|
Name |
Accession |
Description |
Interval |
E-value |
| GDEase |
cd01303 |
Guanine deaminase (GDEase). Guanine deaminase is an aminohydrolase responsible for the ... |
1-370 |
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: 592.33 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 335335018 1 MPGLVDTHIHASQYSFAGSSIDLPLLEWLTKYTFPAEHRFQNIDFAEEVYTRVVRRTLKNGTTTACYFATIHTDSSLLLA 80
Cdd:cd01303 64 LPGFIDTHIHAPQYANIGSGLGEPLLDWLETYTFPEEAKFADPAYAREVYGRFLDELLRNGTTTACYFATIHPESTEALF 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 335335018 81 DITDKFGQRAFVGKVCMDLNDtfPEYK-ETTEESIKETERFVSEMLQKnYSRVKPIVTPRFSLSCSETLMGELGNIAKT- 158
Cdd:cd01303 144 EEAAKRGQRAIAGKVCMDRNA--PEYYrDTAESSYRDTKRLIERWHGK-SGRVKPAITPRFAPSCSEELLAALGKLAKEh 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 335335018 159 RDLHIQSHISENRDEVEAVKNLYPSYKNYTSVYDKNNLLTNKTVMAHGCYLSAEELNVFHERGASIAHCPNSNLSLSSGF 238
Cdd:cd01303 221 PDLHIQTHISENLDEIAWVKELFPGARDYLDVYDKYGLLTEKTVLAHCVHLSEEEFNLLKERGASVAHCPTSNLFLGSGL 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 335335018 239 LNVLEVLKHEVKIGLGTDVAGGYSYSMLDAIRRAVMVSNILLINKVNEKSLTLKEVFRLATLGGSQALGLDGEIGNFEVG 318
Cdd:cd01303 301 FDVRKLLDAGIKVGLGTDVGGGTSFSMLDTLRQAYKVSRLLGYELGGHAKLSPAEAFYLATLGGAEALGLDDKIGNFEVG 380
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 335335018 319 KEFDAILINPKASDSPIDLfygDFFGDISEAVIQKFLYLGDDRNIEEVYVGG 370
Cdd:cd01303 381 KEFDAVVIDPSATPLLADR---MFRVESLEEALFKFLYLGDDRNIREVYVAG 429
|
|
| guan_deamin |
TIGR02967 |
guanine deaminase; This model describes guanine deaminase, which hydrolyzes guanine to ... |
1-370 |
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: 540.30 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 335335018 1 MPGLVDTHIHASQYSFAGSsIDLPLLEWLTKYTFPAEHRFQNIDFAEEVYTRVVRRTLKNGTTTACYFATIHTDSSLLLA 80
Cdd:TIGR02967 44 MPGFIDTHIHYPQTEMIAS-YGEQLLEWLEKYTFPTEARFADPDHAEEVAEFFLDELLRNGTTTALVFATVHPESVDALF 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 335335018 81 DITDKFGQRAFVGKVCMDLNdtFPEY-KETTEESIKETERFVSEMLQKNysRVKPIVTPRFSLSCSETLMGELGNIAKTR 159
Cdd:TIGR02967 123 EAALKRGMRMIAGKVLMDRN--APDYlRDTAESSYDESKALIERWHGKG--RLLYAVTPRFAPTSSPEQLAAAGELAKEY 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 335335018 160 -DLHIQSHISENRDEVEAVKNLYPSYKNYTSVYDKNNLLTNKTVMAHGCYLSAEELNVFHERGASIAHCPNSNLSLSSGF 238
Cdd:TIGR02967 199 pDVYVQTHLSENKDEIAWVKELFPEAKDYLDVYDHYGLLGRRSVFAHCIHLSDEECQRLAETGAAIAHCPTSNLFLGSGL 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 335335018 239 LNVLEVLKHEVKIGLGTDVAGGYSYSMLDAIRRAVMVSNILlinkvnEKSLTLKEVFRLATLGGSQALGLDGEIGNFEVG 318
Cdd:TIGR02967 279 FNLKKALEHGVRVGLGTDVGGGTSFSMLQTLREAYKVSQLQ------GARLSPFEAFYLATLGGARALDLDDRIGNFEPG 352
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 335335018 319 KEFDAILINPKASDSPIDLFYGdffGDISEAVIQKFLYLGDDRNIEEVYVGG 370
Cdd:TIGR02967 353 KEADFVVLDPAATPLLALRFEG---ADTLEDKLFKLMYLGDDRNVAETYVAG 401
|
|
| SsnA |
COG0402 |
Cytosine/adenosine deaminase or related metal-dependent hydrolase [Nucleotide transport and ... |
1-374 |
7.72e-116 |
|
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: 342.96 E-value: 7.72e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 335335018 1 MPGLVDTHIHASQYSFAGSSIDLPLLEWLTKYTFPAEHRFqNIDFAEEVYTRVVRRTLKNGTTTACYFATIHTDSSLLLA 80
Cdd:COG0402 58 LPGLVNTHTHLPQTLLRGLADDLPLLDWLEEYIWPLEARL-DPEDVYAGALLALAEMLRSGTTTVADFYYVHPESADALA 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 335335018 81 DITDKFGQRAFVGKVCMDLNdtFPE-YKETTEESIKETERFVSEMLQKNYSRVKPIVTPRFSLSCSETLMGELGNIAKTR 159
Cdd:COG0402 137 EAAAEAGIRAVLGRGLMDRG--FPDgLREDADEGLADSERLIERWHGAADGRIRVALAPHAPYTVSPELLRAAAALAREL 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 335335018 160 DLHIQSHISENRDEVEAVKNLYPsyKNYTSVYDKNNLLTNKTVMAHGCYLSAEELNVFHERGASIAHCPNSNLSLSSGFL 239
Cdd:COG0402 215 GLPLHTHLAETRDEVEWVLELYG--KRPVEYLDELGLLGPRTLLAHCVHLTDEEIALLAETGASVAHCPTSNLKLGSGIA 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 335335018 240 NVLEVLKHEVKIGLGTDVAGG-YSYSMLDAIRRAVMVSNILlinKVNEKSLTLKEVFRLATLGGSQALGLDGEIGNFEVG 318
Cdd:COG0402 293 PVPRLLAAGVRVGLGTDGAASnNSLDMFEEMRLAALLQRLR---GGDPTALSAREALEMATLGGARALGLDDEIGSLEPG 369
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 335335018 319 KEFDAILINPKASD-SPIDlfygdffgdiseAVIQKFLYLGDDRNIEEVYVGGKQVV 374
Cdd:COG0402 370 KRADLVVLDLDAPHlAPLH------------DPLSALVYAADGRDVRTVWVAGRVVV 414
|
|
| PRK09228 |
PRK09228 |
guanine deaminase; Provisional |
1-373 |
3.79e-105 |
|
guanine deaminase; Provisional
Pssm-ID: 236419 [Multi-domain] Cd Length: 433 Bit Score: 316.36 E-value: 3.79e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 335335018 1 MPGLVDTHIHASQYSFAGSsidlP---LLEWLTKYTFPAEHRFQNIDFAEEVYTRVVRRTLKNGTTTACYFATIHTDSsl 77
Cdd:PRK09228 69 LPGFIDTHIHYPQTDMIAS----YgeqLLDWLNTYTFPEERRFADPAYAREVAEFFLDELLRNGTTTALVFGTVHPQS-- 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 335335018 78 lladiTDKF-------GQRAFVGKVCMDLNdtFPEY-KETTEESIKETERfvseMLQK--NYSRVKPIVTPRFSLSCSET 147
Cdd:PRK09228 143 -----VDALfeaaearNMRMIAGKVLMDRN--APDGlRDTAESGYDDSKA----LIERwhGKGRLLYAITPRFAPTSTPE 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 335335018 148 LMGELGNIAKTR-DLHIQSHISENRDEVEAVKNLYPSYKNYTSVYDKNNLLTNKTVMAHGCYLSAEELNVFHERGASIAH 226
Cdd:PRK09228 212 QLEAAGALAREHpDVWIQTHLSENLDEIAWVKELFPEARDYLDVYERYGLLGPRAVFAHCIHLEDRERRRLAETGAAIAF 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 335335018 227 CPNSNLSLSSGFLNVLEVLKHEVKIGLGTDVAGGYSYSMLDAIRRAVMVSnillinKVNEKSLTLKEVFRLATLGGSQAL 306
Cdd:PRK09228 292 CPTSNLFLGSGLFDLKRADAAGVRVGLGTDVGGGTSFSMLQTMNEAYKVQ------QLQGYRLSPFQAFYLATLGGARAL 365
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 335335018 307 GLDGEIGNFEVGKEFDAILINPKA----------SDSPIDLFYGdffgdiseaviqkFLYLGDDRNIEEVYVGGKQV 373
Cdd:PRK09228 366 GLDDRIGNLAPGKEADFVVLDPAAtpllalrtarAESLEELLFA-------------LMTLGDDRAVAETYVAGRPV 429
|
|
| ATZ_TRZ_like |
cd01298 |
TRZ/ATZ family contains enzymes from the atrazine degradation pathway and related hydrolases. ... |
1-374 |
1.72e-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: 1.72e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 335335018 1 MPGLVDTHIHASQYSFAGSSIDLPLLEWLTKYTFPAEHRFQnidfAEEVY--TRV-VRRTLKNGTTTAC--YFatIHTDS 75
Cdd:cd01298 55 MPGLVNTHTHLAMTLLRGLADDLPLMEWLKDLIWPLERLLT----EEDVYlgALLaLAEMIRSGTTTFAdmYF--FYPDA 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 335335018 76 sllLADITDKFGQRAFVGKVCMDLNDtfpEYKETTEESIKETERFVSEMLQKNYSRVKPIVTPRFSLSCSETLMGELGNI 155
Cdd:cd01298 129 ---VAEAAEELGIRAVLGRGIMDLGT---EDVEETEEALAEAERLIREWHGAADGRIRVALAPHAPYTCSDELLREVAEL 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 335335018 156 AKTRDLHIQSHISENRDEVEAVKNLYpsykNYTSV-Y-DKNNLLTNKTVMAHGCYLSAEELNVFHERGASIAHCPNSNLS 233
Cdd:cd01298 203 AREYGVPLHIHLAETEDEVEESLEKY----GKRPVeYlEELGLLGPDVVLAHCVWLTDEEIELLAETGTGVAHNPASNMK 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 335335018 234 LSSGFLNVLEVLKHEVKIGLGTD-VAGGYSYSMLDAIRRAvmvsniLLINKV---NEKSLTLKEVFRLATLGGSQALGLD 309
Cdd:cd01298 279 LASGIAPVPEMLEAGVNVGLGTDgAASNNNLDMFEEMRLA------ALLQKLahgDPTALPAEEALEMATIGGAKALGLD 352
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 335335018 310 gEIGNFEVGKEFDAILINPkasDSPidlfygDFFG---DISEAViqkflYLGDDRNIEEVYVGGKQVV 374
Cdd:cd01298 353 -EIGSLEVGKKADLILIDL---DGP------HLLPvhdPISHLV-----YSANGGDVDTVIVNGRVVM 405
|
|
| PRK07228 |
PRK07228 |
5'-deoxyadenosine deaminase; |
1-327 |
8.69e-62 |
|
5'-deoxyadenosine deaminase;
Pssm-ID: 180895 [Multi-domain] Cd Length: 445 Bit Score: 204.85 E-value: 8.69e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 335335018 1 MPGLVDTHIHASQYSFAGSSIDLPLLEWLTKYTFPAE--HRfqnidfAEEVYTRV---VRRTLKNGTTTACYFATI-HTD 74
Cdd:PRK07228 55 IPGLIQGHIHLCQTLFRGIADDLELLDWLKDRIWPLEaaHD------AESMYYSAllgIGELIESGTTTIVDMESVhHTD 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 335335018 75 SSL-LLADItdkfGQRAFVGKVCMDLNDTFPE-YKETTEESIKETERFVSEMLQKNYSRVKPIVTPRFSLSCSETLMGEL 152
Cdd:PRK07228 129 SAFeAAGES----GIRAVLGKVMMDYGDDVPEgLQEDTEASLAESVRLLEKWHGADNGRIRYAFTPRFAVSCTEELLRGV 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 335335018 153 GNIAKTRDLHIQSHISENRDEVEAVKNlYPSYKNYTsVYDKNNLLTNKTVMAHGCYLSAEELNVFHERGASIAHCPNSNL 232
Cdd:PRK07228 205 RDLADEYGVRIHTHASENRGEIETVEE-ETGMRNIH-YLDEVGLTGEDLILAHCVWLDEEEREILAETGTHVTHCPSSNL 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 335335018 233 SLSSGFLNVLEVLKHEVKIGLGTDvaGGYSYSMLDA---IRRAVmvsnilLINKVNE---KSLTLKEVFRLATLGGSQAL 306
Cdd:PRK07228 283 KLASGIAPVPDLLERGINVALGAD--GAPCNNTLDPfteMRQAA------LIQKVDRlgpTAMPARTVFEMATLGGAKAA 354
|
330 340
....*....|....*....|.
gi 335335018 307 GLDGEIGNFEVGKEFDAILIN 327
Cdd:PRK07228 355 GFEDEIGSLEEGKKADLAILD 375
|
|
| Amidohydro_1 |
pfam01979 |
Amidohydrolase family; This family of enzymes are a a large metal dependent hydrolase ... |
1-373 |
1.38e-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: 188.09 E-value: 1.38e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 335335018 1 MPGLVDTHIHASQYSFAGSSIDLpllewltkytfpaehrfqniDFAEEVYTRVVRRTLKNGTTTACYFATIHTDSSLLLA 80
Cdd:pfam01979 3 LPGLIDAHVHLEMGLLRGIPVPP--------------------EFAYEALRLGITTMLKSGTTTVLDMGATTSTGIEALL 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 335335018 81 DITDK--FGQRAFVGKVCMDLNDTFPEYKETTEESIKETErfvsEMLQKNYSRVKPIVTPRFSLSCSETLMGELGNIAKT 158
Cdd:pfam01979 63 EAAEElpLGLRFLGPGCSLDTDGELEGRKALREKLKAGAE----FIKGMADGVVFVGLAPHGAPTFSDDELKAALEEAKK 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 335335018 159 RDLHIQSHISENRDEVEAVKNLYPS---YKNYTSVYDKNNLL-TNKTVMAHGCYLSAEELNVFHER--GASIAHCPNSNL 232
Cdd:pfam01979 139 YGLPVAIHALETKGEVEDAIAAFGGgieHGTHLEVAESGGLLdIIKLILAHGVHLSPTEANLLAEHlkGAGVAHCPFSNS 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 335335018 233 SLSSGFLNVLEVLKHEVKIGLGTDVAG-GYSYSMLDAIRRAVmvsnilLINKVNEKSLTLKEVFRLATLGGSQALGLDGE 311
Cdd:pfam01979 219 KLRSGRIALRKALEDGVKVGLGTDGAGsGNSLNMLEELRLAL------ELQFDPEGGLSPLEALRMATINPAKALGLDDK 292
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 335335018 312 IGNFEVGKEFDAILINPKasdspidlfygdffgdiseaVIQKFLYLGDDRNIEEVYVGGKQV 373
Cdd:pfam01979 293 VGSIEVGKDADLVVVDLD--------------------PLAAFFGLKPDGNVKKVIVKGKIV 334
|
|
| PRK08393 |
PRK08393 |
N-ethylammeline chlorohydrolase; Provisional |
2-374 |
1.55e-46 |
|
N-ethylammeline chlorohydrolase; Provisional
Pssm-ID: 181411 [Multi-domain] Cd Length: 424 Bit Score: 164.20 E-value: 1.55e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 335335018 2 PGLVDTHIHASQYSFAGSSIDLPLLEWLTKYTFPAEHRFQNIDFAEEVYTRVVRrTLKNGTTT--ACYFatiHTDSsllL 79
Cdd:PRK08393 54 PGFINAHTHSPMVLLRGLADDVPLMEWLQNYIWPRERKLKRKDIYWGAYLGLLE-MIKSGTTTfvDMYF---HMEE---V 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 335335018 80 ADITDKFGQRAFVGKVCMDLNDtfpeyKETTEESIKETERFVSEMLQKNYSRVKPIVTPRFSLSCSETLMGELGNIAKTR 159
Cdd:PRK08393 127 AKATLEVGLRGYLSYGMVDLGD-----EEKREKEIKETEKLMEFIEKLNSPRVHFVFGPHAPYTCSLALLKWVREKAREW 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 335335018 160 DLHIQSHISENRDEVEAVKNLYPsyKNYTSVYDKNNLLTNKTVMAHGCYLSAEELNVFHERGASIAHCPNSNLSLSSGFL 239
Cdd:PRK08393 202 NKLITIHLSETMDEIKQIREKYG--KSPVVLLDEIGFLNEDVIAAHGVWLSSRDIRILASAGVTVAHNPASNMKLGSGVM 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 335335018 240 NVLEVLKHEVKIGLGTDvaGGYSYSMLDAIRRAVMVSnilLINKVNEKSLTL---KEVFRLATLGGSQALGLDGeiGNFE 316
Cdd:PRK08393 280 PLRKLLNAGVNVALGTD--GAASNNNLDMLREMKLAA---LLHKVHNLDPTIadaETVFRMATQNGAKALGLKA--GVIK 352
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 335335018 317 VGKEFDAILIN-PKASDSPIDlfygdffgdiseAVIQKFLYLGDDRNIEEVYVGGKQVV 374
Cdd:PRK08393 353 EGYLADIAVIDfNRPHLRPIN------------NPISHLVYSANGNDVETTIVDGKIVM 399
|
|
| PRK06038 |
PRK06038 |
N-ethylammeline chlorohydrolase; Provisional |
1-329 |
9.43e-44 |
|
N-ethylammeline chlorohydrolase; Provisional
Pssm-ID: 180363 [Multi-domain] Cd Length: 430 Bit Score: 156.83 E-value: 9.43e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 335335018 1 MPGLVDTHIHASQYSFAGSSIDLPLLEWLTKYTFPAEHRFQnidfAEEVYTRVVRRTL---KNGTTTacyFAT--IHTDS 75
Cdd:PRK06038 54 MPGLVNTHTHAAMTLFRGYADDLPLAEWLNDHIWPAEAKLT----AEDVYAGSLLACLemiKSGTTS---FADmyFYMDE 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 335335018 76 SlllADITDKFGQRAFVGKVCMDLNDTfpeykETTEESIKETERFVSEMLQKNYSRVKPIVTPRFSLSCSETLMGELGNI 155
Cdd:PRK06038 127 V---AKAVEESGLRAALSYGMIDLGDD-----EKGEAELKEGKRFVKEWHGAADGRIKVMYGPHAPYTCSEEFLSKVKKL 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 335335018 156 AKTRDLHIQSHISENRDEVEAVKNLYpsykNYTSVY--DKNNLLTNKTVMAHGCYLSAEELNVFHERGASIAHCPNSNLS 233
Cdd:PRK06038 199 ANKDGVGIHIHVLETEAELNQMKEQY----GMCSVNylDDIGFLGPDVLAAHCVWLSDGDIEILRERGVNVSHNPVSNMK 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 335335018 234 LSSGFLNVLEVLKHEVKIGLGTD-VAGGYSYSMLDAIRRAVMVSNillINKVNEKSLTLKEVFRLATLGGSQALGLdgEI 312
Cdd:PRK06038 275 LASGIAPVPKLLERGVNVSLGTDgCASNNNLDMFEEMKTAALLHK---VNTMDPTALPARQVLEMATVNGAKALGI--NT 349
|
330
....*....|....*..
gi 335335018 313 GNFEVGKEFDAILINPK 329
Cdd:PRK06038 350 GMLKEGYLADIIIVDMN 366
|
|
| PRK06687 |
PRK06687 |
TRZ/ATZ family protein; |
1-374 |
4.70e-42 |
|
TRZ/ATZ family protein;
Pssm-ID: 180657 [Multi-domain] Cd Length: 419 Bit Score: 152.08 E-value: 4.70e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 335335018 1 MPGLVDTHIHASQYSFAGSSIDLPLLEWLTKYTFPAEHRFqNIDFAEEVYTRVVRRTLKNGTTTacyFATIHTDSSLLLA 80
Cdd:PRK06687 57 MPGLVNCHTHSAMTGLRGIRDDSNLHEWLNDYIWPAESEF-TPDMTTNAVKEALTEMLQSGTTT---FNDMYNPNGVDIQ 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 335335018 81 DITDKFGQRafvGKVCMDLNDTFPEYKETTEESIKETERFVSEMLQKNYSRVKPIVTPRFSLSCSETLMGELGNIAKTRD 160
Cdd:PRK06687 133 QIYQVVKTS---KMRCYFSPTLFSSETETTAETISRTRSIIDEILKYKNPNFKVMVAPHSPYSCSRDLLEASLEMAKELN 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 335335018 161 LHIQSHISENRDEVEAVKNLYPsyKNYTSVYDKNNLLTNKTVMAHGCYLSAEELNVFHERGASIAHCPNSNLSLSSGFLN 240
Cdd:PRK06687 210 IPLHVHVAETKEESGIILKRYG--KRPLAFLEELGYLDHPSVFAHGVELNEREIERLASSQVAIAHNPISNLKLASGIAP 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 335335018 241 VLEVLKHEVKIGLGTD-VAGGYSYSMLDAIRRAVMVSNillINKVNEKSLTLKEVFRLATLGGSQALGLDGEIGNFEVGK 319
Cdd:PRK06687 288 IIQLQKAGVAVGIATDsVASNNNLDMFEEGRTAALLQK---MKSGDASQFPIETALKVLTIEGAKALGMENQIGSLEVGK 364
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 335335018 320 EFDAILINPKASdspIDLFygdffgdISEAVIQKFLYLGDDRNIEEVYVGGKQVV 374
Cdd:PRK06687 365 QADFLVIQPQGK---IHLQ-------PQENMLSHLVYAVKSSDVDDVYIAGEQVV 409
|
|
| PRK09045 |
PRK09045 |
TRZ/ATZ family hydrolase; |
1-374 |
3.92e-41 |
|
TRZ/ATZ family hydrolase;
Pssm-ID: 236366 [Multi-domain] Cd Length: 443 Bit Score: 150.06 E-value: 3.92e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 335335018 1 MPGLVDTHIHASQYSFAGSSIDLPLLEWLTKYTFPAEHRFQNIDFAEEVYTRVVRRTLKNGTTTA--CYFatiHTDSsll 78
Cdd:PRK09045 65 IPGLINAHTHAAMSLLRGLADDLPLMTWLQDHIWPAEGAWVSEEFVRDGTLLAIAEMLRGGTTCFndMYF---FPEA--- 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 335335018 79 LADITDKFGQRAFVGKVCMDlndtFP-EYKETTEESI----KETERFvsemlqKNYSRVKPIVTPRFSLSCSETLMGELG 153
Cdd:PRK09045 139 AAEAAHQAGMRAQIGMPVLD----FPtAWASDADEYLakglELHDQW------RHHPLISTAFAPHAPYTVSDENLERIR 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 335335018 154 NIAKTRDLHIQSHISENRDEVEAvknlypSYKNY----TSVYDKNNLLTNKTVMAHGCYLSAEELNVFHERGASIAHCPN 229
Cdd:PRK09045 209 TLAEQLDLPIHIHLHETAQEIAD------SLKQHgqrpLARLARLGLLGPRLIAVHMTQLTDAEIALLAETGCSVVHCPE 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 335335018 230 SNLSLSSGFLNVLEVLKHEVKIGLGTD-VAGGYSYSMLDAIRRAVMVSnillinKV---NEKSLTLKEVFRLATLGGSQA 305
Cdd:PRK09045 283 SNLKLASGFCPVAKLLQAGVNVALGTDgAASNNDLDLFGEMRTAALLA------KAvagDATALPAHTALRMATLNGARA 356
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 335335018 306 LGLDGEIGNFEVGKEFDAILINPKASDS-PIdlfygdfFGDISEAViqkflYLGDDRNIEEVYVGGKQVV 374
Cdd:PRK09045 357 LGLDDEIGSLEPGKQADLVAVDLSGLETqPV-------YDPVSQLV-----YAAGREQVSHVWVAGKQLL 414
|
|
| PRK15493 |
PRK15493 |
bifunctional S-methyl-5'-thioadenosine deaminase/S-adenosylhomocysteine deaminase; |
1-374 |
1.43e-33 |
|
bifunctional S-methyl-5'-thioadenosine deaminase/S-adenosylhomocysteine deaminase;
Pssm-ID: 185390 [Multi-domain] Cd Length: 435 Bit Score: 129.41 E-value: 1.43e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 335335018 1 MPGLVDTHIHASQYSFAGSSIDLPLLEWLTKYTFPAEHRFQNiDFAEEVYTRVVRRTLKNGTTT-ACYFATIHTDSSLLL 79
Cdd:PRK15493 58 LPGLVNTHTHVVMSLLRGIGDDMLLQPWLETRIWPLESQFTP-ELAVASTELGLLEMVKSGTTSfSDMFNPIGVDQDAIM 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 335335018 80 ADITDKfGQRAFVGKVCMDLNDtfpeyKETTEESIKETERFVSEMLQKNySRVKPIVTPRFSLSCSETLMGELGNIAKTR 159
Cdd:PRK15493 137 ETVSRS-GMRAAVSRTLFSFGT-----KEDEKKAIEEAEKYVKRYYNES-GMLTTMVAPHSPYTCSTELLEECARIAVEN 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 335335018 160 DLHIQSHISENRDEVEAVKNLYPsyKNYTSVYDKNNLLTNKTVMAHGCYLSAEELNVFHERGASIAHCPNSNLSLSSGFL 239
Cdd:PRK15493 210 QTMVHIHLSETEREVRDIEAQYG--KRPVEYAASCGLFKRPTVIAHGVVLNDNERAFLAEHDVRVAHNPNSNLKLGSGIA 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 335335018 240 NVLEVLKHEVKIGLGTD-VAGGYSYSMLDAIRRAVMVSNILlinKVNEKSLTLKEVFRLATLGGSQALGLDgEIGNFEVG 318
Cdd:PRK15493 288 NVKAMLEAGIKVGIATDsVASNNNLDMFEEMRIATLLQKGI---HQDATALPVETALTLATKGAAEVIGMK-QTGSLEVG 363
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 335335018 319 KEFDAILINP--KASDSPidlfygdffgdiSEAVIQKFLYLGDDRNIEEVYVGGKQVV 374
Cdd:PRK15493 364 KCADFITIDPsnKPHLQP------------ADEVLSHLVYAASGKDISDVIINGKRVV 409
|
|
| PRK06380 |
PRK06380 |
metal-dependent hydrolase; Provisional |
1-371 |
3.47e-25 |
|
metal-dependent hydrolase; Provisional
Pssm-ID: 180548 [Multi-domain] Cd Length: 418 Bit Score: 105.74 E-value: 3.47e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 335335018 1 MPGLVDTHIHASQYSFAGSSIDLPLLEWLTKyTFPAEHRFQNidfaEEVYTRV---VRRTLKNGTTTacyFATIHTDSSL 77
Cdd:PRK06380 53 MPGLINTHAHVGMTASKGLFDDVDLEEFLMK-TFKYDSKRTR----EGIYNSAklgMYEMINSGITA---FVDLYYSEDI 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 335335018 78 LlADITDKFGQRAFVGKVCMDlndtfPEYKETTEESIKETERFVSEMLQKNYsrVKPIVTPRFSLSCSETLMGELGNIAK 157
Cdd:PRK06380 125 I-AKAAEELGIRAFLSWAVLD-----EEITTQKGDPLNNAENFIREHRNEEL--VTPSIGVQGIYVANDETYLKAKEIAE 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 335335018 158 TRDLHIQSHISENRDEVeavknlYPSYKNY----TSVYDKNNLLTNKTVMAHGCYLSAEELNVFHERGASIAHCPNSNLS 233
Cdd:PRK06380 197 KYDTIMHMHLSETRKEV------YDHVKRTgerpVEHLEKIGFLNSKLIAAHCVWATYHEIKLLSKNGVKVSWNSVSNFK 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 335335018 234 LSS-GFLNVLEVLKHEVKIGLGTDVAGgySYSMLDAIrRAVMVSNILLINKVNEKSLT-LKEVFRLATLGGSQALGLDGe 311
Cdd:PRK06380 271 LGTgGSPPIPEMLDNGINVTIGTDSNG--SNNSLDMF-EAMKFSALSVKNERWDASIIkAQEILDFATINAAKALELNA- 346
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 335335018 312 iGNFEVGKEFDAILINPKASdSPIDLFYGDFFGDIseaviqkfLYLGDDRNIEEVYVGGK 371
Cdd:PRK06380 347 -GSIEVGKLADLVILDARAP-NMIPTRKNNIVSNI--------VYSLNPLNVDHVIVNGK 396
|
|
| PRK12393 |
PRK12393 |
amidohydrolase; Provisional |
2-374 |
1.20e-23 |
|
amidohydrolase; Provisional
Pssm-ID: 237088 [Multi-domain] Cd Length: 457 Bit Score: 101.68 E-value: 1.20e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 335335018 2 PGLVDTHIHASQYSFAG--SSIDLPLLEWL--TKYTFPA---EHRFQ---NIDFAEevytrvvrrTLKNGTTTAC----- 66
Cdd:PRK12393 59 PGWVNTHHHLFQSLLKGvpAGINQSLTAWLaaVPYRFRArfdEDLFRlaaRIGLVE---------LLRSGCTTVAdhhyl 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 335335018 67 YFATIHTDSSLLLADITDKFGQRaFV---GKVCMDLNDTfPEYK-----ETTEESIKETERFVSEMLQKNYSRVKPIV-- 136
Cdd:PRK12393 130 YHPGMPFDTGDILFDEAEALGMR-FVlcrGGATQTRGDH-PGLPtalrpETLDQMLADVERLVSRYHDASPDSLRRVVva 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 335335018 137 --TPRFSLScsETLMGELGNIAKTRDLHIQSHISENRDEVEAVKNLYpsykNYTSVY--DKNNLLTNKTVMAHGCYLSAE 212
Cdd:PRK12393 208 ptTPTFSLP--PELLREVARAARGMGLRLHSHLSETVDYVDFCREKY----GMTPVQfvAEHDWLGPDVWFAHLVKLDAE 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 335335018 213 ELNVFHERGASIAHCPNSNLSLSSGFLNVLEVLKHEVKIGLGTD-VAGGYSYSMLDAIRRAVMVSNILlinkVNEKSLTL 291
Cdd:PRK12393 282 EIALLAQTGTGIAHCPQSNGRLGSGIAPALAMEAAGVPVSLGVDgAASNESADMLSEAHAAWLLHRAE----GGADATTV 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 335335018 292 KEVFRLATLGGSQALGLDgEIGNFEVGKEFDAILINpkaSDSPidLFYGdfFGDISEAVIQKflylGDDRNIEEVYVGGK 371
Cdd:PRK12393 358 EDVVHWGTAGGARVLGLD-AIGTLAVGQAADLAIYD---LDDP--RFFG--LHDPAIAPVAC----GGPAPVKALLVNGR 425
|
...
gi 335335018 372 QVV 374
Cdd:PRK12393 426 PVV 428
|
|
| PRK08203 |
PRK08203 |
hydroxydechloroatrazine ethylaminohydrolase; Reviewed |
1-322 |
1.03e-22 |
|
hydroxydechloroatrazine ethylaminohydrolase; Reviewed
Pssm-ID: 236184 [Multi-domain] Cd Length: 451 Bit Score: 98.77 E-value: 1.03e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 335335018 1 MPGLVDTHIHASQYSFAG--SSIDLPLLEWLTK-YTFPAehrfqNIDfAEEVY--TRV-VRRTLKNGTTTAcyfaTIH-- 72
Cdd:PRK08203 58 TPGLVNTHHHFYQTLTRAlpAAQDAELFPWLTTlYPVWA-----RLT-PEMVRvaTQTaLAELLLSGCTTS----SDHhy 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 335335018 73 ---TDSSLLLADITD---KFGQRAFVGKVCMDLN--------DTFPEyketTEESI-KETERFVSEMLQKN-YSRVKPIV 136
Cdd:PRK08203 128 lfpNGLRDALDDQIEaarEIGMRFHATRGSMSLGesdgglppDSVVE----DEDAIlADSQRLIDRYHDPGpGAMLRIAL 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 335335018 137 TPRFSLSCSETLMGELGNIAKTRDLHIQSHISENRDEVEAVKNLYpsykNYTSV-Y-DKNNLLTNKTVMAHGCYLSAEEL 214
Cdd:PRK08203 204 APCSPFSVSRELMRESAALARRLGVRLHTHLAETLDEEAFCLERF----GMRPVdYlEDLGWLGPDVWLAHCVHLDDAEI 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 335335018 215 NVFHERGASIAHCPNSNLSLSSGFLNVLEVLKHEVKIGLGTD-VAGGYSYSMLDAIRRAvmvsniLLINKV--NEKSLTL 291
Cdd:PRK08203 280 ARLARTGTGVAHCPCSNMRLASGIAPVRELRAAGVPVGLGVDgSASNDGSNLIGEARQA------LLLQRLryGPDAMTA 353
|
330 340 350
....*....|....*....|....*....|.
gi 335335018 292 KEVFRLATLGGSQALGLDgEIGNFEVGKEFD 322
Cdd:PRK08203 354 REALEWATLGGARVLGRD-DIGSLAPGKLAD 383
|
|
| Met_dep_hydrolase_D |
cd01312 |
Metallo-dependent hydrolases, subgroup D is part of the superfamily of metallo-dependent ... |
1-322 |
6.44e-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: 90.20 E-value: 6.44e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 335335018 1 MPGLVDTHIH------ASQYSFAGSSIdlplleWLTKY-TFPAEHRFQNidfAEEVYTRVVRRTLKNGTTTAcyfATIHT 73
Cdd:cd01312 30 LPGLINAHTHlefsanVAQFTYGRFRA------WLLSViNSRDELLKQP---WEEAIRQGIRQMLESGTTSI---GAISS 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 335335018 74 DSSLLLADITDKFGQRAFVGKVCMDlNDTFPEYKETTEESIKETERFVSemlqknySRVKPIVTPRFSLSCSETLMGELG 153
Cdd:cd01312 98 DGSLLPALASSGLRGVFFNEVIGSN-PSAIDFKGETFLERFKRSKSFES-------QLFIPAISPHAPYSVHPELAQDLI 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 335335018 154 NIAKTRDLHIQSHISENRDEVEAV-------KNLYPSY---KNYTSVYDKNNL------LTNKTVMAHGCYLSAEELNVF 217
Cdd:cd01312 170 DLAKKLNLPLSTHFLESKEEREWLeeskgwfKHFWESFlklPKPKKLATAIDFldmlggLGTRVSFVHCVYANLEEAEIL 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 335335018 218 HERGASIAHCPNSNLSLSSGFLNVLEVLKHEVKIGLGTD-VAGGYSYSMLDAIRravmvSNILLINKVNEKSLTlKEVFR 296
Cdd:cd01312 250 ASRGASIALCPRSNRLLNGGKLDVSELKKAGIPVSLGTDgLSSNISLSLLDELR-----ALLDLHPEEDLLELA-SELLL 323
|
330 340
....*....|....*....|....*.
gi 335335018 297 LATLGGSQALGLdgEIGNFEVGKEFD 322
Cdd:cd01312 324 MATLGGARALGL--NNGEIEAGKRAD 347
|
|
| PRK08418 |
PRK08418 |
metal-dependent hydrolase; |
154-374 |
8.87e-20 |
|
metal-dependent hydrolase;
Pssm-ID: 181419 [Multi-domain] Cd Length: 408 Bit Score: 90.03 E-value: 8.87e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 335335018 154 NIAKTRDLHIQSHISENRDEVEAVKNLYPSYKNY--------TSVYDKNNLL----TNKTVMAHGCYLSAEELNVFHERG 221
Cdd:PRK08418 197 QLAKKENLLVSTHFLESKAEREWLEESKGWFKKFfekflkepKPLYTPKEFLelfkGLRTLFTHCVYASEEELEKIKSKN 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 335335018 222 ASIAHCPNSNLSLSSGFLNVLEVLKHEVKIGLGTD-VAGGYSYSMLDAIRRAVMVSNillinkvNEKSLTL-KEVFRLAT 299
Cdd:PRK08418 277 ASITHCPFSNRLLSNKALDLEKAKKAGINYSIATDgLSSNISLSLLDELRAALLTHA-------NMPLLELaKILLLSAT 349
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 335335018 300 LGGSQALGLD-GEIgnfEVGKEFDAILINpkasdspidlfYGDFFGDISEAVIQKFLYlgdDRNIEEVYVGGKQVV 374
Cdd:PRK08418 350 RYGAKALGLNnGEI---KEGKDADLSVFE-----------LPEECTKKEQLPLQFILH---AKEVKKLFIGGKEVK 408
|
|
| metallo-dependent_hydrolases |
cd01292 |
Superfamily of metallo-dependent hydrolases (also called amidohydrolase superfamily) is a ... |
4-305 |
1.83e-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: 1.83e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 335335018 4 LVDTHIHASQYSFAGssIDLPLLEWLTKYTFPAEHRFQNIDFAEEvytrvvrrTLKNGTTTAC-----YFATIHTDSSLL 78
Cdd:cd01292 1 FIDTHVHLDGSALRG--TRLNLELKEAEELSPEDLYEDTLRALEA--------LLAGGVTTVVdmgstPPPTTTKAAIEA 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 335335018 79 LAD-ITDKFGQRAFVGKVCMDLNdtfPEYKETTEESIKETERFVsemlqknYSRVKPIVTPRFSLSCSETLMGELGNI-- 155
Cdd:cd01292 71 VAEaARASAGIRVVLGLGIPGVP---AAVDEDAEALLLELLRRG-------LELGAVGLKLAGPYTATGLSDESLRRVle 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 335335018 156 -AKTRDLHIQSHISENRDEVEAVKNLYpsyknytsvydKNNLLTNKTVMAHGCYLSAEELNVFHERGASIAHCPNSNLSL 234
Cdd:cd01292 141 eARKLGLPVVIHAGELPDPTRALEDLV-----------ALLRLGGRVVIGHVSHLDPELLELLKEAGVSLEVCPLSNYLL 209
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 335335018 235 SS---GFLNVLEVLKHEVKIGLGTDVAGGYSYSMLDAIRRAVMVSNILLinkvneksLTLKEVFRLATLGGSQA 305
Cdd:cd01292 210 GRdgeGAEALRRLLELGIRVTLGTDGPPHPLGTDLLALLRLLLKVLRLG--------LSLEEALRLATINPARA 275
|
|
| PRK08204 |
PRK08204 |
hypothetical protein; Provisional |
1-371 |
1.86e-19 |
|
hypothetical protein; Provisional
Pssm-ID: 181288 [Multi-domain] Cd Length: 449 Bit Score: 89.29 E-value: 1.86e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 335335018 1 MPGLVDTHIHASQYSFAGSSIDLPLLEWLTKYTFPAEHRFQnidfAEEVY--TRV-VRRTLKNGTTTACYFATI-----H 72
Cdd:PRK08204 56 MPGLVDTHRHTWQSVLRGIGADWTLQTYFREIHGNLGPMFR----PEDVYiaNLLgALEALDAGVTTLLDWSHInnspeH 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 335335018 73 TDSSLL-LADItdkfGQRA--FVGKVCMDLNDTFpeykETTEESIKETERFVSEMLQKNYSRVK---PIVTPRFSlsCSE 146
Cdd:PRK08204 132 ADAAIRgLAEA----GIRAvfAHGSPGPSPYWPF----DSVPHPREDIRRVKKRYFSSDDGLLTlglAIRGPEFS--SWE 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 335335018 147 TLMGELGnIAKTRDLHIQSHISenrdeveavknLYPSYKNYTSV--YDKNNLLTNKTVMAHGCYLSAEELNVFHERGASI 224
Cdd:PRK08204 202 VARADFR-LARELGLPISMHQG-----------FGPWGATPRGVeqLHDAGLLGPDLNLVHGNDLSDDELKLLADSGGSF 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 335335018 225 AHCPNSNLSLSSGFLNVLEVLKHEVKIGLGTDVAGGYSYSMLDAIR------RAVMVSNILLINKV--NEKSLTLKEVFR 296
Cdd:PRK08204 270 SVTPEIEMMMGHGYPVTGRLLAHGVRPSLGVDVVTSTGGDMFTQMRfalqaeRARDNAVHLREGGMppPRLTLTARQVLE 349
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 335335018 297 LATLGGSQALGLDGEIGNFEVGKEFDAILINPKAsdspIDLFYgdfFGDISEAVIQkflyLGDDRNIEEVYVGGK 371
Cdd:PRK08204 350 WATIEGARALGLEDRIGSLTPGKQADLVLIDATD----LNLAP---VHDPVGAVVQ----SAHPGNVDSVMVAGR 413
|
|
| PRK07203 |
PRK07203 |
putative aminohydrolase SsnA; |
1-279 |
1.37e-17 |
|
putative aminohydrolase SsnA;
Pssm-ID: 235963 [Multi-domain] Cd Length: 442 Bit Score: 83.83 E-value: 1.37e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 335335018 1 MPGLVDTHIHAsqYS-FA-GSSIDLP----LLEWLTKYTFpaehrfqNIDFA---EEVYTRVVRRTL---KNGTTT---- 64
Cdd:PRK07203 58 MPGLINSHNHI--YSgLArGMMANIPpppdFISILKNLWW-------RLDRAltlEDVYYSALICSLeaiKNGVTTvfdh 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 335335018 65 -ACYFATihTDSSLLLADITDKFGQRafvGKVCMDLNDTFPEykETTEESIKETERFVSEMLQKNYSRVKPIVTPRFSLS 143
Cdd:PRK07203 129 hASPNYI--GGSLFTIADAAKKVGLR---AMLCYETSDRDGE--KELQEGVEENIRFIKHIDEAKDDMVEAMFGLHASFT 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 335335018 144 CS-ETL------MGELGniaktRDLHIqsHISENRDEVEAVKNLYpsYKNYTSVYDKNNLLTNKTVMAHGCYLSAEELNV 216
Cdd:PRK07203 202 LSdATLekcreaVKETG-----RGYHI--HVAEGIYDVSDSHKKY--GKDIVERLADFGLLGEKTLAAHCIYLSDEEIDL 272
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 335335018 217 FHERGASIAHCPNSNLSLSSGFLNVLEVLKHEVKIGLGTDvagGYSYSMLDAIRravmVSNIL 279
Cdd:PRK07203 273 LKETDTFVVHNPESNMGNAVGYNPVLEMIKNGILLGLGTD---GYTSDMFESYK----VANFK 328
|
|
| archeal_chlorohydrolases |
cd01305 |
Predicted chlorohydrolases. These metallo-dependent hydrolases from archea are part of the ... |
1-303 |
2.07e-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: 72.43 E-value: 2.07e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 335335018 1 MPGLVDTHIHASQYSFAGSSIDLPLLEwLTKYTFPAEHRF--QNIDFAEEVYTR-VVRRTLKNGTTTACYFATIHTDSSL 77
Cdd:cd01305 3 IPALVNAHTHLGDSAIKEVGDGLPLDD-LVAPPDGLKHRLlaQADDRELAEAMRkVLRDMRETGIGAFADFREGGVEGIE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 335335018 78 LLADITDKFgqrAFVGKVCMDlndtFPEYKETTEESIKETERFvsemlqkNYSrvkpivtprfslSCSETLMGELGNIAK 157
Cdd:cd01305 82 LLRRALGKL---PVPFEVILG----RPTEPDDPEILLEVADGL-------GLS------------SANDVDLEDILELLR 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 335335018 158 TRDLHIQSHISENRD-----EVEAVKNLYPsyknytsvydknNLLTnktvmaHGCYLSAEELNVFHERGASIAHCPNSNL 232
Cdd:cd01305 136 RRGKLFAIHASETREsvgmtDIERALDLEP------------DLLV------HGTHLTDEDLELVRENGVPVVLCPRSNL 197
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 335335018 233 SLSSGFLNVLEVLKHEVKIGLGTDVAGGYSYSMLDAIRRAVMVSNILlinkvneKSLTLKEVFRLATLGGS 303
Cdd:cd01305 198 YFGVGIPPVAELLKLGIKVLLGTDNVMVNEPDMWAEMEFLAKYSRLQ-------GYLSPLEILRMATVNAA 261
|
|
| PRK06151 |
PRK06151 |
N-ethylammeline chlorohydrolase; Provisional |
1-374 |
6.96e-14 |
|
N-ethylammeline chlorohydrolase; Provisional
Pssm-ID: 180428 [Multi-domain] Cd Length: 488 Bit Score: 72.77 E-value: 6.96e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 335335018 1 MPGLVDTHIHasqysfagSSIDLPLL------EWLTKYTFPAEHRFQNidfAEEVYTRVVRRT---------LKNGTTTA 65
Cdd:PRK06151 56 GPGFIDLDAL--------SDLDTTILgldngpGWAKGRVWSRDYVEAG---RREMYTPEELAFqkryafaqlLRNGITTA 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 335335018 66 CYFATI-------HTDSSLLLADITDKFGQRAFVG-------KVCMDLNDTFPEYKETT-EESIKETERFVSEMLQKNYS 130
Cdd:PRK06151 125 MPIASLfyrqwaeTYAEFAAAAEAAGRLGLRVYLGpayrsggSVLEADGSLEVVFDEARgLAGLEEAIAFIKRVDGAHNG 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 335335018 131 RVKPIVTPRFSLSCSETLMGELGNIAKTRDLHIQSHISENRDEVEAVKNLYpsykNYTS--VYDKNNLLTNKTVMAHGCY 208
Cdd:PRK06151 205 LVRGMLAPDRIETCTVDLLRRTAAAARELGCPVRLHCAQGVLEVETVRRLH----GTTPleWLADVGLLGPRLLIPHATY 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 335335018 209 LS---------AEELNVFHERGASIAHCPnSNLSLSSGFLNVLEVLKHE-VKIGLGTDVAggysysmldairRAVMVSNI 278
Cdd:PRK06151 281 ISgsprlnysgGDDLALLAEHGVSIVHCP-LVSARHGSALNSFDRYREAgINLALGTDTF------------PPDMVMNM 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 335335018 279 ---LLINKVNEKSLT---LKEVFRLATLGGSQALGLDgEIGNFEVGKEFDAILINPKasdspiDLFYGDFFGDISEAVIQ 352
Cdd:PRK06151 348 rvgLILGRVVEGDLDaasAADLFDAATLGGARALGRD-DLGRLAPGAKADIVVFDLD------GLHMGPVFDPIRTLVTG 420
|
410 420
....*....|....*....|..
gi 335335018 353 kflylGDDRNIEEVYVGGKQVV 374
Cdd:PRK06151 421 -----GSGRDVRAVFVDGRVVM 437
|
|
| PRK07213 |
PRK07213 |
chlorohydrolase; Provisional |
166-330 |
1.16e-10 |
|
chlorohydrolase; Provisional
Pssm-ID: 235969 [Multi-domain] Cd Length: 375 Bit Score: 62.36 E-value: 1.16e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 335335018 166 HISENRDEVEAVKNLYpsykNYTSVYDKNNLLTNKTVMAHGCYLSAEELNVFHERGASIAHCPNSNLSLSSGFLNVLEVL 245
Cdd:PRK07213 198 HAAEHKGSVEYSLEKY----GMTEIERLINLGFKPDFIVHATHPSNDDLELLKENNIPVVVCPRANASFNVGLPPLNEML 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 335335018 246 KHEVKIGLGTDVAGGYSYSM---LDAIRRAVmvsnillinkvnekSLTLKEVFRLATLGGSQALGLDgEIGNFEVGKEFD 322
Cdd:PRK07213 274 EKGILLGIGTDNFMANSPSIfreMEFIYKLY--------------HIEPKEILKMATINGAKILGLI-NVGLIEEGFKAD 338
|
....*...
gi 335335018 323 AILINPKA 330
Cdd:PRK07213 339 FTFIKPTN 346
|
|
| HutI |
COG1228 |
Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport ... |
1-374 |
1.79e-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: 1.79e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 335335018 1 MPGLVDTHIHasqysFAGSSIDLPLLEWLTKYTfPAEHRFQNIDfaeevytRVVRRTLKNGTTTAcyFATIHTDSSLLLA 80
Cdd:COG1228 64 LPGLIDAHTH-----LGLGGGRAVEFEAGGGIT-PTVDLVNPAD-------KRLRRALAAGVTTV--RDLPGGPLGLRDA 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 335335018 81 DITDKF----GQRAFVGKVCMDLNDTFPEYketteeSIKETERFVSEMLQKNYSRVKPIVT---PRFSLSCSETLMGElg 153
Cdd:COG1228 129 IIAGESkllpGPRVLAAGPALSLTGGAHAR------GPEEARAALRELLAEGADYIKVFAEggaPDFSLEELRAILEA-- 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 335335018 154 niAKTRDLHIQSHISENRDEVEAVKNlypsykNYTSVydknnlltnktvmAHGCYLSAEELNVFHERGASIAhCPNSNLS 233
Cdd:COG1228 201 --AHALGLPVAAHAHQADDIRLAVEA------GVDSI-------------EHGTYLDDEVADLLAEAGTVVL-VPTLSLF 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 335335018 234 LSSGFL------------------NVLEVLKHEVKIGLGTDVAGGYS--YSMLDAIRRAVMVSnillinkvneksLTLKE 293
Cdd:COG1228 259 LALLEGaaapvaakarkvreaalaNARRLHDAGVPVALGTDAGVGVPpgRSLHRELALAVEAG------------LTPEE 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 335335018 294 VFRLATLGGSQALGLDGEIGNFEVGKEFDAILINpkasdspidlfyGDFFGDISeaviqkflYLgddRNIEEVYVGGKQV 373
Cdd:COG1228 327 ALRAATINAAKALGLDDDVGSLEPGKLADLVLLD------------GDPLEDIA--------YL---EDVRAVMKDGRVV 383
|
.
gi 335335018 374 V 374
Cdd:COG1228 384 D 384
|
|
| Met_dep_hydrolase_E |
cd01313 |
Metallo-dependent hydrolases, subgroup D is part of the superfamily of metallo-dependent ... |
161-371 |
3.39e-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: 3.39e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 335335018 161 LHIqsHISENRDEVEAVknLYPSYKNYTSVYDKNNLLTNKTVMAHGCYLSAEELNVFHERGASIAHCPNSNLSLSSGFLN 240
Cdd:cd01313 222 VHI--HLAEQPKEVDDC--LAAHGRRPVELLLDHGHLDARWCLVHATHLTDNETLLLGRSGAVVGLCPTTEANLGDGIFP 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 335335018 241 VLEVLKHEVKIGLGTDVAGG-----------YSYSMLDAiRRAVMVSnillinkvnEKSLTLKEVFRLATLGGSQALGLD 309
Cdd:cd01313 298 AAALLAAGGRIGIGSDSNARidlleelrqleYSQRLRDR-ARNVLAT---------AGGSSARALLDAALAGGAQALGLA 367
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 335335018 310 geIGNFEVGKEFDAILInpkASDSPidlfygDFFGDISEAVIQKFLYLGDDRNIEEVYVGGK 371
Cdd:cd01313 368 --TGALEAGARADLLSL---DLDHP------SLAGALPDTLLDAWVFAAGDREVRDVVVGGR 418
|
|
| Amidohydro_3 |
pfam07969 |
Amidohydrolase family; |
203-374 |
1.12e-05 |
|
Amidohydrolase family;
Pssm-ID: 400360 [Multi-domain] Cd Length: 464 Bit Score: 47.14 E-value: 1.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 335335018 203 MAHGC---YLSAEELNVFHERGASIAHCPNSNLSLS------------SGFLNVLEVLKHEVKIGLGTDVAGGySYSMLD 267
Cdd:pfam07969 298 IEHAQgvvPYTYSQIERVAALGGAAGVQPVFDPLWGdwlqdrlgaeraRGLTPVKELLNAGVKVALGSDAPVG-PFDPWP 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 335335018 268 AIRRAVM-----VSNILLInkvnEKSLTLKEVFRLATLGGSQALGLDGEIGNFEVGKEFDAILINpkasdspIDLFygdf 342
Cdd:pfam07969 377 RIGAAVMrqtagGGEVLGP----DEELSLEEALALYTSGPAKALGLEDRKGTLGVGKDADLVVLD-------DDPL---- 441
|
170 180 190
....*....|....*....|....*....|..
gi 335335018 343 fgDISEAVIqkflylgDDRNIEEVYVGGKQVV 374
Cdd:pfam07969 442 --TVDPPAI-------ADIRVRLTVVDGRVVY 464
|
|
| PRK09229 |
PRK09229 |
N-formimino-L-glutamate deiminase; Validated |
161-374 |
5.21e-05 |
|
N-formimino-L-glutamate deiminase; Validated
Pssm-ID: 236420 [Multi-domain] Cd Length: 456 Bit Score: 44.84 E-value: 5.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 335335018 161 LHIqsHISENRDEVEAVKNLY---PsyknyTSVYDKNNLLTNKTVMAHGCYLSAEELNVFHERGASIAHCPNSNLSLSSG 237
Cdd:PRK09229 231 VHI--HIAEQTKEVDDCLAWSgarP-----VEWLLDHAPVDARWCLVHATHLTDAETARLARSGAVAGLCPTTEANLGDG 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 335335018 238 FLNVLEVLKHEVKIGLGTDvaggySYSMLDAI---------------RRAVMVSNillinkvnEKSLTLKEVFRLATLGG 302
Cdd:PRK09229 304 IFPAVDYLAAGGRFGIGSD-----SHVSIDLVeelrlleygqrlrdrRRNVLAAA--------AQPSVGRRLFDAALAGG 370
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 335335018 303 SQALGLDgeIGNFEVGKEFDAILINPkasDSPidlfygDFFGDISEAVIQKFLYLGDDRNIEEVYVGGKQVV 374
Cdd:PRK09229 371 AQALGRA--IGGLAVGARADLVVLDL---DHP------ALAGREGDALLDRWVFAGGDAAVRDVWVAGRWVV 431
|
|
| Imidazolone-5PH |
cd01296 |
Imidazolonepropionase/imidazolone-5-propionate hydrolase (Imidazolone-5PH) catalyzes the third ... |
203-353 |
7.64e-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: 7.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 335335018 203 MAHGCYLSAEELNVFHERGASIAHCPNSNLSLSSGFLNVLEVLKHEVKIGLGTDVAGGySY---SMLDAIRRAVmvsnIL 279
Cdd:cd01296 233 ADHLEHTSDEGIAALAEAGTVAVLLPGTAFSLRETYPPARKLIDAGVPVALGTDFNPG-SSptsSMPLVMHLAC----RL 307
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 335335018 280 LinkvnekSLTLKEVFRLATLGGSQALGLDGEIGNFEVGKEFDAILINpkaSDSPIDLFYgdFFG-DISEAVIQK 353
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 ... |
232-327 |
1.38e-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: 1.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 335335018 232 LSLSSGFLNVLEVLKHEVKIGLGTD-----VAGGYSYSMLdairrAVMVsnillinkvnEKSLTLKEVFRLATLGGSQAL 306
Cdd:cd01299 247 LVLEAGRDALRRAHKAGVKIAFGTDagfpvPPHGWNAREL-----ELLV----------KAGGTPAEALRAATANAAELL 311
|
90 100
....*....|....*....|.
gi 335335018 307 GLDGEIGNFEVGKEFDAILIN 327
Cdd:cd01299 312 GLSDELGVIEAGKLADLLVVD 332
|
|
| nagA |
PRK11170 |
N-acetylglucosamine-6-phosphate deacetylase; Provisional |
259-319 |
8.73e-03 |
|
N-acetylglucosamine-6-phosphate deacetylase; Provisional
Pssm-ID: 183010 Cd Length: 382 Bit Score: 38.03 E-value: 8.73e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 335335018 259 GGYSYSMLDAIRravmvsnilliNKVNEKSLTLKEVFRLATLGGSQALGLDGEIGNFEVGK 319
Cdd:PRK11170 307 SGSALTMIEAVR-----------NLVEHVGIALDEALRMATLYPARAIGVDKRLGSIEAGK 356
|
|
| |
