|
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 4731644 13 FRGTFVHSTWTCPMEvLRDHLLGVSDSGKIVFLEESSQQEKLAKEW--CFKPCEIRELSHHEFFMPGLVDTHIHAPQYAF 90
Cdd:cd01303 1 FRGTFIHTKSLPELE-LVEDALRVVEDGLIVVVDGNIIAAGAAETLkrAAKPGARVIDSPNQFILPGFIDTHIHAPQYAN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4731644 91 AGSNVDLPLLDWLNKYTFPTEKRFQSTDVAEEVYTRVVRRTLKNGTTTACYFGTIHTDSSLILAEITDKFGQRAFVGKVC 170
Cdd:cd01303 80 IGSGLGEPLLDWLETYTFPEEAKFADPAYAREVYGRFLDELLRNGTTTACYFATIHPESTEALFEEAAKRGQRAIAGKVC 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4731644 171 MDLNNtvPEYK-ETTEESVKETERFVSEMLQKnYSRVKPIVTPRFSLSCTETLMSELGNIAKTH-DLYIQSHISENREEI 248
Cdd:cd01303 160 MDRNA--PEYYrDTAESSYRDTKRLIERWHGK-SGRVKPAITPRFAPSCSEELLAALGKLAKEHpDLHIQTHISENLDEI 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4731644 249 EAVKSLYPGYKNYTDVYDKNNLLTNKTVMAHGCYLSEEELNVFSERGASIAHCPNSNLSLSSGLLNVLDVLKHKVKIGLG 328
Cdd:cd01303 237 AWVKELFPGARDYLDVYDKYGLLTEKTVLAHCVHLSEEEFNLLKERGASVAHCPTSNLFLGSGLFDVRKLLDAGIKVGLG 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4731644 329 TDVAGGYSYSMLDAIRRAVMVSNVLLINKVNEKSLTLKEVFRLATLGGSQALGLDREIGNFEVGKDFDALLINPRASDSP 408
Cdd:cd01303 317 TDVGGGTSFSMLDTLRQAYKVSRLLGYELGGHAKLSPAEAFYLATLGGAEALGLDDKIGNFEVGKEFDAVVIDPSATPLL 396
|
410 420 430
....*....|....*....|....*....|....*.
gi 4731644 409 IDLfcgDFVGDISEAVIQKFLYLGDDRNIEEVYVGG 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: 535.30 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4731644 26 MEVLRDHLLGVSDsGKIVFLEESSQQeklaKEWCFKPCEIRELSHHeFFMPGLVDTHIHAPQYAFAGSnVDLPLLDWLNK 105
Cdd:TIGR02967 1 LEYFEDGLLVVEN-GRIVAVGDYAEL----KETLPAGVEIDDYRGH-LIMPGFIDTHIHYPQTEMIAS-YGEQLLEWLEK 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4731644 106 YTFPTEKRFQSTDVAEEVYTRVVRRTLKNGTTTACYFGTIHTDSSLILAEITDKFGQRAFVGKVCMDLNntVPEY-KETT 184
Cdd:TIGR02967 74 YTFPTEARFADPDHAEEVAEFFLDELLRNGTTTALVFATVHPESVDALFEAALKRGMRMIAGKVLMDRN--APDYlRDTA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4731644 185 EESVKETERFVSEMLQKNysRVKPIVTPRFSLSCTETLMSELGNIAKTH-DLYIQSHISENREEIEAVKSLYPGYKNYTD 263
Cdd:TIGR02967 152 ESSYDESKALIERWHGKG--RLLYAVTPRFAPTSSPEQLAAAGELAKEYpDVYVQTHLSENKDEIAWVKELFPEAKDYLD 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4731644 264 VYDKNNLLTNKTVMAHGCYLSEEELNVFSERGASIAHCPNSNLSLSSGLLNVLDVLKHKVKIGLGTDVAGGYSYSMLDAI 343
Cdd:TIGR02967 230 VYDHYGLLGRRSVFAHCIHLSDEECQRLAETGAAIAHCPTSNLFLGSGLFNLKKALEHGVRVGLGTDVGGGTSFSMLQTL 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4731644 344 RRAVMVSNVLlinkvnEKSLTLKEVFRLATLGGSQALGLDREIGNFEVGKDFDALLINPRASDSPIDLFCGdfvGDISEA 423
Cdd:TIGR02967 310 REAYKVSQLQ------GARLSPFEAFYLATLGGARALDLDDRIGNFEPGKEADFVVLDPAATPLLALRFEG---ADTLED 380
|
410 420
....*....|....*....|.
gi 4731644 424 VIQKFLYLGDDRNIEEVYVGG 444
Cdd:TIGR02967 381 KLFKLMYLGDDRNVAETYVAG 401
|
|
| SsnA |
COG0402 |
Cytosine/adenosine deaminase or related metal-dependent hydrolase [Nucleotide transport and ... |
11-448 |
7.79e-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: 7.79e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4731644 11 LIFRGTFVHsTWTCPMEVLRDHLLGVSDsGKIVFLEESSQQEKLakewcFKPCEIRELSHHeFFMPGLVDTHIHAPQYAF 90
Cdd:COG0402 2 LLIRGAWVL-TMDPAGGVLEDGAVLVED-GRIAAVGPGAELPAR-----YPAAEVIDAGGK-LVLPGLVNTHTHLPQTLL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4731644 91 AGSNVDLPLLDWLNKYTFPTEKRFqSTDVAEEVYTRVVRRTLKNGTTTACYFGTIHTDSSLILAEITDKFGQRAFVGKVC 170
Cdd:COG0402 74 RGLADDLPLLDWLEEYIWPLEARL-DPEDVYAGALLALAEMLRSGTTTVADFYYVHPESADALAEAAAEAGIRAVLGRGL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4731644 171 MDLNnTVPEYKETTEESVKETERFVSEMLQKNYSRVKPIVTPRFSLSCTETLMSELGNIAKTHDLYIQSHISENREEIEA 250
Cdd:COG0402 153 MDRG-FPDGLREDADEGLADSERLIERWHGAADGRIRVALAPHAPYTVSPELLRAAAALARELGLPLHTHLAETRDEVEW 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4731644 251 VKSLYPgyKNYTDVYDKNNLLTNKTVMAHGCYLSEEELNVFSERGASIAHCPNSNLSLSSGLLNVLDVLKHKVKIGLGTD 330
Cdd:COG0402 232 VLELYG--KRPVEYLDELGLLGPRTLLAHCVHLTDEEIALLAETGASVAHCPTSNLKLGSGIAPVPRLLAAGVRVGLGTD 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4731644 331 VAGG-YSYSMLDAIRRAVMVSNVLlinKVNEKSLTLKEVFRLATLGGSQALGLDREIGNFEVGKDFDALLINPRASD-SP 408
Cdd:COG0402 310 GAASnNSLDMFEEMRLAALLQRLR---GGDPTALSAREALEMATLGGARALGLDDEIGSLEPGKRADLVVLDLDAPHlAP 386
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 4731644 409 IDlfcgdfvgdiseAVIQKFLYLGDDRNIEEVYVGGKQVV 448
Cdd:COG0402 387 LH------------DPLSALVYAADGRDVRTVWVAGRVVV 414
|
|
| PRK09228 |
PRK09228 |
guanine deaminase; Provisional |
64-447 |
7.20e-104 |
|
guanine deaminase; Provisional
Pssm-ID: 236419 [Multi-domain] Cd Length: 433 Bit Score: 315.98 E-value: 7.20e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4731644 64 EIRELSHHeFFMPGLVDTHIHAPQYAFAGSNVDlPLLDWLNKYTFPTEKRFQSTDVAEEVYTRVVRRTLKNGTTTACYFG 143
Cdd:PRK09228 59 EVTDYRGK-LILPGFIDTHIHYPQTDMIASYGE-QLLDWLNTYTFPEERRFADPAYAREVAEFFLDELLRNGTTTALVFG 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4731644 144 TIHTDSSLILAEITDKFGQRAFVGKVCMDLNntVPEY-KETTEESVKETERfvseMLQK--NYSRVKPIVTPRFSLSCTE 220
Cdd:PRK09228 137 TVHPQSVDALFEAAEARNMRMIAGKVLMDRN--APDGlRDTAESGYDDSKA----LIERwhGKGRLLYAITPRFAPTSTP 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4731644 221 TLMSELGNIAKTH-DLYIQSHISENREEIEAVKSLYPGYKNYTDVYDKNNLLTNKTVMAHGCYLSEEELNVFSERGASIA 299
Cdd:PRK09228 211 EQLEAAGALAREHpDVWIQTHLSENLDEIAWVKELFPEARDYLDVYERYGLLGPRAVFAHCIHLEDRERRRLAETGAAIA 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4731644 300 HCPNSNLSLSSGLLNVLDVLKHKVKIGLGTDVAGGYSYSMLDAIRRAVMVSnvllinKVNEKSLTLKEVFRLATLGGSQA 379
Cdd:PRK09228 291 FCPTSNLFLGSGLFDLKRADAAGVRVGLGTDVGGGTSFSMLQTMNEAYKVQ------QLQGYRLSPFQAFYLATLGGARA 364
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 4731644 380 LGLDREIGNFEVGKDFDALLINPRASdSPIDLFCgDFVGDISEAVIQKFLyLGDDRNIEEVYVGGKQV 447
Cdd:PRK09228 365 LGLDDRIGNLAPGKEADFVVLDPAAT-PLLALRT-ARAESLEELLFALMT-LGDDRAVAETYVAGRPV 429
|
|
| ATZ_TRZ_like |
cd01298 |
TRZ/ATZ family contains enzymes from the atrazine degradation pathway and related hydrolases. ... |
75-448 |
2.00e-61 |
|
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: 205.13 E-value: 2.00e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4731644 75 MPGLVDTHIHAPQYAFAGSNVDLPLLDWLNKYTFPTEKRFqstdVAEEVY--TRV-VRRTLKNGTTTACYFGTIHTDssl 151
Cdd:cd01298 55 MPGLVNTHTHLAMTLLRGLADDLPLMEWLKDLIWPLERLL----TEEDVYlgALLaLAEMIRSGTTTFADMYFFYPD--- 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4731644 152 ILAEITDKFGQRAFVGKVCMDLNNTVPEykeTTEESVKETERFVSEMLQKNYSRVKPIVTPRFSLSCTETLMSELGNIAK 231
Cdd:cd01298 128 AVAEAAEELGIRAVLGRGIMDLGTEDVE---ETEEALAEAERLIREWHGAADGRIRVALAPHAPYTCSDELLREVAELAR 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4731644 232 THDLYIQSHISENREEIEAVKSLYpGyKNYTDVYDKNNLLTNKTVMAHGCYLSEEELNVFSERGASIAHCPNSNLSLSSG 311
Cdd:cd01298 205 EYGVPLHIHLAETEDEVEESLEKY-G-KRPVEYLEELGLLGPDVVLAHCVWLTDEEIELLAETGTGVAHNPASNMKLASG 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4731644 312 LLNVLDVLKHKVKIGLGTD-VAGGYSYSMLDAIRRAvmvsnvLLINKV---NEKSLTLKEVFRLATLGGSQALGLDrEIG 387
Cdd:cd01298 283 IAPVPEMLEAGVNVGLGTDgAASNNNLDMFEEMRLA------ALLQKLahgDPTALPAEEALEMATIGGAKALGLD-EIG 355
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 4731644 388 NFEVGKDFDALLINPRASD-SPIDlfcgdfvGDISEAViqkflYLGDDRNIEEVYVGGKQVV 448
Cdd:cd01298 356 SLEVGKKADLILIDLDGPHlLPVH-------DPISHLV-----YSANGGDVDTVIVNGRVVM 405
|
|
| PRK07228 |
PRK07228 |
5'-deoxyadenosine deaminase; |
75-401 |
1.42e-58 |
|
5'-deoxyadenosine deaminase;
Pssm-ID: 180895 [Multi-domain] Cd Length: 445 Bit Score: 198.69 E-value: 1.42e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4731644 75 MPGLVDTHIHAPQYAFAGSNVDLPLLDWLNKYTFPTEKrfqSTDvAEEVYTRV---VRRTLKNGTTTACYFGTI-HTDSS 150
Cdd:PRK07228 55 IPGLIQGHIHLCQTLFRGIADDLELLDWLKDRIWPLEA---AHD-AESMYYSAllgIGELIESGTTTIVDMESVhHTDSA 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4731644 151 LilaEITDKFGQRAFVGKVCMDLNNTVPE-YKETTEESVKETERFVSEMLQKNYSRVKPIVTPRFSLSCTETLMSELGNI 229
Cdd:PRK07228 131 F---EAAGESGIRAVLGKVMMDYGDDVPEgLQEDTEASLAESVRLLEKWHGADNGRIRYAFTPRFAVSCTEELLRGVRDL 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4731644 230 AKTHDLYIQSHISENREEIEAVKSlYPGYKNYTdVYDKNNLLTNKTVMAHGCYLSEEELNVFSERGASIAHCPNSNLSLS 309
Cdd:PRK07228 208 ADEYGVRIHTHASENRGEIETVEE-ETGMRNIH-YLDEVGLTGEDLILAHCVWLDEEEREILAETGTHVTHCPSSNLKLA 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4731644 310 SGLLNVLDVLKHKVKIGLGTDvaGGYSYSMLDA---IRRAVmvsnvlLINKVNE---KSLTLKEVFRLATLGGSQALGLD 383
Cdd:PRK07228 286 SGIAPVPDLLERGINVALGAD--GAPCNNTLDPfteMRQAA------LIQKVDRlgpTAMPARTVFEMATLGGAKAAGFE 357
|
330
....*....|....*...
gi 4731644 384 REIGNFEVGKDFDALLIN 401
Cdd:PRK07228 358 DEIGSLEEGKKADLAILD 375
|
|
| Amidohydro_1 |
pfam01979 |
Amidohydrolase family; This family of enzymes are a a large metal dependent hydrolase ... |
75-447 |
2.74e-52 |
|
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: 179.23 E-value: 2.74e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4731644 75 MPGLVDTHIHAPQYAFAGSNVDLplldwlnkytfptekrfqstDVAEEVYTRVVRRTLKNGTTTACYFGTIHTDSSLILA 154
Cdd:pfam01979 3 LPGLIDAHVHLEMGLLRGIPVPP--------------------EFAYEALRLGITTMLKSGTTTVLDMGATTSTGIEALL 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4731644 155 EITDK--FGQRAFVGKVCMDLNntvpeykETTEESVKETERFVSEM---LQKNYSRVKPIVTPRFSLSCTETLMSELGNI 229
Cdd:pfam01979 63 EAAEElpLGLRFLGPGCSLDTD-------GELEGRKALREKLKAGAefiKGMADGVVFVGLAPHGAPTFSDDELKAALEE 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4731644 230 AKTHDLYIQSHISENREEIEAVKSLYPG---YKNYTDVYDKNNLL-TNKTVMAHGCYLSEEELNVFSER--GASIAHCPN 303
Cdd:pfam01979 136 AKKYGLPVAIHALETKGEVEDAIAAFGGgieHGTHLEVAESGGLLdIIKLILAHGVHLSPTEANLLAEHlkGAGVAHCPF 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4731644 304 SNLSLSSGLLNVLDVLKHKVKIGLGTDVAG-GYSYSMLDAIRRAVmvsnvlLINKVNEKSLTLKEVFRLATLGGSQALGL 382
Cdd:pfam01979 216 SNSKLRSGRIALRKALEDGVKVGLGTDGAGsGNSLNMLEELRLAL------ELQFDPEGGLSPLEALRMATINPAKALGL 289
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 4731644 383 DREIGNFEVGKDFDALLINPRasdspidlfcgdfvgdiseaVIQKFLYLGDDRNIEEVYVGGKQV 447
Cdd:pfam01979 290 DDKVGSIEVGKDADLVVVDLD--------------------PLAAFFGLKPDGNVKKVIVKGKIV 334
|
|
| PRK08393 |
PRK08393 |
N-ethylammeline chlorohydrolase; Provisional |
71-382 |
5.45e-44 |
|
N-ethylammeline chlorohydrolase; Provisional
Pssm-ID: 181411 [Multi-domain] Cd Length: 424 Bit Score: 159.20 E-value: 5.45e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4731644 71 HEFFMPGLVDTHIHAPQYAFAGSNVDLPLLDWLNKYTFPTEKRFQSTDVAEEVYTRVVRrTLKNGTTTAC--YFgtiHTD 148
Cdd:PRK08393 49 GSVVSPGFINAHTHSPMVLLRGLADDVPLMEWLQNYIWPRERKLKRKDIYWGAYLGLLE-MIKSGTTTFVdmYF---HME 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4731644 149 SsliLAEITDKFGQRAFVGKVCMDLNNtvpeyKETTEESVKETERFVSEMLQKNYSRVKPIVTPRFSLSCTETLMSELGN 228
Cdd:PRK08393 125 E---VAKATLEVGLRGYLSYGMVDLGD-----EEKREKEIKETEKLMEFIEKLNSPRVHFVFGPHAPYTCSLALLKWVRE 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4731644 229 IAKTHDLYIQSHISENREEIEAVKSLYPgyKNYTDVYDKNNLLTNKTVMAHGCYLSEEELNVFSERGASIAHCPNSNLSL 308
Cdd:PRK08393 197 KAREWNKLITIHLSETMDEIKQIREKYG--KSPVVLLDEIGFLNEDVIAAHGVWLSSRDIRILASAGVTVAHNPASNMKL 274
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 4731644 309 SSGLLNVLDVLKHKVKIGLGTDvaGGYSYSMLDAIRRAVMVSnvlLINKVNEKSLTL---KEVFRLATLGGSQALGL 382
Cdd:PRK08393 275 GSGVMPLRKLLNAGVNVALGTD--GAASNNNLDMLREMKLAA---LLHKVHNLDPTIadaETVFRMATQNGAKALGL 346
|
|
| PRK09045 |
PRK09045 |
TRZ/ATZ family hydrolase; |
16-402 |
3.44e-37 |
|
TRZ/ATZ family hydrolase;
Pssm-ID: 236366 [Multi-domain] Cd Length: 443 Bit Score: 141.20 E-value: 3.44e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4731644 16 TFVHSTWTCPME----VLRDHLLGVSDsGKIVFLeeSSQQEKLAKewcFKPCEIRELSHHeFFMPGLVDTHIHAPQYAFA 91
Cdd:PRK09045 9 LLIEARWIVPVEpagvVLEDHAVAIRD-GRIVAI--LPRAEARAR---YAAAETVELPDH-VLIPGLINAHTHAAMSLLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4731644 92 GSNVDLPLLDWLNKYTFPTEKRFQSTD---------VAEevytrvvrrTLKNGTTTA--CYFgtiHTDsslILAEITDKF 160
Cdd:PRK09045 82 GLADDLPLMTWLQDHIWPAEGAWVSEEfvrdgtllaIAE---------MLRGGTTCFndMYF---FPE---AAAEAAHQA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4731644 161 GQRAFVGKVCMDlnntVP-EYKETTEES----VKETERFvsemlqKNYSRVKPIVTPRFSLSCTETLMSELGNIAKTHDL 235
Cdd:PRK09045 147 GMRAQIGMPVLD----FPtAWASDADEYlakgLELHDQW------RHHPLISTAFAPHAPYTVSDENLERIRTLAEQLDL 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4731644 236 YIQSHISENREEIE-AVKS--------LypgyknytdvyDKNNLLTNKTVMAHGCYLSEEELNVFSERGASIAHCPNSNL 306
Cdd:PRK09045 217 PIHIHLHETAQEIAdSLKQhgqrplarL-----------ARLGLLGPRLIAVHMTQLTDAEIALLAETGCSVVHCPESNL 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4731644 307 SLSSGLLNVLDVLKHKVKIGLGTD-VAGGYSYSMLDAIRRAVMVSNVLlinKVNEKSLTLKEVFRLATLGGSQALGLDRE 385
Cdd:PRK09045 286 KLASGFCPVAKLLQAGVNVALGTDgAASNNDLDLFGEMRTAALLAKAV---AGDATALPAHTALRMATLNGARALGLDDE 362
|
410 420
....*....|....*....|....
gi 4731644 386 IGNFEVGK-------DFDALLINP 402
Cdd:PRK09045 363 IGSLEPGKqadlvavDLSGLETQP 386
|
|
| PRK06038 |
PRK06038 |
N-ethylammeline chlorohydrolase; Provisional |
70-403 |
9.45e-37 |
|
N-ethylammeline chlorohydrolase; Provisional
Pssm-ID: 180363 [Multi-domain] Cd Length: 430 Bit Score: 139.89 E-value: 9.45e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4731644 70 HHEFFMPGLVDTHIHAPQYAFAGSNVDLPLLDWLNKYTFPTEKRFQstdvAEEVYTRVVRRTL---KNGTTT--ACYFGT 144
Cdd:PRK06038 49 KGSVVMPGLVNTHTHAAMTLFRGYADDLPLAEWLNDHIWPAEAKLT----AEDVYAGSLLACLemiKSGTTSfaDMYFYM 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4731644 145 IHTdsslilAEITDKFGQRAFVGKVCMDLNNTvpeykETTEESVKETERFVSEMLQKNYSRVKPIVTPRFSLSCTETLMS 224
Cdd:PRK06038 125 DEV------AKAVEESGLRAALSYGMIDLGDD-----EKGEAELKEGKRFVKEWHGAADGRIKVMYGPHAPYTCSEEFLS 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4731644 225 ELGNIAKTHDLYIQSHISENREEIEAVKSLYPgyKNYTDVYDKNNLLTNKTVMAHGCYLSEEELNVFSERGASIAHCPNS 304
Cdd:PRK06038 194 KVKKLANKDGVGIHIHVLETEAELNQMKEQYG--MCSVNYLDDIGFLGPDVLAAHCVWLSDGDIEILRERGVNVSHNPVS 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4731644 305 NLSLSSGLLNVLDVLKHKVKIGLGTD-VAGGYSYSMLDAIRRAVMVSNVlliNKVNEKSLTLKEVFRLATLGGSQALGLd 383
Cdd:PRK06038 272 NMKLASGIAPVPKLLERGVNVSLGTDgCASNNNLDMFEEMKTAALLHKV---NTMDPTALPARQVLEMATVNGAKALGI- 347
|
330 340
....*....|....*....|
gi 4731644 384 rEIGNFEVGKDFDALLINPR 403
Cdd:PRK06038 348 -NTGMLKEGYLADIIIVDMN 366
|
|
| PRK06687 |
PRK06687 |
TRZ/ATZ family protein; |
23-448 |
7.43e-36 |
|
TRZ/ATZ family protein;
Pssm-ID: 180657 [Multi-domain] Cd Length: 419 Bit Score: 137.06 E-value: 7.43e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4731644 23 TC--PMEVLRDHLLGVSDSgKIV--------FLEESSQQEKLAKEWcfkpceirelshhefFMPGLVDTHIHAPQYAFAG 92
Cdd:PRK06687 11 TCdqDFHVYLDGILAVKDS-QIVyvgqdkpaFLEQAEQIIDYQGAW---------------IMPGLVNCHTHSAMTGLRG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4731644 93 SNVDLPLLDWLNKYTFPTEKRFqSTDVAEEVYTRVVRRTLKNGTTTacyFGTIHTDSSLILAEITDKFGQRafvGKVCMD 172
Cdd:PRK06687 75 IRDDSNLHEWLNDYIWPAESEF-TPDMTTNAVKEALTEMLQSGTTT---FNDMYNPNGVDIQQIYQVVKTS---KMRCYF 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4731644 173 LNNTVPEYKETTEESVKETERFVSEMLQKNYSRVKPIVTPRFSLSCTETLMSELGNIAKTHDLYIQSHISENREEIEAVK 252
Cdd:PRK06687 148 SPTLFSSETETTAETISRTRSIIDEILKYKNPNFKVMVAPHSPYSCSRDLLEASLEMAKELNIPLHVHVAETKEESGIIL 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4731644 253 SLYPgyKNYTDVYDKNNLLTNKTVMAHGCYLSEEELNVFSERGASIAHCPNSNLSLSSGLLNVLDVLKHKVKIGLGTD-V 331
Cdd:PRK06687 228 KRYG--KRPLAFLEELGYLDHPSVFAHGVELNEREIERLASSQVAIAHNPISNLKLASGIAPIIQLQKAGVAVGIATDsV 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4731644 332 AGGYSYSMLDAIRRAVMVSNvllINKVNEKSLTLKEVFRLATLGGSQALGLDREIGNFEVGKDFDALLINPRASdspIDL 411
Cdd:PRK06687 306 ASNNNLDMFEEGRTAALLQK---MKSGDASQFPIETALKVLTIEGAKALGMENQIGSLEVGKQADFLVIQPQGK---IHL 379
|
410 420 430
....*....|....*....|....*....|....*..
gi 4731644 412 FcgdfvgdISEAVIQKFLYLGDDRNIEEVYVGGKQVV 448
Cdd:PRK06687 380 Q-------PQENMLSHLVYAVKSSDVDDVYIAGEQVV 409
|
|
| PRK15493 |
PRK15493 |
bifunctional S-methyl-5'-thioadenosine deaminase/S-adenosylhomocysteine deaminase; |
72-448 |
7.85e-29 |
|
bifunctional S-methyl-5'-thioadenosine deaminase/S-adenosylhomocysteine deaminase;
Pssm-ID: 185390 [Multi-domain] Cd Length: 435 Bit Score: 117.85 E-value: 7.85e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4731644 72 EFFMPGLVDTHIHAPQYAFAGSNVDLPLLDWLNKYTFPTEKRFqSTDVAEEVYTRVVRRTLKNGTTT-ACYFGTIHTDSS 150
Cdd:PRK15493 55 KWVLPGLVNTHTHVVMSLLRGIGDDMLLQPWLETRIWPLESQF-TPELAVASTELGLLEMVKSGTTSfSDMFNPIGVDQD 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4731644 151 LILaEITDKFGQRAFVGKVCMDLNNtvpeyKETTEESVKETERFVSEMLQKNySRVKPIVTPRFSLSCTETLMSELGNIA 230
Cdd:PRK15493 134 AIM-ETVSRSGMRAAVSRTLFSFGT-----KEDEKKAIEEAEKYVKRYYNES-GMLTTMVAPHSPYTCSTELLEECARIA 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4731644 231 KTHDLYIQSHISENREEIEAVKSLYPgyKNYTDVYDKNNLLTNKTVMAHGCYLSEEELNVFSERGASIAHCPNSNLSLSS 310
Cdd:PRK15493 207 VENQTMVHIHLSETEREVRDIEAQYG--KRPVEYAASCGLFKRPTVIAHGVVLNDNERAFLAEHDVRVAHNPNSNLKLGS 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4731644 311 GLLNVLDVLKHKVKIGLGTD-VAGGYSYSMLDAIRRAVMVSNVLlinKVNEKSLTLKEVFRLATLGGSQALGLdREIGNF 389
Cdd:PRK15493 285 GIANVKAMLEAGIKVGIATDsVASNNNLDMFEEMRIATLLQKGI---HQDATALPVETALTLATKGAAEVIGM-KQTGSL 360
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 4731644 390 EVGKDFDALLINPraSDSPidlfcgdfVGDISEAVIQKFLYLGDDRNIEEVYVGGKQVV 448
Cdd:PRK15493 361 EVGKCADFITIDP--SNKP--------HLQPADEVLSHLVYAASGKDISDVIINGKRVV 409
|
|
| PRK06380 |
PRK06380 |
metal-dependent hydrolase; Provisional |
75-445 |
1.23e-23 |
|
metal-dependent hydrolase; Provisional
Pssm-ID: 180548 [Multi-domain] Cd Length: 418 Bit Score: 102.27 E-value: 1.23e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4731644 75 MPGLVDTHIHAPQYAFAGSNVDLPLLDWLNKyTFptekRFQSTDVAEEVYTRV---VRRTLKNGTTTacyFGTIHTDSSL 151
Cdd:PRK06380 53 MPGLINTHAHVGMTASKGLFDDVDLEEFLMK-TF----KYDSKRTREGIYNSAklgMYEMINSGITA---FVDLYYSEDI 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4731644 152 IlAEITDKFGQRAFVGKVCMDlnntvPEYKETTEESVKETERFVSEMLQKNYsrVKPIVTPRFSLSCTETLMSELGNIAK 231
Cdd:PRK06380 125 I-AKAAEELGIRAFLSWAVLD-----EEITTQKGDPLNNAENFIREHRNEEL--VTPSIGVQGIYVANDETYLKAKEIAE 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4731644 232 THDLYIQSHISENREEI-EAVKSLypGYKNyTDVYDKNNLLTNKTVMAHGCYLSEEELNVFSERGASIAHCPNSNLSLSS 310
Cdd:PRK06380 197 KYDTIMHMHLSETRKEVyDHVKRT--GERP-VEHLEKIGFLNSKLIAAHCVWATYHEIKLLSKNGVKVSWNSVSNFKLGT 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4731644 311 GLLNVL-DVLKHKVKIGLGTDVAGG-YSYSMLDAIRRAVMVSNvlliNKVNEKSLT-LKEVFRLATLGGSQALGLDReiG 387
Cdd:PRK06380 274 GGSPPIpEMLDNGINVTIGTDSNGSnNSLDMFEAMKFSALSVK----NERWDASIIkAQEILDFATINAAKALELNA--G 347
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 4731644 388 NFEVGKDFDALLINPRASdSPIDLFCGDFVGDIseaviqkfLYLGDDRNIEEVYVGGK 445
Cdd:PRK06380 348 SIEVGKLADLVILDARAP-NMIPTRKNNIVSNI--------VYSLNPLNVDHVIVNGK 396
|
|
| PRK08203 |
PRK08203 |
hydroxydechloroatrazine ethylaminohydrolase; Reviewed |
75-448 |
2.01e-19 |
|
hydroxydechloroatrazine ethylaminohydrolase; Reviewed
Pssm-ID: 236184 [Multi-domain] Cd Length: 451 Bit Score: 90.30 E-value: 2.01e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4731644 75 MPGLVDTHIHAPQY---AFAGSnVDLPLLDWLnKYTFPTEKRFqsTDVAEEVYTRV-VRRTLKNGTTTAC---Y-FGTIH 146
Cdd:PRK08203 58 TPGLVNTHHHFYQTltrALPAA-QDAELFPWL-TTLYPVWARL--TPEMVRVATQTaLAELLLSGCTTSSdhhYlFPNGL 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4731644 147 TDSSLILAEITDKFGQRAFVGKVCMDL---------NNTVpeykETTEESVKETERFVSEMLQKN-YSRVKPIVTPRFSL 216
Cdd:PRK08203 134 RDALDDQIEAAREIGMRFHATRGSMSLgesdgglppDSVV----EDEDAILADSQRLIDRYHDPGpGAMLRIALAPCSPF 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4731644 217 SCTETLMSELGNIAKTHDLYIQSHISENREEIEAVKSLY---PgyknyTDVYDKNNLLTNKTVMAHGCYLSEEELNVFSE 293
Cdd:PRK08203 210 SVSRELMRESAALARRLGVRLHTHLAETLDEEAFCLERFgmrP-----VDYLEDLGWLGPDVWLAHCVHLDDAEIARLAR 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4731644 294 RGASIAHCPNSNLSLSSGLLNVLDVLKHKVKIGLGTD-VAGGYSYSMLDAIRRAvmvsnvLLINKV--NEKSLTLKEVFR 370
Cdd:PRK08203 285 TGTGVAHCPCSNMRLASGIAPVRELRAAGVPVGLGVDgSASNDGSNLIGEARQA------LLLQRLryGPDAMTAREALE 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4731644 371 LATLGGSQALGLDrEIGNFEVGKDFD-AL--LINPRASDSpidlfcgdfvGDISEAviqkfLYLGDDRNIEEVYVGGKQV 447
Cdd:PRK08203 359 WATLGGARVLGRD-DIGSLAPGKLADlALfdLDELRFAGA----------HDPVAA-----LVLCGPPRADRVMVGGRWV 422
|
.
gi 4731644 448 V 448
Cdd:PRK08203 423 V 423
|
|
| Met_dep_hydrolase_D |
cd01312 |
Metallo-dependent hydrolases, subgroup D is part of the superfamily of metallo-dependent ... |
40-396 |
1.84e-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: 86.73 E-value: 1.84e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4731644 40 GKIVFLEESSQQEKLAkewcfkPCEIrelshHEFF-----MPGLVDTHIHapqYAFAGSNVDL---PLLDWLNkyTFPTE 111
Cdd:cd01312 1 DKILEVGDYEKLEKRY------PGAK-----HEFFpngvlLPGLINAHTH---LEFSANVAQFtygRFRAWLL--SVINS 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4731644 112 KRFQSTDVAEEVYTRVVRRTLKNGTTTAcyfGTIHTDssLILAEITDKFGQRAFVGKVCMDLNNTVPEYKETTEEsvket 191
Cdd:cd01312 65 RDELLKQPWEEAIRQGIRQMLESGTTSI---GAISSD--GSLLPALASSGLRGVFFNEVIGSNPSAIDFKGETFL----- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4731644 192 ERFVSEMLQKNySRVKPIVTPRFSLSCTETLMSELGNIAKTHDLYIQSHISENREEIEAVKSLYPGYKNY---------- 261
Cdd:cd01312 135 ERFKRSKSFES-QLFIPAISPHAPYSVHPELAQDLIDLAKKLNLPLSTHFLESKEEREWLEESKGWFKHFwesflklpkp 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4731644 262 ------TDVYDKNNLLTNKTVMAHGCYLSEEELNVFSERGASIAHCPNSNLSLSSGLLNVLDVLKHKVKIGLGTD-VAGG 334
Cdd:cd01312 214 kklataIDFLDMLGGLGTRVSFVHCVYANLEEAEILASRGASIALCPRSNRLLNGGKLDVSELKKAGIPVSLGTDgLSSN 293
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 4731644 335 YSYSMLDAIRravmvSNVLLINKVNEKSLTlKEVFRLATLGGSQALGLdrEIGNFEVGKDFD 396
Cdd:cd01312 294 ISLSLLDELR-----ALLDLHPEEDLLELA-SELLLMATLGGARALGL--NNGEIEAGKRAD 347
|
|
| PRK08418 |
PRK08418 |
metal-dependent hydrolase; |
75-448 |
2.94e-17 |
|
metal-dependent hydrolase;
Pssm-ID: 181419 [Multi-domain] Cd Length: 408 Bit Score: 83.48 E-value: 2.94e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4731644 75 MPGLVDTHIHapqYAFAGSNVDLPLLD---WLNKYTfptEKRFQ-STDVAEEVYTRVVRRTLKNGTTTacyFGTIhtDSS 150
Cdd:PRK08418 57 LPAFINPHTH---LEFSANKTTLDYGDfipWLGSVI---NHREDlLEKCKGALIQQAINEMLKSGVGT---IGAI--SSF 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4731644 151 LILAEITDKFGQRA-FVGKVCMDLNNTVPEYKETTEESVKETERFVSEM------LQKNYSrVKPIvtprfslsctetLM 223
Cdd:PRK08418 126 GIDLEICAKSPLRVvFFNEILGSNASAVDELYQDFLARFEESKKFKSKKfipaiaIHSPYS-VHPI------------LA 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4731644 224 SELGNIAKTHDLYIQSHISENREEIEAVKSLYPGYKNY--------TDVYDKNNLL----TNKTVMAHGCYLSEEELNVF 291
Cdd:PRK08418 193 KKALQLAKKENLLVSTHFLESKAEREWLEESKGWFKKFfekflkepKPLYTPKEFLelfkGLRTLFTHCVYASEEELEKI 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4731644 292 SERGASIAHCPNSNLSLSSGLLNVLDVLKHKVKIGLGTD-VAGGYSYSMLDAIRRAVMVSNvllinkvNEKSLTL-KEVF 369
Cdd:PRK08418 273 KSKNASITHCPFSNRLLSNKALDLEKAKKAGINYSIATDgLSSNISLSLLDELRAALLTHA-------NMPLLELaKILL 345
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 4731644 370 RLATLGGSQALGLdrEIGNFEVGKDFDALLINPRASdspidlfcgdfVGDISEAVIQKFLYlgdDRNIEEVYVGGKQVV 448
Cdd:PRK08418 346 LSATRYGAKALGL--NNGEIKEGKDADLSVFELPEE-----------CTKKEQLPLQFILH---AKEVKKLFIGGKEVK 408
|
|
| metallo-dependent_hydrolases |
cd01292 |
Superfamily of metallo-dependent hydrolases (also called amidohydrolase superfamily) is a ... |
78-379 |
6.69e-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: 6.69e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4731644 78 LVDTHIHAPQYAFAGSNVDLPLLdwlnkytfptEKRFQSTDVAEEVYTRVVRRTLKNGTTTACYFGTIHTDS------SL 151
Cdd:cd01292 1 FIDTHVHLDGSALRGTRLNLELK----------EAEELSPEDLYEDTLRALEALLAGGVTTVVDMGSTPPPTttkaaiEA 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4731644 152 ILAEITDKFGQRAFVGKVCMDLNNtvpEYKETTEESVKETERFVsemlqknYSRVKPIVTPRFSLSCTETLMSELGNI-- 229
Cdd:cd01292 71 VAEAARASAGIRVVLGLGIPGVPA---AVDEDAEALLLELLRRG-------LELGAVGLKLAGPYTATGLSDESLRRVle 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4731644 230 -AKTHDLYIQSHISENREEIEAVKSLYpgyknytdvydKNNLLTNKTVMAHGCYLSEEELNVFSERGASIAHCPNSNLSL 308
Cdd:cd01292 141 eARKLGLPVVIHAGELPDPTRALEDLV-----------ALLRLGGRVVIGHVSHLDPELLELLKEAGVSLEVCPLSNYLL 209
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 4731644 309 SSGLLNVLDV---LKHKVKIGLGTDVAGGYSYSMLDAIRRAVMVSNVLLinkvneksLTLKEVFRLATLGGSQA 379
Cdd:cd01292 210 GRDGEGAEALrrlLELGIRVTLGTDGPPHPLGTDLLALLRLLLKVLRLG--------LSLEEALRLATINPARA 275
|
|
| PRK08204 |
PRK08204 |
hypothetical protein; Provisional |
75-445 |
1.65e-16 |
|
hypothetical protein; Provisional
Pssm-ID: 181288 [Multi-domain] Cd Length: 449 Bit Score: 81.20 E-value: 1.65e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4731644 75 MPGLVDTHIHAPQYAFAGSNVDLPLLDwlnkYTFPTEKRFQSTDVAEEVY--TRV-VRRTLKNGTTTACYFGTI-----H 146
Cdd:PRK08204 56 MPGLVDTHRHTWQSVLRGIGADWTLQT----YFREIHGNLGPMFRPEDVYiaNLLgALEALDAGVTTLLDWSHInnspeH 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4731644 147 TDSSLI-LAEItdkfGQRAfvgKVCMDLNNTVPEYKETTEES-VKETERFVSEMLQKNYSRVK---PIVTPRFSlsCTET 221
Cdd:PRK08204 132 ADAAIRgLAEA----GIRA---VFAHGSPGPSPYWPFDSVPHpREDIRRVKKRYFSSDDGLLTlglAIRGPEFS--SWEV 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4731644 222 LMSELGnIAKTHDLYIQSHISEnreeieavkslypGYKNYTD----VYDKNNLLTNKTVMAHGCYLSEEELNVFSERGAS 297
Cdd:PRK08204 203 ARADFR-LARELGLPISMHQGF-------------GPWGATPrgveQLHDAGLLGPDLNLVHGNDLSDDELKLLADSGGS 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4731644 298 IAHCPNSNLSLSSGLLNVLDVLKHKVKIGLGTDVAGGYSYSMLDAIR------RAVMVSNVLLINKV--NEKSLTLKEVF 369
Cdd:PRK08204 269 FSVTPEIEMMMGHGYPVTGRLLAHGVRPSLGVDVVTSTGGDMFTQMRfalqaeRARDNAVHLREGGMppPRLTLTARQVL 348
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 4731644 370 RLATLGGSQALGLDREIGNFEVGKDFDALLINPRAsdspIDLFCgdfVGDISEAVIQkflyLGDDRNIEEVYVGGK 445
Cdd:PRK08204 349 EWATIEGARALGLEDRIGSLTPGKQADLVLIDATD----LNLAP---VHDPVGAVVQ----SAHPGNVDSVMVAGR 413
|
|
| PRK12393 |
PRK12393 |
amidohydrolase; Provisional |
76-396 |
4.88e-13 |
|
amidohydrolase; Provisional
Pssm-ID: 237088 [Multi-domain] Cd Length: 457 Bit Score: 70.87 E-value: 4.88e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4731644 76 PGLVDTHIHAPQYAFAG--SNVDLPLLDWLNKYTFPTEKRFQstdvaEEVYTRVVR----RTLKNGTTTAC-----YFGT 144
Cdd:PRK12393 59 PGWVNTHHHLFQSLLKGvpAGINQSLTAWLAAVPYRFRARFD-----EDLFRLAARiglvELLRSGCTTVAdhhylYHPG 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4731644 145 IHTDSSLILAEITDKFGQRaFVgkVC---------MDLNNTVPEYKETTEESVKETERFVSEMLQKNYSRVKPIV----T 211
Cdd:PRK12393 134 MPFDTGDILFDEAEALGMR-FV--LCrggatqtrgDHPGLPTALRPETLDQMLADVERLVSRYHDASPDSLRRVVvaptT 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4731644 212 PRFSLscTETLMSELGNIAKTHDLYIQSHISENREEIEAVKSLYPgyKNYTDVYDKNNLLTNKTVMAHGCYLSEEELNVF 291
Cdd:PRK12393 211 PTFSL--PPELLREVARAARGMGLRLHSHLSETVDYVDFCREKYG--MTPVQFVAEHDWLGPDVWFAHLVKLDAEEIALL 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4731644 292 SERGASIAHCPNSNLSLSSGLLNVLDVLKHKVKIGLGTD-VAGGYSYSMLDAIRRAVMVSNVLlinkVNEKSLTLKEVFR 370
Cdd:PRK12393 287 AQTGTGIAHCPQSNGRLGSGIAPALAMEAAGVPVSLGVDgAASNESADMLSEAHAAWLLHRAE----GGADATTVEDVVH 362
|
330 340
....*....|....*....|....*.
gi 4731644 371 LATLGGSQALGLDrEIGNFEVGKDFD 396
Cdd:PRK12393 363 WGTAGGARVLGLD-AIGTLAVGQAAD 387
|
|
| HutI |
COG1228 |
Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport ... |
75-448 |
6.53e-12 |
|
Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440841 [Multi-domain] Cd Length: 386 Bit Score: 66.91 E-value: 6.53e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4731644 75 MPGLVDTHIHapqYAFAGSNVDlplldwlnkyTFPTEKRFQSTDVAEEVYTRVVRRTLKNGTTTACyfgtIHTDSSLILA 154
Cdd:COG1228 64 LPGLIDAHTH---LGLGGGRAV----------EFEAGGGITPTVDLVNPADKRLRRALAAGVTTVR----DLPGGPLGLR 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4731644 155 EITDK------FGQRAFVGKVCMDLNNTVPEYketteeSVKETERFVSEMLQKNYSRVKPIVT---PRFSLSCTETLMSE 225
Cdd:COG1228 127 DAIIAgeskllPGPRVLAAGPALSLTGGAHAR------GPEEARAALRELLAEGADYIKVFAEggaPDFSLEELRAILEA 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4731644 226 lgniAKTHDLYIQSHISENREEIEAVKSlypGYKnytdvydknnlltnktVMAHGCYLSEEELNVFSERGASI------- 298
Cdd:COG1228 201 ----AHALGLPVAAHAHQADDIRLAVEA---GVD----------------SIEHGTYLDDEVADLLAEAGTVVlvptlsl 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4731644 299 --AHCPNSNLSLSSGLLNVLDV--------LKHKVKIGLGTDVAGGYS--YSMLDAIRRAVMVSnvllinkvneksLTLK 366
Cdd:COG1228 258 flALLEGAAAPVAAKARKVREAalanarrlHDAGVPVALGTDAGVGVPpgRSLHRELALAVEAG------------LTPE 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4731644 367 EVFRLATLGGSQALGLDREIGNFEVGKDFDALLINprasdspidlfcGDFVGDISeaviqkflYLgddRNIEEVYVGGKQ 446
Cdd:COG1228 326 EALRAATINAAKALGLDDDVGSLEPGKLADLVLLD------------GDPLEDIA--------YL---EDVRAVMKDGRV 382
|
..
gi 4731644 447 VV 448
Cdd:COG1228 383 VD 384
|
|
| PRK06151 |
PRK06151 |
N-ethylammeline chlorohydrolase; Provisional |
75-425 |
6.76e-12 |
|
N-ethylammeline chlorohydrolase; Provisional
Pssm-ID: 180428 [Multi-domain] Cd Length: 488 Bit Score: 67.37 E-value: 6.76e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4731644 75 MPGLVDTHIHapqyafagSNVDLPLLDWLNKytfPTEK--RFQSTDVAE----EVYTRVVRRT---------LKNGTTTA 139
Cdd:PRK06151 56 GPGFIDLDAL--------SDLDTTILGLDNG---PGWAkgRVWSRDYVEagrrEMYTPEELAFqkryafaqlLRNGITTA 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4731644 140 CYFGTI-------HTDSSLILAEITDKFGQRAFVGKVCM--------DLNNTVPEYKETTEESVKETERFVSEMLQKNYS 204
Cdd:PRK06151 125 MPIASLfyrqwaeTYAEFAAAAEAAGRLGLRVYLGPAYRsggsvleaDGSLEVVFDEARGLAGLEEAIAFIKRVDGAHNG 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4731644 205 RVKPIVTPRFSLSCTETLMSELGNIAKTHDLYIQSHISENREEIEAVKSLYPgyKNYTDVYDKNNLLTNKTVMAHGCYLS 284
Cdd:PRK06151 205 LVRGMLAPDRIETCTVDLLRRTAAAARELGCPVRLHCAQGVLEVETVRRLHG--TTPLEWLADVGLLGPRLLIPHATYIS 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4731644 285 E---------EELNVFSERGASIAHCPNSNLSLSSGLLNVLDVLKHKVKIGLGTDVAggysysmldairRAVMVSNV--- 352
Cdd:PRK06151 283 GsprlnysggDDLALLAEHGVSIVHCPLVSARHGSALNSFDRYREAGINLALGTDTF------------PPDMVMNMrvg 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4731644 353 LLINKVNEKSLT---LKEVFRLATLGGSQALGLDrEIGNFEVGKDFDALLINPR-----ASDSPID--LFCGdfVGDISE 422
Cdd:PRK06151 351 LILGRVVEGDLDaasAADLFDAATLGGARALGRD-DLGRLAPGAKADIVVFDLDglhmgPVFDPIRtlVTGG--SGRDVR 427
|
...
gi 4731644 423 AVI 425
Cdd:PRK06151 428 AVF 430
|
|
| PRK07203 |
PRK07203 |
putative aminohydrolase SsnA; |
75-353 |
1.56e-10 |
|
putative aminohydrolase SsnA;
Pssm-ID: 235963 [Multi-domain] Cd Length: 442 Bit Score: 62.65 E-value: 1.56e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4731644 75 MPGLVDTHIHApqY-AFA-GSNVDLP----LLDWLNKYTFPTEKRFQSTDVAEEVYTRVVRrTLKNGTTTA----CYFGT 144
Cdd:PRK07203 58 MPGLINSHNHI--YsGLArGMMANIPpppdFISILKNLWWRLDRALTLEDVYYSALICSLE-AIKNGVTTVfdhhASPNY 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4731644 145 IhTDSSLILAEITDKFGQRAFVGKVCMDLNNtvpeyKETTEESVKETERFVSEMLQKNYSRVKPIVT--PRFSLScTETL 222
Cdd:PRK07203 135 I-GGSLFTIADAAKKVGLRAMLCYETSDRDG-----EKELQEGVEENIRFIKHIDEAKDDMVEAMFGlhASFTLS-DATL 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4731644 223 mSELGNIAKTHDLYIQSHISENREEIEAVKSLYpgYKNYTDVYDKNNLLTNKTVMAHGCYLSEEELNVFSERGASIAHCP 302
Cdd:PRK07203 208 -EKCREAVKETGRGYHIHVAEGIYDVSDSHKKY--GKDIVERLADFGLLGEKTLAAHCIYLSDEEIDLLKETDTFVVHNP 284
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 4731644 303 NSNLSLSSGLLNVLDVLKHKVKIGLGTDvagGYSYSMLDAIRravmVSNVL 353
Cdd:PRK07203 285 ESNMGNAVGYNPVLEMIKNGILLGLGTD---GYTSDMFESYK----VANFK 328
|
|
| archeal_chlorohydrolases |
cd01305 |
Predicted chlorohydrolases. These metallo-dependent hydrolases from archea are part of the ... |
75-377 |
1.46e-08 |
|
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: 55.48 E-value: 1.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4731644 75 MPGLVDTHIHAPQYAFAGSNVDLPLLD---WLN--KYTFPTekrfQSTDVAEEVYTR-VVRRTLKNGTTTACYFGTIHTD 148
Cdd:cd01305 3 IPALVNAHTHLGDSAIKEVGDGLPLDDlvaPPDglKHRLLA----QADDRELAEAMRkVLRDMRETGIGAFADFREGGVE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4731644 149 SSLILAEITDKFgqrAFVGKVCMDLnntvPEYKETTEESVKETERFvsemlqkNYSrvkpivtprfslSCTETLMSELGN 228
Cdd:cd01305 79 GIELLRRALGKL---PVPFEVILGR----PTEPDDPEILLEVADGL-------GLS------------SANDVDLEDILE 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4731644 229 IAKTHDLYIQSHISENRE-----EIEAVKSLYPgyknytdvydknNLLTnktvmaHGCYLSEEELNVFSERGASIAHCPN 303
Cdd:cd01305 133 LLRRRGKLFAIHASETREsvgmtDIERALDLEP------------DLLV------HGTHLTDEDLELVRENGVPVVLCPR 194
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 4731644 304 SNLSLSSGLLNVLDVLKHKVKIGLGTDVAGGYSYSMLDAIRRAVMVSNVLlinkvneKSLTLKEVFRLATLGGS 377
Cdd:cd01305 195 SNLYFGVGIPPVAELLKLGIKVLLGTDNVMVNEPDMWAEMEFLAKYSRLQ-------GYLSPLEILRMATVNAA 261
|
|
| Met_dep_hydrolase_E |
cd01313 |
Metallo-dependent hydrolases, subgroup D is part of the superfamily of metallo-dependent ... |
240-445 |
2.13e-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: 55.92 E-value: 2.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4731644 240 HISENREEIEAVKSlYPGYKNYTDVYDkNNLLTNKTVMAHGCYLSEEELNVFSERGASIAHCPNSNLSLSSGLLNVLDVL 319
Cdd:cd01313 225 HLAEQPKEVDDCLA-AHGRRPVELLLD-HGHLDARWCLVHATHLTDNETLLLGRSGAVVGLCPTTEANLGDGIFPAAALL 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4731644 320 KHKVKIGLGTDVAGG-----------YSYSMLDAIRravmvsNVLlinkVNEKSLTLKEVFRLATLGGSQALGLDreIGN 388
Cdd:cd01313 303 AAGGRIGIGSDSNARidlleelrqleYSQRLRDRAR------NVL----ATAGGSSARALLDAALAGGAQALGLA--TGA 370
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 4731644 389 FEVGKDFDALLInprASDSPidlfcgDFVGDISEAVIQKFLYLGDDRNIEEVYVGGK 445
Cdd:cd01313 371 LEAGARADLLSL---DLDHP------SLAGALPDTLLDAWVFAAGDREVRDVVVGGR 418
|
|
| Amidohydro_3 |
pfam07969 |
Amidohydrolase family; |
319-448 |
1.05e-05 |
|
Amidohydrolase family;
Pssm-ID: 400360 [Multi-domain] Cd Length: 464 Bit Score: 47.53 E-value: 1.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4731644 319 LKHKVKIGLGTDVAGGySYSMLDAIRRAVM-----VSNVLLInkvnEKSLTLKEVFRLATLGGSQALGLDREIGNFEVGK 393
Cdd:pfam07969 355 LNAGVKVALGSDAPVG-PFDPWPRIGAAVMrqtagGGEVLGP----DEELSLEEALALYTSGPAKALGLEDRKGTLGVGK 429
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 4731644 394 DFDALLINprasdspIDLFcgdfvgDISEAVIqkflylgDDRNIEEVYVGGKQVV 448
Cdd:pfam07969 430 DADLVVLD-------DDPL------TVDPPAI-------ADIRVRLTVVDGRVVY 464
|
|
| PRK07213 |
PRK07213 |
chlorohydrolase; Provisional |
240-404 |
2.45e-04 |
|
chlorohydrolase; Provisional
Pssm-ID: 235969 [Multi-domain] Cd Length: 375 Bit Score: 43.10 E-value: 2.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4731644 240 HISENREEIEAVKSLYpgykNYTDVYDKNNLLTNKTVMAHGCYLSEEELNVFSERGASIAHCPNSNLSLSSGLLNVLDVL 319
Cdd:PRK07213 198 HAAEHKGSVEYSLEKY----GMTEIERLINLGFKPDFIVHATHPSNDDLELLKENNIPVVVCPRANASFNVGLPPLNEML 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4731644 320 KHKVKIGLGTDVAGGYSYSM---LDAIRRAVmvsnvllinkvnekSLTLKEVFRLATLGGSQALGLDReIGNFEVGKDFD 396
Cdd:PRK07213 274 EKGILLGIGTDNFMANSPSIfreMEFIYKLY--------------HIEPKEILKMATINGAKILGLIN-VGLIEEGFKAD 338
|
....*...
gi 4731644 397 ALLINPRA 404
Cdd:PRK07213 339 FTFIKPTN 346
|
|
| Met_dep_hydrolase_A |
cd01299 |
Metallo-dependent hydrolases, subgroup A is part of the superfamily of metallo-dependent ... |
320-404 |
2.28e-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: 39.97 E-value: 2.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4731644 320 KHKVKIGLGTD-----VAGGYSYSMLdairrAVMVsnvllinkvnEKSLTLKEVFRLATLGGSQALGLDREIGNFEVGKD 394
Cdd:cd01299 261 KAGVKIAFGTDagfpvPPHGWNAREL-----ELLV----------KAGGTPAEALRAATANAAELLGLSDELGVIEAGKL 325
|
90
....*....|..
gi 4731644 395 FDALLI--NPRA 404
Cdd:cd01299 326 ADLLVVdgDPLE 337
|
|
| NagA |
COG1820 |
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism]; |
338-402 |
2.49e-03 |
|
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism];
Pssm-ID: 441425 [Multi-domain] Cd Length: 373 Bit Score: 40.08 E-value: 2.49e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 4731644 338 SMLDAIRRAVMVSNVllinkvnekslTLKEVFRLATLGGSQALGLDREIGNFEVGKDFDALLINP 402
Cdd:COG1820 308 TMDDAVRNLVEWTGL-----------PLEEAVRMASLNPARALGLDDRKGSIAPGKDADLVVLDD 361
|
|
| Imidazolone-5PH |
cd01296 |
Imidazolonepropionase/imidazolone-5-propionate hydrolase (Imidazolone-5PH) catalyzes the third ... |
277-412 |
4.63e-03 |
|
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: 39.16 E-value: 4.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4731644 277 MAHGCYLSEEELNVFSERGASIAHCPNSNLSLSSGLLNVLDVLKHKVKIGLGTDVAGGySY---SMLDAIRRAVmvsnVL 353
Cdd:cd01296 233 ADHLEHTSDEGIAALAEAGTVAVLLPGTAFSLRETYPPARKLIDAGVPVALGTDFNPG-SSptsSMPLVMHLAC----RL 307
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 4731644 354 LinkvnekSLTLKEVFRLATLGGSQALGLDREIGNFEVGKDFDALLINpraSDSPIDLF 412
Cdd:cd01296 308 M-------RMTPEEALTAATINAAAALGLGETVGSLEVGKQADLVILD---APSYEHLA 356
|
|
| nagA |
PRK11170 |
N-acetylglucosamine-6-phosphate deacetylase; Provisional |
333-393 |
5.72e-03 |
|
N-acetylglucosamine-6-phosphate deacetylase; Provisional
Pssm-ID: 183010 Cd Length: 382 Bit Score: 38.80 E-value: 5.72e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 4731644 333 GGYSYSMLDAIRravmvsnvlliNKVNEKSLTLKEVFRLATLGGSQALGLDREIGNFEVGK 393
Cdd:PRK11170 307 SGSALTMIEAVR-----------NLVEHVGIALDEALRMATLYPARAIGVDKRLGSIEAGK 356
|
|
| NagA |
cd00854 |
N-acetylglucosamine-6-phosphate deacetylase, NagA, catalyzes the hydrolysis of the N-acetyl ... |
338-402 |
6.56e-03 |
|
N-acetylglucosamine-6-phosphate deacetylase, NagA, catalyzes the hydrolysis of the N-acetyl group of N-acetyl-glucosamine-6-phosphate (GlcNAc-6-P) to glucosamine 6-phosphate and acetate. This is the first committed step in the biosynthetic pathway to amino-sugar-nucleotides, which is needed for cell wall peptidoglycan and teichoic acid biosynthesis. Deacetylation of N-acetylglucosamine is also important in lipopolysaccharide synthesis and cell wall recycling.
Pssm-ID: 238434 [Multi-domain] Cd Length: 374 Bit Score: 38.71 E-value: 6.56e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 4731644 338 SMLDAIRRAVMVSNVllinkvnekslTLKEVFRLATLGGSQALGLDREIGNFEVGKDFDALLINP 402
Cdd:cd00854 310 TMDQAVRNMVKWGGC-----------PLEEAVRMASLNPAKLLGLDDRKGSLKPGKDADLVVLDD 363
|
|
| PRK09229 |
PRK09229 |
N-formimino-L-glutamate deiminase; Validated |
317-448 |
8.23e-03 |
|
N-formimino-L-glutamate deiminase; Validated
Pssm-ID: 236420 [Multi-domain] Cd Length: 456 Bit Score: 38.29 E-value: 8.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4731644 317 DVLKHKVKIGLGTDvaggySYSMLDAI---------------RRAVMVSnvllinkvNEKSLTLKEVFRLATLGGSQALG 381
Cdd:PRK09229 309 DYLAAGGRFGIGSD-----SHVSIDLVeelrlleygqrlrdrRRNVLAA--------AAQPSVGRRLFDAALAGGAQALG 375
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 4731644 382 ldREIGNFEVGKDFDALLINPrasDSPidlfcgDFVGDISEAVIQKFLYLGDDRNIEEVYVGGKQVV 448
Cdd:PRK09229 376 --RAIGGLAVGARADLVVLDL---DHP------ALAGREGDALLDRWVFAGGDAAVRDVWVAGRWVV 431
|
|
| |
