224246933 25 VALLNGRIERIGDLHDARAS-----EQIDAAGRVLAPGFIDVHTH 64
Cdd:cd01296 1 IAIRDGRIAAVGPAASLPAPgpaaaEEIDAGGRAVTPGLVDCHTH 45
|
|
| PRK12393 |
PRK12393 |
amidohydrolase; Provisional |
4-64 |
8.34e-05 |
|
amidohydrolase; Provisional
Pssm-ID: 237088 [Multi-domain] Cd Length: 457 Bit Score: 45.06 E-value: 8.34e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1224246933 4 DTLIRNALVI----DGSNAPGYAADVALLNGRIERIGDLHDARASEQIDAAGRVLAPGFIDVHTH 64
Cdd:PRK12393 3 SLLIRNAAAImtglPGDAARLGGPDIRIRDGRIAAIGALTPLPGERVIDATDCVVYPGWVNTHHH 67
|
|
| Met_dep_hydrolase_B |
cd01307 |
Metallo-dependent hydrolases, subgroup B is part of the superfamily of metallo-dependent ... |
24-92 |
1.27e-04 |
|
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: 44.24 E-value: 1.27e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1224246933 24 DVALLNGRIERIG-DLHDARASEQIDAAGRVLAPGFIDVHTH---DDTVVIRQPQMLpKLSQGVTTVI-VGNCG 92
Cdd:cd01307 1 DVAIENGKIAAVGaALAAPAATQIVDAGGCYVSPGWIDLHVHvyqGGTRYGDRPDMI-GVKSGVTTVVdAGSAG 73
|
|
| ureC |
PRK13206 |
urease subunit alpha; Reviewed |
4-181 |
1.70e-04 |
|
urease subunit alpha; Reviewed
Pssm-ID: 237304 [Multi-domain] Cd Length: 573 Bit Score: 43.93 E-value: 1.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224246933 4 DTLIRNALVIDGSNApgYAADVALLNGRIERIG-------------DLHDARASEQIDAAGRVLAPGFIDVHTHddtvVI 70
Cdd:PRK13206 72 DTVITGAVILDHWGI--VKADVGIRDGRIVAIGkagnpdimdgvhpDLVIGPSTEIIAGNGRILTAGAIDCHVH----FI 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224246933 71 RQPQMLPKLSQGVTTVIVGNCGISAapvslrgdppdpmnllGTSAAFVYPTFRDYREAVEAANT-TLNVAAL-VGHTalr 148
Cdd:PRK13206 146 CPQIVDEALAAGITTLIGGGTGPAE----------------GSKATTVTPGAWHLARMLEALDGwPVNVALLgKGNT--- 206
|
170 180 190
....*....|....*....|....*....|...
gi 1224246933 149 snhlddllrsASAEeitAMREQLResleAGALG 181
Cdd:PRK13206 207 ----------VSAE---ALWEQLR----GGAGG 222
|
|
| PRK07575 |
PRK07575 |
dihydroorotase; Provisional |
1-64 |
2.43e-04 |
|
dihydroorotase; Provisional
Pssm-ID: 236055 [Multi-domain] Cd Length: 438 Bit Score: 43.51 E-value: 2.43e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1224246933 1 MLYDTLIRNALVIDGSNAPgYAADVALLNGRIERIGDLHDARASEQ-IDAAGRVLAPGFIDVHTH 64
Cdd:PRK07575 1 MMMSLLIRNARILLPSGEL-LLGDVLVEDGKIVAIAPEISATAVDTvIDAEGLTLLPGVIDPQVH 64
|
|
| PRK07228 |
PRK07228 |
5'-deoxyadenosine deaminase; |
4-64 |
3.82e-04 |
|
5'-deoxyadenosine deaminase;
Pssm-ID: 180895 [Multi-domain] Cd Length: 445 Bit Score: 42.68 E-value: 3.82e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1224246933 4 DTLIRNA-LVIDGSNAPGYAADVALLNGRIERIGD-LHDARASEQIDAAGRVLAPGFIDVHTH 64
Cdd:PRK07228 2 TILIKNAgIVTMNAKREIVDGDVLIEDDRIAAVGDrLDLEDYDDHIDATGKVVIPGLIQGHIH 64
|
|
| metallo-dependent_hydrolases |
cd01292 |
Superfamily of metallo-dependent hydrolases (also called amidohydrolase superfamily) is a ... |
58-266 |
5.30e-04 |
|
Superfamily of metallo-dependent hydrolases (also called amidohydrolase superfamily) is 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 family includes urease alpha, adenosine deaminase, phosphotriesterase dihydroorotases, allantoinases, hydantoinases, AMP-, adenine and cytosine deaminases, imidazolonepropionase, aryldialkylphosphatase, chlorohydrolases, formylmethanofuran dehydrogenases and others.
Pssm-ID: 238617 [Multi-domain] Cd Length: 275 Bit Score: 41.94 E-value: 5.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224246933 58 FIDVHTHddtvvIRQPQMLPKLSQGVTTVIVGNCGISAAPVSLRGDPPDPMNLLGTSAAFVYP-----TFRDYREAVEAA 132
Cdd:cd01292 1 FIDTHVH-----LDGSALRGTRLNLELKEAEELSPEDLYEDTLRALEALLAGGVTTVVDMGSTpppttTKAAIEAVAEAA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224246933 133 NTTLNVAALVGHTALRSNHLDDLLRSASaeeitaMREQLRESLEAGALGLSTGLAYaSAFSASTDEVMQLSEELTAFGAV 212
Cdd:cd01292 76 RASAGIRVVLGLGIPGVPAAVDEDAEAL------LLELLRRGLELGAVGLKLAGPY-TATGLSDESLRRVLEEARKLGLP 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1224246933 213 YTTHLRSEFAPvLEAMDEAFQIGRHAkSPVIISHLKCAGVGNWGRSPQLLAALE 266
Cdd:cd01292 149 VVIHAGELPDP-TRALEDLVALLRLG-GRVVIGHVSHLDPELLELLKEAGVSLE 200
|
|
| FMDH_A |
cd01304 |
Formylmethanofuran dehydrogenase (FMDH) subunit A; Methanogenic bacteria and archea derive ... |
7-64 |
8.25e-04 |
|
Formylmethanofuran dehydrogenase (FMDH) subunit A; Methanogenic bacteria and archea derive the energy for autotrophic growth from methanogenesis, the reduction of CO2 with molecular hydrogen as the electron donor. FMDH catalyzes the first step in methanogenesis, the formyl-methanofuran synthesis. In this step, CO2 is bound to methanofuran and subsequently reduced to the formyl state with electrons derived from hydrogen.
Pssm-ID: 238629 [Multi-domain] Cd Length: 541 Bit Score: 42.02 E-value: 8.25e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1224246933 7 IRNALVIDGSNA-PGYAADVALLNGRIerIGDLHDARASEQIDAAGRVLAPGFIDVHTH 64
Cdd:cd01304 1 IKNGTVYDPLNGiNGEKMDIFIRDGKI--VESSSGAKPAKVIDASGKVVMAGGVDMHSH 57
|
|
| DHOase_IIb |
cd01318 |
Dihydroorotase (DHOase), subgroup IIb; DHOases catalyze the reversible interconversion of ... |
379-438 |
8.26e-04 |
|
Dihydroorotase (DHOase), subgroup IIb; DHOases catalyze the reversible interconversion of carbamoyl aspartate to dihydroorotate, a key reaction in pyrimidine biosynthesis. This group contains the archeal members of the DHOase family.
Pssm-ID: 238643 [Multi-domain] Cd Length: 361 Bit Score: 41.55 E-value: 8.26e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224246933 379 PRVLGHFSRdvGLFPLHTAVHKMTGLSAARFGLKQRGEIRAGHWADLVLFDPLTIRDVAD 438
Cdd:cd01318 276 PLMLTLVNK--GILSLSRVVRLTSHNPARIFGIKNKGRIAEGYDADLTVVDLKEERTIRA 333
|
|
| PRK15446 |
PRK15446 |
phosphonate metabolism protein PhnM; Provisional |
4-63 |
8.48e-04 |
|
phosphonate metabolism protein PhnM; Provisional
Pssm-ID: 237967 [Multi-domain] Cd Length: 383 Bit Score: 41.70 E-value: 8.48e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1224246933 4 DTLIRNAL------VIDGSnapgyaadVALLNGRIERIGDlHDARASEQIDAAGRVLAPGFIDVHT 63
Cdd:PRK15446 3 EMILSNARlvlpdeVVDGS--------LLIEDGRIAAIDP-GASALPGAIDAEGDYLLPGLVDLHT 59
|
|
| hutI |
TIGR01224 |
imidazolonepropionase; This enzyme catalyzes the third step in histidine degradation. [Energy ... |
30-64 |
1.02e-03 |
|
imidazolonepropionase; This enzyme catalyzes the third step in histidine degradation. [Energy metabolism, Amino acids and amines]
Pssm-ID: 273512 [Multi-domain] Cd Length: 377 Bit Score: 41.24 E-value: 1.02e-03
10 20 30
....*....|....*....|....*....|....*...
gi 1224246933 30 GRIERIGDLHDA---RASEQIDAAGRVLAPGFIDVHTH 64
Cdd:TIGR01224 11 GKIVWIGQLAALpgeEATEIIDCGGGLVTPGLVDPHTH 48
|
|
| Met_dep_hydrolase_C |
cd01309 |
Metallo-dependent hydrolases, subgroup C is part of the superfamily of metallo-dependent ... |
29-64 |
1.13e-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: 41.14 E-value: 1.13e-03
10 20 30
....*....|....*....|....*....|....*..
gi 1224246933 29 NGRIERIGDLHDARASEQ-IDAAGRVLAPGFIDVHTH 64
Cdd:cd01309 1 DGKIVAVGAEITTPADAEvIDAKGKHVTPGLIDAHSH 37
|
|
| PRK09228 |
PRK09228 |
guanine deaminase; Provisional |
5-64 |
1.26e-03 |
|
guanine deaminase; Provisional
Pssm-ID: 236419 [Multi-domain] Cd Length: 433 Bit Score: 40.94 E-value: 1.26e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1224246933 5 TLIRNALV--------IDGSNAPGYAADVALL--NGRIERIGDLHDARAS-----EQIDAAGRVLAPGFIDVHTH 64
Cdd:PRK09228 4 KAYRGRLLhftadpaeVDDEDALRYIEDGLLLveDGRIVAAGPYAELRAQlpadaEVTDYRGKLILPGFIDTHIH 78
|
|
| PLN02303 |
PLN02303 |
urease |
4-92 |
1.32e-03 |
|
urease
Pssm-ID: 215172 [Multi-domain] Cd Length: 837 Bit Score: 41.27 E-value: 1.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224246933 4 DTLIRNALVIDGSNApgYAADVALLNGRIERIG-----DLHDARAS--------EQIDAAGRVLAPGFIDVHTHddtvVI 70
Cdd:PLN02303 335 DTVITNAVIIDYTGI--YKADIGIKDGLIVGIGkagnpDVMDGVTSnmivgvntEVIAGEGMIVTAGGIDCHVH----FI 408
|
90 100
....*....|....*....|..
gi 1224246933 71 RQPQMLPKLSQGVTTVIVGNCG 92
Cdd:PLN02303 409 CPQLATEAIASGITTLVGGGTG 430
|
|
| ureC |
PRK13308 |
urease subunit alpha; Reviewed |
4-92 |
1.90e-03 |
|
urease subunit alpha; Reviewed
Pssm-ID: 183965 [Multi-domain] Cd Length: 569 Bit Score: 40.85 E-value: 1.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224246933 4 DTLIRNALVIDGSnAPGYAADVALLNGRIERIG-------------DLHDARASEQIDAAGRVLAPGFIDVHTHDDTvvi 70
Cdd:PRK13308 69 DFVLCNVTVIDPV-LGIVKGDIGIRDGRIVGIGkagnpdimdgvdpRLVVGPGTDVRPAEGLIATPGAIDVHVHFDS--- 144
|
90 100
....*....|....*....|...
gi 1224246933 71 rqPQMLPK-LSQGVTTVIVGNCG 92
Cdd:PRK13308 145 --AQLVDHaLASGITTMLGGGLG 165
|
|
| PRK07627 |
PRK07627 |
dihydroorotase; Provisional |
7-88 |
2.02e-03 |
|
dihydroorotase; Provisional
Pssm-ID: 181059 [Multi-domain] Cd Length: 425 Bit Score: 40.43 E-value: 2.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224246933 7 IRNALVIDGSNAPGYAADVALLNGRIERIG----DLHDARaseQIDAAGRVLAPGFIDVhthddTVVIRQP--------- 73
Cdd:PRK07627 5 IKGGRLIDPAAGTDRQADLYVAAGKIAAIGqapaGFNADK---TIDASGLIVCPGLVDL-----SARLREPgyeykatle 76
|
90
....*....|....*.
gi 1224246933 74 -QMLPKLSQGVTTVIV 88
Cdd:PRK07627 77 sEMAAAVAGGVTSLVC 92
|
|
| PRK04250 |
PRK04250 |
dihydroorotase; Provisional |
1-64 |
2.07e-03 |
|
dihydroorotase; Provisional
Pssm-ID: 235265 [Multi-domain] Cd Length: 398 Bit Score: 40.52 E-value: 2.07e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1224246933 1 MLYDTLIRNALVIDGSnapgyaadVALLNGRIERIGdLHDARASEQIDAAGRVLAPGFIDVHTH 64
Cdd:PRK04250 1 VLEGKFLLKGRIVEGG--------IGIENGRISKIS-LRDLKGKEVIKVKGGIILPGLIDVHVH 55
|
|
| PRK10027 |
PRK10027 |
cryptic adenine deaminase; Provisional |
4-87 |
2.51e-03 |
|
cryptic adenine deaminase; Provisional
Pssm-ID: 182201 [Multi-domain] Cd Length: 588 Bit Score: 40.20 E-value: 2.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224246933 4 DTLIRNALVIDGSNAPGYAADVALLNGRIERIG-DLHDARASEQIDAAGRVLAPGFIDVHTHddtvvIRQPQMLP----- 77
Cdd:PRK10027 31 DYIIDNVSILDLINGGEISGPIVIKGRYIAGVGaEYADAPALQRIDARGATAVPGFIDAHLH-----IESSMMTPvtfet 105
|
90
....*....|.
gi 1224246933 78 -KLSQGVTTVI 87
Cdd:PRK10027 106 aTLPRGLTTVI 116
|
|
| PRK07203 |
PRK07203 |
putative aminohydrolase SsnA; |
1-64 |
4.00e-03 |
|
putative aminohydrolase SsnA;
Pssm-ID: 235963 [Multi-domain] Cd Length: 442 Bit Score: 39.53 E-value: 4.00e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224246933 1 MLydtLIRNALVI--DGSNAPGYAADVALLNGRIERIGDLHDARA----SEQIDAAGRVLAPGFIDVHTH 64
Cdd:PRK07203 1 ML---LIGNGTAItrDPAKPVIEDGAIAIEGNVIVEIGTTDELKAkypdAEFIDAKGKLIMPGLINSHNH 67
|
|
| AdeC |
cd01295 |
Adenine deaminase (AdeC) directly deaminates adenine to form hypoxanthine. This reaction is ... |
48-90 |
5.33e-03 |
|
Adenine deaminase (AdeC) directly deaminates adenine to form hypoxanthine. This reaction is part of one of the adenine salvage pathways, as well as the degradation pathway. It is important for adenine utilization as a purine, as well as a nitrogen source in bacteria and archea.
Pssm-ID: 238620 [Multi-domain] Cd Length: 422 Bit Score: 39.13 E-value: 5.33e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1224246933 48 DAAGRVLAPGFIDVHTHddtvvIRQPQMLPK------LSQGVTTVIVGN 90
Cdd:cd01295 1 DAEGKYIVPGFIDAHLH-----IESSMLTPSefakavLPHGTTTVIADP 44
|
|
| |
