|
Name |
Accession |
Description |
Interval |
E-value |
| D-HYD |
cd01314 |
D-hydantoinases (D-HYD) also called dihydropyrimidases (DHPase) and related proteins; DHPases ... |
7-460 |
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: 729.79 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21362535 7 LLIRGGRIVNDDFSQVADVLVEDGVVRALGRDLlppeDASRGLRILDAAGKLVLPGGIDTHTHMQFPFMGSQSVDDFYQG 86
Cdd:cd01314 1 LIIKNGTIVTADGSFKADILIEDGKIVAIGPNL----EAPGGVEVIDATGKYVLPGGIDPHTHLELPFMGTVTADDFESG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21362535 87 TKAALAGGTTMIIDFAIPQKGSSLIEAFETWRNWADPKVCCDYSLHVAVTWWSDKVKEEMKTLArDKGVNSFKMFMAYKG 166
Cdd:cd01314 77 TRAAAAGGTTTIIDFAIPNKGQSLLEAVEKWRGKADGKSVIDYGFHMIITDWTDSVIEELPELV-KKGISSFKVFMAYKG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21362535 167 LYMVQDEQLYAAFSQCKEIGAIAQVHAENGDLIAEGAKKMLALGITGPEGHELCRPEAVEAEATLRAITIASAVNCPLYV 246
Cdd:cd01314 156 LLMVDDEELLDVLKRAKELGALVMVHAENGDVIAELQKKLLAQGKTGPEYHALSRPPEVEAEATARAIRLAELAGAPLYI 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21362535 247 VHVMSKSAAKVVADARRAGNVVYGEPIAAGLGTDGRQYWsEEWSHAAHHVMGPPLRPDpLTPGFLMDLLANGDLTTTGSD 326
Cdd:cd01314 236 VHVSSKEAADEIARARKKGLPVYGETCPQYLLLDDSDYW-KDWFEGAKYVCSPPLRPK-EDQEALWDGLSSGTLQTVGSD 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21362535 327 NCTFNTCQKALGKDDFTKIPNGVNGVEDRMSVIWEKGVHSGKMDENRFVAVTSTNAAKIFNLYPKKGRIAVGSDADIVIW 406
Cdd:cd01314 314 HCPFNFAQKARGKDDFTKIPNGVPGVETRMPLLWSEGVAKGRITLEKFVELTSTNPAKIFGLYPRKGTIAVGSDADLVIW 393
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 21362535 407 DPEATRRISAKTHHQAVNFNIFEGMVCHGVPLVTISRGRVVYEAGVFNVTAGHG 460
Cdd:cd01314 394 DPNAEKTISADTHHHNVDYNIFEGMKVKGWPVVTISRGKVVVEDGELVGEKGSG 447
|
|
| D-hydantoinase |
TIGR02033 |
D-hydantoinase; This model represents the D-hydantoinase (dihydropyrimidinase) which primarily ... |
7-465 |
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: 643.28 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21362535 7 LLIRGGRIVNDDFSQVADVLVEDGVVRALGRDLLPPEdasrGLRILDAAGKLVLPGGIDTHTHMQFPFMGSQSVDDFYQG 86
Cdd:TIGR02033 1 LLIKGGTVVNADDVFQADVLIEGGKIVAVGDNLIPPD----AVEVIDATGKYVLPGGIDVHTHLEMPFGGTTTADDFFTG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21362535 87 TKAALAGGTTMIIDFAIPQKGSSLIEAFETWRNWADPKVCCDYSLHVAVTWWSDKVKEEMKTLARDKGVNSFKMFMAYKG 166
Cdd:TIGR02033 77 TKAAAAGGTTTIIDFVVPEKGSSLTEALETWHEKAEGKSVIDYGFHMDITHWNDSVLEEHIPEVKEEGINSFKVFMAYKN 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21362535 167 LYMVQDEQLYAAFSQCKEIGAIAQVHAENGDLIAEGAKKMLALGITGPEGHELCRPEAVEAEATLRAITIASAVNCPLYV 246
Cdd:TIGR02033 157 LLMVDDEELFEILKRLKELGALLQVHAENGDIIAELQARMLAQGITGPEYHALSRPPELEAEAVARAITLAALADAPLYV 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21362535 247 VHVMSKSAAKVVADARRAGNVVYGEPIAAGLGTDGRQYWsEEWSHAAHHVMGPPLRpDPLTPGFLMDLLANGDLTTTGSD 326
Cdd:TIGR02033 237 VHVSTKDAADEIAQARKKGQPVFGETCPQYLVLDDTHYD-KPGFEGAKYVCSPPLR-EPEDQDALWSALSSGALQTVGSD 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21362535 327 NCTFNTCQK-ALGKDDFTKIPNGVNGVEDRMSVIWEKGVHSGKMDENRFVAVTSTNAAKIFNLYPKKGRIAVGSDADIVI 405
Cdd:TIGR02033 315 HCTFNFAQKkAIGKDDFTKIPNGGPGVEERMSLLFDEGVAKGRITLEKFVEVTSTNPAKIFNLYPRKGTIAVGSDADIVI 394
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 21362535 406 WDPEATRRISAKTHHQAVNFNIFEGMVCHGVPLVTISRGRVVYEAGVFNVTAGHGKFIPR 465
Cdd:TIGR02033 395 WDPNRTTVISAETHHSNADYNPFEGFKVRGAPVSVLSRGRVVVEDGQLVGTAGAGRFVKR 454
|
|
| PRK08323 |
PRK08323 |
phenylhydantoinase; Validated |
6-472 |
0e+00 |
|
phenylhydantoinase; Validated
Pssm-ID: 236240 [Multi-domain] Cd Length: 459 Bit Score: 640.30 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21362535 6 RLLIRGGRIVNDDFSQVADVLVEDGVVRALGRDllppedasRGLRILDAAGKLVLPGGIDTHTHMQFPFMGSQSVDDFYQ 85
Cdd:PRK08323 2 STLIKNGTVVTADDTYKADVLIEDGKIAAIGAN--------LGDEVIDATGKYVMPGGIDPHTHMEMPFGGTVSSDDFET 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21362535 86 GTKAALAGGTTMIIDFAIPQKGSSLIEAFETWRNWADPKVCCDYSLHVAVTWWSDKVKEEMKTLArDKGVNSFKMFMAYK 165
Cdd:PRK08323 74 GTRAAACGGTTTIIDFALQPKGQSLREALEAWHGKAAGKAVIDYGFHMIITDWNEVVLDEMPELV-EEGITSFKLFMAYK 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21362535 166 GLYMVQDEQLYAAFSQCKEIGAIAQVHAENGDLIAEGAKKMLALGITGPEGHELCRPEAVEAEATLRAITIASAVNCPLY 245
Cdd:PRK08323 153 GALMLDDDELLRALQRAAELGALPMVHAENGDAIAYLQAKLLAEGKTGPEYHALSRPPEVEGEATNRAIMLAELAGAPLY 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21362535 246 VVHVMSKSAAKVVADARRAGNVVYGEPIAAGLGTDGRQYWSEEWSHAAHHVMGPPLRP----DPLTPGflmdlLANGDLT 321
Cdd:PRK08323 233 IVHVSCKEALEAIRRARARGQRVFGETCPQYLLLDESEYDGPDWFEGAKYVMSPPLRDkehqDALWRG-----LQDGDLQ 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21362535 322 TTGSDNCTFNTCQKA-LGKDDFTKIPNGVNGVEDRMSVIWEKGVHSGKMDENRFVAVTSTNAAKIFNLYPKKGRIAVGSD 400
Cdd:PRK08323 308 VVATDHCPFCFEQKKqLGRGDFTKIPNGTPGVEDRMPLLFSEGVMTGRITLNRFVELTSTNPAKIFGLYPRKGTIAVGAD 387
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 21362535 401 ADIVIWDPEATRRISAKTHHQAVNFNIFEGMVCHGVPLVTISRGRVVYEAGVFNVTAGHGKFIPRQPFAEYI 472
Cdd:PRK08323 388 ADIVIWDPNATKTISASTLHSNVDYNPYEGFEVTGWPVTTLSRGEVVVEDGEFRGKAGHGRFLKRKPFQAVV 459
|
|
| PLN02942 |
PLN02942 |
dihydropyrimidinase |
1-491 |
0e+00 |
|
dihydropyrimidinase
Pssm-ID: 178530 Cd Length: 486 Bit Score: 634.57 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21362535 1 MAPQGRLLIRGGRIVNDDFSQVADVLVEDGVVRALGRDLLPPEDAsrglRILDAAGKLVLPGGIDTHTHMQFPFMGSQSV 80
Cdd:PLN02942 1 GASSTKILIKGGTVVNAHHQELADVYVEDGIIVAVAPNLKVPDDV----RVIDATGKFVMPGGIDPHTHLAMPFMGTETI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21362535 81 DDFYQGTKAALAGGTTMIIDFAIPQKGSsLIEAFETWRNWADpKVCCDYSLHVAVTWWSDKVKEEMKTLARDKGVNSFKM 160
Cdd:PLN02942 77 DDFFSGQAAALAGGTTMHIDFVIPVNGN-LLAGYEAYEKKAE-KSCMDYGFHMAITKWDDTVSRDMETLVKEKGINSFKF 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21362535 161 FMAYKGLYMVQDEQLYAAFSQCKEIGAIAQVHAENGDLIAEGAKKMLALGITGPEGHELCRPEAVEAEATLRAITIASAV 240
Cdd:PLN02942 155 FMAYKGSLMVTDELLLEGFKRCKSLGALAMVHAENGDAVFEGQKRMIELGITGPEGHALSRPPLLEGEATARAIRLAKFV 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21362535 241 NCPLYVVHVMSKSAAKVVADARRAGNVVYGEPIAAGLGTDGRQYWSEEWSHAAHHVMGPPLRPDPlTPGFLMDLLANGDL 320
Cdd:PLN02942 235 NTPLYVVHVMSIDAMEEIARARKSGQRVIGEPVVSGLVLDDSKLWDPDFTIASKYVMSPPIRPAG-HGKALQAALSSGIL 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21362535 321 TTTGSDNCTFNTCQKALGKDDFTKIPNGVNGVEDRMSVIWEKGVHSGKMDENRFVAVTSTNAAKIFNLYPKKGRIAVGSD 400
Cdd:PLN02942 314 QLVGTDHCPFNSTQKAFGKDDFRKIPNGVNGIEERMHLVWDTMVESGQISPTDYVRVTSTECAKIFNIYPRKGAILAGSD 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21362535 401 ADIVIWDPEATRRISAKTHHQAVNFNIFEGMVCHGVPLVTISRGRVVYEAGVFNVTAGHGKFIPRQPFAeYIYKRIKQRD 480
Cdd:PLN02942 394 ADIIILNPNSTFTISAKTHHSRIDTNVYEGRRGKGKVEVTISQGRVVWENGELKVVRGSGRYIEMPPFS-YLFDGIQKAD 472
|
490
....*....|....
gi 21362535 481 QTCTP---VPVKRA 491
Cdd:PLN02942 473 AAYLSslrAPVKRT 486
|
|
| AllB |
COG0044 |
Dihydroorotase or related cyclic amidohydrolase [Nucleotide transport and metabolism]; ... |
8-465 |
3.64e-142 |
|
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: 416.41 E-value: 3.64e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21362535 8 LIRGGRIVNDDFSQVADVLVEDGVVRALGRDLLPPEDAsrglRILDAAGKLVLPGGIDTHTHMQFPFMGSQsvDDFYQGT 87
Cdd:COG0044 1 LIKNGRVVDPGGLERADVLIEDGRIAAIGPDLAAPEAA----EVIDATGLLVLPGLIDLHVHLREPGLEHK--EDIETGT 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21362535 88 KAALAGGTTMIIDFAIPQKGSSLIEAFETWRNWADPKVCCDYSLHVAVTWWSDKVKEEMKTLArDKGVNSFKMFMAYKGL 167
Cdd:COG0044 75 RAAAAGGVTTVVDMPNTNPVTDTPEALEFKLARAEEKALVDVGPHGALTKGLGENLAELGALA-EAGAVAFKVFMGSDDG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21362535 168 YMVQD-EQLYAAFSQCKEIGAIAQVHAENGDLIAEGAKkmlALGITGPEGHELCRPEAVEAEATLRAITIASAVNCPLYV 246
Cdd:COG0044 154 NPVLDdGLLRRALEYAAEFGALVAVHAEDPDLIRGGVM---NEGKTSPRLGLKGRPAEAEEEAVARDIALAEETGARLHI 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21362535 247 VHVMSKSAAKVVADARRAGNVVYGE--PiaaglgtdgrQY--WSEEW--SHAAHHVMGPPLRP--DPLTpgfLMDLLANG 318
Cdd:COG0044 231 VHVSTAEAVELIREAKARGLPVTAEvcP----------HHltLTDEDleRYGTNFKVNPPLRTeeDREA---LWEGLADG 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21362535 319 DLTTTGSDNCTFNTCQKAlgkDDFTKIPNGVNGVEDRMSVIWEKGVHSGKMDENRFVAVTSTNAAKIFNLyPKKGRIAVG 398
Cdd:COG0044 298 TIDVIATDHAPHTLEEKE---LPFAEAPNGIPGLETALPLLLTELVHKGRLSLERLVELLSTNPARIFGL-PRKGRIAVG 373
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 21362535 399 SDADIVIWDPEATRRISAKTHHQAVNFNIFEGMVCHGVPLVTISRGRVVYEAGVFnVTAGHGKFIPR 465
Cdd:COG0044 374 ADADLVLFDPDAEWTVTAEDLHSKSKNTPFEGRELTGRVVATIVRGRVVYEDGEV-VGEPRGRFLRR 439
|
|
| PRK13404 |
PRK13404 |
dihydropyrimidinase; Provisional |
3-465 |
2.34e-131 |
|
dihydropyrimidinase; Provisional
Pssm-ID: 184033 [Multi-domain] Cd Length: 477 Bit Score: 390.21 E-value: 2.34e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21362535 3 PQGRLLIRGGRIVNDDFSQVADVLVEDGVVRALGRDLLPpedasrGLRILDAAGKLVLPGGIDTHTHM-QFPFMGSQSVD 81
Cdd:PRK13404 2 MAFDLVIRGGTVVTATDTFQADIGIRGGRIAALGEGLGP------GAREIDATGRLVLPGGVDSHCHIdQPSGDGIMMAD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21362535 82 DFYQGTKAALAGGTTMIIDFAIPQKGSSLIEAFETWRNWADPKVCCDYSLHVAVTWWSDKV-KEEMKTLARDkGVNSFKM 160
Cdd:PRK13404 76 DFYTGTVSAAFGGTTTVIPFAAQHRGQSLREAVEDYHRRAAGKAVIDYAFHLIVADPTEEVlTEELPALIAQ-GYTSFKV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21362535 161 FMAYKGLyMVQDEQLYAAFSQCKEIGAIAQVHAENGDLIAEGAKKMLALGITGPEGHELCRPEAVEAEATLRAITIASAV 240
Cdd:PRK13404 155 FMTYDDL-KLDDRQILDVLAVARRHGAMVMVHAENHDMIAWLTKRLLAAGLTAPKYHAISRPMLAEREATHRAIALAELV 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21362535 241 NCPLYVVHVMSKSAAKVVADARRAGNVVYGEP-------IAAGLGTDGrqywseewSHAAHHVMGPPLRpDPLTPGFLMD 313
Cdd:PRK13404 234 DVPILIVHVSGREAAEQIRRARGRGLKIFAETcpqylflTAEDLDRPG--------MEGAKYICSPPPR-DKANQEAIWN 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21362535 314 LLANGDLTTTGSDNCTFN---TCQKALGKDD--FTKIPNGVNGVEDRMSVIWEKGVHSGKMDENRFVAVTSTNAAKIFNL 388
Cdd:PRK13404 305 GLADGTFEVFSSDHAPFRfddTDGKLAAGANpsFKAIANGIPGIETRLPLLFSEGVVKGRISLNRFVALTSTNPAKLYGL 384
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 21362535 389 YPKKGRIAVGSDADIVIWDPEATRRISAKTHHQAVNFNIFEGMVCHGVPLVTISRGRVVYEAGVFNVTAGHGKFIPR 465
Cdd:PRK13404 385 YPRKGAIAIGADADIAIWDPDREVTITNADLHHAADYTPYEGMRVTGWPVTVLSRGRVVVEDGELVAERGSGQFLAR 461
|
|
| L-HYD_ALN |
cd01315 |
L-Hydantoinases (L-HYDs) and Allantoinase (ALN); L-Hydantoinases are a member of the ... |
7-463 |
7.44e-74 |
|
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: 240.65 E-value: 7.44e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21362535 7 LLIRGGRIVNDDFSQVADVLVEDGVVRALGRDLLPPEdasrGLRILDAAGKLVLPGGIDTHTHMQFPfmGSQSVDDFYQG 86
Cdd:cd01315 2 LVIKNGRVVTPDGVREADIAVKGGKIAAIGPDIANTE----AEEVIDAGGLVVMPGLIDTHVHINEP--GRTEWEGFETG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21362535 87 TKAALAGGTTMIIDF---AIPQkgSSLIEAFETWRNWADPKvccdysLHVAVTWWSDKVK---EEMKTLArDKGVNSFKM 160
Cdd:cd01315 76 TKAAAAGGITTIIDMplnSIPP--TTTVENLEAKLEAAQGK------LHVDVGFWGGLVPgnlDQLRPLD-EAGVVGFKC 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21362535 161 FMAYKGLYM---VQDEQLYAAFSQCKEIGAIAQVHAENGDLIAEGAKKMLALGITGPEGHELCRPEAVEAEATLRAITIA 237
Cdd:cd01315 147 FLCPSGVDEfpaVDDEQLEEAMKELAKTGSVLAVHAENPEITEALQEQAKAKGKRDYRDYLASRPVFTEVEAIQRILLLA 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21362535 238 SAVNCPLYVVHVMSKSAAKVVADARRAGNVVYGEPIAAGLGTDGRQYwseEWSHAAHHVmGPPLRpDPLTPGFLMDLLAN 317
Cdd:cd01315 227 KETGCRLHIVHLSSAEAVPLIREARAEGVDVTVETCPHYLTFTAEDV---PDGGTEFKC-APPIR-DAANQEQLWEALEN 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21362535 318 GDLTTTGSDN--CTFNtcQKALGKDDFTKIPNGVNGVEDRMSVIWEKGVHSGKMDENRFVAVTSTNAAKIFNLYPKKGRI 395
Cdd:cd01315 302 GDIDMVVSDHspCTPE--LKLLGKGDFFKAWGGISGLQLGLPVMLTEAVNKRGLSLEDIARLMCENPAKLFGLSHQKGRI 379
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 21362535 396 AVGSDADIVIWDPEATRRISA---KTHHQAvnfNIFEGMVCHGVPLVTISRGRVVYEAGVFnVTAGHGKFI 463
Cdd:cd01315 380 AVGYDADFVVWDPEEEFTVDAedlYYKNKI---SPYVGRTLKGRVHATILRGTVVYQDGEV-VGEPLGQLL 446
|
|
| Cyclic_amidohydrolases |
cd01302 |
Cyclic amidohydrolases, including hydantoinase, dihydropyrimidinase, allantoinase, and ... |
57-440 |
1.18e-69 |
|
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: 226.50 E-value: 1.18e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21362535 57 KLVLPGGIDTHTHMQFPFMGSQSvDDFYQGTKAALAGGTTMIIDFAIPQKGSSLIEAFETWRNWADPKVCCDYSLHVAVt 136
Cdd:cd01302 1 LLVLPGFIDIHVHLRDPGGTTYK-EDFESGSRAAAAGGVTTVIDMPNTGPPPIDLPAIELKIKLAEESSYVDFSFHAGI- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21362535 137 wWSDKVKEEMKtLARDKGVNSFKMFMAYK--GLYMVQDEQLYAAFSQCKEIGAIAQVHAEngdliaegakkmlalgitgp 214
Cdd:cd01302 79 -GPGDVTDELK-KLFDAGINSLKVFMNYYfgELFDVDDGTLMRTFLEIASRGGPVMVHAE-------------------- 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21362535 215 eghelcrpeaveaeatlRAITIASAVNCPLYVVHVMSKSAAKVVADARRAGNVVYGEPIAAGLGTDgRQYWSEEWSHAah 294
Cdd:cd01302 137 -----------------RAAQLAEEAGANVHIAHVSSGEALELIKFAKNKGVKVTCEVCPHHLFLD-ESMLRLNGAWG-- 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21362535 295 hVMGPPLRPdPLTPGFLMDLLANGDLTTTGSDNCTFNTCQKALGKDdFTKIPNGVNGVEDRMSVIWEKGVHSGkMDENRF 374
Cdd:cd01302 197 -KVNPPLRS-KEDREALWEGVKNGKIDTIASDHAPHSKEEKESGKD-IWKAPPGFPGLETRLPILLTEGVKRG-LSLETL 272
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 21362535 375 VAVTSTNAAKIFNLYPKKgRIAVGSDADIVIWDPEATRRISAKTHHQAVNFNIFEGMVCHGVPLVT 440
Cdd:cd01302 273 VEILSENPARIFGLYPKG-TIAVGYDADLVIVDPKKEWKVTAEEIESKADWTPFEGMEVTGKPVST 337
|
|
| PRK02382 |
PRK02382 |
dihydroorotase; Provisional |
7-464 |
6.61e-62 |
|
dihydroorotase; Provisional
Pssm-ID: 179417 [Multi-domain] Cd Length: 443 Bit Score: 209.12 E-value: 6.61e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21362535 7 LLIRGGRIVNDDFSQVADVLVEDGVVRALGRDLlppeDASRGLRILDAAGKLVLPGGIDTHTHmqFPFMGSQSVDDFYQG 86
Cdd:PRK02382 4 ALLKDGRVYYNNSLQPRDVRIDGGKITAVGKDL----DGSSSEEVIDARGMLLLPGGIDVHVH--FREPGYTHKETWYTG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21362535 87 TKAALAGGTTMIIDfaIPQKGSSLI--EAFETWRNWADPKVCCDYSLHVAVTWWSDKVKEEMktlarDKGVNSF-KMFMA 163
Cdd:PRK02382 78 SRSAAAGGVTTVVD--QPNTDPPTVdgESFDEKAELAARKSIVDFGINGGVTGNWDPLESLW-----ERGVFALgEIFMA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21362535 164 YKGLYMVQDEQLYA-AFSQCKEIGAIAQVHAENGDLIAEGAKkmLALGITGPEGHELCRPEAVEAEATLRAITIASAVNC 242
Cdd:PRK02382 151 DSTGGMGIDEELFEeALAEAARLGVLATVHAEDEDLFDELAK--LLKGDADADAWSAYRPAAAEAAAVERALEVASETGA 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21362535 243 PLYVVHVmskSAAKVVADARRAGNVVYGEP--------IAAGLGTDGRqywseewshaahhvMGPPLRPDPLTPGfLMDL 314
Cdd:PRK02382 229 RIHIAHI---STPEGVDAARREGITCEVTPhhlflsrrDWERLGTFGK--------------MNPPLRSEKRREA-LWER 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21362535 315 LANGDLTTTGSDNCTFNTCQKALgkdDFTKIPNGVNGVEDRMSVIWEkGVHSGKMDENRFVAVTSTNAAKIFNLyPKKGR 394
Cdd:PRK02382 291 LNDGTIDVVASDHAPHTREEKDA---DIWDAPSGVPGVETMLPLLLA-AVRKNRLPLERVRDVTAANPARIFGL-DGKGR 365
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 21362535 395 IAVGSDADIVIWDPEATRRISAKTHHQAVNFNIFEGMVchGV-PLVTISRGRVVYEAGVFNVTAGHGKFIP 464
Cdd:PRK02382 366 IAEGYDADLVLVDPDAAREIRGDDLHSKAGWTPFEGME--GVfPELTMVRGTVVWDGDDINAKRGRGEFLR 434
|
|
| PRK06189 |
PRK06189 |
allantoinase; Provisional |
7-467 |
2.53e-51 |
|
allantoinase; Provisional
Pssm-ID: 235732 [Multi-domain] Cd Length: 451 Bit Score: 181.44 E-value: 2.53e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21362535 7 LLIRGGRIVNDDFSQVADVLVEDGVVRALGrdllpPEDASRGLRILDAAGKLVLPGGIDTHTHMQFPfmGSQSVDDFYQG 86
Cdd:PRK06189 5 LIIRGGKVVTPEGVYRADIGIKNGKIAEIA-----PEISSPAREIIDADGLYVFPGMIDVHVHFNEP--GRTHWEGFATG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21362535 87 TKAALAGGTTMIIDFAIPQKGSSLI-EAFETWRNWADPKVCCDYSLhvavtwWSDKV---KEEMKTLArDKGVNSFKMFM 162
Cdd:PRK06189 78 SAALAAGGCTTYFDMPLNSIPPTVTrEALDAKAELARQKSAVDFAL------WGGLVpgnLEHLRELA-EAGVIGFKAFM 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21362535 163 AYKGLY---MVQDEQLYAAFSQCKEIGAIAQVHAENGDLIAEGAKKMLALGITGPEGHELCRPEAVEAEATLRAITIASA 239
Cdd:PRK06189 151 SNSGTDefrSSDDLTLYEGMKEIAALGKILALHAESDALTRHLTTQARQQGKTDVRDYLESRPVVAELEAVQRALLYAQE 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21362535 240 VNCPLYVVHVMSKSAAKVVADARRAGNVVYGEPIAAGLGTDGRQYwsEEWSHAAHhvMGPPLRpDPLTPGFLMDLLANGD 319
Cdd:PRK06189 231 TGCPLHFVHISSGKAVALIAEAKKRGVDVSVETCPHYLLFTEEDF--ERIGAVAK--CAPPLR-SRSQKEELWRGLLAGE 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21362535 320 LTTTGSDNctfNTCQKALGK-DDFTKIPNGVNGVEDRMSVIWEKGVHSGKMDENRFVAVTSTNAAKIFNLyPKKGRIAVG 398
Cdd:PRK06189 306 IDMISSDH---SPCPPELKEgDDFFLVWGGISGGQSTLLVMLTEGYIERGIPLETIARLLATNPAKRFGL-PQKGRLEVG 381
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 21362535 399 SDADIVIWDPEATRRISAKTHHQAVNFNIFEGMVCHGVPLVTISRGRVVYEAGVFNVTAgHGKFIPRQP 467
Cdd:PRK06189 382 ADADFVLVDLDETYTLTKEDLFYRHKQSPYEGRTFPGRVVATYLRGQCVYQDGEVFPPP-RGQLLRPSV 449
|
|
| pyrC_multi |
TIGR00857 |
dihydroorotase, multifunctional complex type; In contrast to the homodimeric type of ... |
23-450 |
6.03e-51 |
|
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: 179.18 E-value: 6.03e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21362535 23 ADVLVEDGVVRALGRDLLPPEDAsrglrILDAAGKLVLPGGIDTHTHMQFPfmGSQSVDDFYQGTKAALAGGTTMIIDFA 102
Cdd:TIGR00857 6 VDILVEGGRIKKIGKLRIPPDAE-----VIDAKGLLVLPGFIDLHVHLRDP--GEEYKEDIESGSKAAAHGGFTTVADMP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21362535 103 IPQKGSSLIEAFETWRNWADPKVCCDYSLHVAVTWwSDKVKEEMKTLARDKGVNSFKMFMAYkGLYMVQDEQLYAAFSQC 182
Cdd:TIGR00857 79 NTKPPIDTPETLEWKLQRLKKVSLVDVHLYGGVTQ-GNQGKELTEAYELKEAGAVGRMFTDD-GSEVQDILSMRRALEYA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21362535 183 KEIGAIAQVHAENGDLIAEGAKKmlaLGITGPEGHELCRPEAVEAEATLRAITIASAVNCPLYVVHVMSKSAAKVVADAR 262
Cdd:TIGR00857 157 AIAGVPIALHAEDPDLIYGGVMH---EGPSAAQLGLPARPPEAEEVAVARLLELAKHAGCPVHICHISTKESLELIVKAK 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21362535 263 RAGNVVYGE--P--------IAAGLGTDGRqywseewshaahhvMGPPLRPD----PLTPGFLmdllaNGDLTTTGSDNC 328
Cdd:TIGR00857 234 SQGIKITAEvtPhhlllseeDVARLDGNGK--------------VNPPLREKedrlALIEGLK-----DGIIDIIATDHA 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21362535 329 TFNTCQKALGkddFTKIPNGVNGVEDRMSVIWEkGVHSGKMDENRFVAVTSTNAAKIFNLyPKKGRIAVGSDADIVIWDP 408
Cdd:TIGR00857 295 PHTLEEKTKE---FAAAPPGIPGLETALPLLLQ-LLVKGLISLKDLIRMLSINPARIFGL-PDKGTLEEGNPADITVFDL 369
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 21362535 409 EATRRISAKTHHQAVNFNIFEGMVCHGVPLVTISRGRVVYEA 450
Cdd:TIGR00857 370 KKEWTINAETFYSKAKNTPFEGMSLKGKPIATILRGKVVYED 411
|
|
| DHOase_IIb |
cd01318 |
Dihydroorotase (DHOase), subgroup IIb; DHOases catalyze the reversible interconversion of ... |
56-444 |
4.71e-39 |
|
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: 145.94 E-value: 4.71e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21362535 56 GKLVLPGGIDTHTHMQFPfmGSQSVDDFYQGTKAALAGGTTMIIDFAIPQKGSSLIEAFETWRNWADPKVCCDYSLHVAV 135
Cdd:cd01318 1 GLLILPGVIDIHVHFREP--GLTYKEDFVSGSRAAAAGGVTTVMDMPNTKPPTTTAEALYEKLRLAAAKSVVDYGLYFGV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21362535 136 TwwSDKVKEEMKTLardkGVNSFKMFMA-YKGLYMVQDEQLYAAFSQCKEIGAiaqVHAENGDLIAEGAKKMLALGItgp 214
Cdd:cd01318 79 T--GSEDLEELDKA----PPAGYKIFMGdSTGDLLDDEETLERIFAEGSVLVT---FHAEDEDRLRENRKELKGESA--- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21362535 215 egHELCRPEAVEAEATLRAITIASAVNCPLYVVHVMSKSAAKVVADARRAGNV-------VYGEPIAAGLGTDGRqywse 287
Cdd:cd01318 147 --HPRIRDAEAAAVATARALKLARRHGARLHICHVSTPEELKLIKKAKPGVTVevtphhlFLDVEDYDRLGTLGK----- 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21362535 288 ewshaahhvMGPPLRPDPLTPGfLMDLLANGDLTTTGSDNCTFNTCQKALGkddFTKIPNGVNGVEDRMSVIWEKgVHSG 367
Cdd:cd01318 220 ---------VNPPLRSREDRKA-LLQALADGRIDVIASDHAPHTLEEKRKG---YPAAPSGIPGVETALPLMLTL-VNKG 285
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 21362535 368 KMDENRFVAVTSTNAAKIFNLyPKKGRIAVGSDADIVIWDPEATRRISAKTHHQAVNFNIFEGMVCHGVPLVTISRG 444
Cdd:cd01318 286 ILSLSRVVRLTSHNPARIFGI-KNKGRIAEGYDADLTVVDLKEERTIRAEEFHSKAGWTPFEGFEVTGFPVMTIVRG 361
|
|
| PRK08044 |
PRK08044 |
allantoinase AllB; |
7-464 |
8.04e-38 |
|
allantoinase AllB;
Pssm-ID: 169193 [Multi-domain] Cd Length: 449 Bit Score: 144.23 E-value: 8.04e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21362535 7 LLIRGGRIVNDDFSQVADVLVEDGVVRALGRDLLPPEdasrglRILDAAGKLVLPGGIDTHTHMQFPfmGSQSVDDFYQG 86
Cdd:PRK08044 5 LIIKNGTVILENEARVVDIAVKGGKIAAIGQDLGDAK------EVMDASGLVVSPGMVDAHTHISEP--GRSHWEGYETG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21362535 87 TKAALAGGTTMIIDFAIPQKGSSLIEA-FETWRNWADPKVCCDY-SLHVAVTWWSDKVKEemktlARDKGVNSFKMFMAY 164
Cdd:PRK08044 77 TRAAAKGGITTMIEMPLNQLPATVDRAsIELKFDAAKGKLTIDAaQLGGLVSYNLDRLHE-----LDEVGVVGFKCFVAT 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21362535 165 KG-------LYMVQDEQLYAAFSQCKEIGAIAQVHAENG---DLIAEGAKKMlalGITGPEGHELCRPEAVEAEATLRAI 234
Cdd:PRK08044 152 CGdrgidndFRDVNDWQFYKGAQKLGELGQPVLVHCENAlicDELGEEAKRE---GRVTAHDYVASRPVFTEVEAIRRVL 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21362535 235 TIASAVNCPLYVVHVMSKSAAKVVADARRAGNVVYGEPIAAGLGTDGRQYwsEEWSHAAHhvMGPPLRPDPLTPGfLMDL 314
Cdd:PRK08044 229 YLAKVAGCRLHVCHISSPEGVEEVTRARQEGQDVTCESCPHYFVLDTDQF--EEIGTLAK--CSPPIRDLENQKG-MWEK 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21362535 315 LANGDLTTTGSDNctfNTCQKALGKDDFTKIPNGVNGVEDRMSVIWEKGVHSGKMDENRFVAVTSTNAAKIFNLyPKKGR 394
Cdd:PRK08044 304 LFNGEIDCLVSDH---SPCPPEMKAGNIMEAWGGIAGLQNCMDVMFDEAVQKRGMSLPMFGKLMATNAADIFGL-QQKGR 379
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 21362535 395 IAVGSDADIVIWDPEATRRISAKTHHQAVNFNIFEGMVCHGVPLVTISRGRVVY--EAGVFNvtAGHGKFIP 464
Cdd:PRK08044 380 IAPGKDADFVFIQPNSSYVLKNEDLEYRHKVSPYVGRTIGARITKTILRGDVIYdiEQGFPV--APKGQFIL 449
|
|
| pyrC |
PRK09357 |
dihydroorotase; Validated |
5-450 |
3.19e-36 |
|
dihydroorotase; Validated
Pssm-ID: 236479 [Multi-domain] Cd Length: 423 Bit Score: 139.17 E-value: 3.19e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21362535 5 GRLLIRGGRIVN-DDFSQVADVLVEDGVVRALGRDLLPPEDasrglRILDAAGKLVLPGGIDTHTHMQFPfmGSQSVDDF 83
Cdd:PRK09357 1 MMILIKNGRVIDpKGLDEVADVLIDDGKIAAIGENIEAEGA-----EVIDATGLVVAPGLVDLHVHLREP--GQEDKETI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21362535 84 YQGTKAALAGG---------TTMIIDfaipqkgsSLIEAFETWRNWADPKVCcdyslHV----AVTwwsdkVKEEMKTLA 150
Cdd:PRK09357 74 ETGSRAAAAGGfttvvampnTKPVID--------TPEVVEYVLDRAKEAGLV-----DVlpvgAIT-----KGLAGEELT 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21362535 151 rdkgvnSFKMFMAYK-------GLYmVQDEQL-YAAFSQCKEIG-AIAQvHAENGDLIAEGA----KKMLALGITGpegh 217
Cdd:PRK09357 136 ------EFGALKEAGvvafsddGIP-VQDARLmRRALEYAKALDlLIAQ-HCEDPSLTEGGVmnegEVSARLGLPG---- 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21362535 218 elcRPEAVEAEATLRAITIASAVNCPLYVVHVMSKSAAKVVADARRAGNVVYGE--PiaaglgtdgrqywseewshaaHH 295
Cdd:PRK09357 204 ---IPAVAEEVMIARDVLLAEATGARVHICHVSTAGSVELIRWAKALGIKVTAEvtP---------------------HH 259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21362535 296 V---------------MGPPLRpDPLTPGFLMDLLANGDLTTTGSD---------NCtfntcqkalgkdDFTKIPNGVNG 351
Cdd:PRK09357 260 LlltdedlltydpnykVNPPLR-TEEDREALIEGLKDGTIDAIATDhaphareekEC------------EFEAAPFGITG 326
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21362535 352 VEDRMSVIWEKGVHSGKMDENRFVAVTSTNAAKIFNLypKKGRIAVGSDADIVIWDPEATRRISAKTHHQAVNFNIFEGM 431
Cdd:PRK09357 327 LETALSLLYTTLVKTGLLDLEQLLEKMTINPARILGL--PAGPLAEGEPADLVIFDPEAEWTVDGEDFASKGKNTPFIGM 404
|
490
....*....|....*....
gi 21362535 432 VCHGVPLVTISRGRVVYEA 450
Cdd:PRK09357 405 KLKGKVVYTIVDGKIVYQD 423
|
|
| PRK09060 |
PRK09060 |
dihydroorotase; Validated |
7-447 |
1.32e-34 |
|
dihydroorotase; Validated
Pssm-ID: 181632 [Multi-domain] Cd Length: 444 Bit Score: 135.05 E-value: 1.32e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21362535 7 LLIRGGRIVNDDFSQVADVLVEDGVVRALGRdllpPEDASRGlRILDAAGKLVLPGGIDTHTHMQFPfmGSQSVDDFYQG 86
Cdd:PRK09060 7 LILKGGTVVNPDGEGRADIGIRDGRIAAIGD----LSGASAG-EVIDCRGLHVLPGVIDSQVHFREP--GLEHKEDLETG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21362535 87 TKAALAGGTTMIidFAIPQKGSSLI--EAFETWRNWADPKVCCDYSLHVAVTwwSDKVkEEMKTLARDKGVNSFKMFM-A 163
Cdd:PRK09060 80 SRAAVLGGVTAV--FEMPNTNPLTTtaEALADKLARARHRMHCDFAFYVGGT--RDNA-DELAELERLPGCAGIKVFMgS 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21362535 164 YKGLYMVQ-DEQLYAAFsqcKEIGAIAQVHAENGDLIAEgaKKMLAlgITG-PEGHELCRPEAVEAEATLRAITIASAVN 241
Cdd:PRK09060 155 STGDLLVEdDEGLRRIL---RNGRRRAAFHSEDEYRLRE--RKGLR--VEGdPSSHPVWRDEEAALLATRRLVRLARETG 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21362535 242 CPLYVVHVMSKSAAKVVADARRAGNV--------VYGEPIAAGLGTdgrqywseewshaaHHVMGPPLRpDPLTPGFLMD 313
Cdd:PRK09060 228 RRIHVLHVSTAEEIDFLADHKDVATVevtphhltLAAPECYERLGT--------------LAQMNPPIR-DARHRDGLWR 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21362535 314 LLANGDLTTTGSDNCTFNTCQKALgkdDFTKIPNGVNGVEDRMSVIWEKgVHSGKMDENRFVAVTSTNAAKIFNLyPKKG 393
Cdd:PRK09060 293 GVRQGVVDVLGSDHAPHTLEEKAK---PYPASPSGMTGVQTLVPIMLDH-VNAGRLSLERFVDLTSAGPARIFGI-AGKG 367
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 21362535 394 RIAVGSDADIVIWDPEATRRISAKTHHQAVNFNIFEGMVCHGVPLVTISRGRVV 447
Cdd:PRK09060 368 RIAVGYDADFTIVDLKRRETITNEWIASRCGWTPYDGKEVTGWPVGTIVRGQRV 421
|
|
| DHOase_IIa |
cd01317 |
Dihydroorotase (DHOase), subgroup IIa; DHOases catalyze the reversible interconversion of ... |
48-440 |
5.03e-31 |
|
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: 123.89 E-value: 5.03e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21362535 48 GLRILDAAGKLVLPGGIDTHTHMQFPfmGSQSVDDFYQGTKAALAGGTTMII-----DFAIPQKgssliEAFETWRNWAD 122
Cdd:cd01317 1 DAEVIDAEGKILAPGLVDLHVHLREP--GFEYKETLESGAKAAAAGGFTTVVcmpntNPVIDNP-----AVVELLKNRAK 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21362535 123 PkvccdySLHVAVTWWS-----DKVKE--EMKTLArDKGVNSFkmfmAYKGLYMVQDEQLYAAFSQCKEIGAIAQVHAEN 195
Cdd:cd01317 74 D------VGIVRVLPIGaltkgLKGEEltEIGELL-EAGAVGF----SDDGKPIQDAELLRRALEYAAMLDLPIIVHPED 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21362535 196 GDLIAEGA----KKMLALGITGpeghelcRPEAVEAEATLRAITIASAVNCPLYVVHVMSKSAAKVVADARRAGnvvygE 271
Cdd:cd01317 143 PSLAGGGVmnegKVASRLGLPG-------IPPEAETIMVARDLELAEATGARVHFQHLSTARSLELIRKAKAKG-----L 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21362535 272 PIAAG------LGTDgrqywSEEWSHAAHHVMGPPLR--PDPLtpgFLMDLLANGDLTTTGSDNCTFNTCQKALGKDDft 343
Cdd:cd01317 211 PVTAEvtphhlLLDD-----EALESYDTNAKVNPPLRseEDRE---ALIEALKDGTIDAIASDHAPHTDEEKDLPFAE-- 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21362535 344 kIPNGVNGVEDRMSVIWEKGVHSGKMDENRFVAVTSTNAAKIFNLYPkkGRIAVGSDADIVIWDPEATRRISAKTHHQAV 423
Cdd:cd01317 281 -APPGIIGLETALPLLWTLLVKGGLLTLPDLIRALSTNPAKILGLPP--GRLEVGAPADLVLFDPDAEWIVDEETFRSKS 357
|
410
....*....|....*..
gi 21362535 424 NFNIFEGMVCHGVPLVT 440
Cdd:cd01317 358 KNTPFDGQKLKGRVLAT 374
|
|
| PRK07575 |
PRK07575 |
dihydroorotase; Provisional |
3-461 |
4.87e-30 |
|
dihydroorotase; Provisional
Pssm-ID: 236055 [Multi-domain] Cd Length: 438 Bit Score: 122.09 E-value: 4.87e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21362535 3 PQGRLLIRGGRIVNDDFS-QVADVLVEDGVVRALGRDLLPPEDAsrglRILDAAGKLVLPGGIDTHTHMQFPfmGSQSVD 81
Cdd:PRK07575 1 MMMSLLIRNARILLPSGElLLGDVLVEDGKIVAIAPEISATAVD----TVIDAEGLTLLPGVIDPQVHFREP--GLEHKE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21362535 82 DFYQGTKAALAGGTTMIIDFAIPQKGSSLIEAFETWRNWADPKVCCDYSLHVAVTwwSDKVkEEMKTLARDKGVnsfKMF 161
Cdd:PRK07575 75 DLFTASRACAKGGVTSFLEMPNTKPLTTTQAALDDKLARAAEKCVVNYGFFIGAT--PDNL-PELLTANPTCGI---KIF 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21362535 162 M-AYKGLYMVQDE-QLYAAFSQCKEIgaIAqVHAENGDLIAEgAKKMLAlGITGPEGHELCRPEAVEAEATLRAITIASA 239
Cdd:PRK07575 149 MgSSHGPLLVDEEaALERIFAEGTRL--IA-VHAEDQARIRA-RRAEFA-GISDPADHSQIQDEEAALLATRLALKLSKK 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21362535 240 VNCPLYVVHVMSKSAAKVVADARRAGNVVYGEPIAAGLGTDGrqYwsEEWSHAAHhvMGPPLRpDPLTPGFLMDLLANGD 319
Cdd:PRK07575 224 YQRRLHILHLSTAIEAELLRQDKPSWVTAEVTPQHLLLNTDA--Y--ERIGTLAQ--MNPPLR-SPEDNEALWQALRDGV 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21362535 320 LTTTGSDNCTFNTCQKALGkddFTKIPNGVNGVEDRMSVIWEKgVHSGKMDENRFVAVTSTNAAKIFNLyPKKGRIAVGS 399
Cdd:PRK07575 297 IDFIATDHAPHTLEEKAQP---YPNSPSGMPGVETSLPLMLTA-AMRGKCTVAQVVRWMSTAVARAYGI-PNKGRIAPGY 371
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 21362535 400 DADIVIWDPEATRRISAKTHHQAVNFNIFEGMVCHGVPLVTISRGRVVYEAGVFNvTAGHGK 461
Cdd:PRK07575 372 DADLVLVDLNTYRPVRREELLTKCGWSPFEGWNLTGWPVTTIVGGQIVFDRGQVN-TEVRGQ 432
|
|
| PLN02795 |
PLN02795 |
allantoinase |
12-451 |
1.03e-29 |
|
allantoinase
Pssm-ID: 178392 [Multi-domain] Cd Length: 505 Bit Score: 122.19 E-value: 1.03e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21362535 12 GRIVNDDFSQVADVLVEDGVVRALGRDLLPPEDASRGlRILDAAGKLVLPGGIDTHTHMQFPfmGSQSVDDFYQGTKAAL 91
Cdd:PLN02795 51 KRVVTPAGVIPGAVEVEGGRIVSVTKEEEAPKSQKKP-HVLDYGNAVVMPGLIDVHVHLNEP--GRTEWEGFPTGTKAAA 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21362535 92 AGGTTMIIDF---AIPQKGSSliEAFETWRNWADPKvccdysLHVAVTWWSDKVKE------EMKTLArDKGVNSFKMFM 162
Cdd:PLN02795 128 AGGITTLVDMplnSFPSTTSV--ETLELKIEAAKGK------LYVDVGFWGGLVPEnahnasVLEELL-DAGALGLKSFM 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21362535 163 AYKGL---YMVQDEQLYAAFSQCKEIGAIAQVHAENGDLIAEGAkkMLALGITGPEGHELCRPEAVEAEATLRAITIAS- 238
Cdd:PLN02795 199 CPSGIndfPMTTATHIKAALPVLAKYGRPLLVHAEVVSPVESDS--RLDADPRSYSTYLKSRPPSWEQEAIRQLLEVAKd 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21362535 239 ------AVNCPLYVVHVM-SKSAAKVVADARRAGNVVYGEPIAAGLGTDgrqywSEEWSHAA-HHVMGPPLRpDPLTPGF 310
Cdd:PLN02795 277 trpggvAEGAHVHIVHLSdAESSLELIKEAKAKGDSVTVETCPHYLAFS-----AEEIPDGDtRYKCAPPIR-DAANREL 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21362535 311 LMDLLANGDLTTTGSDNCTFNTCQKALGKDDFTKIPNGVNGVEDRMSVIWEKGVHSGkMDENRFVAVTSTNAAKIFNLyP 390
Cdd:PLN02795 351 LWKALLDGDIDMLSSDHSPSPPDLKLLEEGNFLRAWGGISSLQFVLPATWTAGRAYG-LTLEQLARWWSERPAKLAGL-D 428
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 21362535 391 KKGRIAVGSDADIVIWDPEATRRI--SAKTHHQAVNFNIFEGMVCHGVPLVTISRGRVVYEAG 451
Cdd:PLN02795 429 SKGAIAPGKDADIVVWDPEAEFVLdeSYPIYHKHKSLSPYLGTKLSGKVIATFVRGNLVFLEG 491
|
|
| Amidohydro_1 |
pfam01979 |
Amidohydrolase family; This family of enzymes are a a large metal dependent hydrolase ... |
58-447 |
2.06e-24 |
|
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: 104.12 E-value: 2.06e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21362535 58 LVLPGGIDTHTHMQFPFM------GSQSVDDFYQGTKAALAGGTTMIIDFAI--PQKGSSLIEAFEtwRNWADPKVC--- 126
Cdd:pfam01979 1 IVLPGLIDAHVHLEMGLLrgipvpPEFAYEALRLGITTMLKSGTTTVLDMGAttSTGIEALLEAAE--ELPLGLRFLgpg 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21362535 127 ----CDYSLHVAVTWWsDKVKEEMKTLARDKGVNSFKMFMAYkGLYMVQDEQLYAAFSQCKEIGAIAQVHAENGDLIAEG 202
Cdd:pfam01979 79 csldTDGELEGRKALR-EKLKAGAEFIKGMADGVVFVGLAPH-GAPTFSDDELKAALEEAKKYGLPVAIHALETKGEVED 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21362535 203 AKKmlALGITGPEGHELcrpEAVEAEATLRAITIASAVNcplyvVHVMSKSAAKVVADARRAGNVVYgePIAAGLGTDGR 282
Cdd:pfam01979 157 AIA--AFGGGIEHGTHL---EVAESGGLLDIIKLILAHG-----VHLSPTEANLLAEHLKGAGVAHC--PFSNSKLRSGR 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21362535 283 qywseewshaahhvmgPPLRpdpltpgflmDLLANGDLTTTGSDNCtfntcqkaLGKDDFTKIPNGVNGVEDRmsviwek 362
Cdd:pfam01979 225 ----------------IALR----------KALEDGVKVGLGTDGA--------GSGNSLNMLEELRLALELQ------- 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21362535 363 GVHSGKMDENRFVAVTSTNAAKIFNLYPKKGRIAVGSDADIVIWDPEATrrisakthhqavnfNIFEGMVCHGVPLVTIS 442
Cdd:pfam01979 264 FDPEGGLSPLEALRMATINPAKALGLDDKVGSIEVGKDADLVVVDLDPL--------------AAFFGLKPDGNVKKVIV 329
|
....*
gi 21362535 443 RGRVV 447
Cdd:pfam01979 330 KGKIV 334
|
|
| PRK04250 |
PRK04250 |
dihydroorotase; Provisional |
5-451 |
6.68e-24 |
|
dihydroorotase; Provisional
Pssm-ID: 235265 [Multi-domain] Cd Length: 398 Bit Score: 103.69 E-value: 6.68e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21362535 5 GRLLIRGgRIVNddfsqvADVLVEDGVVRALGRDLLppedasRGLRILDAAGKLVLPGGIDTHTHMQ-FPFMGSQSVDdf 83
Cdd:PRK04250 4 GKFLLKG-RIVE------GGIGIENGRISKISLRDL------KGKEVIKVKGGIILPGLIDVHVHLRdFEESYKETIE-- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21362535 84 yQGTKAALAGGTTMIIDfaIPQKGSSLI--EAFETWRNWADPKVCCDYSLHVAVTWWSDKVKEEMKTLardkgvnsFKMF 161
Cdd:PRK04250 69 -SGTKAALHGGITLVFD--MPNTKPPIMdeKTYEKRMRIAEKKSYADYALNFLIAGNCEKAEEIKADF--------YKIF 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21362535 162 M--AYKGLYMVQDEQLYaafsqcKEIGAIAQVHAENGDLIAEgakkmlalgitGPEghelcRPEAVEAEATLRAITIASA 239
Cdd:PRK04250 138 MgaSTGGIFSENFEVDY------ACAPGIVSVHAEDPELIRE-----------FPE-----RPPEAEVVAIERALEAGKK 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21362535 240 VNCPLYVVHVMSKSAAKVVADARRAGNVVYGEPiaaglgtdgrqywseewshaaHHVM--------------GPPLRpDP 305
Cdd:PRK04250 196 LKKPLHICHISTKDGLKLILKSNLPWVSFEVTP---------------------HHLFltrkdyernpllkvYPPLR-SE 253
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21362535 306 LTPGFLMDLLANGDLttTGSDNCTFNTCQKALGKddftkipNGVNGVEDRMSVIWEkGVHSGKMDENRFVAVTSTNAAKI 385
Cdd:PRK04250 254 EDRKALWENFSKIPI--IASDHAPHTLEDKEAGA-------AGIPGLETEVPLLLD-AANKGMISLFDIVEKMHDNPARI 323
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 21362535 386 FNLypkKGR-IAVGSDADIVIWDPEATRRISAKTHHQAVNFNIFEGMVCHGVPLVTISRGRVVYEAG 451
Cdd:PRK04250 324 FGI---KNYgIEEGNYANFAVFDMKKEWTIKAEELYTKAGWTPYEGFKLKGKVIMTILRGEVVMEDD 387
|
|
| PRK01211 |
PRK01211 |
dihydroorotase; Provisional |
16-465 |
1.69e-19 |
|
dihydroorotase; Provisional
Pssm-ID: 179247 [Multi-domain] Cd Length: 409 Bit Score: 90.69 E-value: 1.69e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21362535 16 NDDFSQVAdVLVEDGVVRALGRDLlppedASRGLRILDAAgklVLPGGIDTHTHMQFPfmGSQSVDDFYQGTKAALAGGT 95
Cdd:PRK01211 10 KGKFDYLE-IEVEDGKIKSIKKDA-----GNIGKKELKGA---ILPAATDIHVHFRTP--GETEKEDFSTGTLSAIFGGT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21362535 96 TMIIDFA---IPQKGsslIEAFETWRNWADPKVCCDYSLHVAVTWWSDKVKEEMKTlardkgvnSFKMFMA---YKGLYM 169
Cdd:PRK01211 79 TFIMDMPnnnIPIKD---YNAFSDKLGRVAPKAYVDFSLYSMETGNNALILDERSI--------GLKVYMGgttNTNGTD 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21362535 170 VQDEQLyaafSQCKEIGAIAQVHAENGDLIAEGAKKMLALgitgpEGHELCRPEAVEAEAtlraitIASAVNCPLYVVHV 249
Cdd:PRK01211 148 IEGGEI----KKINEANIPVFFHAELSECLRKHQFESKNL-----RDHDLARPIECEIKA------VKYVKNLDLKTKII 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21362535 250 MSKSAAKVVADARRAGN----VVYGEpiaAGLGTDGRqywseewshaahhvMGPPLRpDPLTPGFLMDLLANGDLTTTGS 325
Cdd:PRK01211 213 AHVSSIDVIGRFLREVTphhlLLNDD---MPLGSYGK--------------VNPPLR-DRWTQERLLEEYISGRFDILSS 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21362535 326 DNCTFNTCQKAlgkdDFTKIPNGVNGVEDRMSVIWEKgVHSGKMDENRFVAVTSTNAAKIFNLypKKGRIAVGSDADIVI 405
Cdd:PRK01211 275 DHAPHTEEDKQ----EFEYAKSGIIGVETRVPLFLAL-VKKKILPLDVLYKTAIERPASLFGI--KKGKIEEGYDADFMA 347
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 21362535 406 WDPEATRRISAKTHHQAVNFNIFEGMVCHgVPLVTISRGRVV---YEagvfNVTAGHGKFIPR 465
Cdd:PRK01211 348 FDFTNIKKINDKRLHSKCPVSPFNGFDAI-FPSHVIMRGEVVidnYE----LISERTGKFVPK 405
|
|
| HutI |
COG1228 |
Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport ... |
2-432 |
4.17e-15 |
|
Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440841 [Multi-domain] Cd Length: 386 Bit Score: 76.92 E-value: 4.17e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21362535 2 APQGRLLIRGGRIVNDDFSQV---ADVLVEDGVVRALGR--DLLPPEDAsrglRILDAAGKLVLPGGIDTHTHMQFPFMG 76
Cdd:COG1228 5 AQAGTLLITNATLVDGTGGGVienGTVLVEDGKIAAVGPaaDLAVPAGA----EVIDATGKTVLPGLIDAHTHLGLGGGR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21362535 77 SQS----------VDDFYQGTK---AALAGGTTMIIDfaipQKGSSL-----IEAFETWRNWADPKVCCDYSLHV---AV 135
Cdd:COG1228 81 AVEfeagggitptVDLVNPADKrlrRALAAGVTTVRD----LPGGPLglrdaIIAGESKLLPGPRVLAAGPALSLtggAH 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21362535 136 TWWSDKVKEEMKTLARDkGVNSFKMFMAYKGLYMvQDEQLYAAFSQCKEIGAIAQVHAENgdliAEGAKKMLALGITGPE 215
Cdd:COG1228 157 ARGPEEARAALRELLAE-GADYIKVFAEGGAPDF-SLEELRAILEAAHALGLPVAAHAHQ----ADDIRLAVEAGVDSIE 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21362535 216 GHELCRPEAVE--AEA---------TLRAITIASAVNCPLYVVHVMSKSAAKVVADARRAGnvvygepIAAGLGTDGRQY 284
Cdd:COG1228 231 HGTYLDDEVADllAEAgtvvlvptlSLFLALLEGAAAPVAAKARKVREAALANARRLHDAG-------VPVALGTDAGVG 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21362535 285 WSEEWShaAHHVMGpplrpdpltpgflmdLLANGDLTTtgsdnctfntcQKALgkddftkipngvngvedrmsviwekgv 364
Cdd:COG1228 304 VPPGRS--LHRELA---------------LAVEAGLTP-----------EEAL--------------------------- 328
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 21362535 365 hsgkmdenrfVAVTStNAAKIFNLYPKKGRIAVGSDADIVIWDPEATRRISAkthHQAVNFNIFEGMV 432
Cdd:COG1228 329 ----------RAATI-NAAKALGLDDDVGSLEPGKLADLVLLDGDPLEDIAY---LEDVRAVMKDGRV 382
|
|
| PRK09236 |
PRK09236 |
dihydroorotase; Reviewed |
6-454 |
5.29e-15 |
|
dihydroorotase; Reviewed
Pssm-ID: 181716 Cd Length: 444 Bit Score: 77.22 E-value: 5.29e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21362535 6 RLLIRGGRIVNDDFSQVADVLVEDGVVRALGRDLlppeDASRGLRILDAAGKLVLPGGIDTHTHMQFPfmGSQSVDDFYQ 85
Cdd:PRK09236 3 RILIKNARIVNEGKIFEGDVLIENGRIAKIASSI----SAKSADTVIDAAGRYLLPGMIDDQVHFREP--GLTHKGDIAS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21362535 86 GTKAALAGGTTMIIDF--AIPQkgSSLIEAFETWRNWADPKVCCDYSLHVAVTwwSDKVkEEMKTL--ARDKGVnsfKMF 161
Cdd:PRK09236 77 ESRAAVAGGITSFMEMpnTNPP--TTTLEALEAKYQIAAQRSLANYSFYFGAT--NDNL-DEIKRLdpKRVCGV---KVF 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21362535 162 M-AYKGLYMVQDEQ-LYAAFSQCKEIgaIAqVHAENGDLIAEGAKKMLAL---GITgPEGHELCRPEAVEAEATLRAITI 236
Cdd:PRK09236 149 MgASTGNMLVDNPEtLERIFRDAPTL--IA-THCEDTPTIKANLAKYKEKygdDIP-AEMHPLIRSAEACYKSSSLAVSL 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21362535 237 ASAVNCPLYVVHVmskSAAKVVADARRAgnvvygePIAaglgtdGRQYWSEEwshAAHHvmgppL---RPDPLTPGF--- 310
Cdd:PRK09236 225 AKKHGTRLHVLHI---STAKELSLFENG-------PLA------EKRITAEV---CVHH-----LwfdDSDYARLGNlik 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21362535 311 -------------LMDLLANGDLTTTGSDNCTFNTCQKALGkddFTKIPNGVNGVEDRMSVIWEKgVHSGKMDENRFVAV 377
Cdd:PRK09236 281 cnpaiktasdreaLRQALADDRIDVIATDHAPHTWEEKQGP---YFQAPSGLPLVQHALPALLEL-VHEGKLSLEKVVEK 356
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 21362535 378 TSTNAAKIFNLyPKKGRIAVGSDADIVIWDPEATRRISAKTHHQAVNFNIFEGMVCHGVPLVTISRGRVVYEAGVFN 454
Cdd:PRK09236 357 TSHAPAILFDI-KERGFIREGYWADLVLVDLNSPWTVTKENILYKCGWSPFEGRTFRSRVATTFVNGQLVYHNGQLV 432
|
|
| SsnA |
COG0402 |
Cytosine/adenosine deaminase or related metal-dependent hydrolase [Nucleotide transport and ... |
6-449 |
4.49e-14 |
|
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: 74.09 E-value: 4.49e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21362535 6 RLLIRGGRIVNDDFSQV----ADVLVEDGVVRALGRDLlPPEDASRGLRILDAAGKLVLPGGIDTHTHM----------- 70
Cdd:COG0402 1 DLLIRGAWVLTMDPAGGvledGAVLVEDGRIAAVGPGA-ELPARYPAAEVIDAGGKLVLPGLVNTHTHLpqtllrgladd 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21362535 71 ----------QFPFMGSQSVDDFYQGTKAA----LAGGTTMIIDFAIPQKGSS--LIEAFETW--RNWAdPKVCCDYSLH 132
Cdd:COG0402 80 lplldwleeyIWPLEARLDPEDVYAGALLAlaemLRSGTTTVADFYYVHPESAdaLAEAAAEAgiRAVL-GRGLMDRGFP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21362535 133 VAVTWWSDKVKEEMKTLAR---DKGVNSFKMFMAYKGLYMVQDEQLYAAFSQCKEIGAIAQVH-AENGDLIAEGAKK--- 205
Cdd:COG0402 159 DGLREDADEGLADSERLIErwhGAADGRIRVALAPHAPYTVSPELLRAAAALARELGLPLHTHlAETRDEVEWVLELygk 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21362535 206 -----MLALGITGPE---GHelcrpeAV---EAE-ATLRAiTIASAVNCPLyvvhvmskSAAKV------VADARRAGNV 267
Cdd:COG0402 239 rpveyLDELGLLGPRtllAH------CVhltDEEiALLAE-TGASVAHCPT--------SNLKLgsgiapVPRLLAAGVR 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21362535 268 VygepiaaGLGTDGrqYWS-------EEWSHAAHHVMGPPLRPDPLTPGflmDLLangDLTTTGSdnctfntcQKALGKD 340
Cdd:COG0402 304 V-------GLGTDG--AASnnsldmfEEMRLAALLQRLRGGDPTALSAR---EAL---EMATLGG--------ARALGLD 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21362535 341 DFTkipngvngvedrmsviwekgvhsgkmdenrfvavtstnaakifnlypkkGRIAVGSDADIVIWDPEATRRISAKTHH 420
Cdd:COG0402 361 DEI-------------------------------------------------GSLEPGKRADLVVLDLDAPHLAPLHDPL 391
|
490 500
....*....|....*....|....*....
gi 21362535 421 QAVNFNIFEGMVCHgvplvTISRGRVVYE 449
Cdd:COG0402 392 SALVYAADGRDVRT-----VWVAGRVVVR 415
|
|
| D-aminoacylase |
cd01297 |
D-aminoacylases (N-acyl-D-Amino acid amidohydrolases) catalyze the hydrolysis of ... |
7-458 |
4.92e-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: 70.79 E-value: 4.92e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21362535 7 LLIRGGRIV----NDDFSqvADVLVEDGVVRALGRDLLPPedasrGLRILDAAGKLVLPGGIDTHTHMQFPFMGSQSVdd 82
Cdd:cd01297 2 LVIRNGTVVdgtgAPPFT--ADVGIRDGRIAAIGPILSTS-----AREVIDAAGLVVAPGFIDVHTHYDGQVFWDPDL-- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21362535 83 fyqgTKAALAGGTTMII----------DFAIPQKGSSLIEAF--------ETWRNWAD-----------PKVCCDY---S 130
Cdd:cd01297 73 ----RPSSRQGVTTVVLgncgvspapaNPDDLARLIMLMEGLvalgeglpWGWATFAEyldalearppaVNVAALVghaA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21362535 131 LHVAVTWWSDKVK-----EEMKTLAR---DKGVNSFKMFMAY-KGLYMVQDEqLYAAFSQCKEIGAIAQVHAEN-GDLIA 200
Cdd:cd01297 149 LRRAVMGLDAREAteeelAKMRELLRealEAGALGISTGLAYaPRLYAGTAE-LVALARVAARYGGVYQTHVRYeGDSIL 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21362535 201 EGAKKMLALGitgpeghelcrpeaveaEATLRAITIASAVNCPLYVVHVMSKSAAKVVAdARRAGNVVYGE--PIAAGLG 278
Cdd:cd01297 228 EALDELLRLG-----------------RETGRPVHISHLKSAGAPNWGKIDRLLALIEA-ARAEGLQVTADvyPYGAGSE 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21362535 279 TDGRqywseEWshAAHHVM------GPPLRPDPLTpgflmdllangdltttgsdNCTFNtcqKALGKddftkipngvnGV 352
Cdd:cd01297 290 DDVR-----RI--MAHPVVmggsdgGALGKPHPRS-------------------YGDFT---RVLGH-----------YV 329
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21362535 353 EDRMSVIWEKGVHsgKMdenrfvavtSTNAAKIFNLYpKKGRIAVGSDADIVIWDPEATRRISAKT--HHQAVnfnifeg 430
Cdd:cd01297 330 RERKLLSLEEAVR--KM---------TGLPARVFGLA-DRGRIAPGYRADIVVFDPDTLADRATFTrpNQPAE------- 390
|
490 500
....*....|....*....|....*....
gi 21362535 431 mvchGVPLVTISrGRVVYEAGVFN-VTAG 458
Cdd:cd01297 391 ----GIEAVLVN-GVPVVRDGAFTgARPG 414
|
|
| PRK09059 |
PRK09059 |
dihydroorotase; Validated |
7-450 |
2.46e-12 |
|
dihydroorotase; Validated
Pssm-ID: 181631 [Multi-domain] Cd Length: 429 Bit Score: 68.91 E-value: 2.46e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21362535 7 LLIRGGRIVND--DFSQVADVLVEDGVVRALGRDLLP---PEDASrglrILDAAGKLVLPGGIDTHTHMQFPfmGSQSVD 81
Cdd:PRK09059 5 ILLANARIIDPsrGLDEIGTVLIEDGVIVAAGKGAGNqgaPEGAE----IVDCAGKAVAPGLVDARVFVGEP--GAEHRE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21362535 82 DFYQGTKAALAGGTTMII-----DFAIPQkgSSLIE-AFETWRNWADPKVccdyslHVAVTWWSDKVKEEMKT--LARDK 153
Cdd:PRK09059 79 TIASASRAAAAGGVTSIImmpdtDPVIDD--VALVEfVKRTARDTAIVNI------HPAAAITKGLAGEEMTEfgLLRAA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21362535 154 GVNSFkmfmaYKGLYMVQDEQ-LYAAFSQCKEIGAIAQVHAENGDLIAEGA--KKMLA--LGITG-PeghelCRPEAVEA 227
Cdd:PRK09059 151 GAVAF-----TDGRRSVANTQvMRRALTYARDFDAVIVHETRDPDLGGNGVmnEGLFAswLGLSGiP-----REAEVIPL 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21362535 228 EATLR--AITI----ASAVNCPLyvvhvmsksAAKVVADARRAgnvvyGEPIAAGLgtdgrqywseewshAAHHV----- 296
Cdd:PRK09059 221 ERDLRlaALTRgryhAAQISCAE---------SAEALRRAKDR-----GLKVTAGV--------------SINHLslnen 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21362535 297 ----------MGPPLRP--DPLTpgfLMDLLANGDLTTTGSDNCTFNTCQKALgkdDFTKIPNGVNGVEDRMSVIWeKGV 364
Cdd:PRK09059 273 digeyrtffkLSPPLRTedDRVA---MVEAVASGTIDIIVSSHDPQDVDTKRL---PFSEAAAGAIGLETLLAAAL-RLY 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21362535 365 HSGKMDENRFVAVTSTNAAKIFNLypKKGRIAVGSDADIVIWDPEATRRISAKTHHQAVNFNIFEGMVCHGVPLVTISRG 444
Cdd:PRK09059 346 HNGEVPLLRLIEALSTRPAEIFGL--PAGTLKPGAPADIIVIDLDEPWVVDPEDLKSRSKNTPFEEARFQGRVVRTIVAG 423
|
....*.
gi 21362535 445 RVVYEA 450
Cdd:PRK09059 424 KTVYEL 429
|
|
| PRK09237 |
PRK09237 |
amidohydrolase/deacetylase family metallohydrolase; |
7-69 |
5.74e-11 |
|
amidohydrolase/deacetylase family metallohydrolase;
Pssm-ID: 236423 [Multi-domain] Cd Length: 380 Bit Score: 64.10 E-value: 5.74e-11
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 21362535 7 LLIRGGRIVN--DDFSQVADVLVEDGVVRALGRDLlppeDASRGLRILDAAGKLVLPGGIDTHTH 69
Cdd:PRK09237 1 LLLRGGRVIDpaNGIDGVIDIAIEDGKIAAVAGDI----DGSQAKKVIDLSGLYVSPGWIDLHVH 61
|
|
| ATZ_TRZ_like |
cd01298 |
TRZ/ATZ family contains enzymes from the atrazine degradation pathway and related hydrolases. ... |
7-100 |
7.30e-11 |
|
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: 64.15 E-value: 7.30e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21362535 7 LLIRGGRIVNDDFSQV---ADVLVEDGVVRALGRDLLPPEDAsrGLRILDAAGKLVLPGGIDTHTHMQ------------ 71
Cdd:cd01298 1 ILIRNGTIVTTDPRRVledGDVLVEDGRIVAVGPALPLPAYP--ADEVIDAKGKVVMPGLVNTHTHLAmtllrgladdlp 78
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 21362535 72 ---------FPFMGSQSVDDFYQGTKAALA----GGTTMIID 100
Cdd:cd01298 79 lmewlkdliWPLERLLTEEDVYLGALLALAemirSGTTTFAD 120
|
|
| Met_dep_hydrolase_B |
cd01307 |
Metallo-dependent hydrolases, subgroup B is part of the superfamily of metallo-dependent ... |
24-407 |
1.03e-09 |
|
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: 60.03 E-value: 1.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21362535 24 DVLVEDGVVRALGRDLLPPEDAsrglRILDAAGKLVLPGGIDTHTHMqFPFMGSQSVD-DFYqgtkaALAGGTTMIIDfa 102
Cdd:cd01307 1 DVAIENGKIAAVGAALAAPAAT----QIVDAGGCYVSPGWIDLHVHV-YQGGTRYGDRpDMI-----GVKSGVTTVVD-- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21362535 103 ipqKGSSLIEAFETWRnwadpkvccdyslhvavtwwsdkvkeemKTLARDKGVNSFkmfmAYKGLYMV-QDEQLYAAFSQ 181
Cdd:cd01307 69 ---AGSAGADNIDGFR----------------------------YTVIERSATRVY----AFLNISRVgLVAQDELPDPD 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21362535 182 CKEIGAIAQVHAENGDLIAeGAKKMLALGITGPEGHELCRpeaveaeatlRAITIASAVNCPLYvVHVMSKSA--AKVVA 259
Cdd:cd01307 114 NIDEDAVVAAAREYPDVIV-GLKARASKSVVGEWGIKPLE----------LAKKIAKEADLPLM-VHIGSPPPilDEVVP 181
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21362535 260 DARRaGNVVygepiaaglgtdgrqywseewSHAAHHVMGPPLRPDPLTPGFLMDLLANG---DLtTTGSDNCTFNTCQKA 336
Cdd:cd01307 182 LLRR-GDVL---------------------THCFNGKPNGIVDEEGEVLPLVRRARERGvifDV-GHGTASFSFRVARAA 238
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21362535 337 ---------LGKDDFTKipNGVNGVEDRMSVIWEKGVHSGKMDENRFVAVTsTNAAKIFNLyPKKGRIAVGSDADIVIWD 407
Cdd:cd01307 239 iaagllpdtISSDIHGR--NRTNGPVYALATTLSKLLALGMPLEEVIEAVT-ANPARMLGL-AEIGTLAVGYDADLTVFD 314
|
|
| metallo-dependent_hydrolases |
cd01292 |
Superfamily of metallo-dependent hydrolases (also called amidohydrolase superfamily) is a ... |
64-281 |
5.71e-09 |
|
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: 57.34 E-value: 5.71e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21362535 64 IDTHTHMQFP----------------FMGSQSVDDFYQGTKAALAGGTTMIIDFAIPQKGSSLIEAFETWRNWADP---- 123
Cdd:cd01292 2 IDTHVHLDGSalrgtrlnlelkeaeeLSPEDLYEDTLRALEALLAGGVTTVVDMGSTPPPTTTKAAIEAVAEAARAsagi 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21362535 124 -KVCCDYSLHVAVTWWSDKVKEEMKTLAR--DKGVNSFKMFMAYKGlYMVQDEQLYAAFSQCKEIGAIAQVHAENGDLIA 200
Cdd:cd01292 82 rVVLGLGIPGVPAAVDEDAEALLLELLRRglELGAVGLKLAGPYTA-TGLSDESLRRVLEEARKLGLPVVIHAGELPDPT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21362535 201 EGAKKMLALGITGPE---GHELCRPEAVEAEATLRAITIASavnCPLYVVHVMSKS-AAKVVADARRAGNVVygepiaaG 276
Cdd:cd01292 161 RALEDLVALLRLGGRvviGHVSHLDPELLELLKEAGVSLEV---CPLSNYLLGRDGeGAEALRRLLELGIRV-------T 230
|
....*
gi 21362535 277 LGTDG 281
Cdd:cd01292 231 LGTDG 235
|
|
| CAD_DHOase |
cd01316 |
The eukaryotic CAD protein is a trifunctional enzyme of carbamoylphosphate ... |
60-460 |
9.56e-09 |
|
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: 57.08 E-value: 9.56e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21362535 60 LPGGIDTHTHMQFPfmGSQSVDDFYQGTKAALAGGTTMIIdfAIPQKGSSLI--EAFETWRNWADPKVCCDYSLHVAVTw 137
Cdd:cd01316 5 LPGLIDVHVHLREP--GATHKEDFASGTKAALAGGFTMVR--AMPNTNPSIVdvASLKLVQSLAQAKARCDYAFSIGAT- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21362535 138 wSDKVKeEMKTLARDKGVNSFKMFMAYKGLYMVQDEQLYAAFSQCKEIGAIAqVHAENGDLIAegakkmlalgitgpegh 217
Cdd:cd01316 80 -STNAA-TVGELASEAVGLKFYLNETFSTLILDKITAWASHFNAWPSTKPIV-THAKSQTLAA----------------- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21362535 218 elcrpeaveaeatlrAITIASAVNCPLYVVHVMSKSAAKVVADARRAGNVVYGE--PIAAGLGTDGRQYWSEEwshaahh 295
Cdd:cd01316 140 ---------------VLLLASLHNRSIHICHVSSKEEINLIRLAKARGLKVTCEvsPHHLFLSQDDLPRGQYE------- 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21362535 296 vmGPPLRPDPLTPGFLMDLLANGDLTTTGSdnctfntCQKALGKDDFTKIPNGVNGVEDRMSVIWeKGVHSGKMDENRFV 375
Cdd:cd01316 198 --VRPFLPTREDQEALWENLDYIDCFATDH-------APHTLAEKTGNKPPPGFPGVETSLPLLL-TAVHEGRLTIEDIV 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21362535 376 AVTSTNAAKIFNLYPKkgriavgSDADIVIwDPEATRRISAKTHHQAVNFNIFEGMVCHGVPLVTISRGRVVYEAGVFNV 455
Cdd:cd01316 268 DRLHTNPKRIFNLPPQ-------SDTYVEV-DLDEEWTIPKNPLQSKKGWTPFEGKKVKGKVQRVVLRGETAFIDGEIVA 339
|
....*
gi 21362535 456 TAGHG 460
Cdd:cd01316 340 PPGFG 344
|
|
| NagA |
cd00854 |
N-acetylglucosamine-6-phosphate deacetylase, NagA, catalyzes the hydrolysis of the N-acetyl ... |
7-69 |
1.98e-08 |
|
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: 56.43 E-value: 1.98e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 21362535 7 LLIRGGRIVNDDFSQVADVLVEDGVVRALGrdllPPEDASRGLRILDAAGKLVLPGGIDTHTH 69
Cdd:cd00854 1 LIIKNARILTPGGLEDGAVLVEDGKIVAIG----PEDELEEADEIIDLKGQYLVPGFIDIHIH 59
|
|
| PRK08204 |
PRK08204 |
hypothetical protein; Provisional |
6-69 |
2.55e-08 |
|
hypothetical protein; Provisional
Pssm-ID: 181288 [Multi-domain] Cd Length: 449 Bit Score: 56.16 E-value: 2.55e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 21362535 6 RLLIRGGRIVNDD----FSQVADVLVEDGVVRALGRDLLPPEDAsrglrILDAAGKLVLPGGIDTHTH 69
Cdd:PRK08204 3 RTLIRGGTVLTMDpaigDLPRGDILIEGDRIAAVAPSIEAPDAE-----VVDARGMIVMPGLVDTHRH 65
|
|
| Imidazolone-5PH |
cd01296 |
Imidazolonepropionase/imidazolone-5-propionate hydrolase (Imidazolone-5PH) catalyzes the third ... |
25-99 |
2.62e-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: 55.73 E-value: 2.62e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 21362535 25 VLVEDGVVRALGRDLLPPEDASRGLRILDAAGKLVLPGGIDTHTHMQFpfmGSQSVDDFYqgtkAALAGGTTMII 99
Cdd:cd01296 1 IAIRDGRIAAVGPAASLPAPGPAAAEEIDAGGRAVTPGLVDCHTHLVF---AGDRVDEFA----ARLAGASYEEI 68
|
|
| pyrC |
PRK00369 |
dihydroorotase; Provisional |
56-457 |
3.99e-08 |
|
dihydroorotase; Provisional
Pssm-ID: 234738 [Multi-domain] Cd Length: 392 Bit Score: 55.54 E-value: 3.99e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21362535 56 GKLVLPGGIDTHTHMQfpfmGSQSV--DDFYQGTKAALAGGTTMIIDFAIPQKGSSLIEAFETWRNWADPKVCCDYSLHV 133
Cdd:PRK00369 42 GTLILPGAIDLHVHLR----GLKLSykEDVASGTSEAAYGGVTLVADMPNTIPPLNTPEAITEKLAELEYYSRVDYFVYS 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21362535 134 AVTwwsdKVKEEMKTLardkGVNSFKMFMAykglymvqdeqlyaafsqckeigaiaqvhaengDLIAEGAKKMLA----L 209
Cdd:PRK00369 118 GVT----KDPEKVDKL----PIAGYKIFPE---------------------------------DLEREETFRVLLksrkL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21362535 210 GITGPEGHELCRPEaveaEATLRAI--TIASavncpLYV------VHVMSKSAAKVVADARRAGNVVYGEPIAAGLGTDG 281
Cdd:PRK00369 157 KILHPEVPLALKSN----RKLRRNCwyEIAA-----LYYvkdyqnVHITHASNPRTVRLAKELGFTVDITPHHLLVNGEK 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21362535 282 RQYWSeewshaahhvMGPPLRpDPLTPGFLMDLLANGDltTTGSDNCTFNTCQKalgKDDFTKIPNGVNGVEDRMSVIWE 361
Cdd:PRK00369 228 DCLTK----------VNPPIR-DINERLWLLQALSEVD--AIASDHAPHSSFEK---LQPYEVCPPGIAALSFTPPFIYT 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21362535 362 KgVHSGKMDENRFVAVTSTNAAKIFNLypKKGRIAVGSDADIVIWDPEATRriSAKTHHQAVNfNIFEGMVCHGVPLVTI 441
Cdd:PRK00369 292 L-VSKGILSIDRAVELISTNPARILGI--PYGEIKEGYRANFTVIQFEDWR--YSTKYSKVIE-TPLDGFELKASVYATI 365
|
410
....*....|....*..
gi 21362535 442 SRGRVVYEAG-VFNVTA 457
Cdd:PRK00369 366 VQGKLAYLEGeVFPVKG 382
|
|
| YtcJ |
COG1574 |
Predicted amidohydrolase YtcJ [General function prediction only]; |
7-70 |
7.07e-08 |
|
Predicted amidohydrolase YtcJ [General function prediction only];
Pssm-ID: 441182 [Multi-domain] Cd Length: 535 Bit Score: 54.80 E-value: 7.07e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 21362535 7 LLIRGGRI--VNDDFSQVADVLVEDGVVRALGRDLLPPEDASRGLRILDAAGKLVLPGGIDTHTHM 70
Cdd:COG1574 10 LLLTNGRIytMDPAQPVAEAVAVRDGRIVAVGSDAEVRALAGPATEVIDLGGKTVLPGFIDAHVHL 75
|
|
| PRK07369 |
PRK07369 |
dihydroorotase; Provisional |
21-420 |
9.66e-08 |
|
dihydroorotase; Provisional
Pssm-ID: 236002 [Multi-domain] Cd Length: 418 Bit Score: 54.22 E-value: 9.66e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21362535 21 QVADVLVEDGVVRALGRDLLP-PEDAsrglRILDAAGKLVLPGGIDTHTHMQFPfmGSQSVDDFYQGTKAALAGGTT--- 96
Cdd:PRK07369 20 RIADVLIEDGKIQAIEPHIDPiPPDT----QIIDASGLILGPGLVDLYSHSGEP--GFEERETLASLAAAAAAGGFTrva 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21362535 97 MIIDFAIPQKGSSLIEAFETWRNWADPkvccdyslhVAVTWW---SDKVKEEMKTLARD---KGVNSFKMFMAYKGLYMV 170
Cdd:PRK07369 94 ILPDTFPPLDNPATLARLQQQAQQIPP---------VQLHFWgalTLGGQGKQLTELAElaaAGVVGFTDGQPLENLALL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21362535 171 QDEQLYA-------AFSQCKeigaiAQVHAeNGdLIAEGAKKmLALGITGpeghelcRPEAVEAEATLRAITIASAVNCP 243
Cdd:PRK07369 165 RRLLEYLkplgkpvALWPCD-----RSLAG-NG-VMREGLLA-LRLGLPG-------DPASAETTALAALLELVAAIGTP 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21362535 244 lyvVHVMSKSAAKVV-----ADARragnvvyGEPIAAglgtdgrqywSEEWshaaHHVMG---------PPLRPDPltP- 308
Cdd:PRK07369 230 ---VHLMRISTARSVeliaqAKAR-------GLPITA----------STTW----MHLLLdtealasydPNLRLDP--Pl 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21362535 309 GFLMDLLA------NGDLTTTGSDNCTFNTCQKALGkddFTKIPNGVNGVEDRMSVIWEKGVHSGKMDENRFVAVTSTNA 382
Cdd:PRK07369 284 GNPSDRQAliegvrTGVIDAIAIDHAPYTYEEKTVA---FAEAPPGAIGLELALPLLWQNLVETGELSALQLWQALSTNP 360
|
410 420 430
....*....|....*....|....*....|....*...
gi 21362535 383 AKIFNLYPKkgRIAVGSDADIVIWDPEATRRISAKTHH 420
Cdd:PRK07369 361 ARCLGQEPP--SLAPGQPAELILFDPQKTWTVSAQTLH 396
|
|
| NagA |
COG1820 |
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism]; |
8-96 |
1.60e-07 |
|
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism];
Pssm-ID: 441425 [Multi-domain] Cd Length: 373 Bit Score: 53.56 E-value: 1.60e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21362535 8 LIRGGRIVNDD-FSQVADVLVEDGVVRALGrdllppEDASRGLRILDAAGKLVLPGGIDTHTH--MQFPFMgSQSVDDFY 84
Cdd:COG1820 1 AITNARIFTGDgVLEDGALLIEDGRIAAIG------PGAEPDAEVIDLGGGYLAPGFIDLHVHggGGVDFM-DGTPEALR 73
|
90
....*....|..
gi 21362535 85 QGTKAALAGGTT 96
Cdd:COG1820 74 TIARAHARHGTT 85
|
|
| Amidohydro_3 |
pfam07969 |
Amidohydrolase family; |
50-448 |
3.30e-07 |
|
Amidohydrolase family;
Pssm-ID: 400360 [Multi-domain] Cd Length: 464 Bit Score: 52.92 E-value: 3.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21362535 50 RILDAAGKLVLPGGIDTHTHM--QFPFMGSQSVDDFYQGTKAALAGGTTmiiDFAIPQKGSSLIEAFETWRNWADPKVCC 127
Cdd:pfam07969 1 EVIDAKGRLVLPGFVDPHTHLdgGGLNLRELRLPDVLPNAVVKGQAGRT---PKGRWLVGEGWDEAQFAETRFPYALADL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21362535 128 D------------YSLHVAV---------------------------TWW------SDKVKEEMKTLARDKGVNSFKMFM 162
Cdd:pfam07969 78 DevapdgpvllraLHTHAAVansaaldlagitkatedppggeiardaNGEgltgllREGAYALPPLLAREAEAAAVAAAL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21362535 163 AY---KGLYMVQDEQLYAAFSQckEIGAIAQVHAE-----------------NGDLIAEGAKKMLALGITG--------P 214
Cdd:pfam07969 158 AAlpgFGITSVDGGGGNVHSLD--DYEPLRELTAAeklkelldaperlglphSIYELRIGAMKLFADGVLGsrtaalteP 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21362535 215 EGHELCRPEAVEAEATL-RAITIASAVNCPLYVV------------HVMSKSAAKVVADARRA----GNVVYG----EPI 273
Cdd:pfam07969 236 YFDAPGTGWPDFEDEALaELVAAARERGLDVAIHaigdatidtaldAFEAVAEKLGNQGRVRIehaqGVVPYTysqiERV 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21362535 274 AAGLGTDGRQYWSeeWSHAAHHVMGP--PLRPDPLTPgfLMDLLANGDLTTTGSDN--CTFntcqkalgkDDFTKIPNGV 349
Cdd:pfam07969 316 AALGGAAGVQPVF--DPLWGDWLQDRlgAERARGLTP--VKELLNAGVKVALGSDApvGPF---------DPWPRIGAAV 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21362535 350 NG-VEDRMSVIWEkgvhSGKMDENRFVAVTSTNAAKIFNLYPKKGRIAVGSDADIVIWDPEATRRISAKTHHQAVnfnif 428
Cdd:pfam07969 383 MRqTAGGGEVLGP----DEELSLEEALALYTSGPAKALGLEDRKGTLGVGKDADLVVLDDDPLTVDPPAIADIRV----- 453
|
490 500
....*....|....*....|
gi 21362535 429 egmvchgvpLVTISRGRVVY 448
Cdd:pfam07969 454 ---------RLTVVDGRVVY 464
|
|
| COG3653 |
COG3653 |
N-acyl-D-aspartate/D-glutamate deacylase [Secondary metabolites biosynthesis, transport and ... |
7-469 |
3.53e-07 |
|
N-acyl-D-aspartate/D-glutamate deacylase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442870 [Multi-domain] Cd Length: 528 Bit Score: 52.87 E-value: 3.53e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21362535 7 LLIRGGRIVndDFS----QVADVLVEDGVVRALGRdlLPPEDASRglrILDAAGKLVLPGGIDTHTHMQFPFMGSQSVDD 82
Cdd:COG3653 4 LLIRGGTVV--DGTgappFRADVAIKGGRIVAVGD--LAAAEAAR---VIDATGLVVAPGFIDIHTHYDLQLLWDPRLEP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21362535 83 F-YQGTkaalaggTTMII-------DFAIPQKGSSLIEAFETW--------RNWADPKvccDY----------------- 129
Cdd:COG3653 77 SlRQGV-------TTVVMgncgvsfAPVRPEDRDRLIDLMEGVegipegldWDWESFG---EYldalerrglgvnvaslv 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21362535 130 ---SLHVAVTWWSDKV--KEE---MKTLARDK------GVNSfkmfmaykGLYMVqdEQLYAAFsqcKEIGAIAQVHAEN 195
Cdd:COG3653 147 ghgTLRAYVMGLDDRPptPEElarMRALLREAmeagalGLST--------GLIYV--PGTYAST---DELVALAKVVAEY 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21362535 196 GDLIAegakkmlalGITGPEGHELCrpEAVEAeatlrAITIASAVNCPLYVVHV---------MSKSAAKVVADARRAG- 265
Cdd:COG3653 214 GGVYQ---------SHMRDEGDGLL--EAVDE-----LIRIGREAGVPVHISHLkaagkpnwgKADEVLALIEAARAEGl 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21362535 266 NV---VYGEPI------------AAGLGTDG--------------RQYWSEEWSHAAHHVMG---------PPLRP---- 303
Cdd:COG3653 278 DVtadVYPYPAgstglgallppwAAAGGLDErlarlrdpatrariRAEIEEGLPDNLLGRGGwdnilisdsPPNEPlvgk 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21362535 304 -----------DPLTpgFLMDLLANGDL----------------------TTTGSDNC--------TFNTCQKALGKddf 342
Cdd:COG3653 358 slaeiaaergvDPAD--AALDLLLEEDGrvlivyfimseedvrellrhpwVMIGSDGGlggkahprAYGTFPRVLGH--- 432
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21362535 343 tkipngvnGVEDR--MSViwEKGVHsgKMdenrfvavTStNAAKIFNLyPKKGRIAVGSDADIVIWDPEatrRISAK-TH 419
Cdd:COG3653 433 --------YVRERgvLSL--EEAVR--KL--------TS-LPADRLGL-KDRGLLRPGYRADLVVFDPA---TLADRaTF 487
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|
gi 21362535 420 HQAVNFNifEGMVChgvplvTISRGRVVYEAGVFNvTAGHGKFIPRQPFA 469
Cdd:COG3653 488 DLPAQRA--DGIRA------VIVNGVVVVEDGKPT-GARPGRVLRGGGAA 528
|
|
| FwdA |
COG1229 |
Formylmethanofuran dehydrogenase subunit A [Energy production and conversion]; |
7-69 |
5.59e-07 |
|
Formylmethanofuran dehydrogenase subunit A [Energy production and conversion];
Pssm-ID: 440842 Cd Length: 554 Bit Score: 52.12 E-value: 5.59e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 21362535 7 LLIRGGRI------VNDDfsqVADVLVEDGVVRAlgrdllPPEDAsRGLRILDAAGKLVLPGGIDTHTH 69
Cdd:COG1229 3 LIIKNGRVydpangIDGE---VMDIAIKDGKIVE------EPSDP-KDAKVIDASGKVVMAGGVDIHTH 61
|
|
| PRK15446 |
PRK15446 |
phosphonate metabolism protein PhnM; Provisional |
6-97 |
8.14e-07 |
|
phosphonate metabolism protein PhnM; Provisional
Pssm-ID: 237967 [Multi-domain] Cd Length: 383 Bit Score: 51.33 E-value: 8.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21362535 6 RLLIRGGRIVNDDFSQVADVLVEDGVVRALGrdllppEDASRGLRILDAAGKLVLPGGIDTHT-----HMQ------FPF 74
Cdd:PRK15446 3 EMILSNARLVLPDEVVDGSLLIEDGRIAAID------PGASALPGAIDAEGDYLLPGLVDLHTdnlekHLAprpgvdWPA 76
|
90 100
....*....|....*....|....
gi 21362535 75 MGS-QSVDdfyqgTKAALAGGTTM 97
Cdd:PRK15446 77 DAAlAAHD-----AQLAAAGITTV 95
|
|
| PRK08393 |
PRK08393 |
N-ethylammeline chlorohydrolase; Provisional |
7-69 |
9.51e-07 |
|
N-ethylammeline chlorohydrolase; Provisional
Pssm-ID: 181411 [Multi-domain] Cd Length: 424 Bit Score: 51.34 E-value: 9.51e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 21362535 7 LLIRGGRIV-NDDFSQV-ADVLVEDGVVRALGRDLLPPEDAsrglrILDAAGKLVLPGGIDTHTH 69
Cdd:PRK08393 3 ILIKNGYVIyGENLKVIrADVLIEGNKIVEVKRNINKPADT-----VIDASGSVVSPGFINAHTH 62
|
|
| PRK08417 |
PRK08417 |
metal-dependent hydrolase; |
299-449 |
1.87e-06 |
|
metal-dependent hydrolase;
Pssm-ID: 236262 [Multi-domain] Cd Length: 386 Bit Score: 50.09 E-value: 1.87e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21362535 299 PPLRPDPlTPGFLMDLLANGDLTTTGSDNC-TFNTcqkalgKDD--FTKIPNGVNGVEDRMSVIWEKGVHSGKMDENRFV 375
Cdd:PRK08417 249 PPLRSKE-DRLALLEALKEGKIDFLTSLHSaKSNS------KKDlaFDEAAFGIDSICEYFSLCYTYLVKEGIITWSELS 321
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 21362535 376 AVTSTNAAKIFNLypKKGRIAVGSDADIVIWDPEAtrRISAKTHHQAVNFNIFEGMVCHgvplvTISRGRVVYE 449
Cdd:PRK08417 322 RFTSYNPAQFLGL--NSGEIEVGKEADLVLFDPNE--STIIDDNFSLYSGDELYGKIEA-----VIIKGKLYLE 386
|
|
| Bact_CD |
cd01293 |
Bacterial cytosine deaminase and related metal-dependent hydrolases. Cytosine deaminases (CDs) ... |
8-122 |
2.31e-06 |
|
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: 49.94 E-value: 2.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21362535 8 LIRGGRIVNDDFSQVaDVLVEDGVVRALGRDLLPPEDASRglriLDAAGKLVLPGGIDTHTHMQFPFMG----------- 76
Cdd:cd01293 1 LLRNARLADGGTALV-DIAIEDGRIAAIGPALAVPPDAEE----VDAKGRLVLPAFVDPHIHLDKTFTGgrwpnnsggtl 75
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 21362535 77 ------------SQSVDDFYQ----GTKAALAGGTTMI-----IDFAIPQKG-SSLIEAFETWRNWAD 122
Cdd:cd01293 76 leaiiaweerklLLTAEDVKEraerALELAIAHGTTAIrthvdVDPAAGLKAlEALLELREEWADLID 143
|
|
| PRK09061 |
PRK09061 |
D-glutamate deacylase; Validated |
6-468 |
2.73e-06 |
|
D-glutamate deacylase; Validated
Pssm-ID: 236369 [Multi-domain] Cd Length: 509 Bit Score: 50.08 E-value: 2.73e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21362535 6 RLLIRGGRIVNDD--FSQVADVLVEDGVVRALGRDLLPPEdasrglRILDAAGKLVLPGGIDTHTHmqfpfmgSQSV-DD 82
Cdd:PRK09061 20 DLVIRNGRVVDPEtgLDAVRDVGIKGGKIAAVGTAAIEGD------RTIDATGLVVAPGFIDLHAH-------GQSVaAY 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21362535 83 FYQgtkaALAGGTTMIidfaipqkgssLIEAfetwrnWADPkvccdyslhvaVTWWSDKVKEEMKTLarDKGVNSFKMFM 162
Cdd:PRK09061 87 RMQ----AFDGVTTAL-----------ELEA------GVLP-----------VARWYAEQAGEGRPL--NYGASVGWTPA 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21362535 163 AYKGLYMVQDEQLYAAFSQC------KEIGAIAQVHAENGDLIAEGAKKMlALGI---------TGP-EGHELCRPEA-- 224
Cdd:PRK09061 133 RIAVLTGPQAEGTIADFGKAlgdprwQERAATPAELAEILELLEQGLDEG-ALGIgigagyapgTGHkEYLELARLAAra 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21362535 225 -----------------VEAEATLRAITIASAVNCPLYVVHVMSKS------AAKVVADARRAGNVVYGE--PIAAGLGT 279
Cdd:PRK09061 212 gvptythvrylsnvdprSSVDAYQELIAAAAETGAHMHICHVNSTSlrdidrCLALVEKAQAQGLDVTTEayPYGAGSTV 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21362535 280 DGRQYWSEEWSHAahhvMGppLRPDPL---------------------TPG------------------------FLMDL 314
Cdd:PRK09061 292 VGAAFFDPGWLER----MG--LGYGSLqwvetgerlltreelaklranDPGglvlihfldednprdralldrsvlFPGAA 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21362535 315 LANGDLTTTGSDNCTFNTCQKALGKDDFTKiPNGvNG---------VEDRMSVIWEKGVHsgKMdenrfvavtSTNAAKI 385
Cdd:PRK09061 366 IASDAMPWTWSDGTVYEGDAWPLPEDAVSH-PRS-AGtfarflreyVRERKALSLLEAIR--KC---------TLMPAQI 432
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21362535 386 FNLY----PKKGRIAVGSDADIVIWDPEatrRISAKTHHQAVNfnifegMVCHGVPLVTISrGRVVYEAGVFNVTAGHGK 461
Cdd:PRK09061 433 LEDSvpamRRKGRLQAGADADIVVFDPE---TITDRATFEDPN------RPSEGVRHVLVN-GVPVVSNGELVRDARPGR 502
|
....*..
gi 21362535 462 FIpRQPF 468
Cdd:PRK09061 503 PV-RRPV 508
|
|
| PRK07228 |
PRK07228 |
5'-deoxyadenosine deaminase; |
5-69 |
3.99e-06 |
|
5'-deoxyadenosine deaminase;
Pssm-ID: 180895 [Multi-domain] Cd Length: 445 Bit Score: 49.23 E-value: 3.99e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 21362535 5 GRLLIRGGRIVNDDFSQV---ADVLVEDGVVRALGRDLLPPEDAsrglRILDAAGKLVLPGGIDTHTH 69
Cdd:PRK07228 1 MTILIKNAGIVTMNAKREivdGDVLIEDDRIAAVGDRLDLEDYD----DHIDATGKVVIPGLIQGHIH 64
|
|
| NagA |
COG1820 |
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism]; |
375-409 |
4.55e-06 |
|
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism];
Pssm-ID: 441425 [Multi-domain] Cd Length: 373 Bit Score: 48.94 E-value: 4.55e-06
10 20 30
....*....|....*....|....*....|....*
gi 21362535 375 VAVTSTNAAKIFNLYPKKGRIAVGSDADIVIWDPE 409
Cdd:COG1820 328 VRMASLNPARALGLDDRKGSIAPGKDADLVVLDDD 362
|
|
| PRK08203 |
PRK08203 |
hydroxydechloroatrazine ethylaminohydrolase; Reviewed |
6-70 |
1.16e-05 |
|
hydroxydechloroatrazine ethylaminohydrolase; Reviewed
Pssm-ID: 236184 [Multi-domain] Cd Length: 451 Bit Score: 47.92 E-value: 1.16e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21362535 6 RLLIRGGRIV---NDDFSQVAD--VLVEDGVVRALGRDLLPPEDASRglrILDAAGKLVLPGGIDTHTHM 70
Cdd:PRK08203 2 TLWIKNPLAIvtmDAARREIADggLVVEGGRIVEVGPGGALPQPADE---VFDARGHVVTPGLVNTHHHF 68
|
|
| AdeC |
COG1001 |
Adenine deaminase [Nucleotide transport and metabolism]; |
7-100 |
1.81e-05 |
|
Adenine deaminase [Nucleotide transport and metabolism];
Pssm-ID: 440625 [Multi-domain] Cd Length: 559 Bit Score: 47.40 E-value: 1.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21362535 7 LLIRGGRIVNddfsqV-------ADVLVEDGVVRALGRDLLPpedasrGLRILDAAGKLVLPGGIDTHTHMQFPFMgsqS 79
Cdd:COG1001 7 LVIKNGRLVN-----VftgeileGDIAIAGGRIAGVGDYIGE------ATEVIDAAGRYLVPGFIDGHVHIESSMV---T 72
|
90 100
....*....|....*....|..
gi 21362535 80 VDDFYqgtKAALAGGTT-MIID 100
Cdd:COG1001 73 PAEFA---RAVLPHGTTtVIAD 91
|
|
| PRK05985 |
PRK05985 |
cytosine deaminase; Provisional |
7-76 |
1.91e-05 |
|
cytosine deaminase; Provisional
Pssm-ID: 180337 [Multi-domain] Cd Length: 391 Bit Score: 46.85 E-value: 1.91e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21362535 7 LLIRGGRivnDDFSQVADVLVEDGVVRALGRDLLPPEdasrGLRILDAAGKLVLPGGIDTHTHMQFPFMG 76
Cdd:PRK05985 4 LLFRNVR---PAGGAAVDILIRDGRIAAIGPALAAPP----GAEVEDGGGALALPGLVDGHIHLDKTFWG 66
|
|
| PRK09228 |
PRK09228 |
guanine deaminase; Provisional |
25-73 |
2.66e-05 |
|
guanine deaminase; Provisional
Pssm-ID: 236419 [Multi-domain] Cd Length: 433 Bit Score: 46.72 E-value: 2.66e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 21362535 25 VLVEDGVVRALG--RDLLPpeDASRGLRILDAAGKLVLPGGIDTHTHmqFP 73
Cdd:PRK09228 34 LLVEDGRIVAAGpyAELRA--QLPADAEVTDYRGKLILPGFIDTHIH--YP 80
|
|
| PRK07583 |
PRK07583 |
cytosine deaminase; |
23-122 |
6.40e-05 |
|
cytosine deaminase;
Pssm-ID: 236062 Cd Length: 438 Bit Score: 45.36 E-value: 6.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21362535 23 ADVLVEDGVVRALgrdlLPPEDASRGLRILDAAGKLVLPGGIDTHTHM-------QFP-----FMGSQ-----------S 79
Cdd:PRK07583 41 VDIEIADGKIAAI----LPAGGAPDELPAVDLKGRMVWPCFVDMHTHLdkghiwpRSPnpdgtFPGALdavtadreahwS 116
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 21362535 80 VDDFYQ----GTKAALAGGTTMI---IDFAIPQKGSSLiEAFETWRN-WAD 122
Cdd:PRK07583 117 AEDLYRrmefGLRCAYAHGTSAIrthLDSFAPQAAISW-EVFAELREaWAG 166
|
|
| YtcJ_like |
cd01300 |
YtcJ_like metal dependent amidohydrolases. YtcJ is a Bacillus subtilis ORF of unknown function. ... |
24-70 |
1.67e-04 |
|
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: 44.22 E-value: 1.67e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 21362535 24 DVLVEDGVVRALGRDLLPPEDASRGLRILDAAGKLVLPGGIDTHTHM 70
Cdd:cd01300 1 AVAVRDGRIVAVGSDAEAKALKGPATEVIDLKGKTVLPGFIDSHSHL 47
|
|
| Met_dep_hydrolase_C |
cd01309 |
Metallo-dependent hydrolases, subgroup C is part of the superfamily of metallo-dependent ... |
29-69 |
2.32e-04 |
|
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: 43.45 E-value: 2.32e-04
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 21362535 29 DGVVRALGRDLLPPEDAsrglRILDAAGKLVLPGGIDTHTH 69
Cdd:cd01309 1 DGKIVAVGAEITTPADA----EVIDAKGKHVTPGLIDAHSH 37
|
|
| FMDH_A |
cd01304 |
Formylmethanofuran dehydrogenase (FMDH) subunit A; Methanogenic bacteria and archea derive ... |
9-69 |
3.23e-04 |
|
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: 43.17 E-value: 3.23e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 21362535 9 IRGGRIV---NDDFSQVADVLVEDGVVRAlgrdllPPEDASRGlRILDAAGKLVLPGGIDTHTH 69
Cdd:cd01304 1 IKNGTVYdplNGINGEKMDIFIRDGKIVE------SSSGAKPA-KVIDASGKVVMAGGVDMHSH 57
|
|
| PRK06038 |
PRK06038 |
N-ethylammeline chlorohydrolase; Provisional |
7-69 |
4.41e-04 |
|
N-ethylammeline chlorohydrolase; Provisional
Pssm-ID: 180363 [Multi-domain] Cd Length: 430 Bit Score: 42.82 E-value: 4.41e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 21362535 7 LLIRGGRIVNDDFSQV--ADVLVEDGVVRALGRDllPPEDASRglrILDAAGKLVLPGGIDTHTH 69
Cdd:PRK06038 4 IIIKNAYVLTMDAGDLkkGSVVIEDGTITEVSES--TPGDADT---VIDAKGSVVMPGLVNTHTH 63
|
|
| PRK07627 |
PRK07627 |
dihydroorotase; Provisional |
6-96 |
5.99e-04 |
|
dihydroorotase; Provisional
Pssm-ID: 181059 [Multi-domain] Cd Length: 425 Bit Score: 42.36 E-value: 5.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21362535 6 RLLIRGGRIVN--DDFSQVADVLVEDGVVRALGRdllPPEDASRGlRILDAAGKLVLPGGIDTHTHMQFPFMGsqsvddf 83
Cdd:PRK07627 2 KIHIKGGRLIDpaAGTDRQADLYVAAGKIAAIGQ---APAGFNAD-KTIDASGLIVCPGLVDLSARLREPGYE------- 70
|
90
....*....|....*...
gi 21362535 84 YQGT-----KAALAGGTT 96
Cdd:PRK07627 71 YKATlesemAAAVAGGVT 88
|
|
| GDEase |
cd01303 |
Guanine deaminase (GDEase). Guanine deaminase is an aminohydrolase responsible for the ... |
27-77 |
9.01e-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: 41.88 E-value: 9.01e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 21362535 27 VEDGVVRALGRDLLPPEDASR-------GLRILDAAGKLVLPGGIDTHTHM-QFPFMGS 77
Cdd:cd01303 24 VEDGLIVVVDGNIIAAGAAETlkraakpGARVIDSPNQFILPGFIDTHIHApQYANIGS 82
|
|
| PRK07203 |
PRK07203 |
putative aminohydrolase SsnA; |
7-69 |
1.69e-03 |
|
putative aminohydrolase SsnA;
Pssm-ID: 235963 [Multi-domain] Cd Length: 442 Bit Score: 40.69 E-value: 1.69e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 21362535 7 LLIRGGRIVNDD----FSQVADVLVEDGVVRALG-RDLLppEDASRGLRILDAAGKLVLPGGIDTHTH 69
Cdd:PRK07203 2 LLIGNGTAITRDpakpVIEDGAIAIEGNVIVEIGtTDEL--KAKYPDAEFIDAKGKLIMPGLINSHNH 67
|
|
| Isoaspartyl-dipeptidase |
cd01308 |
Isoaspartyl dipeptidase hydrolyzes the beta-L-isoaspartyl linkages in dipeptides, as part of ... |
377-409 |
1.81e-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: 40.84 E-value: 1.81e-03
10 20 30
....*....|....*....|....*....|...
gi 21362535 377 VTSTNAAKIFNLYpKKGRIAVGSDADIVIWDPE 409
Cdd:cd01308 330 VITSNVARILKLR-KKGEIQPGFDADLVILDKD 361
|
|
| ureC |
PRK13207 |
urease subunit alpha; Reviewed |
23-98 |
3.58e-03 |
|
urease subunit alpha; Reviewed
Pssm-ID: 237305 [Multi-domain] Cd Length: 568 Bit Score: 40.16 E-value: 3.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21362535 23 ADVLVEDGVVRALGR----DLLPPEDA--SRGLRILDAAGKLVLPGGIDTHTHmqfpFMGSQSVDdfyqgtkAALAGG-T 95
Cdd:PRK13207 85 ADIGIKDGRIVAIGKagnpDIQDGVDIiiGPGTEVIAGEGLIVTAGGIDTHIH----FICPQQIE-------EALASGvT 153
|
...
gi 21362535 96 TMI 98
Cdd:PRK13207 154 TMI 156
|
|
| PRK07572 |
PRK07572 |
cytosine deaminase; Validated |
7-70 |
4.23e-03 |
|
cytosine deaminase; Validated
Pssm-ID: 181039 Cd Length: 426 Bit Score: 39.62 E-value: 4.23e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 21362535 7 LLIRGGRIvnDDFSQVADVLVEDGVVRALGrdllpPEDASRGLRILDAAGKLVLPGGIDTHTHM 70
Cdd:PRK07572 4 LIVRNANL--PDGRTGIDIGIAGGRIAAVE-----PGLQAEAAEEIDAAGRLVSPPFVDPHFHM 60
|
|
| Met_dep_hydrolase_C |
cd01309 |
Metallo-dependent hydrolases, subgroup C is part of the superfamily of metallo-dependent ... |
376-407 |
5.95e-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: 5.95e-03
10 20 30
....*....|....*....|....*....|..
gi 21362535 376 AVTStNAAKIFNLYPKKGRIAVGSDADIVIWD 407
Cdd:cd01309 308 AITI-NPAKILGIEDRVGSLEPGKDADLVVWN 338
|
|
| Urease_alpha |
cd00375 |
Urease alpha-subunit; Urease is a nickel-dependent metalloenzyme that catalyzes the hydrolysis ... |
23-99 |
6.47e-03 |
|
Urease alpha-subunit; Urease is a nickel-dependent metalloenzyme that catalyzes the hydrolysis of urea to form ammonia and carbon dioxide. Nickel-dependent ureases are found in bacteria, fungi and plants. Their primary role is to allow the use of external and internally generated urea as a nitrogen source. The enzyme consists of 3 subunits, alpha, beta and gamma, which can be fused and present on a single protein chain and which in turn forms multimers, mainly trimers. The large alpha subunit is the catalytic domain containing an active site with a bi-nickel center complexed by a carbamylated lysine. The beta and gamma subunits play a role in subunit association to form the higher order trimers.
Pssm-ID: 238221 [Multi-domain] Cd Length: 567 Bit Score: 39.23 E-value: 6.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21362535 23 ADVLVEDGVVRALGR----DLLPPEDAS----RGLRILDAAGKLVLPGGIDTHTHMQFPfmgsqsvddfyQGTKAALAGG 94
Cdd:cd00375 83 ADIGIKDGRIVAIGKagnpDIMDGVTPNmivgPSTEVIAGEGKIVTAGGIDTHVHFICP-----------QQIEEALASG 151
|
....*
gi 21362535 95 TTMII 99
Cdd:cd00375 152 ITTMI 156
|
|
| |
