|
Name |
Accession |
Description |
Interval |
E-value |
| EF_0837 |
TIGR03583 |
probable amidohydrolase EF_0837/AHA_3915; Members of this family of relatively uncommon ... |
2-365 |
0e+00 |
|
probable amidohydrolase EF_0837/AHA_3915; Members of this family of relatively uncommon proteins are found in both Gram-positive (e.g. Enterococcus faecalis) and Gram-negative (e.g. Aeromonas hydrophila) bacteria, as part of a cluster of conserved proteins. These proteins resemble aminohydrolases (see pfam01979), including dihydroorotases. The function is unknown. [Hypothetical proteins, Conserved]
Pssm-ID: 132622 Cd Length: 365 Bit Score: 653.32 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446382075 2 FDLLLRHARLVDDTLTNIALQDGKIAALG-DVDGPALKTIDLRGECFVSAGWIDSHVHCYPTSPIYHDEPDSVGIATGVT 80
Cdd:TIGR03583 1 YDLLIKNGRTVNGTPVDIAIEDGKIAAVGtTITGSAKQTIDLEGETYVSAGWIDDHTHCFPKSALYYDEPDEIGVKTGVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446382075 81 TVVDAGSTGADDIDDFYTLTRDATTDVYALLNVSRVGLIAQNELANMANIDADAVRQAVKRHPDFIVGLKARMSSSVVGV 160
Cdd:TIGR03583 81 TVVDAGSTGADDIDDFYRLAQQAKTNVFALLNISRIGLVAQDELADLSNLDASAVKQAVERYPDFIVGLKARMSKSVVGD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446382075 161 NGITPLERAKAMQQENGNLPLMVHIGNNPPDLDEIAERLTAGDIITHCYNGKPNRILRPDGELRASVTRALARGVRLDVG 240
Cdd:TIGR03583 161 NGIEPLEIAKQIQQENLELPLMVHIGSAPPELDEILALMEKGDVLTHCFNGKPNGILRETGEVKPSVLEAYNRGVILDVG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446382075 241 HGTASLSFAVAKRAISLGILPHTISSDIYCRNRINGPVHSLANVMSKFLAIGMSLPQVIACVTANAADSLNLKTKGRLQP 320
Cdd:TIGR03583 241 HGTASFSFHVAEKAKRAGIFPDTISTDIYIRNRINGPVYSLATVMSKFLALGYSLEEVIEKVTKNAAEILKLTQKGRLQE 320
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 446382075 321 GLDADLTLFTLKRQPTVLVDAENDSLQAEELLTPLAAIRAGKGYM 365
Cdd:TIGR03583 321 GYDADLTIFTVKAEPKKLTDSEGDSRIAEEQIKPLAVIIGGEYYE 365
|
|
| PRK09237 |
PRK09237 |
amidohydrolase/deacetylase family metallohydrolase; |
4-377 |
0e+00 |
|
amidohydrolase/deacetylase family metallohydrolase;
Pssm-ID: 236423 [Multi-domain] Cd Length: 380 Bit Score: 610.70 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446382075 4 LLLRHARLVD-----DTLTNIALQDGKIAALG-DVDGP-ALKTIDLRGeCFVSAGWIDSHVHCYPTSPIYHDEPDSVGIA 76
Cdd:PRK09237 1 LLLRGGRVIDpangiDGVIDIAIEDGKIAAVAgDIDGSqAKKVIDLSG-LYVSPGWIDLHVHVYPGSTPYGDEPDEVGVR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446382075 77 TGVTTVVDAGSTGADDIDDFYTLTRDAT-TDVYALLNVSRVGLIAQNELANMANIDADAVRQAVKRHPDFIVGLKARMSS 155
Cdd:PRK09237 80 SGVTTVVDAGSAGADNFDDFRKLTIEASkTRVLAFLNISRIGLLAQDELADLEDIDADAVAEAVKRNPDFIVGIKARMSS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446382075 156 SVVGVNGITPLERAKAMQQeNGNLPLMVHIGNNPPDLDEIAERLTAGDIITHCYNGKPNRILRPDGELRASVTRALARGV 235
Cdd:PRK09237 160 SVVGDNGIEPLELAKAIAA-EANLPLMVHIGNPPPSLEEILELLRPGDILTHCFNGKPNRILDEDGELRPSVLEALERGV 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446382075 236 RLDVGHGTASLSFAVAKRAISLGILPHTISSDIYCRNRINGPVHSLANVMSKFLAIGMSLPQVIACVTANAADSLNLKTK 315
Cdd:PRK09237 239 RLDVGHGTASFSFKVAEAAIAAGILPDTISTDIYCRNRINGPVYSLATVMSKFLALGMPLEEVIAAVTKNAADALRLPEL 318
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446382075 316 GRLQPGLDADLTLFTLKRQPTVLVDAENDSLQAEELLTPLAAIRAGKGYMTEQGSAEHAFDF 377
Cdd:PRK09237 319 GRLQVGSDADLTLFTLKDGPFTLTDSEGDSLIGERLLTPLATVRGGKVVLTEQGSAEHAFDA 380
|
|
| COG3964 |
COG3964 |
Predicted amidohydrolase [General function prediction only]; |
3-373 |
0e+00 |
|
Predicted amidohydrolase [General function prediction only];
Pssm-ID: 443164 [Multi-domain] Cd Length: 376 Bit Score: 560.56 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446382075 3 DLLLRHARLVD-----DTLTNIALQDGKIAALGD--VDGPALKTIDLRGeCFVSAGWIDSHVHCYPTSPIYHDEPDSVGI 75
Cdd:COG3964 1 DLLIKGGRVIDpangiDGVMDIAIKDGKIAAVAKdiDAAEAKKVIDASG-LYVTPGLIDLHTHVFPGGTDYGVDPDGVGV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446382075 76 ATGVTTVVDAGSTGADDIDDFY-TLTRDATTDVYALLNVSRVGLIAQNELANMANIDADAVRQAVKRHPDFIVGLKARMS 154
Cdd:COG3964 80 RSGVTTVVDAGSAGAANFDGFRkYVIDPSKTRVLAFLNISGIGLVGGNELQDLDDIDPDATAAAAEANPDFIVGIKVRAS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446382075 155 SSVVGVNGITPLERAKAMQQEnGNLPLMVHIGNNPPDLDEIAERLTAGDIITHCYNGKPNRILRPDGELRASVTRALARG 234
Cdd:COG3964 160 KGVVGDNGIEPLKRAKEAAKE-AGLPLMVHIGNPPPPLDEVLDLLRPGDILTHCFNGKPNGILDEDGKVRPSVREARKRG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446382075 235 VRLDVGHGTASLSFAVAKRAISLGILPHTISSDIYCRNrINGPVHSLANVMSKFLAIGMSLPQVIACVTANAADSLNLKT 314
Cdd:COG3964 239 VLFDVGHGGASFSFKVAEPAIAQGFLPDTISTDLHTRN-MNGPVFDLATVMSKFLALGMPLEEVIAAVTWNPARAIGLPE 317
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 446382075 315 KGRLQPGLDADLTLFTLKRQPTVLVDAENDSLQAEELLTPLAAIRAGKGYMTEQGSAEH 373
Cdd:COG3964 318 LGTLSVGADADITIFDLREGPFGFTDSEGETLEGDRLLEPEATVRGGKVVYDLNGIAAP 376
|
|
| Met_dep_hydrolase_B |
cd01307 |
Metallo-dependent hydrolases, subgroup B is part of the superfamily of metallo-dependent ... |
18-354 |
0e+00 |
|
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: 506.10 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446382075 18 NIALQDGKIAALGDVD-GPALKTIDLRGECFVSAGWIDSHVHCYPTSPIYHDEPDSVGIATGVTTVVDAGSTGADDIDDF 96
Cdd:cd01307 1 DVAIENGKIAAVGAALaAPAATQIVDAGGCYVSPGWIDLHVHVYQGGTRYGDRPDMIGVKSGVTTVVDAGSAGADNIDGF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446382075 97 -YTLTRDATTDVYALLNVSRVGLIAQNELANMANIDADAVRQAVKRHPDFIVGLKARMSSSVVGVNGITPLERAKAMQQE 175
Cdd:cd01307 81 rYTVIERSATRVYAFLNISRVGLVAQDELPDPDNIDEDAVVAAAREYPDVIVGLKARASKSVVGEWGIKPLELAKKIAKE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446382075 176 NgNLPLMVHIGNNPPDLDEIAERLTAGDIITHCYNGKPNRILRPDGELRASVTRALARGVRLDVGHGTASLSFAVAKRAI 255
Cdd:cd01307 161 A-DLPLMVHIGSPPPILDEVVPLLRRGDVLTHCFNGKPNGIVDEEGEVLPLVRRARERGVIFDVGHGTASFSFRVARAAI 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446382075 256 SLGILPHTISSDIYCRNRINGPVHSLANVMSKFLAIGMSLPQVIACVTANAADSLNLKTKGRLQPGLDADLTLFTLKRQP 335
Cdd:cd01307 240 AAGLLPDTISSDIHGRNRTNGPVYALATTLSKLLALGMPLEEVIEAVTANPARMLGLAEIGTLAVGYDADLTVFDLKDGR 319
|
330
....*....|....*....
gi 446382075 336 TVLVDAENDSLQAEELLTP 354
Cdd:cd01307 320 VELVDSEGDTLIAERLLVP 338
|
|
| PRK12394 |
PRK12394 |
metallo-dependent hydrolase; |
2-362 |
2.84e-70 |
|
metallo-dependent hydrolase;
Pssm-ID: 183497 [Multi-domain] Cd Length: 379 Bit Score: 225.02 E-value: 2.84e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446382075 2 FDLLLRHARLVDDTLTN-----IALQDGKIAALGDVDGPALKT-IDLRGeCFVSAGWIDSHVH-CYPTSPIyHDEPDSVG 74
Cdd:PRK12394 3 NDILITNGHIIDPARNIneinnLRIINDIIVDADKYPVASETRiIHADG-CIVTPGLIDYHAHvFYDGTEG-GVRPDMYM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446382075 75 IATGVTTVVDAGSTGADDIDDFY-TLTRDATTDVYALLNVSRVGLIAQNELANM--ANIDADAVRQAVKRHPDFIVGLKA 151
Cdd:PRK12394 81 PPNGVTTVVDAGSAGTANFDAFYrTVICASKVRIKAFLTVSPPGQTWSGYQENYdpDNIDENKIHALFRQYRNVLQGLKL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446382075 152 RMSSSVVGVNGITPLERAKAMQQENGnLPLMVHIGNNPPDLDEIAERLTAGDIITHCYNGKPNRILRPDGELRASVTRAL 231
Cdd:PRK12394 161 RVQTEDIAEYGLKPLTETLRIANDLR-CPVAVHSTHPVLPMKELVSLLRRGDIIAHAFHGKGSTILTEEGAVLAEVRQAR 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446382075 232 ARGVRLDVGHGTASLSFAVAKRAISLGILPHTISSDIYCRNRINGPVHSLANVMSKFLAIGMSLPQVIACVTANAADSLN 311
Cdd:PRK12394 240 ERGVIFDAANGRSHFDMNVARRAIANGFLPDIISSDLSTITKLAWPVYSLPWVLSKYLALGMALEDVINACTHTPAVLMG 319
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 446382075 312 LKTK-GRLQPGLDADLTLFTLKRQPTVLVDAENDSLQAEELLTPLAAIRAGK 362
Cdd:PRK12394 320 MAAEiGTLAPGAFADIAIFKLKNRHVEFADIHGETLTGTHVLVPQMTIKSGE 371
|
|
| HutI |
COG1228 |
Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport ... |
3-329 |
6.34e-17 |
|
Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440841 [Multi-domain] Cd Length: 386 Bit Score: 81.55 E-value: 6.34e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446382075 3 DLLLRHARLVDDT----LTN--IALQDGKIAALG---DVDGPA-LKTIDLRGeCFVSAGWIDSHVHCYPTSPIYHDEPDS 72
Cdd:COG1228 9 TLLITNATLVDGTgggvIENgtVLVEDGKIAAVGpaaDLAVPAgAEVIDATG-KTVLPGLIDAHTHLGLGGGRAVEFEAG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446382075 73 VGIAT------------------GVTTVVDAGStgaddidDFYTLTRDATTDVYALLNVSRV----GLIAQNELANMANI 130
Cdd:COG1228 88 GGITPtvdlvnpadkrlrralaaGVTTVRDLPG-------GPLGLRDAIIAGESKLLPGPRVlaagPALSLTGGAHARGP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446382075 131 D--ADAVRQAVKRHPDFIvglKARMSSsvvGVNGITPLERAKAMQQE-NGNLPLMVHIgnnpPDLDEIAERLTAG-DIIT 206
Cdd:COG1228 161 EeaRAALRELLAEGADYI---KVFAEG---GAPDFSLEELRAILEAAhALGLPVAAHA----HQADDIRLAVEAGvDSIE 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446382075 207 HCYNGKPNRI----------LRPDGELRASVTRALARGVRLDVGHGTAsLSFAVAKRAISLGIlPHTISSDIycrNRING 276
Cdd:COG1228 231 HGTYLDDEVAdllaeagtvvLVPTLSLFLALLEGAAAPVAAKARKVRE-AALANARRLHDAGV-PVALGTDA---GVGVP 305
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 446382075 277 PVHSLANVMSKFLAIGMSLPQVIACVTANAADSLNLKTK-GRLQPGLDADLTLF 329
Cdd:COG1228 306 PGRSLHRELALAVEAGLTPEEALRAATINAAKALGLDDDvGSLEPGKLADLVLL 359
|
|
| AllB |
COG0044 |
Dihydroorotase or related cyclic amidohydrolase [Nucleotide transport and metabolism]; ... |
5-343 |
3.70e-15 |
|
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: 76.28 E-value: 3.70e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446382075 5 LLRHARLVDD---TLTNIALQDGKIAALGD--VDGPALKTIDLRGeCFVSAGWIDSHVHCyptspiyhDEP---DSVGIA 76
Cdd:COG0044 1 LIKNGRVVDPgglERADVLIEDGRIAAIGPdlAAPEAAEVIDATG-LLVLPGLIDLHVHL--------REPgleHKEDIE 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446382075 77 T--------GVTTVVDAGST--GADDIDDFYTLTRDATTDVYAllNVSRVGLIAQNELANMANIdadavrQAVKRHPdfI 146
Cdd:COG0044 72 TgtraaaagGVTTVVDMPNTnpVTDTPEALEFKLARAEEKALV--DVGPHGALTKGLGENLAEL------GALAEAG--A 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446382075 147 VGLKARMSSSvvGVNGITP-------LERAKAMqqengNLPLMVHignnPPDLDEIAERL-TAGDIITHCY-NGKPnril 217
Cdd:COG0044 142 VAFKVFMGSD--DGNPVLDdgllrraLEYAAEF-----GALVAVH----AEDPDLIRGGVmNEGKTSPRLGlKGRP---- 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446382075 218 rPDGELRAsVTRA--LAR--GVRLDVGHGTASLSFAVAKRA------ISLGILPH------------------------- 262
Cdd:COG0044 207 -AEAEEEA-VARDiaLAEetGARLHIVHVSTAEAVELIREAkarglpVTAEVCPHhltltdedlerygtnfkvnpplrte 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446382075 263 ----------------TISSD-------------IYCRNRINGPVHSLANVMSKFLAIG-MSLPQVIACVTANAADSLNL 312
Cdd:COG0044 285 edrealwegladgtidVIATDhaphtleekelpfAEAPNGIPGLETALPLLLTELVHKGrLSLERLVELLSTNPARIFGL 364
|
410 420 430
....*....|....*....|....*....|.
gi 446382075 313 KTKGRLQPGLDADLTLFTLKRqpTVLVDAEN 343
Cdd:COG0044 365 PRKGRIAVGADADLVLFDPDA--EWTVTAED 393
|
|
| AdeC |
COG1001 |
Adenine deaminase [Nucleotide transport and metabolism]; |
2-58 |
6.54e-10 |
|
Adenine deaminase [Nucleotide transport and metabolism];
Pssm-ID: 440625 [Multi-domain] Cd Length: 559 Bit Score: 60.50 E-value: 6.54e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446382075 2 FDLLLRHARLVD----DTL-TNIALQDGKIAALGDVDGPALKTIDLRGeCFVSAGWIDSHVH 58
Cdd:COG1001 5 ADLVIKNGRLVNvftgEILeGDIAIAGGRIAGVGDYIGEATEVIDAAG-RYLVPGFIDGHVH 65
|
|
| PRK06189 |
PRK06189 |
allantoinase; Provisional |
1-337 |
1.46e-09 |
|
allantoinase; Provisional
Pssm-ID: 235732 [Multi-domain] Cd Length: 451 Bit Score: 59.33 E-value: 1.46e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446382075 1 MFDLLLRHARLVDDTLT---NIALQDGKIAALG-DVDGPALKTIDLRGEcFVSAGWIDSHVHcyptspiyHDEP---DSV 73
Cdd:PRK06189 2 MYDLIIRGGKVVTPEGVyraDIGIKNGKIAEIApEISSPAREIIDADGL-YVFPGMIDVHVH--------FNEPgrtHWE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446382075 74 GIATGVTTVVDAGSTGADDI---DDFYTLTRDATTDVYALLNVSRV-------GLIAQN--ELANMANIDAdavrqavkr 141
Cdd:PRK06189 73 GFATGSAALAAGGCTTYFDMplnSIPPTVTREALDAKAELARQKSAvdfalwgGLVPGNleHLRELAEAGV--------- 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446382075 142 hpdfiVGLKARMSSSvvgvnGITPLERA------KAMQQ-ENGNLPLMVHIGNnppdlDEIAERLTA-----GDIITHCY 209
Cdd:PRK06189 144 -----IGFKAFMSNS-----GTDEFRSSddltlyEGMKEiAALGKILALHAES-----DALTRHLTTqarqqGKTDVRDY 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446382075 210 -NGKP--------NRILR--------------PDGELRASVTRALARGVRLDVGHGTASLSF---------AVAKRAISL 257
Cdd:PRK06189 209 lESRPvvaeleavQRALLyaqetgcplhfvhiSSGKAVALIAEAKKRGVDVSVETCPHYLLFteedferigAVAKCAPPL 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446382075 258 -----------GILP---HTISSDIY-CRNR-------------INGPVHSLANVMSK-FLAIGMSLPQVIACVTANAAD 308
Cdd:PRK06189 289 rsrsqkeelwrGLLAgeiDMISSDHSpCPPElkegddfflvwggISGGQSTLLVMLTEgYIERGIPLETIARLLATNPAK 368
|
410 420
....*....|....*....|....*....
gi 446382075 309 SLNLKTKGRLQPGLDADLTLFTLKRQPTV 337
Cdd:PRK06189 369 RFGLPQKGRLEVGADADFVLVDLDETYTL 397
|
|
| D-aminoacylase |
cd01297 |
D-aminoacylases (N-acyl-D-Amino acid amidohydrolases) catalyze the hydrolysis of ... |
3-336 |
2.23e-09 |
|
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: 58.46 E-value: 2.23e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446382075 3 DLLLRHARLVDDT-----LTNIALQDGKIAALGDVDG-PALKTIDLRGeCFVSAGWIDSHVHcYPTsPIYHDEPDSVGIA 76
Cdd:cd01297 1 DLVIRNGTVVDGTgappfTADVGIRDGRIAAIGPILStSAREVIDAAG-LVVAPGFIDVHTH-YDG-QVFWDPDLRPSSR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446382075 77 TGVTTVVD--AGSTGA-----DDIDDFYTLT-------------------------RDATTDVYAL-----LNVSRVGLI 119
Cdd:cd01297 78 QGVTTVVLgnCGVSPApanpdDLARLIMLMEglvalgeglpwgwatfaeyldaleaRPPAVNVAALvghaaLRRAVMGLD 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446382075 120 A----QNELANMANIDADAVRQAVkrhpdfiVGL---KARMSSSVVGVNGITPLerAKAMQQENGnlPLMVH-------I 185
Cdd:cd01297 158 AreatEEELAKMRELLREALEAGA-------LGIstgLAYAPRLYAGTAELVAL--ARVAARYGG--VYQTHvryegdsI 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446382075 186 GNNPPDLDEIAERLTAGDIITHC-YNGKPNriLRPDGELRASVTRALARGVRldvghgtaslsfavakraISLGILPHTI 264
Cdd:cd01297 227 LEALDELLRLGRETGRPVHISHLkSAGAPN--WGKIDRLLALIEAARAEGLQ------------------VTADVYPYGA 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446382075 265 SSDIYCRNRINGPVHS-----LANVMSKFLAIG---------------MSLPQVIACVTANAADSLNLKTKGRLQPGLDA 324
Cdd:cd01297 287 GSEDDVRRIMAHPVVMggsdgGALGKPHPRSYGdftrvlghyvrerklLSLEEAVRKMTGLPARVFGLADRGRIAPGYRA 366
|
410
....*....|....*
gi 446382075 325 DLTLF---TLKRQPT 336
Cdd:cd01297 367 DIVVFdpdTLADRAT 381
|
|
| Isoaspartyl-dipeptidase |
cd01308 |
Isoaspartyl dipeptidase hydrolyzes the beta-L-isoaspartyl linkages in dipeptides, as part of ... |
24-330 |
2.61e-09 |
|
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: 58.17 E-value: 2.61e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446382075 24 GKIAALGD----VDGPALKTIDLRGEcFVSAGWIDSHVHCY-------PTSpiyhDEPD---SVGIATGVTTVVdaGSTG 89
Cdd:cd01308 25 GKILAIEDqlnlPGYENVTVVDLHGK-ILVPGFIDQHVHIIggggeggPST----RTPEvtlSDLTTAGVTTVV--GCLG 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446382075 90 ADDI----DDFY-------------------------TLTRDATTDVYALLNVSRVGLIA-------QNELANMANIDAD 133
Cdd:cd01308 98 TDGIsrsmEDLLakaraleeegitcfvytgsyevptrTITGSIRKDLLLIDKVIGVGEIAisdhrssQPTVEELARIAAE 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446382075 134 AVrqavkrhpdfIVGLKARMSSSVV-----GVNGITPLERAKAMQQENGNLPLMVHIGNNPPDLDEIAERLTAGDIITHC 208
Cdd:cd01308 178 AR----------VGGLLGGKAGIVHihlgdGKRALSPIFELIEETEIPITQFLPTHINRTAPLFEQGVEFAKMGGTIDLT 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446382075 209 YNGKPNriLRPDGELRAS--VTRALARGVRLD----VGHGTASL-SFAVAKRAISLGIlphtissdiycrnrinGPVHSL 281
Cdd:cd01308 248 SSIDPQ--FRKEGEVRPSeaLKRLLEQGVPLEritfSSDGNGSLpKFDENGNLVGLGV----------------GSVDTL 309
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 446382075 282 AN-VMSKFLAIGMSLPQVIACVTANAADSLNLKTKGRLQPGLDADLTLFT 330
Cdd:cd01308 310 LReVREAVKCGDIPLEVALRVITSNVARILKLRKKGEIQPGFDADLVILD 359
|
|
| PRK13404 |
PRK13404 |
dihydropyrimidinase; Provisional |
2-103 |
1.52e-08 |
|
dihydropyrimidinase; Provisional
Pssm-ID: 184033 [Multi-domain] Cd Length: 477 Bit Score: 56.24 E-value: 1.52e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446382075 2 FDLLLRHARLV--DDTLT-NIALQDGKIAALGDVDGPALKTIDLRGEcFVSAGWIDSHVHCyptspiyhDEPDSVGIATG 78
Cdd:PRK13404 4 FDLVIRGGTVVtaTDTFQaDIGIRGGRIAALGEGLGPGAREIDATGR-LVLPGGVDSHCHI--------DQPSGDGIMMA 74
|
90 100
....*....|....*....|....*
gi 446382075 79 vttvvdagstgaddiDDFYTLTRDA 103
Cdd:PRK13404 75 ---------------DDFYTGTVSA 84
|
|
| PRK09061 |
PRK09061 |
D-glutamate deacylase; Validated |
1-97 |
5.66e-08 |
|
D-glutamate deacylase; Validated
Pssm-ID: 236369 [Multi-domain] Cd Length: 509 Bit Score: 54.32 E-value: 5.66e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446382075 1 MFDLLLRHARLVD-----DTLTNIALQDGKIAALGDVDGPALKTIDLRGECfVSAGWID--SHVHCYPTspiyhdepDSV 73
Cdd:PRK09061 18 PYDLVIRNGRVVDpetglDAVRDVGIKGGKIAAVGTAAIEGDRTIDATGLV-VAPGFIDlhAHGQSVAA--------YRM 88
|
90 100
....*....|....*....|....
gi 446382075 74 GIATGVTTVVDAGStGADDIDDFY 97
Cdd:PRK09061 89 QAFDGVTTALELEA-GVLPVARWY 111
|
|
| Amidohydro_1 |
pfam01979 |
Amidohydrolase family; This family of enzymes are a a large metal dependent hydrolase ... |
47-343 |
5.83e-07 |
|
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: 50.96 E-value: 5.83e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446382075 47 FVSAGWIDSHVH-CYPTSPIYHDEPDSV------GIAT----GVTTVVDAGSTGADDIDDFYTLTRDATTDVYALLNVSR 115
Cdd:pfam01979 1 IVLPGLIDAHVHlEMGLLRGIPVPPEFAyealrlGITTmlksGTTTVLDMGATTSTGIEALLEAAEELPLGLRFLGPGCS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446382075 116 VGLIAQNElanmaniDADAVRQAVKRHPDFIVGLKARMSSSVVGVNG--ITPLERAKAMQQE--NGNLPLMVHIGNNPPD 191
Cdd:pfam01979 81 LDTDGELE-------GRKALREKLKAGAEFIKGMADGVVFVGLAPHGapTFSDDELKAALEEakKYGLPVAIHALETKGE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446382075 192 LdEIAERLTAGDII--THCYNGKPNRILRPDGELRA-----SVTRALARGVRLDvGHGTASLSFAV---------AKRAI 255
Cdd:pfam01979 154 V-EDAIAAFGGGIEhgTHLEVAESGGLLDIIKLILAhgvhlSPTEANLLAEHLK-GAGVAHCPFSNsklrsgriaLRKAL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446382075 256 SLGILpHTISSDIYCRNRINGPVHSLANVM--SKFLAIGMSLPQVIACVTANAADSLNL-KTKGRLQPGLDADLTLFTLK 332
Cdd:pfam01979 232 EDGVK-VGLGTDGAGSGNSLNMLEELRLALelQFDPEGGLSPLEALRMATINPAKALGLdDKVGSIEVGKDADLVVVDLD 310
|
330
....*....|.
gi 446382075 333 RQPTVLVDAEN 343
Cdd:pfam01979 311 PLAAFFGLKPD 321
|
|
| metallo-dependent_hydrolases |
cd01292 |
Superfamily of metallo-dependent hydrolases (also called amidohydrolase superfamily) is a ... |
53-307 |
1.36e-06 |
|
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: 49.25 E-value: 1.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446382075 53 IDSHVH-CYPTSPIYHDEPDSVG--------------------IATGVTTVVDAGSTGADDID-DFYTLTRDA-----TT 105
Cdd:cd01292 2 IDTHVHlDGSALRGTRLNLELKEaeelspedlyedtlralealLAGGVTTVVDMGSTPPPTTTkAAIEAVAEAarasaGI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446382075 106 DVYALLNVSRVGliaqnelANMANIDADAVRQAVKR-HPDFIVGLKARMSSSVVGVNGITPLERAKAMQQEngNLPLMVH 184
Cdd:cd01292 82 RVVLGLGIPGVP-------AAVDEDAEALLLELLRRgLELGAVGLKLAGPYTATGLSDESLRRVLEEARKL--GLPVVIH 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446382075 185 IGNNPPDLDEIAE-----RLTAGDIITHCYNGKPNrilrpdgelraSVTRALARGVRLDVGHGTASLSF------AVAKR 253
Cdd:cd01292 153 AGELPDPTRALEDlvallRLGGRVVIGHVSHLDPE-----------LLELLKEAGVSLEVCPLSNYLLGrdgegaEALRR 221
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446382075 254 AISLGILPhTISSDiycrnrinGPVHSLA-------NVMSKFLAIGMSLPQVIACVTANAA 307
Cdd:cd01292 222 LLELGIRV-TLGTD--------GPPHPLGtdllallRLLLKVLRLGLSLEEALRLATINPA 273
|
|
| PRK07572 |
PRK07572 |
cytosine deaminase; Validated |
1-58 |
2.00e-06 |
|
cytosine deaminase; Validated
Pssm-ID: 181039 Cd Length: 426 Bit Score: 49.25 E-value: 2.00e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446382075 1 MFDLLLRHARLVDD-TLTNIALQDGKIAALG-DVDGPALKTIDLRGEcFVSAGWIDSHVH 58
Cdd:PRK07572 1 MFDLIVRNANLPDGrTGIDIGIAGGRIAAVEpGLQAEAAEEIDAAGR-LVSPPFVDPHFH 59
|
|
| D-HYD |
cd01314 |
D-hydantoinases (D-HYD) also called dihydropyrimidases (DHPase) and related proteins; DHPases ... |
4-84 |
2.56e-06 |
|
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: 49.14 E-value: 2.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446382075 4 LLLRHARLVDDT---LTNIALQDGKIAALGD--VDGPALKTIDLRGeCFVSAGWIDSHVHCY-PTSPIYH-DEPDS---V 73
Cdd:cd01314 1 LIIKNGTIVTADgsfKADILIEDGKIVAIGPnlEAPGGVEVIDATG-KYVLPGGIDPHTHLElPFMGTVTaDDFESgtrA 79
|
90
....*....|.
gi 446382075 74 GIATGVTTVVD 84
Cdd:cd01314 80 AAAGGTTTIID 90
|
|
| SsnA |
COG0402 |
Cytosine/adenosine deaminase or related metal-dependent hydrolase [Nucleotide transport and ... |
3-333 |
2.73e-06 |
|
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: 49.05 E-value: 2.73e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446382075 3 DLLLRHARLV--DDTLT-----NIALQDGKIAALGD-----VDGPALKTIDLRGeCFVSAGWIDSHVHcYPTSP------ 64
Cdd:COG0402 1 DLLIRGAWVLtmDPAGGvledgAVLVEDGRIAAVGPgaelpARYPAAEVIDAGG-KLVLPGLVNTHTH-LPQTLlrglad 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446382075 65 -----------IYHDE----PDSVG----------IATGVTTVVdagstgaddidDFYTLTRDATTDVYALLNVSRVGLI 119
Cdd:COG0402 79 dlplldwleeyIWPLEarldPEDVYagallalaemLRSGTTTVA-----------DFYYVHPESADALAEAAAEAGIRAV 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446382075 120 AQNEL--ANMANIDADAVRQAVKRHPDFIVGLKARMSSSVVGvnGITP----------LERAKAMQQENGnLPLMVHIGN 187
Cdd:COG0402 148 LGRGLmdRGFPDGLREDADEGLADSERLIERWHGAADGRIRV--ALAPhapytvspelLRAAAALARELG-LPLHTHLAE 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446382075 188 NPPDLDEIAER--------------------------LTAGDI---------ITHCyngkpnrilrPDGELR-----ASV 227
Cdd:COG0402 225 TRDEVEWVLELygkrpveyldelgllgprtllahcvhLTDEEIallaetgasVAHC----------PTSNLKlgsgiAPV 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446382075 228 TRALARGVRL----DVGHGTASLS-FAVAKRAISLGILPHTISSDiycrnringpvhslanvmskflaigMSLPQVIACV 302
Cdd:COG0402 295 PRLLAAGVRVglgtDGAASNNSLDmFEEMRLAALLQRLRGGDPTA-------------------------LSAREALEMA 349
|
410 420 430
....*....|....*....|....*....|..
gi 446382075 303 TANAADSLNLKTK-GRLQPGLDADLTLFTLKR 333
Cdd:COG0402 350 TLGGARALGLDDEiGSLEPGKRADLVVLDLDA 381
|
|
| L-HYD_ALN |
cd01315 |
L-Hydantoinases (L-HYDs) and Allantoinase (ALN); L-Hydantoinases are a member of the ... |
3-342 |
3.09e-06 |
|
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: 48.82 E-value: 3.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446382075 3 DLLLRHARLV-DDTLT--NIALQDGKIAALGD--VDGPALKTIDLrGECFVSAGWIDSHVHCyptspiyhDEPDSV---G 74
Cdd:cd01315 1 DLVIKNGRVVtPDGVReaDIAVKGGKIAAIGPdiANTEAEEVIDA-GGLVVMPGLIDTHVHI--------NEPGRTeweG 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446382075 75 IAT--------GVTTVVD------AGSTGADDIDDFYTLTRDATTDVYALLNvsrvGLIAQN--ELANMANIDAdavrqa 138
Cdd:cd01315 72 FETgtkaaaagGITTIIDmplnsiPPTTTVENLEAKLEAAQGKLHVDVGFWG----GLVPGNldQLRPLDEAGV------ 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446382075 139 vkrhpdfiVGLKARMSSSVVG-VNGITPLERAKAMQQ-ENGNLPLMVHIGNNPPDLDEIAERLTAGDIITHCY-NGKPnr 215
Cdd:cd01315 142 --------VGFKCFLCPSGVDeFPAVDDEQLEEAMKElAKTGSVLAVHAENPEITEALQEQAKAKGKRDYRDYlASRP-- 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446382075 216 ilrPDGELRAsVTRAL----ARGVRLDVGHGTASLSFAVAKRAISLGI------LPH--TISSD--------IYC----R 271
Cdd:cd01315 212 ---VFTEVEA-IQRILllakETGCRLHIVHLSSAEAVPLIREARAEGVdvtvetCPHylTFTAEdvpdggteFKCappiR 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446382075 272 NRIN---------------------------------------GPVHSLANVMSKFLAIG-----MSLPQVIACVTANAA 307
Cdd:cd01315 288 DAANqeqlwealengdidmvvsdhspctpelkllgkgdffkawGGISGLQLGLPVMLTEAvnkrgLSLEDIARLMCENPA 367
|
410 420 430
....*....|....*....|....*....|....*.
gi 446382075 308 DSLNLKT-KGRLQPGLDADLTLFTLkrQPTVLVDAE 342
Cdd:cd01315 368 KLFGLSHqKGRIAVGYDADFVVWDP--EEEFTVDAE 401
|
|
| PRK09060 |
PRK09060 |
dihydroorotase; Validated |
1-58 |
3.10e-06 |
|
dihydroorotase; Validated
Pssm-ID: 181632 [Multi-domain] Cd Length: 444 Bit Score: 48.76 E-value: 3.10e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446382075 1 MFDLLLRHARLVDD---TLTNIALQDGKIAALGDVDG-PALKTIDLRGeCFVSAGWIDSHVH 58
Cdd:PRK09060 4 TFDLILKGGTVVNPdgeGRADIGIRDGRIAAIGDLSGaSAGEVIDCRG-LHVLPGVIDSQVH 64
|
|
| PRK08044 |
PRK08044 |
allantoinase AllB; |
292-354 |
6.26e-06 |
|
allantoinase AllB;
Pssm-ID: 169193 [Multi-domain] Cd Length: 449 Bit Score: 47.93 E-value: 6.26e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446382075 292 GMSLPQVIACVTANAADSLNLKTKGRLQPGLDADLtLFTLKRQPTVLvdaENDSLQAEELLTP 354
Cdd:PRK08044 354 GMSLPMFGKLMATNAADIFGLQQKGRIAPGKDADF-VFIQPNSSYVL---KNEDLEYRHKVSP 412
|
|
| PRK05985 |
PRK05985 |
cytosine deaminase; Provisional |
1-58 |
5.97e-05 |
|
cytosine deaminase; Provisional
Pssm-ID: 180337 [Multi-domain] Cd Length: 391 Bit Score: 44.54 E-value: 5.97e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446382075 1 MFDLLLRHARLVDDTLTNIALQDGKIAALGD--VDGPALKTIDLRGEcFVSAGWIDSHVH 58
Cdd:PRK05985 1 MTDLLFRNVRPAGGAAVDILIRDGRIAAIGPalAAPPGAEVEDGGGA-LALPGLVDGHIH 59
|
|
| PhnM |
cd01306 |
PhnM is believed to be a subunit of the membrane associated C-P lyase complex. C-P lyase is ... |
292-326 |
6.15e-05 |
|
PhnM is believed to be a subunit of the membrane associated C-P lyase complex. C-P lyase is thought to catalyze the direct cleavage of inactivated C-P bonds to yield inorganic phosphate and the corresponding hydrocarbons. It is responsible for cleavage of alkylphosphonates, which are utilized as sole phosphorus sources by many bacteria.
Pssm-ID: 238631 Cd Length: 325 Bit Score: 44.58 E-value: 6.15e-05
10 20 30
....*....|....*....|....*....|....*
gi 446382075 292 GMSLPQVIACVTANAADSLNLKTKGRLQPGLDADL 326
Cdd:cd01306 272 GWSLPEAVALVSANPARAVGLTDRGSIAPGKRADL 306
|
|
| ATZ_TRZ_like |
cd01298 |
TRZ/ATZ family contains enzymes from the atrazine degradation pathway and related hydrolases. ... |
4-333 |
6.21e-05 |
|
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: 44.50 E-value: 6.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446382075 4 LLLRHARLV----DDTLTN--IALQDGKIAALGD----VDGPALKTIDLRGeCFVSAGWIDSHVHCY-----------PT 62
Cdd:cd01298 1 ILIRNGTIVttdpRRVLEDgdVLVEDGRIVAVGPalplPAYPADEVIDAKG-KVVMPGLVNTHTHLAmtllrgladdlPL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446382075 63 SPIYHD---------EPDSVGIAT----------GVTTVVDAgstgaddiddfYTLTRDATTDVYALLNVsRV----GLI 119
Cdd:cd01298 80 MEWLKDliwplerllTEEDVYLGAllalaemirsGTTTFADM-----------YFFYPDAVAEAAEELGI-RAvlgrGIM 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446382075 120 AQNE--LANMANIDADAVRQAVKRHpdfivGLKARMSSSVVGVNGI---TP--LERAKAMQQENGnLPLMVHIGNNPPDL 192
Cdd:cd01298 148 DLGTedVEETEEALAEAERLIREWH-----GAADGRIRVALAPHAPytcSDelLREVAELAREYG-VPLHIHLAETEDEV 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446382075 193 DEIAER--------------------------LTAGDI---------ITHCyngkpnrilrPDGELR-----ASVTRALA 232
Cdd:cd01298 222 EESLEKygkrpveyleelgllgpdvvlahcvwLTDEEIellaetgtgVAHN----------PASNMKlasgiAPVPEMLE 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446382075 233 RGVRLDVG-HGTAS---LSFAVAKRAISLgilphtissdiycrnrINGPVHSLANVMSKFLAIGMslpqviacVTANAAD 308
Cdd:cd01298 292 AGVNVGLGtDGAASnnnLDMFEEMRLAAL----------------LQKLAHGDPTALPAEEALEM--------ATIGGAK 347
|
410 420
....*....|....*....|....*
gi 446382075 309 SLNLKTKGRLQPGLDADLTLFTLKR 333
Cdd:cd01298 348 ALGLDEIGSLEVGKKADLILIDLDG 372
|
|
| NagA |
COG1820 |
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism]; |
292-330 |
7.88e-05 |
|
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism];
Pssm-ID: 441425 [Multi-domain] Cd Length: 373 Bit Score: 44.32 E-value: 7.88e-05
10 20 30 40
....*....|....*....|....*....|....*....|
gi 446382075 292 GMSLPQVIACVTANAADSLNL-KTKGRLQPGLDADLTLFT 330
Cdd:COG1820 321 GLPLEEAVRMASLNPARALGLdDRKGSIAPGKDADLVVLD 360
|
|
| Imidazolone-5PH |
cd01296 |
Imidazolonepropionase/imidazolone-5-propionate hydrolase (Imidazolone-5PH) catalyzes the third ... |
246-329 |
1.07e-04 |
|
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: 43.79 E-value: 1.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446382075 246 LSFAVAKRAISLGIlPHTISSDIycrNRINGPVHSLANVMSkfLAI---GMSLPQVIACVTANAADSLNL-KTKGRLQPG 321
Cdd:cd01296 266 ETYPPARKLIDAGV-PVALGTDF---NPGSSPTSSMPLVMH--LACrlmRMTPEEALTAATINAAAALGLgETVGSLEVG 339
|
....*...
gi 446382075 322 LDADLTLF 329
Cdd:cd01296 340 KQADLVIL 347
|
|
| YtcJ |
COG1574 |
Predicted amidohydrolase YtcJ [General function prediction only]; |
3-58 |
1.08e-04 |
|
Predicted amidohydrolase YtcJ [General function prediction only];
Pssm-ID: 441182 [Multi-domain] Cd Length: 535 Bit Score: 44.02 E-value: 1.08e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446382075 3 DLLLRHARL--VDDTL---TNIALQDGKIAALGDVD------GPALKTIDLRGeCFVSAGWIDSHVH 58
Cdd:COG1574 9 DLLLTNGRIytMDPAQpvaEAVAVRDGRIVAVGSDAevralaGPATEVIDLGG-KTVLPGFIDAHVH 74
|
|
| PRK08323 |
PRK08323 |
phenylhydantoinase; Validated |
2-107 |
1.19e-04 |
|
phenylhydantoinase; Validated
Pssm-ID: 236240 [Multi-domain] Cd Length: 459 Bit Score: 44.01 E-value: 1.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446382075 2 FDLLLRHARLVDDTLT---NIALQDGKIAALGDVDGPalKTIDLRGeCFVSAGWIDSHVHCyptspiyhdEPDSVGIATg 78
Cdd:PRK08323 1 MSTLIKNGTVVTADDTykaDVLIEDGKIAAIGANLGD--EVIDATG-KYVMPGGIDPHTHM---------EMPFGGTVS- 67
|
90 100 110
....*....|....*....|....*....|...
gi 446382075 79 vttvvdagstgaddIDDFYTLTRDA----TTDV 107
Cdd:PRK08323 68 --------------SDDFETGTRAAacggTTTI 86
|
|
| PRK15446 |
PRK15446 |
phosphonate metabolism protein PhnM; Provisional |
1-329 |
1.54e-04 |
|
phosphonate metabolism protein PhnM; Provisional
Pssm-ID: 237967 [Multi-domain] Cd Length: 383 Bit Score: 43.24 E-value: 1.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446382075 1 MFDLLLRHARLV--DDTLT-NIALQDGKIAALGDVDGPALKTIDLRGeCFVSAGWIDSH-------------VHCYPTSP 64
Cdd:PRK15446 1 MMEMILSNARLVlpDEVVDgSLLIEDGRIAAIDPGASALPGAIDAEG-DYLLPGLVDLHtdnlekhlaprpgVDWPADAA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446382075 65 IYhdEPDSVGIATGVTTVVDAGSTGADDIDDFytltrdattdvyallnvsrvgliaqnELANMANIDADAVRQAVKR--- 141
Cdd:PRK15446 80 LA--AHDAQLAAAGITTVFDALSVGDEEDGGL--------------------------RSRDLARKLIDAIEEARARgll 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446382075 142 -------------HPDFIVGLKARMSSSVVG---VNGITP-------LERAKAMQQENGNLplmvhignNPPDLDEIAER 198
Cdd:PRK15446 132 radhrlhlrceltNPDALELFEALLAHPRVDlvsLMDHTPgqrqfrdLEKYREYYAGKYGL--------SDEEFDAFVEE 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446382075 199 LTAGdiitHCYNGKPNRilrpdgelRASVTRALARGVRL---D----------VGHGTA----SLSFAVAKRAISLGIL- 260
Cdd:PRK15446 204 RIAL----SARYAPPNR--------RAIAALARARGIPLashDddtpehvaeaHALGVAiaefPTTLEAARAARALGMSv 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446382075 261 ----P-------HT----------------ISSDIYcrnringPvhslanvMSKFLAI-------GMSLPQVIACVTANA 306
Cdd:PRK15446 272 lmgaPnvvrggsHSgnvsaldlaaaglldiLSSDYY-------P-------ASLLDAAfrladdgGLDLPQAVALVTANP 337
|
410 420
....*....|....*....|...
gi 446382075 307 ADSLNLKTKGRLQPGLDADLTLF 329
Cdd:PRK15446 338 ARAAGLDDRGEIAPGKRADLVRV 360
|
|
| ureC |
PRK13308 |
urease subunit alpha; Reviewed |
3-94 |
2.36e-04 |
|
urease subunit alpha; Reviewed
Pssm-ID: 183965 [Multi-domain] Cd Length: 569 Bit Score: 43.16 E-value: 2.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446382075 3 DLLLRHARLVDDTL----TNIALQDGKIAALG---------DVD-----GPALKTIDLRGeCFVSAGWIDSHVHCypTSP 64
Cdd:PRK13308 69 DFVLCNVTVIDPVLgivkGDIGIRDGRIVGIGkagnpdimdGVDprlvvGPGTDVRPAEG-LIATPGAIDVHVHF--DSA 145
|
90 100 110
....*....|....*....|....*....|
gi 446382075 65 IYHDEpdsvGIATGVTTVVDAGSTGADDID 94
Cdd:PRK13308 146 QLVDH----ALASGITTMLGGGLGPTVGID 171
|
|
| pyrC |
PRK09357 |
dihydroorotase; Validated |
4-58 |
3.02e-04 |
|
dihydroorotase; Validated
Pssm-ID: 236479 [Multi-domain] Cd Length: 423 Bit Score: 42.49 E-value: 3.02e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446382075 4 LLLRHARLVD----DTLTNIALQDGKIAALG-DVDGPALKTIDLRGeCFVSAGWIDSHVH 58
Cdd:PRK09357 3 ILIKNGRVIDpkglDEVADVLIDDGKIAAIGeNIEAEGAEVIDATG-LVVAPGLVDLHVH 61
|
|
| Cyclic_amidohydrolases |
cd01302 |
Cyclic amidohydrolases, including hydantoinase, dihydropyrimidinase, allantoinase, and ... |
284-340 |
8.30e-04 |
|
Cyclic amidohydrolases, including hydantoinase, dihydropyrimidinase, allantoinase, and dihydroorotase, are involved in the metabolism of pyrimidines and purines, sharing the property of hydrolyzing the cyclic amide bond of each substrate to the corresponding N-carbamyl amino acids. Allantoinases catalyze the degradation of purines, while dihydropyrimidinases and hydantoinases, a microbial counterpart of dihydropyrimidinase, are involved in pyrimidine degradation. Dihydroorotase participates in the de novo synthesis of pyrimidines.
Pssm-ID: 238627 [Multi-domain] Cd Length: 337 Bit Score: 40.84 E-value: 8.30e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 446382075 284 VMSKFLAIGMSLPQVIACVTANAADSLNLKTKGRLQPGLDADLTLFTLKRQPTVLVD 340
Cdd:cd01302 258 LLTEGVKRGLSLETLVEILSENPARIFGLYPKGTIAVGYDADLVIVDPKKEWKVTAE 314
|
|
| PRK07575 |
PRK07575 |
dihydroorotase; Provisional |
294-353 |
1.73e-03 |
|
dihydroorotase; Provisional
Pssm-ID: 236055 [Multi-domain] Cd Length: 438 Bit Score: 40.04 E-value: 1.73e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446382075 294 SLPQVIACVTANAADSLNLKTKGRLQPGLDADLTLFTLKRQPTVLvdaendslqAEELLT 353
Cdd:PRK07575 343 TVAQVVRWMSTAVARAYGIPNKGRIAPGYDADLVLVDLNTYRPVR---------REELLT 393
|
|
| FMDH_A |
cd01304 |
Formylmethanofuran dehydrogenase (FMDH) subunit A; Methanogenic bacteria and archea derive ... |
12-58 |
2.82e-03 |
|
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: 39.70 E-value: 2.82e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 446382075 12 VDDTLTNIALQDGKIAALGDVDGPAlKTIDLRGeCFVSAGWIDSHVH 58
Cdd:cd01304 13 INGEKMDIFIRDGKIVESSSGAKPA-KVIDASG-KVVMAGGVDMHSH 57
|
|
| Bact_CD |
cd01293 |
Bacterial cytosine deaminase and related metal-dependent hydrolases. Cytosine deaminases (CDs) ... |
5-58 |
3.26e-03 |
|
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: 39.15 E-value: 3.26e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 446382075 5 LLRHARLVD--DTLTNIALQDGKIAALG--DVDGPALKTIDLRGEcFVSAGWIDSHVH 58
Cdd:cd01293 1 LLRNARLADggTALVDIAIEDGRIAAIGpaLAVPPDAEEVDAKGR-LVLPAFVDPHIH 57
|
|
| ureB |
PRK13985 |
urease subunit alpha; |
2-91 |
6.44e-03 |
|
urease subunit alpha;
Pssm-ID: 184438 [Multi-domain] Cd Length: 568 Bit Score: 38.34 E-value: 6.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446382075 2 FDLLLRHARLVDDT---LTNIALQDGKIAALG--------DVDGPAL----KTIDLRGE-CFVSAGWIDSHVHCYPTSPI 65
Cdd:PRK13985 65 LDLIITNALIIDYTgiyKADIGIKDGKIAGIGkggnkdmqDGVKNNLsvgpATEALAGEgLIVTAGGIDTHIHFISPQQI 144
|
90 100
....*....|....*....|....*.
gi 446382075 66 yhdepdSVGIATGVTTVVDAGSTGAD 91
Cdd:PRK13985 145 ------PTAFASGVTTMIGGGTGPAD 164
|
|
| PRK02382 |
PRK02382 |
dihydroorotase; Provisional |
293-334 |
7.17e-03 |
|
dihydroorotase; Provisional
Pssm-ID: 179417 [Multi-domain] Cd Length: 443 Bit Score: 38.09 E-value: 7.17e-03
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 446382075 293 MSLPQVIACVTANAADSLNLKTKGRLQPGLDADLTLFTLKRQ 334
Cdd:PRK02382 341 LPLERVRDVTAANPARIFGLDGKGRIAEGYDADLVLVDPDAA 382
|
|
| |
