|
Name |
Accession |
Description |
Interval |
E-value |
| PRK09230 |
PRK09230 |
cytosine deaminase; Provisional |
1-407 |
0e+00 |
|
cytosine deaminase; Provisional
Pssm-ID: 181713 Cd Length: 426 Bit Score: 626.34 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997698 1 MKIINARLRHQEALYTLELQDGLINSITPQAAAQAAETSDIDAQQKLVIPPFVEPHIHLDATLTAGEPEWNMSGTLFEGI 80
Cdd:PRK09230 6 MTIKNARLPGKEGLWQITIEDGKISAIEPQSEASLEAGEVLDAEGGLAIPPFIEPHIHLDTTQTAGEPNWNQSGTLFEGI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997698 81 ARWSQRKESVTVEDTRQRALKTIGMLRDNGVQHVRTHIDVTDPSLTALEAMLEVKKEAAHLIDLQIVAFPQEGIESFPGG 160
Cdd:PRK09230 86 ERWAERKALLTHEDVKQRAWQTLKWQIANGIQHVRTHVDVSDPTLTALKAMLEVKEEVAPWVDLQIVAFPQEGILSYPNG 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997698 161 RELMTRAIEMGADVVGGIPHYENTRDKGVSSLSFLMDLAQRHGCLVDVHCDETDDPQSRFLEVLAEEARVRGMGAQVTAS 240
Cdd:PRK09230 166 EALLEEALRLGADVVGAIPHFEFTREYGVESLHKAFALAQKYDRLIDVHCDEIDDEQSRFVETVAALAHREGMGARVTAS 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997698 241 HTCAMGSYDNAYCSKLFRLLKASGINFISCPTESIHLQGRFDSWPKRRGVTRVAELDRAGINVCFAQDSIQDPWYPLGNG 320
Cdd:PRK09230 246 HTTAMHSYNGAYTSRLFRLLKMSGINFVANPLVNIHLQGRFDTYPKRRGITRVKEMLEAGINVCFGHDDVFDPWYPLGTA 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997698 321 NIMRILDAGLHICHMLGYEDLQRCLDLITDNSARTLCLGDnYGIAEGRPANLLILDAHNDYDAVRRQAKVLTSIRHGKII 400
Cdd:PRK09230 326 NMLQVLHMGLHVCQLMGYGQINDGLNLITTHSARTLNLQD-YGIEVGNPANLIILPAENGFDAVRRQVPVRYSIRHGKVI 404
|
....*..
gi 490997698 401 MQRQAEQ 407
Cdd:PRK09230 405 AETQPAQ 411
|
|
| Bact_CD |
cd01293 |
Bacterial cytosine deaminase and related metal-dependent hydrolases. Cytosine deaminases (CDs) ... |
3-400 |
0e+00 |
|
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: 509.10 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997698 3 IINARLR-HQEALYTLELQDGLINSITPQAAAQAAETsDIDAQQKLVIPPFVEPHIHLDATLTAGEPEWNMSGTLFEGIA 81
Cdd:cd01293 2 LRNARLAdGGTALVDIAIEDGRIAAIGPALAVPPDAE-EVDAKGRLVLPAFVDPHIHLDKTFTGGRWPNNSGGTLLEAII 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997698 82 RWSQRKESVTVEDTRQRALKTIGMLRDNGVQHVRTHIDVTDPS-LTALEAMLEVKKEAAHLIDLQIVAFPQEGIESFPGG 160
Cdd:cd01293 81 AWEERKLLLTAEDVKERAERALELAIAHGTTAIRTHVDVDPAAgLKALEALLELREEWADLIDLQIVAFPQHGLLSTPGG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997698 161 RELMTRAIEMGADVVGGIPHYEnTRDKGVSSLSFLMDLAQRHGCLVDVHCDETDDPQSRFLEVLAEEARVRGMGAQVTAS 240
Cdd:cd01293 161 EELMREALKMGADVVGGIPPAE-IDEDGEESLDTLFELAQEHGLDIDLHLDETDDPGSRTLEELAEEAERRGMQGRVTCS 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997698 241 HTCAMGSYDNAYCSKLFRLLKASGINFISCPTESIHLQGRFDSWPKRRGVTRVAELDRAGINVCFAQDSIQDPWYPLGNG 320
Cdd:cd01293 240 HATALGSLPEAEVSRLADLLAEAGISVVSLPPINLYLQGREDTTPKRRGVTPVKELRAAGVNVALGSDNVRDPWYPFGSG 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997698 321 NIMRILDAGLHICHMLGYEDLQRCLDLITDNSARTLCLGDnYGIAEGRPANLLILDAHNDYDAVRRQAKVLTSIRHGKII 400
Cdd:cd01293 320 DMLEVANLAAHIAQLGTPEDLALALDLITGNAARALGLED-YGIKVGCPADLVLLDAEDVAEAVARQPPRRVVIRKGRVV 398
|
|
| PRK07572 |
PRK07572 |
cytosine deaminase; Validated |
3-400 |
1.96e-150 |
|
cytosine deaminase; Validated
Pssm-ID: 181039 Cd Length: 426 Bit Score: 432.91 E-value: 1.96e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997698 3 IINARLRHQEALYTLELQDGLINSITPQAAAQAAETsdIDAQQKLVIPPFVEPHIHLDATLTAGEPEWNMSGTLFEGIAR 82
Cdd:PRK07572 6 VRNANLPDGRTGIDIGIAGGRIAAVEPGLQAEAAEE--IDAAGRLVSPPFVDPHFHMDATLSYGLPRVNASGTLLEGIAL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997698 83 WSQRKESVTVEDTRQRALKTIGMLRDNGVQHVRTHIDVTDPSLTALEAMLEVKKEAAHLIDLQIVAFPQEGIESFPGGRE 162
Cdd:PRK07572 84 WGELKPLLTQEALVERALRYCDWAVARGLLAIRSHVDVCDPRLLAVEALLEVRERVAPYLDLQLVAFPQDGVLRSPGAVD 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997698 163 LMTRAIEMGADVVGGIPHYENTRDKGVSSLSFLMDLAQRHGCLVDVHCDETDDPQSRFLEVLAEEARVRGMGAQVTASHT 242
Cdd:PRK07572 164 NLERALDMGVDVVGGIPHFERTMADGAESVRLLCEIAAERGLRVDMHCDESDDPLSRHIETLAAETQRLGLQGRVAGSHL 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997698 243 CAMGSYDNAYCSKLFRLLKASGINFISCPTESIHLQGRFDSWPKRRGVTRVAELDRAGINVCFAQDSIQDPWYPLGNGNI 322
Cdd:PRK07572 244 TSMHSMDNYYVSKLIPLMAEAGVNAIANPLINITLQGRHDTYPKRRGMTRVPELMAAGINVAFGHDCVMDPWYSLGSGDM 323
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490997698 323 MRILDAGLHICHMLGYEDLQRCLDLITDNSARTLCLgDNYGIAEGRPANLLILDAHNDYDAVRRQAKVLTSIRHGKII 400
Cdd:PRK07572 324 LEVAHMGLHVAQMTGQDAMRACFDAVTVNPARIMGL-EGYGLEPGCNADLVLLQARDPIEAIRLRAARLAVIRRGKVI 400
|
|
| PRK05985 |
PRK05985 |
cytosine deaminase; Provisional |
3-400 |
8.97e-67 |
|
cytosine deaminase; Provisional
Pssm-ID: 180337 [Multi-domain] Cd Length: 391 Bit Score: 217.49 E-value: 8.97e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997698 3 IINARLRHQEALYTLeLQDGLINSITPQAAAQAAETSdIDAQQKLVIPPFVEPHIHLDATLTaGEPeW---NMSGTLFEG 79
Cdd:PRK05985 6 FRNVRPAGGAAVDIL-IRDGRIAAIGPALAAPPGAEV-EDGGGALALPGLVDGHIHLDKTFW-GDP-WypnEPGPSLRER 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997698 80 IArwSQRKESVTVE-DTRQRALKTIGMLRDNGVQHVRTHIDVtDPS--LTALEAMLEVKKEAAHLIDLQIVAFPQEGIES 156
Cdd:PRK05985 82 IA--NERRRRAASGhPAAERALALARAAAAAGTTAMRSHVDV-DPDagLRHLEAVLAARETLRGLIDIQIVAFPQSGVLS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997698 157 FPGGRELMTRAIEMGADVVGGIPHYENTRDKgVSSLSFLMDLAQRHGCLVDVHCDETDDPQSRFLEVLAEEARVRGMGAQ 236
Cdd:PRK05985 159 RPGTAELLDAALRAGADVVGGLDPAGIDGDP-EGQLDIVFGLAERHGVGIDIHLHEPGELGAFQLERIAARTRALGMQGR 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997698 237 VTASHTCAMGSYDNAYCSKLFRLLKASGINFISCPtesihlqgrfdswPKRRGVTRVAELDRAGINVCFAQDSIQDPWYP 316
Cdd:PRK05985 238 VAVSHAFCLGDLPEREVDRLAERLAEAGVAIMTNA-------------PGSVPVPPVAALRAAGVTVFGGNDGIRDTWWP 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997698 317 LGNGNImrildagLHICHMLGY-------EDLQRCLDLITDNSARTLCLgDNYGIAEGRPANLLILDAHNDYDAVRRQAK 389
Cdd:PRK05985 305 YGNGDM-------LERAMLIGYrsgfrtdDELAAALDCVTHGGARALGL-EDYGLAVGARADFVLVDAETVAEAVVAVPV 376
|
410
....*....|.
gi 490997698 390 VLTSIRHGKII 400
Cdd:PRK05985 377 RRLVVRGGRIV 387
|
|
| PRK06846 |
PRK06846 |
putative deaminase; Validated |
13-406 |
3.03e-50 |
|
putative deaminase; Validated
Pssm-ID: 235873 [Multi-domain] Cd Length: 410 Bit Score: 174.43 E-value: 3.03e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997698 13 ALYTLELQDGLINSITPQAAAQAAETSDIDAQQKLVIPPFVEPHIHLDATLTAGepEWNMS---GTLFEGIAR--WSQRK 87
Cdd:PRK06846 30 ALCTLEIQDGKIVAIRPNKQVPDATLPTYDANGLLMLPAFREMHIHLDKTYYGG--PWKACrpaKTIQDRIELeqKELPE 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997698 88 ESVTvedTRQRALKTIGMLRDNGVQHVRTHIDVtDPS--LTALEAMLEVKKEAAHLIDLQIVAFPQEGI---ESFPggre 162
Cdd:PRK06846 108 LLPT---TQERAEKLIELLQSKGATHIRSHCNI-DPVigLKNLENLQAALERYKDGFTYEIVAFPQHGLlrsNSEP---- 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997698 163 LMTRAIEMGADVVGGI-PhyeNTRDKGVS-SLSFLMDLAQRHGCLVDVHCDETDDPQSRFLEVLAEEARVRGMGAQVTAS 240
Cdd:PRK06846 180 LMREAMKMGAHLVGGVdP---ASVDGAIEkSLDTMFQIAVDFNKGVDIHLHDTGPLGVATIKYLVETTEEAQWKGKVTIS 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997698 241 HTCAMGSYDNAYCSKLFRLLKASGINFIScptesihlqgrfdSWPKRRGVTRVAELDRAGINVCFAQDSIQDPWYPLGNG 320
Cdd:PRK06846 257 HAFALGDLNEEEVEELAERLAAQGISITS-------------TVPIGRLHMPIPLLHDKGVKVSLGTDSVIDHWSPFGTG 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997698 321 NIMRILDaglHICHMLGYED---LQRCLDLITDNsarTLCLGDNyG----IAEGRPANLLILDAHNDYDAVRRQAKVLTS 393
Cdd:PRK06846 324 DMLEKAN---LLAELYRWSDersLSRSLALATGG---VLPLNDE-GervwPKVGDEASFVLVDASCSAEAVARQSPRTAV 396
|
410
....*....|...
gi 490997698 394 IRHGKIIMQRQAE 406
Cdd:PRK06846 397 FHKGQLVAGSLAG 409
|
|
| PRK07583 |
PRK07583 |
cytosine deaminase; |
13-409 |
4.25e-44 |
|
cytosine deaminase;
Pssm-ID: 236062 Cd Length: 438 Bit Score: 158.99 E-value: 4.25e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997698 13 ALYTLELQDGLINSITPqAAAQAAETSDIDAQQKLVIPPFVEPHIHLDATLTagepeW----NMSGTlFEG--------- 79
Cdd:PRK07583 39 VLVDIEIADGKIAAILP-AGGAPDELPAVDLKGRMVWPCFVDMHTHLDKGHI-----WprspNPDGT-FPGaldavtadr 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997698 80 IARWSQrkesvtvEDTRQR---ALKTIgmlRDNGVQHVRTHIDVTDP-SLTALEAMLEVKKEAAHLIDLQIVA-FPQEGI 154
Cdd:PRK07583 112 EAHWSA-------EDLYRRmefGLRCA---YAHGTSAIRTHLDSFAPqAAISWEVFAELREAWAGRIALQAVSlVPLDAY 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997698 155 ESfPGGRELMTRAIEMGAdVVGGIPHYENTRDkgvSSLSFLMDLAQRHGCLVDVHCDETDDPQSRFLEVLAEEARVRGMG 234
Cdd:PRK07583 182 LT-DAGERLADLVAEAGG-LLGGVTYMNPDLD---AQLDRLFRLARERGLDLDLHVDETGDPASRTLKAVAEAALRNGFE 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997698 235 AQVTASHTCAMGSYDNAYCSKLFRLLKASGINFISCPTESIHLQGRFDSW-PKRRGVTRVAELDRAGINVCFAQDSIQDP 313
Cdd:PRK07583 257 GKVTCGHCCSLAVQPEEQAQATIALVAEAGIAIVSLPMCNLYLQDRQPGRtPRWRGVTLVHELKAAGIPVAVASDNCRDP 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997698 314 WYPLGNGNIMRILDAGLHICHM-LGYEDLQRcldLITDNSARTLCLGDNYGIAEGRPANLLILDAhndydavRRQAKVLT 392
Cdd:PRK07583 337 FYAYGDHDMLEVFREAVRILHLdHPYDDWPA---AVTTTPADIMGLPDLGRIAVGAPADLVLFKA-------RSFSELLS 406
|
410
....*....|....*..
gi 490997698 393 SIRHGKIIMqRQAEQIH 409
Cdd:PRK07583 407 RPQSDRIVL-RAGKPID 422
|
|
| Amidohydro_3 |
pfam07969 |
Amidohydrolase family; |
41-400 |
1.08e-36 |
|
Amidohydrolase family;
Pssm-ID: 400360 [Multi-domain] Cd Length: 464 Bit Score: 139.20 E-value: 1.08e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997698 41 IDAQQKLVIPPFVEPHIHLDA------TLTAGEPEWNMSGTLFEGIAR------WSQRKESVTVE----DTRQ------- 97
Cdd:pfam07969 3 IDAKGRLVLPGFVDPHTHLDGgglnlrELRLPDVLPNAVVKGQAGRTPkgrwlvGEGWDEAQFAEtrfpYALAdldevap 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997698 98 ------RALKTIGMLRDN-GVQHVRTHIDVTDPSLTALEAM-------------------LEVKKEAAHLIDLQIVAFPQ 151
Cdd:pfam07969 83 dgpvllRALHTHAAVANSaALDLAGITKATEDPPGGEIARDangegltgllregayalppLLAREAEAAAVAAALAALPG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997698 152 EGIESFPGG--------------------------------------RELMTRAIEMGADVVGGIPH------YENTRDK 187
Cdd:pfam07969 163 FGITSVDGGggnvhslddyeplreltaaeklkelldaperlglphsiYELRIGAMKLFADGVLGSRTaaltepYFDAPGT 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997698 188 GVSS-----LSFLMDLAQRHGCLVDVHCDETDDPQSrFLEVLAEEARVRGMGAQVTASHTCAMGSYDNAYCSKLFRLLKA 262
Cdd:pfam07969 243 GWPDfedeaLAELVAAARERGLDVAIHAIGDATIDT-ALDAFEAVAEKLGNQGRVRIEHAQGVVPYTYSQIERVAALGGA 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997698 263 SGINFISCPTESIHLQGRFDSwPKRRGVTRVAELDRAGINVCFAQDSIQ---DPWYPLGnGNIMRILDAGLHICHMLGYE 339
Cdd:pfam07969 322 AGVQPVFDPLWGDWLQDRLGA-ERARGLTPVKELLNAGVKVALGSDAPVgpfDPWPRIG-AAVMRQTAGGGEVLGPDEEL 399
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490997698 340 DLQRCLDLITDNSARTLCLGDNYG-IAEGRPANLLILDAhnDYDAV----RRQAKVLTSIRHGKII 400
Cdd:pfam07969 400 SLEEALALYTSGPAKALGLEDRKGtLGVGKDADLVVLDD--DPLTVdppaIADIRVRLTVVDGRVV 463
|
|
| PRK06886 |
PRK06886 |
hypothetical protein; Validated |
87-358 |
2.04e-29 |
|
hypothetical protein; Validated
Pssm-ID: 180740 Cd Length: 329 Bit Score: 116.47 E-value: 2.04e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997698 87 KESVTVEDTRQRALKTIGMLRDNGVQHVRTHIDVtDP--SLTALEAMLEVKKEAAHLIDLQIVAFPQEGIESfPGGRELM 164
Cdd:PRK06886 59 KRNSTVEDYYARFSQAIELMISQGVTAFGTFVDI-DPicEDRAIIAAHKAREVYKHDIILKFANQTLKGVIE-PTAKKWF 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997698 165 TRAIEMgADVVGGIPH-YENTRDKGVSSLSFLMDLAQRHGCLVDVHCDETDDPQSRFLEVLAEEARVRGMGAQVTASHTC 243
Cdd:PRK06886 137 DIGSEM-VDMIGGLPYrDELDYGRGLEAMDILLDTAKSLGKMVHVHVDQFNTPKEKETEQLCDKTIEHGMQGRVVAIHGI 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997698 244 AMGSYDNAYCSKLFRLLKASGINFISCPTESIHLQGRFDSWPKRRGVTRVAELDRAGINVCFAQDSIQDPWYPLGNGNI- 322
Cdd:PRK06886 216 SIGAHSKEYRYRLYQKMREADMMVIACPMAWIDSNRKEDLMPFHNALTPADEMIPEGITVALGTDNICDYMVPLCEGDMw 295
|
250 260 270
....*....|....*....|....*....|....*...
gi 490997698 323 --MRILDAGlhiCHmlgYEDLQRCLDLITDNSARTLCL 358
Cdd:PRK06886 296 qeLSLLAAG---CR---FYDLDEMVNIASINGRKVLGL 327
|
|
| metallo-dependent_hydrolases |
cd01292 |
Superfamily of metallo-dependent hydrolases (also called amidohydrolase superfamily) is a ... |
52-354 |
2.63e-18 |
|
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: 84.31 E-value: 2.63e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997698 52 FVEPHIHLDATLTAGEPEWNmsgtlfegiarWSQRKESVTVEDTRQRALKTIGMLRDNGVQHVrtHIDVTDPSLTALEAM 131
Cdd:cd01292 1 FIDTHVHLDGSALRGTRLNL-----------ELKEAEELSPEDLYEDTLRALEALLAGGVTTV--VDMGSTPPPTTTKAA 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997698 132 LEVKKEAAHLIDLQIVAF--------PQEGIESFPGGRELMTRAIEMGADVVGGIPHYEnTRDKGVSSLSFLMDLAQRHG 203
Cdd:cd01292 68 IEAVAEAARASAGIRVVLglgipgvpAAVDEDAEALLLELLRRGLELGAVGLKLAGPYT-ATGLSDESLRRVLEEARKLG 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997698 204 CLVDVHCDETDDPQSRFLEVLAeearVRGMGAQVTASHTcamgsydNAYCSKLFRLLKASGINFISCPtesihlQGRFDS 283
Cdd:cd01292 147 LPVVIHAGELPDPTRALEDLVA----LLRLGGRVVIGHV-------SHLDPELLELLKEAGVSLEVCP------LSNYLL 209
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490997698 284 WPKRRGVTRVAELDRAGINVCFAQD--SIQDPWYPLgngNIMRILDAGLhichmLGYEDLQRCLDLITDNSAR 354
Cdd:cd01292 210 GRDGEGAEALRRLLELGIRVTLGTDgpPHPLGTDLL---ALLRLLLKVL-----RLGLSLEEALRLATINPAR 274
|
|
| SsnA |
COG0402 |
Cytosine/adenosine deaminase or related metal-dependent hydrolase [Nucleotide transport and ... |
17-403 |
1.57e-12 |
|
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: 68.70 E-value: 1.57e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997698 17 LELQDGLINSITPQAAAQAAETSD--IDAQQKLVIPPFVEPHIHLDATLTAGEPEwnmSGTLFEGIARWSQRKESV-TVE 93
Cdd:COG0402 24 VLVEDGRIAAVGPGAELPARYPAAevIDAGGKLVLPGLVNTHTHLPQTLLRGLAD---DLPLLDWLEEYIWPLEARlDPE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997698 94 DTRQRALKTIG-MLRdNGVQHVRTHIDVTDPSLTAL-EAMLEVKKEAAHLIDLQIVAFPQEGIESFPGGRELMTRAIE-- 169
Cdd:COG0402 101 DVYAGALLALAeMLR-SGTTTVADFYYVHPESADALaEAAAEAGIRAVLGRGLMDRGFPDGLREDADEGLADSERLIErw 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997698 170 ---MGADVVGGI-PH--YENTRDkgvsSLSFLMDLAQRHGCLVDVHCDET----DDPQSRF----LEVLAEEArvrGMGA 235
Cdd:COG0402 180 hgaADGRIRVALaPHapYTVSPE----LLRAAAALARELGLPLHTHLAETrdevEWVLELYgkrpVEYLDELG---LLGP 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997698 236 QVTASHTCAMGSYDnaycsklFRLLKASGINFISCPTeSIHLQGrfdswpkrRGVTRVAELDRAGINVCFAQDSiqdpwy 315
Cdd:COG0402 253 RTLLAHCVHLTDEE-------IALLAETGASVAHCPT-SNLKLG--------SGIAPVPRLLAAGVRVGLGTDG------ 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997698 316 PLGNGNI-----MRILdAGLHICHMLGYEDL--QRCLDLITDNSARTLCLGDNYG-IAEGRPANLLILD--------AHN 379
Cdd:COG0402 311 AASNNSLdmfeeMRLA-ALLQRLRGGDPTALsaREALEMATLGGARALGLDDEIGsLEPGKRADLVVLDldaphlapLHD 389
|
410 420
....*....|....*....|....*..
gi 490997698 380 DYDAVRRQAK---VLTSIRHGKIIMQR 403
Cdd:COG0402 390 PLSALVYAADgrdVRTVWVAGRVVVRD 416
|
|
| HutI |
COG1228 |
Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport ... |
3-400 |
5.46e-10 |
|
Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440841 [Multi-domain] Cd Length: 386 Bit Score: 60.74 E-value: 5.46e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997698 3 IINARL---RHQEAL--YTLELQDGLINSITPQAAAQA-AETSDIDAQQKLVIPPFVEPHIHLDATlTAGEPEWNMSGtl 76
Cdd:COG1228 12 ITNATLvdgTGGGVIenGTVLVEDGKIAAVGPAADLAVpAGAEVIDATGKTVLPGLIDAHTHLGLG-GGRAVEFEAGG-- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997698 77 feGIArwsqrkesvTVEDTRQRALKTIGMLRDNGVQHVRthidvtDPSLTALEAMLEVKKEAAHLIDLQIVAFPQEGIES 156
Cdd:COG1228 89 --GIT---------PTVDLVNPADKRLRRALAAGVTTVR------DLPGGPLGLRDAIIAGESKLLPGPRVLAAGPALSL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997698 157 FPGG--------RELMTRAIEMGADVV-----GGIPHYenTRDkgvsSLSFLMDLAQRHGCLVDVHCDETDDPQsrflev 223
Cdd:COG1228 152 TGGAhargpeeaRAALRELLAEGADYIkvfaeGGAPDF--SLE----ELRAILEAAHALGLPVAAHAHQADDIR------ 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997698 224 LAEEARVRgmgaqvTASHTCAMgsydnayCSKLFRLLKASGInFISCPT----ESIHLQGRFDSWPKRRGV-----TRVA 294
Cdd:COG1228 220 LAVEAGVD------SIEHGTYL-------DDEVADLLAEAGT-VVLVPTlslfLALLEGAAAPVAAKARKVreaalANAR 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997698 295 ELDRAGINVCFAQDSIQDPWYPLGNGNIMRIL-DAGLhichmlgyeDLQRCLDLITDNSARTLCLGDNYG-IAEGRPANL 372
Cdd:COG1228 286 RLHDAGVPVALGTDAGVGVPPGRSLHRELALAvEAGL---------TPEEALRAATINAAKALGLDDDVGsLEPGKLADL 356
|
410 420 430
....*....|....*....|....*....|
gi 490997698 373 LILDAH--NDYDAVRRQAKVltsIRHGKII 400
Cdd:COG1228 357 VLLDGDplEDIAYLEDVRAV---MKDGRVV 383
|
|
| Imidazolone-5PH |
cd01296 |
Imidazolonepropionase/imidazolone-5-propionate hydrolase (Imidazolone-5PH) catalyzes the third ... |
21-384 |
3.71e-08 |
|
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: 54.96 E-value: 3.71e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997698 21 DGLINSITPQAAAQA---AETSDIDAQQKLVIPPFVEPHIHLdatLTAG----EPEWNMSGTLFEGIARWSQRKESvTVE 93
Cdd:cd01296 5 DGRIAAVGPAASLPApgpAAAEEIDAGGRAVTPGLVDCHTHL---VFAGdrvdEFAARLAGASYEEILAAGGGILS-TVR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997698 94 DTR--------QRALKTIGMLRDNGVQHVRT----HIDvTDPSLTALEAMLEVKKEaaHLID-----LQIVAFPQEGies 156
Cdd:cd01296 81 ATRaasedelfASALRRLARMLRHGTTTVEVksgyGLD-LETELKMLRVIRRLKEE--GPVDlvstfLGAHAVPPEY--- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997698 157 fpGGRELMTRAIEmgADVVGGIPHYENTR------DKGVSSL---SFLMDLAQRHGCLVDVHCDEtddpqsrfLEVLAEE 227
Cdd:cd01296 155 --KGREEYIDLVI--EEVLPAVAEENLADfcdvfcEKGAFSLeqsRRILEAAKEAGLPVKIHADE--------LSNIGGA 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997698 228 ARVRGMGAqVTASHTCAMGSYDnaycsklFRLLKASGINFISCPTESIHLqgrfdswpkRRGVTRVAELDRAGINVCFAQ 307
Cdd:cd01296 223 ELAAELGA-LSADHLEHTSDEG-------IAALAEAGTVAVLLPGTAFSL---------RETYPPARKLIDAGVPVALGT 285
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490997698 308 DSiqDPW-YPLGNGNIMRILDAGLHicHMlgyeDLQRCLDLITDNSARTLCLGDNYG-IAEGRPANLLILDAhNDYDAV 384
Cdd:cd01296 286 DF--NPGsSPTSSMPLVMHLACRLM--RM----TPEEALTAATINAAAALGLGETVGsLEVGKQADLVILDA-PSYEHL 355
|
|
| Amidohydro_1 |
pfam01979 |
Amidohydrolase family; This family of enzymes are a a large metal dependent hydrolase ... |
47-400 |
3.82e-06 |
|
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: 48.65 E-value: 3.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997698 47 LVIPPFVEPHIHLDATLTAGEPEwnmsgtlfegiarwsqrKESVTVEDTRQRALKTIGmlrdNGVQHVRTHIDVTDpslT 126
Cdd:pfam01979 1 IVLPGLIDAHVHLEMGLLRGIPV-----------------PPEFAYEALRLGITTMLK----SGTTTVLDMGATTS---T 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997698 127 ALEAMLEVKKEAAHLIDLQIVAFPQEGIESFPGGRELMTRAIEmGADV----------VGGIPH--YENTRDkgvsSLSF 194
Cdd:pfam01979 57 GIEALLEAAEELPLGLRFLGPGCSLDTDGELEGRKALREKLKA-GAEFikgmadgvvfVGLAPHgaPTFSDD----ELKA 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997698 195 LMDLAQRHGCLVDVHCDETDDpqsrflevLAEEARVRGMGAQVTASHTCAMGSY-----------DNAYCSK-----LFR 258
Cdd:pfam01979 132 ALEEAKKYGLPVAIHALETKG--------EVEDAIAAFGGGIEHGTHLEVAESGglldiiklilaHGVHLSPteanlLAE 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997698 259 LLKASGINFISCPTESIhlqgrfdswpkRRGVTRVAELDRAGINVCFAQDSiqdpwypLGNGNIMRILDAGLHICHML-- 336
Cdd:pfam01979 204 HLKGAGVAHCPFSNSKL-----------RSGRIALRKALEDGVKVGLGTDG-------AGSGNSLNMLEELRLALELQfd 265
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490997698 337 --GYEDLQRCLDLITDNSARTLCLGDNYG-IAEGRPANLLILDAH--NDYDAVRRQAKVLTSIRHGKII 400
Cdd:pfam01979 266 peGGLSPLEALRMATINPAKALGLDDKVGsIEVGKDADLVVVDLDplAAFFGLKPDGNVKKVIVKGKIV 334
|
|
| ATZ_TRZ_like |
cd01298 |
TRZ/ATZ family contains enzymes from the atrazine degradation pathway and related hydrolases. ... |
20-402 |
1.75e-04 |
|
TRZ/ATZ family contains enzymes from the atrazine degradation pathway and related hydrolases. Atrazine, a chlorinated herbizide, can be catabolized by a variety of different bacteria. The first three steps of the atrazine dehalogenation pathway are catalyzed by atrazine chlorohydrolase (AtzA), hydroxyatrazine ethylaminohydrolase (AtzB), and N-isopropylammelide N-isopropylaminohydrolase (AtzC). All three enzymes belong to the superfamily of metal dependent hydrolases. AtzA and AtzB, beside other related enzymes are represented in this CD.
Pssm-ID: 238623 [Multi-domain] Cd Length: 411 Bit Score: 43.34 E-value: 1.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997698 20 QDGLINSI---TPQAAAQAAETsdIDAQQKLVIPPFVEPHIHLDATLTAGEP------EWnmsgtLFEGIARWSQRKesv 90
Cdd:cd01298 25 EDGRIVAVgpaLPLPAYPADEV--IDAKGKVVMPGLVNTHTHLAMTLLRGLAddlplmEW-----LKDLIWPLERLL--- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997698 91 TVEDTRQRALKTIG-MLR-------DNGVQH------------VRTHI--DVTDPSLTALEAMLEVKKEAAHLIDLqiva 148
Cdd:cd01298 95 TEEDVYLGALLALAeMIRsgtttfaDMYFFYpdavaeaaeelgIRAVLgrGIMDLGTEDVEETEEALAEAERLIRE---- 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997698 149 fpqegIESFPGGrelMTRAiemgadVVGgiPHYENTrdkgvSSLSFLM---DLAQRHGCLVDVHCDETDDPQSRF----- 220
Cdd:cd01298 171 -----WHGAADG---RIRV------ALA--PHAPYT-----CSDELLRevaELAREYGVPLHIHLAETEDEVEESlekyg 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997698 221 ---LEVLAEearvRG-MGAQVTASHtcamgsydnayCSKL----FRLLKASGINFISCPTESIHLQGrfdswpkrrGVTR 292
Cdd:cd01298 230 krpVEYLEE----LGlLGPDVVLAH-----------CVWLtdeeIELLAETGTGVAHNPASNMKLAS---------GIAP 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997698 293 VAELDRAGINVCFAQDSiqdpwYPLGNG-NIMRILDAGLHIcHMLGYEDL-----QRCLDLITDNSARTLCLGDNYGIAE 366
Cdd:cd01298 286 VPEMLEAGVNVGLGTDG-----AASNNNlDMFEEMRLAALL-QKLAHGDPtalpaEEALEMATIGGAKALGLDEIGSLEV 359
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 490997698 367 GRPANLLILD--------AHNDYDAVRRQAK---VLTSIRHGKIIMQ 402
Cdd:cd01298 360 GKKADLILIDldgphllpVHDPISHLVYSANggdVDTVIVNGRVVME 406
|
|
| pyrC |
PRK09357 |
dihydroorotase; Validated |
1-59 |
1.28e-03 |
|
dihydroorotase; Validated
Pssm-ID: 236479 [Multi-domain] Cd Length: 423 Bit Score: 40.95 E-value: 1.28e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 490997698 1 MKIINARLRHQEAlyTLELQDGLINSITPQAAAQAAETsdIDAQQKLVIPPFVEPHIHL 59
Cdd:PRK09357 8 GRVIDPKGLDEVA--DVLIDDGKIAAIGENIEAEGAEV--IDATGLVVAPGLVDLHVHL 62
|
|
| pyrC |
PRK09357 |
dihydroorotase; Validated |
337-403 |
6.98e-03 |
|
dihydroorotase; Validated
Pssm-ID: 236479 [Multi-domain] Cd Length: 423 Bit Score: 38.25 E-value: 6.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997698 337 GYEDLQRCLDLITDNSARTLCLGDNYgIAEGRPANLLILD---------------AHND-YDAVRRQAKVLTSIRHGKII 400
Cdd:PRK09357 342 GLLDLEQLLEKMTINPARILGLPAGP-LAEGEPADLVIFDpeaewtvdgedfaskGKNTpFIGMKLKGKVVYTIVDGKIV 420
|
...
gi 490997698 401 MQR 403
Cdd:PRK09357 421 YQD 423
|
|
| NagA |
cd00854 |
N-acetylglucosamine-6-phosphate deacetylase, NagA, catalyzes the hydrolysis of the N-acetyl ... |
1-58 |
8.10e-03 |
|
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: 38.33 E-value: 8.10e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 490997698 1 MKIINARLRHQEALY--TLELQDGLINSITPQAAAQAAETsDIDAQQKLVIPPFVEPHIH 58
Cdd:cd00854 1 LIIKNARILTPGGLEdgAVLVEDGKIVAIGPEDELEEADE-IIDLKGQYLVPGFIDIHIH 59
|
|
| D-aminoacylase |
cd01297 |
D-aminoacylases (N-acyl-D-Amino acid amidohydrolases) catalyze the hydrolysis of ... |
20-64 |
9.39e-03 |
|
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: 38.05 E-value: 9.39e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 490997698 20 QDGLINSITPQAAAQAAETsdIDAQQKLVIPPFVEPHIHLDATLT 64
Cdd:cd01297 25 RDGRIAAIGPILSTSAREV--IDAAGLVVAPGFIDVHTHYDGQVF 67
|
|
| |
