|
Name |
Accession |
Description |
Interval |
E-value |
| PRK09229 |
PRK09229 |
N-formimino-L-glutamate deiminase; Validated |
4-440 |
2.29e-173 |
|
N-formimino-L-glutamate deiminase; Validated
Pssm-ID: 236420 [Multi-domain] Cd Length: 456 Bit Score: 493.21 E-value: 2.29e-173
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497631771 4 STAYWCEWAWLPGGPVPGVLVETE-DGRITSVSEVDDPGGARRLGGLVLPGMANAHSHAFHRALRGRT---SAGKGTFWT 79
Cdd:PRK09229 2 MTTLFAERALLPDGWARNVRLTVDaDGRIAAVEPGAAPAGAERLAGPVLPGMPNLHSHAFQRAMAGLTevrGPPQDSFWS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497631771 80 WRDQMYKVAARLDPESYHRLATAVFAEMALSGMTCVGEFHYLHHAPGGQRYSDPNAMGAALAQAAADAGIRLTLLDTCYL 159
Cdd:PRK09229 82 WRELMYRFALRLTPDQLEAIARQLYVEMLEAGYTSVGEFHYLHHDPDGTPYADPAEMALRIVAAARAAGIGLTLLPVLYA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497631771 160 AGGFG-KPVEGVQLRYTDgDVSAWADRVDEFKPA---GDHVRVGAALHSVRAVPAEAIPGVVEWAGGaDAPLHAHLSEQR 235
Cdd:PRK09229 162 HSGFGgQPPNPGQRRFIN-DPDGFLRLLEALRRAlaaLPGARLGLAPHSLRAVTPDQLAAVLALAAP-DGPVHIHIAEQT 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497631771 236 AENEACLAAHGCTPTQLLASHGALGESTTAVHATHLAPGDLPLLGGSGTGVCLCPTTEADLADGIGPASALAVAGSPLSV 315
Cdd:PRK09229 240 KEVDDCLAWSGARPVEWLLDHAPVDARWCLVHATHLTDAETARLARSGAVAGLCPTTEANLGDGIFPAVDYLAAGGRFGI 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497631771 316 GSDGHSVIDQFAEVQAVESYMRLSQETRGNFTPAD-------LVTMATASGHRALGWsDAGWIGAGARADLVAVGLDSAR 388
Cdd:PRK09229 320 GSDSHVSIDLVEELRLLEYGQRLRDRRRNVLAAAAqpsvgrrLFDAALAGGAQALGR-AIGGLAVGARADLVVLDLDHPA 398
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 497631771 389 LAGVPPEAV----VSAASADDVRDVVVDGRLVVRDGTHRLVPDLAERMRDSVAALL 440
Cdd:PRK09229 399 LAGREGDALldrwVFAGGDAAVRDVWVAGRWVVRDGRHRLREAIAAAFRAALAALL 454
|
|
| hutF |
TIGR02022 |
formiminoglutamate deiminase; In some species, histidine utilization goes via urocanate to ... |
4-440 |
1.56e-132 |
|
formiminoglutamate deiminase; In some species, histidine utilization goes via urocanate to glutamate in four step, the last being removal of formamide. This model describes an alternate fourth step, formiminoglutamate hydrolase, which leads to N-formyl-L-glutamate. This product may be acted on by formylglutamate amidohydrolase (TIGR02017) and bypass glutamate as a product during its degradation. Alternatively, removal of formate (by EC 3.5.1.68) would yield glutamate. [Energy metabolism, Amino acids and amines]
Pssm-ID: 273931 [Multi-domain] Cd Length: 454 Bit Score: 389.50 E-value: 1.56e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497631771 4 STAYWCEWAWLPGGPVPGVLVETEDGRITSVSE-VDDPGGARRLGGLVLPGMANAHSHAFHRALRGRT---SAGKGTFWT 79
Cdd:TIGR02022 1 MHVYWAERALLPDGWAEGVRIAVADGRILAIETgVPAAPGDERLSGPLLPGLANLHSHAFQRAMAGLAevaGSGGDSFWT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497631771 80 WRDQMYKVAARLDPESYHRLATAVFAEMALSGMTCVGEFHYLHHAPGGQRYSDPNAMGAALAQAAADAGIRLTLLDTCYL 159
Cdd:TIGR02022 81 WRELMYRFADRLTPEQLQAIARQLYVEMLEAGFTRVGEFHYLHHAPDGTPYADPAEMAERIAAAAADAGIGLTLLPVFYA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497631771 160 AGGFG-KPVEGVQLRYTDgDVSAWADRVDEFKP---AGDHVRVGAALHSVRAVPAEAIPGVVEWAGGAdAPLHAHLSEQR 235
Cdd:TIGR02022 161 HSGFGgAAPNPGQRRFIH-DPERFARLVEVLRRtlaAQPGAVLGLAPHSLRAVTPEQLAAVLQASDRQ-APVHIHVAEQQ 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497631771 236 AENEACLAAHGCTPTQLLASHGALGESTTAVHATHLAPGDLPLLGGSGTGVCLCPTTEADLADGIGPASALAVAGSPLSV 315
Cdd:TIGR02022 239 KEVDDCLAWSGRRPVEWLLDHGPVDARWCLVHATHLTDEETKLLAKSGAVAGLCPTTEANLGDGIFPAVDFAAAGGRFGI 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497631771 316 GSDGHSVIDQFAEVQAVESYMRLSQETRGNFTPA-------DLVTMATASGHRALGWsDAGWIGAGARADLVAVGLDSAR 388
Cdd:TIGR02022 319 GSDSHVLIDVAEELRQLEYGQRLRDRARNVLAAGpgpsvgrALYDAALLGGAQALGR-ATGGLRAGARADFLTLDGDHPR 397
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 497631771 389 LAGVPPEAV----VSAASADDVRDVVVDGRLVVRDGTHRLVPDLAERMRDSVAALL 440
Cdd:TIGR02022 398 LAGALGDSLldrwLFAGGKAAVRDVWVGGRWVVRDGRHALREEIGRAFAKVLRALL 453
|
|
| Met_dep_hydrolase_E |
cd01313 |
Metallo-dependent hydrolases, subgroup D is part of the superfamily of metallo-dependent ... |
12-401 |
2.45e-129 |
|
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: 379.88 E-value: 2.45e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497631771 12 AWLPGGPVPGVLVET-EDGRITSVSEVDDPGGARRLGGLVLPGMANAHSHAFHRALRGRTSAGK---GTFWTWRDQMYKV 87
Cdd:cd01313 1 ALLPEGWERNVRIEVdADGRIAAVNPDTATEAVALLGGALLPGMPNLHSHAFQRAMAGLTEYRGsaaDSFWTWRELMYRF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497631771 88 AARLDPESYHRLATAVFAEMALSGMTCVGEFHYLHHAPGGQRYSDPNAMGAALAQAAADAGIRLTLLDTCYLAGGFG-KP 166
Cdd:cd01313 81 AARLTPEQIEAIARQLYIEMLLAGITAVGEFHYVHHDPDGTPYADPAELAQRVIAAASDAGIGITLLPVLYARAGFGgPA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497631771 167 VEGVQLRYTDGDVSAWADRVDEFK--PAGDHVRVGAALHSVRAVPAEAIPGVVEWAGGaDAPLHAHLSEQRAENEACLAA 244
Cdd:cd01313 161 PNPGQRRFINGYEDFLGLLEKALRavKEHAAARIGVAPHSLRAVPAEQLAALAALASE-KAPVHIHLAEQPKEVDDCLAA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497631771 245 HGCTPTQLLASHGALGESTTAVHATHLAPGDLPLLGGSGTGVCLCPTTEADLADGIGPASALAVAGSPLSVGSDGHSVID 324
Cdd:cd01313 240 HGRRPVELLLDHGHLDARWCLVHATHLTDNETLLLGRSGAVVGLCPTTEANLGDGIFPAAALLAAGGRIGIGSDSNARID 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497631771 325 QFAEVQAVESYMRLSQETRGNF------TPADLVTMATASGHRALGWsDAGWIGAGARADLVAVGLDSARLAGVPPEAVV 398
Cdd:cd01313 320 LLEELRQLEYSQRLRDRARNVLataggsSARALLDAALAGGAQALGL-ATGALEAGARADLLSLDLDHPSLAGALPDTLL 398
|
...
gi 497631771 399 SAA 401
Cdd:cd01313 399 DAW 401
|
|
| SsnA |
COG0402 |
Cytosine/adenosine deaminase or related metal-dependent hydrolase [Nucleotide transport and ... |
7-419 |
1.71e-89 |
|
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: 277.86 E-value: 1.71e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497631771 7 YWCEWAWL-----PGGPVPGVLVETEDGRITSVSEVDDP----GGARRL---GGLVLPGMANAHSHAFHRALRGRtsAGK 74
Cdd:COG0402 2 LLIRGAWVltmdpAGGVLEDGAVLVEDGRIAAVGPGAELparyPAAEVIdagGKLVLPGLVNTHTHLPQTLLRGL--ADD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497631771 75 GTFWTWRDQ-MYKVAARLDPESYHRLATAVFAEMALSGMTCVGEFHYLHHApggqrysdpnaMGAALAQAAADAGIRLTL 153
Cdd:COG0402 80 LPLLDWLEEyIWPLEARLDPEDVYAGALLALAEMLRSGTTTVADFYYVHPE-----------SADALAEAAAEAGIRAVL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497631771 154 LDTCYLAGGFGKPVEGVQ--LRYTDGDVSAWADRvdefkpAGDHVRVGAALHSVRAVPAEAIPGVVEWAGGADAPLHAHL 231
Cdd:COG0402 149 GRGLMDRGFPDGLREDADegLADSERLIERWHGA------ADGRIRVALAPHAPYTVSPELLRAAAALARELGLPLHTHL 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497631771 232 SEQRAENEACLAAHGCTPTQLLASHGALGESTTAVHATHLAPGDLPLLGGSGTGVCLCPTTEADLADGIGPASALAVAGS 311
Cdd:COG0402 223 AETRDEVEWVLELYGKRPVEYLDELGLLGPRTLLAHCVHLTDEEIALLAETGASVAHCPTSNLKLGSGIAPVPRLLAAGV 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497631771 312 PLSVGSDG---HSVIDQFAEVQAVESYMRLSQETRGNFTPADLVTMATASGHRALGWSD-AGWIGAGARADLVAVGLDSA 387
Cdd:COG0402 303 RVGLGTDGaasNNSLDMFEEMRLAALLQRLRGGDPTALSAREALEMATLGGARALGLDDeIGSLEPGKRADLVVLDLDAP 382
|
410 420 430
....*....|....*....|....*....|....
gi 497631771 388 RLAGV--PPEAVVSAASADDVRDVVVDGRLVVRD 419
Cdd:COG0402 383 HLAPLhdPLSALVYAADGRDVRTVWVAGRVVVRD 416
|
|
| Amidohydro_1 |
pfam01979 |
Amidohydrolase family; This family of enzymes are a a large metal dependent hydrolase ... |
49-398 |
1.92e-27 |
|
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: 111.82 E-value: 1.92e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497631771 49 LVLPGMANAHSHAFHRALRGRTSAGKgtfwtwrdqmykvaarldpESYHRLATAVfAEMALSGMTCVGEFHYLHHapggq 128
Cdd:pfam01979 1 IVLPGLIDAHVHLEMGLLRGIPVPPE-------------------FAYEALRLGI-TTMLKSGTTTVLDMGATTS----- 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497631771 129 rysdPNAMGAALAQAAADAGIRLTLLDTCYLAGGFGKPVEGVQLRYTDGDVSawadrvdEFKPAGDHVRVGAALHSVRAV 208
Cdd:pfam01979 56 ----TGIEALLEAAEELPLGLRFLGPGCSLDTDGELEGRKALREKLKAGAEF-------IKGMADGVVFVGLAPHGAPTF 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497631771 209 PAEAIPGVVEWAGGADAPLHAHLSEQRAENEACLAAHGC-----TPTQLLASHGALGESTTA-VHATHLAPGDLPLLG-- 280
Cdd:pfam01979 125 SDDELKAALEEAKKYGLPVAIHALETKGEVEDAIAAFGGgiehgTHLEVAESGGLLDIIKLIlAHGVHLSPTEANLLAeh 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497631771 281 GSGTGVCLCPTTEADLADGIGPASALAVAGSPLSVGSDGHSVIDQFAEVQAVESYMRLSQETRGNFTPADLVTMATASGH 360
Cdd:pfam01979 205 LKGAGVAHCPFSNSKLRSGRIALRKALEDGVKVGLGTDGAGSGNSLNMLEELRLALELQFDPEGGLSPLEALRMATINPA 284
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 497631771 361 RALGWSD-AGWIGAGARADLVAVGLDS-ARLAGVPPEAVV 398
Cdd:pfam01979 285 KALGLDDkVGSIEVGKDADLVVVDLDPlAAFFGLKPDGNV 324
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK09229 |
PRK09229 |
N-formimino-L-glutamate deiminase; Validated |
4-440 |
2.29e-173 |
|
N-formimino-L-glutamate deiminase; Validated
Pssm-ID: 236420 [Multi-domain] Cd Length: 456 Bit Score: 493.21 E-value: 2.29e-173
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497631771 4 STAYWCEWAWLPGGPVPGVLVETE-DGRITSVSEVDDPGGARRLGGLVLPGMANAHSHAFHRALRGRT---SAGKGTFWT 79
Cdd:PRK09229 2 MTTLFAERALLPDGWARNVRLTVDaDGRIAAVEPGAAPAGAERLAGPVLPGMPNLHSHAFQRAMAGLTevrGPPQDSFWS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497631771 80 WRDQMYKVAARLDPESYHRLATAVFAEMALSGMTCVGEFHYLHHAPGGQRYSDPNAMGAALAQAAADAGIRLTLLDTCYL 159
Cdd:PRK09229 82 WRELMYRFALRLTPDQLEAIARQLYVEMLEAGYTSVGEFHYLHHDPDGTPYADPAEMALRIVAAARAAGIGLTLLPVLYA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497631771 160 AGGFG-KPVEGVQLRYTDgDVSAWADRVDEFKPA---GDHVRVGAALHSVRAVPAEAIPGVVEWAGGaDAPLHAHLSEQR 235
Cdd:PRK09229 162 HSGFGgQPPNPGQRRFIN-DPDGFLRLLEALRRAlaaLPGARLGLAPHSLRAVTPDQLAAVLALAAP-DGPVHIHIAEQT 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497631771 236 AENEACLAAHGCTPTQLLASHGALGESTTAVHATHLAPGDLPLLGGSGTGVCLCPTTEADLADGIGPASALAVAGSPLSV 315
Cdd:PRK09229 240 KEVDDCLAWSGARPVEWLLDHAPVDARWCLVHATHLTDAETARLARSGAVAGLCPTTEANLGDGIFPAVDYLAAGGRFGI 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497631771 316 GSDGHSVIDQFAEVQAVESYMRLSQETRGNFTPAD-------LVTMATASGHRALGWsDAGWIGAGARADLVAVGLDSAR 388
Cdd:PRK09229 320 GSDSHVSIDLVEELRLLEYGQRLRDRRRNVLAAAAqpsvgrrLFDAALAGGAQALGR-AIGGLAVGARADLVVLDLDHPA 398
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 497631771 389 LAGVPPEAV----VSAASADDVRDVVVDGRLVVRDGTHRLVPDLAERMRDSVAALL 440
Cdd:PRK09229 399 LAGREGDALldrwVFAGGDAAVRDVWVAGRWVVRDGRHRLREAIAAAFRAALAALL 454
|
|
| hutF |
TIGR02022 |
formiminoglutamate deiminase; In some species, histidine utilization goes via urocanate to ... |
4-440 |
1.56e-132 |
|
formiminoglutamate deiminase; In some species, histidine utilization goes via urocanate to glutamate in four step, the last being removal of formamide. This model describes an alternate fourth step, formiminoglutamate hydrolase, which leads to N-formyl-L-glutamate. This product may be acted on by formylglutamate amidohydrolase (TIGR02017) and bypass glutamate as a product during its degradation. Alternatively, removal of formate (by EC 3.5.1.68) would yield glutamate. [Energy metabolism, Amino acids and amines]
Pssm-ID: 273931 [Multi-domain] Cd Length: 454 Bit Score: 389.50 E-value: 1.56e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497631771 4 STAYWCEWAWLPGGPVPGVLVETEDGRITSVSE-VDDPGGARRLGGLVLPGMANAHSHAFHRALRGRT---SAGKGTFWT 79
Cdd:TIGR02022 1 MHVYWAERALLPDGWAEGVRIAVADGRILAIETgVPAAPGDERLSGPLLPGLANLHSHAFQRAMAGLAevaGSGGDSFWT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497631771 80 WRDQMYKVAARLDPESYHRLATAVFAEMALSGMTCVGEFHYLHHAPGGQRYSDPNAMGAALAQAAADAGIRLTLLDTCYL 159
Cdd:TIGR02022 81 WRELMYRFADRLTPEQLQAIARQLYVEMLEAGFTRVGEFHYLHHAPDGTPYADPAEMAERIAAAAADAGIGLTLLPVFYA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497631771 160 AGGFG-KPVEGVQLRYTDgDVSAWADRVDEFKP---AGDHVRVGAALHSVRAVPAEAIPGVVEWAGGAdAPLHAHLSEQR 235
Cdd:TIGR02022 161 HSGFGgAAPNPGQRRFIH-DPERFARLVEVLRRtlaAQPGAVLGLAPHSLRAVTPEQLAAVLQASDRQ-APVHIHVAEQQ 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497631771 236 AENEACLAAHGCTPTQLLASHGALGESTTAVHATHLAPGDLPLLGGSGTGVCLCPTTEADLADGIGPASALAVAGSPLSV 315
Cdd:TIGR02022 239 KEVDDCLAWSGRRPVEWLLDHGPVDARWCLVHATHLTDEETKLLAKSGAVAGLCPTTEANLGDGIFPAVDFAAAGGRFGI 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497631771 316 GSDGHSVIDQFAEVQAVESYMRLSQETRGNFTPA-------DLVTMATASGHRALGWsDAGWIGAGARADLVAVGLDSAR 388
Cdd:TIGR02022 319 GSDSHVLIDVAEELRQLEYGQRLRDRARNVLAAGpgpsvgrALYDAALLGGAQALGR-ATGGLRAGARADFLTLDGDHPR 397
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 497631771 389 LAGVPPEAV----VSAASADDVRDVVVDGRLVVRDGTHRLVPDLAERMRDSVAALL 440
Cdd:TIGR02022 398 LAGALGDSLldrwLFAGGKAAVRDVWVGGRWVVRDGRHALREEIGRAFAKVLRALL 453
|
|
| Met_dep_hydrolase_E |
cd01313 |
Metallo-dependent hydrolases, subgroup D is part of the superfamily of metallo-dependent ... |
12-401 |
2.45e-129 |
|
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: 379.88 E-value: 2.45e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497631771 12 AWLPGGPVPGVLVET-EDGRITSVSEVDDPGGARRLGGLVLPGMANAHSHAFHRALRGRTSAGK---GTFWTWRDQMYKV 87
Cdd:cd01313 1 ALLPEGWERNVRIEVdADGRIAAVNPDTATEAVALLGGALLPGMPNLHSHAFQRAMAGLTEYRGsaaDSFWTWRELMYRF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497631771 88 AARLDPESYHRLATAVFAEMALSGMTCVGEFHYLHHAPGGQRYSDPNAMGAALAQAAADAGIRLTLLDTCYLAGGFG-KP 166
Cdd:cd01313 81 AARLTPEQIEAIARQLYIEMLLAGITAVGEFHYVHHDPDGTPYADPAELAQRVIAAASDAGIGITLLPVLYARAGFGgPA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497631771 167 VEGVQLRYTDGDVSAWADRVDEFK--PAGDHVRVGAALHSVRAVPAEAIPGVVEWAGGaDAPLHAHLSEQRAENEACLAA 244
Cdd:cd01313 161 PNPGQRRFINGYEDFLGLLEKALRavKEHAAARIGVAPHSLRAVPAEQLAALAALASE-KAPVHIHLAEQPKEVDDCLAA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497631771 245 HGCTPTQLLASHGALGESTTAVHATHLAPGDLPLLGGSGTGVCLCPTTEADLADGIGPASALAVAGSPLSVGSDGHSVID 324
Cdd:cd01313 240 HGRRPVELLLDHGHLDARWCLVHATHLTDNETLLLGRSGAVVGLCPTTEANLGDGIFPAAALLAAGGRIGIGSDSNARID 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497631771 325 QFAEVQAVESYMRLSQETRGNF------TPADLVTMATASGHRALGWsDAGWIGAGARADLVAVGLDSARLAGVPPEAVV 398
Cdd:cd01313 320 LLEELRQLEYSQRLRDRARNVLataggsSARALLDAALAGGAQALGL-ATGALEAGARADLLSLDLDHPSLAGALPDTLL 398
|
...
gi 497631771 399 SAA 401
Cdd:cd01313 399 DAW 401
|
|
| SsnA |
COG0402 |
Cytosine/adenosine deaminase or related metal-dependent hydrolase [Nucleotide transport and ... |
7-419 |
1.71e-89 |
|
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: 277.86 E-value: 1.71e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497631771 7 YWCEWAWL-----PGGPVPGVLVETEDGRITSVSEVDDP----GGARRL---GGLVLPGMANAHSHAFHRALRGRtsAGK 74
Cdd:COG0402 2 LLIRGAWVltmdpAGGVLEDGAVLVEDGRIAAVGPGAELparyPAAEVIdagGKLVLPGLVNTHTHLPQTLLRGL--ADD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497631771 75 GTFWTWRDQ-MYKVAARLDPESYHRLATAVFAEMALSGMTCVGEFHYLHHApggqrysdpnaMGAALAQAAADAGIRLTL 153
Cdd:COG0402 80 LPLLDWLEEyIWPLEARLDPEDVYAGALLALAEMLRSGTTTVADFYYVHPE-----------SADALAEAAAEAGIRAVL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497631771 154 LDTCYLAGGFGKPVEGVQ--LRYTDGDVSAWADRvdefkpAGDHVRVGAALHSVRAVPAEAIPGVVEWAGGADAPLHAHL 231
Cdd:COG0402 149 GRGLMDRGFPDGLREDADegLADSERLIERWHGA------ADGRIRVALAPHAPYTVSPELLRAAAALARELGLPLHTHL 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497631771 232 SEQRAENEACLAAHGCTPTQLLASHGALGESTTAVHATHLAPGDLPLLGGSGTGVCLCPTTEADLADGIGPASALAVAGS 311
Cdd:COG0402 223 AETRDEVEWVLELYGKRPVEYLDELGLLGPRTLLAHCVHLTDEEIALLAETGASVAHCPTSNLKLGSGIAPVPRLLAAGV 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497631771 312 PLSVGSDG---HSVIDQFAEVQAVESYMRLSQETRGNFTPADLVTMATASGHRALGWSD-AGWIGAGARADLVAVGLDSA 387
Cdd:COG0402 303 RVGLGTDGaasNNSLDMFEEMRLAALLQRLRGGDPTALSAREALEMATLGGARALGLDDeIGSLEPGKRADLVVLDLDAP 382
|
410 420 430
....*....|....*....|....*....|....
gi 497631771 388 RLAGV--PPEAVVSAASADDVRDVVVDGRLVVRD 419
Cdd:COG0402 383 HLAPLhdPLSALVYAADGRDVRTVWVAGRVVVRD 416
|
|
| ATZ_TRZ_like |
cd01298 |
TRZ/ATZ family contains enzymes from the atrazine degradation pathway and related hydrolases. ... |
20-420 |
1.31e-49 |
|
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: 173.54 E-value: 1.31e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497631771 20 PGVLVEteDGRITSVSEVDDPG---GARRL---GGLVLPGMANAHSHAFHRALRGRTSAGkgTFWTW-RDQMYKVAARLD 92
Cdd:cd01298 20 GDVLVE--DGRIVAVGPALPLPaypADEVIdakGKVVMPGLVNTHTHLAMTLLRGLADDL--PLMEWlKDLIWPLERLLT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497631771 93 PESYHRLATAVFAEMALSGMTCVGEFHYLHHApggqrysdpnamgaALAQAAADAGIRltlldTCYLAGGFGKPVEGVQ- 171
Cdd:cd01298 96 EEDVYLGALLALAEMIRSGTTTFADMYFFYPD--------------AVAEAAEELGIR-----AVLGRGIMDLGTEDVEe 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497631771 172 ----LRYTDGDVSAWADrvdefkPAGDHVRVGAALHSVRAVPAEAIPGVVEWAGGADAPLHAHLSEQRAENEACLAAHGC 247
Cdd:cd01298 157 teeaLAEAERLIREWHG------AADGRIRVALAPHAPYTCSDELLREVAELAREYGVPLHIHLAETEDEVEESLEKYGK 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497631771 248 TPTQLLASHGALGESTTAVHATHLAPGDLPLLGGSGTGVCLCPTTEADLADGIGPASALAVAGSPLSVGSDGHSV---ID 324
Cdd:cd01298 231 RPVEYLEELGLLGPDVVLAHCVWLTDEEIELLAETGTGVAHNPASNMKLASGIAPVPEMLEAGVNVGLGTDGAASnnnLD 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497631771 325 QFAEVQAVESYMRLSQETRGNFTPADLVTMATASGHRALGWSDAGWIGAGARADLVAVGLDSARLAGV--PPEAVVSAAS 402
Cdd:cd01298 311 MFEEMRLAALLQKLAHGDPTALPAEEALEMATIGGAKALGLDEIGSLEVGKKADLILIDLDGPHLLPVhdPISHLVYSAN 390
|
410
....*....|....*...
gi 497631771 403 ADDVRDVVVDGRLVVRDG 420
Cdd:cd01298 391 GGDVDTVIVNGRVVMEDG 408
|
|
| PRK12393 |
PRK12393 |
amidohydrolase; Provisional |
27-440 |
5.02e-40 |
|
amidohydrolase; Provisional
Pssm-ID: 237088 [Multi-domain] Cd Length: 457 Bit Score: 149.06 E-value: 5.02e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497631771 27 EDGRITSVSEVDDPGGARRL---GGLVLPGMANAHSHAFHRALRGRTSAGKGTFWTW-RDQMYKVAARLDPESYHRLATA 102
Cdd:PRK12393 31 RDGRIAAIGALTPLPGERVIdatDCVVYPGWVNTHHHLFQSLLKGVPAGINQSLTAWlAAVPYRFRARFDEDLFRLAARI 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497631771 103 VFAEMALSGMTCVGEFHYLHHAPGGQRYSDpnamgaALAQAAADAGIRLTL-----LDTCYLAGGFGKPVEGVQLRYTDG 177
Cdd:PRK12393 111 GLVELLRSGCTTVADHHYLYHPGMPFDTGD------ILFDEAEALGMRFVLcrggaTQTRGDHPGLPTALRPETLDQMLA 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497631771 178 DVSAWADRVDEFKPAGDHVRVGAALHSVRAVPAEAIPGVVEWAGGADAPLHAHLSEQRAENEACLAAHGCTPTQLLASHG 257
Cdd:PRK12393 185 DVERLVSRYHDASPDSLRRVVVAPTTPTFSLPPELLREVARAARGMGLRLHSHLSETVDYVDFCREKYGMTPVQFVAEHD 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497631771 258 ALGESTTAVHATHLAPGDLPLLGGSGTGVCLCPTTEADLADGIGPASALAVAGSPLSVGSDGhSVIDQFAEVQAVESYMR 337
Cdd:PRK12393 265 WLGPDVWFAHLVKLDAEEIALLAQTGTGIAHCPQSNGRLGSGIAPALAMEAAGVPVSLGVDG-AASNESADMLSEAHAAW 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497631771 338 LSQETRGN---FTPADLVTMATASGHRALGWSDAGWIGAGARADLVAVGLDSARLAGV--PPEAVVSAASADDVRDVVVD 412
Cdd:PRK12393 344 LLHRAEGGadaTTVEDVVHWGTAGGARVLGLDAIGTLAVGQAADLAIYDLDDPRFFGLhdPAIAPVACGGPAPVKALLVN 423
|
410 420 430
....*....|....*....|....*....|
gi 497631771 413 GRLVVRDGThrlVP--DLAERMRDSVAALL 440
Cdd:PRK12393 424 GRPVVENGA---IPglDLAELRHDARAAVR 450
|
|
| PRK08203 |
PRK08203 |
hydroxydechloroatrazine ethylaminohydrolase; Reviewed |
21-440 |
1.88e-38 |
|
hydroxydechloroatrazine ethylaminohydrolase; Reviewed
Pssm-ID: 236184 [Multi-domain] Cd Length: 451 Bit Score: 144.61 E-value: 1.88e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497631771 21 GVLVEteDGRITSV--SEVDDPGGARRL---GGLVLPGMANAHSHAFHRALRGRTSAGKGTFWTWRDQMYKVAARLDPES 95
Cdd:PRK08203 25 GLVVE--GGRIVEVgpGGALPQPADEVFdarGHVVTPGLVNTHHHFYQTLTRALPAAQDAELFPWLTTLYPVWARLTPEM 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497631771 96 YHRLATAVFAEMALSGMTCVGEFHYLHhaPGGQRysdpnAMGAALAQAAADAGIRLTL----LDTCYLAGGFgKPVEGVQ 171
Cdd:PRK08203 103 VRVATQTALAELLLSGCTTSSDHHYLF--PNGLR-----DALDDQIEAAREIGMRFHAtrgsMSLGESDGGL-PPDSVVE 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497631771 172 lryTDGDVSAWADR-VDEFKPAGDH--VRVGAALHSVRAVPAEAIPGVVEWAGGADAPLHAHLSEQRAENEACLAAHGCT 248
Cdd:PRK08203 175 ---DEDAILADSQRlIDRYHDPGPGamLRIALAPCSPFSVSRELMRESAALARRLGVRLHTHLAETLDEEAFCLERFGMR 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497631771 249 PTQLLASHGALGESTTAVHATHLAPGDLPLLGGSGTGVCLCPTTEADLADGIGPASALAVAGSPLSVGSDGHSVIDQFAE 328
Cdd:PRK08203 252 PVDYLEDLGWLGPDVWLAHCVHLDDAEIARLARTGTGVAHCPCSNMRLASGIAPVRELRAAGVPVGLGVDGSASNDGSNL 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497631771 329 VQAVESYMRLSQETRG--NFTPADLVTMATASGHRALGWSDAGWIGAGARADLVAVGLDSARLAGV--PPEAVVSAAsAD 404
Cdd:PRK08203 332 IGEARQALLLQRLRYGpdAMTAREALEWATLGGARVLGRDDIGSLAPGKLADLALFDLDELRFAGAhdPVAALVLCG-PP 410
|
410 420 430
....*....|....*....|....*....|....*...
gi 497631771 405 DVRDVVVDGRLVVRDGTHRLV--PDLAERMRDSVAALL 440
Cdd:PRK08203 411 RADRVMVGGRWVVRDGQLTTLdlAALIARHRAAARRLA 448
|
|
| Amidohydro_1 |
pfam01979 |
Amidohydrolase family; This family of enzymes are a a large metal dependent hydrolase ... |
49-398 |
1.92e-27 |
|
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: 111.82 E-value: 1.92e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497631771 49 LVLPGMANAHSHAFHRALRGRTSAGKgtfwtwrdqmykvaarldpESYHRLATAVfAEMALSGMTCVGEFHYLHHapggq 128
Cdd:pfam01979 1 IVLPGLIDAHVHLEMGLLRGIPVPPE-------------------FAYEALRLGI-TTMLKSGTTTVLDMGATTS----- 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497631771 129 rysdPNAMGAALAQAAADAGIRLTLLDTCYLAGGFGKPVEGVQLRYTDGDVSawadrvdEFKPAGDHVRVGAALHSVRAV 208
Cdd:pfam01979 56 ----TGIEALLEAAEELPLGLRFLGPGCSLDTDGELEGRKALREKLKAGAEF-------IKGMADGVVFVGLAPHGAPTF 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497631771 209 PAEAIPGVVEWAGGADAPLHAHLSEQRAENEACLAAHGC-----TPTQLLASHGALGESTTA-VHATHLAPGDLPLLG-- 280
Cdd:pfam01979 125 SDDELKAALEEAKKYGLPVAIHALETKGEVEDAIAAFGGgiehgTHLEVAESGGLLDIIKLIlAHGVHLSPTEANLLAeh 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497631771 281 GSGTGVCLCPTTEADLADGIGPASALAVAGSPLSVGSDGHSVIDQFAEVQAVESYMRLSQETRGNFTPADLVTMATASGH 360
Cdd:pfam01979 205 LKGAGVAHCPFSNSKLRSGRIALRKALEDGVKVGLGTDGAGSGNSLNMLEELRLALELQFDPEGGLSPLEALRMATINPA 284
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 497631771 361 RALGWSD-AGWIGAGARADLVAVGLDS-ARLAGVPPEAVV 398
Cdd:pfam01979 285 KALGLDDkVGSIEVGKDADLVVVDLDPlAAFFGLKPDGNV 324
|
|
| PRK06038 |
PRK06038 |
N-ethylammeline chlorohydrolase; Provisional |
16-420 |
1.73e-26 |
|
N-ethylammeline chlorohydrolase; Provisional
Pssm-ID: 180363 [Multi-domain] Cd Length: 430 Bit Score: 110.61 E-value: 1.73e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497631771 16 GGPVPGVLVeTEDGRITSVSEvDDPGGARRL----GGLVLPGMANAHSHAFHRALRGrtSAGKGTFWTW-RDQMYKVAAR 90
Cdd:PRK06038 17 GDLKKGSVV-IEDGTITEVSE-STPGDADTVidakGSVVMPGLVNTHTHAAMTLFRG--YADDLPLAEWlNDHIWPAEAK 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497631771 91 LDPESYHRLATAVFAEMALSGMTCVGEFhYLHHAPGGQRYSDpnamgaalaqaaadAGIRLTLldtCYLAGGFGKPVEG- 169
Cdd:PRK06038 93 LTAEDVYAGSLLACLEMIKSGTTSFADM-YFYMDEVAKAVEE--------------SGLRAAL---SYGMIDLGDDEKGe 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497631771 170 VQLRYTDGDVSAWADRVDefkpagDHVRVGAALHSVRAVPAEAIPGVVEWAGGADAPLHAHLSEQRAENEACLAAHGCTP 249
Cdd:PRK06038 155 AELKEGKRFVKEWHGAAD------GRIKVMYGPHAPYTCSEEFLSKVKKLANKDGVGIHIHVLETEAELNQMKEQYGMCS 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497631771 250 TQLLASHGALGESTTAVHATHLAPGDLPLLGGSGTGVCLCPTTEADLADGIGPASALAVAGSPLSVGSDGHSV---IDQF 326
Cdd:PRK06038 229 VNYLDDIGFLGPDVLAAHCVWLSDGDIEILRERGVNVSHNPVSNMKLASGIAPVPKLLERGVNVSLGTDGCASnnnLDMF 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497631771 327 AEVQAVESYMRLSQETRGNFTPADLVTMATASGHRALGwSDAGWIGAGARADLVAVGLDSARLAGV--PPEAVVSAASAD 404
Cdd:PRK06038 309 EEMKTAALLHKVNTMDPTALPARQVLEMATVNGAKALG-INTGMLKEGYLADIIIVDMNKPHLTPVrdVPSHLVYSASGS 387
|
410
....*....|....*.
gi 497631771 405 DVRDVVVDGRLVVRDG 420
Cdd:PRK06038 388 DVDTTIVDGRILMEDY 403
|
|
| PRK09045 |
PRK09045 |
TRZ/ATZ family hydrolase; |
28-386 |
2.91e-25 |
|
TRZ/ATZ family hydrolase;
Pssm-ID: 236366 [Multi-domain] Cd Length: 443 Bit Score: 107.30 E-value: 2.91e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497631771 28 DGRITSVSEVDD------PGGARRLGGLVL-PGMANAHSHAFHRALRGrtSAGKGTFWTW-RDQMYKVAARLDPESYHRL 99
Cdd:PRK09045 35 DGRIVAILPRAEararyaAAETVELPDHVLiPGLINAHTHAAMSLLRG--LADDLPLMTWlQDHIWPAEGAWVSEEFVRD 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497631771 100 ATAV-FAEMALSGMTCVGEfHYLHHAPGGQRYSDpnamgaalaqaaadAGIR----LTLLD--TCYLAGGFGKPVEGVQL 172
Cdd:PRK09045 113 GTLLaIAEMLRGGTTCFND-MYFFPEAAAEAAHQ--------------AGMRaqigMPVLDfpTAWASDADEYLAKGLEL 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497631771 173 RytdgdvsawadrvDEFKpagDHVRVGAAL--HSVRAVPAEAIPGVVEWAGGADAPLHAHLSEQRAENEACLAAHGCTPT 250
Cdd:PRK09045 178 H-------------DQWR---HHPLISTAFapHAPYTVSDENLERIRTLAEQLDLPIHIHLHETAQEIADSLKQHGQRPL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497631771 251 QLLASHGALGESTTAVHATHLAPGDLPLLGGSGTGVCLCPTTEADLADGIGPASALAVAGSPLSVGSDG---HSVIDQFA 327
Cdd:PRK09045 242 ARLARLGLLGPRLIAVHMTQLTDAEIALLAETGCSVVHCPESNLKLASGFCPVAKLLQAGVNVALGTDGaasNNDLDLFG 321
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 497631771 328 EvqavesyMR----LSQETRGNFT--PADLV-TMATASGHRALGWSD-AGWIGAGARADLVAVGLDS 386
Cdd:PRK09045 322 E-------MRtaalLAKAVAGDATalPAHTAlRMATLNGARALGLDDeIGSLEPGKQADLVAVDLSG 381
|
|
| PRK06687 |
PRK06687 |
TRZ/ATZ family protein; |
21-420 |
1.30e-19 |
|
TRZ/ATZ family protein;
Pssm-ID: 180657 [Multi-domain] Cd Length: 419 Bit Score: 90.45 E-value: 1.30e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497631771 21 GVLVeTEDGRITSVSEvDDPGGARRL-------GGLVLPGMANAHSHAFHRALRGRTSAGKGTFWTwRDQMYKVAARLDP 93
Cdd:PRK06687 22 GILA-VKDSQIVYVGQ-DKPAFLEQAeqiidyqGAWIMPGLVNCHTHSAMTGLRGIRDDSNLHEWL-NDYIWPAESEFTP 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497631771 94 ESYHRLATAVFAEMALSGMTCVGEFHYLHHAPGGQRYSdpnamgaalaqAAADAGIRltlldtCYLAGG-FGKPVEGVQl 172
Cdd:PRK06687 99 DMTTNAVKEALTEMLQSGTTTFNDMYNPNGVDIQQIYQ-----------VVKTSKMR------CYFSPTlFSSETETTA- 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497631771 173 rYTDGDVSAWADRVDEFKpaGDHVRVGAALHSVRAVPAEAIPGVVEWAGGADAPLHAHLSEQRAENEACLAAHGCTPTQL 252
Cdd:PRK06687 161 -ETISRTRSIIDEILKYK--NPNFKVMVAPHSPYSCSRDLLEASLEMAKELNIPLHVHVAETKEESGIILKRYGKRPLAF 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497631771 253 LASHGALGESTTAVHATHLAPGDLPLLGGSGTGVCLCPTTEADLADGIGPASALAVAGSPLSVGSD---GHSVIDQFAEV 329
Cdd:PRK06687 238 LEELGYLDHPSVFAHGVELNEREIERLASSQVAIAHNPISNLKLASGIAPIIQLQKAGVAVGIATDsvaSNNNLDMFEEG 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497631771 330 QAVESYMRLSQETRGNFTPADLVTMATASGHRALGWSDA-GWIGAGARADLVAVGlDSARLAGVPPEAVVS----AASAD 404
Cdd:PRK06687 318 RTAALLQKMKSGDASQFPIETALKVLTIEGAKALGMENQiGSLEVGKQADFLVIQ-PQGKIHLQPQENMLShlvyAVKSS 396
|
410
....*....|....*.
gi 497631771 405 DVRDVVVDGRLVVRDG 420
Cdd:PRK06687 397 DVDDVYIAGEQVVKQG 412
|
|
| PRK07228 |
PRK07228 |
5'-deoxyadenosine deaminase; |
24-440 |
4.05e-18 |
|
5'-deoxyadenosine deaminase;
Pssm-ID: 180895 [Multi-domain] Cd Length: 445 Bit Score: 86.21 E-value: 4.05e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497631771 24 VETEDGRITSVSEVDDPGGARRL----GGLVLPGMANAHSHAFHRALRGRtsAGKGTFWTW-RDQMYKVAARLDPESYHR 98
Cdd:PRK07228 24 VLIEDDRIAAVGDRLDLEDYDDHidatGKVVIPGLIQGHIHLCQTLFRGI--ADDLELLDWlKDRIWPLEAAHDAESMYY 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497631771 99 LATAVFAEMALSGMTCVGEFHYLHHApggqrysdpnamgAALAQAAADAGIRLtLLDTCYLAGGFGKPvEGVQlRYTDGD 178
Cdd:PRK07228 102 SALLGIGELIESGTTTIVDMESVHHT-------------DSAFEAAGESGIRA-VLGKVMMDYGDDVP-EGLQ-EDTEAS 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497631771 179 VSAWADRVDEFKPAGD-HVRVGAALHSVRAVPAEAIPGVVEWAGGADAPLHAHLSEQRAENEACLAAHGCTPTQLLASHG 257
Cdd:PRK07228 166 LAESVRLLEKWHGADNgRIRYAFTPRFAVSCTEELLRGVRDLADEYGVRIHTHASENRGEIETVEEETGMRNIHYLDEVG 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497631771 258 ALGESTTAVHATHLAPGDLPLLGGSGTGVCLCPTTEADLADGIGPASALAVAGSPLSVGSDG---HSVIDQFAEvqaves 334
Cdd:PRK07228 246 LTGEDLILAHCVWLDEEEREILAETGTHVTHCPSSNLKLASGIAPVPDLLERGINVALGADGapcNNTLDPFTE------ 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497631771 335 yMRLS------QETRGNFTPADLV-TMATASGHRALGWSD-AGWIGAGARADLVAVGLDSARLAGVPPEAVVS----AAS 402
Cdd:PRK07228 320 -MRQAaliqkvDRLGPTAMPARTVfEMATLGGAKAAGFEDeIGSLEEGKKADLAILDLDGLHATPSHGVDVLShlvyAAH 398
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 497631771 403 ADDVRDVVVDGRLVVRDGTHRLV--PDLAERMRDSVAALL 440
Cdd:PRK07228 399 GSDVETTMVDGKIVMEDGELTTIdaDAVRREANRSIKRLL 438
|
|
| Met_dep_hydrolase_D |
cd01312 |
Metallo-dependent hydrolases, subgroup D is part of the superfamily of metallo-dependent ... |
47-384 |
2.30e-15 |
|
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: 77.10 E-value: 2.30e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497631771 47 GGLVLPGMANAHSHAFHRALRgrTSAGKGTFWTWRDQMYKVAARLDPESYHRLATAVFAEMALSGMTCVGEFhylhhapg 126
Cdd:cd01312 26 NGVLLPGLINAHTHLEFSANV--AQFTYGRFRAWLLSVINSRDELLKQPWEEAIRQGIRQMLESGTTSIGAI-------- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497631771 127 gqrysdpnamgaalaqaaADAGIRLTLLDTCYLAGGFGKPVEG---VQLRYTDGDVSAWADRVDEFKpaGDHVRVGAALH 203
Cdd:cd01312 96 ------------------SSDGSLLPALASSGLRGVFFNEVIGsnpSAIDFKGETFLERFKRSKSFE--SQLFIPAISPH 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497631771 204 SVRAVPAEAIPGVVEWAGGADAPLHAHLSEQRAENEACLAAHG------------------CTPTQLLASHGALGESTTA 265
Cdd:cd01312 156 APYSVHPELAQDLIDLAKKLNLPLSTHFLESKEEREWLEESKGwfkhfwesflklpkpkklATAIDFLDMLGGLGTRVSF 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497631771 266 VHATHLAPGDLPLLGGSGTGVCLCPTTEADLADGIGPASALAVAGSPLSVGSDGHSVIDQFAEVQAVESYMRLSQETRGN 345
Cdd:cd01312 236 VHCVYANLEEAEILASRGASIALCPRSNRLLNGGKLDVSELKKAGIPVSLGTDGLSSNISLSLLDELRALLDLHPEEDLL 315
|
330 340 350
....*....|....*....|....*....|....*....
gi 497631771 346 FTPADLVTMATASGHRALGWsDAGWIGAGARADLVAVGL 384
Cdd:cd01312 316 ELASELLLMATLGGARALGL-NNGEIEAGKRADFAVFEL 353
|
|
| PRK06151 |
PRK06151 |
N-ethylammeline chlorohydrolase; Provisional |
224-421 |
4.87e-15 |
|
N-ethylammeline chlorohydrolase; Provisional
Pssm-ID: 180428 [Multi-domain] Cd Length: 488 Bit Score: 77.00 E-value: 4.87e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497631771 224 DAPLHAHLSEQRAENEACLAAHGCTPTQLLASHGALGESTTAVHATHL---------APGDLPLLGGSGTGVCLCPTTEA 294
Cdd:PRK06151 234 GCPVRLHCAQGVLEVETVRRLHGTTPLEWLADVGLLGPRLLIPHATYIsgsprlnysGGDDLALLAEHGVSIVHCPLVSA 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497631771 295 DLADGIGPASALAVAGSPLSVGSDGHSViDQFAEVQAVESYMRLSQETRGNFTPADLVTMATASGHRALGWSDAGWIGAG 374
Cdd:PRK06151 314 RHGSALNSFDRYREAGINLALGTDTFPP-DMVMNMRVGLILGRVVEGDLDAASAADLFDAATLGGARALGRDDLGRLAPG 392
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 497631771 375 ARADLVAVGLDSARLAGV--PPEAVVSAASADDVRDVVVDGRLVVRDGT 421
Cdd:PRK06151 393 AKADIVVFDLDGLHMGPVfdPIRTLVTGGSGRDVRAVFVDGRVVMEDGR 441
|
|
| PRK08393 |
PRK08393 |
N-ethylammeline chlorohydrolase; Provisional |
216-420 |
1.02e-12 |
|
N-ethylammeline chlorohydrolase; Provisional
Pssm-ID: 181411 [Multi-domain] Cd Length: 424 Bit Score: 69.44 E-value: 1.02e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497631771 216 VVEWAGGADAPLHAHLSEQRAENEACLAAHGCTPTQLLASHGALGESTTAVHATHLAPGDLPLLGGSGTGVCLCPTTEAD 295
Cdd:PRK08393 194 VREKAREWNKLITIHLSETMDEIKQIREKYGKSPVVLLDEIGFLNEDVIAAHGVWLSSRDIRILASAGVTVAHNPASNMK 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497631771 296 LADGIGPASALAVAGSPLSVGSDG---HSVIDQFAEvqavesyMRLSQ--ETRGNFTPA-----DLVTMATASGHRALGW 365
Cdd:PRK08393 274 LGSGVMPLRKLLNAGVNVALGTDGaasNNNLDMLRE-------MKLAAllHKVHNLDPTiadaeTVFRMATQNGAKALGL 346
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 497631771 366 sDAGWIGAGARADLVAVGLDSARLAGV--PPEAVVSAASADDVRDVVVDGRLVVRDG 420
Cdd:PRK08393 347 -KAGVIKEGYLADIAVIDFNRPHLRPInnPISHLVYSANGNDVETTIVDGKIVMLDG 402
|
|
| HutI |
COG1228 |
Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport ... |
16-382 |
7.35e-11 |
|
Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440841 [Multi-domain] Cd Length: 386 Bit Score: 63.44 E-value: 7.35e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497631771 16 GGPVPGVLVETEDGRITSV---SEVDDPGGARRL---GGLVLPGMANAHSHAFHRALRGRTSAGKGTFWTWRDQMYKVAA 89
Cdd:COG1228 23 GGVIENGTVLVEDGKIAAVgpaADLAVPAGAEVIdatGKTVLPGLIDAHTHLGLGGGRAVEFEAGGGITPTVDLVNPADK 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497631771 90 RLDpesyhrlatavfaEMALSGMTCVgefhylhHAPGGqrYSDPNAMGAALAQAAADAGIRLtLLDTCYLAGGFGKPVEG 169
Cdd:COG1228 103 RLR-------------RALAAGVTTV-------RDLPG--GPLGLRDAIIAGESKLLPGPRV-LAAGPALSLTGGAHARG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497631771 170 VQlrytdgdvsAWADRVDEFKPAG-DHVRVGAAlHSVRAVPAEAIPGVVEWAGGADAPLHAHlseqraeneaclaAHGCT 248
Cdd:COG1228 160 PE---------EARAALRELLAEGaDYIKVFAE-GGAPDFSLEELRAILEAAHALGLPVAAH-------------AHQAD 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497631771 249 PTQLLASHGAlgesTTAVHATHLAPGDLPLLGGSGTgVCLCPTTEADLADGIG------------------PASALAVAG 310
Cdd:COG1228 217 DIRLAVEAGV----DSIEHGTYLDDEVADLLAEAGT-VVLVPTLSLFLALLEGaaapvaakarkvreaalaNARRLHDAG 291
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 497631771 311 SPLSVGSDGHSVIDQFAEVQAVESYMrlsqeTRGNFTPADLVTMATASGHRALGWSD-AGWIGAGARADLVAV 382
Cdd:COG1228 292 VPVALGTDAGVGVPPGRSLHRELALA-----VEAGLTPEEALRAATINAAKALGLDDdVGSLEPGKLADLVLL 359
|
|
| GDEase |
cd01303 |
Guanine deaminase (GDEase). Guanine deaminase is an aminohydrolase responsible for the ... |
224-384 |
3.47e-10 |
|
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: 61.52 E-value: 3.47e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497631771 224 DAPLHAHLSEQRAENEACLAAH-GCTP-TQLLASHGALGESTTAVHATHLAPGDLPLLGGSGTGVCLCPTTEADLADGIG 301
Cdd:cd01303 222 DLHIQTHISENLDEIAWVKELFpGARDyLDVYDKYGLLTEKTVLAHCVHLSEEEFNLLKERGASVAHCPTSNLFLGSGLF 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497631771 302 PASALAVAGSPLSVGSD---GHS-----VIDQFAEVQAVESYmRLSQETRgnFTPADLVTMATASGHRALGWSD-AGWIG 372
Cdd:cd01303 302 DVRKLLDAGIKVGLGTDvggGTSfsmldTLRQAYKVSRLLGY-ELGGHAK--LSPAEAFYLATLGGAEALGLDDkIGNFE 378
|
170
....*....|..
gi 497631771 373 AGARADLVAVGL 384
Cdd:cd01303 379 VGKEFDAVVIDP 390
|
|
| PRK07203 |
PRK07203 |
putative aminohydrolase SsnA; |
47-319 |
1.44e-08 |
|
putative aminohydrolase SsnA;
Pssm-ID: 235963 [Multi-domain] Cd Length: 442 Bit Score: 56.48 E-value: 1.44e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497631771 47 GGLVLPGMANAHSH---AFHRALRGRTSAGKGTFWTWRDQMYKVAARLDPESYHRLATAVFAEMALSGMTCVgefhYLHH 123
Cdd:PRK07203 54 GKLIMPGLINSHNHiysGLARGMMANIPPPPDFISILKNLWWRLDRALTLEDVYYSALICSLEAIKNGVTTV----FDHH 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497631771 124 ApggqrysDPNAMG---AALAQAAADAGIRLTLldtCYLAG---GFGKPVEGVQlrytdgDVSAWADRVDEFKpaGDHVR 197
Cdd:PRK07203 130 A-------SPNYIGgslFTIADAAKKVGLRAML---CYETSdrdGEKELQEGVE------ENIRFIKHIDEAK--DDMVE 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497631771 198 VGAALHSVRAVPAEAIPGVVEWAGGADAPLHAHLSEQRAENEACLAAHGCTPTQLLASHGALGESTTAVHATHLAPGDLP 277
Cdd:PRK07203 192 AMFGLHASFTLSDATLEKCREAVKETGRGYHIHVAEGIYDVSDSHKKYGKDIVERLADFGLLGEKTLAAHCIYLSDEEID 271
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 497631771 278 LLGGSGTGVCLCPTTEADLADGIGPASALAVAGSPLSVGSDG 319
Cdd:PRK07203 272 LLKETDTFVVHNPESNMGNAVGYNPVLEMIKNGILLGLGTDG 313
|
|
| PRK08204 |
PRK08204 |
hypothetical protein; Provisional |
17-438 |
3.56e-08 |
|
hypothetical protein; Provisional
Pssm-ID: 181288 [Multi-domain] Cd Length: 449 Bit Score: 55.39 E-value: 3.56e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497631771 17 GPVPGVLVETEDGRITSVSEVDDPGGARRL---GGLVLPGMANAHSHAFHRALRGRtsAGKGTFWTWRDQMY-KVAARLD 92
Cdd:PRK08204 19 GDLPRGDILIEGDRIAAVAPSIEAPDAEVVdarGMIVMPGLVDTHRHTWQSVLRGI--GADWTLQTYFREIHgNLGPMFR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497631771 93 PESYHRlATAVFAEMAL-SGMTCVGEFHYLHHAPggqRYSDpnamgaALAQAAADAGIRLTLldtcylagGFGKPveGVQ 171
Cdd:PRK08204 97 PEDVYI-ANLLGALEALdAGVTTLLDWSHINNSP---EHAD------AAIRGLAEAGIRAVF--------AHGSP--GPS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497631771 172 LRYTDGDVSAWADRVDE-----FKPAGDHVRVGAALHSvravPAEAIPGVV--EWAGGA--DAPLHAHLSeqraeneacL 242
Cdd:PRK08204 157 PYWPFDSVPHPREDIRRvkkryFSSDDGLLTLGLAIRG----PEFSSWEVAraDFRLARelGLPISMHQG---------F 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497631771 243 AAHGCTP--TQLLASHGALGESTTAVHATHLAPGDLPLLGGSGTGVCLCPTTEADLADGIGPASALAVAGSPLSVGSDGH 320
Cdd:PRK08204 224 GPWGATPrgVEQLHDAGLLGPDLNLVHGNDLSDDELKLLADSGGSFSVTPEIEMMMGHGYPVTGRLLAHGVRPSLGVDVV 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497631771 321 SVI--DQFAEVQAVESYMR------LSQET-----RGNFTPADLVTMATASGHRALGWSD-AGWIGAGARADLVAVGLDS 386
Cdd:PRK08204 304 TSTggDMFTQMRFALQAERardnavHLREGgmpppRLTLTARQVLEWATIEGARALGLEDrIGSLTPGKQADLVLIDATD 383
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 497631771 387 ARLAGV--PPEAVVSAASADDVRDVVVDGRLVVRDGTHrLVPDLAERMRDSVAA 438
Cdd:PRK08204 384 LNLAPVhdPVGAVVQSAHPGNVDSVMVAGRAVKRNGKL-LGVDLERLRRLAAAS 436
|
|
| PRK09228 |
PRK09228 |
guanine deaminase; Provisional |
227-382 |
7.77e-07 |
|
guanine deaminase; Provisional
Pssm-ID: 236419 [Multi-domain] Cd Length: 433 Bit Score: 50.96 E-value: 7.77e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497631771 227 LHAHLSEQRAENEACLAAH-GCTP-TQLLASHGALGESTTAVHATHLAPGDLPLLGGSGTGVCLCPTTEADLADGIGPAS 304
Cdd:PRK09228 228 IQTHLSENLDEIAWVKELFpEARDyLDVYERYGLLGPRAVFAHCIHLEDRERRRLAETGAAIAFCPTSNLFLGSGLFDLK 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497631771 305 ALAVAGSPLSVGSD--GHSVIDQFAEVQAVESYMRLSQEtrgNFTPADLVTMATASGHRALGWSDA-GWIGAGARADLVA 381
Cdd:PRK09228 308 RADAAGVRVGLGTDvgGGTSFSMLQTMNEAYKVQQLQGY---RLSPFQAFYLATLGGARALGLDDRiGNLAPGKEADFVV 384
|
.
gi 497631771 382 V 382
Cdd:PRK09228 385 L 385
|
|
| PRK15493 |
PRK15493 |
bifunctional S-methyl-5'-thioadenosine deaminase/S-adenosylhomocysteine deaminase; |
23-420 |
1.89e-06 |
|
bifunctional S-methyl-5'-thioadenosine deaminase/S-adenosylhomocysteine deaminase;
Pssm-ID: 185390 [Multi-domain] Cd Length: 435 Bit Score: 50.06 E-value: 1.89e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497631771 23 LVETEDGRITSVSEVDDPGGARrlGGLVLPGMANAHSHAFHRALRGRTSAGKGTFWTwRDQMYKVAARLDPEsyhrLATA 102
Cdd:PRK15493 32 IIDVNSGEFASDFEVDEVIDMK--GKWVLPGLVNTHTHVVMSLLRGIGDDMLLQPWL-ETRIWPLESQFTPE----LAVA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497631771 103 V----FAEMALSGMTCVGEFhylhhapggqrYSDPNAMGAALAQAAADAGIRLTLLDTCYLAGGFGKPVEGVQlrytdgD 178
Cdd:PRK15493 105 StelgLLEMVKSGTTSFSDM-----------FNPIGVDQDAIMETVSRSGMRAAVSRTLFSFGTKEDEKKAIE------E 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497631771 179 VSAWADRvdeFKPAGDHVRVGAALHSVRAVPAEAIPGVVEWAGGADAPLHAHLSEQRAENEACLAAHGCTPTQLLASHGA 258
Cdd:PRK15493 168 AEKYVKR---YYNESGMLTTMVAPHSPYTCSTELLEECARIAVENQTMVHIHLSETEREVRDIEAQYGKRPVEYAASCGL 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497631771 259 LGESTTAVHATHLAPGDLPLLGGSGTGVCLCPTTEADLADGIGPASALAVAGSPLSVGSD---GHSVIDQFAEVQAVESY 335
Cdd:PRK15493 245 FKRPTVIAHGVVLNDNERAFLAEHDVRVAHNPNSNLKLGSGIANVKAMLEAGIKVGIATDsvaSNNNLDMFEEMRIATLL 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497631771 336 MRLSQETRGNFTPADLVTMATASGHRALGWSDAGWIGAGARADLVAVglDSARLAGV-PPEAVVS----AASADDVRDVV 410
Cdd:PRK15493 325 QKGIHQDATALPVETALTLATKGAAEVIGMKQTGSLEVGKCADFITI--DPSNKPHLqPADEVLShlvyAASGKDISDVI 402
|
410
....*....|
gi 497631771 411 VDGRLVVRDG 420
Cdd:PRK15493 403 INGKRVVWNG 412
|
|
| PRK06380 |
PRK06380 |
metal-dependent hydrolase; Provisional |
201-393 |
5.12e-06 |
|
metal-dependent hydrolase; Provisional
Pssm-ID: 180548 [Multi-domain] Cd Length: 418 Bit Score: 48.34 E-value: 5.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497631771 201 ALHSVRAVPAEAIPGVVEWAGGADAPLHAHLSEQRAENEACLAAHGCTPTQLLASHGALGESTTAVHATHLAPGDLPLLG 280
Cdd:PRK06380 176 GVQGIYVANDETYLKAKEIAEKYDTIMHMHLSETRKEVYDHVKRTGERPVEHLEKIGFLNSKLIAAHCVWATYHEIKLLS 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497631771 281 GSGTGVCLCPTTEADLAD-GIGPASALAVAGSPLSVGSD---GHSVIDQFAEvqavesyMRLSQETRGNF-------TPA 349
Cdd:PRK06380 256 KNGVKVSWNSVSNFKLGTgGSPPIPEMLDNGINVTIGTDsngSNNSLDMFEA-------MKFSALSVKNErwdasiiKAQ 328
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 497631771 350 DLVTMATASGHRALGWsDAGWIGAGARADLVAvgLDSARLAGVP 393
Cdd:PRK06380 329 EILDFATINAAKALEL-NAGSIEVGKLADLVI--LDARAPNMIP 369
|
|
| Imidazolone-5PH |
cd01296 |
Imidazolonepropionase/imidazolone-5-propionate hydrolase (Imidazolone-5PH) catalyzes the third ... |
241-380 |
1.44e-05 |
|
Imidazolonepropionase/imidazolone-5-propionate hydrolase (Imidazolone-5PH) catalyzes the third step in the histidine degradation pathway, the hydrolysis of (S)-3-(5-oxo-4,5-dihydro-3H-imidazol-4-yl)propanoate to N-formimidoyl-L-glutamate. In bacteria, the enzyme is part of histidine utilization (hut) operon.
Pssm-ID: 238621 [Multi-domain] Cd Length: 371 Bit Score: 46.87 E-value: 1.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497631771 241 CLAAHGCTptQLLASHGALgestTAVHATHLAPGDLPLLGGSGTGVCLCPTTEADLADGIGPASALAVAGSPLSVGSD-- 318
Cdd:cd01296 215 ELSNIGGA--ELAAELGAL----SADHLEHTSDEGIAALAEAGTVAVLLPGTAFSLRETYPPARKLIDAGVPVALGTDfn 288
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 497631771 319 -GHSVID--QFAEVQAVeSYMRLsqetrgnfTPADLVTMATASGHRALGWS-DAGWIGAGARADLV 380
Cdd:cd01296 289 pGSSPTSsmPLVMHLAC-RLMRM--------TPEEALTAATINAAAALGLGeTVGSLEVGKQADLV 345
|
|
| PRK07213 |
PRK07213 |
chlorohydrolase; Provisional |
266-398 |
4.08e-05 |
|
chlorohydrolase; Provisional
Pssm-ID: 235969 [Multi-domain] Cd Length: 375 Bit Score: 45.41 E-value: 4.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497631771 266 VHATHLAPGDLPLLGGSGTGVCLCPTTEADLADGIGPASALAVAGSPLSVGSDG--HSVIDQFAEVQAVESYMrlsqetr 343
Cdd:PRK07213 232 VHATHPSNDDLELLKENNIPVVVCPRANASFNVGLPPLNEMLEKGILLGIGTDNfmANSPSIFREMEFIYKLY------- 304
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 497631771 344 gNFTPADLVTMATASGHRALGWSDAGWIGAGARADLVAVGLDSARLAGVPPEAVV 398
Cdd:PRK07213 305 -HIEPKEILKMATINGAKILGLINVGLIEEGFKADFTFIKPTNIKFSKNPYASII 358
|
|
| metallo-dependent_hydrolases |
cd01292 |
Superfamily of metallo-dependent hydrolases (also called amidohydrolase superfamily) is a ... |
56-362 |
2.69e-04 |
|
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: 42.71 E-value: 2.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497631771 56 NAHSHAFHRALRGRtsagkgtfwtWRDQMYKVAARLDPESYHRLATAVFAEMALSGMTCVGEFHYLHHAPggqrySDPNA 135
Cdd:cd01292 3 DTHVHLDGSALRGT----------RLNLELKEAEELSPEDLYEDTLRALEALLAGGVTTVVDMGSTPPPT-----TTKAA 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497631771 136 MGAALAQAAADAGIRLTLLDTCYLAGGFGKPVEGVQLRytdgdvsawadrvDEFKPAGDHVRVGAALHS---VRAVPAEA 212
Cdd:cd01292 68 IEAVAEAARASAGIRVVLGLGIPGVPAAVDEDAEALLL-------------ELLRRGLELGAVGLKLAGpytATGLSDES 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497631771 213 IPGVVEWAGGADAPLHAHLSEQRAENEAclaahgctpTQLLASHGALGESTTAVHATHLAPGDLPLLGGSGTGVCLCPTT 292
Cdd:cd01292 135 LRRVLEEARKLGLPVVIHAGELPDPTRA---------LEDLVALLRLGGRVVIGHVSHLDPELLELLKEAGVSLEVCPLS 205
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 497631771 293 EADLADGIGPASALAVA---GSPLSVGSDGHSV---IDQFAEVQAvesymrLSQETRGNFTPADLVTMATASGHRA 362
Cdd:cd01292 206 NYLLGRDGEGAEALRRLlelGIRVTLGTDGPPHplgTDLLALLRL------LLKVLRLGLSLEEALRLATINPARA 275
|
|
| Met_dep_hydrolase_A |
cd01299 |
Metallo-dependent hydrolases, subgroup A is part of the superfamily of metallo-dependent ... |
309-382 |
1.24e-03 |
|
Metallo-dependent hydrolases, subgroup A is part of the superfamily of metallo-dependent hydrolases, a large group of proteins that show conservation in their 3-dimensional fold (TIM barrel) and in details of their active site. The vast majority of the members have a conserved metal binding site, involving four histidines and one aspartic acid residue. In the common reaction mechanism, the metal ion (or ions) deprotonate a water molecule for a nucleophilic attack on the substrate. The function of this subgroup is unknown.
Pssm-ID: 238624 [Multi-domain] Cd Length: 342 Bit Score: 40.74 E-value: 1.24e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 497631771 309 AGSPLSVGSD-GHSVIDQfaEVQAVESYMRlsqeTRGNFTPADLVTMATASGHRALGWSD-AGWIGAGARADLVAV 382
Cdd:cd01299 262 AGVKIAFGTDaGFPVPPH--GWNARELELL----VKAGGTPAEALRAATANAAELLGLSDeLGVIEAGKLADLLVV 331
|
|
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