|
Name |
Accession |
Description |
Interval |
E-value |
| D-HYD |
cd01314 |
D-hydantoinases (D-HYD) also called dihydropyrimidases (DHPase) and related proteins; DHPases ... |
131-580 |
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: 736.33 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62422571 131 LLIKGGRIINDDQSLYADVYLEDGLIKQIGENLIVPGGVKTIEANGRMVIPGGIDVNTYLQKPSQGMTAADDFFQGTRAA 210
Cdd:cd01314 1 LIIKNGTIVTADGSFKADILIEDGKIVAIGPNLEAPGGVEVIDATGKYVLPGGIDPHTHLELPFMGTVTADDFESGTRAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62422571 211 LVGGTTMIIDHVVPEPGSSLLTSFEKWHEAADTKSCCDYSLHVDITSWYDGVREELEVLVqDKGVNSFQVYMAYKDVYQM 290
Cdd:cd01314 81 AAGGTTTIIDFAIPNKGQSLLEAVEKWRGKADGKSVIDYGFHMIITDWTDSVIEELPELV-KKGISSFKVFMAYKGLLMV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62422571 291 SDSQLYEAFTFLKGLGAVILVHAENGDLIAQEQKRILEMGITGPEGHALSRPEELEAEAVFRAITIAGRINCPVYITKVM 370
Cdd:cd01314 160 DDEELLDVLKRAKELGALVMVHAENGDVIAELQKKLLAQGKTGPEYHALSRPPEVEAEATARAIRLAELAGAPLYIVHVS 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62422571 371 SKSAADIIALARKKGPLVFGEPIAASLGTDGTHYWsKNWAKAAAFVTSPPLSPDpTTPDYLTSLLACGDLQVTGSGHCPY 450
Cdd:cd01314 240 SKEAADEIARARKKGLPVYGETCPQYLLLDDSDYW-KDWFEGAKYVCSPPLRPK-EDQEALWDGLSSGTLQTVGSDHCPF 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62422571 451 STAQKAVGKDNFTLIPEGVNGIEERMTVVWDKAVATGKMDENQFVAVTSTNAAKIFNLYPRKGRIAVGSDADVVIWDPDK 530
Cdd:cd01314 318 NFAQKARGKDDFTKIPNGVPGVETRMPLLWSEGVAKGRITLEKFVELTSTNPAKIFGLYPRKGTIAVGSDADLVIWDPNA 397
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 62422571 531 LKTITAKSHKSAVEYNIFEGMECHGSPLVVISQGKIVFEDGNINVNKGMG 580
Cdd:cd01314 398 EKTISADTHHHNVDYNIFEGMKVKGWPVVTISRGKVVVEDGELVGEKGSG 447
|
|
| D-hydantoinase |
TIGR02033 |
D-hydantoinase; This model represents the D-hydantoinase (dihydropyrimidinase) which primarily ... |
131-585 |
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: 663.31 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62422571 131 LLIKGGRIINDDQSLYADVYLEDGLIKQIGENLIVPGGVKTIEANGRMVIPGGIDVNTYLQKPSQGMTAADDFFQGTRAA 210
Cdd:TIGR02033 1 LLIKGGTVVNADDVFQADVLIEGGKIVAVGDNLIPPDAVEVIDATGKYVLPGGIDVHTHLEMPFGGTTTADDFFTGTKAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62422571 211 LVGGTTMIIDHVVPEPGSSLLTSFEKWHEAADTKSCCDYSLHVDITSWYDGVREELEVLVQDKGVNSFQVYMAYKDVYQM 290
Cdd:TIGR02033 81 AAGGTTTIIDFVVPEKGSSLTEALETWHEKAEGKSVIDYGFHMDITHWNDSVLEEHIPEVKEEGINSFKVFMAYKNLLMV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62422571 291 SDSQLYEAFTFLKGLGAVILVHAENGDLIAQEQKRILEMGITGPEGHALSRPEELEAEAVFRAITIAGRINCPVYITKVM 370
Cdd:TIGR02033 161 DDEELFEILKRLKELGALLQVHAENGDIIAELQARMLAQGITGPEYHALSRPPELEAEAVARAITLAALADAPLYVVHVS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62422571 371 SKSAADIIALARKKGPLVFGEPIAASLGTDGTHYWsKNWAKAAAFVTSPPLSpDPTTPDYLTSLLACGDLQVTGSGHCPY 450
Cdd:TIGR02033 241 TKDAADEIAQARKKGQPVFGETCPQYLVLDDTHYD-KPGFEGAKYVCSPPLR-EPEDQDALWSALSSGALQTVGSDHCTF 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62422571 451 STAQK-AVGKDNFTLIPEGVNGIEERMTVVWDKAVATGKMDENQFVAVTSTNAAKIFNLYPRKGRIAVGSDADVVIWDPD 529
Cdd:TIGR02033 319 NFAQKkAIGKDDFTKIPNGGPGVEERMSLLFDEGVAKGRITLEKFVEVTSTNPAKIFNLYPRKGTIAVGSDADIVIWDPN 398
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 62422571 530 KLKTITAKSHKSAVEYNIFEGMECHGSPLVVISQGKIVFEDGNINVNKGMGRFIPR 585
Cdd:TIGR02033 399 RTTVISAETHHSNADYNPFEGFKVRGAPVSVLSRGRVVVEDGQLVGTAGAGRFVKR 454
|
|
| PRK08323 |
PRK08323 |
phenylhydantoinase; Validated |
130-589 |
0e+00 |
|
phenylhydantoinase; Validated
Pssm-ID: 236240 [Multi-domain] Cd Length: 459 Bit Score: 567.11 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62422571 130 RLLIKGGRIINDDQSLYADVYLEDGLIKQIGENlivpGGVKTIEANGRMVIPGGIDVNTYLQKPSQGMTAADDFFQGTRA 209
Cdd:PRK08323 2 STLIKNGTVVTADDTYKADVLIEDGKIAAIGAN----LGDEVIDATGKYVMPGGIDPHTHMEMPFGGTVSSDDFETGTRA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62422571 210 ALVGGTTMIIDHVVPEPGSSLLTSFEKWHEAADTKSCCDYSLHVDITSWYDGVREELEVLVqDKGVNSFQVYMAYKDVYQ 289
Cdd:PRK08323 78 AACGGTTTIIDFALQPKGQSLREALEAWHGKAAGKAVIDYGFHMIITDWNEVVLDEMPELV-EEGITSFKLFMAYKGALM 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62422571 290 MSDSQLYEAFTFLKGLGAVILVHAENGDLIAQEQKRILEMGITGPEGHALSRPEELEAEAVFRAITIAGRINCPVYITKV 369
Cdd:PRK08323 157 LDDDELLRALQRAAELGALPMVHAENGDAIAYLQAKLLAEGKTGPEYHALSRPPEVEGEATNRAIMLAELAGAPLYIVHV 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62422571 370 MSKSAADIIALARKKGPLVFGEPIAASLGTDGTHYWSKNWAKAAAFVTSPPLSPdPTTPDYLTSLLACGDLQVTGSGHCP 449
Cdd:PRK08323 237 SCKEALEAIRRARARGQRVFGETCPQYLLLDESEYDGPDWFEGAKYVMSPPLRD-KEHQDALWRGLQDGDLQVVATDHCP 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62422571 450 YSTAQKA-VGKDNFTLIPEGVNGIEERMTVVWDKAVATGKMDENQFVAVTSTNAAKIFNLYPRKGRIAVGSDADVVIWDP 528
Cdd:PRK08323 316 FCFEQKKqLGRGDFTKIPNGTPGVEDRMPLLFSEGVMTGRITLNRFVELTSTNPAKIFGLYPRKGTIAVGADADIVIWDP 395
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 62422571 529 DKLKTITAKSHKSAVEYNIFEGMECHGSPLVVISQGKIVFEDGNINVNKGMGRFIPRKAFP 589
Cdd:PRK08323 396 NATKTISASTLHSNVDYNPYEGFEVTGWPVTTLSRGEVVVEDGEFRGKAGHGRFLKRKPFQ 456
|
|
| PLN02942 |
PLN02942 |
dihydropyrimidinase |
126-589 |
0e+00 |
|
dihydropyrimidinase
Pssm-ID: 178530 Cd Length: 486 Bit Score: 529.42 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62422571 126 GQSDRLLIKGGRIINDDQSLYADVYLEDGLIKQIGENLIVPGGVKTIEANGRMVIPGGIDVNTYLQKPSQGMTAADDFFQ 205
Cdd:PLN02942 2 ASSTKILIKGGTVVNAHHQELADVYVEDGIIVAVAPNLKVPDDVRVIDATGKFVMPGGIDPHTHLAMPFMGTETIDDFFS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62422571 206 GTRAALVGGTTMIIDHVVPEPGSsLLTSFEKWHEAADtKSCCDYSLHVDITSWYDGVREELEVLVQDKGVNSFQVYMAYK 285
Cdd:PLN02942 82 GQAAALAGGTTMHIDFVIPVNGN-LLAGYEAYEKKAE-KSCMDYGFHMAITKWDDTVSRDMETLVKEKGINSFKFFMAYK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62422571 286 DVYQMSDSQLYEAFTFLKGLGAVILVHAENGDLIAQEQKRILEMGITGPEGHALSRPEELEAEAVFRAITIAGRINCPVY 365
Cdd:PLN02942 160 GSLMVTDELLLEGFKRCKSLGALAMVHAENGDAVFEGQKRMIELGITGPEGHALSRPPLLEGEATARAIRLAKFVNTPLY 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62422571 366 ITKVMSKSAADIIALARKKGPLVFGEPIAASLGTDGTHYWSKNWAKAAAFVTSPPLSPdPTTPDYLTSLLACGDLQVTGS 445
Cdd:PLN02942 240 VVHVMSIDAMEEIARARKSGQRVIGEPVVSGLVLDDSKLWDPDFTIASKYVMSPPIRP-AGHGKALQAALSSGILQLVGT 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62422571 446 GHCPYSTAQKAVGKDNFTLIPEGVNGIEERMTVVWDKAVATGKMDENQFVAVTSTNAAKIFNLYPRKGRIAVGSDADVVI 525
Cdd:PLN02942 319 DHCPFNSTQKAFGKDDFRKIPNGVNGIEERMHLVWDTMVESGQISPTDYVRVTSTECAKIFNIYPRKGAILAGSDADIII 398
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 62422571 526 WDPDKLKTITAKSHKSAVEYNIFEGMECHGSPLVVISQGKIVFEDGNINVNKGMGRFIPRKAFP 589
Cdd:PLN02942 399 LNPNSTFTISAKTHHSRIDTNVYEGRRGKGKVEVTISQGRVVWENGELKVVRGSGRYIEMPPFS 462
|
|
| AllB |
COG0044 |
Dihydroorotase or related cyclic amidohydrolase [Nucleotide transport and metabolism]; ... |
132-585 |
1.95e-122 |
|
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: 371.73 E-value: 1.95e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62422571 132 LIKGGRIINDDQSLYADVYLEDGLIKQIGENLIVPGGVKTIEANGRMVIPGGIDVNTYLQKPsqGMTAADDFFQGTRAAL 211
Cdd:COG0044 1 LIKNGRVVDPGGLERADVLIEDGRIAAIGPDLAAPEAAEVIDATGLLVLPGLIDLHVHLREP--GLEHKEDIETGTRAAA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62422571 212 VGGTTMIIDHVVPEPGSSLLTSFEKWHEAADTKSCCDYSLHVDITSWYDGVREELEVLVqDKGVNSFQVYMAYKDVYQMS 291
Cdd:COG0044 79 AGGVTTVVDMPNTNPVTDTPEALEFKLARAEEKALVDVGPHGALTKGLGENLAELGALA-EAGAVAFKVFMGSDDGNPVL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62422571 292 DSQ-LYEAFTFLKGLGAVILVHAENGDLIAQeqkRILEMGITGPEGHALSRPEELEAEAVFRAITIAGRINCPVYITKVM 370
Cdd:COG0044 158 DDGlLRRALEYAAEFGALVAVHAEDPDLIRG---GVMNEGKTSPRLGLKGRPAEAEEEAVARDIALAEETGARLHIVHVS 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62422571 371 SKSAADIIALARKKGPLVFGE--P-----IAASLGTDGTHYwsknwakaaafVTSPPLsPDPTTPDYLTSLLACGDLQVT 443
Cdd:COG0044 235 TAEAVELIREAKARGLPVTAEvcPhhltlTDEDLERYGTNF-----------KVNPPL-RTEEDREALWEGLADGTIDVI 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62422571 444 GSGHCPYSTAQKAvgkDNFTLIPEGVNGIEERMTVVWDKAVATGKMDENQFVAVTSTNAAKIFNLyPRKGRIAVGSDADV 523
Cdd:COG0044 303 ATDHAPHTLEEKE---LPFAEAPNGIPGLETALPLLLTELVHKGRLSLERLVELLSTNPARIFGL-PRKGRIAVGADADL 378
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 62422571 524 VIWDPDKLKTITAKSHKSAVEYNIFEGMECHGSPLVVISQGKIVFEDGNInVNKGMGRFIPR 585
Cdd:COG0044 379 VLFDPDAEWTVTAEDLHSKSKNTPFEGRELTGRVVATIVRGRVVYEDGEV-VGEPRGRFLRR 439
|
|
| PRK13404 |
PRK13404 |
dihydropyrimidinase; Provisional |
131-585 |
5.14e-117 |
|
dihydropyrimidinase; Provisional
Pssm-ID: 184033 [Multi-domain] Cd Length: 477 Bit Score: 359.01 E-value: 5.14e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62422571 131 LLIKGGRIINDDQSLYADVYLEDGLIKQIGENLivPGGVKTIEANGRMVIPGGIDVNTYLQKPS-QGMTAADDFFQGTRA 209
Cdd:PRK13404 6 LVIRGGTVVTATDTFQADIGIRGGRIAALGEGL--GPGAREIDATGRLVLPGGVDSHCHIDQPSgDGIMMADDFYTGTVS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62422571 210 ALVGGTTMIIDHVVPEPGSSLLTSFEKWHEAADTKSCCDYSLHVDITSWYDGV-REELEVLVQDkGVNSFQVYMAYkDVY 288
Cdd:PRK13404 84 AAFGGTTTVIPFAAQHRGQSLREAVEDYHRRAAGKAVIDYAFHLIVADPTEEVlTEELPALIAQ-GYTSFKVFMTY-DDL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62422571 289 QMSDSQLYEAFTFLKGLGAVILVHAENGDLIAQEQKRILEMGITGPEGHALSRPEELEAEAVFRAITIAGRINCPVYITK 368
Cdd:PRK13404 162 KLDDRQILDVLAVARRHGAMVMVHAENHDMIAWLTKRLLAAGLTAPKYHAISRPMLAEREATHRAIALAELVDVPILIVH 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62422571 369 VMSKSAADIIALARKKGPLVFGEP-------IAASLGTDGTHywsknwakAAAFVTSPPLSpDPTTPDYLTSLLACGDLQ 441
Cdd:PRK13404 242 VSGREAAEQIRRARGRGLKIFAETcpqylflTAEDLDRPGME--------GAKYICSPPPR-DKANQEAIWNGLADGTFE 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62422571 442 VTGSGHCPY---STAQKAVGKDN--FTLIPEGVNGIEERMTVVWDKAVATGKMDENQFVAVTSTNAAKIFNLYPRKGRIA 516
Cdd:PRK13404 313 VFSSDHAPFrfdDTDGKLAAGANpsFKAIANGIPGIETRLPLLFSEGVVKGRISLNRFVALTSTNPAKLYGLYPRKGAIA 392
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 62422571 517 VGSDADVVIWDPDKLKTITAKSHKSAVEYNIFEGMECHGSPLVVISQGKIVFEDGNINVNKGMGRFIPR 585
Cdd:PRK13404 393 IGADADIAIWDPDREVTITNADLHHAADYTPYEGMRVTGWPVTVLSRGRVVVEDGELVAERGSGQFLAR 461
|
|
| L-HYD_ALN |
cd01315 |
L-Hydantoinases (L-HYDs) and Allantoinase (ALN); L-Hydantoinases are a member of the ... |
131-571 |
3.02e-67 |
|
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: 227.56 E-value: 3.02e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62422571 131 LLIKGGRIINDDQSLYADVYLEDGLIKQIGENLIVPGGVKTIEANGRMVIPGGIDVNTYLQKPsqGMTAADDFFQGTRAA 210
Cdd:cd01315 2 LVIKNGRVVTPDGVREADIAVKGGKIAAIGPDIANTEAEEVIDAGGLVVMPGLIDTHVHINEP--GRTEWEGFETGTKAA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62422571 211 LVGGTTMIIDhvVP---EPGSSLLTSFEKWHEAADTKSccdyslHVDITSWYDGVR---EELEVLVqDKGVNSFQVYMA- 283
Cdd:cd01315 80 AAGGITTIID--MPlnsIPPTTTVENLEAKLEAAQGKL------HVDVGFWGGLVPgnlDQLRPLD-EAGVVGFKCFLCp 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62422571 284 --YKDVYQMSDSQLYEAFTFLKGLGAVILVHAENGDLIAQEQKRILEMGITGPEGHALSRPEELEAEAVFRAITIAGRIN 361
Cdd:cd01315 151 sgVDEFPAVDDEQLEEAMKELAKTGSVLAVHAENPEITEALQEQAKAKGKRDYRDYLASRPVFTEVEAIQRILLLAKETG 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62422571 362 CPVYITKVMSKSAADIIALARKKGPLVFGEpiaaslgtDGTHYWS-------KNwakAAAFVTSPPLSpDPTTPDYLTSL 434
Cdd:cd01315 231 CRLHIVHLSSAEAVPLIREARAEGVDVTVE--------TCPHYLTftaedvpDG---GTEFKCAPPIR-DAANQEQLWEA 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62422571 435 LACGDLQVTGSGHCPYSTAQKAVGKDNFTLIPEGVNGIEERMTVVWDKAVATGKMDENQFVAVTSTNAAKIFNLYPRKGR 514
Cdd:cd01315 299 LENGDIDMVVSDHSPCTPELKLLGKGDFFKAWGGISGLQLGLPVMLTEAVNKRGLSLEDIARLMCENPAKLFGLSHQKGR 378
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 62422571 515 IAVGSDADVVIWDPDKLKTITAKSHKSAVEYNIFEGMECHGSPLVVISQGKIVFEDG 571
Cdd:cd01315 379 IAVGYDADFVVWDPEEEFTVDAEDLYYKNKISPYVGRTLKGRVHATILRGTVVYQDG 435
|
|
| Cyclic_amidohydrolases |
cd01302 |
Cyclic amidohydrolases, including hydantoinase, dihydropyrimidinase, allantoinase, and ... |
179-557 |
7.85e-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: 217.64 E-value: 7.85e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62422571 179 VIPGGIDVNTYLQKPSQGMTAaDDFFQGTRAALVGGTTMIIDHVVPEPGSSLLTSFEKWHEAADTKSCCDYSLHVDITSw 258
Cdd:cd01302 3 VLPGFIDIHVHLRDPGGTTYK-EDFESGSRAAAAGGVTTVIDMPNTGPPPIDLPAIELKIKLAEESSYVDFSFHAGIGP- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62422571 259 yDGVREELEvLVQDKGVNSFQVYMAYK--DVYQMSDSQLYEAFTFLKGLGAVILVHAEngdliaqeqkrilemgitgpeg 336
Cdd:cd01302 81 -GDVTDELK-KLFDAGINSLKVFMNYYfgELFDVDDGTLMRTFLEIASRGGPVMVHAE---------------------- 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62422571 337 halsrpeeleaeavfRAITIAGRINCPVYITKVMSKSAADIIALARKKGPLVFGEPIAASLGTDgTHYWSKNWAKaaaFV 416
Cdd:cd01302 137 ---------------RAAQLAEEAGANVHIAHVSSGEALELIKFAKNKGVKVTCEVCPHHLFLD-ESMLRLNGAW---GK 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62422571 417 TSPPLSPdPTTPDYLTSLLACGDLQVTGSGHCPYSTAQKAVGKDnFTLIPEGVNGIEERMTVVWdKAVATGKMDENQFVA 496
Cdd:cd01302 198 VNPPLRS-KEDREALWEGVKNGKIDTIASDHAPHSKEEKESGKD-IWKAPPGFPGLETRLPILL-TEGVKRGLSLETLVE 274
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 62422571 497 VTSTNAAKIFNLYPrKGRIAVGSDADVVIWDPDKLKTITAKSHKSAVEYNIFEGMECHGSP 557
Cdd:cd01302 275 ILSENPARIFGLYP-KGTIAVGYDADLVIVDPKKEWKVTAEEIESKADWTPFEGMEVTGKP 334
|
|
| PRK02382 |
PRK02382 |
dihydroorotase; Provisional |
131-586 |
2.73e-55 |
|
dihydroorotase; Provisional
Pssm-ID: 179417 [Multi-domain] Cd Length: 443 Bit Score: 195.26 E-value: 2.73e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62422571 131 LLIKGGRIINDDQSLYADVYLEDGLIKQIGENLIVPGGVKTIEANGRMVIPGGIDVNTYLQKPsqGMTAADDFFQGTRAA 210
Cdd:PRK02382 4 ALLKDGRVYYNNSLQPRDVRIDGGKITAVGKDLDGSSSEEVIDARGMLLLPGGIDVHVHFREP--GYTHKETWYTGSRSA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62422571 211 LVGGTTMIIDHVVPEPGSSLLTSFEKWHEAADTKSCCDYSLHvditswyDGVREELEVLVQ--DKGVNSF-QVYMAyKDV 287
Cdd:PRK02382 82 AAGGVTTVVDQPNTDPPTVDGESFDEKAELAARKSIVDFGIN-------GGVTGNWDPLESlwERGVFALgEIFMA-DST 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62422571 288 YQMS-DSQLY-EAFTFLKGLGAVILVHAENGDLIAqEQKRILEmGITGPEGHALSRPEELEAEAVFRAITIAGRINCPVY 365
Cdd:PRK02382 154 GGMGiDEELFeEALAEAARLGVLATVHAEDEDLFD-ELAKLLK-GDADADAWSAYRPAAAEAAAVERALEVASETGARIH 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62422571 366 ITKVmskSAADIIALARKKGPLVFGEPIAASLGTDgthywskNWAKAAAFV-TSPPLSPDPTTpDYLTSLLACGDLQVTG 444
Cdd:PRK02382 232 IAHI---STPEGVDAARREGITCEVTPHHLFLSRR-------DWERLGTFGkMNPPLRSEKRR-EALWERLNDGTIDVVA 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62422571 445 SGHCPYSTAQKAVG-KDnftlIPEGVNGIEERMTVVWdKAVATGKMDENQFVAVTSTNAAKIFNLyPRKGRIAVGSDADV 523
Cdd:PRK02382 301 SDHAPHTREEKDADiWD----APSGVPGVETMLPLLL-AAVRKNRLPLERVRDVTAANPARIFGL-DGKGRIAEGYDADL 374
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 62422571 524 VIWDPDKLKTITAKSHKSAVEYNIFEGMEchGS-PLVVISQGKIVFEDGNINVNKGMGRFIPRK 586
Cdd:PRK02382 375 VLVDPDAAREIRGDDLHSKAGWTPFEGME--GVfPELTMVRGTVVWDGDDINAKRGRGEFLRGR 436
|
|
| allantoinase |
TIGR03178 |
allantoinase; This enzyme carries out the first step in the degradation of allantoin, a ... |
131-584 |
9.13e-54 |
|
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: 191.06 E-value: 9.13e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62422571 131 LLIKGGRIINDDQSLYADVYLEDGLIKQIGENlIVPGGVKTIEANGRMVIPGGIDVNTYLQKPsqGMTAADDFFQGTRAA 210
Cdd:TIGR03178 2 LIIRGGRVILPNGEREADVGVKGGKIAAIGPD-ILGPAAKIIDAGGLVVFPGVVDTHVHINEP--GRTEWEGFETGTRAA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62422571 211 LVGGTTMIIDhvVP---EPGSSLLTSFEKWHEAADTKsccdysLHVDITSWYDGVREELEVL--VQDKGVNSFQVYMAY- 284
Cdd:TIGR03178 79 AAGGITTYID--MPlnsIPATTTRASLEAKFEAAKGK------LAVDVGFWGGLVPYNLDDLreLDEAGVVGFKAFLSPs 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62422571 285 --KDVYQMSDSQLYEAFTFLKGLGAVILVHAENGDLIAQEQKRILEMGITGPEGHALSRPEELEAEAVFRAITIAGRINC 362
Cdd:TIGR03178 151 gdDEFPHVDDWQLYKGMRELARLGQLLLVHAENPAITSALGEEAPPQGGVGADAYLASRPVFAEVEAIRRTLALAKVTGC 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62422571 363 PVYITKVMSKSAADIIALARKKGPLVFGEPIaaslgtdgTHYWSKNWAK----AAAFVTSPPLSpDPTTPDYLTSLLACG 438
Cdd:TIGR03178 231 RVHVVHLSSAEAVELITEAKQEGLDVTVETC--------PHYLTLTAEEvpdgGTLAKCAPPIR-DLANQEGLWEALLNG 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62422571 439 DLQVTGSGHCPYSTAQKAvgKDNFTLIPEGVNGIEERMTVVWDKAVATGKMDENQFVAVTSTNAAKIFNLyPRKGRIAVG 518
Cdd:TIGR03178 302 LIDCVVSDHSPCTPDLKR--AGDFFKAWGGIAGLQSTLDVMFDEAVQKRGLPLEDIARLMATNPAKRFGL-AQKGRIAPG 378
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 62422571 519 SDADVVIWDPDKLKTITAKSHKSAVEYNIFEGMECHGSPLVVISQGKIVFEDGNInVNKGMGRFIP 584
Cdd:TIGR03178 379 KDADFVFVDPDESYTLTPDDLYYRHKVSPYVGRTIGGRVRATYLRGQCIYDDEQF-IGAPKGQLLL 443
|
|
| PRK06189 |
PRK06189 |
allantoinase; Provisional |
131-574 |
3.98e-48 |
|
allantoinase; Provisional
Pssm-ID: 235732 [Multi-domain] Cd Length: 451 Bit Score: 175.66 E-value: 3.98e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62422571 131 LLIKGGRIINDDQSLYADVYLEDGLIKQIGENLIVPGGvKTIEANGRMVIPGGIDVNTYLQKPsqGMTAADDFFQGTRAA 210
Cdd:PRK06189 5 LIIRGGKVVTPEGVYRADIGIKNGKIAEIAPEISSPAR-EIIDADGLYVFPGMIDVHVHFNEP--GRTHWEGFATGSAAL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62422571 211 LVGGTTMIIDhvVPEPGS-SLLT--SFEKWHEAADTKSCCDYSLHVDITSwydGVREELEVLVqDKGVNSFQVYMAYK-- 285
Cdd:PRK06189 82 AAGGCTTYFD--MPLNSIpPTVTreALDAKAELARQKSAVDFALWGGLVP---GNLEHLRELA-EAGVIGFKAFMSNSgt 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62422571 286 DVYQMSDSQ-LYEAFTFLKGLGAVILVHAENGDLIAQEQKRILEMGITGPEGHALSRPEELEAEAVFRAITIAGRINCPV 364
Cdd:PRK06189 156 DEFRSSDDLtLYEGMKEIAALGKILALHAESDALTRHLTTQARQQGKTDVRDYLESRPVVAELEAVQRALLYAQETGCPL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62422571 365 YITKVMSKSAADIIALARKKG--------P--LVFGEPIAASLGTdgthywsknWAKAAafvtsPPLSpDPTTPDYLTSL 434
Cdd:PRK06189 236 HFVHISSGKAVALIAEAKKRGvdvsvetcPhyLLFTEEDFERIGA---------VAKCA-----PPLR-SRSQKEELWRG 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62422571 435 LACGDLQVTGSGHCPYSTAQKAvgKDNFTLIPEGVNGIEERMTVVWDKAVATGKMDENQFVAVTSTNAAKIFNLyPRKGR 514
Cdd:PRK06189 301 LLAGEIDMISSDHSPCPPELKE--GDDFFLVWGGISGGQSTLLVMLTEGYIERGIPLETIARLLATNPAKRFGL-PQKGR 377
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 62422571 515 IAVGSDADVVIWDPDKLKTITAKSHKSAVEYNIFEGMECHGSPLVVISQGKIVFEDGNIN 574
Cdd:PRK06189 378 LEVGADADFVLVDLDETYTLTKEDLFYRHKQSPYEGRTFPGRVVATYLRGQCVYQDGEVF 437
|
|
| DHOase_IIb |
cd01318 |
Dihydroorotase (DHOase), subgroup IIb; DHOases catalyze the reversible interconversion of ... |
176-564 |
1.86e-40 |
|
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: 151.72 E-value: 1.86e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62422571 176 GRMVIPGGIDVNTYLQKPsqGMTAADDFFQGTRAALVGGTTMIIDHVVPEPGSSLLTSFEKWHEAADTKSCCDYSLHVDI 255
Cdd:cd01318 1 GLLILPGVIDIHVHFREP--GLTYKEDFVSGSRAAAAGGVTTVMDMPNTKPPTTTAEALYEKLRLAAAKSVVDYGLYFGV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62422571 256 TSWYDGvrEELEVLvqdkGVNSFQVYMAyKDVYQMSD--SQLYEAFtflKGLGAVILVHAENGDLIAQEQKRILEMGItg 333
Cdd:cd01318 79 TGSEDL--EELDKA----PPAGYKIFMG-DSTGDLLDdeETLERIF---AEGSVLVTFHAEDEDRLRENRKELKGESA-- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62422571 334 pegHALSRPEELEAEAVFRAITIAGRINCPVYITKVmskSAADIIALARKKGP----------LVFGEPIAASLGTdgth 403
Cdd:cd01318 147 ---HPRIRDAEAAAVATARALKLARRHGARLHICHV---STPEELKLIKKAKPgvtvevtphhLFLDVEDYDRLGT---- 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62422571 404 ywsknWAKaaafvTSPPLSpDPTTPDYLTSLLACGDLQVTGSGHCPYSTAQKAVGKDNftlIPEGVNGIEERMTVVWDkA 483
Cdd:cd01318 217 -----LGK-----VNPPLR-SREDRKALLQALADGRIDVIASDHAPHTLEEKRKGYPA---APSGIPGVETALPLMLT-L 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62422571 484 VATGKMDENQFVAVTSTNAAKIFNLyPRKGRIAVGSDADVVIWDPDKLKTITAKSHKSAVEYNIFEGMECHGSPLVVISQ 563
Cdd:cd01318 282 VNKGILSLSRVVRLTSHNPARIFGI-KNKGRIAEGYDADLTVVDLKEERTIRAEEFHSKAGWTPFEGFEVTGFPVMTIVR 360
|
.
gi 62422571 564 G 564
Cdd:cd01318 361 G 361
|
|
| pyrC |
PRK09357 |
dihydroorotase; Validated |
130-570 |
3.56e-37 |
|
dihydroorotase; Validated
Pssm-ID: 236479 [Multi-domain] Cd Length: 423 Bit Score: 144.18 E-value: 3.56e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62422571 130 RLLIKGGRIINDDQSLY-ADVYLEDGLIKQIGENLIVPGgVKTIEANGRMVIPGGIDVNTYLQKPsqGMTAADDFFQGTR 208
Cdd:PRK09357 2 MILIKNGRVIDPKGLDEvADVLIDDGKIAAIGENIEAEG-AEVIDATGLVVAPGLVDLHVHLREP--GQEDKETIETGSR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62422571 209 AALVGGTTMiidhVVPEPG-----SSLLTSFEKWHEAADTKSCcdyslHVD----ITswydgVREELEVLVQDKGVNSFQ 279
Cdd:PRK09357 79 AAAAGGFTT----VVAMPNtkpviDTPEVVEYVLDRAKEAGLV-----DVLpvgaIT-----KGLAGEELTEFGALKEAG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62422571 280 VYMAYKDVYQMSDSQL-YEAFTFLKGLGAVILVHAE----NGDLIAQEQKRILEMGITGpeghalsRPEELEAEAVFRAI 354
Cdd:PRK09357 145 VVAFSDDGIPVQDARLmRRALEYAKALDLLIAQHCEdpslTEGGVMNEGEVSARLGLPG-------IPAVAEEVMIARDV 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62422571 355 TIAGRINCPVYITKVMSKSAADIIALARKKGPlvfgePIAA------------SLGTDGTHYwsknwaKAAafvtsPPLS 422
Cdd:PRK09357 218 LLAEATGARVHICHVSTAGSVELIRWAKALGI-----KVTAevtphhllltdeDLLTYDPNY------KVN-----PPLR 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62422571 423 pDPTTPDYLTSLLACGDLQVTGSGHCPYSTAQKAVGkdnFTLIPEGVNGIEERMTVVWDKAVATGKMDENQFVAVTSTNA 502
Cdd:PRK09357 282 -TEEDREALIEGLKDGTIDAIATDHAPHAREEKECE---FEAAPFGITGLETALSLLYTTLVKTGLLDLEQLLEKMTINP 357
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 62422571 503 AKIFNLYPrkGRIAVGSDADVVIWDPDKLKTITAKSHKSAVEYNIFEGMECHGSPLVVISQGKIVFED 570
Cdd:PRK09357 358 ARILGLPA--GPLAEGEPADLVIFDPEAEWTVDGEDFASKGKNTPFIGMKLKGKVVYTIVDGKIVYQD 423
|
|
| PRK07575 |
PRK07575 |
dihydroorotase; Provisional |
128-574 |
3.57e-34 |
|
dihydroorotase; Provisional
Pssm-ID: 236055 [Multi-domain] Cd Length: 438 Bit Score: 135.57 E-value: 3.57e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62422571 128 SDRLLIKGGRIINDDQSLY-ADVYLEDGLIKQIGENLIVPGGVKTIEANGRMVIPGGIDVNTYLQKPsqGMTAADDFFQG 206
Cdd:PRK07575 2 MMSLLIRNARILLPSGELLlGDVLVEDGKIVAIAPEISATAVDTVIDAEGLTLLPGVIDPQVHFREP--GLEHKEDLFTA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62422571 207 TRAALVGGTTMIIDHVVPEPgssLLTSFEKWHEA---ADTKSCCDYSLHVDITSwydgvrEELEVLVQDKGVNSFQVYMA 283
Cdd:PRK07575 80 SRACAKGGVTSFLEMPNTKP---LTTTQAALDDKlarAAEKCVVNYGFFIGATP------DNLPELLTANPTCGIKIFMG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62422571 284 YKDVYQMSDSQLYEAFTFLKGlGAVILVHAENgdliaqeQKRILE-----MGITGPEGHALSRPEELEAEAVFRAITIAG 358
Cdd:PRK07575 151 SSHGPLLVDEEAALERIFAEG-TRLIAVHAED-------QARIRArraefAGISDPADHSQIQDEEAALLATRLALKLSK 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62422571 359 RINCPVYITKVmsKSAADIIALARKKGPLVFGE--PIAASLGTDgthywskNWAKAAAFV-TSPPLSpDPTTPDYLTSLL 435
Cdd:PRK07575 223 KYQRRLHILHL--STAIEAELLRQDKPSWVTAEvtPQHLLLNTD-------AYERIGTLAqMNPPLR-SPEDNEALWQAL 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62422571 436 ACGDLQVTGSGHCPYSTAQKAVGKDNftlIPEGVNGIEERMTVVWDKAVAtGKMDENQFVAVTSTNAAKIFNLyPRKGRI 515
Cdd:PRK07575 293 RDGVIDFIATDHAPHTLEEKAQPYPN---SPSGMPGVETSLPLMLTAAMR-GKCTVAQVVRWMSTAVARAYGI-PNKGRI 367
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 62422571 516 AVGSDADVVIWDPDKLKTITAKSHKSAVEYNIFEGMECHGSPLVVISQGKIVFEDGNIN 574
Cdd:PRK07575 368 APGYDADLVLVDLNTYRPVRREELLTKCGWSPFEGWNLTGWPVTTIVGGQIVFDRGQVN 426
|
|
| PRK08044 |
PRK08044 |
allantoinase AllB; |
131-529 |
2.13e-33 |
|
allantoinase AllB;
Pssm-ID: 169193 [Multi-domain] Cd Length: 449 Bit Score: 133.83 E-value: 2.13e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62422571 131 LLIKGGRIINDDQSLYADVYLEDGLIKQIGENLivPGGVKTIEANGRMVIPGGIDVNTYLQKPsqGMTAADDFFQGTRAA 210
Cdd:PRK08044 5 LIIKNGTVILENEARVVDIAVKGGKIAAIGQDL--GDAKEVMDASGLVVSPGMVDAHTHISEP--GRSHWEGYETGTRAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62422571 211 LVGGTTMIIDHVVPE-PGSSLLTSFEKWHEAADTKSCCDYSLHVDITSW-YDGVREELEVlvqdkGVNSFQVYMAY---- 284
Cdd:PRK08044 81 AKGGITTMIEMPLNQlPATVDRASIELKFDAAKGKLTIDAAQLGGLVSYnLDRLHELDEV-----GVVGFKCFVATcgdr 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62422571 285 ---KDVYQMSDSQLYEAFTFLKGLGAVILVHAENG---DLIAQEQKRileMGITGPEGHALSRPEELEAEAVFRAITIAG 358
Cdd:PRK08044 156 gidNDFRDVNDWQFYKGAQKLGELGQPVLVHCENAlicDELGEEAKR---EGRVTAHDYVASRPVFTEVEAIRRVLYLAK 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62422571 359 RINCPVYITKVMSKSAADIIALARKKGPLVFGEPIaaslgtdgTHYWSKNWAKAAAFVT----SPPLSpDPTTPDYLTSL 434
Cdd:PRK08044 233 VAGCRLHVCHISSPEGVEEVTRARQEGQDVTCESC--------PHYFVLDTDQFEEIGTlakcSPPIR-DLENQKGMWEK 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62422571 435 LACGDLQVTGSGHCPYSTAQKAvgkDNFTLIPEGVNGIEERMTVVWDKAVATGKMDENQFVAVTSTNAAKIFNLyPRKGR 514
Cdd:PRK08044 304 LFNGEIDCLVSDHSPCPPEMKA---GNIMEAWGGIAGLQNCMDVMFDEAVQKRGMSLPMFGKLMATNAADIFGL-QQKGR 379
|
410
....*....|....*
gi 62422571 515 IAVGSDADVVIWDPD 529
Cdd:PRK08044 380 IAPGKDADFVFIQPN 394
|
|
| DHOase_IIa |
cd01317 |
Dihydroorotase (DHOase), subgroup IIa; DHOases catalyze the reversible interconversion of ... |
168-558 |
1.88e-32 |
|
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: 129.28 E-value: 1.88e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62422571 168 GVKTIEANGRMVIPGGIDVNTYLQKPSQgmTAADDFFQGTRAALVGGTTMII--DHVVPEPGSSLLTSFEKwHEAADTKS 245
Cdd:cd01317 1 DAEVIDAEGKILAPGLVDLHVHLREPGF--EYKETLESGAKAAAAGGFTTVVcmPNTNPVIDNPAVVELLK-NRAKDVGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62422571 246 CCDYSLhVDITSWYDGVR-EELEVLVqDKGVNSFqvymAYKDVYQMSDSQLYEAFTFLKGLGAVILVHAENGDL----IA 320
Cdd:cd01317 78 VRVLPI-GALTKGLKGEElTEIGELL-EAGAVGF----SDDGKPIQDAELLRRALEYAAMLDLPIIVHPEDPSLagggVM 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62422571 321 QEQKRILEMGITGpeghalsRPEELEAEAVFRAITIAGRINCPVYITKVMSKSAADIIALARKKGPLVFGEPIAASL--- 397
Cdd:cd01317 152 NEGKVASRLGLPG-------IPPEAETIMVARDLELAEATGARVHFQHLSTARSLELIRKAKAKGLPVTAEVTPHHLlld 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62422571 398 GTDGTHYwsknwakAAAFVTSPPLSpDPTTPDYLTSLLACGDLQVTGSGHCPYSTAQKAVGkdnFTLIPEGVNGIEERMT 477
Cdd:cd01317 225 DEALESY-------DTNAKVNPPLR-SEEDREALIEALKDGTIDAIASDHAPHTDEEKDLP---FAEAPPGIIGLETALP 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62422571 478 VVWDKAVATGKMDENQFVAVTSTNAAKIFNLYPrkGRIAVGSDADVVIWDPDKLKTITAKSHKSAVEYNIFEGMECHGSP 557
Cdd:cd01317 294 LLWTLLVKGGLLTLPDLIRALSTNPAKILGLPP--GRLEVGAPADLVLFDPDAEWIVDEETFRSKSKNTPFDGQKLKGRV 371
|
.
gi 62422571 558 L 558
Cdd:cd01317 372 L 372
|
|
| PLN02795 |
PLN02795 |
allantoinase |
136-574 |
3.57e-27 |
|
allantoinase
Pssm-ID: 178392 [Multi-domain] Cd Length: 505 Bit Score: 116.03 E-value: 3.57e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62422571 136 GRIINDDQSLYADVYLEDGLIKQIGENLIVPG---GVKTIEANGRMVIPGGIDVNTYLQKPsqGMTAADDFFQGTRAALV 212
Cdd:PLN02795 51 KRVVTPAGVIPGAVEVEGGRIVSVTKEEEAPKsqkKPHVLDYGNAVVMPGLIDVHVHLNEP--GRTEWEGFPTGTKAAAA 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62422571 213 GGTTMIIDhvVP---EPGSSLLTSFEKWHEAADTKsccdysLHVDITSWYDGVRE------ELEVLVqDKGVNSFQVYM- 282
Cdd:PLN02795 129 GGITTLVD--MPlnsFPSTTSVETLELKIEAAKGK------LYVDVGFWGGLVPEnahnasVLEELL-DAGALGLKSFMc 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62422571 283 --AYKDVYQMSDSQLYEAFTFLKGLGAVILVHAENGDLIAQEQKriLEMGITGPEGHALSRPEELEAEAVFRAITIAGRI 360
Cdd:PLN02795 200 psGINDFPMTTATHIKAALPVLAKYGRPLLVHAEVVSPVESDSR--LDADPRSYSTYLKSRPPSWEQEAIRQLLEVAKDT 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62422571 361 N-------CPVYITKVM-SKSAADIIALARKKGPLVFGEPIAaslgtdgtHYWsknwAKAAA--------FVTSPPLSpD 424
Cdd:PLN02795 278 RpggvaegAHVHIVHLSdAESSLELIKEAKAKGDSVTVETCP--------HYL----AFSAEeipdgdtrYKCAPPIR-D 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62422571 425 PTTPDYLTSLLACGDLQVTGSGHCPYSTAQKAVGKDNFTLIPEGVNGIEERMTVVWDKAVATGkMDENQFVAVTSTNAAK 504
Cdd:PLN02795 345 AANRELLWKALLDGDIDMLSSDHSPSPPDLKLLEEGNFLRAWGGISSLQFVLPATWTAGRAYG-LTLEQLARWWSERPAK 423
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 62422571 505 IFNLyPRKGRIAVGSDADVVIWDP------DKLKTITAKsHKSAVEYNifeGMECHGSPLVVISQGKIVFEDGNIN 574
Cdd:PLN02795 424 LAGL-DSKGAIAPGKDADIVVWDPeaefvlDESYPIYHK-HKSLSPYL---GTKLSGKVIATFVRGNLVFLEGKHA 494
|
|
| PRK04250 |
PRK04250 |
dihydroorotase; Provisional |
136-583 |
8.45e-26 |
|
dihydroorotase; Provisional
Pssm-ID: 235265 [Multi-domain] Cd Length: 398 Bit Score: 110.24 E-value: 8.45e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62422571 136 GRIINDDQSLYADVYLEDGLIKQIGENLIvpGGVKTIEANGRMVIPGGIDVNTYLQkpsqgmtaadDFFQ--------GT 207
Cdd:PRK04250 4 GKFLLKGRIVEGGIGIENGRISKISLRDL--KGKEVIKVKGGIILPGLIDVHVHLR----------DFEEsyketiesGT 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62422571 208 RAALVGGTTMIIDHVVPEPGSSLLTSFEKWHEAADTKSCCDYSLHVDITSWYDGVREELEvlvqdkgvNSFQVYM--AYK 285
Cdd:PRK04250 72 KAALHGGITLVFDMPNTKPPIMDEKTYEKRMRIAEKKSYADYALNFLIAGNCEKAEEIKA--------DFYKIFMgaSTG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62422571 286 DVYQMSDSQLYEAftflkgLGAVILVHAENGDLIAQEqkrilemgitgPEghalsRPEELEAEAVFRAITIAGRINCPVY 365
Cdd:PRK04250 144 GIFSENFEVDYAC------APGIVSVHAEDPELIREF-----------PE-----RPPEAEVVAIERALEAGKKLKKPLH 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62422571 366 ITKVMSKSAADIIalARKKGPLVFGEPIAASLgtdgtHYWSKNWAKAAAFVTSPPLSpdpTTPDYLTSLLACGDLQVTGS 445
Cdd:PRK04250 202 ICHISTKDGLKLI--LKSNLPWVSFEVTPHHL-----FLTRKDYERNPLLKVYPPLR---SEEDRKALWENFSKIPIIAS 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62422571 446 GHCPYSTAQKAVGKdnftlipEGVNGIEERMTVVWDkAVATGKMDENQFVAVTSTNAAKIFNlYPRKGrIAVGSDADVVI 525
Cdd:PRK04250 272 DHAPHTLEDKEAGA-------AGIPGLETEVPLLLD-AANKGMISLFDIVEKMHDNPARIFG-IKNYG-IEEGNYANFAV 341
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 62422571 526 WDPDKLKTITAKSHKSAVEYNIFEGMECHGSPLVVISQGKIVFEDGNInVNKGMGRFI 583
Cdd:PRK04250 342 FDMKKEWTIKAEELYTKAGWTPYEGFKLKGKVIMTILRGEVVMEDDEI-IGKPRGVRI 398
|
|
| PRK01211 |
PRK01211 |
dihydroorotase; Provisional |
146-585 |
1.05e-24 |
|
dihydroorotase; Provisional
Pssm-ID: 179247 [Multi-domain] Cd Length: 409 Bit Score: 107.25 E-value: 1.05e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62422571 146 YADVYLEDGLIKQIGENLivpGGVKTIEANGrMVIPGGIDVNTYLQKPsqGMTAADDFFQGTRAALVGGTTMIIDHVVPE 225
Cdd:PRK01211 15 YLEIEVEDGKIKSIKKDA---GNIGKKELKG-AILPAATDIHVHFRTP--GETEKEDFSTGTLSAIFGGTTFIMDMPNNN 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62422571 226 PGSSLLTSFEKWHEAADTKSCCDYSLHVDITSwydgvreeLEVLVQDKGVNSFQVYMAYKDVYQMSDSQLYEAfTFLKGL 305
Cdd:PRK01211 89 IPIKDYNAFSDKLGRVAPKAYVDFSLYSMETG--------NNALILDERSIGLKVYMGGTTNTNGTDIEGGEI-KKINEA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62422571 306 GAVILVHAENGDLIAQ---EQKRILEmgitgpegHALSRPEELEAEAVfraitiaGRINCPVYITKVMS-KSAADIIA-L 380
Cdd:PRK01211 160 NIPVFFHAELSECLRKhqfESKNLRD--------HDLARPIECEIKAV-------KYVKNLDLKTKIIAhVSSIDVIGrF 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62422571 381 ARKKGP--LVFGEPIaaSLGTDGThywsknwakaaafvTSPPLSPDPTTPDYLTSLLAcGDLQVTGSGHCPYSTAQKAvg 458
Cdd:PRK01211 225 LREVTPhhLLLNDDM--PLGSYGK--------------VNPPLRDRWTQERLLEEYIS-GRFDILSSDHAPHTEEDKQ-- 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62422571 459 kdNFTLIPEGVNGIEERMTVVWdKAVATGKMDENQFVAVTSTNAAKIFNLypRKGRIAVGSDADVVIWDPDKLKTITAKS 538
Cdd:PRK01211 286 --EFEYAKSGIIGVETRVPLFL-ALVKKKILPLDVLYKTAIERPASLFGI--KKGKIEEGYDADFMAFDFTNIKKINDKR 360
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 62422571 539 HKSAVEYNIFEGMECHgSPLVVISQGKIVFEDGNInVNKGMGRFIPR 585
Cdd:PRK01211 361 LHSKCPVSPFNGFDAI-FPSHVIMRGEVVIDNYEL-ISERTGKFVPK 405
|
|
| PRK09060 |
PRK09060 |
dihydroorotase; Validated |
131-581 |
8.92e-23 |
|
dihydroorotase; Validated
Pssm-ID: 181632 [Multi-domain] Cd Length: 444 Bit Score: 101.92 E-value: 8.92e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62422571 131 LLIKGGRIINDDQSLYADVYLEDGLIKQIGENLIVPGGvKTIEANGRMVIPGGIDVNTYLQKPsqGMTAADDFFQGTRAA 210
Cdd:PRK09060 7 LILKGGTVVNPDGEGRADIGIRDGRIAAIGDLSGASAG-EVIDCRGLHVLPGVIDSQVHFREP--GLEHKEDLETGSRAA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62422571 211 LVGGTTMIIDHVVPEPGSSLLTSFEKWHEAADTKSCCDYSLHVDITSwyDGVRE--ELEVLvqdKGVNSFQVYM--AYKD 286
Cdd:PRK09060 84 VLGGVTAVFEMPNTNPLTTTAEALADKLARARHRMHCDFAFYVGGTR--DNADElaELERL---PGCAGIKVFMgsSTGD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62422571 287 VYQMSDSQLYEAftfLKGLGAVILVHAENgDLIAQEQKRILEMGitGPEGHALSRPEELEAEAVFRAITIAGRINCPVYI 366
Cdd:PRK09060 159 LLVEDDEGLRRI---LRNGRRRAAFHSED-EYRLRERKGLRVEG--DPSSHPVWRDEEAALLATRRLVRLARETGRRIHV 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62422571 367 TKVmskSAADIIA-LARKKG-------P--LVFGEPIA-ASLGTdgthYWSKNwakaaafvtsPPLSpDPTTPDYLTSLL 435
Cdd:PRK09060 233 LHV---STAEEIDfLADHKDvatvevtPhhLTLAAPECyERLGT----LAQMN----------PPIR-DARHRDGLWRGV 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62422571 436 ACGDLQVTGSGHCPYSTAQKAvgkDNFTLIPEGVNGIEERMTVVWDKaVATGKMDENQFVAVTSTNAAKIFNLyPRKGRI 515
Cdd:PRK09060 295 RQGVVDVLGSDHAPHTLEEKA---KPYPASPSGMTGVQTLVPIMLDH-VNAGRLSLERFVDLTSAGPARIFGI-AGKGRI 369
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 62422571 516 AVGSDADVVIWDPDKLKTITAKSHKSAVEYNIFEGMECHGSPLVVISQGKIVFEDGNInVNKGMGR 581
Cdd:PRK09060 370 AVGYDADFTIVDLKRRETITNEWIASRCGWTPYDGKEVTGWPVGTIVRGQRVMWDGEL-VGPPTGE 434
|
|
| Amidohydro_1 |
pfam01979 |
Amidohydrolase family; This family of enzymes are a a large metal dependent hydrolase ... |
178-567 |
1.55e-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: 90.25 E-value: 1.55e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62422571 178 MVIPGGIDVNTYLQ------KPSQGMTAADDFFQGTRAALVGGTTMIIDHvvpepGSSLLTSFEKWHEAAD--------- 242
Cdd:pfam01979 1 IVLPGLIDAHVHLEmgllrgIPVPPEFAYEALRLGITTMLKSGTTTVLDM-----GATTSTGIEALLEAAEelplglrfl 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62422571 243 TKSCC---DYSLHVDITSWyDGVREELEVLVQDKGVNsFQVYMAYKDVYQMSDSQLYEAFTFLKGLGAVILVHAENGDLI 319
Cdd:pfam01979 76 GPGCSldtDGELEGRKALR-EKLKAGAEFIKGMADGV-VFVGLAPHGAPTFSDDELKAALEEAKKYGLPVAIHALETKGE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62422571 320 AQEQKRIlemgitgpeghalsrpeeleaeavfraitIAGRINCPVYITKVMSKSAADIIALARKkgplvfgepiaaslgt 399
Cdd:pfam01979 154 VEDAIAA-----------------------------FGGGIEHGTHLEVAESGGLLDIIKLILA---------------- 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62422571 400 DGTHYWSKNWAKAAAFVTSPPLSPDPTTPDYLTS-------LLACGDLQVTGSGHCpystaqkaVGKDNFTLIPEGVNGI 472
Cdd:pfam01979 189 HGVHLSPTEANLLAEHLKGAGVAHCPFSNSKLRSgrialrkALEDGVKVGLGTDGA--------GSGNSLNMLEELRLAL 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62422571 473 EERmtvvwdkAVATGKMDENQFVAVTSTNAAKIFNLYPRKGRIAVGSDADVVIWDPDKLktitakshksaveyNIFEGME 552
Cdd:pfam01979 261 ELQ-------FDPEGGLSPLEALRMATINPAKALGLDDKVGSIEVGKDADLVVVDLDPL--------------AAFFGLK 319
|
410
....*....|....*
gi 62422571 553 CHGSPLVVISQGKIV 567
Cdd:pfam01979 320 PDGNVKKVIVKGKIV 334
|
|
| PRK09236 |
PRK09236 |
dihydroorotase; Reviewed |
129-574 |
9.03e-17 |
|
dihydroorotase; Reviewed
Pssm-ID: 181716 Cd Length: 444 Bit Score: 83.38 E-value: 9.03e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62422571 129 DRLLIKGGRIINDDQSLYADVYLEDGLIKQIGENLIVPGGVKTIEANGRMVIPGGIDVNTYLQKPsqGMTAADDFFQGTR 208
Cdd:PRK09236 2 KRILIKNARIVNEGKIFEGDVLIENGRIAKIASSISAKSADTVIDAAGRYLLPGMIDDQVHFREP--GLTHKGDIASESR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62422571 209 AALVGGTTMIID--HVVPePGSSLLTSFEKWHEAAdTKSCCDYSLHVDITSwyDGVrEELEVLvqDK----GVNSFqvym 282
Cdd:PRK09236 80 AAVAGGITSFMEmpNTNP-PTTTLEALEAKYQIAA-QRSLANYSFYFGATN--DNL-DEIKRL--DPkrvcGVKVF---- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62422571 283 aykdvyqMSDS---QLYEAFTFLKGLGA----VILVHAENGDLI-AQEQKRILEMG--ITgPEGHALSRpeelEAEAVFR 352
Cdd:PRK09236 149 -------MGAStgnMLVDNPETLERIFRdaptLIATHCEDTPTIkANLAKYKEKYGddIP-AEMHPLIR----SAEACYK 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62422571 353 ----AITIAGRINcpvyiTK--VMSKSAADIIALARkKGPLVfGEPIAASLGTDGTHYWSKNWAKAAAFVTSPPLSPDPT 426
Cdd:PRK09236 217 ssslAVSLAKKHG-----TRlhVLHISTAKELSLFE-NGPLA-EKRITAEVCVHHLWFDDSDYARLGNLIKCNPAIKTAS 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62422571 427 TPDYLTSLLACGDLQVTGSGHCPYSTAQKAVGkdnFTLIPEGVNGIEERMTVVWDKaVATGKMDENQFVAVTSTNAAKIF 506
Cdd:PRK09236 290 DREALRQALADDRIDVIATDHAPHTWEEKQGP---YFQAPSGLPLVQHALPALLEL-VHEGKLSLEKVVEKTSHAPAILF 365
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 62422571 507 NLyPRKGRIAVGSDADVVIWDPDKLKTITAKSHKSAVEYNIFEGMECHGSPLVVISQGKIVFEDGNIN 574
Cdd:PRK09236 366 DI-KERGFIREGYWADLVLVDLNSPWTVTKENILYKCGWSPFEGRTFRSRVATTFVNGQLVYHNGQLV 432
|
|
| CAD_DHOase |
cd01316 |
The eukaryotic CAD protein is a trifunctional enzyme of carbamoylphosphate ... |
180-580 |
2.18e-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: 77.88 E-value: 2.18e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62422571 180 IPGGIDVNTYLQKPsqGMTAADDFFQGTRAALVGGTTMIidHVVPEPGSSLL--TSFEKWHEAADTKSCCDYSLHVDITS 257
Cdd:cd01316 5 LPGLIDVHVHLREP--GATHKEDFASGTKAALAGGFTMV--RAMPNTNPSIVdvASLKLVQSLAQAKARCDYAFSIGATS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62422571 258 WYDGVREELevlvQDKGVNSFQVYMAYKDVYQMSD-SQLYEAFTFLKGLGAVIlVHAENGDLIAqeqkrILEMgitgpeG 336
Cdd:cd01316 81 TNAATVGEL----ASEAVGLKFYLNETFSTLILDKiTAWASHFNAWPSTKPIV-THAKSQTLAA-----VLLL------A 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62422571 337 HALSRpeeleaeavfraitiagrincPVYITKVMSKSAADIIALARKKGPLVFGEPIAASLgtdgthYWSKNWAKAAAFV 416
Cdd:cd01316 145 SLHNR---------------------SIHICHVSSKEEINLIRLAKARGLKVTCEVSPHHL------FLSQDDLPRGQYE 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62422571 417 TSPPLsPDPTTPDYLTSLLACGDlqVTGSGHCPYSTAQKAVGKdnftlIPEGVNGIEERMTVVWdKAVATGKMDENQFVA 496
Cdd:cd01316 198 VRPFL-PTREDQEALWENLDYID--CFATDHAPHTLAEKTGNK-----PPPGFPGVETSLPLLL-TAVHEGRLTIEDIVD 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62422571 497 VTSTNAAKIFNLYPrkgriavgsDADVVI-WDPDKLKTITAKSHKSAVEYNIFEGMECHGSPLVVISQGKIVFEDGNINV 575
Cdd:cd01316 269 RLHTNPKRIFNLPP---------QSDTYVeVDLDEEWTIPKNPLQSKKGWTPFEGKKVKGKVQRVVLRGETAFIDGEIVA 339
|
....*
gi 62422571 576 NKGMG 580
Cdd:cd01316 340 PPGFG 344
|
|
| pyrC |
PRK00369 |
dihydroorotase; Provisional |
148-587 |
2.29e-13 |
|
dihydroorotase; Provisional
Pssm-ID: 234738 [Multi-domain] Cd Length: 392 Bit Score: 72.49 E-value: 2.29e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62422571 148 DVYLEDGlIKQIGENLIVpgGVKTIEANGR---------MVIPGGIDVNTYLQkpsqGMTAA--DDFFQGTRAALVGGTT 216
Cdd:PRK00369 8 KAYLGKE-IKEICINFDR--RIKEIKSRCKpdldlpqgtLILPGAIDLHVHLR----GLKLSykEDVASGTSEAAYGGVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62422571 217 MIID--HVVPePGSSLLTSFEKWHEAADtKSCCDYSLhvditswYDGVREELEVLvqDK-GVNSFQVYMaykdvyqmSDS 293
Cdd:PRK00369 81 LVADmpNTIP-PLNTPEAITEKLAELEY-YSRVDYFV-------YSGVTKDPEKV--DKlPIAGYKIFP--------EDL 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62422571 294 QLYEAFTFLKGLGAVILVHAENGDLIAQEQKrilemgitgpeghaLSRPEELEAEAVFraiTIAGRINcpVYITKVmskS 373
Cdd:PRK00369 142 EREETFRVLLKSRKLKILHPEVPLALKSNRK--------------LRRNCWYEIAALY---YVKDYQN--VHITHA---S 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62422571 374 AADIIALARKKGplvfgepiaasLGTDGT-HYWSKNWAKAAAFVTSPPLSpDPTTPDYLTSLLACGDLQVtgSGHCPYST 452
Cdd:PRK00369 200 NPRTVRLAKELG-----------FTVDITpHHLLVNGEKDCLTKVNPPIR-DINERLWLLQALSEVDAIA--SDHAPHSS 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62422571 453 AQKavgKDNFTLIPEGVNGIEERMTVVWdKAVATGKMDENQFVAVTSTNAAKIFNLypRKGRIAVGSDADVVI--WDPDK 530
Cdd:PRK00369 266 FEK---LQPYEVCPPGIAALSFTPPFIY-TLVSKGILSIDRAVELISTNPARILGI--PYGEIKEGYRANFTViqFEDWR 339
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 62422571 531 LKTITAKshksaVEYNIFEGMECHGSPLVVISQGKIVFEDGNINVNKGMGRFIPRKA 587
Cdd:PRK00369 340 YSTKYSK-----VIETPLDGFELKASVYATIVQGKLAYLEGEVFPVKGINPFGERKR 391
|
|
| HutI |
COG1228 |
Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport ... |
127-570 |
2.12e-10 |
|
Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440841 [Multi-domain] Cd Length: 386 Bit Score: 63.06 E-value: 2.12e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62422571 127 QSDRLLIKGGRIIN-DDQSLY--ADVYLEDGLIKQIGEN--LIVPGGVKTIEANGRMVIPGGIDVNTYL---------QK 192
Cdd:COG1228 6 QAGTLLITNATLVDgTGGGVIenGTVLVEDGKIAAVGPAadLAVPAGAEVIDATGKTVLPGLIDAHTHLglgggraveFE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62422571 193 PSQGMTAADDFFQGT----RAALVGGTTMIIDHvvpePGSSL----------LTSFEKWH-EAADTKSCCDYSLHvdiTS 257
Cdd:COG1228 86 AGGGITPTVDLVNPAdkrlRRALAAGVTTVRDL----PGGPLglrdaiiageSKLLPGPRvLAAGPALSLTGGAH---AR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62422571 258 WYDGVREELEVLVQDkGVNSFQVYMAYKDvYQMSDSQLYEAFTFLKGLGAVILVHAENGDLIaqeqKRILEMGITGPEgH 337
Cdd:COG1228 159 GPEEARAALRELLAE-GADYIKVFAEGGA-PDFSLEELRAILEAAHALGLPVAAHAHQADDI----RLAVEAGVDSIE-H 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62422571 338 ALSRPEEleaeavfraitiagrincpvyitkvmsksaadIIALARKKGPLVfgepiaaslgtdgthywsknwakaaafvt 417
Cdd:COG1228 232 GTYLDDE--------------------------------VADLLAEAGTVV----------------------------- 250
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62422571 418 sppLSPDPTTPDYLTSLLACGDLQVTGSGHC-PYSTAQK--------AVGKDNFTLIPEGVNGIEErmtvvWDKAVATGk 488
Cdd:COG1228 251 ---LVPTLSLFLALLEGAAAPVAAKARKVREaALANARRlhdagvpvALGTDAGVGVPPGRSLHRE-----LALAVEAG- 321
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62422571 489 MDENQ-FVAVTStNAAKIFNLYPRKGRIAVGSDADVVIWDPDKLKTITAkshksaveynifegmecHGSPLVVISQGKIV 567
Cdd:COG1228 322 LTPEEaLRAATI-NAAKALGLDDDVGSLEPGKLADLVLLDGDPLEDIAY-----------------LEDVRAVMKDGRVV 383
|
...
gi 62422571 568 FED 570
Cdd:COG1228 384 DRS 386
|
|
| PRK07369 |
PRK07369 |
dihydroorotase; Provisional |
147-541 |
4.59e-10 |
|
dihydroorotase; Provisional
Pssm-ID: 236002 [Multi-domain] Cd Length: 418 Bit Score: 62.31 E-value: 4.59e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62422571 147 ADVYLEDGLIKQIGENLI-VPGGVKTIEANGRMVIPGGIDVNTYLQKPsqGMTAADDFFQGTRAALVGGTTMI------- 218
Cdd:PRK07369 22 ADVLIEDGKIQAIEPHIDpIPPDTQIIDASGLILGPGLVDLYSHSGEP--GFEERETLASLAAAAAAGGFTRVailpdtf 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62422571 219 --IDHvvPEPGSSLLTSFE-----KWHE-AADTKSCCDYSLhvdiTSWYDgvreelevLVQdKGVNSFqvymaykdvyqm 290
Cdd:PRK07369 100 ppLDN--PATLARLQQQAQqippvQLHFwGALTLGGQGKQL----TELAE--------LAA-AGVVGF------------ 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62422571 291 SDSQ-------LYEAFTFLKGLGAVILVHAENGDL----IAQEQKRILEMGITGpeghalsRPEELEAEAVFRAITIAGR 359
Cdd:PRK07369 153 TDGQplenlalLRRLLEYLKPLGKPVALWPCDRSLagngVMREGLLALRLGLPG-------DPASAETTALAALLELVAA 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62422571 360 INCPVYITKVMSKSAADIIALARKKGPlvfgePIAAS-------LGTDGTHYWSKNWAKAaafvtsPPLsPDPTTPDYLT 432
Cdd:PRK07369 226 IGTPVHLMRISTARSVELIAQAKARGL-----PITASttwmhllLDTEALASYDPNLRLD------PPL-GNPSDRQALI 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62422571 433 SLLACGDLQVTGSGHCPYSTAQKAVGkdnFTLIPEGVNGIEERMTVVWDKAVATGKMDENQFVAVTSTNAAKIFNLYPRk 512
Cdd:PRK07369 294 EGVRTGVIDAIAIDHAPYTYEEKTVA---FAEAPPGAIGLELALPLLWQNLVETGELSALQLWQALSTNPARCLGQEPP- 369
|
410 420
....*....|....*....|....*....
gi 62422571 513 gRIAVGSDADVVIWDPDKLKTITAKSHKS 541
Cdd:PRK07369 370 -SLAPGQPAELILFDPQKTWTVSAQTLHS 397
|
|
| NagA |
cd00854 |
N-acetylglucosamine-6-phosphate deacetylase, NagA, catalyzes the hydrolysis of the N-acetyl ... |
131-529 |
2.19e-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: 56.82 E-value: 2.19e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62422571 131 LLIKGGRIINDDQSLYADVYLEDGLIKQIGENLIVPGGVKTIEANGRMVIPGGIDVNTYlqkpsqG------MTAADDFF 204
Cdd:cd00854 1 LIIKNARILTPGGLEDGAVLVEDGKIVAIGPEDELEEADEIIDLKGQYLVPGFIDIHIH------GgggadfMDGTAEAL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62422571 205 QGTRAALV--GGTTMiidhvVPepgsSLLT-SFEKWHEAADtksccdyslhvditswydgvreelevlvqdkgvnsfqvy 281
Cdd:cd00854 75 KTIAEALAkhGTTSF-----LP----TTVTaPPEEIAKALA--------------------------------------- 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62422571 282 mAYKDVYQmsdsqlyeaftflKGLGAVIL-VHAEnGDLIAQEQKrilemgitG--PEGHALS-RPEELE-----AEAVFR 352
Cdd:cd00854 107 -AIAEAIA-------------EGQGAEILgIHLE-GPFISPEKK--------GahPPEYLRApDPEELKkwleaAGGLIK 163
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62422571 353 AITIAGRIncpvyitkvmsKSAADIIALARKKGplvfgepIAASLG-TDGTHYWSKNWAKAAA-FVT------SPPLSPD 424
Cdd:cd00854 164 LVTLAPEL-----------DGALELIRYLVERG-------IIVSIGhSDATYEQAVAAFEAGAtHVThlfnamSPLHHRE 225
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62422571 425 P-------TTPDYLTSLLAcgDLQvtgsgHCPYST---AQKAVGKDNFTLI---------PEGVNGIEERMTVVWDKAV- 484
Cdd:cd00854 226 PgvvgaalSDDDVYAELIA--DGI-----HVHPAAvrlAYRAKGADKIVLVtdamaaaglPDGEYELGGQTVTVKDGVAr 298
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 62422571 485 -ATG-------KMDE-------------NQFVAVTSTNAAKIFNLYPRKGRIAVGSDADVVIWDPD 529
Cdd:cd00854 299 lADGtlagstlTMDQavrnmvkwggcplEEAVRMASLNPAKLLGLDDRKGSLKPGKDADLVVLDDD 364
|
|
| D-aminoacylase |
cd01297 |
D-aminoacylases (N-acyl-D-Amino acid amidohydrolases) catalyze the hydrolysis of ... |
131-571 |
3.56e-08 |
|
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: 56.15 E-value: 3.56e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62422571 131 LLIKGGRIIndDQS----LYADVYLEDGLIKQIGENLIVPgGVKTIEANGRMVIPGGIDVNTYlqkpSQGMTAADDFFqg 206
Cdd:cd01297 2 LVIRNGTVV--DGTgappFTADVGIRDGRIAAIGPILSTS-AREVIDAAGLVVAPGFIDVHTH----YDGQVFWDPDL-- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62422571 207 TRAALVGGTTMIIDhvvpEPGSSLltsfekwheaadtksccdYSLHVDITSWYDGVREELEVLVQDKGVnSFQVYMAYKD 286
Cdd:cd01297 73 RPSSRQGVTTVVLG----NCGVSP------------------APANPDDLARLIMLMEGLVALGEGLPW-GWATFAEYLD 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62422571 287 VYQMSDSQLYEAFTFlkGLGAV-ILVHAENGDLIAQEQ----KRILE-------MGI-TG----PEGHAlsRPEELEAEA 349
Cdd:cd01297 130 ALEARPPAVNVAALV--GHAALrRAVMGLDAREATEEElakmRELLRealeagaLGIsTGlayaPRLYA--GTAELVALA 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62422571 350 vfraiTIAGRINCpVYITKVMSKSAA------DIIALARKKG-PLVFgepiaASLGTDGTHYWSKnWAKAAAFVTSPPLS 422
Cdd:cd01297 206 -----RVAARYGG-VYQTHVRYEGDSilealdELLRLGRETGrPVHI-----SHLKSAGAPNWGK-IDRLLALIEAARAE 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62422571 423 PDPTTPD---YLTSLLA-------------CGDLQVTGSGHC------PYSTAQKAVGKDNFTLiPEGVngieERMTvvw 480
Cdd:cd01297 274 GLQVTADvypYGAGSEDdvrrimahpvvmgGSDGGALGKPHPrsygdfTRVLGHYVRERKLLSL-EEAV----RKMT--- 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62422571 481 dkavatgkmdenqfvavtsTNAAKIFNLYPRkGRIAVGSDADVVIWDPDKLK---TITAKSHKSaveynifEGMEchgsp 557
Cdd:cd01297 346 -------------------GLPARVFGLADR-GRIAPGYRADIVVFDPDTLAdraTFTRPNQPA-------EGIE----- 393
|
490
....*....|....
gi 62422571 558 LVVISqGKIVFEDG 571
Cdd:cd01297 394 AVLVN-GVPVVRDG 406
|
|
| ATZ_TRZ_like |
cd01298 |
TRZ/ATZ family contains enzymes from the atrazine degradation pathway and related hydrolases. ... |
131-574 |
5.70e-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: 52.20 E-value: 5.70e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62422571 131 LLIKGGRIINDDQS---LYADVYLEDGLIKQIGENLIVPG--GVKTIEANGRMVIPGGIDVNT----------------- 188
Cdd:cd01298 1 ILIRNGTIVTTDPRrvlEDGDVLVEDGRIVAVGPALPLPAypADEVIDAKGKVVMPGLVNTHThlamtllrgladdlplm 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62422571 189 -YLQK---PSQGMTAADDFFQGTRAALV----GGTTMIIDHVVPEPGSSLltsfekwhEAADtKSccdyslhvditswyd 260
Cdd:cd01298 81 eWLKDliwPLERLLTEEDVYLGALLALAemirSGTTTFADMYFFYPDAVA--------EAAE-EL--------------- 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62422571 261 GVREELEVLVQDKGVnsfqvymayKDVYQMSDSqLYEAFTFLKglgaviLVHAENGDLIaqeqkRILeMGITGPEghaLS 340
Cdd:cd01298 137 GIRAVLGRGIMDLGT---------EDVEETEEA-LAEAERLIR------EWHGAADGRI-----RVA-LAPHAPY---TC 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62422571 341 RPEELEaeavfRAITIAGRINCPVYITkvMSKSAADI-IALARK-KGPLVFgepiAASLGTDGTHYWsknwakAAAFVTs 418
Cdd:cd01298 192 SDELLR-----EVAELAREYGVPLHIH--LAETEDEVeESLEKYgKRPVEY----LEELGLLGPDVV------LAHCVW- 253
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62422571 419 pplspdpTTPDYLTsLLACGDLQVTgsgHCPYSTAQKAVGkdnFTLIPE----GVN---------------GIEE-RMTV 478
Cdd:cd01298 254 -------LTDEEIE-LLAETGTGVA---HNPASNMKLASG---IAPVPEmleaGVNvglgtdgaasnnnldMFEEmRLAA 319
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62422571 479 VWDKAVA--TGKMDENQFVAVTSTNAAKIFNLyPRKGRIAVGSDADVVIWDPDKLKTITAKSHKSAVEYNifegmeCHGS 556
Cdd:cd01298 320 LLQKLAHgdPTALPAEEALEMATIGGAKALGL-DEIGSLEVGKKADLILIDLDGPHLLPVHDPISHLVYS------ANGG 392
|
490 500
....*....|....*....|
gi 62422571 557 P--LVVISqGKIVFEDGNIN 574
Cdd:cd01298 393 DvdTVIVN-GRVVMEDGELL 411
|
|
| NagA |
COG1820 |
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism]; |
495-529 |
1.44e-06 |
|
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism];
Pssm-ID: 441425 [Multi-domain] Cd Length: 373 Bit Score: 50.87 E-value: 1.44e-06
10 20 30
....*....|....*....|....*....|....*
gi 62422571 495 VAVTSTNAAKIFNLYPRKGRIAVGSDADVVIWDPD 529
Cdd:COG1820 328 VRMASLNPARALGLDDRKGSIAPGKDADLVVLDDD 362
|
|
| PRK07228 |
PRK07228 |
5'-deoxyadenosine deaminase; |
130-221 |
4.63e-06 |
|
5'-deoxyadenosine deaminase;
Pssm-ID: 180895 [Multi-domain] Cd Length: 445 Bit Score: 49.61 E-value: 4.63e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62422571 130 RLLIKGGRIINDDQS---LYADVYLEDGLIKQIGENLIVPGGVKTIEANGRMVIPGGIDVNTYL-QKPSQG--------- 196
Cdd:PRK07228 2 TILIKNAGIVTMNAKreiVDGDVLIEDDRIAAVGDRLDLEDYDDHIDATGKVVIPGLIQGHIHLcQTLFRGiaddlelld 81
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 62422571 197 --------MTAADDFFQGTRAALVG-------GTTMIIDH 221
Cdd:PRK07228 82 wlkdriwpLEAAHDAESMYYSALLGigeliesGTTTIVDM 121
|
|
| PRK09237 |
PRK09237 |
amidohydrolase/deacetylase family metallohydrolase; |
131-188 |
5.20e-06 |
|
amidohydrolase/deacetylase family metallohydrolase;
Pssm-ID: 236423 [Multi-domain] Cd Length: 380 Bit Score: 49.08 E-value: 5.20e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 62422571 131 LLIKGGRIINDDQSLYA--DVYLEDGLIKQIGENLIVPGGVKTIEANGRMVIPGGIDVNT 188
Cdd:PRK09237 1 LLLRGGRVIDPANGIDGviDIAIEDGKIAAVAGDIDGSQAKKVIDLSGLYVSPGWIDLHV 60
|
|
| PRK07627 |
PRK07627 |
dihydroorotase; Provisional |
130-570 |
6.22e-06 |
|
dihydroorotase; Provisional
Pssm-ID: 181059 [Multi-domain] Cd Length: 425 Bit Score: 49.29 E-value: 6.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62422571 130 RLLIKGGRIIN-----DDQslyADVYLEDGLIKQIGEnliVPGGV---KTIEANGRMVIPGGIDVNTYLQKPsqGMTAAD 201
Cdd:PRK07627 2 KIHIKGGRLIDpaagtDRQ---ADLYVAAGKIAAIGQ---APAGFnadKTIDASGLIVCPGLVDLSARLREP--GYEYKA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62422571 202 DFFQGTRAALVGGTTMII-----DHVVPEPGSSLLTSF--EKWHEAadtksccdyslHV----DITSWYDGVR-EELEVL 269
Cdd:PRK07627 74 TLESEMAAAVAGGVTSLVcppdtDPVLDEPGLVEMLKFraRNLNQA-----------HVyplgALTVGLKGEVlTEMVEL 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62422571 270 VQDKGVNSFQVymaykDVyQMSDSQ-LYEAFTFLKGLG-AVILvhaengdliaQEQKRILEMGITGPEGHALSR------ 341
Cdd:PRK07627 143 TEAGCVGFSQA-----NV-PVVDTQvLLRALQYASTFGfTVWL----------RPLDAFLGRGGVAASGAVASRlglsgv 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62422571 342 PEELEAEAVFRAITIAGRINCPVYITKVMSKSAADIIALARKKgplvfGEPIAASLGTDGTH-------YWSKNwakaaa 414
Cdd:PRK07627 207 PVAAETIALHTIFELMRVTGARVHLARLSSAAGVALVRAAKAE-----GLPVTCDVGVNHVHlidvdigYFDSQ------ 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62422571 415 FVTSPPLSpDPTTPDYLTSLLACGDLQVTGSGHCPystaqkaVGKDNfTLIP-----EGVNGIEE--RMTVVWdkAVATg 487
Cdd:PRK07627 276 FRLDPPLR-SQRDREAIRAALADGTIDAICSDHTP-------VDDDE-KLLPfaeatPGATGLELllPLTLKW--ADEA- 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62422571 488 KMDENQFVAVTSTNAAKIFNLypRKGRIAVGSDADVVIWDPDKLKTITAKSHKSAVEYNIFEGMECHGSPLVVISQGKIV 567
Cdd:PRK07627 344 KVPLARALARITSAPARVLGL--PAGRLAEGAPADLCVFDPDAHWRVEPRALKSQGKNTPFLGYELPGRVRATLVAGQVA 421
|
...
gi 62422571 568 FED 570
Cdd:PRK07627 422 FER 424
|
|
| PRK09061 |
PRK09061 |
D-glutamate deacylase; Validated |
126-218 |
8.26e-06 |
|
D-glutamate deacylase; Validated
Pssm-ID: 236369 [Multi-domain] Cd Length: 509 Bit Score: 48.92 E-value: 8.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62422571 126 GQSDRLLIKGGRIINDDQSLYA--DVYLEDGLIKQIGENLIvpGGVKTIEANGRMVIPGGIDVNtylqkpSQGMTAADDF 203
Cdd:PRK09061 16 MAPYDLVIRNGRVVDPETGLDAvrDVGIKGGKIAAVGTAAI--EGDRTIDATGLVVAPGFIDLH------AHGQSVAAYR 87
|
90
....*....|....*
gi 62422571 204 FQgtraALVGGTTMI 218
Cdd:PRK09061 88 MQ----AFDGVTTAL 98
|
|
| Amidohydro_3 |
pfam07969 |
Amidohydrolase family; |
448-550 |
3.10e-05 |
|
Amidohydrolase family;
Pssm-ID: 400360 [Multi-domain] Cd Length: 464 Bit Score: 47.14 E-value: 3.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62422571 448 CPYSTAQKAVGKDnfTLIPEGVNGIEERMTVvwdkavatgkmdeNQFVAVTSTNAAKIFNLYPRKGRIAVGSDADVVIWD 527
Cdd:pfam07969 373 DPWPRIGAAVMRQ--TAGGGEVLGPDEELSL-------------EEALALYTSGPAKALGLEDRKGTLGVGKDADLVVLD 437
|
90 100
....*....|....*....|...
gi 62422571 528 PDKLKTITAKSHKSAVEYNIFEG 550
Cdd:pfam07969 438 DDPLTVDPPAIADIRVRLTVVDG 460
|
|
| NagA |
COG1820 |
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism]; |
132-186 |
3.23e-05 |
|
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism];
Pssm-ID: 441425 [Multi-domain] Cd Length: 373 Bit Score: 46.63 E-value: 3.23e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 62422571 132 LIKGGRIINDDQSLY-ADVYLEDGLIKQIGENliVPGGVKTIEANGRMVIPGGIDV 186
Cdd:COG1820 1 AITNARIFTGDGVLEdGALLIEDGRIAAIGPG--AEPDAEVIDLGGGYLAPGFIDL 54
|
|
| PRK08204 |
PRK08204 |
hypothetical protein; Provisional |
129-226 |
4.25e-05 |
|
hypothetical protein; Provisional
Pssm-ID: 181288 [Multi-domain] Cd Length: 449 Bit Score: 46.53 E-value: 4.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62422571 129 DRLLIKGGRIINDDQSL----YADVYLEDGLIKQIGENlIVPGGVKTIEANGRMVIPG------------------GIDV 186
Cdd:PRK08204 2 KRTLIRGGTVLTMDPAIgdlpRGDILIEGDRIAAVAPS-IEAPDAEVVDARGMIVMPGlvdthrhtwqsvlrgigaDWTL 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 62422571 187 NTYLQKPSQGMTAA---DDFFQGTRA----ALVGGTTMIID--HVVPEP 226
Cdd:PRK08204 81 QTYFREIHGNLGPMfrpEDVYIANLLgaleALDAGVTTLLDwsHINNSP 129
|
|
| Met_dep_hydrolase_C |
cd01309 |
Metallo-dependent hydrolases, subgroup C is part of the superfamily of metallo-dependent ... |
482-554 |
6.98e-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: 6.98e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 62422571 482 KAVATGKMDENQFVAVTStNAAKIFNLYPRKGRIAVGSDADVVIWDPDKLKTiTAKshksaVEYNIFEGMECH 554
Cdd:cd01309 294 KAVKYGLSYEEALKAITI-NPAKILGIEDRVGSLEPGKDADLVVWNGDPLEP-TSK-----PEQVYIDGRLVY 359
|
|
| Bact_CD |
cd01293 |
Bacterial cytosine deaminase and related metal-dependent hydrolases. Cytosine deaminases (CDs) ... |
132-192 |
4.31e-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: 43.39 E-value: 4.31e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 62422571 132 LIKGGRIINDDQSLYaDVYLEDGLIKQIGENLIVPGGVKTIEANGRMVIPGGIDVNTYLQK 192
Cdd:cd01293 1 LLRNARLADGGTALV-DIAIEDGRIAAIGPALAVPPDAEEVDAKGRLVLPAFVDPHIHLDK 60
|
|
| PRK15446 |
PRK15446 |
phosphonate metabolism protein PhnM; Provisional |
130-188 |
1.02e-03 |
|
phosphonate metabolism protein PhnM; Provisional
Pssm-ID: 237967 [Multi-domain] Cd Length: 383 Bit Score: 42.09 E-value: 1.02e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 62422571 130 RLLIKGGRIINDDQSLYADVYLEDGLIKQIGENLIVPGGvkTIEANGRMVIPGGIDVNT 188
Cdd:PRK15446 3 EMILSNARLVLPDEVVDGSLLIEDGRIAAIDPGASALPG--AIDAEGDYLLPGLVDLHT 59
|
|
| PRK09061 |
PRK09061 |
D-glutamate deacylase; Validated |
510-585 |
2.65e-03 |
|
D-glutamate deacylase; Validated
Pssm-ID: 236369 [Multi-domain] Cd Length: 509 Bit Score: 40.83 E-value: 2.65e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 62422571 510 PRKGRIAVGSDADVVIWDPDKLK---TITAKSHKSaveynifEGMEcHgsplvVISQGKIVFEDGNINVNKGMGRFIPR 585
Cdd:PRK09061 441 RRKGRLQAGADADIVVFDPETITdraTFEDPNRPS-------EGVR-H-----VLVNGVPVVSNGELVRDARPGRPVRR 506
|
|
| Imidazolone-5PH |
cd01296 |
Imidazolonepropionase/imidazolone-5-propionate hydrolase (Imidazolone-5PH) catalyzes the third ... |
483-527 |
2.81e-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: 2.81e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 62422571 483 AVATGKMDENQFVAVTSTNAAKIFNLYPRKGRIAVGSDADVVIWD 527
Cdd:cd01296 304 ACRLMRMTPEEALTAATINAAAALGLGETVGSLEVGKQADLVILD 348
|
|
| Isoaspartyl-dipeptidase |
cd01308 |
Isoaspartyl dipeptidase hydrolyzes the beta-L-isoaspartyl linkages in dipeptides, as part of ... |
497-537 |
4.15e-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: 4.15e-03
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 62422571 497 VTSTNAAKIFNLYPrKGRIAVGSDADVVIWDPD-KLKTITAK 537
Cdd:cd01308 330 VITSNVARILKLRK-KGEIQPGFDADLVILDKDlDINSVIAK 370
|
|
| PRK05985 |
PRK05985 |
cytosine deaminase; Provisional |
147-197 |
7.27e-03 |
|
cytosine deaminase; Provisional
Pssm-ID: 180337 [Multi-domain] Cd Length: 391 Bit Score: 39.15 E-value: 7.27e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 62422571 147 ADVYLEDGLIKQIGENLIVPGGVKTIEANGRMVIPGGIDVNTYLQKPSQGM 197
Cdd:PRK05985 17 VDILIRDGRIAAIGPALAAPPGAEVEDGGGALALPGLVDGHIHLDKTFWGD 67
|
|
| FMDH_A |
cd01304 |
Formylmethanofuran dehydrogenase (FMDH) subunit A; Methanogenic bacteria and archea derive ... |
133-189 |
8.14e-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: 39.32 E-value: 8.14e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 62422571 133 IKGGRIINDDQSLYA---DVYLEDGlikQIGENLIVPGGVKTIEANGRMVIPGGIDVNTY 189
Cdd:cd01304 1 IKNGTVYDPLNGINGekmDIFIRDG---KIVESSSGAKPAKVIDASGKVVMAGGVDMHSH 57
|
|
| COG3653 |
COG3653 |
N-acyl-D-aspartate/D-glutamate deacylase [Secondary metabolites biosynthesis, transport and ... |
502-587 |
8.92e-03 |
|
N-acyl-D-aspartate/D-glutamate deacylase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442870 [Multi-domain] Cd Length: 528 Bit Score: 39.00 E-value: 8.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62422571 502 AAKIFNLYPRkGRIAVGSDADVVIWDPDKLK-TITA-KSHKSAveynifEGMEChgsplVVISqGKIVFEDGNINvNKGM 579
Cdd:COG3653 453 PADRLGLKDR-GLLRPGYRADLVVFDPATLAdRATFdLPAQRA------DGIRA-----VIVN-GVVVVEDGKPT-GARP 518
|
....*...
gi 62422571 580 GRFIPRKA 587
Cdd:COG3653 519 GRVLRGGG 526
|
|
| |
