|
Name |
Accession |
Description |
Interval |
E-value |
| D-HYD |
cd01314 |
D-hydantoinases (D-HYD) also called dihydropyrimidases (DHPase) and related proteins; DHPases ... |
17-466 |
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: 734.79 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503051 17 LLIKGGRIINDDQSLYADVYLEDGLIKQIGENLIVPGGVKTIEANGRMVIPGGIDVNTYLQKPSQGMTAADDFFQGTRAA 96
Cdd:cd01314 1 LIIKNGTIVTADGSFKADILIEDGKIVAIGPNLEAPGGVEVIDATGKYVLPGGIDPHTHLELPFMGTVTADDFESGTRAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503051 97 LVGGTTMIIDHVVPEPGSSLLTSFEKWHEAADTKSCCDYSLHVDITSWYDGVREELEVLVqDKGVNSFQVYMAYKDVYQM 176
Cdd:cd01314 81 AAGGTTTIIDFAIPNKGQSLLEAVEKWRGKADGKSVIDYGFHMIITDWTDSVIEELPELV-KKGISSFKVFMAYKGLLMV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503051 177 SDSQLYEAFTFLKGLGAVILVHAENGDLIAQEQKRILEMGITGPEGHALSRPEELEAEAVFRAITIAGRINCPVYITKVM 256
Cdd:cd01314 160 DDEELLDVLKRAKELGALVMVHAENGDVIAELQKKLLAQGKTGPEYHALSRPPEVEAEATARAIRLAELAGAPLYIVHVS 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503051 257 SKSAADIIALARKKGPLVFGEPIAASLGTDGTHYWsKNWAKAAAFVTSPPLSPDpTTPDYLTSLLACGDLQVTGSGHCPY 336
Cdd:cd01314 240 SKEAADEIARARKKGLPVYGETCPQYLLLDDSDYW-KDWFEGAKYVCSPPLRPK-EDQEALWDGLSSGTLQTVGSDHCPF 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503051 337 STAQKAVGKDNFTLIPEGVNGIEERMTVVWDKAVATGKMDENQFVAVTSTNAAKIFNLYPRKGRIAVGSDADVVIWDPDK 416
Cdd:cd01314 318 NFAQKARGKDDFTKIPNGVPGVETRMPLLWSEGVAKGRITLEKFVELTSTNPAKIFGLYPRKGTIAVGSDADLVIWDPNA 397
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 4503051 417 LKTITAKSHKSAVEYNIFEGMECHGSPLVVISQGKIVFEDGNINVNKGMG 466
Cdd:cd01314 398 EKTISADTHHHNVDYNIFEGMKVKGWPVVTISRGKVVVEDGELVGEKGSG 447
|
|
| D-hydantoinase |
TIGR02033 |
D-hydantoinase; This model represents the D-hydantoinase (dihydropyrimidinase) which primarily ... |
17-471 |
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: 664.08 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503051 17 LLIKGGRIINDDQSLYADVYLEDGLIKQIGENLIVPGGVKTIEANGRMVIPGGIDVNTYLQKPSQGMTAADDFFQGTRAA 96
Cdd:TIGR02033 1 LLIKGGTVVNADDVFQADVLIEGGKIVAVGDNLIPPDAVEVIDATGKYVLPGGIDVHTHLEMPFGGTTTADDFFTGTKAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503051 97 LVGGTTMIIDHVVPEPGSSLLTSFEKWHEAADTKSCCDYSLHVDITSWYDGVREELEVLVQDKGVNSFQVYMAYKDVYQM 176
Cdd:TIGR02033 81 AAGGTTTIIDFVVPEKGSSLTEALETWHEKAEGKSVIDYGFHMDITHWNDSVLEEHIPEVKEEGINSFKVFMAYKNLLMV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503051 177 SDSQLYEAFTFLKGLGAVILVHAENGDLIAQEQKRILEMGITGPEGHALSRPEELEAEAVFRAITIAGRINCPVYITKVM 256
Cdd:TIGR02033 161 DDEELFEILKRLKELGALLQVHAENGDIIAELQARMLAQGITGPEYHALSRPPELEAEAVARAITLAALADAPLYVVHVS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503051 257 SKSAADIIALARKKGPLVFGEPIAASLGTDGTHYWsKNWAKAAAFVTSPPLSpDPTTPDYLTSLLACGDLQVTGSGHCPY 336
Cdd:TIGR02033 241 TKDAADEIAQARKKGQPVFGETCPQYLVLDDTHYD-KPGFEGAKYVCSPPLR-EPEDQDALWSALSSGALQTVGSDHCTF 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503051 337 STAQK-AVGKDNFTLIPEGVNGIEERMTVVWDKAVATGKMDENQFVAVTSTNAAKIFNLYPRKGRIAVGSDADVVIWDPD 415
Cdd:TIGR02033 319 NFAQKkAIGKDDFTKIPNGGPGVEERMSLLFDEGVAKGRITLEKFVEVTSTNPAKIFNLYPRKGTIAVGSDADIVIWDPN 398
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 4503051 416 KLKTITAKSHKSAVEYNIFEGMECHGSPLVVISQGKIVFEDGNINVNKGMGRFIPR 471
Cdd:TIGR02033 399 RTTVISAETHHSNADYNPFEGFKVRGAPVSVLSRGRVVVEDGQLVGTAGAGRFVKR 454
|
|
| PRK08323 |
PRK08323 |
phenylhydantoinase; Validated |
16-475 |
0e+00 |
|
phenylhydantoinase; Validated
Pssm-ID: 236240 [Multi-domain] Cd Length: 459 Bit Score: 569.03 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503051 16 RLLIKGGRIINDDQSLYADVYLEDGLIKQIGENlivpGGVKTIEANGRMVIPGGIDVNTYLQKPSQGMTAADDFFQGTRA 95
Cdd:PRK08323 2 STLIKNGTVVTADDTYKADVLIEDGKIAAIGAN----LGDEVIDATGKYVMPGGIDPHTHMEMPFGGTVSSDDFETGTRA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503051 96 ALVGGTTMIIDHVVPEPGSSLLTSFEKWHEAADTKSCCDYSLHVDITSWYDGVREELEVLVqDKGVNSFQVYMAYKDVYQ 175
Cdd:PRK08323 78 AACGGTTTIIDFALQPKGQSLREALEAWHGKAAGKAVIDYGFHMIITDWNEVVLDEMPELV-EEGITSFKLFMAYKGALM 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503051 176 MSDSQLYEAFTFLKGLGAVILVHAENGDLIAQEQKRILEMGITGPEGHALSRPEELEAEAVFRAITIAGRINCPVYITKV 255
Cdd:PRK08323 157 LDDDELLRALQRAAELGALPMVHAENGDAIAYLQAKLLAEGKTGPEYHALSRPPEVEGEATNRAIMLAELAGAPLYIVHV 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503051 256 MSKSAADIIALARKKGPLVFGEPIAASLGTDGTHYWSKNWAKAAAFVTSPPLSPdPTTPDYLTSLLACGDLQVTGSGHCP 335
Cdd:PRK08323 237 SCKEALEAIRRARARGQRVFGETCPQYLLLDESEYDGPDWFEGAKYVMSPPLRD-KEHQDALWRGLQDGDLQVVATDHCP 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503051 336 YSTAQKA-VGKDNFTLIPEGVNGIEERMTVVWDKAVATGKMDENQFVAVTSTNAAKIFNLYPRKGRIAVGSDADVVIWDP 414
Cdd:PRK08323 316 FCFEQKKqLGRGDFTKIPNGTPGVEDRMPLLFSEGVMTGRITLNRFVELTSTNPAKIFGLYPRKGTIAVGADADIVIWDP 395
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 4503051 415 DKLKTITAKSHKSAVEYNIFEGMECHGSPLVVISQGKIVFEDGNINVNKGMGRFIPRKAFP 475
Cdd:PRK08323 396 NATKTISASTLHSNVDYNPYEGFEVTGWPVTTLSRGEVVVEDGEFRGKAGHGRFLKRKPFQ 456
|
|
| PLN02942 |
PLN02942 |
dihydropyrimidinase |
12-475 |
0e+00 |
|
dihydropyrimidinase
Pssm-ID: 178530 Cd Length: 486 Bit Score: 532.11 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503051 12 ITSDRLLIKGGRIINDDQSLYADVYLEDGLIKQIGENLIVPGGVKTIEANGRMVIPGGIDVNTYLQKPSQGMTAADDFFQ 91
Cdd:PLN02942 2 ASSTKILIKGGTVVNAHHQELADVYVEDGIIVAVAPNLKVPDDVRVIDATGKFVMPGGIDPHTHLAMPFMGTETIDDFFS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503051 92 GTRAALVGGTTMIIDHVVPEPGSsLLTSFEKWHEAADtKSCCDYSLHVDITSWYDGVREELEVLVQDKGVNSFQVYMAYK 171
Cdd:PLN02942 82 GQAAALAGGTTMHIDFVIPVNGN-LLAGYEAYEKKAE-KSCMDYGFHMAITKWDDTVSRDMETLVKEKGINSFKFFMAYK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503051 172 DVYQMSDSQLYEAFTFLKGLGAVILVHAENGDLIAQEQKRILEMGITGPEGHALSRPEELEAEAVFRAITIAGRINCPVY 251
Cdd:PLN02942 160 GSLMVTDELLLEGFKRCKSLGALAMVHAENGDAVFEGQKRMIELGITGPEGHALSRPPLLEGEATARAIRLAKFVNTPLY 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503051 252 ITKVMSKSAADIIALARKKGPLVFGEPIAASLGTDGTHYWSKNWAKAAAFVTSPPLSPdPTTPDYLTSLLACGDLQVTGS 331
Cdd:PLN02942 240 VVHVMSIDAMEEIARARKSGQRVIGEPVVSGLVLDDSKLWDPDFTIASKYVMSPPIRP-AGHGKALQAALSSGILQLVGT 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503051 332 GHCPYSTAQKAVGKDNFTLIPEGVNGIEERMTVVWDKAVATGKMDENQFVAVTSTNAAKIFNLYPRKGRIAVGSDADVVI 411
Cdd:PLN02942 319 DHCPFNSTQKAFGKDDFRKIPNGVNGIEERMHLVWDTMVESGQISPTDYVRVTSTECAKIFNIYPRKGAILAGSDADIII 398
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 4503051 412 WDPDKLKTITAKSHKSAVEYNIFEGMECHGSPLVVISQGKIVFEDGNINVNKGMGRFIPRKAFP 475
Cdd:PLN02942 399 LNPNSTFTISAKTHHSRIDTNVYEGRRGKGKVEVTISQGRVVWENGELKVVRGSGRYIEMPPFS 462
|
|
| AllB |
COG0044 |
Dihydroorotase or related cyclic amidohydrolase [Nucleotide transport and metabolism]; ... |
18-471 |
3.20e-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: 374.81 E-value: 3.20e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503051 18 LIKGGRIINDDQSLYADVYLEDGLIKQIGENLIVPGGVKTIEANGRMVIPGGIDVNTYLQKPsqGMTAADDFFQGTRAAL 97
Cdd:COG0044 1 LIKNGRVVDPGGLERADVLIEDGRIAAIGPDLAAPEAAEVIDATGLLVLPGLIDLHVHLREP--GLEHKEDIETGTRAAA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503051 98 VGGTTMIIDHVVPEPGSSLLTSFEKWHEAADTKSCCDYSLHVDITSWYDGVREELEVLVqDKGVNSFQVYMAYKDVYQMS 177
Cdd:COG0044 79 AGGVTTVVDMPNTNPVTDTPEALEFKLARAEEKALVDVGPHGALTKGLGENLAELGALA-EAGAVAFKVFMGSDDGNPVL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503051 178 DSQ-LYEAFTFLKGLGAVILVHAENGDLIAQeqkRILEMGITGPEGHALSRPEELEAEAVFRAITIAGRINCPVYITKVM 256
Cdd:COG0044 158 DDGlLRRALEYAAEFGALVAVHAEDPDLIRG---GVMNEGKTSPRLGLKGRPAEAEEEAVARDIALAEETGARLHIVHVS 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503051 257 SKSAADIIALARKKGPLVFGE--P-----IAASLGTDGTHYwsknwakaaafVTSPPLsPDPTTPDYLTSLLACGDLQVT 329
Cdd:COG0044 235 TAEAVELIREAKARGLPVTAEvcPhhltlTDEDLERYGTNF-----------KVNPPL-RTEEDREALWEGLADGTIDVI 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503051 330 GSGHCPYSTAQKAvgkDNFTLIPEGVNGIEERMTVVWDKAVATGKMDENQFVAVTSTNAAKIFNLyPRKGRIAVGSDADV 409
Cdd:COG0044 303 ATDHAPHTLEEKE---LPFAEAPNGIPGLETALPLLLTELVHKGRLSLERLVELLSTNPARIFGL-PRKGRIAVGADADL 378
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 4503051 410 VIWDPDKLKTITAKSHKSAVEYNIFEGMECHGSPLVVISQGKIVFEDGNInVNKGMGRFIPR 471
Cdd:COG0044 379 VLFDPDAEWTVTAEDLHSKSKNTPFEGRELTGRVVATIVRGRVVYEDGEV-VGEPRGRFLRR 439
|
|
| PRK13404 |
PRK13404 |
dihydropyrimidinase; Provisional |
17-471 |
3.96e-121 |
|
dihydropyrimidinase; Provisional
Pssm-ID: 184033 [Multi-domain] Cd Length: 477 Bit Score: 365.95 E-value: 3.96e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503051 17 LLIKGGRIINDDQSLYADVYLEDGLIKQIGENLivPGGVKTIEANGRMVIPGGIDVNTYLQKPS-QGMTAADDFFQGTRA 95
Cdd:PRK13404 6 LVIRGGTVVTATDTFQADIGIRGGRIAALGEGL--GPGAREIDATGRLVLPGGVDSHCHIDQPSgDGIMMADDFYTGTVS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503051 96 ALVGGTTMIIDHVVPEPGSSLLTSFEKWHEAADTKSCCDYSLHVDITSWYDGV-REELEVLVQDkGVNSFQVYMAYkDVY 174
Cdd:PRK13404 84 AAFGGTTTVIPFAAQHRGQSLREAVEDYHRRAAGKAVIDYAFHLIVADPTEEVlTEELPALIAQ-GYTSFKVFMTY-DDL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503051 175 QMSDSQLYEAFTFLKGLGAVILVHAENGDLIAQEQKRILEMGITGPEGHALSRPEELEAEAVFRAITIAGRINCPVYITK 254
Cdd:PRK13404 162 KLDDRQILDVLAVARRHGAMVMVHAENHDMIAWLTKRLLAAGLTAPKYHAISRPMLAEREATHRAIALAELVDVPILIVH 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503051 255 VMSKSAADIIALARKKGPLVFGEP-------IAASLGTDGTHywsknwakAAAFVTSPPLSpDPTTPDYLTSLLACGDLQ 327
Cdd:PRK13404 242 VSGREAAEQIRRARGRGLKIFAETcpqylflTAEDLDRPGME--------GAKYICSPPPR-DKANQEAIWNGLADGTFE 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503051 328 VTGSGHCPY---STAQKAVGKDN--FTLIPEGVNGIEERMTVVWDKAVATGKMDENQFVAVTSTNAAKIFNLYPRKGRIA 402
Cdd:PRK13404 313 VFSSDHAPFrfdDTDGKLAAGANpsFKAIANGIPGIETRLPLLFSEGVVKGRISLNRFVALTSTNPAKLYGLYPRKGAIA 392
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 4503051 403 VGSDADVVIWDPDKLKTITAKSHKSAVEYNIFEGMECHGSPLVVISQGKIVFEDGNINVNKGMGRFIPR 471
Cdd:PRK13404 393 IGADADIAIWDPDREVTITNADLHHAADYTPYEGMRVTGWPVTVLSRGRVVVEDGELVAERGSGQFLAR 461
|
|
| L-HYD_ALN |
cd01315 |
L-Hydantoinases (L-HYDs) and Allantoinase (ALN); L-Hydantoinases are a member of the ... |
17-457 |
9.87e-69 |
|
L-Hydantoinases (L-HYDs) and Allantoinase (ALN); L-Hydantoinases are a member of the dihydropyrimidinase family, which catalyzes the reversible hydrolytic ring opening of dihydropyrimidines and hydantoins (five-membered cyclic diamides used in biotechnology). But L-HYDs differ by having an L-enantio specificity and by lacking activity on possible natural substrates such as dihydropyrimidines. Allantoinase catalyzes the hydrolytic cleavage of the five-member ring of allantoin (5-ureidohydantoin) to form allantoic acid.
Pssm-ID: 238640 [Multi-domain] Cd Length: 447 Bit Score: 228.71 E-value: 9.87e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503051 17 LLIKGGRIINDDQSLYADVYLEDGLIKQIGENLIVPGGVKTIEANGRMVIPGGIDVNTYLQKPsqGMTAADDFFQGTRAA 96
Cdd:cd01315 2 LVIKNGRVVTPDGVREADIAVKGGKIAAIGPDIANTEAEEVIDAGGLVVMPGLIDTHVHINEP--GRTEWEGFETGTKAA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503051 97 LVGGTTMIIDhvVP---EPGSSLLTSFEKWHEAADTKSccdyslHVDITSWYDGVR---EELEVLVqDKGVNSFQVYMA- 169
Cdd:cd01315 80 AAGGITTIID--MPlnsIPPTTTVENLEAKLEAAQGKL------HVDVGFWGGLVPgnlDQLRPLD-EAGVVGFKCFLCp 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503051 170 --YKDVYQMSDSQLYEAFTFLKGLGAVILVHAENGDLIAQEQKRILEMGITGPEGHALSRPEELEAEAVFRAITIAGRIN 247
Cdd:cd01315 151 sgVDEFPAVDDEQLEEAMKELAKTGSVLAVHAENPEITEALQEQAKAKGKRDYRDYLASRPVFTEVEAIQRILLLAKETG 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503051 248 CPVYITKVMSKSAADIIALARKKGPLVFGEpiaaslgtDGTHYWS-------KNwakAAAFVTSPPLSpDPTTPDYLTSL 320
Cdd:cd01315 231 CRLHIVHLSSAEAVPLIREARAEGVDVTVE--------TCPHYLTftaedvpDG---GTEFKCAPPIR-DAANQEQLWEA 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503051 321 LACGDLQVTGSGHCPYSTAQKAVGKDNFTLIPEGVNGIEERMTVVWDKAVATGKMDENQFVAVTSTNAAKIFNLYPRKGR 400
Cdd:cd01315 299 LENGDIDMVVSDHSPCTPELKLLGKGDFFKAWGGISGLQLGLPVMLTEAVNKRGLSLEDIARLMCENPAKLFGLSHQKGR 378
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 4503051 401 IAVGSDADVVIWDPDKLKTITAKSHKSAVEYNIFEGMECHGSPLVVISQGKIVFEDG 457
Cdd:cd01315 379 IAVGYDADFVVWDPEEEFTVDAEDLYYKNKISPYVGRTLKGRVHATILRGTVVYQDG 435
|
|
| Cyclic_amidohydrolases |
cd01302 |
Cyclic amidohydrolases, including hydantoinase, dihydropyrimidinase, allantoinase, and ... |
65-443 |
1.63e-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: 216.87 E-value: 1.63e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503051 65 VIPGGIDVNTYLQKPSQGMTAaDDFFQGTRAALVGGTTMIIDHVVPEPGSSLLTSFEKWHEAADTKSCCDYSLHVDITSw 144
Cdd:cd01302 3 VLPGFIDIHVHLRDPGGTTYK-EDFESGSRAAAAGGVTTVIDMPNTGPPPIDLPAIELKIKLAEESSYVDFSFHAGIGP- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503051 145 yDGVREELEvLVQDKGVNSFQVYMAYK--DVYQMSDSQLYEAFTFLKGLGAVILVHAEngdliaqeqkrilemgitgpeg 222
Cdd:cd01302 81 -GDVTDELK-KLFDAGINSLKVFMNYYfgELFDVDDGTLMRTFLEIASRGGPVMVHAE---------------------- 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503051 223 halsrpeeleaeavfRAITIAGRINCPVYITKVMSKSAADIIALARKKGPLVFGEPIAASLGTDgTHYWSKNWAKaaaFV 302
Cdd:cd01302 137 ---------------RAAQLAEEAGANVHIAHVSSGEALELIKFAKNKGVKVTCEVCPHHLFLD-ESMLRLNGAW---GK 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503051 303 TSPPLSPdPTTPDYLTSLLACGDLQVTGSGHCPYSTAQKAVGKDnFTLIPEGVNGIEERMTVVWdKAVATGKMDENQFVA 382
Cdd:cd01302 198 VNPPLRS-KEDREALWEGVKNGKIDTIASDHAPHSKEEKESGKD-IWKAPPGFPGLETRLPILL-TEGVKRGLSLETLVE 274
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 4503051 383 VTSTNAAKIFNLYPrKGRIAVGSDADVVIWDPDKLKTITAKSHKSAVEYNIFEGMECHGSP 443
Cdd:cd01302 275 ILSENPARIFGLYP-KGTIAVGYDADLVIVDPKKEWKVTAEEIESKADWTPFEGMEVTGKP 334
|
|
| PRK02382 |
PRK02382 |
dihydroorotase; Provisional |
17-472 |
4.22e-58 |
|
dihydroorotase; Provisional
Pssm-ID: 179417 [Multi-domain] Cd Length: 443 Bit Score: 200.65 E-value: 4.22e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503051 17 LLIKGGRIINDDQSLYADVYLEDGLIKQIGENLIVPGGVKTIEANGRMVIPGGIDVNTYLQKPsqGMTAADDFFQGTRAA 96
Cdd:PRK02382 4 ALLKDGRVYYNNSLQPRDVRIDGGKITAVGKDLDGSSSEEVIDARGMLLLPGGIDVHVHFREP--GYTHKETWYTGSRSA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503051 97 LVGGTTMIIDHVVPEPGSSLLTSFEKWHEAADTKSCCDYSLHvditswyDGVREELEVLVQ--DKGVNSF-QVYMAyKDV 173
Cdd:PRK02382 82 AAGGVTTVVDQPNTDPPTVDGESFDEKAELAARKSIVDFGIN-------GGVTGNWDPLESlwERGVFALgEIFMA-DST 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503051 174 YQMS-DSQLY-EAFTFLKGLGAVILVHAENGDLIAqEQKRILEmGITGPEGHALSRPEELEAEAVFRAITIAGRINCPVY 251
Cdd:PRK02382 154 GGMGiDEELFeEALAEAARLGVLATVHAEDEDLFD-ELAKLLK-GDADADAWSAYRPAAAEAAAVERALEVASETGARIH 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503051 252 ITKVmskSAADIIALARKKGPLVFGEPIAASLGTDgthywskNWAKAAAFV-TSPPLSPDPTTpDYLTSLLACGDLQVTG 330
Cdd:PRK02382 232 IAHI---STPEGVDAARREGITCEVTPHHLFLSRR-------DWERLGTFGkMNPPLRSEKRR-EALWERLNDGTIDVVA 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503051 331 SGHCPYSTAQKAVG-KDnftlIPEGVNGIEERMTVVWdKAVATGKMDENQFVAVTSTNAAKIFNLyPRKGRIAVGSDADV 409
Cdd:PRK02382 301 SDHAPHTREEKDADiWD----APSGVPGVETMLPLLL-AAVRKNRLPLERVRDVTAANPARIFGL-DGKGRIAEGYDADL 374
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 4503051 410 VIWDPDKLKTITAKSHKSAVEYNIFEGMEchGS-PLVVISQGKIVFEDGNINVNKGMGRFIPRK 472
Cdd:PRK02382 375 VLVDPDAAREIRGDDLHSKAGWTPFEGME--GVfPELTMVRGTVVWDGDDINAKRGRGEFLRGR 436
|
|
| allantoinase |
TIGR03178 |
allantoinase; This enzyme carries out the first step in the degradation of allantoin, a ... |
17-470 |
9.27e-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: 194.14 E-value: 9.27e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503051 17 LLIKGGRIINDDQSLYADVYLEDGLIKQIGENlIVPGGVKTIEANGRMVIPGGIDVNTYLQKPsqGMTAADDFFQGTRAA 96
Cdd:TIGR03178 2 LIIRGGRVILPNGEREADVGVKGGKIAAIGPD-ILGPAAKIIDAGGLVVFPGVVDTHVHINEP--GRTEWEGFETGTRAA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503051 97 LVGGTTMIIDhvVP---EPGSSLLTSFEKWHEAADTKsccdysLHVDITSWYDGVREELEVL--VQDKGVNSFQVYMAY- 170
Cdd:TIGR03178 79 AAGGITTYID--MPlnsIPATTTRASLEAKFEAAKGK------LAVDVGFWGGLVPYNLDDLreLDEAGVVGFKAFLSPs 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503051 171 --KDVYQMSDSQLYEAFTFLKGLGAVILVHAENGDLIAQEQKRILEMGITGPEGHALSRPEELEAEAVFRAITIAGRINC 248
Cdd:TIGR03178 151 gdDEFPHVDDWQLYKGMRELARLGQLLLVHAENPAITSALGEEAPPQGGVGADAYLASRPVFAEVEAIRRTLALAKVTGC 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503051 249 PVYITKVMSKSAADIIALARKKGPLVFGEPIaaslgtdgTHYWSKNWAK----AAAFVTSPPLSpDPTTPDYLTSLLACG 324
Cdd:TIGR03178 231 RVHVVHLSSAEAVELITEAKQEGLDVTVETC--------PHYLTLTAEEvpdgGTLAKCAPPIR-DLANQEGLWEALLNG 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503051 325 DLQVTGSGHCPYSTAQKAvgKDNFTLIPEGVNGIEERMTVVWDKAVATGKMDENQFVAVTSTNAAKIFNLyPRKGRIAVG 404
Cdd:TIGR03178 302 LIDCVVSDHSPCTPDLKR--AGDFFKAWGGIAGLQSTLDVMFDEAVQKRGLPLEDIARLMATNPAKRFGL-AQKGRIAPG 378
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 4503051 405 SDADVVIWDPDKLKTITAKSHKSAVEYNIFEGMECHGSPLVVISQGKIVFEDGNInVNKGMGRFIP 470
Cdd:TIGR03178 379 KDADFVFVDPDESYTLTPDDLYYRHKVSPYVGRTIGGRVRATYLRGQCIYDDEQF-IGAPKGQLLL 443
|
|
| PRK06189 |
PRK06189 |
allantoinase; Provisional |
17-460 |
9.90e-50 |
|
allantoinase; Provisional
Pssm-ID: 235732 [Multi-domain] Cd Length: 451 Bit Score: 178.36 E-value: 9.90e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503051 17 LLIKGGRIINDDQSLYADVYLEDGLIKQIGENLIVPGGvKTIEANGRMVIPGGIDVNTYLQKPsqGMTAADDFFQGTRAA 96
Cdd:PRK06189 5 LIIRGGKVVTPEGVYRADIGIKNGKIAEIAPEISSPAR-EIIDADGLYVFPGMIDVHVHFNEP--GRTHWEGFATGSAAL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503051 97 LVGGTTMIIDhvVPEPGS-SLLT--SFEKWHEAADTKSCCDYSLHVDITSwydGVREELEVLVqDKGVNSFQVYMAYK-- 171
Cdd:PRK06189 82 AAGGCTTYFD--MPLNSIpPTVTreALDAKAELARQKSAVDFALWGGLVP---GNLEHLRELA-EAGVIGFKAFMSNSgt 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503051 172 DVYQMSDSQ-LYEAFTFLKGLGAVILVHAENGDLIAQEQKRILEMGITGPEGHALSRPEELEAEAVFRAITIAGRINCPV 250
Cdd:PRK06189 156 DEFRSSDDLtLYEGMKEIAALGKILALHAESDALTRHLTTQARQQGKTDVRDYLESRPVVAELEAVQRALLYAQETGCPL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503051 251 YITKVMSKSAADIIALARKKG--------P--LVFGEPIAASLGTdgthywsknWAKAAafvtsPPLSpDPTTPDYLTSL 320
Cdd:PRK06189 236 HFVHISSGKAVALIAEAKKRGvdvsvetcPhyLLFTEEDFERIGA---------VAKCA-----PPLR-SRSQKEELWRG 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503051 321 LACGDLQVTGSGHCPYSTAQKAvgKDNFTLIPEGVNGIEERMTVVWDKAVATGKMDENQFVAVTSTNAAKIFNLyPRKGR 400
Cdd:PRK06189 301 LLAGEIDMISSDHSPCPPELKE--GDDFFLVWGGISGGQSTLLVMLTEGYIERGIPLETIARLLATNPAKRFGL-PQKGR 377
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503051 401 IAVGSDADVVIWDPDKLKTITAKSHKSAVEYNIFEGMECHGSPLVVISQGKIVFEDGNIN 460
Cdd:PRK06189 378 LEVGADADFVLVDLDETYTLTKEDLFYRHKQSPYEGRTFPGRVVATYLRGQCVYQDGEVF 437
|
|
| DHOase_IIb |
cd01318 |
Dihydroorotase (DHOase), subgroup IIb; DHOases catalyze the reversible interconversion of ... |
62-450 |
1.72e-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: 153.26 E-value: 1.72e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503051 62 GRMVIPGGIDVNTYLQKPsqGMTAADDFFQGTRAALVGGTTMIIDHVVPEPGSSLLTSFEKWHEAADTKSCCDYSLHVDI 141
Cdd:cd01318 1 GLLILPGVIDIHVHFREP--GLTYKEDFVSGSRAAAAGGVTTVMDMPNTKPPTTTAEALYEKLRLAAAKSVVDYGLYFGV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503051 142 TSWYDGvrEELEVLvqdkGVNSFQVYMAyKDVYQMSD--SQLYEAFtflKGLGAVILVHAENGDLIAQEQKRILEMGItg 219
Cdd:cd01318 79 TGSEDL--EELDKA----PPAGYKIFMG-DSTGDLLDdeETLERIF---AEGSVLVTFHAEDEDRLRENRKELKGESA-- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503051 220 pegHALSRPEELEAEAVFRAITIAGRINCPVYITKVmskSAADIIALARKKGP----------LVFGEPIAASLGTdgth 289
Cdd:cd01318 147 ---HPRIRDAEAAAVATARALKLARRHGARLHICHV---STPEELKLIKKAKPgvtvevtphhLFLDVEDYDRLGT---- 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503051 290 ywsknWAKaaafvTSPPLSpDPTTPDYLTSLLACGDLQVTGSGHCPYSTAQKAVGKDNftlIPEGVNGIEERMTVVWDkA 369
Cdd:cd01318 217 -----LGK-----VNPPLR-SREDRKALLQALADGRIDVIASDHAPHTLEEKRKGYPA---APSGIPGVETALPLMLT-L 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503051 370 VATGKMDENQFVAVTSTNAAKIFNLyPRKGRIAVGSDADVVIWDPDKLKTITAKSHKSAVEYNIFEGMECHGSPLVVISQ 449
Cdd:cd01318 282 VNKGILSLSRVVRLTSHNPARIFGI-KNKGRIAEGYDADLTVVDLKEERTIRAEEFHSKAGWTPFEGFEVTGFPVMTIVR 360
|
.
gi 4503051 450 G 450
Cdd:cd01318 361 G 361
|
|
| pyrC |
PRK09357 |
dihydroorotase; Validated |
16-456 |
9.11e-38 |
|
dihydroorotase; Validated
Pssm-ID: 236479 [Multi-domain] Cd Length: 423 Bit Score: 144.57 E-value: 9.11e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503051 16 RLLIKGGRIINDDQSLY-ADVYLEDGLIKQIGENLIVPGgVKTIEANGRMVIPGGIDVNTYLQKPsqGMTAADDFFQGTR 94
Cdd:PRK09357 2 MILIKNGRVIDPKGLDEvADVLIDDGKIAAIGENIEAEG-AEVIDATGLVVAPGLVDLHVHLREP--GQEDKETIETGSR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503051 95 AALVGGTTMiidhVVPEPG-----SSLLTSFEKWHEAADTKSCcdyslHVD----ITswydgVREELEVLVQDKGVNSFQ 165
Cdd:PRK09357 79 AAAAGGFTT----VVAMPNtkpviDTPEVVEYVLDRAKEAGLV-----DVLpvgaIT-----KGLAGEELTEFGALKEAG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503051 166 VYMAYKDVYQMSDSQL-YEAFTFLKGLGAVILVHAE----NGDLIAQEQKRILEMGITGpeghalsRPEELEAEAVFRAI 240
Cdd:PRK09357 145 VVAFSDDGIPVQDARLmRRALEYAKALDLLIAQHCEdpslTEGGVMNEGEVSARLGLPG-------IPAVAEEVMIARDV 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503051 241 TIAGRINCPVYITKVMSKSAADIIALARKKGPlvfgePIAA------------SLGTDGTHYwsknwaKAAafvtsPPLS 308
Cdd:PRK09357 218 LLAEATGARVHICHVSTAGSVELIRWAKALGI-----KVTAevtphhllltdeDLLTYDPNY------KVN-----PPLR 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503051 309 pDPTTPDYLTSLLACGDLQVTGSGHCPYSTAQKAVGkdnFTLIPEGVNGIEERMTVVWDKAVATGKMDENQFVAVTSTNA 388
Cdd:PRK09357 282 -TEEDREALIEGLKDGTIDAIATDHAPHAREEKECE---FEAAPFGITGLETALSLLYTTLVKTGLLDLEQLLEKMTINP 357
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 4503051 389 AKIFNLYPrkGRIAVGSDADVVIWDPDKLKTITAKSHKSAVEYNIFEGMECHGSPLVVISQGKIVFED 456
Cdd:PRK09357 358 ARILGLPA--GPLAEGEPADLVIFDPEAEWTVDGEDFASKGKNTPFIGMKLKGKVVYTIVDGKIVYQD 423
|
|
| PRK07575 |
PRK07575 |
dihydroorotase; Provisional |
14-460 |
1.49e-34 |
|
dihydroorotase; Provisional
Pssm-ID: 236055 [Multi-domain] Cd Length: 438 Bit Score: 135.57 E-value: 1.49e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503051 14 SDRLLIKGGRIINDDQSLY-ADVYLEDGLIKQIGENLIVPGGVKTIEANGRMVIPGGIDVNTYLQKPsqGMTAADDFFQG 92
Cdd:PRK07575 2 MMSLLIRNARILLPSGELLlGDVLVEDGKIVAIAPEISATAVDTVIDAEGLTLLPGVIDPQVHFREP--GLEHKEDLFTA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503051 93 TRAALVGGTTMIIDHVVPEPgssLLTSFEKWHEA---ADTKSCCDYSLHVDITSwydgvrEELEVLVQDKGVNSFQVYMA 169
Cdd:PRK07575 80 SRACAKGGVTSFLEMPNTKP---LTTTQAALDDKlarAAEKCVVNYGFFIGATP------DNLPELLTANPTCGIKIFMG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503051 170 YKDVYQMSDSQLYEAFTFLKGlGAVILVHAENgdliaqeQKRILE-----MGITGPEGHALSRPEELEAEAVFRAITIAG 244
Cdd:PRK07575 151 SSHGPLLVDEEAALERIFAEG-TRLIAVHAED-------QARIRArraefAGISDPADHSQIQDEEAALLATRLALKLSK 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503051 245 RINCPVYITKVmsKSAADIIALARKKGPLVFGE--PIAASLGTDgthywskNWAKAAAFV-TSPPLSpDPTTPDYLTSLL 321
Cdd:PRK07575 223 KYQRRLHILHL--STAIEAELLRQDKPSWVTAEvtPQHLLLNTD-------AYERIGTLAqMNPPLR-SPEDNEALWQAL 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503051 322 ACGDLQVTGSGHCPYSTAQKAVGKDNftlIPEGVNGIEERMTVVWDKAVAtGKMDENQFVAVTSTNAAKIFNLyPRKGRI 401
Cdd:PRK07575 293 RDGVIDFIATDHAPHTLEEKAQPYPN---SPSGMPGVETSLPLMLTAAMR-GKCTVAQVVRWMSTAVARAYGI-PNKGRI 367
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 4503051 402 AVGSDADVVIWDPDKLKTITAKSHKSAVEYNIFEGMECHGSPLVVISQGKIVFEDGNIN 460
Cdd:PRK07575 368 APGYDADLVLVDLNTYRPVRREELLTKCGWSPFEGWNLTGWPVTTIVGGQIVFDRGQVN 426
|
|
| PRK08044 |
PRK08044 |
allantoinase AllB; |
17-415 |
6.33e-34 |
|
allantoinase AllB;
Pssm-ID: 169193 [Multi-domain] Cd Length: 449 Bit Score: 134.21 E-value: 6.33e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503051 17 LLIKGGRIINDDQSLYADVYLEDGLIKQIGENLivPGGVKTIEANGRMVIPGGIDVNTYLQKPsqGMTAADDFFQGTRAA 96
Cdd:PRK08044 5 LIIKNGTVILENEARVVDIAVKGGKIAAIGQDL--GDAKEVMDASGLVVSPGMVDAHTHISEP--GRSHWEGYETGTRAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503051 97 LVGGTTMIIDHVVPE-PGSSLLTSFEKWHEAADTKSCCDYSLHVDITSW-YDGVREELEVlvqdkGVNSFQVYMAY---- 170
Cdd:PRK08044 81 AKGGITTMIEMPLNQlPATVDRASIELKFDAAKGKLTIDAAQLGGLVSYnLDRLHELDEV-----GVVGFKCFVATcgdr 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503051 171 ---KDVYQMSDSQLYEAFTFLKGLGAVILVHAENG---DLIAQEQKRileMGITGPEGHALSRPEELEAEAVFRAITIAG 244
Cdd:PRK08044 156 gidNDFRDVNDWQFYKGAQKLGELGQPVLVHCENAlicDELGEEAKR---EGRVTAHDYVASRPVFTEVEAIRRVLYLAK 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503051 245 RINCPVYITKVMSKSAADIIALARKKGPLVFGEPIaaslgtdgTHYWSKNWAKAAAFVT----SPPLSpDPTTPDYLTSL 320
Cdd:PRK08044 233 VAGCRLHVCHISSPEGVEEVTRARQEGQDVTCESC--------PHYFVLDTDQFEEIGTlakcSPPIR-DLENQKGMWEK 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503051 321 LACGDLQVTGSGHCPYSTAQKAvgkDNFTLIPEGVNGIEERMTVVWDKAVATGKMDENQFVAVTSTNAAKIFNLyPRKGR 400
Cdd:PRK08044 304 LFNGEIDCLVSDHSPCPPEMKA---GNIMEAWGGIAGLQNCMDVMFDEAVQKRGMSLPMFGKLMATNAADIFGL-QQKGR 379
|
410
....*....|....*
gi 4503051 401 IAVGSDADVVIWDPD 415
Cdd:PRK08044 380 IAPGKDADFVFIQPN 394
|
|
| DHOase_IIa |
cd01317 |
Dihydroorotase (DHOase), subgroup IIa; DHOases catalyze the reversible interconversion of ... |
54-444 |
4.54e-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: 4.54e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503051 54 GVKTIEANGRMVIPGGIDVNTYLQKPSQgmTAADDFFQGTRAALVGGTTMII--DHVVPEPGSSLLTSFEKwHEAADTKS 131
Cdd:cd01317 1 DAEVIDAEGKILAPGLVDLHVHLREPGF--EYKETLESGAKAAAAGGFTTVVcmPNTNPVIDNPAVVELLK-NRAKDVGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503051 132 CCDYSLhVDITSWYDGVR-EELEVLVqDKGVNSFQvymayKDVYQMSDSQ-LYEAFTFLKGLGAVILVHAENGDL----I 205
Cdd:cd01317 78 VRVLPI-GALTKGLKGEElTEIGELL-EAGAVGFS-----DDGKPIQDAElLRRALEYAAMLDLPIIVHPEDPSLagggV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503051 206 AQEQKRILEMGITGpeghalsRPEELEAEAVFRAITIAGRINCPVYITKVMSKSAADIIALARKKGPLVFGEPIAASL-- 283
Cdd:cd01317 151 MNEGKVASRLGLPG-------IPPEAETIMVARDLELAEATGARVHFQHLSTARSLELIRKAKAKGLPVTAEVTPHHLll 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503051 284 -GTDGTHYwsknwakAAAFVTSPPLSpDPTTPDYLTSLLACGDLQVTGSGHCPYSTAQKAVGkdnFTLIPEGVNGIEERM 362
Cdd:cd01317 224 dDEALESY-------DTNAKVNPPLR-SEEDREALIEALKDGTIDAIASDHAPHTDEEKDLP---FAEAPPGIIGLETAL 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503051 363 TVVWDKAVATGKMDENQFVAVTSTNAAKIFNLYPrkGRIAVGSDADVVIWDPDKLKTITAKSHKSAVEYNIFEGMECHGS 442
Cdd:cd01317 293 PLLWTLLVKGGLLTLPDLIRALSTNPAKILGLPP--GRLEVGAPADLVLFDPDAEWIVDEETFRSKSKNTPFDGQKLKGR 370
|
..
gi 4503051 443 PL 444
Cdd:cd01317 371 VL 372
|
|
| PLN02795 |
PLN02795 |
allantoinase |
5-460 |
2.70e-28 |
|
allantoinase
Pssm-ID: 178392 [Multi-domain] Cd Length: 505 Bit Score: 118.34 E-value: 2.70e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503051 5 GKKSIPH--ITSDRLLIKGGRIINDdqslyadVYLEDGLIKQIGENLIVPG---GVKTIEANGRMVIPGGIDVNTYLQKP 79
Cdd:PLN02795 39 SLLPWPHfvLYSKRVVTPAGVIPGA-------VEVEGGRIVSVTKEEEAPKsqkKPHVLDYGNAVVMPGLIDVHVHLNEP 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503051 80 sqGMTAADDFFQGTRAALVGGTTMIIDhvVP---EPGSSLLTSFEKWHEAADTKsccdysLHVDITSWYDGVRE------ 150
Cdd:PLN02795 112 --GRTEWEGFPTGTKAAAAGGITTLVD--MPlnsFPSTTSVETLELKIEAAKGK------LYVDVGFWGGLVPEnahnas 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503051 151 ELEVLVqDKGVNSFQVYM---AYKDVYQMSDSQLYEAFTFLKGLGAVILVHAENGDLIAQEQKriLEMGITGPEGHALSR 227
Cdd:PLN02795 182 VLEELL-DAGALGLKSFMcpsGINDFPMTTATHIKAALPVLAKYGRPLLVHAEVVSPVESDSR--LDADPRSYSTYLKSR 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503051 228 PEELEAEAVFRAITIAGRIN-------CPVYITKVM-SKSAADIIALARKKGPLVFGEPIAaslgtdgtHYWsknwAKAA 299
Cdd:PLN02795 259 PPSWEQEAIRQLLEVAKDTRpggvaegAHVHIVHLSdAESSLELIKEAKAKGDSVTVETCP--------HYL----AFSA 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503051 300 A--------FVTSPPLSpDPTTPDYLTSLLACGDLQVTGSGHCPYSTAQKAVGKDNFTLIPEGVNGIEERMTVVWDKAVA 371
Cdd:PLN02795 327 EeipdgdtrYKCAPPIR-DAANRELLWKALLDGDIDMLSSDHSPSPPDLKLLEEGNFLRAWGGISSLQFVLPATWTAGRA 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503051 372 TGkMDENQFVAVTSTNAAKIFNLyPRKGRIAVGSDADVVIWDP------DKLKTITAKsHKSAVEYnifEGMECHGSPLV 445
Cdd:PLN02795 406 YG-LTLEQLARWWSERPAKLAGL-DSKGAIAPGKDADIVVWDPeaefvlDESYPIYHK-HKSLSPY---LGTKLSGKVIA 479
|
490
....*....|....*
gi 4503051 446 VISQGKIVFEDGNIN 460
Cdd:PLN02795 480 TFVRGNLVFLEGKHA 494
|
|
| PRK04250 |
PRK04250 |
dihydroorotase; Provisional |
22-469 |
9.45e-26 |
|
dihydroorotase; Provisional
Pssm-ID: 235265 [Multi-domain] Cd Length: 398 Bit Score: 109.47 E-value: 9.45e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503051 22 GRIINDDQSLYADVYLEDGLIKQIGENLIvpGGVKTIEANGRMVIPGGIDVNTYLQkpsqgmtaadDFFQ--------GT 93
Cdd:PRK04250 4 GKFLLKGRIVEGGIGIENGRISKISLRDL--KGKEVIKVKGGIILPGLIDVHVHLR----------DFEEsyketiesGT 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503051 94 RAALVGGTTMIIDHVVPEPGSSLLTSFEKWHEAADTKSCCDYSLHVDITSWYDGVREELEvlvqdkgvNSFQVYM--AYK 171
Cdd:PRK04250 72 KAALHGGITLVFDMPNTKPPIMDEKTYEKRMRIAEKKSYADYALNFLIAGNCEKAEEIKA--------DFYKIFMgaSTG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503051 172 DVYQMSDSQLYEAftflkgLGAVILVHAENGDLIAQEqkrilemgitgPEghalsRPEELEAEAVFRAITIAGRINCPVY 251
Cdd:PRK04250 144 GIFSENFEVDYAC------APGIVSVHAEDPELIREF-----------PE-----RPPEAEVVAIERALEAGKKLKKPLH 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503051 252 ITKVMSKSAADIIalARKKGPLVFGEPIAASLgtdgtHYWSKNWAKAAAFVTSPPLSpdpTTPDYLTSLLACGDLQVTGS 331
Cdd:PRK04250 202 ICHISTKDGLKLI--LKSNLPWVSFEVTPHHL-----FLTRKDYERNPLLKVYPPLR---SEEDRKALWENFSKIPIIAS 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503051 332 GHCPYSTAQKAVGKdnftlipEGVNGIEERMTVVWDkAVATGKMDENQFVAVTSTNAAKIFNlYPRKGrIAVGSDADVVI 411
Cdd:PRK04250 272 DHAPHTLEDKEAGA-------AGIPGLETEVPLLLD-AANKGMISLFDIVEKMHDNPARIFG-IKNYG-IEEGNYANFAV 341
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 4503051 412 WDPDKLKTITAKSHKSAVEYNIFEGMECHGSPLVVISQGKIVFEDGNInVNKGMGRFI 469
Cdd:PRK04250 342 FDMKKEWTIKAEELYTKAGWTPYEGFKLKGKVIMTILRGEVVMEDDEI-IGKPRGVRI 398
|
|
| PRK01211 |
PRK01211 |
dihydroorotase; Provisional |
32-471 |
9.74e-25 |
|
dihydroorotase; Provisional
Pssm-ID: 179247 [Multi-domain] Cd Length: 409 Bit Score: 106.87 E-value: 9.74e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503051 32 YADVYLEDGLIKQIGENLivpGGVKTIEANGrMVIPGGIDVNTYLQKPsqGMTAADDFFQGTRAALVGGTTMIIDHVVPE 111
Cdd:PRK01211 15 YLEIEVEDGKIKSIKKDA---GNIGKKELKG-AILPAATDIHVHFRTP--GETEKEDFSTGTLSAIFGGTTFIMDMPNNN 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503051 112 PGSSLLTSFEKWHEAADTKSCCDYSLHVDITSwydgvreeLEVLVQDKGVNSFQVYMAYKDVYQMSDSQLYEAfTFLKGL 191
Cdd:PRK01211 89 IPIKDYNAFSDKLGRVAPKAYVDFSLYSMETG--------NNALILDERSIGLKVYMGGTTNTNGTDIEGGEI-KKINEA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503051 192 GAVILVHAENGDLIAQ---EQKRILEmgitgpegHALSRPEELEAEAVfraitiaGRINCPVYITKVMS-KSAADIIA-L 266
Cdd:PRK01211 160 NIPVFFHAELSECLRKhqfESKNLRD--------HDLARPIECEIKAV-------KYVKNLDLKTKIIAhVSSIDVIGrF 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503051 267 ARKKGP--LVFGEPIaaSLGTDGThywsknwakaaafvTSPPLSPDPTTPDYLTSLLAcGDLQVTGSGHCPYSTAQKAvg 344
Cdd:PRK01211 225 LREVTPhhLLLNDDM--PLGSYGK--------------VNPPLRDRWTQERLLEEYIS-GRFDILSSDHAPHTEEDKQ-- 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503051 345 kdNFTLIPEGVNGIEERMTVVWdKAVATGKMDENQFVAVTSTNAAKIFNLypRKGRIAVGSDADVVIWDPDKLKTITAKS 424
Cdd:PRK01211 286 --EFEYAKSGIIGVETRVPLFL-ALVKKKILPLDVLYKTAIERPASLFGI--KKGKIEEGYDADFMAFDFTNIKKINDKR 360
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 4503051 425 HKSAVEYNIFEGMECHgSPLVVISQGKIVFEDGNInVNKGMGRFIPR 471
Cdd:PRK01211 361 LHSKCPVSPFNGFDAI-FPSHVIMRGEVVIDNYEL-ISERTGKFVPK 405
|
|
| PRK09060 |
PRK09060 |
dihydroorotase; Validated |
17-467 |
5.84e-24 |
|
dihydroorotase; Validated
Pssm-ID: 181632 [Multi-domain] Cd Length: 444 Bit Score: 104.62 E-value: 5.84e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503051 17 LLIKGGRIINDDQSLYADVYLEDGLIKQIGENLIVPGGvKTIEANGRMVIPGGIDVNTYLQKPsqGMTAADDFFQGTRAA 96
Cdd:PRK09060 7 LILKGGTVVNPDGEGRADIGIRDGRIAAIGDLSGASAG-EVIDCRGLHVLPGVIDSQVHFREP--GLEHKEDLETGSRAA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503051 97 LVGGTTMIIDHVVPEPGSSLLTSFEKWHEAADTKSCCDYSLHVDITSwyDGVRE--ELEVLvqdKGVNSFQVYM--AYKD 172
Cdd:PRK09060 84 VLGGVTAVFEMPNTNPLTTTAEALADKLARARHRMHCDFAFYVGGTR--DNADElaELERL---PGCAGIKVFMgsSTGD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503051 173 VYQMSDSQLYEAftfLKGLGAVILVHAENgDLIAQEQKRILEMGitGPEGHALSRPEELEAEAVFRAITIAGRINCPVYI 252
Cdd:PRK09060 159 LLVEDDEGLRRI---LRNGRRRAAFHSED-EYRLRERKGLRVEG--DPSSHPVWRDEEAALLATRRLVRLARETGRRIHV 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503051 253 TKVmskSAADIIA-LARKKG-------P--LVFGEPIA-ASLGTdgthYWSKNwakaaafvtsPPLSpDPTTPDYLTSLL 321
Cdd:PRK09060 233 LHV---STAEEIDfLADHKDvatvevtPhhLTLAAPECyERLGT----LAQMN----------PPIR-DARHRDGLWRGV 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503051 322 ACGDLQVTGSGHCPYSTAQKAvgkDNFTLIPEGVNGIEERMTVVWDKaVATGKMDENQFVAVTSTNAAKIFNLyPRKGRI 401
Cdd:PRK09060 295 RQGVVDVLGSDHAPHTLEEKA---KPYPASPSGMTGVQTLVPIMLDH-VNAGRLSLERFVDLTSAGPARIFGI-AGKGRI 369
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 4503051 402 AVGSDADVVIWDPDKLKTITAKSHKSAVEYNIFEGMECHGSPLVVISQGKIVFEDGNInVNKGMGR 467
Cdd:PRK09060 370 AVGYDADFTIVDLKRRETITNEWIASRCGWTPYDGKEVTGWPVGTIVRGQRVMWDGEL-VGPPTGE 434
|
|
| Amidohydro_1 |
pfam01979 |
Amidohydrolase family; This family of enzymes are a a large metal dependent hydrolase ... |
64-453 |
4.49e-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: 4.49e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503051 64 MVIPGGIDVNTYLQ------KPSQGMTAADDFFQGTRAALVGGTTMIIDHvvpepGSSLLTSFEKWHEAAD--------- 128
Cdd:pfam01979 1 IVLPGLIDAHVHLEmgllrgIPVPPEFAYEALRLGITTMLKSGTTTVLDM-----GATTSTGIEALLEAAEelplglrfl 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503051 129 TKSCC---DYSLHVDITSWyDGVREELEVLVQDKGVNsFQVYMAYKDVYQMSDSQLYEAFTFLKGLGAVILVHAENGDLI 205
Cdd:pfam01979 76 GPGCSldtDGELEGRKALR-EKLKAGAEFIKGMADGV-VFVGLAPHGAPTFSDDELKAALEEAKKYGLPVAIHALETKGE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503051 206 AQEQKRIlemgitgpeghalsrpeeleaeavfraitIAGRINCPVYITKVMSKSAADIIALARKkgplvfgepiaaslgt 285
Cdd:pfam01979 154 VEDAIAA-----------------------------FGGGIEHGTHLEVAESGGLLDIIKLILA---------------- 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503051 286 DGTHYWSKNWAKAAAFVTSPPLSPDPTTPDYLTS-------LLACGDLQVTGSGHCpystaqkaVGKDNFTLIPEGVNGI 358
Cdd:pfam01979 189 HGVHLSPTEANLLAEHLKGAGVAHCPFSNSKLRSgrialrkALEDGVKVGLGTDGA--------GSGNSLNMLEELRLAL 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503051 359 EERmtvvwdkAVATGKMDENQFVAVTSTNAAKIFNLYPRKGRIAVGSDADVVIWDPDKLktitakshksaveyNIFEGME 438
Cdd:pfam01979 261 ELQ-------FDPEGGLSPLEALRMATINPAKALGLDDKVGSIEVGKDADLVVVDLDPL--------------AAFFGLK 319
|
410
....*....|....*
gi 4503051 439 CHGSPLVVISQGKIV 453
Cdd:pfam01979 320 PDGNVKKVIVKGKIV 334
|
|
| PRK09236 |
PRK09236 |
dihydroorotase; Reviewed |
15-460 |
6.47e-17 |
|
dihydroorotase; Reviewed
Pssm-ID: 181716 Cd Length: 444 Bit Score: 83.38 E-value: 6.47e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503051 15 DRLLIKGGRIINDDQSLYADVYLEDGLIKQIGENLIVPGGVKTIEANGRMVIPGGIDVNTYLQKPsqGMTAADDFFQGTR 94
Cdd:PRK09236 2 KRILIKNARIVNEGKIFEGDVLIENGRIAKIASSISAKSADTVIDAAGRYLLPGMIDDQVHFREP--GLTHKGDIASESR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503051 95 AALVGGTTMIID--HVVPePGSSLLTSFEKWHEAAdTKSCCDYSLHVDITSwyDGVrEELEVLvqDK----GVNSFqvym 168
Cdd:PRK09236 80 AAVAGGITSFMEmpNTNP-PTTTLEALEAKYQIAA-QRSLANYSFYFGATN--DNL-DEIKRL--DPkrvcGVKVF---- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503051 169 aykdvyqMSDS---QLYEAFTFLKGLGA----VILVHAENGDLI-AQEQKRILEMG--ITgPEGHALSRpeelEAEAVFR 238
Cdd:PRK09236 149 -------MGAStgnMLVDNPETLERIFRdaptLIATHCEDTPTIkANLAKYKEKYGddIP-AEMHPLIR----SAEACYK 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503051 239 ----AITIAGRINcpvyiTK--VMSKSAADIIALARkKGPLVfGEPIAASLGTDGTHYWSKNWAKAAAFVTSPPLSPDPT 312
Cdd:PRK09236 217 ssslAVSLAKKHG-----TRlhVLHISTAKELSLFE-NGPLA-EKRITAEVCVHHLWFDDSDYARLGNLIKCNPAIKTAS 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503051 313 TPDYLTSLLACGDLQVTGSGHCPYSTAQKAVGkdnFTLIPEGVNGIEERMTVVWDKaVATGKMDENQFVAVTSTNAAKIF 392
Cdd:PRK09236 290 DREALRQALADDRIDVIATDHAPHTWEEKQGP---YFQAPSGLPLVQHALPALLEL-VHEGKLSLEKVVEKTSHAPAILF 365
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 4503051 393 NLyPRKGRIAVGSDADVVIWDPDKLKTITAKSHKSAVEYNIFEGMECHGSPLVVISQGKIVFEDGNIN 460
Cdd:PRK09236 366 DI-KERGFIREGYWADLVLVDLNSPWTVTKENILYKCGWSPFEGRTFRSRVATTFVNGQLVYHNGQLV 432
|
|
| CAD_DHOase |
cd01316 |
The eukaryotic CAD protein is a trifunctional enzyme of carbamoylphosphate ... |
66-466 |
1.40e-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: 1.40e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503051 66 IPGGIDVNTYLQKPsqGMTAADDFFQGTRAALVGGTTMIidHVVPEPGSSLL--TSFEKWHEAADTKSCCDYSLHVDITS 143
Cdd:cd01316 5 LPGLIDVHVHLREP--GATHKEDFASGTKAALAGGFTMV--RAMPNTNPSIVdvASLKLVQSLAQAKARCDYAFSIGATS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503051 144 WYDGVREELevlvQDKGVNSFQVYMAYKDVYQMSD-SQLYEAFTFLKGLGAVIlVHAENGDLIAqeqkrILEMgitgpeG 222
Cdd:cd01316 81 TNAATVGEL----ASEAVGLKFYLNETFSTLILDKiTAWASHFNAWPSTKPIV-THAKSQTLAA-----VLLL------A 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503051 223 HALSRpeeleaeavfraitiagrincPVYITKVMSKSAADIIALARKKGPLVFGEPIAASLgtdgthYWSKNWAKAAAFV 302
Cdd:cd01316 145 SLHNR---------------------SIHICHVSSKEEINLIRLAKARGLKVTCEVSPHHL------FLSQDDLPRGQYE 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503051 303 TSPPLsPDPTTPDYLTSLLACGDlqVTGSGHCPYSTAQKAVGKdnftlIPEGVNGIEERMTVVWdKAVATGKMDENQFVA 382
Cdd:cd01316 198 VRPFL-PTREDQEALWENLDYID--CFATDHAPHTLAEKTGNK-----PPPGFPGVETSLPLLL-TAVHEGRLTIEDIVD 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503051 383 VTSTNAAKIFNLYPrkgriavgsDADVVI-WDPDKLKTITAKSHKSAVEYNIFEGMECHGSPLVVISQGKIVFEDGNINV 461
Cdd:cd01316 269 RLHTNPKRIFNLPP---------QSDTYVeVDLDEEWTIPKNPLQSKKGWTPFEGKKVKGKVQRVVLRGETAFIDGEIVA 339
|
....*
gi 4503051 462 NKGMG 466
Cdd:cd01316 340 PPGFG 344
|
|
| pyrC |
PRK00369 |
dihydroorotase; Provisional |
34-473 |
8.12e-14 |
|
dihydroorotase; Provisional
Pssm-ID: 234738 [Multi-domain] Cd Length: 392 Bit Score: 73.26 E-value: 8.12e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503051 34 DVYLEDGlIKQIGENLIVpgGVKTIEANGR---------MVIPGGIDVNTYLQkpsqGMTAA--DDFFQGTRAALVGGTT 102
Cdd:PRK00369 8 KAYLGKE-IKEICINFDR--RIKEIKSRCKpdldlpqgtLILPGAIDLHVHLR----GLKLSykEDVASGTSEAAYGGVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503051 103 MIID--HVVPePGSSLLTSFEKWHEAADtKSCCDYSLhvditswYDGVREELEVLvqDK-GVNSFQVYMaykdvyqmSDS 179
Cdd:PRK00369 81 LVADmpNTIP-PLNTPEAITEKLAELEY-YSRVDYFV-------YSGVTKDPEKV--DKlPIAGYKIFP--------EDL 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503051 180 QLYEAFTFLKGLGAVILVHAENGDLIAQEQKrilemgitgpeghaLSRPEELEAEAVFraiTIAGRINcpVYITKVmskS 259
Cdd:PRK00369 142 EREETFRVLLKSRKLKILHPEVPLALKSNRK--------------LRRNCWYEIAALY---YVKDYQN--VHITHA---S 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503051 260 AADIIALARKKGplvfgepiaasLGTDGT-HYWSKNWAKAAAFVTSPPLSpDPTTPDYLTSLLACGDLQVtgSGHCPYST 338
Cdd:PRK00369 200 NPRTVRLAKELG-----------FTVDITpHHLLVNGEKDCLTKVNPPIR-DINERLWLLQALSEVDAIA--SDHAPHSS 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503051 339 AQKavgKDNFTLIPEGVNGIEERMTVVWdKAVATGKMDENQFVAVTSTNAAKIFNLypRKGRIAVGSDADVVI--WDPDK 416
Cdd:PRK00369 266 FEK---LQPYEVCPPGIAALSFTPPFIY-TLVSKGILSIDRAVELISTNPARILGI--PYGEIKEGYRANFTViqFEDWR 339
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 4503051 417 LKTITAKshksaVEYNIFEGMECHGSPLVVISQGKIVFEDGNINVNKGMGRFIPRKA 473
Cdd:PRK00369 340 YSTKYSK-----VIETPLDGFELKASVYATIVQGKLAYLEGEVFPVKGINPFGERKR 391
|
|
| HutI |
COG1228 |
Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport ... |
13-456 |
7.64e-11 |
|
Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440841 [Multi-domain] Cd Length: 386 Bit Score: 64.21 E-value: 7.64e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503051 13 TSDRLLIKGGRIIN-DDQSLY--ADVYLEDGLIKQIGEN--LIVPGGVKTIEANGRMVIPGGIDVNTYL---------QK 78
Cdd:COG1228 6 QAGTLLITNATLVDgTGGGVIenGTVLVEDGKIAAVGPAadLAVPAGAEVIDATGKTVLPGLIDAHTHLglgggraveFE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503051 79 PSQGMTAADDFFQGT----RAALVGGTTMIIDHvvpePGSSL----------LTSFEKWH-EAADTKSCCDYSLHvdiTS 143
Cdd:COG1228 86 AGGGITPTVDLVNPAdkrlRRALAAGVTTVRDL----PGGPLglrdaiiageSKLLPGPRvLAAGPALSLTGGAH---AR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503051 144 WYDGVREELEVLVQDkGVNSFQVYMAYKDvYQMSDSQLYEAFTFLKGLGAVILVHAENGDLIaqeqKRILEMGITGPEgH 223
Cdd:COG1228 159 GPEEARAALRELLAE-GADYIKVFAEGGA-PDFSLEELRAILEAAHALGLPVAAHAHQADDI----RLAVEAGVDSIE-H 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503051 224 ALSRPEEleaeavfraitiagrincpvyitkvmsksaadIIALARKKGPLVfgepiaaslgtdgthywsknwakaaafvt 303
Cdd:COG1228 232 GTYLDDE--------------------------------VADLLAEAGTVV----------------------------- 250
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503051 304 sppLSPDPTTPDYLTSLLACGDLQVTGSGHC-PYSTAQK--------AVGKDNFTLIPEGVNGIEErmtvvWDKAVATGk 374
Cdd:COG1228 251 ---LVPTLSLFLALLEGAAAPVAAKARKVREaALANARRlhdagvpvALGTDAGVGVPPGRSLHRE-----LALAVEAG- 321
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503051 375 MDENQ-FVAVTStNAAKIFNLYPRKGRIAVGSDADVVIWDPDKLKTITAkshksaveynifegmecHGSPLVVISQGKIV 453
Cdd:COG1228 322 LTPEEaLRAATI-NAAKALGLDDDVGSLEPGKLADLVLLDGDPLEDIAY-----------------LEDVRAVMKDGRVV 383
|
...
gi 4503051 454 FED 456
Cdd:COG1228 384 DRS 386
|
|
| PRK07369 |
PRK07369 |
dihydroorotase; Provisional |
33-427 |
2.34e-10 |
|
dihydroorotase; Provisional
Pssm-ID: 236002 [Multi-domain] Cd Length: 418 Bit Score: 62.70 E-value: 2.34e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503051 33 ADVYLEDGLIKQIGENLI-VPGGVKTIEANGRMVIPGGIDVNTYLQKPsqGMTAADDFFQGTRAALVGGTTMI------- 104
Cdd:PRK07369 22 ADVLIEDGKIQAIEPHIDpIPPDTQIIDASGLILGPGLVDLYSHSGEP--GFEERETLASLAAAAAAGGFTRVailpdtf 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503051 105 --IDHvvPEPGSSLLTSFE-----KWHE-AADTKSCCDYSLhvdiTSWYDgvreelevLVQdKGVNSFqvymaykdvyqm 176
Cdd:PRK07369 100 ppLDN--PATLARLQQQAQqippvQLHFwGALTLGGQGKQL----TELAE--------LAA-AGVVGF------------ 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503051 177 SDSQ-------LYEAFTFLKGLGAVILVHAENGDL----IAQEQKRILEMGITGpeghalsRPEELEAEAVFRAITIAGR 245
Cdd:PRK07369 153 TDGQplenlalLRRLLEYLKPLGKPVALWPCDRSLagngVMREGLLALRLGLPG-------DPASAETTALAALLELVAA 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503051 246 INCPVYITKVMSKSAADIIALARKKGPlvfgePIAAS-------LGTDGTHYWSKNWAKAaafvtsPPLsPDPTTPDYLT 318
Cdd:PRK07369 226 IGTPVHLMRISTARSVELIAQAKARGL-----PITASttwmhllLDTEALASYDPNLRLD------PPL-GNPSDRQALI 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503051 319 SLLACGDLQVTGSGHCPYSTAQKAVGkdnFTLIPEGVNGIEERMTVVWDKAVATGKMDENQFVAVTSTNAAKIFNLYPRk 398
Cdd:PRK07369 294 EGVRTGVIDAIAIDHAPYTYEEKTVA---FAEAPPGAIGLELALPLLWQNLVETGELSALQLWQALSTNPARCLGQEPP- 369
|
410 420
....*....|....*....|....*....
gi 4503051 399 gRIAVGSDADVVIWDPDKLKTITAKSHKS 427
Cdd:PRK07369 370 -SLAPGQPAELILFDPQKTWTVSAQTLHS 397
|
|
| D-aminoacylase |
cd01297 |
D-aminoacylases (N-acyl-D-Amino acid amidohydrolases) catalyze the hydrolysis of ... |
17-457 |
7.34e-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: 61.16 E-value: 7.34e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503051 17 LLIKGGRIIndDQS----LYADVYLEDGLIKQIGENLIVPgGVKTIEANGRMVIPGGIDVNTYlqkpSQGMTAADDFFqg 92
Cdd:cd01297 2 LVIRNGTVV--DGTgappFTADVGIRDGRIAAIGPILSTS-AREVIDAAGLVVAPGFIDVHTH----YDGQVFWDPDL-- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503051 93 TRAALVGGTTMIIDhvvpEPGSSLltsfekwheaadtksccdYSLHVDITSWYDGVREELEVLVQDKGVnSFQVYMAYKD 172
Cdd:cd01297 73 RPSSRQGVTTVVLG----NCGVSP------------------APANPDDLARLIMLMEGLVALGEGLPW-GWATFAEYLD 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503051 173 VYQMSDSQLYEAFTFlkGLGAV-ILVHAENGDLIAQEQ----KRILE-------MGI-TG----PEGHAlsRPEELEAEA 235
Cdd:cd01297 130 ALEARPPAVNVAALV--GHAALrRAVMGLDAREATEEElakmRELLRealeagaLGIsTGlayaPRLYA--GTAELVALA 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503051 236 vfraiTIAGRINCpVYITKVMSKSAA------DIIALARKKG-PLVFgepiaASLGTDGTHYWSKnWAKAAAFVTSPPLS 308
Cdd:cd01297 206 -----RVAARYGG-VYQTHVRYEGDSilealdELLRLGRETGrPVHI-----SHLKSAGAPNWGK-IDRLLALIEAARAE 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503051 309 PDPTTPD---YLTSLLA-------------CGDLQVTGSGHC------PYSTAQKAVGKDNFTLiPEGVngieERMTvvw 366
Cdd:cd01297 274 GLQVTADvypYGAGSEDdvrrimahpvvmgGSDGGALGKPHPrsygdfTRVLGHYVRERKLLSL-EEAV----RKMT--- 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503051 367 dkavatgkmdenqfvavtsTNAAKIFNLYPRkGRIAVGSDADVVIWDPDKLK---TITAKSHKSaveynifEGMEchgsp 443
Cdd:cd01297 346 -------------------GLPARVFGLADR-GRIAPGYRADIVVFDPDTLAdraTFTRPNQPA-------EGIE----- 393
|
490
....*....|....
gi 4503051 444 LVVISqGKIVFEDG 457
Cdd:cd01297 394 AVLVN-GVPVVRDG 406
|
|
| NagA |
cd00854 |
N-acetylglucosamine-6-phosphate deacetylase, NagA, catalyzes the hydrolysis of the N-acetyl ... |
17-415 |
3.29e-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: 55.66 E-value: 3.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503051 17 LLIKGGRIINDDQSLYADVYLEDGLIKQIGENLIVPGGVKTIEANGRMVIPGGIDVNTYlqkpsqG------MTAADDFF 90
Cdd:cd00854 1 LIIKNARILTPGGLEDGAVLVEDGKIVAIGPEDELEEADEIIDLKGQYLVPGFIDIHIH------GgggadfMDGTAEAL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503051 91 QGTRAALV--GGTTMiidhvVPepgsSLLT-SFEKWHEAADtksccdyslhvditswydgvreelevlvqdkgvnsfqvy 167
Cdd:cd00854 75 KTIAEALAkhGTTSF-----LP----TTVTaPPEEIAKALA--------------------------------------- 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503051 168 mAYKDVYQmsdsqlyeaftflKGLGAVIL-VHAEnGDLIAQEQKrilemgitG--PEGHALS-RPEELE-----AEAVFR 238
Cdd:cd00854 107 -AIAEAIA-------------EGQGAEILgIHLE-GPFISPEKK--------GahPPEYLRApDPEELKkwleaAGGLIK 163
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503051 239 AITIAGRIncpvyitkvmsKSAADIIALARKKGplvfgepIAASLG-TDGTHYWSKNWAKAAA-FVT------SPPLSPD 310
Cdd:cd00854 164 LVTLAPEL-----------DGALELIRYLVERG-------IIVSIGhSDATYEQAVAAFEAGAtHVThlfnamSPLHHRE 225
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503051 311 P-------TTPDYLTSLLAcgDLQvtgsgHCPYST---AQKAVGKDNFTLI---------PEGVNGIEERMTVVWDKAV- 370
Cdd:cd00854 226 PgvvgaalSDDDVYAELIA--DGI-----HVHPAAvrlAYRAKGADKIVLVtdamaaaglPDGEYELGGQTVTVKDGVAr 298
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 4503051 371 -ATG-------KMDE-------------NQFVAVTSTNAAKIFNLYPRKGRIAVGSDADVVIWDPD 415
Cdd:cd00854 299 lADGtlagstlTMDQavrnmvkwggcplEEAVRMASLNPAKLLGLDDRKGSLKPGKDADLVVLDDD 364
|
|
| ATZ_TRZ_like |
cd01298 |
TRZ/ATZ family contains enzymes from the atrazine degradation pathway and related hydrolases. ... |
17-460 |
2.96e-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: 52.97 E-value: 2.96e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503051 17 LLIKGGRIINDDQS---LYADVYLEDGLIKQIGENLIVPG--GVKTIEANGRMVIPGGIDVNT----------------- 74
Cdd:cd01298 1 ILIRNGTIVTTDPRrvlEDGDVLVEDGRIVAVGPALPLPAypADEVIDAKGKVVMPGLVNTHThlamtllrgladdlplm 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503051 75 -YLQK---PSQGMTAADDFFQGTRAALV----GGTTMIIDHVVPEPGSSLltsfekwhEAADtKSccdyslhvditswyd 146
Cdd:cd01298 81 eWLKDliwPLERLLTEEDVYLGALLALAemirSGTTTFADMYFFYPDAVA--------EAAE-EL--------------- 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503051 147 GVREELEVLVQDKGVnsfqvymayKDVYQMSDSqLYEAFTFLKglgaviLVHAENGDLIaqeqkRILeMGITGPEghaLS 226
Cdd:cd01298 137 GIRAVLGRGIMDLGT---------EDVEETEEA-LAEAERLIR------EWHGAADGRI-----RVA-LAPHAPY---TC 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503051 227 RPEELEaeavfRAITIAGRINCPVYITkvMSKSAADI-IALARK-KGPLVFgepiAASLGTDGTHYWsknwakAAAFVTs 304
Cdd:cd01298 192 SDELLR-----EVAELAREYGVPLHIH--LAETEDEVeESLEKYgKRPVEY----LEELGLLGPDVV------LAHCVW- 253
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503051 305 pplspdpTTPDYLTsLLACGDLQVTgsgHCPYSTAQKAVGkdnFTLIPE----GVN---------------GIEE-RMTV 364
Cdd:cd01298 254 -------LTDEEIE-LLAETGTGVA---HNPASNMKLASG---IAPVPEmleaGVNvglgtdgaasnnnldMFEEmRLAA 319
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503051 365 VWDKAVA--TGKMDENQFVAVTSTNAAKIFNLyPRKGRIAVGSDADVVIWDPDKLKTITAKSHKSAVEYNifegmeCHGS 442
Cdd:cd01298 320 LLQKLAHgdPTALPAEEALEMATIGGAKALGL-DEIGSLEVGKKADLILIDLDGPHLLPVHDPISHLVYS------ANGG 392
|
490 500
....*....|....*....|
gi 4503051 443 P--LVVISqGKIVFEDGNIN 460
Cdd:cd01298 393 DvdTVIVN-GRVVMEDGELL 411
|
|
| PRK07627 |
PRK07627 |
dihydroorotase; Provisional |
16-456 |
3.05e-07 |
|
dihydroorotase; Provisional
Pssm-ID: 181059 [Multi-domain] Cd Length: 425 Bit Score: 52.76 E-value: 3.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503051 16 RLLIKGGRIIN-----DDQslyADVYLEDGLIKQIGEnliVPGGV---KTIEANGRMVIPGGIDVNTYLQKPsqGMTAAD 87
Cdd:PRK07627 2 KIHIKGGRLIDpaagtDRQ---ADLYVAAGKIAAIGQ---APAGFnadKTIDASGLIVCPGLVDLSARLREP--GYEYKA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503051 88 DFFQGTRAALVGGTTMII-----DHVVPEPGSSLLTSF--EKWHEAadtksccdyslHV----DITSWYDGVR-EELEVL 155
Cdd:PRK07627 74 TLESEMAAAVAGGVTSLVcppdtDPVLDEPGLVEMLKFraRNLNQA-----------HVyplgALTVGLKGEVlTEMVEL 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503051 156 VQDKGVNSFQVymaykDVyQMSDSQ-LYEAFTFLKGLG-AVILvhaengdliaQEQKRILEMGITGPEGHALSR------ 227
Cdd:PRK07627 143 TEAGCVGFSQA-----NV-PVVDTQvLLRALQYASTFGfTVWL----------RPLDAFLGRGGVAASGAVASRlglsgv 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503051 228 PEELEAEAVFRAITIAGRINCPVYITKVMSKSAADIIALARKKgplvfGEPIAASLGTDGTH-------YWSKNwakaaa 300
Cdd:PRK07627 207 PVAAETIALHTIFELMRVTGARVHLARLSSAAGVALVRAAKAE-----GLPVTCDVGVNHVHlidvdigYFDSQ------ 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503051 301 FVTSPPLSpDPTTPDYLTSLLACGDLQVTGSGHCPystaqkaVGKDNfTLIP-----EGVNGIEE--RMTVVWdkAVATg 373
Cdd:PRK07627 276 FRLDPPLR-SQRDREAIRAALADGTIDAICSDHTP-------VDDDE-KLLPfaeatPGATGLELllPLTLKW--ADEA- 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503051 374 KMDENQFVAVTSTNAAKIFNLypRKGRIAVGSDADVVIWDPDKLKTITAKSHKSAVEYNIFEGMECHGSPLVVISQGKIV 453
Cdd:PRK07627 344 KVPLARALARITSAPARVLGL--PAGRLAEGAPADLCVFDPDAHWRVEPRALKSQGKNTPFLGYELPGRVRATLVAGQVA 421
|
...
gi 4503051 454 FED 456
Cdd:PRK07627 422 FER 424
|
|
| NagA |
COG1820 |
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism]; |
381-415 |
9.94e-07 |
|
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism];
Pssm-ID: 441425 [Multi-domain] Cd Length: 373 Bit Score: 51.25 E-value: 9.94e-07
10 20 30
....*....|....*....|....*....|....*
gi 4503051 381 VAVTSTNAAKIFNLYPRKGRIAVGSDADVVIWDPD 415
Cdd:COG1820 328 VRMASLNPARALGLDDRKGSIAPGKDADLVVLDDD 362
|
|
| PRK07228 |
PRK07228 |
5'-deoxyadenosine deaminase; |
16-107 |
2.51e-06 |
|
5'-deoxyadenosine deaminase;
Pssm-ID: 180895 [Multi-domain] Cd Length: 445 Bit Score: 50.00 E-value: 2.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503051 16 RLLIKGGRIINDDQS---LYADVYLEDGLIKQIGENLIVPGGVKTIEANGRMVIPGGIDVNTYL-QKPSQG--------- 82
Cdd:PRK07228 2 TILIKNAGIVTMNAKreiVDGDVLIEDDRIAAVGDRLDLEDYDDHIDATGKVVIPGLIQGHIHLcQTLFRGiaddlelld 81
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 4503051 83 --------MTAADDFFQGTRAALVG-------GTTMIIDH 107
Cdd:PRK07228 82 wlkdriwpLEAAHDAESMYYSALLGigeliesGTTTIVDM 121
|
|
| PRK09237 |
PRK09237 |
amidohydrolase/deacetylase family metallohydrolase; |
17-74 |
3.73e-06 |
|
amidohydrolase/deacetylase family metallohydrolase;
Pssm-ID: 236423 [Multi-domain] Cd Length: 380 Bit Score: 49.46 E-value: 3.73e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503051 17 LLIKGGRIINDDQSLYA--DVYLEDGLIKQIGENLIVPGGVKTIEANGRMVIPGGIDVNT 74
Cdd:PRK09237 1 LLLRGGRVIDPANGIDGviDIAIEDGKIAAVAGDIDGSQAKKVIDLSGLYVSPGWIDLHV 60
|
|
| PRK09061 |
PRK09061 |
D-glutamate deacylase; Validated |
16-104 |
4.52e-06 |
|
D-glutamate deacylase; Validated
Pssm-ID: 236369 [Multi-domain] Cd Length: 509 Bit Score: 49.31 E-value: 4.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503051 16 RLLIKGGRIINDDQSLYA--DVYLEDGLIKQIGENLIvpGGVKTIEANGRMVIPGGIDVNtylqkpSQGMTAADDFFQgt 93
Cdd:PRK09061 20 DLVIRNGRVVDPETGLDAvrDVGIKGGKIAAVGTAAI--EGDRTIDATGLVVAPGFIDLH------AHGQSVAAYRMQ-- 89
|
90
....*....|.
gi 4503051 94 raALVGGTTMI 104
Cdd:PRK09061 90 --AFDGVTTAL 98
|
|
| Amidohydro_3 |
pfam07969 |
Amidohydrolase family; |
334-454 |
8.66e-06 |
|
Amidohydrolase family;
Pssm-ID: 400360 [Multi-domain] Cd Length: 464 Bit Score: 48.30 E-value: 8.66e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503051 334 CPYSTAQKAVGKDnfTLIPEGVNGIEERMTVvwdkavatgkmdeNQFVAVTSTNAAKIFNLYPRKGRIAVGSDADVVIWD 413
Cdd:pfam07969 373 DPWPRIGAAVMRQ--TAGGGEVLGPDEELSL-------------EEALALYTSGPAKALGLEDRKGTLGVGKDADLVVLD 437
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 4503051 414 PDKLKTITAKSHKSAVEYnifegmechgsplvVISQGKIVF 454
Cdd:pfam07969 438 DDPLTVDPPAIADIRVRL--------------TVVDGRVVY 464
|
|
| PRK08204 |
PRK08204 |
hypothetical protein; Provisional |
15-112 |
1.13e-05 |
|
hypothetical protein; Provisional
Pssm-ID: 181288 [Multi-domain] Cd Length: 449 Bit Score: 48.07 E-value: 1.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503051 15 DRLLIKGGRIINDDQSL----YADVYLEDGLIKQIGENlIVPGGVKTIEANGRMVIPG------------------GIDV 72
Cdd:PRK08204 2 KRTLIRGGTVLTMDPAIgdlpRGDILIEGDRIAAVAPS-IEAPDAEVVDARGMIVMPGlvdthrhtwqsvlrgigaDWTL 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 4503051 73 NTYLQKPSQGMTAA---DDFFQGTRA----ALVGGTTMIID--HVVPEP 112
Cdd:PRK08204 81 QTYFREIHGNLGPMfrpEDVYIANLLgaleALDAGVTTLLDwsHINNSP 129
|
|
| NagA |
COG1820 |
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism]; |
18-72 |
2.23e-05 |
|
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism];
Pssm-ID: 441425 [Multi-domain] Cd Length: 373 Bit Score: 47.02 E-value: 2.23e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 4503051 18 LIKGGRIINDDQSLY-ADVYLEDGLIKQIGENliVPGGVKTIEANGRMVIPGGIDV 72
Cdd:COG1820 1 AITNARIFTGDGVLEdGALLIEDGRIAAIGPG--AEPDAEVIDLGGGYLAPGFIDL 54
|
|
| Met_dep_hydrolase_C |
cd01309 |
Metallo-dependent hydrolases, subgroup C is part of the superfamily of metallo-dependent ... |
368-440 |
5.24e-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: 5.24e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 4503051 368 KAVATGKMDENQFVAVTStNAAKIFNLYPRKGRIAVGSDADVVIWDPDKLKTiTAKshksaVEYNIFEGMECH 440
Cdd:cd01309 294 KAVKYGLSYEEALKAITI-NPAKILGIEDRVGSLEPGKDADLVVWNGDPLEP-TSK-----PEQVYIDGRLVY 359
|
|
| Bact_CD |
cd01293 |
Bacterial cytosine deaminase and related metal-dependent hydrolases. Cytosine deaminases (CDs) ... |
18-78 |
2.39e-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: 2.39e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 4503051 18 LIKGGRIINDDQSLYaDVYLEDGLIKQIGENLIVPGGVKTIEANGRMVIPGGIDVNTYLQK 78
Cdd:cd01293 1 LLRNARLADGGTALV-DIAIEDGRIAAIGPALAVPPDAEEVDAKGRLVLPAFVDPHIHLDK 60
|
|
| PRK15446 |
PRK15446 |
phosphonate metabolism protein PhnM; Provisional |
16-74 |
4.42e-04 |
|
phosphonate metabolism protein PhnM; Provisional
Pssm-ID: 237967 [Multi-domain] Cd Length: 383 Bit Score: 42.86 E-value: 4.42e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 4503051 16 RLLIKGGRIINDDQSLYADVYLEDGLIKQIGENLIVPGGvkTIEANGRMVIPGGIDVNT 74
Cdd:PRK15446 3 EMILSNARLVLPDEVVDGSLLIEDGRIAAIDPGASALPG--AIDAEGDYLLPGLVDLHT 59
|
|
| Imidazolone-5PH |
cd01296 |
Imidazolonepropionase/imidazolone-5-propionate hydrolase (Imidazolone-5PH) catalyzes the third ... |
369-413 |
1.87e-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: 1.87e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 4503051 369 AVATGKMDENQFVAVTSTNAAKIFNLYPRKGRIAVGSDADVVIWD 413
Cdd:cd01296 304 ACRLMRMTPEEALTAATINAAAALGLGETVGSLEVGKQADLVILD 348
|
|
| COG3653 |
COG3653 |
N-acyl-D-aspartate/D-glutamate deacylase [Secondary metabolites biosynthesis, transport and ... |
388-473 |
2.85e-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: 2.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503051 388 AAKIFNLYPRkGRIAVGSDADVVIWDPDKLK-TITA-KSHKSAveynifEGMEChgsplVVISqGKIVFEDGNINvNKGM 465
Cdd:COG3653 453 PADRLGLKDR-GLLRPGYRADLVVFDPATLAdRATFdLPAQRA------DGIRA-----VIVN-GVVVVEDGKPT-GARP 518
|
....*...
gi 4503051 466 GRFIPRKA 473
Cdd:COG3653 519 GRVLRGGG 526
|
|
| PRK05985 |
PRK05985 |
cytosine deaminase; Provisional |
33-83 |
3.11e-03 |
|
cytosine deaminase; Provisional
Pssm-ID: 180337 [Multi-domain] Cd Length: 391 Bit Score: 40.30 E-value: 3.11e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 4503051 33 ADVYLEDGLIKQIGENLIVPGGVKTIEANGRMVIPGGIDVNTYLQKPSQGM 83
Cdd:PRK05985 17 VDILIRDGRIAAIGPALAAPPGAEVEDGGGALALPGLVDGHIHLDKTFWGD 67
|
|
| Isoaspartyl-dipeptidase |
cd01308 |
Isoaspartyl dipeptidase hydrolyzes the beta-L-isoaspartyl linkages in dipeptides, as part of ... |
383-423 |
3.87e-03 |
|
Isoaspartyl dipeptidase hydrolyzes the beta-L-isoaspartyl linkages in dipeptides, as part of the degradative pathway to eliminate proteins with beta-L-isoaspartyl peptide bonds, bonds whereby the beta-group of an aspartate forms the peptide link with the amino group of the following amino acid. Formation of this bond is a spontaneous nonenzymatic reaction in nature and can profoundly effect the function of the protein. Isoaspartyl dipeptidase is an octameric enzyme that contains a binuclear zinc center in the active site of each subunit and shows a strong preference of hydrolyzing Asp-Leu dipeptides.
Pssm-ID: 238633 [Multi-domain] Cd Length: 387 Bit Score: 39.68 E-value: 3.87e-03
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 4503051 383 VTSTNAAKIFNLYPrKGRIAVGSDADVVIWDPD-KLKTITAK 423
Cdd:cd01308 330 VITSNVARILKLRK-KGEIQPGFDADLVILDKDlDINSVIAK 370
|
|
| FMDH_A |
cd01304 |
Formylmethanofuran dehydrogenase (FMDH) subunit A; Methanogenic bacteria and archea derive ... |
19-75 |
5.61e-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: 5.61e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503051 19 IKGGRIINDDQSLYA---DVYLEDGlikQIGENLIVPGGVKTIEANGRMVIPGGIDVNTY 75
Cdd:cd01304 1 IKNGTVYDPLNGINGekmDIFIRDG---KIVESSSGAKPAKVIDASGKVVMAGGVDMHSH 57
|
|
| Met_dep_hydrolase_B |
cd01307 |
Metallo-dependent hydrolases, subgroup B is part of the superfamily of metallo-dependent ... |
330-425 |
7.13e-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: 7.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503051 330 GSGHCPYSTAQKAVGKDnftLIPE----------GVNGIEERMTVVWDKAVATGkMDENQFVAVTSTNAAKIFNLyPRKG 399
Cdd:cd01307 226 GTASFSFRVARAAIAAG---LLPDtissdihgrnRTNGPVYALATTLSKLLALG-MPLEEVIEAVTANPARMLGL-AEIG 300
|
90 100
....*....|....*....|....*.
gi 4503051 400 RIAVGSDADVVIWDPDKLKTITAKSH 425
Cdd:cd01307 301 TLAVGYDADLTVFDLKDGRVELVDSE 326
|
|
| |
