|
Name |
Accession |
Description |
Interval |
E-value |
| GDEase |
cd01303 |
Guanine deaminase (GDEase). Guanine deaminase is an aminohydrolase responsible for the ... |
13-444 |
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: 611.20 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753960 13 FRGTFVHSTWTCPMEvLRDHLLGVSDSGKIVFLEESSQQEKLAKEW--CFKPCEIRELSHHEFFMPGLVDTHIHAPQYAF 90
Cdd:cd01303 1 FRGTFIHTKSLPELE-LVEDALRVVEDGLIVVVDGNIIAAGAAETLkrAAKPGARVIDSPNQFILPGFIDTHIHAPQYAN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753960 91 AGSNVDLPLLEWLNKYTFPTEQRFRSTDVAEEVYTRVVRRTLKNGTTTACYFGTIHTDSSLILAEITDKFGQRAFVGKVC 170
Cdd:cd01303 80 IGSGLGEPLLDWLETYTFPEEAKFADPAYAREVYGRFLDELLRNGTTTACYFATIHPESTEALFEEAAKRGQRAIAGKVC 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753960 171 MDLNDtvPEYK-ETTEESVKETERFVSEMLQKnYPRVKPIVTPRFTLSCTETLMSELGNIAKTH-DLYIQSHISENREEI 248
Cdd:cd01303 160 MDRNA--PEYYrDTAESSYRDTKRLIERWHGK-SGRVKPAITPRFAPSCSEELLAALGKLAKEHpDLHIQTHISENLDEI 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753960 249 EAVKSLYPSYKNYTDVYDKNNLLTNKTVMAHGCYLSEEELNIFSERGASIAHCPNSNLSLSSGLLNVLEVLKHKVKIGLG 328
Cdd:cd01303 237 AWVKELFPGARDYLDVYDKYGLLTEKTVLAHCVHLSEEEFNLLKERGASVAHCPTSNLFLGSGLFDVRKLLDAGIKVGLG 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753960 329 TDVAGGYSYSMLDAIRRAVMVSNVLLINKVNEKNLTLKEVFRLATLGGSQALGLDSEIGNFEVGKEFDALLINPRASDSP 408
Cdd:cd01303 317 TDVGGGTSFSMLDTLRQAYKVSRLLGYELGGHAKLSPAEAFYLATLGGAEALGLDDKIGNFEVGKEFDAVVIDPSATPLL 396
|
410 420 430
....*....|....*....|....*....|....*.
gi 6753960 409 IDLfygDFVGDISEAVIQKFLYLGDDRNIEEVYVGG 444
Cdd:cd01303 397 ADR---MFRVESLEEALFKFLYLGDDRNIREVYVAG 429
|
|
| guan_deamin |
TIGR02967 |
guanine deaminase; This model describes guanine deaminase, which hydrolyzes guanine to ... |
26-444 |
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: 537.22 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753960 26 MEVLRDHLLGVSDsGKIVFLEESSQQeklaKEWCFKPCEIRELSHHeFFMPGLVDTHIHAPQYAFAGSnVDLPLLEWLNK 105
Cdd:TIGR02967 1 LEYFEDGLLVVEN-GRIVAVGDYAEL----KETLPAGVEIDDYRGH-LIMPGFIDTHIHYPQTEMIAS-YGEQLLEWLEK 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753960 106 YTFPTEQRFRSTDVAEEVYTRVVRRTLKNGTTTACYFGTIHTDSSLILAEITDKFGQRAFVGKVCMDLNdtVPEY-KETT 184
Cdd:TIGR02967 74 YTFPTEARFADPDHAEEVAEFFLDELLRNGTTTALVFATVHPESVDALFEAALKRGMRMIAGKVLMDRN--APDYlRDTA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753960 185 EESVKETERFVSEMLQKNypRVKPIVTPRFTLSCTETLMSELGNIAKTH-DLYIQSHISENREEIEAVKSLYPSYKNYTD 263
Cdd:TIGR02967 152 ESSYDESKALIERWHGKG--RLLYAVTPRFAPTSSPEQLAAAGELAKEYpDVYVQTHLSENKDEIAWVKELFPEAKDYLD 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753960 264 VYDKNNLLTNKTVMAHGCYLSEEELNIFSERGASIAHCPNSNLSLSSGLLNVLEVLKHKVKIGLGTDVAGGYSYSMLDAI 343
Cdd:TIGR02967 230 VYDHYGLLGRRSVFAHCIHLSDEECQRLAETGAAIAHCPTSNLFLGSGLFNLKKALEHGVRVGLGTDVGGGTSFSMLQTL 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753960 344 RRAVMVSNVLlinkvnEKNLTLKEVFRLATLGGSQALGLDSEIGNFEVGKEFDALLINPRASDSPIDLFYGdfvGDISEA 423
Cdd:TIGR02967 310 REAYKVSQLQ------GARLSPFEAFYLATLGGARALDLDDRIGNFEPGKEADFVVLDPAATPLLALRFEG---ADTLED 380
|
410 420
....*....|....*....|.
gi 6753960 424 VIQKFLYLGDDRNIEEVYVGG 444
Cdd:TIGR02967 381 KLFKLMYLGDDRNVAETYVAG 401
|
|
| SsnA |
COG0402 |
Cytosine/adenosine deaminase or related metal-dependent hydrolase [Nucleotide transport and ... |
16-448 |
8.78e-112 |
|
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: 335.64 E-value: 8.78e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753960 16 TFVHSTWTCPM----EVLRDHLLGVSDsGKIVFLEESSQQEKLakewcFKPCEIRELSHHeFFMPGLVDTHIHAPQYAFA 91
Cdd:COG0402 2 LLIRGAWVLTMdpagGVLEDGAVLVED-GRIAAVGPGAELPAR-----YPAAEVIDAGGK-LVLPGLVNTHTHLPQTLLR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753960 92 GSNVDLPLLEWLNKYTFPTEQRFrSTDVAEEVYTRVVRRTLKNGTTTACYFGTIHTDSSLILAEITDKFGQRAFVGKVCM 171
Cdd:COG0402 75 GLADDLPLLDWLEEYIWPLEARL-DPEDVYAGALLALAEMLRSGTTTVADFYYVHPESADALAEAAAEAGIRAVLGRGLM 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753960 172 DLNdTVPEYKETTEESVKETERFVSEMLQKNYPRVKPIVTPRFTLSCTETLMSELGNIAKTHDLYIQSHISENREEIEAV 251
Cdd:COG0402 154 DRG-FPDGLREDADEGLADSERLIERWHGAADGRIRVALAPHAPYTVSPELLRAAAALARELGLPLHTHLAETRDEVEWV 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753960 252 KSLYPsyKNYTDVYDKNNLLTNKTVMAHGCYLSEEELNIFSERGASIAHCPNSNLSLSSGLLNVLEVLKHKVKIGLGTDV 331
Cdd:COG0402 233 LELYG--KRPVEYLDELGLLGPRTLLAHCVHLTDEEIALLAETGASVAHCPTSNLKLGSGIAPVPRLLAAGVRVGLGTDG 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753960 332 AGG-YSYSMLDAIRRAvmvsnvLLINKVNEKN---LTLKEVFRLATLGGSQALGLDSEIGNFEVGKEFDALLINPRASD- 406
Cdd:COG0402 311 AASnNSLDMFEEMRLA------ALLQRLRGGDptaLSAREALEMATLGGARALGLDDEIGSLEPGKRADLVVLDLDAPHl 384
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 6753960 407 SPIDlfygdfvgdiseAVIQKFLYLGDDRNIEEVYVGGKQVV 448
Cdd:COG0402 385 APLH------------DPLSALVYAADGRDVRTVWVAGRVVV 414
|
|
| PRK09228 |
PRK09228 |
guanine deaminase; Provisional |
64-447 |
1.02e-101 |
|
guanine deaminase; Provisional
Pssm-ID: 236419 [Multi-domain] Cd Length: 433 Bit Score: 310.20 E-value: 1.02e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753960 64 EIRELSHHeFFMPGLVDTHIHAPQYAFAGSNVDlPLLEWLNKYTFPTEQRFRSTDVAEEVYTRVVRRTLKNGTTTACYFG 143
Cdd:PRK09228 59 EVTDYRGK-LILPGFIDTHIHYPQTDMIASYGE-QLLDWLNTYTFPEERRFADPAYAREVAEFFLDELLRNGTTTALVFG 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753960 144 TIHTDSSLILAEITDKFGQRAFVGKVCMDLNdtVPEY-KETTEESVKETERFVSEMLQKNypRVKPIVTPRFTLSCTETL 222
Cdd:PRK09228 137 TVHPQSVDALFEAAEARNMRMIAGKVLMDRN--APDGlRDTAESGYDDSKALIERWHGKG--RLLYAITPRFAPTSTPEQ 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753960 223 MSELGNIAKTH-DLYIQSHISENREEIEAVKSLYPSYKNYTDVYDKNNLLTNKTVMAHGCYLSEEELNIFSERGASIAHC 301
Cdd:PRK09228 213 LEAAGALAREHpDVWIQTHLSENLDEIAWVKELFPEARDYLDVYERYGLLGPRAVFAHCIHLEDRERRRLAETGAAIAFC 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753960 302 PNSNLSLSSGLLNVLEVLKHKVKIGLGTDVAGGYSYSMLDAIRRAVMVSnvllinKVNEKNLTLKEVFRLATLGGSQALG 381
Cdd:PRK09228 293 PTSNLFLGSGLFDLKRADAAGVRVGLGTDVGGGTSFSMLQTMNEAYKVQ------QLQGYRLSPFQAFYLATLGGARALG 366
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6753960 382 LDSEIGNFEVGKEFDALLINPRASdSPIDLFYgDFVGDISEAVIQKFLyLGDDRNIEEVYVGGKQV 447
Cdd:PRK09228 367 LDDRIGNLAPGKEADFVVLDPAAT-PLLALRT-ARAESLEELLFALMT-LGDDRAVAETYVAGRPV 429
|
|
| ATZ_TRZ_like |
cd01298 |
TRZ/ATZ family contains enzymes from the atrazine degradation pathway and related hydrolases. ... |
75-448 |
1.12e-63 |
|
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: 211.29 E-value: 1.12e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753960 75 MPGLVDTHIHAPQYAFAGSNVDLPLLEWLNKYTFPTEQRFRstdvAEEVY--TRV-VRRTLKNGTTTACYFGTIHTDssl 151
Cdd:cd01298 55 MPGLVNTHTHLAMTLLRGLADDLPLMEWLKDLIWPLERLLT----EEDVYlgALLaLAEMIRSGTTTFADMYFFYPD--- 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753960 152 ILAEITDKFGQRAFVGKVCMDLNDTVPEykeTTEESVKETERFVSEMLQKNYPRVKPIVTPRFTLSCTETLMSELGNIAK 231
Cdd:cd01298 128 AVAEAAEELGIRAVLGRGIMDLGTEDVE---ETEEALAEAERLIREWHGAADGRIRVALAPHAPYTCSDELLREVAELAR 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753960 232 THDLYIQSHISENREEIEAVKSLY---PsyknyTDVYDKNNLLTNKTVMAHGCYLSEEELNIFSERGASIAHCPNSNLSL 308
Cdd:cd01298 205 EYGVPLHIHLAETEDEVEESLEKYgkrP-----VEYLEELGLLGPDVVLAHCVWLTDEEIELLAETGTGVAHNPASNMKL 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753960 309 SSGLLNVLEVLKHKVKIGLGTD-VAGGYSYSMLDAIRRAvmvsnvLLINKV---NEKNLTLKEVFRLATLGGSQALGLDs 384
Cdd:cd01298 280 ASGIAPVPEMLEAGVNVGLGTDgAASNNNLDMFEEMRLA------ALLQKLahgDPTALPAEEALEMATIGGAKALGLD- 352
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6753960 385 EIGNFEVGKEFDALLINPRASD-SPIDlfygdfvGDISEAViqkflYLGDDRNIEEVYVGGKQVV 448
Cdd:cd01298 353 EIGSLEVGKKADLILIDLDGPHlLPVH-------DPISHLV-----YSANGGDVDTVIVNGRVVM 405
|
|
| PRK07228 |
PRK07228 |
5'-deoxyadenosine deaminase; |
75-401 |
1.23e-56 |
|
5'-deoxyadenosine deaminase;
Pssm-ID: 180895 [Multi-domain] Cd Length: 445 Bit Score: 193.68 E-value: 1.23e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753960 75 MPGLVDTHIHAPQYAFAGSNVDLPLLEWLNKYTFPTEQrfrSTDvAEEVYTRV---VRRTLKNGTTTACYFGTI-HTDSS 150
Cdd:PRK07228 55 IPGLIQGHIHLCQTLFRGIADDLELLDWLKDRIWPLEA---AHD-AESMYYSAllgIGELIESGTTTIVDMESVhHTDSA 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753960 151 LilaEITDKFGQRAFVGKVCMDLNDTVPE-YKETTEESVKETERFVSEMLQKNYPRVKPIVTPRFTLSCTETLMSELGNI 229
Cdd:PRK07228 131 F---EAAGESGIRAVLGKVMMDYGDDVPEgLQEDTEASLAESVRLLEKWHGADNGRIRYAFTPRFAVSCTEELLRGVRDL 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753960 230 AKTHDLYIQSHISENREEIEAVKSlYPSYKNYTdVYDKNNLLTNKTVMAHGCYLSEEELNIFSERGASIAHCPNSNLSLS 309
Cdd:PRK07228 208 ADEYGVRIHTHASENRGEIETVEE-ETGMRNIH-YLDEVGLTGEDLILAHCVWLDEEEREILAETGTHVTHCPSSNLKLA 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753960 310 SGLLNVLEVLKHKVKIGLGTDvaGGYSYSMLDA---IRRAVmvsnvlLINKVNEKN---LTLKEVFRLATLGGSQALGLD 383
Cdd:PRK07228 286 SGIAPVPDLLERGINVALGAD--GAPCNNTLDPfteMRQAA------LIQKVDRLGptaMPARTVFEMATLGGAKAAGFE 357
|
330
....*....|....*...
gi 6753960 384 SEIGNFEVGKEFDALLIN 401
Cdd:PRK07228 358 DEIGSLEEGKKADLAILD 375
|
|
| Amidohydro_1 |
pfam01979 |
Amidohydrolase family; This family of enzymes are a a large metal dependent hydrolase ... |
75-447 |
8.33e-53 |
|
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: 180.39 E-value: 8.33e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753960 75 MPGLVDTHIHAPQYAFAGSNVDLpllewlnkytfpteqrfrstDVAEEVYTRVVRRTLKNGTTTACYFGTIHTDSSLILA 154
Cdd:pfam01979 3 LPGLIDAHVHLEMGLLRGIPVPP--------------------EFAYEALRLGITTMLKSGTTTVLDMGATTSTGIEALL 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753960 155 EITDK--FGQRAFVGKVCMDLNDTVPEYKETTEESVKETErfvsEMLQKNYPRVKPIVTPRFTLSCTETLMSELGNIAKT 232
Cdd:pfam01979 63 EAAEElpLGLRFLGPGCSLDTDGELEGRKALREKLKAGAE----FIKGMADGVVFVGLAPHGAPTFSDDELKAALEEAKK 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753960 233 HDLYIQSHISENREEIEAVKSLYPS---YKNYTDVYDKNNLL-TNKTVMAHGCYLSEEELNIFSER--GASIAHCPNSNL 306
Cdd:pfam01979 139 YGLPVAIHALETKGEVEDAIAAFGGgieHGTHLEVAESGGLLdIIKLILAHGVHLSPTEANLLAEHlkGAGVAHCPFSNS 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753960 307 SLSSGLLNVLEVLKHKVKIGLGTDVAG-GYSYSMLDAIRRAVmvsnvlLINKVNEKNLTLKEVFRLATLGGSQALGLDSE 385
Cdd:pfam01979 219 KLRSGRIALRKALEDGVKVGLGTDGAGsGNSLNMLEELRLAL------ELQFDPEGGLSPLEALRMATINPAKALGLDDK 292
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6753960 386 IGNFEVGKEFDALLINPRasdspidlfygdfvgdiseaVIQKFLYLGDDRNIEEVYVGGKQV 447
Cdd:pfam01979 293 VGSIEVGKDADLVVVDLD--------------------PLAAFFGLKPDGNVKKVIVKGKIV 334
|
|
| PRK08393 |
PRK08393 |
N-ethylammeline chlorohydrolase; Provisional |
71-448 |
1.54e-46 |
|
N-ethylammeline chlorohydrolase; Provisional
Pssm-ID: 181411 [Multi-domain] Cd Length: 424 Bit Score: 166.13 E-value: 1.54e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753960 71 HEFFMPGLVDTHIHAPQYAFAGSNVDLPLLEWLNKYTFPTEQRFRSTDVAEEVYTRVVRrTLKNGTTTAC--YFgtiHTD 148
Cdd:PRK08393 49 GSVVSPGFINAHTHSPMVLLRGLADDVPLMEWLQNYIWPRERKLKRKDIYWGAYLGLLE-MIKSGTTTFVdmYF---HME 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753960 149 SsliLAEITDKFGQRAFVGKVCMDLNDtvpeyKETTEESVKETERFVSEMLQKNYPRVKPIVTPRFTLSCTETLMSELGN 228
Cdd:PRK08393 125 E---VAKATLEVGLRGYLSYGMVDLGD-----EEKREKEIKETEKLMEFIEKLNSPRVHFVFGPHAPYTCSLALLKWVRE 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753960 229 IAKTHDLYIQSHISENREEIEAVKSLYPsyKNYTDVYDKNNLLTNKTVMAHGCYLSEEELNIFSERGASIAHCPNSNLSL 308
Cdd:PRK08393 197 KAREWNKLITIHLSETMDEIKQIREKYG--KSPVVLLDEIGFLNEDVIAAHGVWLSSRDIRILASAGVTVAHNPASNMKL 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753960 309 SSGLLNVLEVLKHKVKIGLGTDvaGGYSYSMLDAIRRAVMVSnvlLINKVNEKNLTL---KEVFRLATLGGSQALGLDSe 385
Cdd:PRK08393 275 GSGVMPLRKLLNAGVNVALGTD--GAASNNNLDMLREMKLAA---LLHKVHNLDPTIadaETVFRMATQNGAKALGLKA- 348
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6753960 386 iGNFEVGKEFDALLINPRASD-SPIDlfygdfvgdiseAVIQKFLYLGDDRNIEEVYVGGKQVV 448
Cdd:PRK08393 349 -GVIKEGYLADIAVIDFNRPHlRPIN------------NPISHLVYSANGNDVETTIVDGKIVM 399
|
|
| PRK09045 |
PRK09045 |
TRZ/ATZ family hydrolase; |
16-396 |
8.02e-39 |
|
TRZ/ATZ family hydrolase;
Pssm-ID: 236366 [Multi-domain] Cd Length: 443 Bit Score: 145.82 E-value: 8.02e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753960 16 TFVHSTWTCPME----VLRDHLLGVSDsGKIVFLeeSSQQEKLAKewcFKPCEIRELSHHeFFMPGLVDTHIHAPQYAFA 91
Cdd:PRK09045 9 LLIEARWIVPVEpagvVLEDHAVAIRD-GRIVAI--LPRAEARAR---YAAAETVELPDH-VLIPGLINAHTHAAMSLLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753960 92 GSNVDLPLLEWLNKYTFPTEQRFRSTD---------VAEevytrvvrrTLKNGTTTA--CYFgtiHTDsslILAEITDKF 160
Cdd:PRK09045 82 GLADDLPLMTWLQDHIWPAEGAWVSEEfvrdgtllaIAE---------MLRGGTTCFndMYF---FPE---AAAEAAHQA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753960 161 GQRAFVGKVCMDlndtVP-EYKETTEES----VKETERFvsemlqKNYPRVKPIVTPR--FTLScTETLmSELGNIAKTH 233
Cdd:PRK09045 147 GMRAQIGMPVLD----FPtAWASDADEYlakgLELHDQW------RHHPLISTAFAPHapYTVS-DENL-ERIRTLAEQL 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753960 234 DLYIQSHISENREEIEAvkslypSYKNY----TDVYDKNNLLTNKTVMAHGCYLSEEELNIFSERGASIAHCPNSNLSLS 309
Cdd:PRK09045 215 DLPIHIHLHETAQEIAD------SLKQHgqrpLARLARLGLLGPRLIAVHMTQLTDAEIALLAETGCSVVHCPESNLKLA 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753960 310 SGLLNVLEVLKHKVKIGLGTD-VAGGYSYSMLDAIRRAVMVSnvllinkvneKNLTL-------KEVFRLATLGGSQALG 381
Cdd:PRK09045 289 SGFCPVAKLLQAGVNVALGTDgAASNNDLDLFGEMRTAALLA----------KAVAGdatalpaHTALRMATLNGARALG 358
|
410
....*....|....*
gi 6753960 382 LDSEIGNFEVGKEFD 396
Cdd:PRK09045 359 LDDEIGSLEPGKQAD 373
|
|
| PRK06038 |
PRK06038 |
N-ethylammeline chlorohydrolase; Provisional |
70-403 |
2.27e-38 |
|
N-ethylammeline chlorohydrolase; Provisional
Pssm-ID: 180363 [Multi-domain] Cd Length: 430 Bit Score: 144.12 E-value: 2.27e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753960 70 HHEFFMPGLVDTHIHAPQYAFAGSNVDLPLLEWLNKYTFPTEQRFRstdvAEEVYTRVVRRTL---KNGTTT--ACYFGT 144
Cdd:PRK06038 49 KGSVVMPGLVNTHTHAAMTLFRGYADDLPLAEWLNDHIWPAEAKLT----AEDVYAGSLLACLemiKSGTTSfaDMYFYM 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753960 145 IHTdsslilAEITDKFGQRAFVGKVCMDLNDTvpeykETTEESVKETERFVSEMLQKNYPRVKPIVTPRFTLSCTETLMS 224
Cdd:PRK06038 125 DEV------AKAVEESGLRAALSYGMIDLGDD-----EKGEAELKEGKRFVKEWHGAADGRIKVMYGPHAPYTCSEEFLS 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753960 225 ELGNIAKTHDLYIQSHISENREEIEAVKSLYPsyKNYTDVYDKNNLLTNKTVMAHGCYLSEEELNIFSERGASIAHCPNS 304
Cdd:PRK06038 194 KVKKLANKDGVGIHIHVLETEAELNQMKEQYG--MCSVNYLDDIGFLGPDVLAAHCVWLSDGDIEILRERGVNVSHNPVS 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753960 305 NLSLSSGLLNVLEVLKHKVKIGLGTD-VAGGYSYSMLDAIRRAVmvsnvlLINKVNEKNLTL---KEVFRLATLGGSQAL 380
Cdd:PRK06038 272 NMKLASGIAPVPKLLERGVNVSLGTDgCASNNNLDMFEEMKTAA------LLHKVNTMDPTAlpaRQVLEMATVNGAKAL 345
|
330 340
....*....|....*....|...
gi 6753960 381 GLDSeiGNFEVGKEFDALLINPR 403
Cdd:PRK06038 346 GINT--GMLKEGYLADIIIVDMN 366
|
|
| PRK06687 |
PRK06687 |
TRZ/ATZ family protein; |
23-448 |
3.00e-37 |
|
TRZ/ATZ family protein;
Pssm-ID: 180657 [Multi-domain] Cd Length: 419 Bit Score: 140.91 E-value: 3.00e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753960 23 TC--PMEVLRDHLLGVSDSgKIV--------FLEESSQQEKLAKEWcfkpceirelshhefFMPGLVDTHIHAPQYAFAG 92
Cdd:PRK06687 11 TCdqDFHVYLDGILAVKDS-QIVyvgqdkpaFLEQAEQIIDYQGAW---------------IMPGLVNCHTHSAMTGLRG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753960 93 SNVDLPLLEWLNKYTFPTEQRFrSTDVAEEVYTRVVRRTLKNGTTTacyFGTIHTDSSLILAEITDKFGQRafvGKVCMD 172
Cdd:PRK06687 75 IRDDSNLHEWLNDYIWPAESEF-TPDMTTNAVKEALTEMLQSGTTT---FNDMYNPNGVDIQQIYQVVKTS---KMRCYF 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753960 173 LNDTVPEYKETTEESVKETERFVSEMLQKNYPRVKPIVTPRFTLSCTETLMSELGNIAKTHDLYIQSHISENREEIEAVK 252
Cdd:PRK06687 148 SPTLFSSETETTAETISRTRSIIDEILKYKNPNFKVMVAPHSPYSCSRDLLEASLEMAKELNIPLHVHVAETKEESGIIL 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753960 253 SLYPsyKNYTDVYDKNNLLTNKTVMAHGCYLSEEELNIFSERGASIAHCPNSNLSLSSGLLNVLEVLKHKVKIGLGTD-V 331
Cdd:PRK06687 228 KRYG--KRPLAFLEELGYLDHPSVFAHGVELNEREIERLASSQVAIAHNPISNLKLASGIAPIIQLQKAGVAVGIATDsV 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753960 332 AGGYSYSMLDAIRRAVMVSNvllINKVNEKNLTLKEVFRLATLGGSQALGLDSEIGNFEVGKEFDALLINPRASdspIDL 411
Cdd:PRK06687 306 ASNNNLDMFEEGRTAALLQK---MKSGDASQFPIETALKVLTIEGAKALGMENQIGSLEVGKQADFLVIQPQGK---IHL 379
|
410 420 430
....*....|....*....|....*....|....*..
gi 6753960 412 FygdfvgdISEAVIQKFLYLGDDRNIEEVYVGGKQVV 448
Cdd:PRK06687 380 Q-------PQENMLSHLVYAVKSSDVDDVYIAGEQVV 409
|
|
| PRK15493 |
PRK15493 |
bifunctional S-methyl-5'-thioadenosine deaminase/S-adenosylhomocysteine deaminase; |
72-448 |
9.55e-28 |
|
bifunctional S-methyl-5'-thioadenosine deaminase/S-adenosylhomocysteine deaminase;
Pssm-ID: 185390 [Multi-domain] Cd Length: 435 Bit Score: 114.77 E-value: 9.55e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753960 72 EFFMPGLVDTHIHAPQYAFAGSNVDLPLLEWLNKYTFPTEQRFrSTDVAEEVYTRVVRRTLKNGTTT-ACYFGTIHTDSS 150
Cdd:PRK15493 55 KWVLPGLVNTHTHVVMSLLRGIGDDMLLQPWLETRIWPLESQF-TPELAVASTELGLLEMVKSGTTSfSDMFNPIGVDQD 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753960 151 LILaEITDKFGQRAFVGKVCMDLNDtvpeyKETTEESVKETERFVSEMLQKNyPRVKPIVTPRFTLSCTETLMSELGNIA 230
Cdd:PRK15493 134 AIM-ETVSRSGMRAAVSRTLFSFGT-----KEDEKKAIEEAEKYVKRYYNES-GMLTTMVAPHSPYTCSTELLEECARIA 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753960 231 KTHDLYIQSHISENREEIEAVKSLYPsyKNYTDVYDKNNLLTNKTVMAHGCYLSEEELNIFSERGASIAHCPNSNLSLSS 310
Cdd:PRK15493 207 VENQTMVHIHLSETEREVRDIEAQYG--KRPVEYAASCGLFKRPTVIAHGVVLNDNERAFLAEHDVRVAHNPNSNLKLGS 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753960 311 GLLNVLEVLKHKVKIGLGTD-VAGGYSYSMLDAIRRAVMVSNVLlinKVNEKNLTLKEVFRLATLGGSQALGLdSEIGNF 389
Cdd:PRK15493 285 GIANVKAMLEAGIKVGIATDsVASNNNLDMFEEMRIATLLQKGI---HQDATALPVETALTLATKGAAEVIGM-KQTGSL 360
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 6753960 390 EVGKEFDALLINPraSDSPidlfygdfVGDISEAVIQKFLYLGDDRNIEEVYVGGKQVV 448
Cdd:PRK15493 361 EVGKCADFITIDP--SNKP--------HLQPADEVLSHLVYAASGKDISDVIINGKRVV 409
|
|
| PRK06380 |
PRK06380 |
metal-dependent hydrolase; Provisional |
75-445 |
1.33e-24 |
|
metal-dependent hydrolase; Provisional
Pssm-ID: 180548 [Multi-domain] Cd Length: 418 Bit Score: 105.35 E-value: 1.33e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753960 75 MPGLVDTHIHAPQYAFAGSNVDLPLLEWLNKyTFpteqRFRSTDVAEEVYTRV---VRRTLKNGTTTacyFGTIHTDSSL 151
Cdd:PRK06380 53 MPGLINTHAHVGMTASKGLFDDVDLEEFLMK-TF----KYDSKRTREGIYNSAklgMYEMINSGITA---FVDLYYSEDI 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753960 152 IlAEITDKFGQRAFVGKVCMDlndtvPEYKETTEESVKETERFVSEMLQKNYprVKPIVTPRFTLSCTETLMSELGNIAK 231
Cdd:PRK06380 125 I-AKAAEELGIRAFLSWAVLD-----EEITTQKGDPLNNAENFIREHRNEEL--VTPSIGVQGIYVANDETYLKAKEIAE 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753960 232 THDLYIQSHISENREEIeavkslYPSYKNY----TDVYDKNNLLTNKTVMAHGCYLSEEELNIFSERGASIAHCPNSNLS 307
Cdd:PRK06380 197 KYDTIMHMHLSETRKEV------YDHVKRTgerpVEHLEKIGFLNSKLIAAHCVWATYHEIKLLSKNGVKVSWNSVSNFK 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753960 308 LSSGLLNVL-EVLKHKVKIGLGTDVAGG-YSYSMLDAIR-RAVMVSNvlliNKVNEKNLTLKEVFRLATLGGSQALGLDS 384
Cdd:PRK06380 271 LGTGGSPPIpEMLDNGINVTIGTDSNGSnNSLDMFEAMKfSALSVKN----ERWDASIIKAQEILDFATINAAKALELNA 346
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6753960 385 eiGNFEVGKEFDALLINPRASdSPIDLFYGDFVGDIseaviqkfLYLGDDRNIEEVYVGGK 445
Cdd:PRK06380 347 --GSIEVGKLADLVILDARAP-NMIPTRKNNIVSNI--------VYSLNPLNVDHVIVNGK 396
|
|
| PRK08203 |
PRK08203 |
hydroxydechloroatrazine ethylaminohydrolase; Reviewed |
75-448 |
2.58e-19 |
|
hydroxydechloroatrazine ethylaminohydrolase; Reviewed
Pssm-ID: 236184 [Multi-domain] Cd Length: 451 Bit Score: 89.91 E-value: 2.58e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753960 75 MPGLVDTHIHAPQY---AFAGSnVDLPLLEWLnKYTFPTEQRFrsTDVAEEVYTRV-VRRTLKNGTTTAC---Y-FGTIH 146
Cdd:PRK08203 58 TPGLVNTHHHFYQTltrALPAA-QDAELFPWL-TTLYPVWARL--TPEMVRVATQTaLAELLLSGCTTSSdhhYlFPNGL 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753960 147 TDSSLILAEITDKFGQRAFVGKVCMDLN--------DTVpeyKETTEESVKETERFVSE--------MLQknyprvkpI- 209
Cdd:PRK08203 134 RDALDDQIEAAREIGMRFHATRGSMSLGesdgglppDSV---VEDEDAILADSQRLIDRyhdpgpgaMLR--------Ia 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753960 210 VTPRFTLSCTETLMSELGNIAKTHDLYIQSHISENREEIEAVKSLY---PsyknyTDVYDKNNLLTNKTVMAHGCYLSEE 286
Cdd:PRK08203 203 LAPCSPFSVSRELMRESAALARRLGVRLHTHLAETLDEEAFCLERFgmrP-----VDYLEDLGWLGPDVWLAHCVHLDDA 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753960 287 ELNIFSERGASIAHCPNSNLSLSSGLLNVLEVLKHKVKIGLGTD-VAGGYSYSMLDAIRRAvmvsnvLLINKV--NEKNL 363
Cdd:PRK08203 278 EIARLARTGTGVAHCPCSNMRLASGIAPVRELRAAGVPVGLGVDgSASNDGSNLIGEARQA------LLLQRLryGPDAM 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753960 364 TLKEVFRLATLGGSQALGLDsEIGNFEVGKEFD-AL--LINPRASDSpidlfygdfvGDISEAviqkfLYLGDDRNIEEV 440
Cdd:PRK08203 352 TAREALEWATLGGARVLGRD-DIGSLAPGKLADlALfdLDELRFAGA----------HDPVAA-----LVLCGPPRADRV 415
|
....*...
gi 6753960 441 YVGGKQVV 448
Cdd:PRK08203 416 MVGGRWVV 423
|
|
| PRK08204 |
PRK08204 |
hypothetical protein; Provisional |
75-445 |
1.84e-18 |
|
hypothetical protein; Provisional
Pssm-ID: 181288 [Multi-domain] Cd Length: 449 Bit Score: 87.37 E-value: 1.84e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753960 75 MPGLVDTHIHAPQYAFAGSNVDLPLLEWLNKYTFPTEQRFRSTDVaeEVYTRV-VRRTLKNGTTTACYFGTI-----HTD 148
Cdd:PRK08204 56 MPGLVDTHRHTWQSVLRGIGADWTLQTYFREIHGNLGPMFRPEDV--YIANLLgALEALDAGVTTLLDWSHInnspeHAD 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753960 149 SSLI-LAEItdkfGQRA--FVGKVcmdlNDTVPEYKETTEESVKETERFVSEMLQKNYPRVK---PIVTPRFtlSCTETL 222
Cdd:PRK08204 134 AAIRgLAEA----GIRAvfAHGSP----GPSPYWPFDSVPHPREDIRRVKKRYFSSDDGLLTlglAIRGPEF--SSWEVA 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753960 223 MSELGnIAKTHDLYIQSHISenreeieavksLYPSYKNYTDV--YDKNNLLTNKTVMAHGCYLSEEELNIFSERGASIAH 300
Cdd:PRK08204 204 RADFR-LARELGLPISMHQG-----------FGPWGATPRGVeqLHDAGLLGPDLNLVHGNDLSDDELKLLADSGGSFSV 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753960 301 CPNSNLSLSSGLLNVLEVLKHKVKIGLGTDVAGGYSYSMLDAIR------RAVMVSNVLLINKV--NEKNLTLKEVFRLA 372
Cdd:PRK08204 272 TPEIEMMMGHGYPVTGRLLAHGVRPSLGVDVVTSTGGDMFTQMRfalqaeRARDNAVHLREGGMppPRLTLTARQVLEWA 351
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6753960 373 TLGGSQALGLDSEIGNFEVGKEFDALLINPRAsdspIDLFYgdfVGDISEAVIQkflyLGDDRNIEEVYVGGK 445
Cdd:PRK08204 352 TIEGARALGLEDRIGSLTPGKQADLVLIDATD----LNLAP---VHDPVGAVVQ----SAHPGNVDSVMVAGR 413
|
|
| Met_dep_hydrolase_D |
cd01312 |
Metallo-dependent hydrolases, subgroup D is part of the superfamily of metallo-dependent ... |
40-396 |
8.32e-18 |
|
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: 84.81 E-value: 8.32e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753960 40 GKIVFLEESSQQEKLAkewcfkPCEIrelshHEFF-----MPGLVDTHIHapqYAFAGSNVDL---PLLEWLNkyTFPTE 111
Cdd:cd01312 1 DKILEVGDYEKLEKRY------PGAK-----HEFFpngvlLPGLINAHTH---LEFSANVAQFtygRFRAWLL--SVINS 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753960 112 QRFRSTDVAEEVYTRVVRRTLKNGTTTAcyfGTIHTDssLILAEITDKFGQRAFVGKVCMDLNDTVPEYKETTEEsvket 191
Cdd:cd01312 65 RDELLKQPWEEAIRQGIRQMLESGTTSI---GAISSD--GSLLPALASSGLRGVFFNEVIGSNPSAIDFKGETFL----- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753960 192 ERFVSEMLQKNyPRVKPIVTPRFTLSCTETLMSELGNIAKTHDLYIQSHISENREEIEavksLYPSYKNYTDVYDKNNL- 270
Cdd:cd01312 135 ERFKRSKSFES-QLFIPAISPHAPYSVHPELAQDLIDLAKKLNLPLSTHFLESKEERE----WLEESKGWFKHFWESFLk 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753960 271 -------------------LTNKTVMAHGCYLSEEELNIFSERGASIAHCPNSNLSLSSGLLNVLEVLKHKVKIGLGTD- 330
Cdd:cd01312 210 lpkpkklataidfldmlggLGTRVSFVHCVYANLEEAEILASRGASIALCPRSNRLLNGGKLDVSELKKAGIPVSLGTDg 289
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6753960 331 VAGGYSYSMLDAIRravmvSNVLLINKVNEKNLTlKEVFRLATLGGSQALGLdsEIGNFEVGKEFD 396
Cdd:cd01312 290 LSSNISLSLLDELR-----ALLDLHPEEDLLELA-SELLLMATLGGARALGL--NNGEIEAGKRAD 347
|
|
| metallo-dependent_hydrolases |
cd01292 |
Superfamily of metallo-dependent hydrolases (also called amidohydrolase superfamily) is a ... |
78-379 |
7.02e-17 |
|
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: 80.46 E-value: 7.02e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753960 78 LVDTHIHAPQYAFAGSNVDLPLLEWLNKYTFPTEQRFRstdvaeevytRVVRRTLKNGTTTACYFGTIHTDS------SL 151
Cdd:cd01292 1 FIDTHVHLDGSALRGTRLNLELKEAEELSPEDLYEDTL----------RALEALLAGGVTTVVDMGSTPPPTttkaaiEA 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753960 152 ILAEITDKFGQRAFVGKVCMDlndtvpEYKETTEESVKETERFVSEMLQKNYPRVKPIVTPRFTLSCTETLMSELGnIAK 231
Cdd:cd01292 71 VAEAARASAGIRVVLGLGIPG------VPAAVDEDAEALLLELLRRGLELGAVGLKLAGPYTATGLSDESLRRVLE-EAR 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753960 232 THDLYIQSHISENREEIEAVKSLYpsyknytdvydKNNLLTNKTVMAHGCYLSEEELNIFSERGASIAHCPNSNLSLSSG 311
Cdd:cd01292 144 KLGLPVVIHAGELPDPTRALEDLV-----------ALLRLGGRVVIGHVSHLDPELLELLKEAGVSLEVCPLSNYLLGRD 212
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6753960 312 LLN---VLEVLKHKVKIGLGTDVAGGYSYSMLDAIRRAVMVSNVLlinkvnekNLTLKEVFRLATLGGSQA 379
Cdd:cd01292 213 GEGaeaLRRLLELGIRVTLGTDGPPHPLGTDLLALLRLLLKVLRL--------GLSLEEALRLATINPARA 275
|
|
| PRK08418 |
PRK08418 |
metal-dependent hydrolase; |
75-448 |
7.21e-17 |
|
metal-dependent hydrolase;
Pssm-ID: 181419 [Multi-domain] Cd Length: 408 Bit Score: 82.32 E-value: 7.21e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753960 75 MPGLVDTHIHapqYAFAGSNVDL---PLLEWLNKYTFPTEQRFRSTDvaEEVYTRVVRRTLKNGTTTacyFGTIhtDSSL 151
Cdd:PRK08418 57 LPAFINPHTH---LEFSANKTTLdygDFIPWLGSVINHREDLLEKCK--GALIQQAINEMLKSGVGT---IGAI--SSFG 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753960 152 ILAEITDKFGQRA-FVGKVCMDLNDTVPEYKETTEESVKETERFVSEMLqknyprvKPIVTPRFTLSCTETLMSELGNIA 230
Cdd:PRK08418 127 IDLEICAKSPLRVvFFNEILGSNASAVDELYQDFLARFEESKKFKSKKF-------IPAIAIHSPYSVHPILAKKALQLA 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753960 231 KTHDLYIQSHISENREEIEAV-------KSLYPSY-KNYTDVYDKNNLL----TNKTVMAHGCYLSEEELNIFSERGASI 298
Cdd:PRK08418 200 KKENLLVSTHFLESKAEREWLeeskgwfKKFFEKFlKEPKPLYTPKEFLelfkGLRTLFTHCVYASEEELEKIKSKNASI 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753960 299 AHCPNSNLSLSSGLLNVLEVLKHKVKIGLGTD-VAGGYSYSMLDAIRRAVMVSNvllinkvNEKNLTL-KEVFRLATLGG 376
Cdd:PRK08418 280 THCPFSNRLLSNKALDLEKAKKAGINYSIATDgLSSNISLSLLDELRAALLTHA-------NMPLLELaKILLLSATRYG 352
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6753960 377 SQALGLDSeiGNFEVGKEFDALLINprasdspidlfYGDFVGDISEAVIQKFLYlgdDRNIEEVYVGGKQVV 448
Cdd:PRK08418 353 AKALGLNN--GEIKEGKDADLSVFE-----------LPEECTKKEQLPLQFILH---AKEVKKLFIGGKEVK 408
|
|
| PRK12393 |
PRK12393 |
amidohydrolase; Provisional |
76-448 |
4.70e-14 |
|
amidohydrolase; Provisional
Pssm-ID: 237088 [Multi-domain] Cd Length: 457 Bit Score: 73.95 E-value: 4.70e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753960 76 PGLVDTHIHAPQYAFAG--SNVDLPLLEWLNKYTFP-----TEQRFRstdvaeeVYTRV-VRRTLKNGTTTAC-----YF 142
Cdd:PRK12393 59 PGWVNTHHHLFQSLLKGvpAGINQSLTAWLAAVPYRfrarfDEDLFR-------LAARIgLVELLRSGCTTVAdhhylYH 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753960 143 GTIHTDSSLILAEITDKFGQRaFVgkVC---------MDLNDTVPEYKETTEESVKETERFVSEMLQKNYPRVKPIV--- 210
Cdd:PRK12393 132 PGMPFDTGDILFDEAEALGMR-FV--LCrggatqtrgDHPGLPTALRPETLDQMLADVERLVSRYHDASPDSLRRVVvap 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753960 211 -TPRFTLscTETLMSELGNIAKTHDLYIQSHISENREEIEAVKSLYPsyKNYTDVYDKNNLLTNKTVMAHGCYLSEEELN 289
Cdd:PRK12393 209 tTPTFSL--PPELLREVARAARGMGLRLHSHLSETVDYVDFCREKYG--MTPVQFVAEHDWLGPDVWFAHLVKLDAEEIA 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753960 290 IFSERGASIAHCPNSNLSLSSGLLNVLEVLKHKVKIGLGTD-VAGGYSYSMLDAIRRAVMVSNVLlinkVNEKNLTLKEV 368
Cdd:PRK12393 285 LLAQTGTGIAHCPQSNGRLGSGIAPALAMEAAGVPVSLGVDgAASNESADMLSEAHAAWLLHRAE----GGADATTVEDV 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753960 369 FRLATLGGSQALGLDsEIGNFEVGKEFD-AL--LINPRasdspidlFYGdfVGDISEAVIQKflylGDDRNIEEVYVGGK 445
Cdd:PRK12393 361 VHWGTAGGARVLGLD-AIGTLAVGQAADlAIydLDDPR--------FFG--LHDPAIAPVAC----GGPAPVKALLVNGR 425
|
...
gi 6753960 446 QVV 448
Cdd:PRK12393 426 PVV 428
|
|
| PRK06151 |
PRK06151 |
N-ethylammeline chlorohydrolase; Provisional |
75-448 |
4.63e-13 |
|
N-ethylammeline chlorohydrolase; Provisional
Pssm-ID: 180428 [Multi-domain] Cd Length: 488 Bit Score: 70.84 E-value: 4.63e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753960 75 MPGLVDTHIHapqyafagSNVDLPLL------EWLNKYTFP---TEQRFRSTDVAEEV---YTRVVRRTLKNGTTTACYF 142
Cdd:PRK06151 56 GPGFIDLDAL--------SDLDTTILgldngpGWAKGRVWSrdyVEAGRREMYTPEELafqKRYAFAQLLRNGITTAMPI 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753960 143 GTI-------HTDSSLILAEITDKFGQRAFVGKVCM--------DLNDTVPEYKETTEESVKETERFVSEMLQKNYPRVK 207
Cdd:PRK06151 128 ASLfyrqwaeTYAEFAAAAEAAGRLGLRVYLGPAYRsggsvleaDGSLEVVFDEARGLAGLEEAIAFIKRVDGAHNGLVR 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753960 208 PIVTPRFTLSCTETLMSELGNIAKTHDLYIQSHISENREEIEAVKSLYPsyKNYTDVYDKNNLLTNKTVMAHGCYLSE-- 285
Cdd:PRK06151 208 GMLAPDRIETCTVDLLRRTAAAARELGCPVRLHCAQGVLEVETVRRLHG--TTPLEWLADVGLLGPRLLIPHATYISGsp 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753960 286 -------EELNIFSERGASIAHCPNSNLSLSSGLLNVLEVLKHKVKIGLGTDVAggysysmldairRAVMVSNV---LLI 355
Cdd:PRK06151 286 rlnysggDDLALLAEHGVSIVHCPLVSARHGSALNSFDRYREAGINLALGTDTF------------PPDMVMNMrvgLIL 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753960 356 NKVNEKNLT---LKEVFRLATLGGSQALGLDsEIGNFEVGKEFDALLINPRasdspiDLFYGDFVGDISEAVIQkflylG 432
Cdd:PRK06151 354 GRVVEGDLDaasAADLFDAATLGGARALGRD-DLGRLAPGAKADIVVFDLD------GLHMGPVFDPIRTLVTG-----G 421
|
410
....*....|....*.
gi 6753960 433 DDRNIEEVYVGGKQVV 448
Cdd:PRK06151 422 SGRDVRAVFVDGRVVM 437
|
|
| PRK07203 |
PRK07203 |
putative aminohydrolase SsnA; |
75-353 |
2.56e-12 |
|
putative aminohydrolase SsnA;
Pssm-ID: 235963 [Multi-domain] Cd Length: 442 Bit Score: 68.42 E-value: 2.56e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753960 75 MPGLVDTHIHApqY-AFA-GSNVDLP----LLEWLNKYTFpteqRFRSTDVAEEVYTRVVRRTL---KNGTTTA----CY 141
Cdd:PRK07203 58 MPGLINSHNHI--YsGLArGMMANIPpppdFISILKNLWW----RLDRALTLEDVYYSALICSLeaiKNGVTTVfdhhAS 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753960 142 FGTIhTDSSLILAEITDKFGQRafvGKVCMDLNDTVPEykETTEESVKETERFVSEMLQKNYPRVKPIVT--PRFTLScT 219
Cdd:PRK07203 132 PNYI-GGSLFTIADAAKKVGLR---AMLCYETSDRDGE--KELQEGVEENIRFIKHIDEAKDDMVEAMFGlhASFTLS-D 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753960 220 ETLmSELGNIAKTHDLYIQSHISENREEIEAvkSLYPSYKNYTDVYDKNNLLTNKTVMAHGCYLSEEELNIFSERGASIA 299
Cdd:PRK07203 205 ATL-EKCREAVKETGRGYHIHVAEGIYDVSD--SHKKYGKDIVERLADFGLLGEKTLAAHCIYLSDEEIDLLKETDTFVV 281
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 6753960 300 HCPNSNLSLSSGLLNVLEVLKHKVKIGLGTDvagGYSYSMLDAIRravmVSNVL 353
Cdd:PRK07203 282 HNPESNMGNAVGYNPVLEMIKNGILLGLGTD---GYTSDMFESYK----VANFK 328
|
|
| HutI |
COG1228 |
Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport ... |
75-448 |
1.56e-10 |
|
Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440841 [Multi-domain] Cd Length: 386 Bit Score: 62.67 E-value: 1.56e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753960 75 MPGLVDTHIHapqYAFAGSNVDlpllewlnkyTFPTEQRFRSTDVAEEVYTRVVRRTLKNGTTTACyfgtIHTDSSLILA 154
Cdd:COG1228 64 LPGLIDAHTH---LGLGGGRAV----------EFEAGGGITPTVDLVNPADKRLRRALAAGVTTVR----DLPGGPLGLR 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753960 155 EITDK------FGQRAFVGKVCMDLNDTVPEYketteeSVKETERFVSEMLQKNYPRVKPIVT---PRFTLSCTETLMSE 225
Cdd:COG1228 127 DAIIAgeskllPGPRVLAAGPALSLTGGAHAR------GPEEARAALRELLAEGADYIKVFAEggaPDFSLEELRAILEA 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753960 226 lgniAKTHDLYIQSHISENREEIEAVKSlypsyknytdvydknnlltNKTVMAHGCYLSEEELNIFSERGASI------- 298
Cdd:COG1228 201 ----AHALGLPVAAHAHQADDIRLAVEA-------------------GVDSIEHGTYLDDEVADLLAEAGTVVlvptlsl 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753960 299 --AHCPNSNLSLSSGLLNVLEV--------LKHKVKIGLGTDVAGGYS--YSMLDAIRRAVMVsnvllinkvnekNLTLK 366
Cdd:COG1228 258 flALLEGAAAPVAAKARKVREAalanarrlHDAGVPVALGTDAGVGVPpgRSLHRELALAVEA------------GLTPE 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753960 367 EVFRLATLGGSQALGLDSEIGNFEVGKEFDALLINprasdspidlfyGDFVGDISeaviqkflYLgddRNIEEVYVGGKQ 446
Cdd:COG1228 326 EALRAATINAAKALGLDDDVGSLEPGKLADLVLLD------------GDPLEDIA--------YL---EDVRAVMKDGRV 382
|
..
gi 6753960 447 VV 448
Cdd:COG1228 383 VD 384
|
|
| archeal_chlorohydrolases |
cd01305 |
Predicted chlorohydrolases. These metallo-dependent hydrolases from archea are part of the ... |
75-377 |
2.20e-09 |
|
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: 58.18 E-value: 2.20e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753960 75 MPGLVDTHIHAPQYAFAGSNVDLPLLE---WLN--KYTFPTEQRFRSTDVAEEvytRVVRRTLKNGTTTACYFGTIHTDS 149
Cdd:cd01305 3 IPALVNAHTHLGDSAIKEVGDGLPLDDlvaPPDglKHRLLAQADDRELAEAMR---KVLRDMRETGIGAFADFREGGVEG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753960 150 SLILAEITDKFgqrAFVGKVCMDlNDTVPEYKETTEEsvketerfVSEMLQKNYPRvkpivtprftlsctETLMSELGNI 229
Cdd:cd01305 80 IELLRRALGKL---PVPFEVILG-RPTEPDDPEILLE--------VADGLGLSSAN--------------DVDLEDILEL 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753960 230 AKTHDLYIQSHISENRE-----EIEAVKSLYPsyknytdvydknNLLTnktvmaHGCYLSEEELNIFSERGASIAHCPNS 304
Cdd:cd01305 134 LRRRGKLFAIHASETREsvgmtDIERALDLEP------------DLLV------HGTHLTDEDLELVRENGVPVVLCPRS 195
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6753960 305 NLSLSSGLLNVLEVLKHKVKIGLGTDVAGGYSYSMLDAIRRAVMVSNVLliNKVNEknltlKEVFRLATLGGS 377
Cdd:cd01305 196 NLYFGVGIPPVAELLKLGIKVLLGTDNVMVNEPDMWAEMEFLAKYSRLQ--GYLSP-----LEILRMATVNAA 261
|
|
| Met_dep_hydrolase_E |
cd01313 |
Metallo-dependent hydrolases, subgroup D is part of the superfamily of metallo-dependent ... |
240-445 |
1.20e-08 |
|
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: 56.70 E-value: 1.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753960 240 HISENREEIEAVksLYPSYKNYTDVYDKNNLLTNKTVMAHGCYLSEEELNIFSERGASIAHCPNSNLSLSSGLLNVLEVL 319
Cdd:cd01313 225 HLAEQPKEVDDC--LAAHGRRPVELLLDHGHLDARWCLVHATHLTDNETLLLGRSGAVVGLCPTTEANLGDGIFPAAALL 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753960 320 KHKVKIGLGTDVAGG-----------YSYSMLDAIRravmvsNVLlinkVNEKNLTLKEVFRLATLGGSQALGLDSeiGN 388
Cdd:cd01313 303 AAGGRIGIGSDSNARidlleelrqleYSQRLRDRAR------NVL----ATAGGSSARALLDAALAGGAQALGLAT--GA 370
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 6753960 389 FEVGKEFDALLInprASDSPidlfygDFVGDISEAVIQKFLYLGDDRNIEEVYVGGK 445
Cdd:cd01313 371 LEAGARADLLSL---DLDHP------SLAGALPDTLLDAWVFAAGDREVRDVVVGGR 418
|
|
| PRK07213 |
PRK07213 |
chlorohydrolase; Provisional |
240-404 |
8.32e-06 |
|
chlorohydrolase; Provisional
Pssm-ID: 235969 [Multi-domain] Cd Length: 375 Bit Score: 47.73 E-value: 8.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753960 240 HISENREEIEAVKSLYpsykNYTDVYDKNNLLTNKTVMAHGCYLSEEELNIFSERGASIAHCPNSNLSLSSGLLNVLEVL 319
Cdd:PRK07213 198 HAAEHKGSVEYSLEKY----GMTEIERLINLGFKPDFIVHATHPSNDDLELLKENNIPVVVCPRANASFNVGLPPLNEML 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753960 320 KHKVKIGLGTDVAGGYSYSM---LDAIRRAVmvsnvllinkvnekNLTLKEVFRLATLGGSQALGLDsEIGNFEVGKEFD 396
Cdd:PRK07213 274 EKGILLGIGTDNFMANSPSIfreMEFIYKLY--------------HIEPKEILKMATINGAKILGLI-NVGLIEEGFKAD 338
|
....*...
gi 6753960 397 ALLINPRA 404
Cdd:PRK07213 339 FTFIKPTN 346
|
|
| Amidohydro_3 |
pfam07969 |
Amidohydrolase family; |
315-448 |
9.40e-06 |
|
Amidohydrolase family;
Pssm-ID: 400360 [Multi-domain] Cd Length: 464 Bit Score: 47.91 E-value: 9.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753960 315 VLEVLKHKVKIGLGTDVAGGySYSMLDAIRRAVM-----VSNVLLINKVneknLTLKEVFRLATLGGSQALGLDSEIGNF 389
Cdd:pfam07969 351 VKELLNAGVKVALGSDAPVG-PFDPWPRIGAAVMrqtagGGEVLGPDEE----LSLEEALALYTSGPAKALGLEDRKGTL 425
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 6753960 390 EVGKEFDALLINprasdspIDLFygdfvgDISEAVIqkflylgDDRNIEEVYVGGKQVV 448
Cdd:pfam07969 426 GVGKDADLVVLD-------DDPL------TVDPPAI-------ADIRVRLTVVDGRVVY 464
|
|
| Imidazolone-5PH |
cd01296 |
Imidazolonepropionase/imidazolone-5-propionate hydrolase (Imidazolone-5PH) catalyzes the third ... |
277-427 |
6.78e-04 |
|
Imidazolonepropionase/imidazolone-5-propionate hydrolase (Imidazolone-5PH) catalyzes the third step in the histidine degradation pathway, the hydrolysis of (S)-3-(5-oxo-4,5-dihydro-3H-imidazol-4-yl)propanoate to N-formimidoyl-L-glutamate. In bacteria, the enzyme is part of histidine utilization (hut) operon.
Pssm-ID: 238621 [Multi-domain] Cd Length: 371 Bit Score: 41.86 E-value: 6.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753960 277 MAHGCYLSEEELNIFSERGASIAHCPNSNLSLSSGLLNVLEVLKHKVKIGLGTDVAGGySY---SMLDAIRRAVmvsnvl 353
Cdd:cd01296 233 ADHLEHTSDEGIAALAEAGTVAVLLPGTAFSLRETYPPARKLIDAGVPVALGTDFNPG-SSptsSMPLVMHLAC------ 305
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6753960 354 linkVNEKnLTLKEVFRLATLGGSQALGLDSEIGNFEVGKEFDALLINpraSDSPIDLFYgDFVGDISEAVIQK 427
Cdd:cd01296 306 ----RLMR-MTPEEALTAATINAAAALGLGETVGSLEVGKQADLVILD---APSYEHLAY-RFGVNLVEYVIKN 370
|
|
| nagA |
PRK11170 |
N-acetylglucosamine-6-phosphate deacetylase; Provisional |
333-393 |
3.21e-03 |
|
N-acetylglucosamine-6-phosphate deacetylase; Provisional
Pssm-ID: 183010 Cd Length: 382 Bit Score: 39.57 E-value: 3.21e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6753960 333 GGYSYSMLDAIRravmvsnvlliNKVNEKNLTLKEVFRLATLGGSQALGLDSEIGNFEVGK 393
Cdd:PRK11170 307 SGSALTMIEAVR-----------NLVEHVGIALDEALRMATLYPARAIGVDKRLGSIEAGK 356
|
|
| Met_dep_hydrolase_A |
cd01299 |
Metallo-dependent hydrolases, subgroup A is part of the superfamily of metallo-dependent ... |
320-404 |
4.99e-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: 38.81 E-value: 4.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753960 320 KHKVKIGLGTD-----VAGGYSYSMLdairrAVMVsnvllinkvnEKNLTLKEVFRLATLGGSQALGLDSEIGNFEVGKE 394
Cdd:cd01299 261 KAGVKIAFGTDagfpvPPHGWNAREL-----ELLV----------KAGGTPAEALRAATANAAELLGLSDELGVIEAGKL 325
|
90
....*....|..
gi 6753960 395 FDALLI--NPRA 404
Cdd:cd01299 326 ADLLVVdgDPLE 337
|
|
| PRK09229 |
PRK09229 |
N-formimino-L-glutamate deiminase; Validated |
369-448 |
9.71e-03 |
|
N-formimino-L-glutamate deiminase; Validated
Pssm-ID: 236420 [Multi-domain] Cd Length: 456 Bit Score: 38.29 E-value: 9.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6753960 369 FRLATLGGSQALGLDseIGNFEVGKEFDALLINPrasDSPidlfygDFVGDISEAVIQKFLYLGDDRNIEEVYVGGKQVV 448
Cdd:PRK09229 363 FDAALAGGAQALGRA--IGGLAVGARADLVVLDL---DHP------ALAGREGDALLDRWVFAGGDAAVRDVWVAGRWVV 431
|
|
| |
