|
Name |
Accession |
Description |
Interval |
E-value |
| D-HYD |
cd01314 |
D-hydantoinases (D-HYD) also called dihydropyrimidases (DHPase) and related proteins; DHPases ... |
15-464 |
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: 735.18 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568815722 15 LLIKGGRIINDDQSLYADVYLEDGLIKQIGENLIVPGGVKTIEANGRMVIPGGIDVNTYLQKPSQGMTAADDFFQGTRAA 94
Cdd:cd01314 1 LIIKNGTIVTADGSFKADILIEDGKIVAIGPNLEAPGGVEVIDATGKYVLPGGIDPHTHLELPFMGTVTADDFESGTRAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568815722 95 LVGGTTMIIDHVVPEPGSSLLTSFEKWHEAADTKSCCDYSLHVDITSWYDGVREELEVLVqDKGVNSFQVYMAYKDVYQM 174
Cdd:cd01314 81 AAGGTTTIIDFAIPNKGQSLLEAVEKWRGKADGKSVIDYGFHMIITDWTDSVIEELPELV-KKGISSFKVFMAYKGLLMV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568815722 175 SDSQLYEAFTFLKGLGAVILVHAENGDLIAQEQKRILEMGITGPEGHALSRPEELEAEAVFRAITIAGRINCPVYITKVM 254
Cdd:cd01314 160 DDEELLDVLKRAKELGALVMVHAENGDVIAELQKKLLAQGKTGPEYHALSRPPEVEAEATARAIRLAELAGAPLYIVHVS 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568815722 255 SKSAADIIALARKKGPLVFGEPIAASLGTDGTHYWsKNWAKAAAFVTSPPLSPDpTTPDYLTSLLACGDLQVTGSGHCPY 334
Cdd:cd01314 240 SKEAADEIARARKKGLPVYGETCPQYLLLDDSDYW-KDWFEGAKYVCSPPLRPK-EDQEALWDGLSSGTLQTVGSDHCPF 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568815722 335 STAQKAVGKDNFTLIPEGVNGIEERMTVVWDKAVATGKMDENQFVAVTSTNAAKIFNLYPRKGRIAVGSDADVVIWDPDK 414
Cdd:cd01314 318 NFAQKARGKDDFTKIPNGVPGVETRMPLLWSEGVAKGRITLEKFVELTSTNPAKIFGLYPRKGTIAVGSDADLVIWDPNA 397
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 568815722 415 LKTITAKSHKSAVEYNIFEGMECHGSPLVVISQGKIVFEDGNINVNKGMG 464
Cdd:cd01314 398 EKTISADTHHHNVDYNIFEGMKVKGWPVVTISRGKVVVEDGELVGEKGSG 447
|
|
| D-hydantoinase |
TIGR02033 |
D-hydantoinase; This model represents the D-hydantoinase (dihydropyrimidinase) which primarily ... |
15-469 |
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: 664.47 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568815722 15 LLIKGGRIINDDQSLYADVYLEDGLIKQIGENLIVPGGVKTIEANGRMVIPGGIDVNTYLQKPSQGMTAADDFFQGTRAA 94
Cdd:TIGR02033 1 LLIKGGTVVNADDVFQADVLIEGGKIVAVGDNLIPPDAVEVIDATGKYVLPGGIDVHTHLEMPFGGTTTADDFFTGTKAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568815722 95 LVGGTTMIIDHVVPEPGSSLLTSFEKWHEAADTKSCCDYSLHVDITSWYDGVREELEVLVQDKGVNSFQVYMAYKDVYQM 174
Cdd:TIGR02033 81 AAGGTTTIIDFVVPEKGSSLTEALETWHEKAEGKSVIDYGFHMDITHWNDSVLEEHIPEVKEEGINSFKVFMAYKNLLMV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568815722 175 SDSQLYEAFTFLKGLGAVILVHAENGDLIAQEQKRILEMGITGPEGHALSRPEELEAEAVFRAITIAGRINCPVYITKVM 254
Cdd:TIGR02033 161 DDEELFEILKRLKELGALLQVHAENGDIIAELQARMLAQGITGPEYHALSRPPELEAEAVARAITLAALADAPLYVVHVS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568815722 255 SKSAADIIALARKKGPLVFGEPIAASLGTDGTHYWsKNWAKAAAFVTSPPLSpDPTTPDYLTSLLACGDLQVTGSGHCPY 334
Cdd:TIGR02033 241 TKDAADEIAQARKKGQPVFGETCPQYLVLDDTHYD-KPGFEGAKYVCSPPLR-EPEDQDALWSALSSGALQTVGSDHCTF 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568815722 335 STAQK-AVGKDNFTLIPEGVNGIEERMTVVWDKAVATGKMDENQFVAVTSTNAAKIFNLYPRKGRIAVGSDADVVIWDPD 413
Cdd:TIGR02033 319 NFAQKkAIGKDDFTKIPNGGPGVEERMSLLFDEGVAKGRITLEKFVEVTSTNPAKIFNLYPRKGTIAVGSDADIVIWDPN 398
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 568815722 414 KLKTITAKSHKSAVEYNIFEGMECHGSPLVVISQGKIVFEDGNINVNKGMGRFIPR 469
Cdd:TIGR02033 399 RTTVISAETHHSNADYNPFEGFKVRGAPVSVLSRGRVVVEDGQLVGTAGAGRFVKR 454
|
|
| PRK08323 |
PRK08323 |
phenylhydantoinase; Validated |
14-473 |
0e+00 |
|
phenylhydantoinase; Validated
Pssm-ID: 236240 [Multi-domain] Cd Length: 459 Bit Score: 569.42 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568815722 14 RLLIKGGRIINDDQSLYADVYLEDGLIKQIGENlivpGGVKTIEANGRMVIPGGIDVNTYLQKPSQGMTAADDFFQGTRA 93
Cdd:PRK08323 2 STLIKNGTVVTADDTYKADVLIEDGKIAAIGAN----LGDEVIDATGKYVMPGGIDPHTHMEMPFGGTVSSDDFETGTRA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568815722 94 ALVGGTTMIIDHVVPEPGSSLLTSFEKWHEAADTKSCCDYSLHVDITSWYDGVREELEVLVqDKGVNSFQVYMAYKDVYQ 173
Cdd:PRK08323 78 AACGGTTTIIDFALQPKGQSLREALEAWHGKAAGKAVIDYGFHMIITDWNEVVLDEMPELV-EEGITSFKLFMAYKGALM 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568815722 174 MSDSQLYEAFTFLKGLGAVILVHAENGDLIAQEQKRILEMGITGPEGHALSRPEELEAEAVFRAITIAGRINCPVYITKV 253
Cdd:PRK08323 157 LDDDELLRALQRAAELGALPMVHAENGDAIAYLQAKLLAEGKTGPEYHALSRPPEVEGEATNRAIMLAELAGAPLYIVHV 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568815722 254 MSKSAADIIALARKKGPLVFGEPIAASLGTDGTHYWSKNWAKAAAFVTSPPLSPdPTTPDYLTSLLACGDLQVTGSGHCP 333
Cdd:PRK08323 237 SCKEALEAIRRARARGQRVFGETCPQYLLLDESEYDGPDWFEGAKYVMSPPLRD-KEHQDALWRGLQDGDLQVVATDHCP 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568815722 334 YSTAQKA-VGKDNFTLIPEGVNGIEERMTVVWDKAVATGKMDENQFVAVTSTNAAKIFNLYPRKGRIAVGSDADVVIWDP 412
Cdd:PRK08323 316 FCFEQKKqLGRGDFTKIPNGTPGVEDRMPLLFSEGVMTGRITLNRFVELTSTNPAKIFGLYPRKGTIAVGADADIVIWDP 395
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568815722 413 DKLKTITAKSHKSAVEYNIFEGMECHGSPLVVISQGKIVFEDGNINVNKGMGRFIPRKAFP 473
Cdd:PRK08323 396 NATKTISASTLHSNVDYNPYEGFEVTGWPVTTLSRGEVVVEDGEFRGKAGHGRFLKRKPFQ 456
|
|
| PLN02942 |
PLN02942 |
dihydropyrimidinase |
12-473 |
0e+00 |
|
dihydropyrimidinase
Pssm-ID: 178530 Cd Length: 486 Bit Score: 530.96 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568815722 12 SDRLLIKGGRIINDDQSLYADVYLEDGLIKQIGENLIVPGGVKTIEANGRMVIPGGIDVNTYLQKPSQGMTAADDFFQGT 91
Cdd:PLN02942 4 STKILIKGGTVVNAHHQELADVYVEDGIIVAVAPNLKVPDDVRVIDATGKFVMPGGIDPHTHLAMPFMGTETIDDFFSGQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568815722 92 RAALVGGTTMIIDHVVPEPGSsLLTSFEKWHEAADtKSCCDYSLHVDITSWYDGVREELEVLVQDKGVNSFQVYMAYKDV 171
Cdd:PLN02942 84 AAALAGGTTMHIDFVIPVNGN-LLAGYEAYEKKAE-KSCMDYGFHMAITKWDDTVSRDMETLVKEKGINSFKFFMAYKGS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568815722 172 YQMSDSQLYEAFTFLKGLGAVILVHAENGDLIAQEQKRILEMGITGPEGHALSRPEELEAEAVFRAITIAGRINCPVYIT 251
Cdd:PLN02942 162 LMVTDELLLEGFKRCKSLGALAMVHAENGDAVFEGQKRMIELGITGPEGHALSRPPLLEGEATARAIRLAKFVNTPLYVV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568815722 252 KVMSKSAADIIALARKKGPLVFGEPIAASLGTDGTHYWSKNWAKAAAFVTSPPLSPdPTTPDYLTSLLACGDLQVTGSGH 331
Cdd:PLN02942 242 HVMSIDAMEEIARARKSGQRVIGEPVVSGLVLDDSKLWDPDFTIASKYVMSPPIRP-AGHGKALQAALSSGILQLVGTDH 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568815722 332 CPYSTAQKAVGKDNFTLIPEGVNGIEERMTVVWDKAVATGKMDENQFVAVTSTNAAKIFNLYPRKGRIAVGSDADVVIWD 411
Cdd:PLN02942 321 CPFNSTQKAFGKDDFRKIPNGVNGIEERMHLVWDTMVESGQISPTDYVRVTSTECAKIFNIYPRKGAILAGSDADIIILN 400
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568815722 412 PDKLKTITAKSHKSAVEYNIFEGMECHGSPLVVISQGKIVFEDGNINVNKGMGRFIPRKAFP 473
Cdd:PLN02942 401 PNSTFTISAKTHHSRIDTNVYEGRRGKGKVEVTISQGRVVWENGELKVVRGSGRYIEMPPFS 462
|
|
| AllB |
COG0044 |
Dihydroorotase or related cyclic amidohydrolase [Nucleotide transport and metabolism]; ... |
16-469 |
2.82e-125 |
|
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: 375.20 E-value: 2.82e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568815722 16 LIKGGRIINDDQSLYADVYLEDGLIKQIGENLIVPGGVKTIEANGRMVIPGGIDVNTYLQKPsqGMTAADDFFQGTRAAL 95
Cdd:COG0044 1 LIKNGRVVDPGGLERADVLIEDGRIAAIGPDLAAPEAAEVIDATGLLVLPGLIDLHVHLREP--GLEHKEDIETGTRAAA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568815722 96 VGGTTMIIDHVVPEPGSSLLTSFEKWHEAADTKSCCDYSLHVDITSWYDGVREELEVLVqDKGVNSFQVYMAYKDVYQMS 175
Cdd:COG0044 79 AGGVTTVVDMPNTNPVTDTPEALEFKLARAEEKALVDVGPHGALTKGLGENLAELGALA-EAGAVAFKVFMGSDDGNPVL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568815722 176 DSQ-LYEAFTFLKGLGAVILVHAENGDLIAQeqkRILEMGITGPEGHALSRPEELEAEAVFRAITIAGRINCPVYITKVM 254
Cdd:COG0044 158 DDGlLRRALEYAAEFGALVAVHAEDPDLIRG---GVMNEGKTSPRLGLKGRPAEAEEEAVARDIALAEETGARLHIVHVS 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568815722 255 SKSAADIIALARKKGPLVFGE--P-----IAASLGTDGTHYwsknwakaaafVTSPPLsPDPTTPDYLTSLLACGDLQVT 327
Cdd:COG0044 235 TAEAVELIREAKARGLPVTAEvcPhhltlTDEDLERYGTNF-----------KVNPPL-RTEEDREALWEGLADGTIDVI 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568815722 328 GSGHCPYSTAQKAvgkDNFTLIPEGVNGIEERMTVVWDKAVATGKMDENQFVAVTSTNAAKIFNLyPRKGRIAVGSDADV 407
Cdd:COG0044 303 ATDHAPHTLEEKE---LPFAEAPNGIPGLETALPLLLTELVHKGRLSLERLVELLSTNPARIFGL-PRKGRIAVGADADL 378
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568815722 408 VIWDPDKLKTITAKSHKSAVEYNIFEGMECHGSPLVVISQGKIVFEDGNInVNKGMGRFIPR 469
Cdd:COG0044 379 VLFDPDAEWTVTAEDLHSKSKNTPFEGRELTGRVVATIVRGRVVYEDGEV-VGEPRGRFLRR 439
|
|
| PRK13404 |
PRK13404 |
dihydropyrimidinase; Provisional |
15-469 |
2.19e-121 |
|
dihydropyrimidinase; Provisional
Pssm-ID: 184033 [Multi-domain] Cd Length: 477 Bit Score: 366.33 E-value: 2.19e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568815722 15 LLIKGGRIINDDQSLYADVYLEDGLIKQIGENLivPGGVKTIEANGRMVIPGGIDVNTYLQKPS-QGMTAADDFFQGTRA 93
Cdd:PRK13404 6 LVIRGGTVVTATDTFQADIGIRGGRIAALGEGL--GPGAREIDATGRLVLPGGVDSHCHIDQPSgDGIMMADDFYTGTVS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568815722 94 ALVGGTTMIIDHVVPEPGSSLLTSFEKWHEAADTKSCCDYSLHVDITSWYDGV-REELEVLVQDkGVNSFQVYMAYkDVY 172
Cdd:PRK13404 84 AAFGGTTTVIPFAAQHRGQSLREAVEDYHRRAAGKAVIDYAFHLIVADPTEEVlTEELPALIAQ-GYTSFKVFMTY-DDL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568815722 173 QMSDSQLYEAFTFLKGLGAVILVHAENGDLIAQEQKRILEMGITGPEGHALSRPEELEAEAVFRAITIAGRINCPVYITK 252
Cdd:PRK13404 162 KLDDRQILDVLAVARRHGAMVMVHAENHDMIAWLTKRLLAAGLTAPKYHAISRPMLAEREATHRAIALAELVDVPILIVH 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568815722 253 VMSKSAADIIALARKKGPLVFGEP-------IAASLGTDGTHywsknwakAAAFVTSPPLSpDPTTPDYLTSLLACGDLQ 325
Cdd:PRK13404 242 VSGREAAEQIRRARGRGLKIFAETcpqylflTAEDLDRPGME--------GAKYICSPPPR-DKANQEAIWNGLADGTFE 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568815722 326 VTGSGHCPY---STAQKAVGKDN--FTLIPEGVNGIEERMTVVWDKAVATGKMDENQFVAVTSTNAAKIFNLYPRKGRIA 400
Cdd:PRK13404 313 VFSSDHAPFrfdDTDGKLAAGANpsFKAIANGIPGIETRLPLLFSEGVVKGRISLNRFVALTSTNPAKLYGLYPRKGAIA 392
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568815722 401 VGSDADVVIWDPDKLKTITAKSHKSAVEYNIFEGMECHGSPLVVISQGKIVFEDGNINVNKGMGRFIPR 469
Cdd:PRK13404 393 IGADADIAIWDPDREVTITNADLHHAADYTPYEGMRVTGWPVTVLSRGRVVVEDGELVAERGSGQFLAR 461
|
|
| L-HYD_ALN |
cd01315 |
L-Hydantoinases (L-HYDs) and Allantoinase (ALN); L-Hydantoinases are a member of the ... |
15-455 |
8.85e-69 |
|
L-Hydantoinases (L-HYDs) and Allantoinase (ALN); L-Hydantoinases are a member of the dihydropyrimidinase family, which catalyzes the reversible hydrolytic ring opening of dihydropyrimidines and hydantoins (five-membered cyclic diamides used in biotechnology). But L-HYDs differ by having an L-enantio specificity and by lacking activity on possible natural substrates such as dihydropyrimidines. Allantoinase catalyzes the hydrolytic cleavage of the five-member ring of allantoin (5-ureidohydantoin) to form allantoic acid.
Pssm-ID: 238640 [Multi-domain] Cd Length: 447 Bit Score: 229.10 E-value: 8.85e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568815722 15 LLIKGGRIINDDQSLYADVYLEDGLIKQIGENLIVPGGVKTIEANGRMVIPGGIDVNTYLQKPsqGMTAADDFFQGTRAA 94
Cdd:cd01315 2 LVIKNGRVVTPDGVREADIAVKGGKIAAIGPDIANTEAEEVIDAGGLVVMPGLIDTHVHINEP--GRTEWEGFETGTKAA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568815722 95 LVGGTTMIIDhvVP---EPGSSLLTSFEKWHEAADTKSccdyslHVDITSWYDGVR---EELEVLVqDKGVNSFQVYMA- 167
Cdd:cd01315 80 AAGGITTIID--MPlnsIPPTTTVENLEAKLEAAQGKL------HVDVGFWGGLVPgnlDQLRPLD-EAGVVGFKCFLCp 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568815722 168 --YKDVYQMSDSQLYEAFTFLKGLGAVILVHAENGDLIAQEQKRILEMGITGPEGHALSRPEELEAEAVFRAITIAGRIN 245
Cdd:cd01315 151 sgVDEFPAVDDEQLEEAMKELAKTGSVLAVHAENPEITEALQEQAKAKGKRDYRDYLASRPVFTEVEAIQRILLLAKETG 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568815722 246 CPVYITKVMSKSAADIIALARKKGPLVFGEpiaaslgtDGTHYWS-------KNwakAAAFVTSPPLSpDPTTPDYLTSL 318
Cdd:cd01315 231 CRLHIVHLSSAEAVPLIREARAEGVDVTVE--------TCPHYLTftaedvpDG---GTEFKCAPPIR-DAANQEQLWEA 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568815722 319 LACGDLQVTGSGHCPYSTAQKAVGKDNFTLIPEGVNGIEERMTVVWDKAVATGKMDENQFVAVTSTNAAKIFNLYPRKGR 398
Cdd:cd01315 299 LENGDIDMVVSDHSPCTPELKLLGKGDFFKAWGGISGLQLGLPVMLTEAVNKRGLSLEDIARLMCENPAKLFGLSHQKGR 378
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 568815722 399 IAVGSDADVVIWDPDKLKTITAKSHKSAVEYNIFEGMECHGSPLVVISQGKIVFEDG 455
Cdd:cd01315 379 IAVGYDADFVVWDPEEEFTVDAEDLYYKNKISPYVGRTLKGRVHATILRGTVVYQDG 435
|
|
| Cyclic_amidohydrolases |
cd01302 |
Cyclic amidohydrolases, including hydantoinase, dihydropyrimidinase, allantoinase, and ... |
63-441 |
1.14e-65 |
|
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: 217.26 E-value: 1.14e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568815722 63 VIPGGIDVNTYLQKPSQGMTAaDDFFQGTRAALVGGTTMIIDHVVPEPGSSLLTSFEKWHEAADTKSCCDYSLHVDITSw 142
Cdd:cd01302 3 VLPGFIDIHVHLRDPGGTTYK-EDFESGSRAAAAGGVTTVIDMPNTGPPPIDLPAIELKIKLAEESSYVDFSFHAGIGP- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568815722 143 yDGVREELEvLVQDKGVNSFQVYMAYK--DVYQMSDSQLYEAFTFLKGLGAVILVHAEngdliaqeqkrilemgitgpeg 220
Cdd:cd01302 81 -GDVTDELK-KLFDAGINSLKVFMNYYfgELFDVDDGTLMRTFLEIASRGGPVMVHAE---------------------- 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568815722 221 halsrpeeleaeavfRAITIAGRINCPVYITKVMSKSAADIIALARKKGPLVFGEPIAASLGTDgTHYWSKNWAKaaaFV 300
Cdd:cd01302 137 ---------------RAAQLAEEAGANVHIAHVSSGEALELIKFAKNKGVKVTCEVCPHHLFLD-ESMLRLNGAW---GK 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568815722 301 TSPPLSPdPTTPDYLTSLLACGDLQVTGSGHCPYSTAQKAVGKDnFTLIPEGVNGIEERMTVVWdKAVATGKMDENQFVA 380
Cdd:cd01302 198 VNPPLRS-KEDREALWEGVKNGKIDTIASDHAPHSKEEKESGKD-IWKAPPGFPGLETRLPILL-TEGVKRGLSLETLVE 274
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568815722 381 VTSTNAAKIFNLYPrKGRIAVGSDADVVIWDPDKLKTITAKSHKSAVEYNIFEGMECHGSP 441
Cdd:cd01302 275 ILSENPARIFGLYP-KGTIAVGYDADLVIVDPKKEWKVTAEEIESKADWTPFEGMEVTGKP 334
|
|
| PRK02382 |
PRK02382 |
dihydroorotase; Provisional |
15-470 |
4.99e-58 |
|
dihydroorotase; Provisional
Pssm-ID: 179417 [Multi-domain] Cd Length: 443 Bit Score: 200.26 E-value: 4.99e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568815722 15 LLIKGGRIINDDQSLYADVYLEDGLIKQIGENLIVPGGVKTIEANGRMVIPGGIDVNTYLQKPsqGMTAADDFFQGTRAA 94
Cdd:PRK02382 4 ALLKDGRVYYNNSLQPRDVRIDGGKITAVGKDLDGSSSEEVIDARGMLLLPGGIDVHVHFREP--GYTHKETWYTGSRSA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568815722 95 LVGGTTMIIDHVVPEPGSSLLTSFEKWHEAADTKSCCDYSLHvditswyDGVREELEVLVQ--DKGVNSF-QVYMAyKDV 171
Cdd:PRK02382 82 AAGGVTTVVDQPNTDPPTVDGESFDEKAELAARKSIVDFGIN-------GGVTGNWDPLESlwERGVFALgEIFMA-DST 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568815722 172 YQMS-DSQLY-EAFTFLKGLGAVILVHAENGDLIAqEQKRILEmGITGPEGHALSRPEELEAEAVFRAITIAGRINCPVY 249
Cdd:PRK02382 154 GGMGiDEELFeEALAEAARLGVLATVHAEDEDLFD-ELAKLLK-GDADADAWSAYRPAAAEAAAVERALEVASETGARIH 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568815722 250 ITKVmskSAADIIALARKKGPLVFGEPIAASLGTDgthywskNWAKAAAFV-TSPPLSPDPTTpDYLTSLLACGDLQVTG 328
Cdd:PRK02382 232 IAHI---STPEGVDAARREGITCEVTPHHLFLSRR-------DWERLGTFGkMNPPLRSEKRR-EALWERLNDGTIDVVA 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568815722 329 SGHCPYSTAQKAVG-KDnftlIPEGVNGIEERMTVVWdKAVATGKMDENQFVAVTSTNAAKIFNLyPRKGRIAVGSDADV 407
Cdd:PRK02382 301 SDHAPHTREEKDADiWD----APSGVPGVETMLPLLL-AAVRKNRLPLERVRDVTAANPARIFGL-DGKGRIAEGYDADL 374
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568815722 408 VIWDPDKLKTITAKSHKSAVEYNIFEGMEchGS-PLVVISQGKIVFEDGNINVNKGMGRFIPRK 470
Cdd:PRK02382 375 VLVDPDAAREIRGDDLHSKAGWTPFEGME--GVfPELTMVRGTVVWDGDDINAKRGRGEFLRGR 436
|
|
| allantoinase |
TIGR03178 |
allantoinase; This enzyme carries out the first step in the degradation of allantoin, a ... |
15-468 |
7.33e-56 |
|
allantoinase; This enzyme carries out the first step in the degradation of allantoin, a ring-opening hydrolysis. The seed members of this model are all in the vicinity of other genes involved in the processes of xanthine/urate/allantoin catabolism. Although not included in the seed, many eukaryotic homologs of this family are included above the trusted cutoff. Below the noise cutoff are related hydantoinases.
Pssm-ID: 163175 [Multi-domain] Cd Length: 443 Bit Score: 194.52 E-value: 7.33e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568815722 15 LLIKGGRIINDDQSLYADVYLEDGLIKQIGENlIVPGGVKTIEANGRMVIPGGIDVNTYLQKPsqGMTAADDFFQGTRAA 94
Cdd:TIGR03178 2 LIIRGGRVILPNGEREADVGVKGGKIAAIGPD-ILGPAAKIIDAGGLVVFPGVVDTHVHINEP--GRTEWEGFETGTRAA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568815722 95 LVGGTTMIIDhvVP---EPGSSLLTSFEKWHEAADTKsccdysLHVDITSWYDGVREELEVL--VQDKGVNSFQVYMAY- 168
Cdd:TIGR03178 79 AAGGITTYID--MPlnsIPATTTRASLEAKFEAAKGK------LAVDVGFWGGLVPYNLDDLreLDEAGVVGFKAFLSPs 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568815722 169 --KDVYQMSDSQLYEAFTFLKGLGAVILVHAENGDLIAQEQKRILEMGITGPEGHALSRPEELEAEAVFRAITIAGRINC 246
Cdd:TIGR03178 151 gdDEFPHVDDWQLYKGMRELARLGQLLLVHAENPAITSALGEEAPPQGGVGADAYLASRPVFAEVEAIRRTLALAKVTGC 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568815722 247 PVYITKVMSKSAADIIALARKKGPLVFGEPIaaslgtdgTHYWSKNWAK----AAAFVTSPPLSpDPTTPDYLTSLLACG 322
Cdd:TIGR03178 231 RVHVVHLSSAEAVELITEAKQEGLDVTVETC--------PHYLTLTAEEvpdgGTLAKCAPPIR-DLANQEGLWEALLNG 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568815722 323 DLQVTGSGHCPYSTAQKAvgKDNFTLIPEGVNGIEERMTVVWDKAVATGKMDENQFVAVTSTNAAKIFNLyPRKGRIAVG 402
Cdd:TIGR03178 302 LIDCVVSDHSPCTPDLKR--AGDFFKAWGGIAGLQSTLDVMFDEAVQKRGLPLEDIARLMATNPAKRFGL-AQKGRIAPG 378
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568815722 403 SDADVVIWDPDKLKTITAKSHKSAVEYNIFEGMECHGSPLVVISQGKIVFEDGNInVNKGMGRFIP 468
Cdd:TIGR03178 379 KDADFVFVDPDESYTLTPDDLYYRHKVSPYVGRTIGGRVRATYLRGQCIYDDEQF-IGAPKGQLLL 443
|
|
| PRK06189 |
PRK06189 |
allantoinase; Provisional |
15-458 |
7.72e-50 |
|
allantoinase; Provisional
Pssm-ID: 235732 [Multi-domain] Cd Length: 451 Bit Score: 178.36 E-value: 7.72e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568815722 15 LLIKGGRIINDDQSLYADVYLEDGLIKQIGENLIVPGGvKTIEANGRMVIPGGIDVNTYLQKPsqGMTAADDFFQGTRAA 94
Cdd:PRK06189 5 LIIRGGKVVTPEGVYRADIGIKNGKIAEIAPEISSPAR-EIIDADGLYVFPGMIDVHVHFNEP--GRTHWEGFATGSAAL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568815722 95 LVGGTTMIIDhvVPEPGS-SLLT--SFEKWHEAADTKSCCDYSLHVDITSwydGVREELEVLVqDKGVNSFQVYMAYK-- 169
Cdd:PRK06189 82 AAGGCTTYFD--MPLNSIpPTVTreALDAKAELARQKSAVDFALWGGLVP---GNLEHLRELA-EAGVIGFKAFMSNSgt 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568815722 170 DVYQMSDSQ-LYEAFTFLKGLGAVILVHAENGDLIAQEQKRILEMGITGPEGHALSRPEELEAEAVFRAITIAGRINCPV 248
Cdd:PRK06189 156 DEFRSSDDLtLYEGMKEIAALGKILALHAESDALTRHLTTQARQQGKTDVRDYLESRPVVAELEAVQRALLYAQETGCPL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568815722 249 YITKVMSKSAADIIALARKKG--------P--LVFGEPIAASLGTdgthywsknWAKAAafvtsPPLSpDPTTPDYLTSL 318
Cdd:PRK06189 236 HFVHISSGKAVALIAEAKKRGvdvsvetcPhyLLFTEEDFERIGA---------VAKCA-----PPLR-SRSQKEELWRG 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568815722 319 LACGDLQVTGSGHCPYSTAQKAvgKDNFTLIPEGVNGIEERMTVVWDKAVATGKMDENQFVAVTSTNAAKIFNLyPRKGR 398
Cdd:PRK06189 301 LLAGEIDMISSDHSPCPPELKE--GDDFFLVWGGISGGQSTLLVMLTEGYIERGIPLETIARLLATNPAKRFGL-PQKGR 377
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 568815722 399 IAVGSDADVVIWDPDKLKTITAKSHKSAVEYNIFEGMECHGSPLVVISQGKIVFEDGNIN 458
Cdd:PRK06189 378 LEVGADADFVLVDLDETYTLTKEDLFYRHKQSPYEGRTFPGRVVATYLRGQCVYQDGEVF 437
|
|
| DHOase_IIb |
cd01318 |
Dihydroorotase (DHOase), subgroup IIb; DHOases catalyze the reversible interconversion of ... |
60-448 |
1.28e-41 |
|
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: 153.64 E-value: 1.28e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568815722 60 GRMVIPGGIDVNTYLQKPsqGMTAADDFFQGTRAALVGGTTMIIDHVVPEPGSSLLTSFEKWHEAADTKSCCDYSLHVDI 139
Cdd:cd01318 1 GLLILPGVIDIHVHFREP--GLTYKEDFVSGSRAAAAGGVTTVMDMPNTKPPTTTAEALYEKLRLAAAKSVVDYGLYFGV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568815722 140 TSWYDGvrEELEVLvqdkGVNSFQVYMAyKDVYQMSD--SQLYEAFtflKGLGAVILVHAENGDLIAQEQKRILEMGItg 217
Cdd:cd01318 79 TGSEDL--EELDKA----PPAGYKIFMG-DSTGDLLDdeETLERIF---AEGSVLVTFHAEDEDRLRENRKELKGESA-- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568815722 218 pegHALSRPEELEAEAVFRAITIAGRINCPVYITKVmskSAADIIALARKKGP----------LVFGEPIAASLGTdgth 287
Cdd:cd01318 147 ---HPRIRDAEAAAVATARALKLARRHGARLHICHV---STPEELKLIKKAKPgvtvevtphhLFLDVEDYDRLGT---- 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568815722 288 ywsknWAKaaafvTSPPLSpDPTTPDYLTSLLACGDLQVTGSGHCPYSTAQKAVGKDNftlIPEGVNGIEERMTVVWDkA 367
Cdd:cd01318 217 -----LGK-----VNPPLR-SREDRKALLQALADGRIDVIASDHAPHTLEEKRKGYPA---APSGIPGVETALPLMLT-L 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568815722 368 VATGKMDENQFVAVTSTNAAKIFNLyPRKGRIAVGSDADVVIWDPDKLKTITAKSHKSAVEYNIFEGMECHGSPLVVISQ 447
Cdd:cd01318 282 VNKGILSLSRVVRLTSHNPARIFGI-KNKGRIAEGYDADLTVVDLKEERTIRAEEFHSKAGWTPFEGFEVTGFPVMTIVR 360
|
.
gi 568815722 448 G 448
Cdd:cd01318 361 G 361
|
|
| pyrC |
PRK09357 |
dihydroorotase; Validated |
14-454 |
9.17e-38 |
|
dihydroorotase; Validated
Pssm-ID: 236479 [Multi-domain] Cd Length: 423 Bit Score: 144.57 E-value: 9.17e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568815722 14 RLLIKGGRIINDDQSLY-ADVYLEDGLIKQIGENLIVPGgVKTIEANGRMVIPGGIDVNTYLQKPsqGMTAADDFFQGTR 92
Cdd:PRK09357 2 MILIKNGRVIDPKGLDEvADVLIDDGKIAAIGENIEAEG-AEVIDATGLVVAPGLVDLHVHLREP--GQEDKETIETGSR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568815722 93 AALVGGTTMiidhVVPEPG-----SSLLTSFEKWHEAADTKSCcdyslHVD----ITswydgVREELEVLVQDKGVNSFQ 163
Cdd:PRK09357 79 AAAAGGFTT----VVAMPNtkpviDTPEVVEYVLDRAKEAGLV-----DVLpvgaIT-----KGLAGEELTEFGALKEAG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568815722 164 VYMAYKDVYQMSDSQL-YEAFTFLKGLGAVILVHAE----NGDLIAQEQKRILEMGITGpeghalsRPEELEAEAVFRAI 238
Cdd:PRK09357 145 VVAFSDDGIPVQDARLmRRALEYAKALDLLIAQHCEdpslTEGGVMNEGEVSARLGLPG-------IPAVAEEVMIARDV 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568815722 239 TIAGRINCPVYITKVMSKSAADIIALARKKGPlvfgePIAA------------SLGTDGTHYwsknwaKAAafvtsPPLS 306
Cdd:PRK09357 218 LLAEATGARVHICHVSTAGSVELIRWAKALGI-----KVTAevtphhllltdeDLLTYDPNY------KVN-----PPLR 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568815722 307 pDPTTPDYLTSLLACGDLQVTGSGHCPYSTAQKAVGkdnFTLIPEGVNGIEERMTVVWDKAVATGKMDENQFVAVTSTNA 386
Cdd:PRK09357 282 -TEEDREALIEGLKDGTIDAIATDHAPHAREEKECE---FEAAPFGITGLETALSLLYTTLVKTGLLDLEQLLEKMTINP 357
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568815722 387 AKIFNLYPrkGRIAVGSDADVVIWDPDKLKTITAKSHKSAVEYNIFEGMECHGSPLVVISQGKIVFED 454
Cdd:PRK09357 358 ARILGLPA--GPLAEGEPADLVIFDPEAEWTVDGEDFASKGKNTPFIGMKLKGKVVYTIVDGKIVYQD 423
|
|
| PRK07575 |
PRK07575 |
dihydroorotase; Provisional |
12-458 |
1.46e-34 |
|
dihydroorotase; Provisional
Pssm-ID: 236055 [Multi-domain] Cd Length: 438 Bit Score: 135.57 E-value: 1.46e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568815722 12 SDRLLIKGGRIINDDQSLY-ADVYLEDGLIKQIGENLIVPGGVKTIEANGRMVIPGGIDVNTYLQKPsqGMTAADDFFQG 90
Cdd:PRK07575 2 MMSLLIRNARILLPSGELLlGDVLVEDGKIVAIAPEISATAVDTVIDAEGLTLLPGVIDPQVHFREP--GLEHKEDLFTA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568815722 91 TRAALVGGTTMIIDHVVPEPgssLLTSFEKWHEA---ADTKSCCDYSLHVDITSwydgvrEELEVLVQDKGVNSFQVYMA 167
Cdd:PRK07575 80 SRACAKGGVTSFLEMPNTKP---LTTTQAALDDKlarAAEKCVVNYGFFIGATP------DNLPELLTANPTCGIKIFMG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568815722 168 YKDVYQMSDSQLYEAFTFLKGlGAVILVHAENgdliaqeQKRILE-----MGITGPEGHALSRPEELEAEAVFRAITIAG 242
Cdd:PRK07575 151 SSHGPLLVDEEAALERIFAEG-TRLIAVHAED-------QARIRArraefAGISDPADHSQIQDEEAALLATRLALKLSK 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568815722 243 RINCPVYITKVmsKSAADIIALARKKGPLVFGE--PIAASLGTDgthywskNWAKAAAFV-TSPPLSpDPTTPDYLTSLL 319
Cdd:PRK07575 223 KYQRRLHILHL--STAIEAELLRQDKPSWVTAEvtPQHLLLNTD-------AYERIGTLAqMNPPLR-SPEDNEALWQAL 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568815722 320 ACGDLQVTGSGHCPYSTAQKAVGKDNftlIPEGVNGIEERMTVVWDKAVAtGKMDENQFVAVTSTNAAKIFNLyPRKGRI 399
Cdd:PRK07575 293 RDGVIDFIATDHAPHTLEEKAQPYPN---SPSGMPGVETSLPLMLTAAMR-GKCTVAQVVRWMSTAVARAYGI-PNKGRI 367
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 568815722 400 AVGSDADVVIWDPDKLKTITAKSHKSAVEYNIFEGMECHGSPLVVISQGKIVFEDGNIN 458
Cdd:PRK07575 368 APGYDADLVLVDLNTYRPVRREELLTKCGWSPFEGWNLTGWPVTTIVGGQIVFDRGQVN 426
|
|
| PRK08044 |
PRK08044 |
allantoinase AllB; |
15-413 |
7.11e-34 |
|
allantoinase AllB;
Pssm-ID: 169193 [Multi-domain] Cd Length: 449 Bit Score: 133.83 E-value: 7.11e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568815722 15 LLIKGGRIINDDQSLYADVYLEDGLIKQIGENLivPGGVKTIEANGRMVIPGGIDVNTYLQKPsqGMTAADDFFQGTRAA 94
Cdd:PRK08044 5 LIIKNGTVILENEARVVDIAVKGGKIAAIGQDL--GDAKEVMDASGLVVSPGMVDAHTHISEP--GRSHWEGYETGTRAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568815722 95 LVGGTTMIIDHVVPE-PGSSLLTSFEKWHEAADTKSCCDYSLHVDITSW-YDGVREELEVlvqdkGVNSFQVYMAY---- 168
Cdd:PRK08044 81 AKGGITTMIEMPLNQlPATVDRASIELKFDAAKGKLTIDAAQLGGLVSYnLDRLHELDEV-----GVVGFKCFVATcgdr 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568815722 169 ---KDVYQMSDSQLYEAFTFLKGLGAVILVHAENG---DLIAQEQKRileMGITGPEGHALSRPEELEAEAVFRAITIAG 242
Cdd:PRK08044 156 gidNDFRDVNDWQFYKGAQKLGELGQPVLVHCENAlicDELGEEAKR---EGRVTAHDYVASRPVFTEVEAIRRVLYLAK 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568815722 243 RINCPVYITKVMSKSAADIIALARKKGPLVFGEPIaaslgtdgTHYWSKNWAKAAAFVT----SPPLSpDPTTPDYLTSL 318
Cdd:PRK08044 233 VAGCRLHVCHISSPEGVEEVTRARQEGQDVTCESC--------PHYFVLDTDQFEEIGTlakcSPPIR-DLENQKGMWEK 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568815722 319 LACGDLQVTGSGHCPYSTAQKAvgkDNFTLIPEGVNGIEERMTVVWDKAVATGKMDENQFVAVTSTNAAKIFNLyPRKGR 398
Cdd:PRK08044 304 LFNGEIDCLVSDHSPCPPEMKA---GNIMEAWGGIAGLQNCMDVMFDEAVQKRGMSLPMFGKLMATNAADIFGL-QQKGR 379
|
410
....*....|....*
gi 568815722 399 IAVGSDADVVIWDPD 413
Cdd:PRK08044 380 IAPGKDADFVFIQPN 394
|
|
| DHOase_IIa |
cd01317 |
Dihydroorotase (DHOase), subgroup IIa; DHOases catalyze the reversible interconversion of ... |
52-442 |
4.45e-33 |
|
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: 130.05 E-value: 4.45e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568815722 52 GVKTIEANGRMVIPGGIDVNTYLQKPSQgmTAADDFFQGTRAALVGGTTMII--DHVVPEPGSSLLTSFEKwHEAADTKS 129
Cdd:cd01317 1 DAEVIDAEGKILAPGLVDLHVHLREPGF--EYKETLESGAKAAAAGGFTTVVcmPNTNPVIDNPAVVELLK-NRAKDVGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568815722 130 CCDYSLhVDITSWYDGVR-EELEVLVqDKGVNSFQvymayKDVYQMSDSQ-LYEAFTFLKGLGAVILVHAENGDL----I 203
Cdd:cd01317 78 VRVLPI-GALTKGLKGEElTEIGELL-EAGAVGFS-----DDGKPIQDAElLRRALEYAAMLDLPIIVHPEDPSLagggV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568815722 204 AQEQKRILEMGITGpeghalsRPEELEAEAVFRAITIAGRINCPVYITKVMSKSAADIIALARKKGPLVFGEPIAASL-- 281
Cdd:cd01317 151 MNEGKVASRLGLPG-------IPPEAETIMVARDLELAEATGARVHFQHLSTARSLELIRKAKAKGLPVTAEVTPHHLll 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568815722 282 -GTDGTHYwsknwakAAAFVTSPPLSpDPTTPDYLTSLLACGDLQVTGSGHCPYSTAQKAVGkdnFTLIPEGVNGIEERM 360
Cdd:cd01317 224 dDEALESY-------DTNAKVNPPLR-SEEDREALIEALKDGTIDAIASDHAPHTDEEKDLP---FAEAPPGIIGLETAL 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568815722 361 TVVWDKAVATGKMDENQFVAVTSTNAAKIFNLYPrkGRIAVGSDADVVIWDPDKLKTITAKSHKSAVEYNIFEGMECHGS 440
Cdd:cd01317 293 PLLWTLLVKGGLLTLPDLIRALSTNPAKILGLPP--GRLEVGAPADLVLFDPDAEWIVDEETFRSKSKNTPFDGQKLKGR 370
|
..
gi 568815722 441 PL 442
Cdd:cd01317 371 VL 372
|
|
| PLN02795 |
PLN02795 |
allantoinase |
20-458 |
5.05e-28 |
|
allantoinase
Pssm-ID: 178392 [Multi-domain] Cd Length: 505 Bit Score: 117.57 E-value: 5.05e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568815722 20 GRIINDDQSLYADVYLEDGLIKQIGENLIVPG---GVKTIEANGRMVIPGGIDVNTYLQKPsqGMTAADDFFQGTRAALV 96
Cdd:PLN02795 51 KRVVTPAGVIPGAVEVEGGRIVSVTKEEEAPKsqkKPHVLDYGNAVVMPGLIDVHVHLNEP--GRTEWEGFPTGTKAAAA 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568815722 97 GGTTMIIDhvVP---EPGSSLLTSFEKWHEAADTKsccdysLHVDITSWYDGVRE------ELEVLVqDKGVNSFQVYM- 166
Cdd:PLN02795 129 GGITTLVD--MPlnsFPSTTSVETLELKIEAAKGK------LYVDVGFWGGLVPEnahnasVLEELL-DAGALGLKSFMc 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568815722 167 --AYKDVYQMSDSQLYEAFTFLKGLGAVILVHAENGDLIAQEQKriLEMGITGPEGHALSRPEELEAEAVFRAITIAGRI 244
Cdd:PLN02795 200 psGINDFPMTTATHIKAALPVLAKYGRPLLVHAEVVSPVESDSR--LDADPRSYSTYLKSRPPSWEQEAIRQLLEVAKDT 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568815722 245 N-------CPVYITKVM-SKSAADIIALARKKGPLVFGEPIAaslgtdgtHYWsknwAKAAA--------FVTSPPLSpD 308
Cdd:PLN02795 278 RpggvaegAHVHIVHLSdAESSLELIKEAKAKGDSVTVETCP--------HYL----AFSAEeipdgdtrYKCAPPIR-D 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568815722 309 PTTPDYLTSLLACGDLQVTGSGHCPYSTAQKAVGKDNFTLIPEGVNGIEERMTVVWDKAVATGkMDENQFVAVTSTNAAK 388
Cdd:PLN02795 345 AANRELLWKALLDGDIDMLSSDHSPSPPDLKLLEEGNFLRAWGGISSLQFVLPATWTAGRAYG-LTLEQLARWWSERPAK 423
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568815722 389 IFNLyPRKGRIAVGSDADVVIWDP------DKLKTITAKsHKSAVEYnifEGMECHGSPLVVISQGKIVFEDGNIN 458
Cdd:PLN02795 424 LAGL-DSKGAIAPGKDADIVVWDPeaefvlDESYPIYHK-HKSLSPY---LGTKLSGKVIATFVRGNLVFLEGKHA 494
|
|
| PRK04250 |
PRK04250 |
dihydroorotase; Provisional |
20-467 |
9.89e-26 |
|
dihydroorotase; Provisional
Pssm-ID: 235265 [Multi-domain] Cd Length: 398 Bit Score: 109.47 E-value: 9.89e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568815722 20 GRIINDDQSLYADVYLEDGLIKQIGENLIvpGGVKTIEANGRMVIPGGIDVNTYLQkpsqgmtaadDFFQ--------GT 91
Cdd:PRK04250 4 GKFLLKGRIVEGGIGIENGRISKISLRDL--KGKEVIKVKGGIILPGLIDVHVHLR----------DFEEsyketiesGT 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568815722 92 RAALVGGTTMIIDHVVPEPGSSLLTSFEKWHEAADTKSCCDYSLHVDITSWYDGVREELEvlvqdkgvNSFQVYM--AYK 169
Cdd:PRK04250 72 KAALHGGITLVFDMPNTKPPIMDEKTYEKRMRIAEKKSYADYALNFLIAGNCEKAEEIKA--------DFYKIFMgaSTG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568815722 170 DVYQMSDSQLYEAftflkgLGAVILVHAENGDLIAQEqkrilemgitgPEghalsRPEELEAEAVFRAITIAGRINCPVY 249
Cdd:PRK04250 144 GIFSENFEVDYAC------APGIVSVHAEDPELIREF-----------PE-----RPPEAEVVAIERALEAGKKLKKPLH 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568815722 250 ITKVMSKSAADIIalARKKGPLVFGEPIAASLgtdgtHYWSKNWAKAAAFVTSPPLSpdpTTPDYLTSLLACGDLQVTGS 329
Cdd:PRK04250 202 ICHISTKDGLKLI--LKSNLPWVSFEVTPHHL-----FLTRKDYERNPLLKVYPPLR---SEEDRKALWENFSKIPIIAS 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568815722 330 GHCPYSTAQKAVGKdnftlipEGVNGIEERMTVVWDkAVATGKMDENQFVAVTSTNAAKIFNlYPRKGrIAVGSDADVVI 409
Cdd:PRK04250 272 DHAPHTLEDKEAGA-------AGIPGLETEVPLLLD-AANKGMISLFDIVEKMHDNPARIFG-IKNYG-IEEGNYANFAV 341
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 568815722 410 WDPDKLKTITAKSHKSAVEYNIFEGMECHGSPLVVISQGKIVFEDGNInVNKGMGRFI 467
Cdd:PRK04250 342 FDMKKEWTIKAEELYTKAGWTPYEGFKLKGKVIMTILRGEVVMEDDEI-IGKPRGVRI 398
|
|
| PRK01211 |
PRK01211 |
dihydroorotase; Provisional |
30-469 |
9.55e-25 |
|
dihydroorotase; Provisional
Pssm-ID: 179247 [Multi-domain] Cd Length: 409 Bit Score: 106.87 E-value: 9.55e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568815722 30 YADVYLEDGLIKQIGENLivpGGVKTIEANGrMVIPGGIDVNTYLQKPsqGMTAADDFFQGTRAALVGGTTMIIDHVVPE 109
Cdd:PRK01211 15 YLEIEVEDGKIKSIKKDA---GNIGKKELKG-AILPAATDIHVHFRTP--GETEKEDFSTGTLSAIFGGTTFIMDMPNNN 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568815722 110 PGSSLLTSFEKWHEAADTKSCCDYSLHVDITSwydgvreeLEVLVQDKGVNSFQVYMAYKDVYQMSDSQLYEAfTFLKGL 189
Cdd:PRK01211 89 IPIKDYNAFSDKLGRVAPKAYVDFSLYSMETG--------NNALILDERSIGLKVYMGGTTNTNGTDIEGGEI-KKINEA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568815722 190 GAVILVHAENGDLIAQ---EQKRILEmgitgpegHALSRPEELEAEAVfraitiaGRINCPVYITKVMS-KSAADIIA-L 264
Cdd:PRK01211 160 NIPVFFHAELSECLRKhqfESKNLRD--------HDLARPIECEIKAV-------KYVKNLDLKTKIIAhVSSIDVIGrF 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568815722 265 ARKKGP--LVFGEPIaaSLGTDGThywsknwakaaafvTSPPLSPDPTTPDYLTSLLAcGDLQVTGSGHCPYSTAQKAvg 342
Cdd:PRK01211 225 LREVTPhhLLLNDDM--PLGSYGK--------------VNPPLRDRWTQERLLEEYIS-GRFDILSSDHAPHTEEDKQ-- 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568815722 343 kdNFTLIPEGVNGIEERMTVVWdKAVATGKMDENQFVAVTSTNAAKIFNLypRKGRIAVGSDADVVIWDPDKLKTITAKS 422
Cdd:PRK01211 286 --EFEYAKSGIIGVETRVPLFL-ALVKKKILPLDVLYKTAIERPASLFGI--KKGKIEEGYDADFMAFDFTNIKKINDKR 360
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 568815722 423 HKSAVEYNIFEGMECHgSPLVVISQGKIVFEDGNInVNKGMGRFIPR 469
Cdd:PRK01211 361 LHSKCPVSPFNGFDAI-FPSHVIMRGEVVIDNYEL-ISERTGKFVPK 405
|
|
| PRK09060 |
PRK09060 |
dihydroorotase; Validated |
15-465 |
5.22e-24 |
|
dihydroorotase; Validated
Pssm-ID: 181632 [Multi-domain] Cd Length: 444 Bit Score: 105.00 E-value: 5.22e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568815722 15 LLIKGGRIINDDQSLYADVYLEDGLIKQIGENLIVPGGvKTIEANGRMVIPGGIDVNTYLQKPsqGMTAADDFFQGTRAA 94
Cdd:PRK09060 7 LILKGGTVVNPDGEGRADIGIRDGRIAAIGDLSGASAG-EVIDCRGLHVLPGVIDSQVHFREP--GLEHKEDLETGSRAA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568815722 95 LVGGTTMIIDHVVPEPGSSLLTSFEKWHEAADTKSCCDYSLHVDITSwyDGVRE--ELEVLvqdKGVNSFQVYM--AYKD 170
Cdd:PRK09060 84 VLGGVTAVFEMPNTNPLTTTAEALADKLARARHRMHCDFAFYVGGTR--DNADElaELERL---PGCAGIKVFMgsSTGD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568815722 171 VYQMSDSQLYEAftfLKGLGAVILVHAENgDLIAQEQKRILEMGitGPEGHALSRPEELEAEAVFRAITIAGRINCPVYI 250
Cdd:PRK09060 159 LLVEDDEGLRRI---LRNGRRRAAFHSED-EYRLRERKGLRVEG--DPSSHPVWRDEEAALLATRRLVRLARETGRRIHV 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568815722 251 TKVmskSAADIIA-LARKKG-------P--LVFGEPIA-ASLGTdgthYWSKNwakaaafvtsPPLSpDPTTPDYLTSLL 319
Cdd:PRK09060 233 LHV---STAEEIDfLADHKDvatvevtPhhLTLAAPECyERLGT----LAQMN----------PPIR-DARHRDGLWRGV 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568815722 320 ACGDLQVTGSGHCPYSTAQKAvgkDNFTLIPEGVNGIEERMTVVWDKaVATGKMDENQFVAVTSTNAAKIFNLyPRKGRI 399
Cdd:PRK09060 295 RQGVVDVLGSDHAPHTLEEKA---KPYPASPSGMTGVQTLVPIMLDH-VNAGRLSLERFVDLTSAGPARIFGI-AGKGRI 369
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568815722 400 AVGSDADVVIWDPDKLKTITAKSHKSAVEYNIFEGMECHGSPLVVISQGKIVFEDGNInVNKGMGR 465
Cdd:PRK09060 370 AVGYDADFTIVDLKRRETITNEWIASRCGWTPYDGKEVTGWPVGTIVRGQRVMWDGEL-VGPPTGE 434
|
|
| Amidohydro_1 |
pfam01979 |
Amidohydrolase family; This family of enzymes are a a large metal dependent hydrolase ... |
62-451 |
4.38e-19 |
|
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: 88.71 E-value: 4.38e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568815722 62 MVIPGGIDVNTYLQ------KPSQGMTAADDFFQGTRAALVGGTTMIIDHvvpepGSSLLTSFEKWHEAAD--------- 126
Cdd:pfam01979 1 IVLPGLIDAHVHLEmgllrgIPVPPEFAYEALRLGITTMLKSGTTTVLDM-----GATTSTGIEALLEAAEelplglrfl 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568815722 127 TKSCC---DYSLHVDITSWyDGVREELEVLVQDKGVNsFQVYMAYKDVYQMSDSQLYEAFTFLKGLGAVILVHAENGDLI 203
Cdd:pfam01979 76 GPGCSldtDGELEGRKALR-EKLKAGAEFIKGMADGV-VFVGLAPHGAPTFSDDELKAALEEAKKYGLPVAIHALETKGE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568815722 204 AQEQKRIlemgitgpeghalsrpeeleaeavfraitIAGRINCPVYITKVMSKSAADIIALARKkgplvfgepiaaslgt 283
Cdd:pfam01979 154 VEDAIAA-----------------------------FGGGIEHGTHLEVAESGGLLDIIKLILA---------------- 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568815722 284 DGTHYWSKNWAKAAAFVTSPPLSPDPTTPDYLTS-------LLACGDLQVTGSGHCpystaqkaVGKDNFTLIPEGVNGI 356
Cdd:pfam01979 189 HGVHLSPTEANLLAEHLKGAGVAHCPFSNSKLRSgrialrkALEDGVKVGLGTDGA--------GSGNSLNMLEELRLAL 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568815722 357 EERmtvvwdkAVATGKMDENQFVAVTSTNAAKIFNLYPRKGRIAVGSDADVVIWDPDKLktitakshksaveyNIFEGME 436
Cdd:pfam01979 261 ELQ-------FDPEGGLSPLEALRMATINPAKALGLDDKVGSIEVGKDADLVVVDLDPL--------------AAFFGLK 319
|
410
....*....|....*
gi 568815722 437 CHGSPLVVISQGKIV 451
Cdd:pfam01979 320 PDGNVKKVIVKGKIV 334
|
|
| PRK09236 |
PRK09236 |
dihydroorotase; Reviewed |
13-458 |
6.37e-17 |
|
dihydroorotase; Reviewed
Pssm-ID: 181716 Cd Length: 444 Bit Score: 83.38 E-value: 6.37e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568815722 13 DRLLIKGGRIINDDQSLYADVYLEDGLIKQIGENLIVPGGVKTIEANGRMVIPGGIDVNTYLQKPsqGMTAADDFFQGTR 92
Cdd:PRK09236 2 KRILIKNARIVNEGKIFEGDVLIENGRIAKIASSISAKSADTVIDAAGRYLLPGMIDDQVHFREP--GLTHKGDIASESR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568815722 93 AALVGGTTMIID--HVVPePGSSLLTSFEKWHEAAdTKSCCDYSLHVDITSwyDGVrEELEVLvqDK----GVNSFqvym 166
Cdd:PRK09236 80 AAVAGGITSFMEmpNTNP-PTTTLEALEAKYQIAA-QRSLANYSFYFGATN--DNL-DEIKRL--DPkrvcGVKVF---- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568815722 167 aykdvyqMSDS---QLYEAFTFLKGLGA----VILVHAENGDLI-AQEQKRILEMG--ITgPEGHALSRpeelEAEAVFR 236
Cdd:PRK09236 149 -------MGAStgnMLVDNPETLERIFRdaptLIATHCEDTPTIkANLAKYKEKYGddIP-AEMHPLIR----SAEACYK 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568815722 237 ----AITIAGRINcpvyiTK--VMSKSAADIIALARkKGPLVfGEPIAASLGTDGTHYWSKNWAKAAAFVTSPPLSPDPT 310
Cdd:PRK09236 217 ssslAVSLAKKHG-----TRlhVLHISTAKELSLFE-NGPLA-EKRITAEVCVHHLWFDDSDYARLGNLIKCNPAIKTAS 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568815722 311 TPDYLTSLLACGDLQVTGSGHCPYSTAQKAVGkdnFTLIPEGVNGIEERMTVVWDKaVATGKMDENQFVAVTSTNAAKIF 390
Cdd:PRK09236 290 DREALRQALADDRIDVIATDHAPHTWEEKQGP---YFQAPSGLPLVQHALPALLEL-VHEGKLSLEKVVEKTSHAPAILF 365
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568815722 391 NLyPRKGRIAVGSDADVVIWDPDKLKTITAKSHKSAVEYNIFEGMECHGSPLVVISQGKIVFEDGNIN 458
Cdd:PRK09236 366 DI-KERGFIREGYWADLVLVDLNSPWTVTKENILYKCGWSPFEGRTFRSRVATTFVNGQLVYHNGQLV 432
|
|
| CAD_DHOase |
cd01316 |
The eukaryotic CAD protein is a trifunctional enzyme of carbamoylphosphate ... |
64-464 |
1.27e-15 |
|
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: 78.26 E-value: 1.27e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568815722 64 IPGGIDVNTYLQKPsqGMTAADDFFQGTRAALVGGTTMIidHVVPEPGSSLL--TSFEKWHEAADTKSCCDYSLHVDITS 141
Cdd:cd01316 5 LPGLIDVHVHLREP--GATHKEDFASGTKAALAGGFTMV--RAMPNTNPSIVdvASLKLVQSLAQAKARCDYAFSIGATS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568815722 142 WYDGVREELevlvQDKGVNSFQVYMAYKDVYQMSD-SQLYEAFTFLKGLGAVIlVHAENGDLIAqeqkrILEMgitgpeG 220
Cdd:cd01316 81 TNAATVGEL----ASEAVGLKFYLNETFSTLILDKiTAWASHFNAWPSTKPIV-THAKSQTLAA-----VLLL------A 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568815722 221 HALSRpeeleaeavfraitiagrincPVYITKVMSKSAADIIALARKKGPLVFGEPIAASLgtdgthYWSKNWAKAAAFV 300
Cdd:cd01316 145 SLHNR---------------------SIHICHVSSKEEINLIRLAKARGLKVTCEVSPHHL------FLSQDDLPRGQYE 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568815722 301 TSPPLsPDPTTPDYLTSLLACGDlqVTGSGHCPYSTAQKAVGKdnftlIPEGVNGIEERMTVVWdKAVATGKMDENQFVA 380
Cdd:cd01316 198 VRPFL-PTREDQEALWENLDYID--CFATDHAPHTLAEKTGNK-----PPPGFPGVETSLPLLL-TAVHEGRLTIEDIVD 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568815722 381 VTSTNAAKIFNLYPrkgriavgsDADVVI-WDPDKLKTITAKSHKSAVEYNIFEGMECHGSPLVVISQGKIVFEDGNINV 459
Cdd:cd01316 269 RLHTNPKRIFNLPP---------QSDTYVeVDLDEEWTIPKNPLQSKKGWTPFEGKKVKGKVQRVVLRGETAFIDGEIVA 339
|
....*
gi 568815722 460 NKGMG 464
Cdd:cd01316 340 PPGFG 344
|
|
| pyrC |
PRK00369 |
dihydroorotase; Provisional |
32-471 |
5.53e-14 |
|
dihydroorotase; Provisional
Pssm-ID: 234738 [Multi-domain] Cd Length: 392 Bit Score: 74.03 E-value: 5.53e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568815722 32 DVYLEDGlIKQIGENLIVpgGVKTIEANGR---------MVIPGGIDVNTYLQkpsqGMTAA--DDFFQGTRAALVGGTT 100
Cdd:PRK00369 8 KAYLGKE-IKEICINFDR--RIKEIKSRCKpdldlpqgtLILPGAIDLHVHLR----GLKLSykEDVASGTSEAAYGGVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568815722 101 MIID--HVVPePGSSLLTSFEKWHEAADtKSCCDYSLhvditswYDGVREELEVLvqDK-GVNSFQVYMaykdvyqmSDS 177
Cdd:PRK00369 81 LVADmpNTIP-PLNTPEAITEKLAELEY-YSRVDYFV-------YSGVTKDPEKV--DKlPIAGYKIFP--------EDL 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568815722 178 QLYEAFTFLKGLGAVILVHAENGDLIAQEQKrilemgitgpeghaLSRPEELEAEAVFraiTIAGRINcpVYITKVmskS 257
Cdd:PRK00369 142 EREETFRVLLKSRKLKILHPEVPLALKSNRK--------------LRRNCWYEIAALY---YVKDYQN--VHITHA---S 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568815722 258 AADIIALARKKGplvfgepiaasLGTDGT-HYWSKNWAKAAAFVTSPPLSpDPTTPDYLTSLLACGDLQVtgSGHCPYST 336
Cdd:PRK00369 200 NPRTVRLAKELG-----------FTVDITpHHLLVNGEKDCLTKVNPPIR-DINERLWLLQALSEVDAIA--SDHAPHSS 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568815722 337 AQKavgKDNFTLIPEGVNGIEERMTVVWdKAVATGKMDENQFVAVTSTNAAKIFNLypRKGRIAVGSDADVVI--WDPDK 414
Cdd:PRK00369 266 FEK---LQPYEVCPPGIAALSFTPPFIY-TLVSKGILSIDRAVELISTNPARILGI--PYGEIKEGYRANFTViqFEDWR 339
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 568815722 415 LKTITAKshksaVEYNIFEGMECHGSPLVVISQGKIVFEDGNINVNKGMGRFIPRKA 471
Cdd:PRK00369 340 YSTKYSK-----VIETPLDGFELKASVYATIVQGKLAYLEGEVFPVKGINPFGERKR 391
|
|
| HutI |
COG1228 |
Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport ... |
12-454 |
9.75e-11 |
|
Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440841 [Multi-domain] Cd Length: 386 Bit Score: 63.83 E-value: 9.75e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568815722 12 SDRLLIKGGRIIN-DDQSLY--ADVYLEDGLIKQIGEN--LIVPGGVKTIEANGRMVIPGGIDVNTYL---------QKP 77
Cdd:COG1228 7 AGTLLITNATLVDgTGGGVIenGTVLVEDGKIAAVGPAadLAVPAGAEVIDATGKTVLPGLIDAHTHLglgggraveFEA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568815722 78 SQGMTAADDFFQGT----RAALVGGTTMIIDHvvpePGSSL----------LTSFEKWH-EAADTKSCCDYSLHvdiTSW 142
Cdd:COG1228 87 GGGITPTVDLVNPAdkrlRRALAAGVTTVRDL----PGGPLglrdaiiageSKLLPGPRvLAAGPALSLTGGAH---ARG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568815722 143 YDGVREELEVLVQDkGVNSFQVYMAYKDvYQMSDSQLYEAFTFLKGLGAVILVHAENGDLIaqeqKRILEMGITGPEgHA 222
Cdd:COG1228 160 PEEARAALRELLAE-GADYIKVFAEGGA-PDFSLEELRAILEAAHALGLPVAAHAHQADDI----RLAVEAGVDSIE-HG 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568815722 223 LSRPEEleaeavfraitiagrincpvyitkvmsksaadIIALARKKGPLVfgepiaaslgtdgthywsknwakaaafvts 302
Cdd:COG1228 233 TYLDDE--------------------------------VADLLAEAGTVV------------------------------ 250
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568815722 303 ppLSPDPTTPDYLTSLLACGDLQVTGSGHC-PYSTAQK--------AVGKDNFTLIPEGVNGIEErmtvvWDKAVATGkM 373
Cdd:COG1228 251 --LVPTLSLFLALLEGAAAPVAAKARKVREaALANARRlhdagvpvALGTDAGVGVPPGRSLHRE-----LALAVEAG-L 322
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568815722 374 DENQ-FVAVTStNAAKIFNLYPRKGRIAVGSDADVVIWDPDKLKTITAkshksaveynifegmecHGSPLVVISQGKIVF 452
Cdd:COG1228 323 TPEEaLRAATI-NAAKALGLDDDVGSLEPGKLADLVLLDGDPLEDIAY-----------------LEDVRAVMKDGRVVD 384
|
..
gi 568815722 453 ED 454
Cdd:COG1228 385 RS 386
|
|
| PRK07369 |
PRK07369 |
dihydroorotase; Provisional |
31-425 |
2.33e-10 |
|
dihydroorotase; Provisional
Pssm-ID: 236002 [Multi-domain] Cd Length: 418 Bit Score: 62.70 E-value: 2.33e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568815722 31 ADVYLEDGLIKQIGENLI-VPGGVKTIEANGRMVIPGGIDVNTYLQKPsqGMTAADDFFQGTRAALVGGTTMI------- 102
Cdd:PRK07369 22 ADVLIEDGKIQAIEPHIDpIPPDTQIIDASGLILGPGLVDLYSHSGEP--GFEERETLASLAAAAAAGGFTRVailpdtf 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568815722 103 --IDHvvPEPGSSLLTSFE-----KWHE-AADTKSCCDYSLhvdiTSWYDgvreelevLVQdKGVNSFqvymaykdvyqm 174
Cdd:PRK07369 100 ppLDN--PATLARLQQQAQqippvQLHFwGALTLGGQGKQL----TELAE--------LAA-AGVVGF------------ 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568815722 175 SDSQ-------LYEAFTFLKGLGAVILVHAENGDL----IAQEQKRILEMGITGpeghalsRPEELEAEAVFRAITIAGR 243
Cdd:PRK07369 153 TDGQplenlalLRRLLEYLKPLGKPVALWPCDRSLagngVMREGLLALRLGLPG-------DPASAETTALAALLELVAA 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568815722 244 INCPVYITKVMSKSAADIIALARKKGPlvfgePIAAS-------LGTDGTHYWSKNWAKAaafvtsPPLsPDPTTPDYLT 316
Cdd:PRK07369 226 IGTPVHLMRISTARSVELIAQAKARGL-----PITASttwmhllLDTEALASYDPNLRLD------PPL-GNPSDRQALI 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568815722 317 SLLACGDLQVTGSGHCPYSTAQKAVGkdnFTLIPEGVNGIEERMTVVWDKAVATGKMDENQFVAVTSTNAAKIFNLYPRk 396
Cdd:PRK07369 294 EGVRTGVIDAIAIDHAPYTYEEKTVA---FAEAPPGAIGLELALPLLWQNLVETGELSALQLWQALSTNPARCLGQEPP- 369
|
410 420
....*....|....*....|....*....
gi 568815722 397 gRIAVGSDADVVIWDPDKLKTITAKSHKS 425
Cdd:PRK07369 370 -SLAPGQPAELILFDPQKTWTVSAQTLHS 397
|
|
| D-aminoacylase |
cd01297 |
D-aminoacylases (N-acyl-D-Amino acid amidohydrolases) catalyze the hydrolysis of ... |
15-455 |
9.26e-10 |
|
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: 60.77 E-value: 9.26e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568815722 15 LLIKGGRIIndDQS----LYADVYLEDGLIKQIGENLIVPgGVKTIEANGRMVIPGGIDVNTYlqkpSQGMTAADDFFqg 90
Cdd:cd01297 2 LVIRNGTVV--DGTgappFTADVGIRDGRIAAIGPILSTS-AREVIDAAGLVVAPGFIDVHTH----YDGQVFWDPDL-- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568815722 91 TRAALVGGTTMIIDhvvpEPGSSLltsfekwheaadtksccdYSLHVDITSWYDGVREELEVLVQDKGVnSFQVYMAYKD 170
Cdd:cd01297 73 RPSSRQGVTTVVLG----NCGVSP------------------APANPDDLARLIMLMEGLVALGEGLPW-GWATFAEYLD 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568815722 171 VYQMSDSQLYEAFTFlkGLGAV-ILVHAENGDLIAQEQ----KRILE-------MGI-TG----PEGHAlsRPEELEAEA 233
Cdd:cd01297 130 ALEARPPAVNVAALV--GHAALrRAVMGLDAREATEEElakmRELLRealeagaLGIsTGlayaPRLYA--GTAELVALA 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568815722 234 vfraiTIAGRINCpVYITKVMSKSAA------DIIALARKKG-PLVFgepiaASLGTDGTHYWSKnWAKAAAFVTSPPLS 306
Cdd:cd01297 206 -----RVAARYGG-VYQTHVRYEGDSilealdELLRLGRETGrPVHI-----SHLKSAGAPNWGK-IDRLLALIEAARAE 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568815722 307 PDPTTPD---YLTSLLA-------------CGDLQVTGSGHC------PYSTAQKAVGKDNFTLiPEGVngieERMTvvw 364
Cdd:cd01297 274 GLQVTADvypYGAGSEDdvrrimahpvvmgGSDGGALGKPHPrsygdfTRVLGHYVRERKLLSL-EEAV----RKMT--- 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568815722 365 dkavatgkmdenqfvavtsTNAAKIFNLYPRkGRIAVGSDADVVIWDPDKLK---TITAKSHKSaveynifEGMEchgsp 441
Cdd:cd01297 346 -------------------GLPARVFGLADR-GRIAPGYRADIVVFDPDTLAdraTFTRPNQPA-------EGIE----- 393
|
490
....*....|....
gi 568815722 442 LVVISqGKIVFEDG 455
Cdd:cd01297 394 AVLVN-GVPVVRDG 406
|
|
| NagA |
cd00854 |
N-acetylglucosamine-6-phosphate deacetylase, NagA, catalyzes the hydrolysis of the N-acetyl ... |
15-413 |
2.76e-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: 56.05 E-value: 2.76e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568815722 15 LLIKGGRIINDDQSLYADVYLEDGLIKQIGENLIVPGGVKTIEANGRMVIPGGIDVNTYlqkpsqG------MTAADDFF 88
Cdd:cd00854 1 LIIKNARILTPGGLEDGAVLVEDGKIVAIGPEDELEEADEIIDLKGQYLVPGFIDIHIH------GgggadfMDGTAEAL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568815722 89 QGTRAALV--GGTTMiidhvVPepgsSLLT-SFEKWHEAADtksccdyslhvditswydgvreelevlvqdkgvnsfqvy 165
Cdd:cd00854 75 KTIAEALAkhGTTSF-----LP----TTVTaPPEEIAKALA--------------------------------------- 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568815722 166 mAYKDVYQmsdsqlyeaftflKGLGAVIL-VHAEnGDLIAQEQKrilemgitG--PEGHALS-RPEELE-----AEAVFR 236
Cdd:cd00854 107 -AIAEAIA-------------EGQGAEILgIHLE-GPFISPEKK--------GahPPEYLRApDPEELKkwleaAGGLIK 163
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568815722 237 AITIAGRIncpvyitkvmsKSAADIIALARKKGplvfgepIAASLG-TDGTHYWSKNWAKAAA-FVT------SPPLSPD 308
Cdd:cd00854 164 LVTLAPEL-----------DGALELIRYLVERG-------IIVSIGhSDATYEQAVAAFEAGAtHVThlfnamSPLHHRE 225
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568815722 309 P-------TTPDYLTSLLAcgDLQvtgsgHCPYST---AQKAVGKDNFTLI---------PEGVNGIEERMTVVWDKAV- 368
Cdd:cd00854 226 PgvvgaalSDDDVYAELIA--DGI-----HVHPAAvrlAYRAKGADKIVLVtdamaaaglPDGEYELGGQTVTVKDGVAr 298
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568815722 369 -ATG-------KMDE-------------NQFVAVTSTNAAKIFNLYPRKGRIAVGSDADVVIWDPD 413
Cdd:cd00854 299 lADGtlagstlTMDQavrnmvkwggcplEEAVRMASLNPAKLLGLDDRKGSLKPGKDADLVVLDDD 364
|
|
| PRK07627 |
PRK07627 |
dihydroorotase; Provisional |
14-454 |
2.80e-07 |
|
dihydroorotase; Provisional
Pssm-ID: 181059 [Multi-domain] Cd Length: 425 Bit Score: 53.14 E-value: 2.80e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568815722 14 RLLIKGGRIIN-----DDQslyADVYLEDGLIKQIGEnliVPGGV---KTIEANGRMVIPGGIDVNTYLQKPsqGMTAAD 85
Cdd:PRK07627 2 KIHIKGGRLIDpaagtDRQ---ADLYVAAGKIAAIGQ---APAGFnadKTIDASGLIVCPGLVDLSARLREP--GYEYKA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568815722 86 DFFQGTRAALVGGTTMII-----DHVVPEPGSSLLTSF--EKWHEAadtksccdyslHV----DITSWYDGVR-EELEVL 153
Cdd:PRK07627 74 TLESEMAAAVAGGVTSLVcppdtDPVLDEPGLVEMLKFraRNLNQA-----------HVyplgALTVGLKGEVlTEMVEL 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568815722 154 VQDKGVNSFQVymaykDVyQMSDSQ-LYEAFTFLKGLG-AVILvhaengdliaQEQKRILEMGITGPEGHALSR------ 225
Cdd:PRK07627 143 TEAGCVGFSQA-----NV-PVVDTQvLLRALQYASTFGfTVWL----------RPLDAFLGRGGVAASGAVASRlglsgv 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568815722 226 PEELEAEAVFRAITIAGRINCPVYITKVMSKSAADIIALARKKgplvfGEPIAASLGTDGTH-------YWSKNwakaaa 298
Cdd:PRK07627 207 PVAAETIALHTIFELMRVTGARVHLARLSSAAGVALVRAAKAE-----GLPVTCDVGVNHVHlidvdigYFDSQ------ 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568815722 299 FVTSPPLSpDPTTPDYLTSLLACGDLQVTGSGHCPystaqkaVGKDNfTLIP-----EGVNGIEE--RMTVVWdkAVATg 371
Cdd:PRK07627 276 FRLDPPLR-SQRDREAIRAALADGTIDAICSDHTP-------VDDDE-KLLPfaeatPGATGLELllPLTLKW--ADEA- 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568815722 372 KMDENQFVAVTSTNAAKIFNLypRKGRIAVGSDADVVIWDPDKLKTITAKSHKSAVEYNIFEGMECHGSPLVVISQGKIV 451
Cdd:PRK07627 344 KVPLARALARITSAPARVLGL--PAGRLAEGAPADLCVFDPDAHWRVEPRALKSQGKNTPFLGYELPGRVRATLVAGQVA 421
|
...
gi 568815722 452 FED 454
Cdd:PRK07627 422 FER 424
|
|
| ATZ_TRZ_like |
cd01298 |
TRZ/ATZ family contains enzymes from the atrazine degradation pathway and related hydrolases. ... |
15-458 |
3.80e-07 |
|
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: 52.59 E-value: 3.80e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568815722 15 LLIKGGRIINDDQS---LYADVYLEDGLIKQIGENLIVPG--GVKTIEANGRMVIPGGIDVNT----------------- 72
Cdd:cd01298 1 ILIRNGTIVTTDPRrvlEDGDVLVEDGRIVAVGPALPLPAypADEVIDAKGKVVMPGLVNTHThlamtllrgladdlplm 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568815722 73 -YLQK---PSQGMTAADDFFQGTRAALV----GGTTMIIDHVVPEPGSSLltsfekwhEAADtKSccdyslhvditswyd 144
Cdd:cd01298 81 eWLKDliwPLERLLTEEDVYLGALLALAemirSGTTTFADMYFFYPDAVA--------EAAE-EL--------------- 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568815722 145 GVREELEVLVQDKGVnsfqvymayKDVYQMSDSqLYEAFTFLKglgaviLVHAENGDLIaqeqkRILeMGITGPEghaLS 224
Cdd:cd01298 137 GIRAVLGRGIMDLGT---------EDVEETEEA-LAEAERLIR------EWHGAADGRI-----RVA-LAPHAPY---TC 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568815722 225 RPEELEaeavfRAITIAGRINCPVYITkvMSKSAADI-IALARK-KGPLVFgepiAASLGTDGTHYWsknwakAAAFVTs 302
Cdd:cd01298 192 SDELLR-----EVAELAREYGVPLHIH--LAETEDEVeESLEKYgKRPVEY----LEELGLLGPDVV------LAHCVW- 253
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568815722 303 pplspdpTTPDYLTsLLACGDLQVTgsgHCPYSTAQKAVGkdnFTLIPE----GVN---------------GIEE-RMTV 362
Cdd:cd01298 254 -------LTDEEIE-LLAETGTGVA---HNPASNMKLASG---IAPVPEmleaGVNvglgtdgaasnnnldMFEEmRLAA 319
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568815722 363 VWDKAVA--TGKMDENQFVAVTSTNAAKIFNLyPRKGRIAVGSDADVVIWDPDKLKTITAKSHKSAVEYNifegmeCHGS 440
Cdd:cd01298 320 LLQKLAHgdPTALPAEEALEMATIGGAKALGL-DEIGSLEVGKKADLILIDLDGPHLLPVHDPISHLVYS------ANGG 392
|
490 500
....*....|....*....|
gi 568815722 441 P--LVVISqGKIVFEDGNIN 458
Cdd:cd01298 393 DvdTVIVN-GRVVMEDGELL 411
|
|
| NagA |
COG1820 |
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism]; |
379-413 |
9.89e-07 |
|
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism];
Pssm-ID: 441425 [Multi-domain] Cd Length: 373 Bit Score: 51.25 E-value: 9.89e-07
10 20 30
....*....|....*....|....*....|....*
gi 568815722 379 VAVTSTNAAKIFNLYPRKGRIAVGSDADVVIWDPD 413
Cdd:COG1820 328 VRMASLNPARALGLDDRKGSIAPGKDADLVVLDDD 362
|
|
| PRK07228 |
PRK07228 |
5'-deoxyadenosine deaminase; |
14-105 |
2.75e-06 |
|
5'-deoxyadenosine deaminase;
Pssm-ID: 180895 [Multi-domain] Cd Length: 445 Bit Score: 50.00 E-value: 2.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568815722 14 RLLIKGGRIINDDQS---LYADVYLEDGLIKQIGENLIVPGGVKTIEANGRMVIPGGIDVNTYL-QKPSQG--------- 80
Cdd:PRK07228 2 TILIKNAGIVTMNAKreiVDGDVLIEDDRIAAVGDRLDLEDYDDHIDATGKVVIPGLIQGHIHLcQTLFRGiaddlelld 81
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 568815722 81 --------MTAADDFFQGTRAALVG-------GTTMIIDH 105
Cdd:PRK07228 82 wlkdriwpLEAAHDAESMYYSALLGigeliesGTTTIVDM 121
|
|
| PRK09237 |
PRK09237 |
amidohydrolase/deacetylase family metallohydrolase; |
15-72 |
3.68e-06 |
|
amidohydrolase/deacetylase family metallohydrolase;
Pssm-ID: 236423 [Multi-domain] Cd Length: 380 Bit Score: 49.46 E-value: 3.68e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 568815722 15 LLIKGGRIINDDQSLYA--DVYLEDGLIKQIGENLIVPGGVKTIEANGRMVIPGGIDVNT 72
Cdd:PRK09237 1 LLLRGGRVIDPANGIDGviDIAIEDGKIAAVAGDIDGSQAKKVIDLSGLYVSPGWIDLHV 60
|
|
| PRK09061 |
PRK09061 |
D-glutamate deacylase; Validated |
14-102 |
4.46e-06 |
|
D-glutamate deacylase; Validated
Pssm-ID: 236369 [Multi-domain] Cd Length: 509 Bit Score: 49.31 E-value: 4.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568815722 14 RLLIKGGRIINDDQSLYA--DVYLEDGLIKQIGENLIvpGGVKTIEANGRMVIPGGIDVNtylqkpSQGMTAADDFFQgt 91
Cdd:PRK09061 20 DLVIRNGRVVDPETGLDAvrDVGIKGGKIAAVGTAAI--EGDRTIDATGLVVAPGFIDLH------AHGQSVAAYRMQ-- 89
|
90
....*....|.
gi 568815722 92 raALVGGTTMI 102
Cdd:PRK09061 90 --AFDGVTTAL 98
|
|
| Amidohydro_3 |
pfam07969 |
Amidohydrolase family; |
332-452 |
8.70e-06 |
|
Amidohydrolase family;
Pssm-ID: 400360 [Multi-domain] Cd Length: 464 Bit Score: 48.30 E-value: 8.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568815722 332 CPYSTAQKAVGKDnfTLIPEGVNGIEERMTVvwdkavatgkmdeNQFVAVTSTNAAKIFNLYPRKGRIAVGSDADVVIWD 411
Cdd:pfam07969 373 DPWPRIGAAVMRQ--TAGGGEVLGPDEELSL-------------EEALALYTSGPAKALGLEDRKGTLGVGKDADLVVLD 437
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 568815722 412 PDKLKTITAKSHKSAVEYnifegmechgsplvVISQGKIVF 452
Cdd:pfam07969 438 DDPLTVDPPAIADIRVRL--------------TVVDGRVVY 464
|
|
| PRK08204 |
PRK08204 |
hypothetical protein; Provisional |
13-110 |
1.12e-05 |
|
hypothetical protein; Provisional
Pssm-ID: 181288 [Multi-domain] Cd Length: 449 Bit Score: 48.07 E-value: 1.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568815722 13 DRLLIKGGRIINDDQSL----YADVYLEDGLIKQIGENlIVPGGVKTIEANGRMVIPG------------------GIDV 70
Cdd:PRK08204 2 KRTLIRGGTVLTMDPAIgdlpRGDILIEGDRIAAVAPS-IEAPDAEVVDARGMIVMPGlvdthrhtwqsvlrgigaDWTL 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 568815722 71 NTYLQKPSQGMTAA---DDFFQGTRA----ALVGGTTMIID--HVVPEP 110
Cdd:PRK08204 81 QTYFREIHGNLGPMfrpEDVYIANLLgaleALDAGVTTLLDwsHINNSP 129
|
|
| NagA |
COG1820 |
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism]; |
16-70 |
2.16e-05 |
|
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism];
Pssm-ID: 441425 [Multi-domain] Cd Length: 373 Bit Score: 47.02 E-value: 2.16e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 568815722 16 LIKGGRIINDDQSLY-ADVYLEDGLIKQIGENliVPGGVKTIEANGRMVIPGGIDV 70
Cdd:COG1820 1 AITNARIFTGDGVLEdGALLIEDGRIAAIGPG--AEPDAEVIDLGGGYLAPGFIDL 54
|
|
| Met_dep_hydrolase_C |
cd01309 |
Metallo-dependent hydrolases, subgroup C is part of the superfamily of metallo-dependent ... |
366-438 |
5.03e-05 |
|
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: 45.77 E-value: 5.03e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568815722 366 KAVATGKMDENQFVAVTStNAAKIFNLYPRKGRIAVGSDADVVIWDPDKLKTiTAKshksaVEYNIFEGMECH 438
Cdd:cd01309 294 KAVKYGLSYEEALKAITI-NPAKILGIEDRVGSLEPGKDADLVVWNGDPLEP-TSK-----PEQVYIDGRLVY 359
|
|
| Bact_CD |
cd01293 |
Bacterial cytosine deaminase and related metal-dependent hydrolases. Cytosine deaminases (CDs) ... |
16-76 |
2.46e-04 |
|
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: 43.77 E-value: 2.46e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568815722 16 LIKGGRIINDDQSLYaDVYLEDGLIKQIGENLIVPGGVKTIEANGRMVIPGGIDVNTYLQK 76
Cdd:cd01293 1 LLRNARLADGGTALV-DIAIEDGRIAAIGPALAVPPDAEEVDAKGRLVLPAFVDPHIHLDK 60
|
|
| PRK15446 |
PRK15446 |
phosphonate metabolism protein PhnM; Provisional |
14-72 |
4.56e-04 |
|
phosphonate metabolism protein PhnM; Provisional
Pssm-ID: 237967 [Multi-domain] Cd Length: 383 Bit Score: 42.86 E-value: 4.56e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 568815722 14 RLLIKGGRIINDDQSLYADVYLEDGLIKQIGENLIVPGGvkTIEANGRMVIPGGIDVNT 72
Cdd:PRK15446 3 EMILSNARLVLPDEVVDGSLLIEDGRIAAIDPGASALPG--AIDAEGDYLLPGLVDLHT 59
|
|
| Imidazolone-5PH |
cd01296 |
Imidazolonepropionase/imidazolone-5-propionate hydrolase (Imidazolone-5PH) catalyzes the third ... |
367-411 |
1.84e-03 |
|
Imidazolonepropionase/imidazolone-5-propionate hydrolase (Imidazolone-5PH) catalyzes the third step in the histidine degradation pathway, the hydrolysis of (S)-3-(5-oxo-4,5-dihydro-3H-imidazol-4-yl)propanoate to N-formimidoyl-L-glutamate. In bacteria, the enzyme is part of histidine utilization (hut) operon.
Pssm-ID: 238621 [Multi-domain] Cd Length: 371 Bit Score: 40.70 E-value: 1.84e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 568815722 367 AVATGKMDENQFVAVTSTNAAKIFNLYPRKGRIAVGSDADVVIWD 411
Cdd:cd01296 304 ACRLMRMTPEEALTAATINAAAALGLGETVGSLEVGKQADLVILD 348
|
|
| COG3653 |
COG3653 |
N-acyl-D-aspartate/D-glutamate deacylase [Secondary metabolites biosynthesis, transport and ... |
386-471 |
2.94e-03 |
|
N-acyl-D-aspartate/D-glutamate deacylase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442870 [Multi-domain] Cd Length: 528 Bit Score: 40.54 E-value: 2.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568815722 386 AAKIFNLYPRkGRIAVGSDADVVIWDPDKLK-TITA-KSHKSAveynifEGMEChgsplVVISqGKIVFEDGNINvNKGM 463
Cdd:COG3653 453 PADRLGLKDR-GLLRPGYRADLVVFDPATLAdRATFdLPAQRA------DGIRA-----VIVN-GVVVVEDGKPT-GARP 518
|
....*...
gi 568815722 464 GRFIPRKA 471
Cdd:COG3653 519 GRVLRGGG 526
|
|
| PRK05985 |
PRK05985 |
cytosine deaminase; Provisional |
31-81 |
3.15e-03 |
|
cytosine deaminase; Provisional
Pssm-ID: 180337 [Multi-domain] Cd Length: 391 Bit Score: 39.92 E-value: 3.15e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 568815722 31 ADVYLEDGLIKQIGENLIVPGGVKTIEANGRMVIPGGIDVNTYLQKPSQGM 81
Cdd:PRK05985 17 VDILIRDGRIAAIGPALAAPPGAEVEDGGGALALPGLVDGHIHLDKTFWGD 67
|
|
| Isoaspartyl-dipeptidase |
cd01308 |
Isoaspartyl dipeptidase hydrolyzes the beta-L-isoaspartyl linkages in dipeptides, as part of ... |
381-421 |
3.63e-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: 40.07 E-value: 3.63e-03
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 568815722 381 VTSTNAAKIFNLYPrKGRIAVGSDADVVIWDPD-KLKTITAK 421
Cdd:cd01308 330 VITSNVARILKLRK-KGEIQPGFDADLVILDKDlDINSVIAK 370
|
|
| FMDH_A |
cd01304 |
Formylmethanofuran dehydrogenase (FMDH) subunit A; Methanogenic bacteria and archea derive ... |
17-73 |
5.59e-03 |
|
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: 39.70 E-value: 5.59e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 568815722 17 IKGGRIINDDQSLYA---DVYLEDGlikQIGENLIVPGGVKTIEANGRMVIPGGIDVNTY 73
Cdd:cd01304 1 IKNGTVYDPLNGINGekmDIFIRDG---KIVESSSGAKPAKVIDASGKVVMAGGVDMHSH 57
|
|
| Met_dep_hydrolase_B |
cd01307 |
Metallo-dependent hydrolases, subgroup B is part of the superfamily of metallo-dependent ... |
328-423 |
7.04e-03 |
|
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: 38.85 E-value: 7.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568815722 328 GSGHCPYSTAQKAVGKDnftLIPE----------GVNGIEERMTVVWDKAVATGkMDENQFVAVTSTNAAKIFNLyPRKG 397
Cdd:cd01307 226 GTASFSFRVARAAIAAG---LLPDtissdihgrnRTNGPVYALATTLSKLLALG-MPLEEVIEAVTANPARMLGL-AEIG 300
|
90 100
....*....|....*....|....*.
gi 568815722 398 RIAVGSDADVVIWDPDKLKTITAKSH 423
Cdd:cd01307 301 TLAVGYDADLTVFDLKDGRVELVDSE 326
|
|
| ureB |
PRK13985 |
urease subunit alpha; |
1-99 |
9.77e-03 |
|
urease subunit alpha;
Pssm-ID: 184438 [Multi-domain] Cd Length: 568 Bit Score: 38.72 E-value: 9.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568815722 1 MQKMNNEVVDKSDrLLIKGGRIINDDQSLYADVYLEDGLIKQIG------------ENLIVPGGVKTIEANGRMVIPGGI 68
Cdd:PRK13985 54 MSQSNNPSKEELD-LIITNALIIDYTGIYKADIGIKDGKIAGIGkggnkdmqdgvkNNLSVGPATEALAGEGLIVTAGGI 132
|
90 100 110
....*....|....*....|....*....|.
gi 568815722 69 DVNTYLQKPSQGMTAaddFFQGTRAALVGGT 99
Cdd:PRK13985 133 DTHIHFISPQQIPTA---FASGVTTMIGGGT 160
|
|
| |
