|
Name |
Accession |
Description |
Interval |
E-value |
| GDEase |
cd01303 |
Guanine deaminase (GDEase). Guanine deaminase is an aminohydrolase responsible for the ... |
2-402 |
0e+00 |
|
Guanine deaminase (GDEase). Guanine deaminase is an aminohydrolase responsible for the conversion of guanine to xanthine and ammonia, the first step to utilize guanine as a nitrogen source. This reaction also removes the guanine base from the pool and therefore can play a role in the regulation of cellular GTP and the guanylate nucleotide pool.
Pssm-ID: 238628 [Multi-domain] Cd Length: 429 Bit Score: 609.28 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191704909 2 FLEEASQQEKLAKEW--CFKPCEIRELSHHEFFMPGLVDTHIHASQYSFAGSSIDLPLLEWLTKYTFPAEHRFQNIDFAE 79
Cdd:cd01303 31 VVDGNIIAAGAAETLkrAAKPGARVIDSPNQFILPGFIDTHIHAPQYANIGSGLGEPLLDWLETYTFPEEAKFADPAYAR 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191704909 80 EVYTRVVRRTLKNGTTTACYFATIHTDSSLLLADITDKFGQRAFVGKVCMDLNDtfPEYK-ETTEESIKETERFVSEMLQ 158
Cdd:cd01303 111 EVYGRFLDELLRNGTTTACYFATIHPESTEALFEEAAKRGQRAIAGKVCMDRNA--PEYYrDTAESSYRDTKRLIERWHG 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191704909 159 KnYSRVKPIVTPRFSLSCSETLMGELGNIAKT-RDLHIQSHISENRDEVEAVKNLYPSYKNYTSVYDKNNLLTNKTVMAH 237
Cdd:cd01303 189 K-SGRVKPAITPRFAPSCSEELLAALGKLAKEhPDLHIQTHISENLDEIAWVKELFPGARDYLDVYDKYGLLTEKTVLAH 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191704909 238 GCYLSAEELNVFHERGASIAHCPNSNLSLSSGFLNVLEVLKHEVKIGLGTDVAGGYSYSMLDAIRRAVMVSNILLINKVN 317
Cdd:cd01303 268 CVHLSEEEFNLLKERGASVAHCPTSNLFLGSGLFDVRKLLDAGIKVGLGTDVGGGTSFSMLDTLRQAYKVSRLLGYELGG 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191704909 318 EKSLTLKEVFRLATLGGSQALGLDGEIGNFEVGKEFDAILINPKASDSPIDLfygDFFGDISEAVIQKFLYLGDDRNIEE 397
Cdd:cd01303 348 HAKLSPAEAFYLATLGGAEALGLDDKIGNFEVGKEFDAVVIDPSATPLLADR---MFRVESLEEALFKFLYLGDDRNIRE 424
|
....*
gi 1191704909 398 VYVGG 402
Cdd:cd01303 425 VYVAG 429
|
|
| guan_deamin |
TIGR02967 |
guanine deaminase; This model describes guanine deaminase, which hydrolyzes guanine to ... |
14-402 |
0e+00 |
|
guanine deaminase; This model describes guanine deaminase, which hydrolyzes guanine to xanthine and ammonia. Xanthine can then be converted to urate by xanthine dehydrogenase, and urate subsequently degraded. In some bacteria, the guanine deaminase gene is found near the xdhABC genes for xanthine dehydrogenase. Non-homologous forms of guanine deaminase also exist, as well as distantly related forms outside the scope of this model. [Purines, pyrimidines, nucleosides, and nucleotides, Other]
Pssm-ID: 132012 [Multi-domain] Cd Length: 401 Bit Score: 556.87 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191704909 14 KEWCFKPCEIRELSHHeFFMPGLVDTHIHASQYSFAGSsIDLPLLEWLTKYTFPAEHRFQNIDFAEEVYTRVVRRTLKNG 93
Cdd:TIGR02967 26 KETLPAGVEIDDYRGH-LIMPGFIDTHIHYPQTEMIAS-YGEQLLEWLEKYTFPTEARFADPDHAEEVAEFFLDELLRNG 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191704909 94 TTTACYFATIHTDSSLLLADITDKFGQRAFVGKVCMDLNdtFPEY-KETTEESIKETERFVSEMLQKNysRVKPIVTPRF 172
Cdd:TIGR02967 104 TTTALVFATVHPESVDALFEAALKRGMRMIAGKVLMDRN--APDYlRDTAESSYDESKALIERWHGKG--RLLYAVTPRF 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191704909 173 SLSCSETLMGELGNIAKTR-DLHIQSHISENRDEVEAVKNLYPSYKNYTSVYDKNNLLTNKTVMAHGCYLSAEELNVFHE 251
Cdd:TIGR02967 180 APTSSPEQLAAAGELAKEYpDVYVQTHLSENKDEIAWVKELFPEAKDYLDVYDHYGLLGRRSVFAHCIHLSDEECQRLAE 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191704909 252 RGASIAHCPNSNLSLSSGFLNVLEVLKHEVKIGLGTDVAGGYSYSMLDAIRRAVMVSNILlinkvnEKSLTLKEVFRLAT 331
Cdd:TIGR02967 260 TGAAIAHCPTSNLFLGSGLFNLKKALEHGVRVGLGTDVGGGTSFSMLQTLREAYKVSQLQ------GARLSPFEAFYLAT 333
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1191704909 332 LGGSQALGLDGEIGNFEVGKEFDAILINPKASDSPIDLFYGdffGDISEAVIQKFLYLGDDRNIEEVYVGG 402
Cdd:TIGR02967 334 LGGARALDLDDRIGNFEPGKEADFVVLDPAATPLLALRFEG---ADTLEDKLFKLMYLGDDRNVAETYVAG 401
|
|
| SsnA |
COG0402 |
Cytosine/adenosine deaminase or related metal-dependent hydrolase [Nucleotide transport and ... |
22-406 |
1.43e-115 |
|
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: 343.73 E-value: 1.43e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191704909 22 EIRELSHHeFFMPGLVDTHIHASQYSFAGSSIDLPLLEWLTKYTFPAEHRFqNIDFAEEVYTRVVRRTLKNGTTTACYFA 101
Cdd:COG0402 48 EVIDAGGK-LVLPGLVNTHTHLPQTLLRGLADDLPLLDWLEEYIWPLEARL-DPEDVYAGALLALAEMLRSGTTTVADFY 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191704909 102 TIHTDSSLLLADITDKFGQRAFVGKVCMDLNdtFPE-YKETTEESIKETERFVSEMLQKNYSRVKPIVTPRFSLSCSETL 180
Cdd:COG0402 126 YVHPESADALAEAAAEAGIRAVLGRGLMDRG--FPDgLREDADEGLADSERLIERWHGAADGRIRVALAPHAPYTVSPEL 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191704909 181 MGELGNIAKTRDLHIQSHISENRDEVEAVKNLYPsyKNYTSVYDKNNLLTNKTVMAHGCYLSAEELNVFHERGASIAHCP 260
Cdd:COG0402 204 LRAAAALARELGLPLHTHLAETRDEVEWVLELYG--KRPVEYLDELGLLGPRTLLAHCVHLTDEEIALLAETGASVAHCP 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191704909 261 NSNLSLSSGFLNVLEVLKHEVKIGLGTDVAGG-YSYSMLDAIRRAVMVSNILlinKVNEKSLTLKEVFRLATLGGSQALG 339
Cdd:COG0402 282 TSNLKLGSGIAPVPRLLAAGVRVGLGTDGAASnNSLDMFEEMRLAALLQRLR---GGDPTALSAREALEMATLGGARALG 358
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1191704909 340 LDGEIGNFEVGKEFDAILINPKASD-SPIDlfygdffgdiseAVIQKFLYLGDDRNIEEVYVGGKQVV 406
Cdd:COG0402 359 LDDEIGSLEPGKRADLVVLDLDAPHlAPLH------------DPLSALVYAADGRDVRTVWVAGRVVV 414
|
|
| PRK09228 |
PRK09228 |
guanine deaminase; Provisional |
22-405 |
9.20e-105 |
|
guanine deaminase; Provisional
Pssm-ID: 236419 [Multi-domain] Cd Length: 433 Bit Score: 316.36 E-value: 9.20e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191704909 22 EIRELSHHeFFMPGLVDTHIHASQYSFAGSsidlP---LLEWLTKYTFPAEHRFQNIDFAEEVYTRVVRRTLKNGTTTAC 98
Cdd:PRK09228 59 EVTDYRGK-LILPGFIDTHIHYPQTDMIAS----YgeqLLDWLNTYTFPEERRFADPAYAREVAEFFLDELLRNGTTTAL 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191704909 99 YFATIHTDSsllladiTDKF-------GQRAFVGKVCMDLNdtFPEY-KETTEESIKETERfvseMLQK--NYSRVKPIV 168
Cdd:PRK09228 134 VFGTVHPQS-------VDALfeaaearNMRMIAGKVLMDRN--APDGlRDTAESGYDDSKA----LIERwhGKGRLLYAI 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191704909 169 TPRFSLSCSETLMGELGNIAKTR-DLHIQSHISENRDEVEAVKNLYPSYKNYTSVYDKNNLLTNKTVMAHGCYLSAEELN 247
Cdd:PRK09228 201 TPRFAPTSTPEQLEAAGALAREHpDVWIQTHLSENLDEIAWVKELFPEARDYLDVYERYGLLGPRAVFAHCIHLEDRERR 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191704909 248 VFHERGASIAHCPNSNLSLSSGFLNVLEVLKHEVKIGLGTDVAGGYSYSMLDAIRRAVMVSnillinKVNEKSLTLKEVF 327
Cdd:PRK09228 281 RLAETGAAIAFCPTSNLFLGSGLFDLKRADAAGVRVGLGTDVGGGTSFSMLQTMNEAYKVQ------QLQGYRLSPFQAF 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191704909 328 RLATLGGSQALGLDGEIGNFEVGKEFDAILINPKA----------SDSPIDLFYGdffgdiseaviqkFLYLGDDRNIEE 397
Cdd:PRK09228 355 YLATLGGARALGLDDRIGNLAPGKEADFVVLDPAAtpllalrtarAESLEELLFA-------------LMTLGDDRAVAE 421
|
....*...
gi 1191704909 398 VYVGGKQV 405
Cdd:PRK09228 422 TYVAGRPV 429
|
|
| ATZ_TRZ_like |
cd01298 |
TRZ/ATZ family contains enzymes from the atrazine degradation pathway and related hydrolases. ... |
33-406 |
4.51e-71 |
|
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: 229.01 E-value: 4.51e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191704909 33 MPGLVDTHIHASQYSFAGSSIDLPLLEWLTKYTFPAEHRFQnidfAEEVY--TRV-VRRTLKNGTTTAC--YFatIHTDS 107
Cdd:cd01298 55 MPGLVNTHTHLAMTLLRGLADDLPLMEWLKDLIWPLERLLT----EEDVYlgALLaLAEMIRSGTTTFAdmYF--FYPDA 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191704909 108 sllLADITDKFGQRAFVGKVCMDLNDtfpEYKETTEESIKETERFVSEMLQKNYSRVKPIVTPRFSLSCSETLMGELGNI 187
Cdd:cd01298 129 ---VAEAAEELGIRAVLGRGIMDLGT---EDVEETEEALAEAERLIREWHGAADGRIRVALAPHAPYTCSDELLREVAEL 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191704909 188 AKTRDLHIQSHISENRDEVEAVKNLYpsykNYTSV-Y-DKNNLLTNKTVMAHGCYLSAEELNVFHERGASIAHCPNSNLS 265
Cdd:cd01298 203 AREYGVPLHIHLAETEDEVEESLEKY----GKRPVeYlEELGLLGPDVVLAHCVWLTDEEIELLAETGTGVAHNPASNMK 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191704909 266 LSSGFLNVLEVLKHEVKIGLGTD-VAGGYSYSMLDAIRRAvmvsniLLINKV---NEKSLTLKEVFRLATLGGSQALGLD 341
Cdd:cd01298 279 LASGIAPVPEMLEAGVNVGLGTDgAASNNNLDMFEEMRLA------ALLQKLahgDPTALPAEEALEMATIGGAKALGLD 352
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1191704909 342 gEIGNFEVGKEFDAILINPkasDSPidlfygDFFG---DISEAViqkflYLGDDRNIEEVYVGGKQVV 406
Cdd:cd01298 353 -EIGSLEVGKKADLILIDL---DGP------HLLPvhdPISHLV-----YSANGGDVDTVIVNGRVVM 405
|
|
| PRK07228 |
PRK07228 |
5'-deoxyadenosine deaminase; |
33-359 |
2.15e-61 |
|
5'-deoxyadenosine deaminase;
Pssm-ID: 180895 [Multi-domain] Cd Length: 445 Bit Score: 204.85 E-value: 2.15e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191704909 33 MPGLVDTHIHASQYSFAGSSIDLPLLEWLTKYTFPAE--HRfqnidfAEEVYTRV---VRRTLKNGTTTACYFATI-HTD 106
Cdd:PRK07228 55 IPGLIQGHIHLCQTLFRGIADDLELLDWLKDRIWPLEaaHD------AESMYYSAllgIGELIESGTTTIVDMESVhHTD 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191704909 107 SSL-LLADItdkfGQRAFVGKVCMDLNDTFPE-YKETTEESIKETERFVSEMLQKNYSRVKPIVTPRFSLSCSETLMGEL 184
Cdd:PRK07228 129 SAFeAAGES----GIRAVLGKVMMDYGDDVPEgLQEDTEASLAESVRLLEKWHGADNGRIRYAFTPRFAVSCTEELLRGV 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191704909 185 GNIAKTRDLHIQSHISENRDEVEAVKNlYPSYKNYTsVYDKNNLLTNKTVMAHGCYLSAEELNVFHERGASIAHCPNSNL 264
Cdd:PRK07228 205 RDLADEYGVRIHTHASENRGEIETVEE-ETGMRNIH-YLDEVGLTGEDLILAHCVWLDEEEREILAETGTHVTHCPSSNL 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191704909 265 SLSSGFLNVLEVLKHEVKIGLGTDvaGGYSYSMLDA---IRRAVmvsnilLINKVNE---KSLTLKEVFRLATLGGSQAL 338
Cdd:PRK07228 283 KLASGIAPVPDLLERGINVALGAD--GAPCNNTLDPfteMRQAA------LIQKVDRlgpTAMPARTVFEMATLGGAKAA 354
|
330 340
....*....|....*....|.
gi 1191704909 339 GLDGEIGNFEVGKEFDAILIN 359
Cdd:PRK07228 355 GFEDEIGSLEEGKKADLAILD 375
|
|
| Amidohydro_1 |
pfam01979 |
Amidohydrolase family; This family of enzymes are a a large metal dependent hydrolase ... |
33-405 |
1.03e-56 |
|
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: 189.64 E-value: 1.03e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191704909 33 MPGLVDTHIHASQYSFAGSSIDLpllewltkytfpaehrfqniDFAEEVYTRVVRRTLKNGTTTACYFATIHTDSSLLLA 112
Cdd:pfam01979 3 LPGLIDAHVHLEMGLLRGIPVPP--------------------EFAYEALRLGITTMLKSGTTTVLDMGATTSTGIEALL 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191704909 113 DITDK--FGQRAFVGKVCMDLNDTFPEYKETTEESIKETErfvsEMLQKNYSRVKPIVTPRFSLSCSETLMGELGNIAKT 190
Cdd:pfam01979 63 EAAEElpLGLRFLGPGCSLDTDGELEGRKALREKLKAGAE----FIKGMADGVVFVGLAPHGAPTFSDDELKAALEEAKK 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191704909 191 RDLHIQSHISENRDEVEAVKNLYPS---YKNYTSVYDKNNLL-TNKTVMAHGCYLSAEELNVFHER--GASIAHCPNSNL 264
Cdd:pfam01979 139 YGLPVAIHALETKGEVEDAIAAFGGgieHGTHLEVAESGGLLdIIKLILAHGVHLSPTEANLLAEHlkGAGVAHCPFSNS 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191704909 265 SLSSGFLNVLEVLKHEVKIGLGTDVAG-GYSYSMLDAIRRAVmvsnilLINKVNEKSLTLKEVFRLATLGGSQALGLDGE 343
Cdd:pfam01979 219 KLRSGRIALRKALEDGVKVGLGTDGAGsGNSLNMLEELRLAL------ELQFDPEGGLSPLEALRMATINPAKALGLDDK 292
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1191704909 344 IGNFEVGKEFDAILINPKasdspidlfygdffgdiseaVIQKFLYLGDDRNIEEVYVGGKQV 405
Cdd:pfam01979 293 VGSIEVGKDADLVVVDLD--------------------PLAAFFGLKPDGNVKKVIVKGKIV 334
|
|
| PRK08393 |
PRK08393 |
N-ethylammeline chlorohydrolase; Provisional |
29-406 |
9.51e-47 |
|
N-ethylammeline chlorohydrolase; Provisional
Pssm-ID: 181411 [Multi-domain] Cd Length: 424 Bit Score: 165.74 E-value: 9.51e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191704909 29 HEFFMPGLVDTHIHASQYSFAGSSIDLPLLEWLTKYTFPAEHRFQNIDFAEEVYTRVVRrTLKNGTTTAC--YFatiHTD 106
Cdd:PRK08393 49 GSVVSPGFINAHTHSPMVLLRGLADDVPLMEWLQNYIWPRERKLKRKDIYWGAYLGLLE-MIKSGTTTFVdmYF---HME 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191704909 107 SsllLADITDKFGQRAFVGKVCMDLNDtfpeyKETTEESIKETERFVSEMLQKNYSRVKPIVTPRFSLSCSETLMGELGN 186
Cdd:PRK08393 125 E---VAKATLEVGLRGYLSYGMVDLGD-----EEKREKEIKETEKLMEFIEKLNSPRVHFVFGPHAPYTCSLALLKWVRE 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191704909 187 IAKTRDLHIQSHISENRDEVEAVKNLYPsyKNYTSVYDKNNLLTNKTVMAHGCYLSAEELNVFHERGASIAHCPNSNLSL 266
Cdd:PRK08393 197 KAREWNKLITIHLSETMDEIKQIREKYG--KSPVVLLDEIGFLNEDVIAAHGVWLSSRDIRILASAGVTVAHNPASNMKL 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191704909 267 SSGFLNVLEVLKHEVKIGLGTDvaGGYSYSMLDAIRRAVMVSnilLINKVNEKSLTL---KEVFRLATLGGSQALGLDGe 343
Cdd:PRK08393 275 GSGVMPLRKLLNAGVNVALGTD--GAASNNNLDMLREMKLAA---LLHKVHNLDPTIadaETVFRMATQNGAKALGLKA- 348
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1191704909 344 iGNFEVGKEFDAILIN-PKASDSPIDlfygdffgdiseAVIQKFLYLGDDRNIEEVYVGGKQVV 406
Cdd:PRK08393 349 -GVIKEGYLADIAVIDfNRPHLRPIN------------NPISHLVYSANGNDVETTIVDGKIVM 399
|
|
| PRK06038 |
PRK06038 |
N-ethylammeline chlorohydrolase; Provisional |
28-361 |
4.11e-44 |
|
N-ethylammeline chlorohydrolase; Provisional
Pssm-ID: 180363 [Multi-domain] Cd Length: 430 Bit Score: 158.76 E-value: 4.11e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191704909 28 HHEFFMPGLVDTHIHASQYSFAGSSIDLPLLEWLTKYTFPAEHRFQnidfAEEVYTRVVRRTL---KNGTTTacyFAT-- 102
Cdd:PRK06038 49 KGSVVMPGLVNTHTHAAMTLFRGYADDLPLAEWLNDHIWPAEAKLT----AEDVYAGSLLACLemiKSGTTS---FADmy 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191704909 103 IHTDSSlllADITDKFGQRAFVGKVCMDLNDTfpeykETTEESIKETERFVSEMLQKNYSRVKPIVTPRFSLSCSETLMG 182
Cdd:PRK06038 122 FYMDEV---AKAVEESGLRAALSYGMIDLGDD-----EKGEAELKEGKRFVKEWHGAADGRIKVMYGPHAPYTCSEEFLS 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191704909 183 ELGNIAKTRDLHIQSHISENRDEVEAVKNLYpsykNYTSVY--DKNNLLTNKTVMAHGCYLSAEELNVFHERGASIAHCP 260
Cdd:PRK06038 194 KVKKLANKDGVGIHIHVLETEAELNQMKEQY----GMCSVNylDDIGFLGPDVLAAHCVWLSDGDIEILRERGVNVSHNP 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191704909 261 NSNLSLSSGFLNVLEVLKHEVKIGLGTD-VAGGYSYSMLDAIRRAVMVSNillINKVNEKSLTLKEVFRLATLGGSQALG 339
Cdd:PRK06038 270 VSNMKLASGIAPVPKLLERGVNVSLGTDgCASNNNLDMFEEMKTAALLHK---VNTMDPTALPARQVLEMATVNGAKALG 346
|
330 340
....*....|....*....|..
gi 1191704909 340 LdgEIGNFEVGKEFDAILINPK 361
Cdd:PRK06038 347 I--NTGMLKEGYLADIIIVDMN 366
|
|
| PRK09045 |
PRK09045 |
TRZ/ATZ family hydrolase; |
18-406 |
2.66e-43 |
|
TRZ/ATZ family hydrolase;
Pssm-ID: 236366 [Multi-domain] Cd Length: 443 Bit Score: 157.00 E-value: 2.66e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191704909 18 FKPCEIRELSHHeFFMPGLVDTHIHASQYSFAGSSIDLPLLEWLTKYTFPAEHRFQNIDFAEEVYTRVVRRTLKNGTTTA 97
Cdd:PRK09045 51 YAAAETVELPDH-VLIPGLINAHTHAAMSLLRGLADDLPLMTWLQDHIWPAEGAWVSEEFVRDGTLLAIAEMLRGGTTCF 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191704909 98 --CYFatiHTDSsllLADITDKFGQRAFVGKVCMDlndtFP-EYKETTEESI----KETERFvsemlqKNYSRVKPIVTP 170
Cdd:PRK09045 130 ndMYF---FPEA---AAEAAHQAGMRAQIGMPVLD----FPtAWASDADEYLakglELHDQW------RHHPLISTAFAP 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191704909 171 RFSLSCSETLMGELGNIAKTRDLHIQSHISENRDEVEAvknlypSYKNY----TSVYDKNNLLTNKTVMAHGCYLSAEEL 246
Cdd:PRK09045 194 HAPYTVSDENLERIRTLAEQLDLPIHIHLHETAQEIAD------SLKQHgqrpLARLARLGLLGPRLIAVHMTQLTDAEI 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191704909 247 NVFHERGASIAHCPNSNLSLSSGFLNVLEVLKHEVKIGLGTD-VAGGYSYSMLDAIRRAVMVSnillinKV---NEKSLT 322
Cdd:PRK09045 268 ALLAETGCSVVHCPESNLKLASGFCPVAKLLQAGVNVALGTDgAASNNDLDLFGEMRTAALLA------KAvagDATALP 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191704909 323 LKEVFRLATLGGSQALGLDGEIGNFEVGKEFDAILINPKASDS-PIdlfygdfFGDISEAViqkflYLGDDRNIEEVYVG 401
Cdd:PRK09045 342 AHTALRMATLNGARALGLDDEIGSLEPGKQADLVAVDLSGLETqPV-------YDPVSQLV-----YAAGREQVSHVWVA 409
|
....*
gi 1191704909 402 GKQVV 406
Cdd:PRK09045 410 GKQLL 414
|
|
| PRK06687 |
PRK06687 |
TRZ/ATZ family protein; |
31-406 |
8.68e-42 |
|
TRZ/ATZ family protein;
Pssm-ID: 180657 [Multi-domain] Cd Length: 419 Bit Score: 152.47 E-value: 8.68e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191704909 31 FFMPGLVDTHIHASQYSFAGSSIDLPLLEWLTKYTFPAEHRFqNIDFAEEVYTRVVRRTLKNGTTTacyFATIHTDSSLL 110
Cdd:PRK06687 55 WIMPGLVNCHTHSAMTGLRGIRDDSNLHEWLNDYIWPAESEF-TPDMTTNAVKEALTEMLQSGTTT---FNDMYNPNGVD 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191704909 111 LADITDKFGQRafvGKVCMDLNDTFPEYKETTEESIKETERFVSEMLQKNYSRVKPIVTPRFSLSCSETLMGELGNIAKT 190
Cdd:PRK06687 131 IQQIYQVVKTS---KMRCYFSPTLFSSETETTAETISRTRSIIDEILKYKNPNFKVMVAPHSPYSCSRDLLEASLEMAKE 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191704909 191 RDLHIQSHISENRDEVEAVKNLYPsyKNYTSVYDKNNLLTNKTVMAHGCYLSAEELNVFHERGASIAHCPNSNLSLSSGF 270
Cdd:PRK06687 208 LNIPLHVHVAETKEESGIILKRYG--KRPLAFLEELGYLDHPSVFAHGVELNEREIERLASSQVAIAHNPISNLKLASGI 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191704909 271 LNVLEVLKHEVKIGLGTD-VAGGYSYSMLDAIRRAVMVSNillINKVNEKSLTLKEVFRLATLGGSQALGLDGEIGNFEV 349
Cdd:PRK06687 286 APIIQLQKAGVAVGIATDsVASNNNLDMFEEGRTAALLQK---MKSGDASQFPIETALKVLTIEGAKALGMENQIGSLEV 362
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 1191704909 350 GKEFDAILINPKASdspIDLFygdffgdISEAVIQKFLYLGDDRNIEEVYVGGKQVV 406
Cdd:PRK06687 363 GKQADFLVIQPQGK---IHLQ-------PQENMLSHLVYAVKSSDVDDVYIAGEQVV 409
|
|
| PRK15493 |
PRK15493 |
bifunctional S-methyl-5'-thioadenosine deaminase/S-adenosylhomocysteine deaminase; |
30-406 |
1.75e-33 |
|
bifunctional S-methyl-5'-thioadenosine deaminase/S-adenosylhomocysteine deaminase;
Pssm-ID: 185390 [Multi-domain] Cd Length: 435 Bit Score: 129.79 E-value: 1.75e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191704909 30 EFFMPGLVDTHIHASQYSFAGSSIDLPLLEWLTKYTFPAEHRFQNiDFAEEVYTRVVRRTLKNGTTT-ACYFATIHTDSS 108
Cdd:PRK15493 55 KWVLPGLVNTHTHVVMSLLRGIGDDMLLQPWLETRIWPLESQFTP-ELAVASTELGLLEMVKSGTTSfSDMFNPIGVDQD 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191704909 109 LLLADITDKfGQRAFVGKVCMDLNDtfpeyKETTEESIKETERFVSEMLQKNySRVKPIVTPRFSLSCSETLMGELGNIA 188
Cdd:PRK15493 134 AIMETVSRS-GMRAAVSRTLFSFGT-----KEDEKKAIEEAEKYVKRYYNES-GMLTTMVAPHSPYTCSTELLEECARIA 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191704909 189 KTRDLHIQSHISENRDEVEAVKNLYPsyKNYTSVYDKNNLLTNKTVMAHGCYLSAEELNVFHERGASIAHCPNSNLSLSS 268
Cdd:PRK15493 207 VENQTMVHIHLSETEREVRDIEAQYG--KRPVEYAASCGLFKRPTVIAHGVVLNDNERAFLAEHDVRVAHNPNSNLKLGS 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191704909 269 GFLNVLEVLKHEVKIGLGTD-VAGGYSYSMLDAIRRAVMVSNILlinKVNEKSLTLKEVFRLATLGGSQALGLDgEIGNF 347
Cdd:PRK15493 285 GIANVKAMLEAGIKVGIATDsVASNNNLDMFEEMRIATLLQKGI---HQDATALPVETALTLATKGAAEVIGMK-QTGSL 360
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1191704909 348 EVGKEFDAILINP--KASDSPidlfygdffgdiSEAVIQKFLYLGDDRNIEEVYVGGKQVV 406
Cdd:PRK15493 361 EVGKCADFITIDPsnKPHLQP------------ADEVLSHLVYAASGKDISDVIINGKRVV 409
|
|
| PRK06380 |
PRK06380 |
metal-dependent hydrolase; Provisional |
33-403 |
1.43e-25 |
|
metal-dependent hydrolase; Provisional
Pssm-ID: 180548 [Multi-domain] Cd Length: 418 Bit Score: 107.28 E-value: 1.43e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191704909 33 MPGLVDTHIHASQYSFAGSSIDLPLLEWLTKyTFPAEHRFQNidfaEEVYTRV---VRRTLKNGTTTacyFATIHTDSSL 109
Cdd:PRK06380 53 MPGLINTHAHVGMTASKGLFDDVDLEEFLMK-TFKYDSKRTR----EGIYNSAklgMYEMINSGITA---FVDLYYSEDI 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191704909 110 LlADITDKFGQRAFVGKVCMDlndtfPEYKETTEESIKETERFVSEMLQKNYsrVKPIVTPRFSLSCSETLMGELGNIAK 189
Cdd:PRK06380 125 I-AKAAEELGIRAFLSWAVLD-----EEITTQKGDPLNNAENFIREHRNEEL--VTPSIGVQGIYVANDETYLKAKEIAE 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191704909 190 TRDLHIQSHISENRDEVeavknlYPSYKNY----TSVYDKNNLLTNKTVMAHGCYLSAEELNVFHERGASIAHCPNSNLS 265
Cdd:PRK06380 197 KYDTIMHMHLSETRKEV------YDHVKRTgerpVEHLEKIGFLNSKLIAAHCVWATYHEIKLLSKNGVKVSWNSVSNFK 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191704909 266 LSS-GFLNVLEVLKHEVKIGLGTDVAGgySYSMLDAIrRAVMVSNILLINKVNEKSLT-LKEVFRLATLGGSQALGLDGe 343
Cdd:PRK06380 271 LGTgGSPPIPEMLDNGINVTIGTDSNG--SNNSLDMF-EAMKFSALSVKNERWDASIIkAQEILDFATINAAKALELNA- 346
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191704909 344 iGNFEVGKEFDAILINPKASdSPIDLFYGDFFGDIseaviqkfLYLGDDRNIEEVYVGGK 403
Cdd:PRK06380 347 -GSIEVGKLADLVILDARAP-NMIPTRKNNIVSNI--------VYSLNPLNVDHVIVNGK 396
|
|
| PRK12393 |
PRK12393 |
amidohydrolase; Provisional |
34-406 |
1.85e-23 |
|
amidohydrolase; Provisional
Pssm-ID: 237088 [Multi-domain] Cd Length: 457 Bit Score: 101.68 E-value: 1.85e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191704909 34 PGLVDTHIHASQYSFAG--SSIDLPLLEWL--TKYTFPA---EHRFQ---NIDFAEevytrvvrrTLKNGTTTAC----- 98
Cdd:PRK12393 59 PGWVNTHHHLFQSLLKGvpAGINQSLTAWLaaVPYRFRArfdEDLFRlaaRIGLVE---------LLRSGCTTVAdhhyl 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191704909 99 YFATIHTDSSLLLADITDKFGQRaFV---GKVCMDLNDTfPEYK-----ETTEESIKETERFVSEMLQKNYSRVKPIV-- 168
Cdd:PRK12393 130 YHPGMPFDTGDILFDEAEALGMR-FVlcrGGATQTRGDH-PGLPtalrpETLDQMLADVERLVSRYHDASPDSLRRVVva 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191704909 169 --TPRFSLScsETLMGELGNIAKTRDLHIQSHISENRDEVEAVKNLYpsykNYTSVY--DKNNLLTNKTVMAHGCYLSAE 244
Cdd:PRK12393 208 ptTPTFSLP--PELLREVARAARGMGLRLHSHLSETVDYVDFCREKY----GMTPVQfvAEHDWLGPDVWFAHLVKLDAE 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191704909 245 ELNVFHERGASIAHCPNSNLSLSSGFLNVLEVLKHEVKIGLGTD-VAGGYSYSMLDAIRRAVMVSNILlinkVNEKSLTL 323
Cdd:PRK12393 282 EIALLAQTGTGIAHCPQSNGRLGSGIAPALAMEAAGVPVSLGVDgAASNESADMLSEAHAAWLLHRAE----GGADATTV 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191704909 324 KEVFRLATLGGSQALGLDgEIGNFEVGKEFDAILINpkaSDSPidLFYGdfFGDISEAVIQKflylGDDRNIEEVYVGGK 403
Cdd:PRK12393 358 EDVVHWGTAGGARVLGLD-AIGTLAVGQAADLAIYD---LDDP--RFFG--LHDPAIAPVAC----GGPAPVKALLVNGR 425
|
...
gi 1191704909 404 QVV 406
Cdd:PRK12393 426 PVV 428
|
|
| PRK08203 |
PRK08203 |
hydroxydechloroatrazine ethylaminohydrolase; Reviewed |
33-354 |
1.55e-22 |
|
hydroxydechloroatrazine ethylaminohydrolase; Reviewed
Pssm-ID: 236184 [Multi-domain] Cd Length: 451 Bit Score: 98.77 E-value: 1.55e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191704909 33 MPGLVDTHIHASQYSFAG--SSIDLPLLEWLTK-YTFPAehrfqNIDfAEEVY--TRV-VRRTLKNGTTTAcyfaTIH-- 104
Cdd:PRK08203 58 TPGLVNTHHHFYQTLTRAlpAAQDAELFPWLTTlYPVWA-----RLT-PEMVRvaTQTaLAELLLSGCTTS----SDHhy 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191704909 105 ---TDSSLLLADITD---KFGQRAFVGKVCMDLN--------DTFPEyketTEESI-KETERFVSEMLQKN-YSRVKPIV 168
Cdd:PRK08203 128 lfpNGLRDALDDQIEaarEIGMRFHATRGSMSLGesdgglppDSVVE----DEDAIlADSQRLIDRYHDPGpGAMLRIAL 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191704909 169 TPRFSLSCSETLMGELGNIAKTRDLHIQSHISENRDEVEAVKNLYpsykNYTSV-Y-DKNNLLTNKTVMAHGCYLSAEEL 246
Cdd:PRK08203 204 APCSPFSVSRELMRESAALARRLGVRLHTHLAETLDEEAFCLERF----GMRPVdYlEDLGWLGPDVWLAHCVHLDDAEI 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191704909 247 NVFHERGASIAHCPNSNLSLSSGFLNVLEVLKHEVKIGLGTD-VAGGYSYSMLDAIRRAvmvsniLLINKV--NEKSLTL 323
Cdd:PRK08203 280 ARLARTGTGVAHCPCSNMRLASGIAPVRELRAAGVPVGLGVDgSASNDGSNLIGEARQA------LLLQRLryGPDAMTA 353
|
330 340 350
....*....|....*....|....*....|.
gi 1191704909 324 KEVFRLATLGGSQALGLDgEIGNFEVGKEFD 354
Cdd:PRK08203 354 REALEWATLGGARVLGRD-DIGSLAPGKLAD 383
|
|
| Met_dep_hydrolase_D |
cd01312 |
Metallo-dependent hydrolases, subgroup D is part of the superfamily of metallo-dependent ... |
29-354 |
2.72e-20 |
|
Metallo-dependent hydrolases, subgroup D 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: 238637 [Multi-domain] Cd Length: 381 Bit Score: 91.74 E-value: 2.72e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191704909 29 HEFF-----MPGLVDTHIH------ASQYSFAGSSIdlplleWLTKY-TFPAEHRFQNidfAEEVYTRVVRRTLKNGTTT 96
Cdd:cd01312 21 HEFFpngvlLPGLINAHTHlefsanVAQFTYGRFRA------WLLSViNSRDELLKQP---WEEAIRQGIRQMLESGTTS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191704909 97 AcyfATIHTDSSLLLADITDKFGQRAFVGKVCMDlNDTFPEYKETTEESIKETERFVSemlqknySRVKPIVTPRFSLSC 176
Cdd:cd01312 92 I---GAISSDGSLLPALASSGLRGVFFNEVIGSN-PSAIDFKGETFLERFKRSKSFES-------QLFIPAISPHAPYSV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191704909 177 SETLMGELGNIAKTRDLHIQSHISENRDEVEAV-------KNLYPSY---KNYTSVYDKNNL------LTNKTVMAHGCY 240
Cdd:cd01312 161 HPELAQDLIDLAKKLNLPLSTHFLESKEEREWLeeskgwfKHFWESFlklPKPKKLATAIDFldmlggLGTRVSFVHCVY 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191704909 241 LSAEELNVFHERGASIAHCPNSNLSLSSGFLNVLEVLKHEVKIGLGTD-VAGGYSYSMLDAIRravmvSNILLINKVNEK 319
Cdd:cd01312 241 ANLEEAEILASRGASIALCPRSNRLLNGGKLDVSELKKAGIPVSLGTDgLSSNISLSLLDELR-----ALLDLHPEEDLL 315
|
330 340 350
....*....|....*....|....*....|....*
gi 1191704909 320 SLTlKEVFRLATLGGSQALGLdgEIGNFEVGKEFD 354
Cdd:cd01312 316 ELA-SELLLMATLGGARALGL--NNGEIEAGKRAD 347
|
|
| metallo-dependent_hydrolases |
cd01292 |
Superfamily of metallo-dependent hydrolases (also called amidohydrolase superfamily) is a ... |
36-337 |
2.46e-19 |
|
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: 87.39 E-value: 2.46e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191704909 36 LVDTHIHASQYSFAGssIDLPLLEWLTKYTFPAEHRFQNIDFAEEvytrvvrrTLKNGTTTAC-----YFATIHTDSSLL 110
Cdd:cd01292 1 FIDTHVHLDGSALRG--TRLNLELKEAEELSPEDLYEDTLRALEA--------LLAGGVTTVVdmgstPPPTTTKAAIEA 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191704909 111 LAD-ITDKFGQRAFVGKVCMDLNdtfPEYKETTEESIKETERFVsemlqknYSRVKPIVTPRFSLSCSETLMGELGNI-- 187
Cdd:cd01292 71 VAEaARASAGIRVVLGLGIPGVP---AAVDEDAEALLLELLRRG-------LELGAVGLKLAGPYTATGLSDESLRRVle 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191704909 188 -AKTRDLHIQSHISENRDEVEAVKNLYpsyknytsvydKNNLLTNKTVMAHGCYLSAEELNVFHERGASIAHCPNSNLSL 266
Cdd:cd01292 141 eARKLGLPVVIHAGELPDPTRALEDLV-----------ALLRLGGRVVIGHVSHLDPELLELLKEAGVSLEVCPLSNYLL 209
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1191704909 267 SS---GFLNVLEVLKHEVKIGLGTDVAGGYSYSMLDAIRRAVMVSNILLinkvneksLTLKEVFRLATLGGSQA 337
Cdd:cd01292 210 GRdgeGAEALRRLLELGIRVTLGTDGPPHPLGTDLLALLRLLLKVLRLG--------LSLEEALRLATINPARA 275
|
|
| PRK08204 |
PRK08204 |
hypothetical protein; Provisional |
33-403 |
2.62e-19 |
|
hypothetical protein; Provisional
Pssm-ID: 181288 [Multi-domain] Cd Length: 449 Bit Score: 89.29 E-value: 2.62e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191704909 33 MPGLVDTHIHASQYSFAGSSIDLPLLEWLTKYTFPAEHRFQnidfAEEVY--TRV-VRRTLKNGTTTACYFATI-----H 104
Cdd:PRK08204 56 MPGLVDTHRHTWQSVLRGIGADWTLQTYFREIHGNLGPMFR----PEDVYiaNLLgALEALDAGVTTLLDWSHInnspeH 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191704909 105 TDSSLL-LADItdkfGQRA--FVGKVCMDLNDTFpeykETTEESIKETERFVSEMLQKNYSRVK---PIVTPRFSlsCSE 178
Cdd:PRK08204 132 ADAAIRgLAEA----GIRAvfAHGSPGPSPYWPF----DSVPHPREDIRRVKKRYFSSDDGLLTlglAIRGPEFS--SWE 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191704909 179 TLMGELGnIAKTRDLHIQSHISenrdeveavknLYPSYKNYTSV--YDKNNLLTNKTVMAHGCYLSAEELNVFHERGASI 256
Cdd:PRK08204 202 VARADFR-LARELGLPISMHQG-----------FGPWGATPRGVeqLHDAGLLGPDLNLVHGNDLSDDELKLLADSGGSF 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191704909 257 AHCPNSNLSLSSGFLNVLEVLKHEVKIGLGTDVAGGYSYSMLDAIR------RAVMVSNILLINKV--NEKSLTLKEVFR 328
Cdd:PRK08204 270 SVTPEIEMMMGHGYPVTGRLLAHGVRPSLGVDVVTSTGGDMFTQMRfalqaeRARDNAVHLREGGMppPRLTLTARQVLE 349
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1191704909 329 LATLGGSQALGLDGEIGNFEVGKEFDAILINPKAsdspIDLFYgdfFGDISEAVIQkflyLGDDRNIEEVYVGGK 403
Cdd:PRK08204 350 WATIEGARALGLEDRIGSLTPGKQADLVLIDATD----LNLAP---VHDPVGAVVQ----SAHPGNVDSVMVAGR 413
|
|
| PRK08418 |
PRK08418 |
metal-dependent hydrolase; |
186-406 |
2.64e-19 |
|
metal-dependent hydrolase;
Pssm-ID: 181419 [Multi-domain] Cd Length: 408 Bit Score: 88.87 E-value: 2.64e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191704909 186 NIAKTRDLHIQSHISENRDEVEAVKNLYPSYKNY--------TSVYDKNNLL----TNKTVMAHGCYLSAEELNVFHERG 253
Cdd:PRK08418 197 QLAKKENLLVSTHFLESKAEREWLEESKGWFKKFfekflkepKPLYTPKEFLelfkGLRTLFTHCVYASEEELEKIKSKN 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191704909 254 ASIAHCPNSNLSLSSGFLNVLEVLKHEVKIGLGTD-VAGGYSYSMLDAIRRAVMVSNillinkvNEKSLTL-KEVFRLAT 331
Cdd:PRK08418 277 ASITHCPFSNRLLSNKALDLEKAKKAGINYSIATDgLSSNISLSLLDELRAALLTHA-------NMPLLELaKILLLSAT 349
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1191704909 332 LGGSQALGLD-GEIgnfEVGKEFDAILINpkasdspidlfYGDFFGDISEAVIQKFLYlgdDRNIEEVYVGGKQVV 406
Cdd:PRK08418 350 RYGAKALGLNnGEI---KEGKDADLSVFE-----------LPEECTKKEQLPLQFILH---AKEVKKLFIGGKEVK 408
|
|
| PRK07203 |
PRK07203 |
putative aminohydrolase SsnA; |
33-311 |
1.21e-17 |
|
putative aminohydrolase SsnA;
Pssm-ID: 235963 [Multi-domain] Cd Length: 442 Bit Score: 84.22 E-value: 1.21e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191704909 33 MPGLVDTHIHAsqYS-FA-GSSIDLP----LLEWLTKYTFpaehrfqNIDFA---EEVYTRVVRRTL---KNGTTT---- 96
Cdd:PRK07203 58 MPGLINSHNHI--YSgLArGMMANIPpppdFISILKNLWW-------RLDRAltlEDVYYSALICSLeaiKNGVTTvfdh 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191704909 97 -ACYFATihTDSSLLLADITDKFGQRafvGKVCMDLNDTFPEykETTEESIKETERFVSEMLQKNYSRVKPIVTPRFSLS 175
Cdd:PRK07203 129 hASPNYI--GGSLFTIADAAKKVGLR---AMLCYETSDRDGE--KELQEGVEENIRFIKHIDEAKDDMVEAMFGLHASFT 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191704909 176 CS-ETL------MGELGniaktRDLHIqsHISENRDEVEAVKNLYpsYKNYTSVYDKNNLLTNKTVMAHGCYLSAEELNV 248
Cdd:PRK07203 202 LSdATLekcreaVKETG-----RGYHI--HVAEGIYDVSDSHKKY--GKDIVERLADFGLLGEKTLAAHCIYLSDEEIDL 272
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1191704909 249 FHERGASIAHCPNSNLSLSSGFLNVLEVLKHEVKIGLGTDvagGYSYSMLDAIRravmVSNIL 311
Cdd:PRK07203 273 LKETDTFVVHNPESNMGNAVGYNPVLEMIKNGILLGLGTD---GYTSDMFESYK----VANFK 328
|
|
| archeal_chlorohydrolases |
cd01305 |
Predicted chlorohydrolases. These metallo-dependent hydrolases from archea are part of the ... |
33-335 |
1.84e-14 |
|
Predicted chlorohydrolases. These metallo-dependent hydrolases from archea are 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. They 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. Some members of this subgroup are predicted to be chlorohyrolases.
Pssm-ID: 238630 [Multi-domain] Cd Length: 263 Bit Score: 72.82 E-value: 1.84e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191704909 33 MPGLVDTHIHASQYSFAGSSIDLPLLEwLTKYTFPAEHRF--QNIDFAEEVYTR-VVRRTLKNGTTTACYFATIHTDSSL 109
Cdd:cd01305 3 IPALVNAHTHLGDSAIKEVGDGLPLDD-LVAPPDGLKHRLlaQADDRELAEAMRkVLRDMRETGIGAFADFREGGVEGIE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191704909 110 LLADITDKFgqrAFVGKVCMDlndtFPEYKETTEESIKETERFvsemlqkNYSrvkpivtprfslSCSETLMGELGNIAK 189
Cdd:cd01305 82 LLRRALGKL---PVPFEVILG----RPTEPDDPEILLEVADGL-------GLS------------SANDVDLEDILELLR 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191704909 190 TRDLHIQSHISENRD-----EVEAVKNLYPsyknytsvydknNLLTnktvmaHGCYLSAEELNVFHERGASIAHCPNSNL 264
Cdd:cd01305 136 RRGKLFAIHASETREsvgmtDIERALDLEP------------DLLV------HGTHLTDEDLELVRENGVPVVLCPRSNL 197
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1191704909 265 SLSSGFLNVLEVLKHEVKIGLGTDVAGGYSYSMLDAIRRAVMVSNILlinkvneKSLTLKEVFRLATLGGS 335
Cdd:cd01305 198 YFGVGIPPVAELLKLGIKVLLGTDNVMVNEPDMWAEMEFLAKYSRLQ-------GYLSPLEILRMATVNAA 261
|
|
| PRK06151 |
PRK06151 |
N-ethylammeline chlorohydrolase; Provisional |
33-406 |
8.96e-14 |
|
N-ethylammeline chlorohydrolase; Provisional
Pssm-ID: 180428 [Multi-domain] Cd Length: 488 Bit Score: 72.77 E-value: 8.96e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191704909 33 MPGLVDTHIHasqysfagSSIDLPLL------EWLTKYTFPAEHRFQNidfAEEVYTRVVRRT---------LKNGTTTA 97
Cdd:PRK06151 56 GPGFIDLDAL--------SDLDTTILgldngpGWAKGRVWSRDYVEAG---RREMYTPEELAFqkryafaqlLRNGITTA 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191704909 98 CYFATI-------HTDSSLLLADITDKFGQRAFVG-------KVCMDLNDTFPEYKETT-EESIKETERFVSEMLQKNYS 162
Cdd:PRK06151 125 MPIASLfyrqwaeTYAEFAAAAEAAGRLGLRVYLGpayrsggSVLEADGSLEVVFDEARgLAGLEEAIAFIKRVDGAHNG 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191704909 163 RVKPIVTPRFSLSCSETLMGELGNIAKTRDLHIQSHISENRDEVEAVKNLYpsykNYTS--VYDKNNLLTNKTVMAHGCY 240
Cdd:PRK06151 205 LVRGMLAPDRIETCTVDLLRRTAAAARELGCPVRLHCAQGVLEVETVRRLH----GTTPleWLADVGLLGPRLLIPHATY 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191704909 241 LS---------AEELNVFHERGASIAHCPnSNLSLSSGFLNVLEVLKHE-VKIGLGTDVAggysysmldairRAVMVSNI 310
Cdd:PRK06151 281 ISgsprlnysgGDDLALLAEHGVSIVHCP-LVSARHGSALNSFDRYREAgINLALGTDTF------------PPDMVMNM 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191704909 311 ---LLINKVNEKSLT---LKEVFRLATLGGSQALGLDgEIGNFEVGKEFDAILINPKasdspiDLFYGDFFGDISEAVIQ 384
Cdd:PRK06151 348 rvgLILGRVVEGDLDaasAADLFDAATLGGARALGRD-DLGRLAPGAKADIVVFDLD------GLHMGPVFDPIRTLVTG 420
|
410 420
....*....|....*....|..
gi 1191704909 385 kflylGDDRNIEEVYVGGKQVV 406
Cdd:PRK06151 421 -----GSGRDVRAVFVDGRVVM 437
|
|
| PRK07213 |
PRK07213 |
chlorohydrolase; Provisional |
198-362 |
1.09e-10 |
|
chlorohydrolase; Provisional
Pssm-ID: 235969 [Multi-domain] Cd Length: 375 Bit Score: 62.75 E-value: 1.09e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191704909 198 HISENRDEVEAVKNLYpsykNYTSVYDKNNLLTNKTVMAHGCYLSAEELNVFHERGASIAHCPNSNLSLSSGFLNVLEVL 277
Cdd:PRK07213 198 HAAEHKGSVEYSLEKY----GMTEIERLINLGFKPDFIVHATHPSNDDLELLKENNIPVVVCPRANASFNVGLPPLNEML 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191704909 278 KHEVKIGLGTDVAGGYSYSM---LDAIRRAVmvsnillinkvnekSLTLKEVFRLATLGGSQALGLDgEIGNFEVGKEFD 354
Cdd:PRK07213 274 EKGILLGIGTDNFMANSPSIfreMEFIYKLY--------------HIEPKEILKMATINGAKILGLI-NVGLIEEGFKAD 338
|
....*...
gi 1191704909 355 AILINPKA 362
Cdd:PRK07213 339 FTFIKPTN 346
|
|
| HutI |
COG1228 |
Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport ... |
33-406 |
2.15e-10 |
|
Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440841 [Multi-domain] Cd Length: 386 Bit Score: 61.90 E-value: 2.15e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191704909 33 MPGLVDTHIHasqysFAGSSIDLPLLEWLTKYTfPAEHRFQNIDfaeevytRVVRRTLKNGTTTAcyFATIHTDSSLLLA 112
Cdd:COG1228 64 LPGLIDAHTH-----LGLGGGRAVEFEAGGGIT-PTVDLVNPAD-------KRLRRALAAGVTTV--RDLPGGPLGLRDA 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191704909 113 DITDKF----GQRAFVGKVCMDLNDTFPEYketteeSIKETERFVSEMLQKNYSRVKPIVT---PRFSLSCSETLMGElg 185
Cdd:COG1228 129 IIAGESkllpGPRVLAAGPALSLTGGAHAR------GPEEARAALRELLAEGADYIKVFAEggaPDFSLEELRAILEA-- 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191704909 186 niAKTRDLHIQSHISENRDEVEAVKNlypsykNYTSVydknnlltnktvmAHGCYLSAEELNVFHERGASIAhCPNSNLS 265
Cdd:COG1228 201 --AHALGLPVAAHAHQADDIRLAVEA------GVDSI-------------EHGTYLDDEVADLLAEAGTVVL-VPTLSLF 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191704909 266 LSSGFL------------------NVLEVLKHEVKIGLGTDVAGGYS--YSMLDAIRRAVMVSnillinkvneksLTLKE 325
Cdd:COG1228 259 LALLEGaaapvaakarkvreaalaNARRLHDAGVPVALGTDAGVGVPpgRSLHRELALAVEAG------------LTPEE 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191704909 326 VFRLATLGGSQALGLDGEIGNFEVGKEFDAILINpkasdspidlfyGDFFGDISeaviqkflYLgddRNIEEVYVGGKQV 405
Cdd:COG1228 327 ALRAATINAAKALGLDDDVGSLEPGKLADLVLLD------------GDPLEDIA--------YL---EDVRAVMKDGRVV 383
|
.
gi 1191704909 406 V 406
Cdd:COG1228 384 D 384
|
|
| Met_dep_hydrolase_E |
cd01313 |
Metallo-dependent hydrolases, subgroup D is part of the superfamily of metallo-dependent ... |
193-403 |
4.08e-10 |
|
Metallo-dependent hydrolases, subgroup D 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: 238638 [Multi-domain] Cd Length: 418 Bit Score: 61.32 E-value: 4.08e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191704909 193 LHIqsHISENRDEVEAVknLYPSYKNYTSVYDKNNLLTNKTVMAHGCYLSAEELNVFHERGASIAHCPNSNLSLSSGFLN 272
Cdd:cd01313 222 VHI--HLAEQPKEVDDC--LAAHGRRPVELLLDHGHLDARWCLVHATHLTDNETLLLGRSGAVVGLCPTTEANLGDGIFP 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191704909 273 VLEVLKHEVKIGLGTDVAGG-----------YSYSMLDAiRRAVMVSnillinkvnEKSLTLKEVFRLATLGGSQALGLD 341
Cdd:cd01313 298 AAALLAAGGRIGIGSDSNARidlleelrqleYSQRLRDR-ARNVLAT---------AGGSSARALLDAALAGGAQALGLA 367
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1191704909 342 geIGNFEVGKEFDAILInpkASDSPidlfygDFFGDISEAVIQKFLYLGDDRNIEEVYVGGK 403
Cdd:cd01313 368 --TGALEAGARADLLSL---DLDHP------SLAGALPDTLLDAWVFAAGDREVRDVVVGGR 418
|
|
| Amidohydro_3 |
pfam07969 |
Amidohydrolase family; |
235-406 |
1.29e-05 |
|
Amidohydrolase family;
Pssm-ID: 400360 [Multi-domain] Cd Length: 464 Bit Score: 47.14 E-value: 1.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191704909 235 MAHGC---YLSAEELNVFHERGASIAHCPNSNLSLS------------SGFLNVLEVLKHEVKIGLGTDVAGGySYSMLD 299
Cdd:pfam07969 298 IEHAQgvvPYTYSQIERVAALGGAAGVQPVFDPLWGdwlqdrlgaeraRGLTPVKELLNAGVKVALGSDAPVG-PFDPWP 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191704909 300 AIRRAVM-----VSNILLInkvnEKSLTLKEVFRLATLGGSQALGLDGEIGNFEVGKEFDAILINpkasdspIDLFygdf 374
Cdd:pfam07969 377 RIGAAVMrqtagGGEVLGP----DEELSLEEALALYTSGPAKALGLEDRKGTLGVGKDADLVVLD-------DDPL---- 441
|
170 180 190
....*....|....*....|....*....|..
gi 1191704909 375 fgDISEAVIqkflylgDDRNIEEVYVGGKQVV 406
Cdd:pfam07969 442 --TVDPPAI-------ADIRVRLTVVDGRVVY 464
|
|
| PRK09229 |
PRK09229 |
N-formimino-L-glutamate deiminase; Validated |
193-406 |
5.98e-05 |
|
N-formimino-L-glutamate deiminase; Validated
Pssm-ID: 236420 [Multi-domain] Cd Length: 456 Bit Score: 44.84 E-value: 5.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191704909 193 LHIqsHISENRDEVEAVKNLY---PsyknyTSVYDKNNLLTNKTVMAHGCYLSAEELNVFHERGASIAHCPNSNLSLSSG 269
Cdd:PRK09229 231 VHI--HIAEQTKEVDDCLAWSgarP-----VEWLLDHAPVDARWCLVHATHLTDAETARLARSGAVAGLCPTTEANLGDG 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191704909 270 FLNVLEVLKHEVKIGLGTDvaggySYSMLDAI---------------RRAVMVSNillinkvnEKSLTLKEVFRLATLGG 334
Cdd:PRK09229 304 IFPAVDYLAAGGRFGIGSD-----SHVSIDLVeelrlleygqrlrdrRRNVLAAA--------AQPSVGRRLFDAALAGG 370
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1191704909 335 SQALGLDgeIGNFEVGKEFDAILINPkasDSPidlfygDFFGDISEAVIQKFLYLGDDRNIEEVYVGGKQVV 406
Cdd:PRK09229 371 AQALGRA--IGGLAVGARADLVVLDL---DHP------ALAGREGDALLDRWVFAGGDAAVRDVWVAGRWVV 431
|
|
| Imidazolone-5PH |
cd01296 |
Imidazolonepropionase/imidazolone-5-propionate hydrolase (Imidazolone-5PH) catalyzes the third ... |
235-385 |
8.73e-05 |
|
Imidazolonepropionase/imidazolone-5-propionate hydrolase (Imidazolone-5PH) catalyzes the third step in the histidine degradation pathway, the hydrolysis of (S)-3-(5-oxo-4,5-dihydro-3H-imidazol-4-yl)propanoate to N-formimidoyl-L-glutamate. In bacteria, the enzyme is part of histidine utilization (hut) operon.
Pssm-ID: 238621 [Multi-domain] Cd Length: 371 Bit Score: 44.17 E-value: 8.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191704909 235 MAHGCYLSAEELNVFHERGASIAHCPNSNLSLSSGFLNVLEVLKHEVKIGLGTDVAGGySY---SMLDAIRRAVmvsnIL 311
Cdd:cd01296 233 ADHLEHTSDEGIAALAEAGTVAVLLPGTAFSLRETYPPARKLIDAGVPVALGTDFNPG-SSptsSMPLVMHLAC----RL 307
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1191704909 312 LinkvnekSLTLKEVFRLATLGGSQALGLDGEIGNFEVGKEFDAILINpkaSDSPIDLFYgdFFG-DISEAVIQK 385
Cdd:cd01296 308 M-------RMTPEEALTAATINAAAALGLGETVGSLEVGKQADLVILD---APSYEHLAY--RFGvNLVEYVIKN 370
|
|
| Met_dep_hydrolase_A |
cd01299 |
Metallo-dependent hydrolases, subgroup A is part of the superfamily of metallo-dependent ... |
264-359 |
1.56e-03 |
|
Metallo-dependent hydrolases, subgroup A is part of the superfamily of metallo-dependent hydrolases, a large group of proteins that show conservation in their 3-dimensional fold (TIM barrel) and in details of their active site. The vast majority of the members have a conserved metal binding site, involving four histidines and one aspartic acid residue. In the common reaction mechanism, the metal ion (or ions) deprotonate a water molecule for a nucleophilic attack on the substrate. The function of this subgroup is unknown.
Pssm-ID: 238624 [Multi-domain] Cd Length: 342 Bit Score: 40.35 E-value: 1.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191704909 264 LSLSSGFLNVLEVLKHEVKIGLGTD-----VAGGYSYSMLdairrAVMVsnillinkvnEKSLTLKEVFRLATLGGSQAL 338
Cdd:cd01299 247 LVLEAGRDALRRAHKAGVKIAFGTDagfpvPPHGWNAREL-----ELLV----------KAGGTPAEALRAATANAAELL 311
|
90 100
....*....|....*....|.
gi 1191704909 339 GLDGEIGNFEVGKEFDAILIN 359
Cdd:cd01299 312 GLSDELGVIEAGKLADLLVVD 332
|
|
| nagA |
PRK11170 |
N-acetylglucosamine-6-phosphate deacetylase; Provisional |
291-351 |
8.49e-03 |
|
N-acetylglucosamine-6-phosphate deacetylase; Provisional
Pssm-ID: 183010 Cd Length: 382 Bit Score: 38.03 E-value: 8.49e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1191704909 291 GGYSYSMLDAIRravmvsnilliNKVNEKSLTLKEVFRLATLGGSQALGLDGEIGNFEVGK 351
Cdd:PRK11170 307 SGSALTMIEAVR-----------NLVEHVGIALDEALRMATLYPARAIGVDKRLGSIEAGK 356
|
|
| |
