|
Name |
Accession |
Description |
Interval |
E-value |
| D-HYD |
cd01314 |
D-hydantoinases (D-HYD) also called dihydropyrimidases (DHPase) and related proteins; DHPases ... |
7-496 |
0e+00 |
|
D-hydantoinases (D-HYD) also called dihydropyrimidases (DHPase) and related proteins; DHPases are a family of enzymes that catalyze the reversible hydrolytic ring opening of the amide bond in five- or six-membered cyclic diamides, like dihydropyrimidine or hydantoin. The hydrolysis of dihydropyrimidines is the second step of reductive catabolism of pyrimidines in human. The hydrolysis of 5-substituted hydantoins in microorganisms leads to enantiomerically pure N-carbamyl amino acids, which are used for the production of antibiotics, peptide hormones, pyrethroids, and pesticides. HYDs are classified depending on their stereoselectivity. This family also includes collapsin response regulators (CRMPs), cytosolic proteins involved in neuronal differentiation and axonal guidance which have strong homology to DHPases, but lack most of the active site residues.
Pssm-ID: 238639 [Multi-domain] Cd Length: 447 Bit Score: 722.08 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530388815 7 LLIRGGRVVNDDFSEVADVLVEDGVVRALGHDLLPPGGApaglRVLDAAGKLVLPGGIDTHTHMQFPFMGSRSIDDFHQG 86
Cdd:cd01314 1 LIIKNGTIVTADGSFKADILIEDGKIVAIGPNLEAPGGV----EVIDATGKYVLPGGIDPHTHLELPFMGTVTADDFESG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530388815 87 TKAALSGGTTMIIDFAIPQKGGSLIEAFETWRSWADPKVCCDYSLHVAVTWWSDQVKEEMKILVqDKGVNSFKMFMAYKD 166
Cdd:cd01314 77 TRAAAAGGTTTIIDFAIPNKGQSLLEAVEKWRGKADGKSVIDYGFHMIITDWTDSVIEELPELV-KKGISSFKVFMAYKG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530388815 167 LYMVTDLELYEAFSRCKEIGAIAQVHAENGDLIAEGAKKMLALGITGPEGHELCRPEAVEAEATLRAITIASAVNCPLYI 246
Cdd:cd01314 156 LLMVDDEELLDVLKRAKELGALVMVHAENGDVIAELQKKLLAQGKTGPEYHALSRPPEVEAEATARAIRLAELAGAPLYI 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530388815 247 VHVMSKSAAKVIADARRDGKVVYGEPIAASLGTDGTHYWnKEWHHAAHHVMGPPLRPDpSTPDFLMNLLANDDLTTTGTD 326
Cdd:cd01314 236 VHVSSKEAADEIARARKKGLPVYGETCPQYLLLDDSDYW-KDWFEGAKYVCSPPLRPK-EDQEALWDGLSSGTLQTVGSD 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530388815 327 NCTFNTCQKALGKDDFTKIPNGVNGVEDRMSVIWEKGVHSGKMDENRFVAVTSTNAAKIFNLYPRKGRIAVGSDADIVIW 406
Cdd:cd01314 314 HCPFNFAQKARGKDDFTKIPNGVPGVETRMPLLWSEGVAKGRITLEKFVELTSTNPAKIFGLYPRKGTIAVGSDADLVIW 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530388815 407 DPKgtrgcrscvafsdngsvyktnmnlplqclanarvhmEERTISAKTHHQAVNFNIFEGMVCHGVPLVTISRGKVVYEA 486
Cdd:cd01314 394 DPN------------------------------------AEKTISADTHHHNVDYNIFEGMKVKGWPVVTISRGKVVVED 437
|
490
....*....|
gi 530388815 487 GVFSVTAGDG 496
Cdd:cd01314 438 GELVGEKGSG 447
|
|
| D-hydantoinase |
TIGR02033 |
D-hydantoinase; This model represents the D-hydantoinase (dihydropyrimidinase) which primarily ... |
7-501 |
0e+00 |
|
D-hydantoinase; This model represents the D-hydantoinase (dihydropyrimidinase) which primarily converts 5,6-dihydrouracil to 3-ureidopropanoate but also acts on dihydrothymine and hydantoin. The enzyme is a metalloenzyme.
Pssm-ID: 273937 [Multi-domain] Cd Length: 454 Bit Score: 635.20 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530388815 7 LLIRGGRVVNDDFSEVADVLVEDGVVRALGHDLLPPGGApaglRVLDAAGKLVLPGGIDTHTHMQFPFMGSRSIDDFHQG 86
Cdd:TIGR02033 1 LLIKGGTVVNADDVFQADVLIEGGKIVAVGDNLIPPDAV----EVIDATGKYVLPGGIDVHTHLEMPFGGTTTADDFFTG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530388815 87 TKAALSGGTTMIIDFAIPQKGGSLIEAFETWRSWADPKVCCDYSLHVAVTWWSDQVKEEMKILVQDKGVNSFKMFMAYKD 166
Cdd:TIGR02033 77 TKAAAAGGTTTIIDFVVPEKGSSLTEALETWHEKAEGKSVIDYGFHMDITHWNDSVLEEHIPEVKEEGINSFKVFMAYKN 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530388815 167 LYMVTDLELYEAFSRCKEIGAIAQVHAENGDLIAEGAKKMLALGITGPEGHELCRPEAVEAEATLRAITIASAVNCPLYI 246
Cdd:TIGR02033 157 LLMVDDEELFEILKRLKELGALLQVHAENGDIIAELQARMLAQGITGPEYHALSRPPELEAEAVARAITLAALADAPLYV 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530388815 247 VHVMSKSAAKVIADARRDGKVVYGEPIAASLGTDGTHYWnKEWHHAAHHVMGPPLRpDPSTPDFLMNLLANDDLTTTGTD 326
Cdd:TIGR02033 237 VHVSTKDAADEIAQARKKGQPVFGETCPQYLVLDDTHYD-KPGFEGAKYVCSPPLR-EPEDQDALWSALSSGALQTVGSD 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530388815 327 NCTFNTCQK-ALGKDDFTKIPNGVNGVEDRMSVIWEKGVHSGKMDENRFVAVTSTNAAKIFNLYPRKGRIAVGSDADIVI 405
Cdd:TIGR02033 315 HCTFNFAQKkAIGKDDFTKIPNGGPGVEERMSLLFDEGVAKGRITLEKFVEVTSTNPAKIFNLYPRKGTIAVGSDADIVI 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530388815 406 WDPKGTrgcrscvafsdngsvyktnmnlplqclanarvhmeeRTISAKTHHQAVNFNIFEGMVCHGVPLVTISRGKVVYE 485
Cdd:TIGR02033 395 WDPNRT------------------------------------TVISAETHHSNADYNPFEGFKVRGAPVSVLSRGRVVVE 438
|
490
....*....|....*.
gi 530388815 486 AGVFSVTAGDGKFIPR 501
Cdd:TIGR02033 439 DGQLVGTAGAGRFVKR 454
|
|
| PRK08323 |
PRK08323 |
phenylhydantoinase; Validated |
6-508 |
0e+00 |
|
phenylhydantoinase; Validated
Pssm-ID: 236240 [Multi-domain] Cd Length: 459 Bit Score: 631.82 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530388815 6 RLLIRGGRVVNDDFSEVADVLVEDGVVRALGHDllppggapAGLRVLDAAGKLVLPGGIDTHTHMQFPFMGSRSIDDFHQ 85
Cdd:PRK08323 2 STLIKNGTVVTADDTYKADVLIEDGKIAAIGAN--------LGDEVIDATGKYVMPGGIDPHTHMEMPFGGTVSSDDFET 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530388815 86 GTKAALSGGTTMIIDFAIPQKGGSLIEAFETWRSWADPKVCCDYSLHVAVTWWSDQVKEEMKILVqDKGVNSFKMFMAYK 165
Cdd:PRK08323 74 GTRAAACGGTTTIIDFALQPKGQSLREALEAWHGKAAGKAVIDYGFHMIITDWNEVVLDEMPELV-EEGITSFKLFMAYK 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530388815 166 DLYMVTDLELYEAFSRCKEIGAIAQVHAENGDLIAEGAKKMLALGITGPEGHELCRPEAVEAEATLRAITIASAVNCPLY 245
Cdd:PRK08323 153 GALMLDDDELLRALQRAAELGALPMVHAENGDAIAYLQAKLLAEGKTGPEYHALSRPPEVEGEATNRAIMLAELAGAPLY 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530388815 246 IVHVMSKSAAKVIADARRDGKVVYGEPIAASLGTDGTHYWNKEWHHAAHHVMGPPLRPDPSTpDFLMNLLANDDLTTTGT 325
Cdd:PRK08323 233 IVHVSCKEALEAIRRARARGQRVFGETCPQYLLLDESEYDGPDWFEGAKYVMSPPLRDKEHQ-DALWRGLQDGDLQVVAT 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530388815 326 DNCTFNTCQKA-LGKDDFTKIPNGVNGVEDRMSVIWEKGVHSGKMDENRFVAVTSTNAAKIFNLYPRKGRIAVGSDADIV 404
Cdd:PRK08323 312 DHCPFCFEQKKqLGRGDFTKIPNGTPGVEDRMPLLFSEGVMTGRITLNRFVELTSTNPAKIFGLYPRKGTIAVGADADIV 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530388815 405 IWDPKGTrgcrscvafsdngsvyktnmnlplqclanarvhmeeRTISAKTHHQAVNFNIFEGMVCHGVPLVTISRGKVVY 484
Cdd:PRK08323 392 IWDPNAT------------------------------------KTISASTLHSNVDYNPYEGFEVTGWPVTTLSRGEVVV 435
|
490 500
....*....|....*....|....
gi 530388815 485 EAGVFSVTAGDGKFIPRKPFAEYI 508
Cdd:PRK08323 436 EDGEFRGKAGHGRFLKRKPFQAVV 459
|
|
| PLN02942 |
PLN02942 |
dihydropyrimidinase |
1-530 |
0e+00 |
|
dihydropyrimidinase
Pssm-ID: 178530 Cd Length: 486 Bit Score: 609.92 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530388815 1 MAAPSRLLIRGGRVVNDDFSEVADVLVEDGVVRALGHDLlppgGAPAGLRVLDAAGKLVLPGGIDTHTHMQFPFMGSRSI 80
Cdd:PLN02942 1 GASSTKILIKGGTVVNAHHQELADVYVEDGIIVAVAPNL----KVPDDVRVIDATGKFVMPGGIDPHTHLAMPFMGTETI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530388815 81 DDFHQGTKAALSGGTTMIIDFAIPQKGgSLIEAFETWRSWADpKVCCDYSLHVAVTWWSDQVKEEMKILVQDKGVNSFKM 160
Cdd:PLN02942 77 DDFFSGQAAALAGGTTMHIDFVIPVNG-NLLAGYEAYEKKAE-KSCMDYGFHMAITKWDDTVSRDMETLVKEKGINSFKF 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530388815 161 FMAYKDLYMVTDLELYEAFSRCKEIGAIAQVHAENGDLIAEGAKKMLALGITGPEGHELCRPEAVEAEATLRAITIASAV 240
Cdd:PLN02942 155 FMAYKGSLMVTDELLLEGFKRCKSLGALAMVHAENGDAVFEGQKRMIELGITGPEGHALSRPPLLEGEATARAIRLAKFV 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530388815 241 NCPLYIVHVMSKSAAKVIADARRDGKVVYGEPIAASLGTDGTHYWNKEWHHAAHHVMGPPLRPdPSTPDFLMNLLANDDL 320
Cdd:PLN02942 235 NTPLYVVHVMSIDAMEEIARARKSGQRVIGEPVVSGLVLDDSKLWDPDFTIASKYVMSPPIRP-AGHGKALQAALSSGIL 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530388815 321 TTTGTDNCTFNTCQKALGKDDFTKIPNGVNGVEDRMSVIWEKGVHSGKMDENRFVAVTSTNAAKIFNLYPRKGRIAVGSD 400
Cdd:PLN02942 314 QLVGTDHCPFNSTQKAFGKDDFRKIPNGVNGIEERMHLVWDTMVESGQISPTDYVRVTSTECAKIFNIYPRKGAILAGSD 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530388815 401 ADIVIWDPKGTrgcrscvafsdngsvyktnmnlplqclanarvhmeeRTISAKTHHQAVNFNIFEGMVCHGVPLVTISRG 480
Cdd:PLN02942 394 ADIIILNPNST------------------------------------FTISAKTHHSRIDTNVYEGRRGKGKVEVTISQG 437
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 530388815 481 KVVYEAGVFSVTAGDGKFIPRKPFAeYIYKRIKQRDRTCTPTPVERAPYK 530
Cdd:PLN02942 438 RVVWENGELKVVRGSGRYIEMPPFS-YLFDGIQKADAAYLSSLRAPVKRT 486
|
|
| AllB |
COG0044 |
Dihydroorotase or related cyclic amidohydrolase [Nucleotide transport and metabolism]; ... |
8-501 |
1.02e-136 |
|
Dihydroorotase or related cyclic amidohydrolase [Nucleotide transport and metabolism]; Dihydroorotase or related cyclic amidohydrolase is part of the Pathway/BioSystem: Pyrimidine biosynthesis
Pssm-ID: 439814 [Multi-domain] Cd Length: 439 Bit Score: 403.70 E-value: 1.02e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530388815 8 LIRGGRVVNDDFSEVADVLVEDGVVRALGHDLLPPGGApaglRVLDAAGKLVLPGGIDTHTHMQFPFMGSRsiDDFHQGT 87
Cdd:COG0044 1 LIKNGRVVDPGGLERADVLIEDGRIAAIGPDLAAPEAA----EVIDATGLLVLPGLIDLHVHLREPGLEHK--EDIETGT 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530388815 88 KAALSGGTTMIIDFAIPQKGGSLIEAFETWRSWADPKVCCDYSLHVAVTWWSDQVKEEMKILVqDKGVNSFKMFMAYKD- 166
Cdd:COG0044 75 RAAAAGGVTTVVDMPNTNPVTDTPEALEFKLARAEEKALVDVGPHGALTKGLGENLAELGALA-EAGAVAFKVFMGSDDg 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530388815 167 LYMVTDLELYEAFSRCKEIGAIAQVHAENGDLIAEGAKkmlALGITGPEGHELCRPEAVEAEATLRAITIASAVNCPLYI 246
Cdd:COG0044 154 NPVLDDGLLRRALEYAAEFGALVAVHAEDPDLIRGGVM---NEGKTSPRLGLKGRPAEAEEEAVARDIALAEETGARLHI 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530388815 247 VHVMSKSAAKVIADARRDGKVVYGE--P-----IAASLGTDGTHYwnkewhhaahhVMGPPLRpDPSTPDFLMNLLANDD 319
Cdd:COG0044 231 VHVSTAEAVELIREAKARGLPVTAEvcPhhltlTDEDLERYGTNF-----------KVNPPLR-TEEDREALWEGLADGT 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530388815 320 LTTTGTDNCTFNTCQKAlgkDDFTKIPNGVNGVEDRMSVIWEKGVHSGKMDENRFVAVTSTNAAKIFNLyPRKGRIAVGS 399
Cdd:COG0044 299 IDVIATDHAPHTLEEKE---LPFAEAPNGIPGLETALPLLLTELVHKGRLSLERLVELLSTNPARIFGL-PRKGRIAVGA 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530388815 400 DADIVIWDPKgtrgcrscvafsdngsvyktnmnlplqclanarvhmEERTISAKTHHQAVNFNIFEGMVCHGVPLVTISR 479
Cdd:COG0044 375 DADLVLFDPD------------------------------------AEWTVTAEDLHSKSKNTPFEGRELTGRVVATIVR 418
|
490 500
....*....|....*....|..
gi 530388815 480 GKVVYEAGVFsVTAGDGKFIPR 501
Cdd:COG0044 419 GRVVYEDGEV-VGEPRGRFLRR 439
|
|
| PRK13404 |
PRK13404 |
dihydropyrimidinase; Provisional |
7-501 |
2.21e-125 |
|
dihydropyrimidinase; Provisional
Pssm-ID: 184033 [Multi-domain] Cd Length: 477 Bit Score: 376.35 E-value: 2.21e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530388815 7 LLIRGGRVVNDDFSEVADVLVEDGVVRALGHDLlppggaPAGLRVLDAAGKLVLPGGIDTHTHM-QFPFMGSRSIDDFHQ 85
Cdd:PRK13404 6 LVIRGGTVVTATDTFQADIGIRGGRIAALGEGL------GPGAREIDATGRLVLPGGVDSHCHIdQPSGDGIMMADDFYT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530388815 86 GTKAALSGGTTMIIDFAIPQKGGSLIEAFETWRSWADPKVCCDYSLHVAVTWWSDQV-KEEMKILVQDkGVNSFKMFMAY 164
Cdd:PRK13404 80 GTVSAAFGGTTTVIPFAAQHRGQSLREAVEDYHRRAAGKAVIDYAFHLIVADPTEEVlTEELPALIAQ-GYTSFKVFMTY 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530388815 165 KDLyMVTDLELYEAFSRCKEIGAIAQVHAENGDLIAEGAKKMLALGITGPEGHELCRPEAVEAEATLRAITIASAVNCPL 244
Cdd:PRK13404 159 DDL-KLDDRQILDVLAVARRHGAMVMVHAENHDMIAWLTKRLLAAGLTAPKYHAISRPMLAEREATHRAIALAELVDVPI 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530388815 245 YIVHVMSKSAAKVIADARRDGKVVYGEP-------IAASLGTDGTHywnkewhhAAHHVMGPPLRpDPSTPDFLMNLLAN 317
Cdd:PRK13404 238 LIVHVSGREAAEQIRRARGRGLKIFAETcpqylflTAEDLDRPGME--------GAKYICSPPPR-DKANQEAIWNGLAD 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530388815 318 DDLTTTGTDNCTFN---TCQKALGKDD--FTKIPNGVNGVEDRMSVIWEKGVHSGKMDENRFVAVTSTNAAKIFNLYPRK 392
Cdd:PRK13404 309 GTFEVFSSDHAPFRfddTDGKLAAGANpsFKAIANGIPGIETRLPLLFSEGVVKGRISLNRFVALTSTNPAKLYGLYPRK 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530388815 393 GRIAVGSDADIVIWDPKgtrgcrscvafsdngsvyktnmnlplqclanarvhmEERTISAKTHHQAVNFNIFEGMVCHGV 472
Cdd:PRK13404 389 GAIAIGADADIAIWDPD------------------------------------REVTITNADLHHAADYTPYEGMRVTGW 432
|
490 500
....*....|....*....|....*....
gi 530388815 473 PLVTISRGKVVYEAGVFSVTAGDGKFIPR 501
Cdd:PRK13404 433 PVTVLSRGRVVVEDGELVAERGSGQFLAR 461
|
|
| L-HYD_ALN |
cd01315 |
L-Hydantoinases (L-HYDs) and Allantoinase (ALN); L-Hydantoinases are a member of the ... |
7-499 |
8.53e-69 |
|
L-Hydantoinases (L-HYDs) and Allantoinase (ALN); L-Hydantoinases are a member of the dihydropyrimidinase family, which catalyzes the reversible hydrolytic ring opening of dihydropyrimidines and hydantoins (five-membered cyclic diamides used in biotechnology). But L-HYDs differ by having an L-enantio specificity and by lacking activity on possible natural substrates such as dihydropyrimidines. Allantoinase catalyzes the hydrolytic cleavage of the five-member ring of allantoin (5-ureidohydantoin) to form allantoic acid.
Pssm-ID: 238640 [Multi-domain] Cd Length: 447 Bit Score: 228.71 E-value: 8.53e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530388815 7 LLIRGGRVVNDDFSEVADVLVEDGVVRALGHDLLPPGGApaglRVLDAAGKLVLPGGIDTHTHMQFPfmGSRSIDDFHQG 86
Cdd:cd01315 2 LVIKNGRVVTPDGVREADIAVKGGKIAAIGPDIANTEAE----EVIDAGGLVVMPGLIDTHVHINEP--GRTEWEGFETG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530388815 87 TKAALSGGTTMIIDF---AIPQKggSLIEAFETWRSWADPKvccdysLHVAVTWW-------SDQVKEemkiLVqDKGVN 156
Cdd:cd01315 76 TKAAAAGGITTIIDMplnSIPPT--TTVENLEAKLEAAQGK------LHVDVGFWgglvpgnLDQLRP----LD-EAGVV 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530388815 157 SFKMFMA---YKDLYMVTDLELYEAFSRCKEIGAIAQVHAENGDLIAEGAKKMLALGITGPEGHELCRPEAVEAEATLRA 233
Cdd:cd01315 143 GFKCFLCpsgVDEFPAVDDEQLEEAMKELAKTGSVLAVHAENPEITEALQEQAKAKGKRDYRDYLASRPVFTEVEAIQRI 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530388815 234 ITIASAVNCPLYIVHVMSKSAAKVIADARRDGKVVYGE--PIAASLGTD-----GTHYwnKEWhhaahhvmgPPLRpDPS 306
Cdd:cd01315 223 LLLAKETGCRLHIVHLSSAEAVPLIREARAEGVDVTVEtcPHYLTFTAEdvpdgGTEF--KCA---------PPIR-DAA 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530388815 307 TPDFLMNLLANDDLTTTGTDN--CTFNtcQKALGKDDFTKIPNGVNGVEDRMSVIWEKGVHSGKMDENRFVAVTSTNAAK 384
Cdd:cd01315 291 NQEQLWEALENGDIDMVVSDHspCTPE--LKLLGKGDFFKAWGGISGLQLGLPVMLTEAVNKRGLSLEDIARLMCENPAK 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530388815 385 IFNLYPRKGRIAVGSDADIVIWDPKgtrgcrscvafsdngsvyktnmnlplqclanarvhmEERTISA---KTHHQAvnf 461
Cdd:cd01315 369 LFGLSHQKGRIAVGYDADFVVWDPE------------------------------------EEFTVDAedlYYKNKI--- 409
|
490 500 510
....*....|....*....|....*....|....*...
gi 530388815 462 NIFEGMVCHGVPLVTISRGKVVYEAGVFSVTAgDGKFI 499
Cdd:cd01315 410 SPYVGRTLKGRVHATILRGTVVYQDGEVVGEP-LGQLL 446
|
|
| Cyclic_amidohydrolases |
cd01302 |
Cyclic amidohydrolases, including hydantoinase, dihydropyrimidinase, allantoinase, and ... |
57-476 |
1.48e-64 |
|
Cyclic amidohydrolases, including hydantoinase, dihydropyrimidinase, allantoinase, and dihydroorotase, are involved in the metabolism of pyrimidines and purines, sharing the property of hydrolyzing the cyclic amide bond of each substrate to the corresponding N-carbamyl amino acids. Allantoinases catalyze the degradation of purines, while dihydropyrimidinases and hydantoinases, a microbial counterpart of dihydropyrimidinase, are involved in pyrimidine degradation. Dihydroorotase participates in the de novo synthesis of pyrimidines.
Pssm-ID: 238627 [Multi-domain] Cd Length: 337 Bit Score: 214.18 E-value: 1.48e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530388815 57 KLVLPGGIDTHTHMQFPFMGSRSiDDFHQGTKAALSGGTTMIIDFAIPQKGGSLIEAFETWRSWADPKVCCDYSLHVAVt 136
Cdd:cd01302 1 LLVLPGFIDIHVHLRDPGGTTYK-EDFESGSRAAAAGGVTTVIDMPNTGPPPIDLPAIELKIKLAEESSYVDFSFHAGI- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530388815 137 wWSDQVKEEMKiLVQDKGVNSFKMFMAYK--DLYMVTDLELYEAFSRCKEIGAIAQVHAEngdliaegakkmlalgitgp 214
Cdd:cd01302 79 -GPGDVTDELK-KLFDAGINSLKVFMNYYfgELFDVDDGTLMRTFLEIASRGGPVMVHAE-------------------- 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530388815 215 eghelcrpeaveaeatlRAITIASAVNCPLYIVHVMSKSAAKVIADARRDGKVVYGEPIAASLGTDgTHYWNKEWHHAah 294
Cdd:cd01302 137 -----------------RAAQLAEEAGANVHIAHVSSGEALELIKFAKNKGVKVTCEVCPHHLFLD-ESMLRLNGAWG-- 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530388815 295 hVMGPPLRPdPSTPDFLMNLLANDDLTTTGTDNCTFNTCQKALGKdDFTKIPNGVNGVEDRMSVIWEKGVHSGkMDENRF 374
Cdd:cd01302 197 -KVNPPLRS-KEDREALWEGVKNGKIDTIASDHAPHSKEEKESGK-DIWKAPPGFPGLETRLPILLTEGVKRG-LSLETL 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530388815 375 VAVTSTNAAKIFNLYPrKGRIAVGSDADIVIWDPKgtrgcrscvafsdngsvyktnmnlplqclanarvhmEERTISAKT 454
Cdd:cd01302 273 VEILSENPARIFGLYP-KGTIAVGYDADLVIVDPK------------------------------------KEWKVTAEE 315
|
410 420
....*....|....*....|..
gi 530388815 455 HHQAVNFNIFEGMVCHGVPLVT 476
Cdd:cd01302 316 IESKADWTPFEGMEVTGKPVST 337
|
|
| PRK02382 |
PRK02382 |
dihydroorotase; Provisional |
7-502 |
1.51e-50 |
|
dihydroorotase; Provisional
Pssm-ID: 179417 [Multi-domain] Cd Length: 443 Bit Score: 179.85 E-value: 1.51e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530388815 7 LLIRGGRVVNDDFSEVADVLVEDGVVRALGHDLLPPGGApaglRVLDAAGKLVLPGGIDTHTHMQFPFMGSRsiDDFHQG 86
Cdd:PRK02382 4 ALLKDGRVYYNNSLQPRDVRIDGGKITAVGKDLDGSSSE----EVIDARGMLLLPGGIDVHVHFREPGYTHK--ETWYTG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530388815 87 TKAALSGGTTMIIDF---AIPQKGGsliEAFETWRSWADPKVCCDYSLHVAVTWWSDQVKEemkilVQDKGVNSF-KMFM 162
Cdd:PRK02382 78 SRSAAAGGVTTVVDQpntDPPTVDG---ESFDEKAELAARKSIVDFGINGGVTGNWDPLES-----LWERGVFALgEIFM 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530388815 163 AYKDLYMVTDLELY-EAFSRCKEIGAIAQVHAENGDLIAEGAKkmLALGITGPEGHELCRPEAVEAEATLRAITIASAVN 241
Cdd:PRK02382 150 ADSTGGMGIDEELFeEALAEAARLGVLATVHAEDEDLFDELAK--LLKGDADADAWSAYRPAAAEAAAVERALEVASETG 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530388815 242 CPLYIVHVMSKSAAKVIADA--------------RRDgkvvygepiAASLGTDGThywnkewhhaahhvMGPPLRPDPST 307
Cdd:PRK02382 228 ARIHIAHISTPEGVDAARREgitcevtphhlflsRRD---------WERLGTFGK--------------MNPPLRSEKRR 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530388815 308 pDFLMNLLANDDLTTTGTDNCTFNTCQKALgkdDFTKIPNGVNGVEDRMSVIWEkGVHSGKMDENRFVAVTSTNAAKIFN 387
Cdd:PRK02382 285 -EALWERLNDGTIDVVASDHAPHTREEKDA---DIWDAPSGVPGVETMLPLLLA-AVRKNRLPLERVRDVTAANPARIFG 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530388815 388 LyPRKGRIAVGSDADIVIWDPKGTrgcrscvafsdngsvyktnmnlplqclanarvhmeeRTISAKTHHQAVNFNIFEGM 467
Cdd:PRK02382 360 L-DGKGRIAEGYDADLVLVDPDAA------------------------------------REIRGDDLHSKAGWTPFEGM 402
|
490 500 510
....*....|....*....|....*....|....*.
gi 530388815 468 VchGV-PLVTISRGKVVYEAGVFSVTAGDGKFIPRK 502
Cdd:PRK02382 403 E--GVfPELTMVRGTVVWDGDDINAKRGRGEFLRGR 436
|
|
| pyrC_multi |
TIGR00857 |
dihydroorotase, multifunctional complex type; In contrast to the homodimeric type of ... |
23-486 |
7.50e-44 |
|
dihydroorotase, multifunctional complex type; In contrast to the homodimeric type of dihydroorotase found in E. coli, this class tends to appear in a large, multifunctional complex with aspartate transcarbamoylase. Homologous domains appear in multifunctional proteins of higher eukaryotes. In some species, including Pseudomonas putida and P. aeruginosa, this protein is inactive but is required as a non-catalytic subunit of aspartate transcarbamoylase (ATCase). In these species, a second, active dihydroorotase is also present. The seed for this model does not include any example of the dihydroorotase domain of eukaryotic multidomain pyrimidine synthesis proteins. All proteins described by this model should represent active and inactive dihydroorotase per se and functionally equivalent domains of multifunctional proteins from higher eukaryotes, but exclude related proteins such as allantoinase. [Purines, pyrimidines, nucleosides, and nucleotides, Pyrimidine ribonucleotide biosynthesis]
Pssm-ID: 273302 [Multi-domain] Cd Length: 411 Bit Score: 160.69 E-value: 7.50e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530388815 23 ADVLVEDGVVRALGHDLLPPGgapagLRVLDAAGKLVLPGGIDTHTHMQFPfmGSRSIDDFHQGTKAALSGGTTMIIDfa 102
Cdd:TIGR00857 6 VDILVEGGRIKKIGKLRIPPD-----AEVIDAKGLLVLPGFIDLHVHLRDP--GEEYKEDIESGSKAAAHGGFTTVAD-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530388815 103 IPQKGGSLIEAFETWRSWADPK--VCCDYSLHVAVTwWSDQVKEEMKIlvqdkgvnsFKMFMA------YKDLY--MVTD 172
Cdd:TIGR00857 77 MPNTKPPIDTPETLEWKLQRLKkvSLVDVHLYGGVT-QGNQGKELTEA---------YELKEAgavgrmFTDDGseVQDI 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530388815 173 LELYEAFSRCKEIGAIAQVHAENGDLIAEGAKKmlaLGITGPEGHELCRPEAVEAEATLRAITIASAVNCPLYIVHVMSK 252
Cdd:TIGR00857 147 LSMRRALEYAAIAGVPIALHAEDPDLIYGGVMH---EGPSAAQLGLPARPPEAEEVAVARLLELAKHAGCPVHICHISTK 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530388815 253 SAAKVIADARRdgkvvYGEPIAASLgtdgthywnkEWHH--------AAHHVMG---PPLRPdPSTPDFLMNLLANDDLT 321
Cdd:TIGR00857 224 ESLELIVKAKS-----QGIKITAEV----------TPHHlllseedvARLDGNGkvnPPLRE-KEDRLALIEGLKDGIID 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530388815 322 TTGTDNCTFNTCQKALGkddFTKIPNGVNGVEDRMSVIWEkGVHSGKMDENRFVAVTSTNAAKIFNLyPRKGRIAVGSDA 401
Cdd:TIGR00857 288 IIATDHAPHTLEEKTKE---FAAAPPGIPGLETALPLLLQ-LLVKGLISLKDLIRMLSINPARIFGL-PDKGTLEEGNPA 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530388815 402 DIVIWDPKgtrgcrscvafsdngsvyktnmnlplqclanarvhmEERTISAKTHHQAVNFNIFEGMVCHGVPLVTISRGK 481
Cdd:TIGR00857 363 DITVFDLK------------------------------------KEWTINAETFYSKAKNTPFEGMSLKGKPIATILRGK 406
|
....*
gi 530388815 482 VVYEA 486
Cdd:TIGR00857 407 VVYED 411
|
|
| PRK06189 |
PRK06189 |
allantoinase; Provisional |
7-489 |
1.10e-43 |
|
allantoinase; Provisional
Pssm-ID: 235732 [Multi-domain] Cd Length: 451 Bit Score: 161.41 E-value: 1.10e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530388815 7 LLIRGGRVVNDDFSEVADVLVEDGVVRALGHDLLPPGGApaglrVLDAAGKLVLPGGIDTHTHMQFPfmGSRSIDDFHQG 86
Cdd:PRK06189 5 LIIRGGKVVTPEGVYRADIGIKNGKIAEIAPEISSPARE-----IIDADGLYVFPGMIDVHVHFNEP--GRTHWEGFATG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530388815 87 TKAALSGGTTMIIDFAIPQKGGSLI-EAFETWRSWADPKVCCDYSLhvavtwWSDQV---KEEMKILVqDKGVNSFKMFM 162
Cdd:PRK06189 78 SAALAAGGCTTYFDMPLNSIPPTVTrEALDAKAELARQKSAVDFAL------WGGLVpgnLEHLRELA-EAGVIGFKAFM 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530388815 163 AY---KDLYMVTDLELYEAFSRCKEIGAIAQVHAENGDLIAEGAKKMLALGITGPEGHELCRPEAVEAEATLRAITIASA 239
Cdd:PRK06189 151 SNsgtDEFRSSDDLTLYEGMKEIAALGKILALHAESDALTRHLTTQARQQGKTDVRDYLESRPVVAELEAVQRALLYAQE 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530388815 240 VNCPLYIVHVMSKSAAKVIADARRDGkvvygepIAASLGTdGTHYWnkewhHAAHHVM---------GPPLRpDPSTPDF 310
Cdd:PRK06189 231 TGCPLHFVHISSGKAVALIAEAKKRG-------VDVSVET-CPHYL-----LFTEEDFerigavakcAPPLR-SRSQKEE 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530388815 311 LMNLLANDDLTTTGTDNctfNTCQKALGK-DDFTKIPNGVNGVEDRMSVIWEKGVHSGKMDENRFVAVTSTNAAKIFNLy 389
Cdd:PRK06189 297 LWRGLLAGEIDMISSDH---SPCPPELKEgDDFFLVWGGISGGQSTLLVMLTEGYIERGIPLETIARLLATNPAKRFGL- 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530388815 390 PRKGRIAVGSDADIVIWDPKgtrgcrscvafsdngsvyktnmnlplqclanarvhmEERTISAKTHHQAVNFNIFEGMVC 469
Cdd:PRK06189 373 PQKGRLEVGADADFVLVDLD------------------------------------ETYTLTKEDLFYRHKQSPYEGRTF 416
|
490 500
....*....|....*....|
gi 530388815 470 HGVPLVTISRGKVVYEAGVF 489
Cdd:PRK06189 417 PGRVVATYLRGQCVYQDGEV 436
|
|
| PRK08044 |
PRK08044 |
allantoinase AllB; |
7-408 |
9.30e-36 |
|
allantoinase AllB;
Pssm-ID: 169193 [Multi-domain] Cd Length: 449 Bit Score: 139.22 E-value: 9.30e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530388815 7 LLIRGGRVVNDDFSEVADVLVEDGVVRALGHDLlppgGAPAglRVLDAAGKLVLPGGIDTHTHMQFPfmGSRSIDDFHQG 86
Cdd:PRK08044 5 LIIKNGTVILENEARVVDIAVKGGKIAAIGQDL----GDAK--EVMDASGLVVSPGMVDAHTHISEP--GRSHWEGYETG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530388815 87 TKAALSGGTTMIIDFAIPQKGGSLIEA-FETWRSWADPKVCCDY-SLHVAVTWWSDQVKEemkilVQDKGVNSFKMFMAY 164
Cdd:PRK08044 77 TRAAAKGGITTMIEMPLNQLPATVDRAsIELKFDAAKGKLTIDAaQLGGLVSYNLDRLHE-----LDEVGVVGFKCFVAT 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530388815 165 -------KDLYMVTDLELYEAFSRCKEIGAIAQVHAENG---DLIAEGAKKMlalGITGPEGHELCRPEAVEAEATLRAI 234
Cdd:PRK08044 152 cgdrgidNDFRDVNDWQFYKGAQKLGELGQPVLVHCENAlicDELGEEAKRE---GRVTAHDYVASRPVFTEVEAIRRVL 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530388815 235 TIASAVNCPLYIVHVMSKSAAKVIADARRDGKVVYGEPIaaslgtdgTHYW---NKEWHHAAHHVM-GPPLRpDPSTPDF 310
Cdd:PRK08044 229 YLAKVAGCRLHVCHISSPEGVEEVTRARQEGQDVTCESC--------PHYFvldTDQFEEIGTLAKcSPPIR-DLENQKG 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530388815 311 LMNLLANDDLTTTGTDNctfNTCQKALGKDDFTKIPNGVNGVEDRMSVIWEKGVHSGKMDENRFVAVTSTNAAKIFNLyP 390
Cdd:PRK08044 300 MWEKLFNGEIDCLVSDH---SPCPPEMKAGNIMEAWGGIAGLQNCMDVMFDEAVQKRGMSLPMFGKLMATNAADIFGL-Q 375
|
410
....*....|....*...
gi 530388815 391 RKGRIAVGSDADIVIWDP 408
Cdd:PRK08044 376 QKGRIAPGKDADFVFIQP 393
|
|
| DHOase_IIb |
cd01318 |
Dihydroorotase (DHOase), subgroup IIb; DHOases catalyze the reversible interconversion of ... |
56-480 |
7.21e-32 |
|
Dihydroorotase (DHOase), subgroup IIb; DHOases catalyze the reversible interconversion of carbamoyl aspartate to dihydroorotate, a key reaction in pyrimidine biosynthesis. This group contains the archeal members of the DHOase family.
Pssm-ID: 238643 [Multi-domain] Cd Length: 361 Bit Score: 126.29 E-value: 7.21e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530388815 56 GKLVLPGGIDTHTHMQFPfmGSRSIDDFHQGTKAALSGGTTMIIDFAIPQKGGSLIEAFETWRSWADPKVCCDYSLHVAV 135
Cdd:cd01318 1 GLLILPGVIDIHVHFREP--GLTYKEDFVSGSRAAAAGGVTTVMDMPNTKPPTTTAEALYEKLRLAAAKSVVDYGLYFGV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530388815 136 TwwSDQVKEEMKILvqdkGVNSFKMFMAYKDLYMVTDLE-LYEAFSRCKEIGAiaqVHAENGDLIAEGAKKMLALGItgp 214
Cdd:cd01318 79 T--GSEDLEELDKA----PPAGYKIFMGDSTGDLLDDEEtLERIFAEGSVLVT---FHAEDEDRLRENRKELKGESA--- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530388815 215 egHELCRPEAVEAEATLRAITIASAVNCPLYIVHVMSKSAAKVIADARRDGKV-------VYGEPIAASLGTdgthyWNK 287
Cdd:cd01318 147 --HPRIRDAEAAAVATARALKLARRHGARLHICHVSTPEELKLIKKAKPGVTVevtphhlFLDVEDYDRLGT-----LGK 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530388815 288 ewhhaahhvMGPPLRpDPSTPDFLMNLLANDDLTTTGTDNCTFNTCQKALGkddFTKIPNGVNGVEDRMSVIWEKgVHSG 367
Cdd:cd01318 220 ---------VNPPLR-SREDRKALLQALADGRIDVIASDHAPHTLEEKRKG---YPAAPSGIPGVETALPLMLTL-VNKG 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530388815 368 KMDENRFVAVTSTNAAKIFNLyPRKGRIAVGSDADIVIWDPKgtrgcrscvafsdngsvyktnmnlplqclanarvhmEE 447
Cdd:cd01318 286 ILSLSRVVRLTSHNPARIFGI-KNKGRIAEGYDADLTVVDLK------------------------------------EE 328
|
410 420 430
....*....|....*....|....*....|...
gi 530388815 448 RTISAKTHHQAVNFNIFEGMVCHGVPLVTISRG 480
Cdd:cd01318 329 RTIRAEEFHSKAGWTPFEGFEVTGFPVMTIVRG 361
|
|
| pyrC |
PRK09357 |
dihydroorotase; Validated |
5-486 |
9.23e-32 |
|
dihydroorotase; Validated
Pssm-ID: 236479 [Multi-domain] Cd Length: 423 Bit Score: 127.23 E-value: 9.23e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530388815 5 SRLLIRGGRVVN-DDFSEVADVLVEDGVVRALGHDLlppggAPAGLRVLDAAGKLVLPGGIDTHTHMQFPfmGSRSIDDF 83
Cdd:PRK09357 1 MMILIKNGRVIDpKGLDEVADVLIDDGKIAAIGENI-----EAEGAEVIDATGLVVAPGLVDLHVHLREP--GQEDKETI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530388815 84 HQGTKAALSGG---------TTMIIDfaipqkggSLIEAFETWRSWADPKVCcdyslHV----AVTwwsdqVKEEMKILV 150
Cdd:PRK09357 74 ETGSRAAAAGGfttvvampnTKPVID--------TPEVVEYVLDRAKEAGLV-----DVlpvgAIT-----KGLAGEELT 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530388815 151 QDKGVNSFKMFMAYKDLYMVTD-LELYEAFSRCKEIG-AIAQvHAENGDLIAEGA----KKMLALGITGpeghelcRPEA 224
Cdd:PRK09357 136 EFGALKEAGVVAFSDDGIPVQDaRLMRRALEYAKALDlLIAQ-HCEDPSLTEGGVmnegEVSARLGLPG-------IPAV 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530388815 225 VEAEATLRAITIASAVNCPLYIVHVMSKSAAKVIADARRdgkvvYGEPIAA------------SLGTDGTHYwnKewhha 292
Cdd:PRK09357 208 AEEVMIARDVLLAEATGARVHICHVSTAGSVELIRWAKA-----LGIKVTAevtphhllltdeDLLTYDPNY--K----- 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530388815 293 ahhvMGPPLRpDPSTPDFLMNLLANDDLTTTGTD---------NCtfntcqkalgkdDFTKIPNGVNGVEDRMSVIWEKG 363
Cdd:PRK09357 276 ----VNPPLR-TEEDREALIEGLKDGTIDAIATDhaphareekEC------------EFEAAPFGITGLETALSLLYTTL 338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530388815 364 VHSGKMDENRFVAVTSTNAAKIFNLYPrkGRIAVGSDADIVIWDPKgtrgcrscvafsdngsvyktnmnlplqclanarv 443
Cdd:PRK09357 339 VKTGLLDLEQLLEKMTINPARILGLPA--GPLAEGEPADLVIFDPE---------------------------------- 382
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 530388815 444 hmEERTISAKTHHQAVNFNIFEGMVCHGVPLVTISRGKVVYEA 486
Cdd:PRK09357 383 --AEWTVDGEDFASKGKNTPFIGMKLKGKVVYTIVDGKIVYQD 423
|
|
| DHOase_IIa |
cd01317 |
Dihydroorotase (DHOase), subgroup IIa; DHOases catalyze the reversible interconversion of ... |
48-412 |
7.71e-30 |
|
Dihydroorotase (DHOase), subgroup IIa; DHOases catalyze the reversible interconversion of carbamoyl aspartate to dihydroorotate, a key reaction in pyrimidine biosynthesis. This subgroup also contains proteins that lack the active site, like unc-33, a C.elegans protein involved in axon growth.
Pssm-ID: 238642 [Multi-domain] Cd Length: 374 Bit Score: 120.80 E-value: 7.71e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530388815 48 GLRVLDAAGKLVLPGGIDTHTHMQFPfmGSRSIDDFHQGTKAALSGGTTMII-----DFAIPQKggSLIEAfeTWRSWAD 122
Cdd:cd01317 1 DAEVIDAEGKILAPGLVDLHVHLREP--GFEYKETLESGAKAAAAGGFTTVVcmpntNPVIDNP--AVVEL--LKNRAKD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530388815 123 PKVCCDYSLhVAVTWwSDQVKE--EMKILVqDKGVNSFKmfmayKDLYMVTDLE-LYEAFSRCKEIGAIAQVHAENGDLI 199
Cdd:cd01317 75 VGIVRVLPI-GALTK-GLKGEEltEIGELL-EAGAVGFS-----DDGKPIQDAElLRRALEYAAMLDLPIIVHPEDPSLA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530388815 200 AEGA----KKMLALGITGpeghelcRPEAVEAEATLRAITIASAVNCPLYIVHVMSKSAAKVIADARRDGkvvygEPIAA 275
Cdd:cd01317 147 GGGVmnegKVASRLGLPG-------IPPEAETIMVARDLELAEATGARVHFQHLSTARSLELIRKAKAKG-----LPVTA 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530388815 276 SLGtdgthywnkeWHH------------AAHHVMgPPLRpDPSTPDFLMNLLANDDLTTTGTDNCTFNTCQKALGKDDft 343
Cdd:cd01317 215 EVT----------PHHlllddealesydTNAKVN-PPLR-SEEDREALIEALKDGTIDAIASDHAPHTDEEKDLPFAE-- 280
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 530388815 344 kIPNGVNGVEDRMSVIWEKGVHSGKMDENRFVAVTSTNAAKIFNLYPrkGRIAVGSDADIVIWDPKGTR 412
Cdd:cd01317 281 -APPGIIGLETALPLLWTLLVKGGLLTLPDLIRALSTNPAKILGLPP--GRLEVGAPADLVLFDPDAEW 346
|
|
| PRK09060 |
PRK09060 |
dihydroorotase; Validated |
1-412 |
2.41e-28 |
|
dihydroorotase; Validated
Pssm-ID: 181632 [Multi-domain] Cd Length: 444 Bit Score: 117.71 E-value: 2.41e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530388815 1 MAAPSRLLIRGGRVVNDDFSEVADVLVEDGVVRALGHdllpPGGAPAGlRVLDAAGKLVLPGGIDTHTHMQFPfmGSRSI 80
Cdd:PRK09060 1 MTQTFDLILKGGTVVNPDGEGRADIGIRDGRIAAIGD----LSGASAG-EVIDCRGLHVLPGVIDSQVHFREP--GLEHK 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530388815 81 DDFHQGTKAALSGGTTMIidFAIPQKGGSLI--EAFETWRSWADPKVCCDYSLHVAVTwwSDQVkEEMKILVQDKGVNSF 158
Cdd:PRK09060 74 EDLETGSRAAVLGGVTAV--FEMPNTNPLTTtaEALADKLARARHRMHCDFAFYVGGT--RDNA-DELAELERLPGCAGI 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530388815 159 KMFM--AYKDLyMVTDLELYEAFSRckEIGAIAQVHAENGDLIAEgaKKMLAlgITG-PEGHELCRPEAVEAEATLRAIT 235
Cdd:PRK09060 149 KVFMgsSTGDL-LVEDDEGLRRILR--NGRRRAAFHSEDEYRLRE--RKGLR--VEGdPSSHPVWRDEEAALLATRRLVR 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530388815 236 IASAVNCPLYIVHVMSKSAAKVIADARRDGKV--------VYGEPIAASLGTdgthywnkewhhaaHHVMGPPLRpDPST 307
Cdd:PRK09060 222 LARETGRRIHVLHVSTAEEIDFLADHKDVATVevtphhltLAAPECYERLGT--------------LAQMNPPIR-DARH 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530388815 308 PDFLMNLLANDDLTTTGTDNCTFNTCQKALgkdDFTKIPNGVNGVEDRMSVIWEKgVHSGKMDENRFVAVTSTNAAKIFN 387
Cdd:PRK09060 287 RDGLWRGVRQGVVDVLGSDHAPHTLEEKAK---PYPASPSGMTGVQTLVPIMLDH-VNAGRLSLERFVDLTSAGPARIFG 362
|
410 420
....*....|....*....|....*
gi 530388815 388 LyPRKGRIAVGSDADIVIWDPKGTR 412
Cdd:PRK09060 363 I-AGKGRIAVGYDADFTIVDLKRRE 386
|
|
| PLN02795 |
PLN02795 |
allantoinase |
12-487 |
5.36e-25 |
|
allantoinase
Pssm-ID: 178392 [Multi-domain] Cd Length: 505 Bit Score: 108.32 E-value: 5.36e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530388815 12 GRVVNDDFSEVADVLVEDGVVRALGHDLLPPGGAPAGlRVLDAAGKLVLPGGIDTHTHMQFPfmGSRSIDDFHQGTKAAL 91
Cdd:PLN02795 51 KRVVTPAGVIPGAVEVEGGRIVSVTKEEEAPKSQKKP-HVLDYGNAVVMPGLIDVHVHLNEP--GRTEWEGFPTGTKAAA 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530388815 92 SGGTTMIIDF---AIPQKggSLIEAFETWRSWADPKvccdysLHVAVTWWSDQVKE------EMKILVqDKGVNSFKMFM 162
Cdd:PLN02795 128 AGGITTLVDMplnSFPST--TSVETLELKIEAAKGK------LYVDVGFWGGLVPEnahnasVLEELL-DAGALGLKSFM 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530388815 163 ---AYKDLYMVTDLELYEAFSRCKEIGAIAQVHAENGDLIAEGAkkMLALGITGPEGHELCRPEAVEAEATLRAITIAS- 238
Cdd:PLN02795 199 cpsGINDFPMTTATHIKAALPVLAKYGRPLLVHAEVVSPVESDS--RLDADPRSYSTYLKSRPPSWEQEAIRQLLEVAKd 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530388815 239 ------AVNCPLYIVHVM-SKSAAKVIADARRDGKVVYGEPIAASLG------TDGthywnkewhhAAHHVMGPPLRpDP 305
Cdd:PLN02795 277 trpggvAEGAHVHIVHLSdAESSLELIKEAKAKGDSVTVETCPHYLAfsaeeiPDG----------DTRYKCAPPIR-DA 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530388815 306 STPDFLMNLLANDDLTTTGTDNCTFNTCQKALGKDDFTKIPNGVNGVEDRMSVIWEKGVHSGkMDENRFVAVTSTNAAKI 385
Cdd:PLN02795 346 ANRELLWKALLDGDIDMLSSDHSPSPPDLKLLEEGNFLRAWGGISSLQFVLPATWTAGRAYG-LTLEQLARWWSERPAKL 424
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530388815 386 FNLyPRKGRIAVGSDADIVIWDPKGTrgcrscvaFSDNGSVyktnmnlplqclanaRVHMEERTISAKTHHQavnfniFE 465
Cdd:PLN02795 425 AGL-DSKGAIAPGKDADIVVWDPEAE--------FVLDESY---------------PIYHKHKSLSPYLGTK------LS 474
|
490 500
....*....|....*....|..
gi 530388815 466 GMVchgvpLVTISRGKVVYEAG 487
Cdd:PLN02795 475 GKV-----IATFVRGNLVFLEG 491
|
|
| PRK07575 |
PRK07575 |
dihydroorotase; Provisional |
4-489 |
2.62e-23 |
|
dihydroorotase; Provisional
Pssm-ID: 236055 [Multi-domain] Cd Length: 438 Bit Score: 102.83 E-value: 2.62e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530388815 4 PSRLLIRGGRVVNDDFS-EVADVLVEDGVVRALGhdllPPGGAPAGLRVLDAAGKLVLPGGIDTHTHMQFPfmGSRSIDD 82
Cdd:PRK07575 2 MMSLLIRNARILLPSGElLLGDVLVEDGKIVAIA----PEISATAVDTVIDAEGLTLLPGVIDPQVHFREP--GLEHKED 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530388815 83 FHQGTKAALSGGTTMIIDFAIPQKGGSLIEAFETWRSWADPKVCCDYSLHVAVTwwSDQVKEemkiLVQDKGVNSFKMFM 162
Cdd:PRK07575 76 LFTASRACAKGGVTSFLEMPNTKPLTTTQAALDDKLARAAEKCVVNYGFFIGAT--PDNLPE----LLTANPTCGIKIFM 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530388815 163 --AYKDLYMVTDLELYEAFSRCKEIgaIAqVHAENGDLIAEgAKKMLAlGITGPEGHELCRPEAVEAEATLRAITIASAV 240
Cdd:PRK07575 150 gsSHGPLLVDEEAALERIFAEGTRL--IA-VHAEDQARIRA-RRAEFA-GISDPADHSQIQDEEAALLATRLALKLSKKY 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530388815 241 NCPLYIVHVMSKSAAKVIADARRDGKVVYGEPIAASLGTD-----GThywnkewhhAAHhvMGPPLRpDPSTPDFLMNLL 315
Cdd:PRK07575 225 QRRLHILHLSTAIEAELLRQDKPSWVTAEVTPQHLLLNTDayeriGT---------LAQ--MNPPLR-SPEDNEALWQAL 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530388815 316 ANDDLTTTGTDNCTFNTCQKALGkddFTKIPNGVNGVEDRMSVIWEKgVHSGKMDENRFVAVTSTNAAKIFNLyPRKGRI 395
Cdd:PRK07575 293 RDGVIDFIATDHAPHTLEEKAQP---YPNSPSGMPGVETSLPLMLTA-AMRGKCTVAQVVRWMSTAVARAYGI-PNKGRI 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530388815 396 AVGSDADIVIWDpkgtrgcrscvafsdngsvyktnMNlplqclanarvhmEERTISAKTHHQAVNFNIFEGMVCHGVPLV 475
Cdd:PRK07575 368 APGYDADLVLVD-----------------------LN-------------TYRPVRREELLTKCGWSPFEGWNLTGWPVT 411
|
490
....*....|....
gi 530388815 476 TISRGKVVYEAGVF 489
Cdd:PRK07575 412 TIVGGQIVFDRGQV 425
|
|
| Amidohydro_1 |
pfam01979 |
Amidohydrolase family; This family of enzymes are a a large metal dependent hydrolase ... |
58-429 |
1.02e-22 |
|
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: 99.50 E-value: 1.02e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530388815 58 LVLPGGIDTHTHMQFPFMGSRSIDD------FHQGTKAALSGGTTMIIDFAIPQKGG--SLIEAFEtwRSWADPKVC--- 126
Cdd:pfam01979 1 IVLPGLIDAHVHLEMGLLRGIPVPPefayeaLRLGITTMLKSGTTTVLDMGATTSTGieALLEAAE--ELPLGLRFLgpg 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530388815 127 ----CDYSLHVAVTWWsDQVKEEMKILVQDKGVNSFKMFMAYKDlYMVTDLELYEAFSRCKEIGAIAQVHAENGDLIAEG 202
Cdd:pfam01979 79 csldTDGELEGRKALR-EKLKAGAEFIKGMADGVVFVGLAPHGA-PTFSDDELKAALEEAKKYGLPVAIHALETKGEVED 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530388815 203 AKKmlALGITGPEGHELcrpEAVEAEATLRAITIASAVNcplyiVHVMSKSAAKVIADARRDGkvVYGEPIAASLGTDGT 282
Cdd:pfam01979 157 AIA--AFGGGIEHGTHL---EVAESGGLLDIIKLILAHG-----VHLSPTEANLLAEHLKGAG--VAHCPFSNSKLRSGR 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530388815 283 hywnkewhhaahhvmgPPLRPdpstpdflmnLLANDDLTTTGTDNCtfntcqkaLGKDDFTKIPNGVNGVEDRmsviwek 362
Cdd:pfam01979 225 ----------------IALRK----------ALEDGVKVGLGTDGA--------GSGNSLNMLEELRLALELQ------- 263
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 530388815 363 GVHSGKMDENRFVAVTSTNAAKIFNLYPRKGRIAVGSDADIVIWDPKGTrgcRSCVAFSDNGSVYKT 429
Cdd:pfam01979 264 FDPEGGLSPLEALRMATINPAKALGLDDKVGSIEVGKDADLVVVDLDPL---AAFFGLKPDGNVKKV 327
|
|
| PRK04250 |
PRK04250 |
dihydroorotase; Provisional |
8-487 |
6.48e-19 |
|
dihydroorotase; Provisional
Pssm-ID: 235265 [Multi-domain] Cd Length: 398 Bit Score: 89.06 E-value: 6.48e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530388815 8 LIRGGRVVNDDFSEvADVLVEDGVVRALGHDLLPpggapaGLRVLDAAGKLVLPGGIDTHTHMQfpfmgsrsidDFHQ-- 85
Cdd:PRK04250 1 VLEGKFLLKGRIVE-GGIGIENGRISKISLRDLK------GKEVIKVKGGIILPGLIDVHVHLR----------DFEEsy 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530388815 86 ------GTKAALSGGTTMIIDfaIPQKGGSLI--EAFETWRSWADPKVCCDYSLHVAVTWWSDQVKEEMKilvqdkgvNS 157
Cdd:PRK04250 64 ketiesGTKAALHGGITLVFD--MPNTKPPIMdeKTYEKRMRIAEKKSYADYALNFLIAGNCEKAEEIKA--------DF 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530388815 158 FKMFM--AYKDLYMvTDLElyeafSRCKEIGAIAQVHAENGDLIAEGakkmlalgitgPEghelcRPEAVEAEATLRAIT 235
Cdd:PRK04250 134 YKIFMgaSTGGIFS-ENFE-----VDYACAPGIVSVHAEDPELIREF-----------PE-----RPPEAEVVAIERALE 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530388815 236 IASAVNCPLYIVHVMSKSAAKVIADARRDGKVVYGEPiaaslgtdgthywnkewhhaaHHVM--------------GPPL 301
Cdd:PRK04250 192 AGKKLKKPLHICHISTKDGLKLILKSNLPWVSFEVTP---------------------HHLFltrkdyernpllkvYPPL 250
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530388815 302 RPDPSTPDFLMNL-----LANDDLTTTGTDnctfntcqKALGKddftkipNGVNGVEDRMSVIWEkGVHSGKMDENRFVA 376
Cdd:PRK04250 251 RSEEDRKALWENFskipiIASDHAPHTLED--------KEAGA-------AGIPGLETEVPLLLD-AANKGMISLFDIVE 314
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530388815 377 VTSTNAAKIFNlYPRKGrIAVGSDADIVIWDPKgtrgcrscvafsdngsvyktnmnlplqclanarvhmEERTISAKTHH 456
Cdd:PRK04250 315 KMHDNPARIFG-IKNYG-IEEGNYANFAVFDMK------------------------------------KEWTIKAEELY 356
|
490 500 510
....*....|....*....|....*....|.
gi 530388815 457 QAVNFNIFEGMVCHGVPLVTISRGKVVYEAG 487
Cdd:PRK04250 357 TKAGWTPYEGFKLKGKVIMTILRGEVVMEDD 387
|
|
| PRK01211 |
PRK01211 |
dihydroorotase; Provisional |
16-407 |
2.45e-16 |
|
dihydroorotase; Provisional
Pssm-ID: 179247 [Multi-domain] Cd Length: 409 Bit Score: 81.06 E-value: 2.45e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530388815 16 NDDFSEVAdVLVEDGVVRALGHDLlppGGAPAglRVLDAAgklVLPGGIDTHTHMQFPfmGSRSIDDFHQGTKAALSGGT 95
Cdd:PRK01211 10 KGKFDYLE-IEVEDGKIKSIKKDA---GNIGK--KELKGA---ILPAATDIHVHFRTP--GETEKEDFSTGTLSAIFGGT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530388815 96 TMIIDFA---IPQKGgslIEAFETWRSWADPKVCCDYSLHVAVTWWSDQVKEEMKIlvqdkgvnSFKMFMAYKDLYMVTD 172
Cdd:PRK01211 79 TFIMDMPnnnIPIKD---YNAFSDKLGRVAPKAYVDFSLYSMETGNNALILDERSI--------GLKVYMGGTTNTNGTD 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530388815 173 LELYEAfSRCKEIGAIAQVHAENGDLIAEGAKKMLALgitgpEGHELCRPEAVEAEAT--LRAITIASAVncplyIVHVm 250
Cdd:PRK01211 148 IEGGEI-KKINEANIPVFFHAELSECLRKHQFESKNL-----RDHDLARPIECEIKAVkyVKNLDLKTKI-----IAHV- 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530388815 251 skSAAKVIADARRDgkvvygepiaaslGTDGTHYWNKEWHHAAHHVMGPPLRpDPSTPDFLMNLLANDDLTTTGTDNCTF 330
Cdd:PRK01211 216 --SSIDVIGRFLRE-------------VTPHHLLLNDDMPLGSYGKVNPPLR-DRWTQERLLEEYISGRFDILSSDHAPH 279
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 530388815 331 NTCQKAlgkdDFTKIPNGVNGVEDRMSVIWEKgVHSGKMDENRFVAVTSTNAAKIFNLypRKGRIAVGSDADIVIWD 407
Cdd:PRK01211 280 TEEDKQ----EFEYAKSGIIGVETRVPLFLAL-VKKKILPLDVLYKTAIERPASLFGI--KKGKIEEGYDADFMAFD 349
|
|
| HutI |
COG1228 |
Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport ... |
2-407 |
4.22e-15 |
|
Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440841 [Multi-domain] Cd Length: 386 Bit Score: 77.31 E-value: 4.22e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530388815 2 AAPSRLLIRGGRVV---NDDFSEVADVLVEDGVVRALGHDLLPPggAPAGLRVLDAAGKLVLPGGIDTHTHMQFPFMGSR 78
Cdd:COG1228 5 AQAGTLLITNATLVdgtGGGVIENGTVLVEDGKIAAVGPAADLA--VPAGAEVIDATGKTVLPGLIDAHTHLGLGGGRAV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530388815 79 S----------IDDFHQGTK---AALSGGTTMIIDfaipqKGGSLIEAFE-----TWRSWADPKV-CCDYSLHV---AVT 136
Cdd:COG1228 83 EfeagggitptVDLVNPADKrlrRALAAGVTTVRD-----LPGGPLGLRDaiiagESKLLPGPRVlAAGPALSLtggAHA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530388815 137 WWSDQVKEEMKILVQDkGVNSFKMFMAYKDLYMvTDLELYEAFSRCKEIGAIAQVHAENgdliAEGAKKMLALGITGPEG 216
Cdd:COG1228 158 RGPEEARAALRELLAE-GADYIKVFAEGGAPDF-SLEELRAILEAAHALGLPVAAHAHQ----ADDIRLAVEAGVDSIEH 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530388815 217 HELCRPEAVE--AEATLRAI--TIASAVNCPLYIVHVMSKSAAKVIADARRDGKVVY--GEPIAasLGTDGthywnkewh 290
Cdd:COG1228 232 GTYLDDEVADllAEAGTVVLvpTLSLFLALLEGAAAPVAAKARKVREAALANARRLHdaGVPVA--LGTDA--------- 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530388815 291 haahhvmGPPLRPDPSTPdFLMNLLANDDLTTtgtdnctfntcQKALgkddftkipngvngvedrmsviwekgvhsgkmd 370
Cdd:COG1228 301 -------GVGVPPGRSLH-RELALAVEAGLTP-----------EEAL--------------------------------- 328
|
410 420 430
....*....|....*....|....*....|....*..
gi 530388815 371 enrfVAVTStNAAKIFNLYPRKGRIAVGSDADIVIWD 407
Cdd:COG1228 329 ----RAATI-NAAKALGLDDDVGSLEPGKLADLVLLD 360
|
|
| D-aminoacylase |
cd01297 |
D-aminoacylases (N-acyl-D-Amino acid amidohydrolases) catalyze the hydrolysis of ... |
7-408 |
1.40e-13 |
|
D-aminoacylases (N-acyl-D-Amino acid amidohydrolases) catalyze the hydrolysis of N-acyl-D-amino acids to produce the corresponding D-amino acids, which are used as intermediates in the synthesis of pesticides, bioactive peptides, and antibiotics.
Pssm-ID: 238622 [Multi-domain] Cd Length: 415 Bit Score: 72.71 E-value: 1.40e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530388815 7 LLIRGGRVV----NDDFSevADVLVEDGVVRALGHDLLPPGGapaglRVLDAAGKLVLPGGIDTHTHMQFPFMGSRSIdd 82
Cdd:cd01297 2 LVIRNGTVVdgtgAPPFT--ADVGIRDGRIAAIGPILSTSAR-----EVIDAAGLVVAPGFIDVHTHYDGQVFWDPDL-- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530388815 83 fhqgTKAALSGGTTMII----------DFAIPQKGGSLIEAF--------ETWRSWAD-----------PKVCCDY---S 130
Cdd:cd01297 73 ----RPSSRQGVTTVVLgncgvspapaNPDDLARLIMLMEGLvalgeglpWGWATFAEyldalearppaVNVAALVghaA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530388815 131 LHVAVTWWSDQVK-----EEMKILVqDKGVNS----FKMFMAYKDLYMVTDLELYEAFSRCKEIGAIAQVHAEN-GDLIA 200
Cdd:cd01297 149 LRRAVMGLDAREAteeelAKMRELL-REALEAgalgISTGLAYAPRLYAGTAELVALARVAARYGGVYQTHVRYeGDSIL 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530388815 201 EGAKKMLALGitgpeghelcrpeaveaEATLRAITIASAVNCPLYIVHVMSKSAAkVIADARRDGKVVYGE--PIAASLg 278
Cdd:cd01297 228 EALDELLRLG-----------------RETGRPVHISHLKSAGAPNWGKIDRLLA-LIEAARAEGLQVTADvyPYGAGS- 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530388815 279 tdgthywnkewhhaahhvmgpplrpdpstPDFLMNLLAnDDLTTTGTD-----------NCTFNtcqKALGKddftkipn 347
Cdd:cd01297 289 -----------------------------EDDVRRIMA-HPVVMGGSDggalgkphprsYGDFT---RVLGH-------- 327
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 530388815 348 gvnGVEDRMSVIWEKGVHsgKMdenrfvavtSTNAAKIFNLYPRkGRIAVGSDADIVIWDP 408
Cdd:cd01297 328 ---YVRERKLLSLEEAVR--KM---------TGLPARVFGLADR-GRIAPGYRADIVVFDP 373
|
|
| PRK09236 |
PRK09236 |
dihydroorotase; Reviewed |
5-409 |
2.29e-11 |
|
dihydroorotase; Reviewed
Pssm-ID: 181716 Cd Length: 444 Bit Score: 66.05 E-value: 2.29e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530388815 5 SRLLIRGGRVVNDDFSEVADVLVEDGVVRALGHDLLPPGGApaglRVLDAAGKLVLPGGIDTHTHMQFPfmGSRSIDDFH 84
Cdd:PRK09236 2 KRILIKNARIVNEGKIFEGDVLIENGRIAKIASSISAKSAD----TVIDAAGRYLLPGMIDDQVHFREP--GLTHKGDIA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530388815 85 QGTKAALSGGTTMIIDF--AIPQKggSLIEAFE------TWRSWAdpkvccDYSLHVAVTwwSDQVkEEMKILvqDK--- 153
Cdd:PRK09236 76 SESRAAVAGGITSFMEMpnTNPPT--TTLEALEakyqiaAQRSLA------NYSFYFGAT--NDNL-DEIKRL--DPkrv 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530388815 154 -GVnsfKMFMAYKDLYM-VTDLELYEA-FSRCKEIgaIAqVHAENGDLIAEGAKKMLAL---GITgPEGHELCRPEAVEA 227
Cdd:PRK09236 143 cGV---KVFMGASTGNMlVDNPETLERiFRDAPTL--IA-THCEDTPTIKANLAKYKEKygdDIP-AEMHPLIRSAEACY 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530388815 228 EATLRAITIASAVNCPLYIVHVmskSAAKVIADARRDgkvvygePIAASLGTDGT---HYW--NKEWHHAAHHVMGPPLR 302
Cdd:PRK09236 216 KSSSLAVSLAKKHGTRLHVLHI---STAKELSLFENG-------PLAEKRITAEVcvhHLWfdDSDYARLGNLIKCNPAI 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530388815 303 PDPSTPDFLMNLLANDDLTTTGTDNCTFNTCQKALGkddFTKIPNGVNGVEDRMSVIWEKgVHSGKMDENRFVAVTSTNA 382
Cdd:PRK09236 286 KTASDREALRQALADDRIDVIATDHAPHTWEEKQGP---YFQAPSGLPLVQHALPALLEL-VHEGKLSLEKVVEKTSHAP 361
|
410 420
....*....|....*....|....*..
gi 530388815 383 AKIFNLyPRKGRIAVGSDADIVIWDPK 409
Cdd:PRK09236 362 AILFDI-KERGFIREGYWADLVLVDLN 387
|
|
| SsnA |
COG0402 |
Cytosine/adenosine deaminase or related metal-dependent hydrolase [Nucleotide transport and ... |
6-102 |
3.11e-11 |
|
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: 65.23 E-value: 3.11e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530388815 6 RLLIRGGRVV--NDDFSEVAD--VLVEDGVVRALGHDLLPPGGAPaGLRVLDAAGKLVLPGGIDTHTHM----------- 70
Cdd:COG0402 1 DLLIRGAWVLtmDPAGGVLEDgaVLVEDGRIAAVGPGAELPARYP-AAEVIDAGGKLVLPGLVNTHTHLpqtllrgladd 79
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 530388815 71 ----------QFPFMGSRSIDDFHQGTKAA----LSGGTTMIIDFA 102
Cdd:COG0402 80 lplldwleeyIWPLEARLDPEDVYAGALLAlaemLRSGTTTVADFY 125
|
|
| PRK09237 |
PRK09237 |
amidohydrolase/deacetylase family metallohydrolase; |
7-100 |
1.26e-10 |
|
amidohydrolase/deacetylase family metallohydrolase;
Pssm-ID: 236423 [Multi-domain] Cd Length: 380 Bit Score: 63.33 E-value: 1.26e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530388815 7 LLIRGGRVVN--DDFSEVADVLVEDGVVRALGHDLLPPGGApaglRVLDAAGKLVLPGGIDTHTHMqFPFMGSRSI--DD 82
Cdd:PRK09237 1 LLLRGGRVIDpaNGIDGVIDIAIEDGKIAAVAGDIDGSQAK----KVIDLSGLYVSPGWIDLHVHV-YPGSTPYGDepDE 75
|
90
....*....|....*...
gi 530388815 83 FhqgtkAALSGGTTmIID 100
Cdd:PRK09237 76 V-----GVRSGVTT-VVD 87
|
|
| ATZ_TRZ_like |
cd01298 |
TRZ/ATZ family contains enzymes from the atrazine degradation pathway and related hydrolases. ... |
7-100 |
1.68e-10 |
|
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: 62.99 E-value: 1.68e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530388815 7 LLIRGGRVVNDDFSEV---ADVLVEDGVVRALGHDLlpPGGAPAGLRVLDAAGKLVLPGGIDTHTHMQ------------ 71
Cdd:cd01298 1 ILIRNGTIVTTDPRRVledGDVLVEDGRIVAVGPAL--PLPAYPADEVIDAKGKVVMPGLVNTHTHLAmtllrgladdlp 78
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 530388815 72 ---------FPFMGSRSIDDFHQGTKAA----LSGGTTMIID 100
Cdd:cd01298 79 lmewlkdliWPLERLLTEEDVYLGALLAlaemIRSGTTTFAD 120
|
|
| PRK09061 |
PRK09061 |
D-glutamate deacylase; Validated |
2-71 |
3.86e-10 |
|
D-glutamate deacylase; Validated
Pssm-ID: 236369 [Multi-domain] Cd Length: 509 Bit Score: 62.40 E-value: 3.86e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 530388815 2 AAPSRLLIRGGRVVNDD--FSEVADVLVEDGVVRALGHDLLppggapAGLRVLDAAGKLVLPGGIDTHTHMQ 71
Cdd:PRK09061 16 MAPYDLVIRNGRVVDPEtgLDAVRDVGIKGGKIAAVGTAAI------EGDRTIDATGLVVAPGFIDLHAHGQ 81
|
|
| PRK09059 |
PRK09059 |
dihydroorotase; Validated |
7-99 |
4.63e-10 |
|
dihydroorotase; Validated
Pssm-ID: 181631 [Multi-domain] Cd Length: 429 Bit Score: 61.97 E-value: 4.63e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530388815 7 LLIRGGRVVND--DFSEVADVLVEDGVVRALGHDLLPpGGAPAGLRVLDAAGKLVLPGGIDTHTHMQFPfmGSRSIDDFH 84
Cdd:PRK09059 5 ILLANARIIDPsrGLDEIGTVLIEDGVIVAAGKGAGN-QGAPEGAEIVDCAGKAVAPGLVDARVFVGEP--GAEHRETIA 81
|
90
....*....|....*
gi 530388815 85 QGTKAALSGGTTMII 99
Cdd:PRK09059 82 SASRAAAAGGVTSII 96
|
|
| metallo-dependent_hydrolases |
cd01292 |
Superfamily of metallo-dependent hydrolases (also called amidohydrolase superfamily) is a ... |
64-281 |
1.06e-08 |
|
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: 56.57 E-value: 1.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530388815 64 IDTHTHMQFPFMGSRSI----------------DDFHQGTKAALSGGTTMIIDFAIPQKGGSLIEAFETWRSWADP---- 123
Cdd:cd01292 2 IDTHVHLDGSALRGTRLnlelkeaeelspedlyEDTLRALEALLAGGVTTVVDMGSTPPPTTTKAAIEAVAEAARAsagi 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530388815 124 -KVCCDYSLHVAVTW---WSDQVKEEMKILVQdKGVNSFKMFMAYKDlYMVTDLELYEAFSRCKEIGAIAQVHAENGDLI 199
Cdd:cd01292 82 rVVLGLGIPGVPAAVdedAEALLLELLRRGLE-LGAVGLKLAGPYTA-TGLSDESLRRVLEEARKLGLPVVIHAGELPDP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530388815 200 AEGAKKMLALGITGPEGH----ELCRPEAVE-AEATLRAITIASAVNCPLYIVHVMSKSAAKVIADARRDGkvvygepia 274
Cdd:cd01292 160 TRALEDLVALLRLGGRVVighvSHLDPELLElLKEAGVSLEVCPLSNYLLGRDGEGAEALRRLLELGIRVT--------- 230
|
....*..
gi 530388815 275 asLGTDG 281
Cdd:cd01292 231 --LGTDG 235
|
|
| YtcJ |
COG1574 |
Predicted amidohydrolase YtcJ [General function prediction only]; |
2-70 |
1.07e-08 |
|
Predicted amidohydrolase YtcJ [General function prediction only];
Pssm-ID: 441182 [Multi-domain] Cd Length: 535 Bit Score: 57.89 E-value: 1.07e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 530388815 2 AAPSRLLIRGGRV--VNDDFSEVADVLVEDGVVRALGHDLLPPGGAPAGLRVLDAAGKLVLPGGIDTHTHM 70
Cdd:COG1574 5 AAAADLLLTNGRIytMDPAQPVAEAVAVRDGRIVAVGSDAEVRALAGPATEVIDLGGKTVLPGFIDAHVHL 75
|
|
| NagA |
COG1820 |
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism]; |
8-96 |
1.08e-08 |
|
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism];
Pssm-ID: 441425 [Multi-domain] Cd Length: 373 Bit Score: 57.03 E-value: 1.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530388815 8 LIRGGRVVNDD-FSEVADVLVEDGVVRALGhdllppGGAPAGLRVLDAAGKLVLPGGIDTHTH--MQFPFMGSrSIDDFH 84
Cdd:COG1820 1 AITNARIFTGDgVLEDGALLIEDGRIAAIG------PGAEPDAEVIDLGGGYLAPGFIDLHVHggGGVDFMDG-TPEALR 73
|
90
....*....|..
gi 530388815 85 QGTKAALSGGTT 96
Cdd:COG1820 74 TIARAHARHGTT 85
|
|
| FwdA |
COG1229 |
Formylmethanofuran dehydrogenase subunit A [Energy production and conversion]; |
5-69 |
1.70e-08 |
|
Formylmethanofuran dehydrogenase subunit A [Energy production and conversion];
Pssm-ID: 440842 Cd Length: 554 Bit Score: 57.12 E-value: 1.70e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 530388815 5 SRLLIRGGRV---VNDDFSEVADVLVEDGVVRALghdllPPGGAPAglRVLDAAGKLVLPGGIDTHTH 69
Cdd:COG1229 1 MELIIKNGRVydpANGIDGEVMDIAIKDGKIVEE-----PSDPKDA--KVIDASGKVVMAGGVDIHTH 61
|
|
| PRK08204 |
PRK08204 |
hypothetical protein; Provisional |
4-69 |
2.29e-08 |
|
hypothetical protein; Provisional
Pssm-ID: 181288 [Multi-domain] Cd Length: 449 Bit Score: 56.55 E-value: 2.29e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530388815 4 PSRLLIRGGRVVNDD----FSEVADVLVEDGVVRALGhdllpPGGAPAGLRVLDAAGKLVLPGGIDTHTH 69
Cdd:PRK08204 1 MKRTLIRGGTVLTMDpaigDLPRGDILIEGDRIAAVA-----PSIEAPDAEVVDARGMIVMPGLVDTHRH 65
|
|
| Imidazolone-5PH |
cd01296 |
Imidazolonepropionase/imidazolone-5-propionate hydrolase (Imidazolone-5PH) catalyzes the third ... |
25-99 |
4.38e-08 |
|
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: 55.34 E-value: 4.38e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 530388815 25 VLVEDGVVRALG--HDLLPPGGAPAglRVLDAAGKLVLPGGIDTHTHmqFPFMGSRSiDDFhqgtKAALSGGTTMII 99
Cdd:cd01296 1 IAIRDGRIAAVGpaASLPAPGPAAA--EEIDAGGRAVTPGLVDCHTH--LVFAGDRV-DEF----AARLAGASYEEI 68
|
|
| CAD_DHOase |
cd01316 |
The eukaryotic CAD protein is a trifunctional enzyme of carbamoylphosphate ... |
60-393 |
5.62e-08 |
|
The eukaryotic CAD protein is a trifunctional enzyme of carbamoylphosphate synthetase-aspartate transcarbamoylase-dihydroorotase, which catalyzes the first three steps of de novo pyrimidine nucleotide biosynthesis. Dihydroorotase (DHOase) catalyzes the third step, the reversible interconversion of carbamoyl aspartate to dihydroorotate.
Pssm-ID: 238641 [Multi-domain] Cd Length: 344 Bit Score: 54.76 E-value: 5.62e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530388815 60 LPGGIDTHTHMQFPfmGSRSIDDFHQGTKAALSGGTTMIIdfAIPQKGGSLI--EAFETWRSWADPKVCCDYSLHVAVTw 137
Cdd:cd01316 5 LPGLIDVHVHLREP--GATHKEDFASGTKAALAGGFTMVR--AMPNTNPSIVdvASLKLVQSLAQAKARCDYAFSIGAT- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530388815 138 wSDQVKEEMKilVQDKGVNSfKMFmaykdlymvtdleLYEAFSRCKEigaiaqvhaengDLIAEGAKKMLALGITgpegh 217
Cdd:cd01316 80 -STNAATVGE--LASEAVGL-KFY-------------LNETFSTLIL------------DKITAWASHFNAWPST----- 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530388815 218 elcRPEAVEAE-ATLRAI-TIASAVNCPLYIVHVMSKSAAKVIADARRDGKVVYGE--PIAASLGTDGTHYWNKEwhhaa 293
Cdd:cd01316 126 ---KPIVTHAKsQTLAAVlLLASLHNRSIHICHVSSKEEINLIRLAKARGLKVTCEvsPHHLFLSQDDLPRGQYE----- 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530388815 294 hhvmGPPLRPDPSTPDFLMNLLANDDLTTTGtdnctfnTCQKALGKDDFTKIPNGVNGVEDRMSVIWeKGVHSGKMDENR 373
Cdd:cd01316 198 ----VRPFLPTREDQEALWENLDYIDCFATD-------HAPHTLAEKTGNKPPPGFPGVETSLPLLL-TAVHEGRLTIED 265
|
330 340
....*....|....*....|
gi 530388815 374 FVAVTSTNAAKIFNLYPRKG 393
Cdd:cd01316 266 IVDRLHTNPKRIFNLPPQSD 285
|
|
| Met_dep_hydrolase_B |
cd01307 |
Metallo-dependent hydrolases, subgroup B is part of the superfamily of metallo-dependent ... |
24-409 |
7.05e-08 |
|
Metallo-dependent hydrolases, subgroup B 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: 238632 [Multi-domain] Cd Length: 338 Bit Score: 54.64 E-value: 7.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530388815 24 DVLVEDGVVRALGHDLLPPGGApaglRVLDAAGKLVLPGGIDTHTHMqFPFMGSRSIDDFHQGTKAalsgGTTMIIDfai 103
Cdd:cd01307 1 DVAIENGKIAAVGAALAAPAAT----QIVDAGGCYVSPGWIDLHVHV-YQGGTRYGDRPDMIGVKS----GVTTVVD--- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530388815 104 pqKGGSLIEAFETWRSwadpkvccdyslHVAvtwwsDQVKEEMKilvqdkgvnsfkmfmAYKDLYMVTDLELYEAFS-RC 182
Cdd:cd01307 69 --AGSAGADNIDGFRY------------TVI-----ERSATRVY---------------AFLNISRVGLVAQDELPDpDN 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530388815 183 KEIGAIAQVHAENGDLIAeGAKKMLALGITGPEGHELCRpeaveaeatlRAITIASAVNCPLYiVHVMSKSA--AKVIAD 260
Cdd:cd01307 115 IDEDAVVAAAREYPDVIV-GLKARASKSVVGEWGIKPLE----------LAKKIAKEADLPLM-VHIGSPPPilDEVVPL 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530388815 261 ARRdGKVVygepiaaslgtdgTHYWNK----------EWHHAAHHVMGPPLRPDpstpdflmnlLANddltttGTDNCTF 330
Cdd:cd01307 183 LRR-GDVL-------------THCFNGkpngivdeegEVLPLVRRARERGVIFD----------VGH------GTASFSF 232
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530388815 331 NTCQKA---------LGKDDFTKipNGVNGVEDRMSVIWEKGVHSGKMDENRFVAVTsTNAAKIFNLyPRKGRIAVGSDA 401
Cdd:cd01307 233 RVARAAiaagllpdtISSDIHGR--NRTNGPVYALATTLSKLLALGMPLEEVIEAVT-ANPARMLGL-AEIGTLAVGYDA 308
|
....*...
gi 530388815 402 DIVIWDPK 409
Cdd:cd01307 309 DLTVFDLK 316
|
|
| NagA |
cd00854 |
N-acetylglucosamine-6-phosphate deacetylase, NagA, catalyzes the hydrolysis of the N-acetyl ... |
7-69 |
1.18e-07 |
|
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: 54.12 E-value: 1.18e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 530388815 7 LLIRGGRVVNDDFSEVADVLVEDGVVRALGhdllPPGGAPAGLRVLDAAGKLVLPGGIDTHTH 69
Cdd:cd00854 1 LIIKNARILTPGGLEDGAVLVEDGKIVAIG----PEDELEEADEIIDLKGQYLVPGFIDIHIH 59
|
|
| Bact_CD |
cd01293 |
Bacterial cytosine deaminase and related metal-dependent hydrolases. Cytosine deaminases (CDs) ... |
8-70 |
1.24e-07 |
|
Bacterial cytosine deaminase and related metal-dependent hydrolases. Cytosine deaminases (CDs) catalyze the deamination of cytosine, producing uracil and ammonia. They play an important role in pyrimidine salvage. CDs are present in prokaryotes and fungi, but not mammalian cells. The bacterial enzymes, but not the fungal enzymes, are related to the adenosine deaminases (ADA). The bacterial enzymes are iron dependent and hexameric.
Pssm-ID: 238618 [Multi-domain] Cd Length: 398 Bit Score: 54.18 E-value: 1.24e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 530388815 8 LIRGGRVVNDDFSEVaDVLVEDGVVRALGHDLLPPGGAPaglrVLDAAGKLVLPGGIDTHTHM 70
Cdd:cd01293 1 LLRNARLADGGTALV-DIAIEDGRIAAIGPALAVPPDAE----EVDAKGRLVLPAFVDPHIHL 58
|
|
| PRK09228 |
PRK09228 |
guanine deaminase; Provisional |
25-73 |
2.39e-07 |
|
guanine deaminase; Provisional
Pssm-ID: 236419 [Multi-domain] Cd Length: 433 Bit Score: 53.27 E-value: 2.39e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 530388815 25 VLVEDGVVRALGH--DLLPpgGAPAGLRVLDAAGKLVLPGGIDTHTHmqFP 73
Cdd:PRK09228 34 LLVEDGRIVAAGPyaELRA--QLPADAEVTDYRGKLILPGFIDTHIH--YP 80
|
|
| PRK08203 |
PRK08203 |
hydroxydechloroatrazine ethylaminohydrolase; Reviewed |
5-70 |
3.06e-07 |
|
hydroxydechloroatrazine ethylaminohydrolase; Reviewed
Pssm-ID: 236184 [Multi-domain] Cd Length: 451 Bit Score: 52.93 E-value: 3.06e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 530388815 5 SRLLIRGGRVV---NDDFSEVAD--VLVEDGVVRALGhdllpPGGAP--AGLRVLDAAGKLVLPGGIDTHTHM 70
Cdd:PRK08203 1 TTLWIKNPLAIvtmDAARREIADggLVVEGGRIVEVG-----PGGALpqPADEVFDARGHVVTPGLVNTHHHF 68
|
|
| PRK05985 |
PRK05985 |
cytosine deaminase; Provisional |
7-78 |
4.56e-07 |
|
cytosine deaminase; Provisional
Pssm-ID: 180337 [Multi-domain] Cd Length: 391 Bit Score: 52.24 E-value: 4.56e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 530388815 7 LLIRGGRvvnDDFSEVADVLVEDGVVRALGhdllPPGGAPAGLRVLDAAGKLVLPGGIDTHTHMQFPFMGSR 78
Cdd:PRK05985 4 LLFRNVR---PAGGAAVDILIRDGRIAAIG----PALAAPPGAEVEDGGGALALPGLVDGHIHLDKTFWGDP 68
|
|
| PRK07583 |
PRK07583 |
cytosine deaminase; |
23-122 |
1.00e-06 |
|
cytosine deaminase;
Pssm-ID: 236062 Cd Length: 438 Bit Score: 51.14 E-value: 1.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530388815 23 ADVLVEDGVVRALghdlLPPGGAPAGLRVLDAAGKLVLPGGIDTHTHM-------QFP-----FMGSR-----------S 79
Cdd:PRK07583 41 VDIEIADGKIAAI----LPAGGAPDELPAVDLKGRMVWPCFVDMHTHLdkghiwpRSPnpdgtFPGALdavtadreahwS 116
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 530388815 80 IDDFHQ----GTKAALSGGTTMI---IDFAIPQKGGSLiEAFETWRS-WAD 122
Cdd:PRK07583 117 AEDLYRrmefGLRCAYAHGTSAIrthLDSFAPQAAISW-EVFAELREaWAG 166
|
|
| PRK15446 |
PRK15446 |
phosphonate metabolism protein PhnM; Provisional |
4-68 |
2.57e-06 |
|
phosphonate metabolism protein PhnM; Provisional
Pssm-ID: 237967 [Multi-domain] Cd Length: 383 Bit Score: 49.79 E-value: 2.57e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 530388815 4 PSRLLIRGGRVVNDDfsEV--ADVLVEDGVVRALGhdllpPGGAPAGlRVLDAAGKLVLPGGIDTHT 68
Cdd:PRK15446 1 MMEMILSNARLVLPD--EVvdGSLLIEDGRIAAID-----PGASALP-GAIDAEGDYLLPGLVDLHT 59
|
|
| PRK08417 |
PRK08417 |
metal-dependent hydrolase; |
348-409 |
3.24e-06 |
|
metal-dependent hydrolase;
Pssm-ID: 236262 [Multi-domain] Cd Length: 386 Bit Score: 49.70 E-value: 3.24e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 530388815 348 GVNGVEDRMSVIWEKGVHSGKMDENRFVAVTSTNAAKIFNLypRKGRIAVGSDADIVIWDPK 409
Cdd:PRK08417 294 GIDSICEYFSLCYTYLVKEGIITWSELSRFTSYNPAQFLGL--NSGEIEVGKEADLVLFDPN 353
|
|
| NagA |
COG1820 |
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism]; |
375-408 |
4.64e-06 |
|
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism];
Pssm-ID: 441425 [Multi-domain] Cd Length: 373 Bit Score: 48.94 E-value: 4.64e-06
10 20 30
....*....|....*....|....*....|....
gi 530388815 375 VAVTSTNAAKIFNLYPRKGRIAVGSDADIVIWDP 408
Cdd:COG1820 328 VRMASLNPARALGLDDRKGSIAPGKDADLVVLDD 361
|
|
| NagA |
cd00854 |
N-acetylglucosamine-6-phosphate deacetylase, NagA, catalyzes the hydrolysis of the N-acetyl ... |
375-411 |
7.37e-06 |
|
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: 48.34 E-value: 7.37e-06
10 20 30
....*....|....*....|....*....|....*..
gi 530388815 375 VAVTSTNAAKIFNLYPRKGRIAVGSDADIVIWDPKGT 411
Cdd:cd00854 330 VRMASLNPAKLLGLDDRKGSLKPGKDADLVVLDDDLN 366
|
|
| PRK08393 |
PRK08393 |
N-ethylammeline chlorohydrolase; Provisional |
7-69 |
1.28e-05 |
|
N-ethylammeline chlorohydrolase; Provisional
Pssm-ID: 181411 [Multi-domain] Cd Length: 424 Bit Score: 47.87 E-value: 1.28e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 530388815 7 LLIRGGRVVNDDFSEV--ADVLVEDGVVRALGHDLLPPGGApaglrVLDAAGKLVLPGGIDTHTH 69
Cdd:PRK08393 3 ILIKNGYVIYGENLKVirADVLIEGNKIVEVKRNINKPADT-----VIDASGSVVSPGFINAHTH 62
|
|
| PRK07369 |
PRK07369 |
dihydroorotase; Provisional |
5-411 |
1.51e-05 |
|
dihydroorotase; Provisional
Pssm-ID: 236002 [Multi-domain] Cd Length: 418 Bit Score: 47.67 E-value: 1.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530388815 5 SRLLIRGGRVVnDDFS---EVADVLVEDGVVRALGHDLLPpggAPAGLRVLDAAGKLVLPGGIDTHTHMQFPfmGSRSID 81
Cdd:PRK07369 2 SNELLQQVRVL-DPVSntdRIADVLIEDGKIQAIEPHIDP---IPPDTQIIDASGLILGPGLVDLYSHSGEP--GFEERE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530388815 82 DFHQGTKAALSGGTTMI---------ID-----FAIPQKGGSLieAFETWRSWAdpkvccDYSLHVA---VTWWSDqvke 144
Cdd:PRK07369 76 TLASLAAAAAAGGFTRVailpdtfppLDnpatlARLQQQAQQI--PPVQLHFWG------ALTLGGQgkqLTELAE---- 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530388815 145 emkiLVQdKGVNSFKMFMAYKDLYMVTD-LELYEAFSRckeigAIAQVhAENGDLIAEG----AKKMLALGITGpeghel 219
Cdd:PRK07369 144 ----LAA-AGVVGFTDGQPLENLALLRRlLEYLKPLGK-----PVALW-PCDRSLAGNGvmreGLLALRLGLPG------ 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530388815 220 cRPEAVEAEATLRAITIASAVNCPlyiVHVMSKSAAK---VIADARRDGKvvygePIAASLgtdgthywnkEWHH----- 291
Cdd:PRK07369 207 -DPASAETTALAALLELVAAIGTP---VHLMRISTARsveLIAQAKARGL-----PITAST----------TWMHllldt 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530388815 292 ---AAHHV---MGPPLrPDPSTPDFLMNLLANDDLTTTGTDNCTFNTCQKALGkddFTKIPNGVNGVEDRMSVIWEKGVH 365
Cdd:PRK07369 268 ealASYDPnlrLDPPL-GNPSDRQALIEGVRTGVIDAIAIDHAPYTYEEKTVA---FAEAPPGAIGLELALPLLWQNLVE 343
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 530388815 366 SGKMDENRFVAVTSTNAAKIFNLYPRkgRIAVGSDADIVIWDPKGT 411
Cdd:PRK07369 344 TGELSALQLWQALSTNPARCLGQEPP--SLAPGQPAELILFDPQKT 387
|
|
| AdeC |
COG1001 |
Adenine deaminase [Nucleotide transport and metabolism]; |
7-70 |
2.18e-05 |
|
Adenine deaminase [Nucleotide transport and metabolism];
Pssm-ID: 440625 [Multi-domain] Cd Length: 559 Bit Score: 47.02 E-value: 2.18e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 530388815 7 LLIRGGRVVNDDFSEV--ADVLVEDGVVRALGHDLLPpggapaGLRVLDAAGKLVLPGGIDTHTHM 70
Cdd:COG1001 7 LVIKNGRLVNVFTGEIleGDIAIAGGRIAGVGDYIGE------ATEVIDAAGRYLVPGFIDGHVHI 66
|
|
| FMDH_A |
cd01304 |
Formylmethanofuran dehydrogenase (FMDH) subunit A; Methanogenic bacteria and archea derive ... |
9-69 |
2.27e-05 |
|
Formylmethanofuran dehydrogenase (FMDH) subunit A; Methanogenic bacteria and archea derive the energy for autotrophic growth from methanogenesis, the reduction of CO2 with molecular hydrogen as the electron donor. FMDH catalyzes the first step in methanogenesis, the formyl-methanofuran synthesis. In this step, CO2 is bound to methanofuran and subsequently reduced to the formyl state with electrons derived from hydrogen.
Pssm-ID: 238629 [Multi-domain] Cd Length: 541 Bit Score: 47.02 E-value: 2.27e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 530388815 9 IRGGRVV---NDDFSEVADVLVEDGVVRAlghdllPPGGAPAGlRVLDAAGKLVLPGGIDTHTH 69
Cdd:cd01304 1 IKNGTVYdplNGINGEKMDIFIRDGKIVE------SSSGAKPA-KVIDASGKVVMAGGVDMHSH 57
|
|
| PRK07228 |
PRK07228 |
5'-deoxyadenosine deaminase; |
5-69 |
3.27e-05 |
|
5'-deoxyadenosine deaminase;
Pssm-ID: 180895 [Multi-domain] Cd Length: 445 Bit Score: 46.53 E-value: 3.27e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 530388815 5 SRLLIRGGRVVNDDFSEV---ADVLVEDGVVRALGhDLLPPGGAPaglRVLDAAGKLVLPGGIDTHTH 69
Cdd:PRK07228 1 MTILIKNAGIVTMNAKREivdGDVLIEDDRIAAVG-DRLDLEDYD---DHIDATGKVVIPGLIQGHIH 64
|
|
| pyrC |
PRK00369 |
dihydroorotase; Provisional |
56-405 |
5.53e-05 |
|
dihydroorotase; Provisional
Pssm-ID: 234738 [Multi-domain] Cd Length: 392 Bit Score: 45.52 E-value: 5.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530388815 56 GKLVLPGGIDTHTHMQFPFMGSRsiDDFHQGTKAALSGGTTMIIDFAIPQKGGSLIEAFETWRSWADPKVCCDYSLHVAV 135
Cdd:PRK00369 42 GTLILPGAIDLHVHLRGLKLSYK--EDVASGTSEAAYGGVTLVADMPNTIPPLNTPEAITEKLAELEYYSRVDYFVYSGV 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530388815 136 TwwsdqvKEEMKILvqDKGVNSFKMFmaykdlymVTDLELYEAFSRCKEIGAIAQVHAENGDLIAEGAKKMLAlgitgpe 215
Cdd:PRK00369 120 T------KDPEKVD--KLPIAGYKIF--------PEDLEREETFRVLLKSRKLKILHPEVPLALKSNRKLRRN------- 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530388815 216 ghelCRPEaveaeatlraitIASavncpLYIVHvmskSAAKV-IADARRDGKVVygepIAASLG--TDGThywnkewhha 292
Cdd:PRK00369 177 ----CWYE------------IAA-----LYYVK----DYQNVhITHASNPRTVR----LAKELGftVDIT---------- 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530388815 293 AHHVM-----------GPPLRpDPSTPDFLMNLLANDDltTTGTDNCTFNTCQKalgKDDFTKIPNGVNGVEDRMSVIWE 361
Cdd:PRK00369 218 PHHLLvngekdcltkvNPPIR-DINERLWLLQALSEVD--AIASDHAPHSSFEK---LQPYEVCPPGIAALSFTPPFIYT 291
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 530388815 362 KgVHSGKMDENRFVAVTSTNAAKIFNLypRKGRIAVGSDADIVI 405
Cdd:PRK00369 292 L-VSKGILSIDRAVELISTNPARILGI--PYGEIKEGYRANFTV 332
|
|
| YtcJ_like |
cd01300 |
YtcJ_like metal dependent amidohydrolases. YtcJ is a Bacillus subtilis ORF of unknown function. ... |
24-70 |
8.87e-05 |
|
YtcJ_like metal dependent amidohydrolases. YtcJ is a Bacillus subtilis ORF of unknown function. The Arabidopsis homolog LAF3 has been identified as a factor required for phytochrome A signalling.
Pssm-ID: 238625 [Multi-domain] Cd Length: 479 Bit Score: 44.99 E-value: 8.87e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 530388815 24 DVLVEDGVVRALGHDLLPPGGAPAGLRVLDAAGKLVLPGGIDTHTHM 70
Cdd:cd01300 1 AVAVRDGRIVAVGSDAEAKALKGPATEVIDLKGKTVLPGFIDSHSHL 47
|
|
| PRK07203 |
PRK07203 |
putative aminohydrolase SsnA; |
7-69 |
2.35e-04 |
|
putative aminohydrolase SsnA;
Pssm-ID: 235963 [Multi-domain] Cd Length: 442 Bit Score: 43.77 E-value: 2.35e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 530388815 7 LLIRGGRVVNDD----FSEVADVLVEDGVVRALGH--DLlppGGAPAGLRVLDAAGKLVLPGGIDTHTH 69
Cdd:PRK07203 2 LLIGNGTAITRDpakpVIEDGAIAIEGNVIVEIGTtdEL---KAKYPDAEFIDAKGKLIMPGLINSHNH 67
|
|
| PRK07627 |
PRK07627 |
dihydroorotase; Provisional |
6-96 |
3.36e-04 |
|
dihydroorotase; Provisional
Pssm-ID: 181059 [Multi-domain] Cd Length: 425 Bit Score: 43.13 E-value: 3.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530388815 6 RLLIRGGRVVN--DDFSEVADVLVEDGVVRALGHdllppggAPAGL---RVLDAAGKLVLPGGIDTHTHMQFPFMGsrsi 80
Cdd:PRK07627 2 KIHIKGGRLIDpaAGTDRQADLYVAAGKIAAIGQ-------APAGFnadKTIDASGLIVCPGLVDLSARLREPGYE---- 70
|
90 100
....*....|....*....|.
gi 530388815 81 ddfHQGT-----KAALSGGTT 96
Cdd:PRK07627 71 ---YKATlesemAAAVAGGVT 88
|
|
| GDEase |
cd01303 |
Guanine deaminase (GDEase). Guanine deaminase is an aminohydrolase responsible for the ... |
17-77 |
3.45e-04 |
|
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: 43.04 E-value: 3.45e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 530388815 17 DDFSEVADVL--VEDGVVRALGHDLLPPGG-------APAGLRVLDAAGKLVLPGGIDTHTHM-QFPFMGS 77
Cdd:cd01303 12 PELELVEDALrvVEDGLIVVVDGNIIAAGAaetlkraAKPGARVIDSPNQFILPGFIDTHIHApQYANIGS 82
|
|
| Amidohydro_3 |
pfam07969 |
Amidohydrolase family; |
50-408 |
5.00e-04 |
|
Amidohydrolase family;
Pssm-ID: 400360 [Multi-domain] Cd Length: 464 Bit Score: 42.90 E-value: 5.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530388815 50 RVLDAAGKLVLPGGIDTHTHMQFPFMGSRSID--DFHQGTKAALSGGTTmiiDFAIPQKGGSLIEAFETWRSWADPKVCC 127
Cdd:pfam07969 1 EVIDAKGRLVLPGFVDPHTHLDGGGLNLRELRlpDVLPNAVVKGQAGRT---PKGRWLVGEGWDEAQFAETRFPYALADL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530388815 128 D------------YSLHVAV---------------------------TWW------SDQVKEEMKILVQDKGVNSFKMFM 162
Cdd:pfam07969 78 DevapdgpvllraLHTHAAVansaaldlagitkatedppggeiardaNGEgltgllREGAYALPPLLAREAEAAAVAAAL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530388815 163 AY----------KDLYMVTDLELYEAFSRCKEIGAIAQVHAE--------NGDLIAEGAKKMLALGITG--------PEG 216
Cdd:pfam07969 158 AAlpgfgitsvdGGGGNVHSLDDYEPLRELTAAEKLKELLDAperlglphSIYELRIGAMKLFADGVLGsrtaaltePYF 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530388815 217 HELCRPEAVEAEATL-RAITIASAVNCPLYIV------------HVMSKSAAKVIADARRD--GKVVYG------EPIAA 275
Cdd:pfam07969 238 DAPGTGWPDFEDEALaELVAAARERGLDVAIHaigdatidtaldAFEAVAEKLGNQGRVRIehAQGVVPytysqiERVAA 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530388815 276 SLGTDGTHYwnKEWHHAAHHVMGPPLRPDPSTPDFLMNLLANDDLTTTGTDN--CTFntcqkalgkDDFTKIPNGVNG-V 352
Cdd:pfam07969 318 LGGAAGVQP--VFDPLWGDWLQDRLGAERARGLTPVKELLNAGVKVALGSDApvGPF---------DPWPRIGAAVMRqT 386
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 530388815 353 EDRMSVIWEkgvhSGKMDENRFVAVTSTNAAKIFNLYPRKGRIAVGSDADIVIWDP 408
Cdd:pfam07969 387 AGGGEVLGP----DEELSLEEALALYTSGPAKALGLEDRKGTLGVGKDADLVVLDD 438
|
|
| PRK07572 |
PRK07572 |
cytosine deaminase; Validated |
7-70 |
9.94e-04 |
|
cytosine deaminase; Validated
Pssm-ID: 181039 Cd Length: 426 Bit Score: 41.54 E-value: 9.94e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 530388815 7 LLIRGGRVvnDDFSEVADVLVEDGVVRALGHDLlppgGAPAGlRVLDAAGKLVLPGGIDTHTHM 70
Cdd:PRK07572 4 LIVRNANL--PDGRTGIDIGIAGGRIAAVEPGL----QAEAA-EEIDAAGRLVSPPFVDPHFHM 60
|
|
| PRK06038 |
PRK06038 |
N-ethylammeline chlorohydrolase; Provisional |
7-69 |
2.95e-03 |
|
N-ethylammeline chlorohydrolase; Provisional
Pssm-ID: 180363 [Multi-domain] Cd Length: 430 Bit Score: 40.12 E-value: 2.95e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 530388815 7 LLIRGGRVVNDDFSEV--ADVLVEDGVVRALGHDllPPGGAPaglRVLDAAGKLVLPGGIDTHTH 69
Cdd:PRK06038 4 IIIKNAYVLTMDAGDLkkGSVVIEDGTITEVSES--TPGDAD---TVIDAKGSVVMPGLVNTHTH 63
|
|
| Met_dep_hydrolase_C |
cd01309 |
Metallo-dependent hydrolases, subgroup C is part of the superfamily of metallo-dependent ... |
376-407 |
3.04e-03 |
|
Metallo-dependent hydrolases, subgroup C 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: 238634 [Multi-domain] Cd Length: 359 Bit Score: 39.99 E-value: 3.04e-03
10 20 30
....*....|....*....|....*....|..
gi 530388815 376 AVTStNAAKIFNLYPRKGRIAVGSDADIVIWD 407
Cdd:cd01309 308 AITI-NPAKILGIEDRVGSLEPGKDADLVVWN 338
|
|
| Isoaspartyl-dipeptidase |
cd01308 |
Isoaspartyl dipeptidase hydrolyzes the beta-L-isoaspartyl linkages in dipeptides, as part of ... |
377-409 |
3.59e-03 |
|
Isoaspartyl dipeptidase hydrolyzes the beta-L-isoaspartyl linkages in dipeptides, as part of the degradative pathway to eliminate proteins with beta-L-isoaspartyl peptide bonds, bonds whereby the beta-group of an aspartate forms the peptide link with the amino group of the following amino acid. Formation of this bond is a spontaneous nonenzymatic reaction in nature and can profoundly effect the function of the protein. Isoaspartyl dipeptidase is an octameric enzyme that contains a binuclear zinc center in the active site of each subunit and shows a strong preference of hydrolyzing Asp-Leu dipeptides.
Pssm-ID: 238633 [Multi-domain] Cd Length: 387 Bit Score: 39.68 E-value: 3.59e-03
10 20 30
....*....|....*....|....*....|...
gi 530388815 377 VTSTNAAKIFNLYPrKGRIAVGSDADIVIWDPK 409
Cdd:cd01308 330 VITSNVARILKLRK-KGEIQPGFDADLVILDKD 361
|
|
| Isoaspartyl-dipeptidase |
cd01308 |
Isoaspartyl dipeptidase hydrolyzes the beta-L-isoaspartyl linkages in dipeptides, as part of ... |
7-70 |
5.71e-03 |
|
Isoaspartyl dipeptidase hydrolyzes the beta-L-isoaspartyl linkages in dipeptides, as part of the degradative pathway to eliminate proteins with beta-L-isoaspartyl peptide bonds, bonds whereby the beta-group of an aspartate forms the peptide link with the amino group of the following amino acid. Formation of this bond is a spontaneous nonenzymatic reaction in nature and can profoundly effect the function of the protein. Isoaspartyl dipeptidase is an octameric enzyme that contains a binuclear zinc center in the active site of each subunit and shows a strong preference of hydrolyzing Asp-Leu dipeptides.
Pssm-ID: 238633 [Multi-domain] Cd Length: 387 Bit Score: 39.30 E-value: 5.71e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 530388815 7 LLIRGGRVVNDDFSEVADVLVEDGVVRALGHDLLPPGGApaGLRVLDAAGKLVLPGGIDTHTHM 70
Cdd:cd01308 2 TLIKNAEVYAPEYLGKKDILIAGGKILAIEDQLNLPGYE--NVTVVDLHGKILVPGFIDQHVHI 63
|
|
| PRK12393 |
PRK12393 |
amidohydrolase; Provisional |
23-70 |
6.38e-03 |
|
amidohydrolase; Provisional
Pssm-ID: 237088 [Multi-domain] Cd Length: 457 Bit Score: 39.28 E-value: 6.38e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 530388815 23 ADVLVEDGVVRALGHdlLPPggaPAGLRVLDAAGKLVLPGGIDTHTHM 70
Cdd:PRK12393 26 PDIRIRDGRIAAIGA--LTP---LPGERVIDATDCVVYPGWVNTHHHL 68
|
|
| Met_dep_hydrolase_C |
cd01309 |
Metallo-dependent hydrolases, subgroup C is part of the superfamily of metallo-dependent ... |
46-69 |
6.98e-03 |
|
Metallo-dependent hydrolases, subgroup C 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: 238634 [Multi-domain] Cd Length: 359 Bit Score: 38.83 E-value: 6.98e-03
10 20
....*....|....*....|....
gi 530388815 46 PAGLRVLDAAGKLVLPGGIDTHTH 69
Cdd:cd01309 14 PADAEVIDAKGKHVTPGLIDAHSH 37
|
|
| |
