|
Name |
Accession |
Description |
Interval |
E-value |
| 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: 763.85 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25742568 17 LLIKGGRIVNDDQSFYADIYMEDGLIKQIGDNLIVPGGVKTIEANGKMVMPGGIDVHTHFQMPYKGMTTVDDFFQGTKAA 96
Cdd:TIGR02033 1 LLIKGGTVVNADDVFQADVLIEGGKIVAVGDNLIPPDAVEVIDATGKYVLPGGIDVHTHLEMPFGGTTTADDFFTGTKAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25742568 97 LAGGTTMIIDHVVPEPESSLTEAYEKWREWADGKSCCDYALHVDITHWNDSVKQEVQNLSKEKGVNSFMVYMAYKDLYQV 176
Cdd:TIGR02033 81 AAGGTTTIIDFVVPEKGSSLTEALETWHEKAEGKSVIDYGFHMDITHWNDSVLEEHIPEVKEEGINSFKVFMAYKNLLMV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25742568 177 SNTELYEIFTCLGELGAIAQVHAENGDIIAQEQARMLEMGITGPEGHVLSRPEELEAEAVFRAITVASQTNCPLYVTKVM 256
Cdd:TIGR02033 161 DDEELFEILKRLKELGALLQVHAENGDIIAELQARMLAQGITGPEYHALSRPPELEAEAVARAITLAALADAPLYVVHVS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25742568 257 SKSAADLISQARKKGNVVFGEPITASLGIDGTHYWsKNWAKAAAFVTSPPLSpDPTTPDYINSLLASGDLQLSGSAHCTF 336
Cdd:TIGR02033 241 TKDAADEIAQARKKGQPVFGETCPQYLVLDDTHYD-KPGFEGAKYVCSPPLR-EPEDQDALWSALSSGALQTVGSDHCTF 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25742568 337 STAQK-AIGKDNFTAIPEGTNGVEERMSVIWDKAVATGKMDENQFVAVTSTNAAKIFNLYPRKGRIAVGSDSDLVIWDPD 415
Cdd:TIGR02033 319 NFAQKkAIGKDDFTKIPNGGPGVEERMSLLFDEGVAKGRITLEKFVEVTSTNPAKIFNLYPRKGTIAVGSDADIVIWDPN 398
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 25742568 416 AVKIVSAKNHQSVAEYNIFEGMELRGAPLVVICQGKIMLEDGNLHVTQGAGRFIPC 471
Cdd:TIGR02033 399 RTTVISAETHHSNADYNPFEGFKVRGAPVSVLSRGRVVVEDGQLVGTAGAGRFVKR 454
|
|
| 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: 736.33 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25742568 17 LLIKGGRIVNDDQSFYADIYMEDGLIKQIGDNLIVPGGVKTIEANGKMVMPGGIDVHTHFQMPYKGMTTVDDFFQGTKAA 96
Cdd:cd01314 1 LIIKNGTIVTADGSFKADILIEDGKIVAIGPNLEAPGGVEVIDATGKYVLPGGIDPHTHLELPFMGTVTADDFESGTRAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25742568 97 LAGGTTMIIDHVVPEPESSLTEAYEKWREWADGKSCCDYALHVDITHWNDSVKQEVQNLSKeKGVNSFMVYMAYKDLYQV 176
Cdd:cd01314 81 AAGGTTTIIDFAIPNKGQSLLEAVEKWRGKADGKSVIDYGFHMIITDWTDSVIEELPELVK-KGISSFKVFMAYKGLLMV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25742568 177 SNTELYEIFTCLGELGAIAQVHAENGDIIAQEQARMLEMGITGPEGHVLSRPEELEAEAVFRAITVASQTNCPLYVTKVM 256
Cdd:cd01314 160 DDEELLDVLKRAKELGALVMVHAENGDVIAELQKKLLAQGKTGPEYHALSRPPEVEAEATARAIRLAELAGAPLYIVHVS 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25742568 257 SKSAADLISQARKKGNVVFGEPITASLGIDGTHYWsKNWAKAAAFVTSPPLSPDpTTPDYINSLLASGDLQLSGSAHCTF 336
Cdd:cd01314 240 SKEAADEIARARKKGLPVYGETCPQYLLLDDSDYW-KDWFEGAKYVCSPPLRPK-EDQEALWDGLSSGTLQTVGSDHCPF 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25742568 337 STAQKAIGKDNFTAIPEGTNGVEERMSVIWDKAVATGKMDENQFVAVTSTNAAKIFNLYPRKGRIAVGSDSDLVIWDPDA 416
Cdd:cd01314 318 NFAQKARGKDDFTKIPNGVPGVETRMPLLWSEGVAKGRITLEKFVELTSTNPAKIFGLYPRKGTIAVGSDADLVIWDPNA 397
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 25742568 417 VKIVSAKNHQSVAEYNIFEGMELRGAPLVVICQGKIMLEDGNLHVTQGAG 466
Cdd:cd01314 398 EKTISADTHHHNVDYNIFEGMKVKGWPVVTISRGKVVVEDGELVGEKGSG 447
|
|
| PRK08323 |
PRK08323 |
phenylhydantoinase; Validated |
16-475 |
0e+00 |
|
phenylhydantoinase; Validated
Pssm-ID: 236240 [Multi-domain] Cd Length: 459 Bit Score: 569.42 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25742568 16 RLLIKGGRIVNDDQSFYADIYMEDGLIKQIGDNlivpGGVKTIEANGKMVMPGGIDVHTHFQMPYKGMTTVDDFFQGTKA 95
Cdd:PRK08323 2 STLIKNGTVVTADDTYKADVLIEDGKIAAIGAN----LGDEVIDATGKYVMPGGIDPHTHMEMPFGGTVSSDDFETGTRA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25742568 96 ALAGGTTMIIDHVVPEPESSLTEAYEKWREWADGKSCCDYALHVDITHWNDSVKQEVQNLSKEkGVNSFMVYMAYKDLYQ 175
Cdd:PRK08323 78 AACGGTTTIIDFALQPKGQSLREALEAWHGKAAGKAVIDYGFHMIITDWNEVVLDEMPELVEE-GITSFKLFMAYKGALM 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25742568 176 VSNTELYEIFTCLGELGAIAQVHAENGDIIAQEQARMLEMGITGPEGHVLSRPEELEAEAVFRAITVASQTNCPLYVTKV 255
Cdd:PRK08323 157 LDDDELLRALQRAAELGALPMVHAENGDAIAYLQAKLLAEGKTGPEYHALSRPPEVEGEATNRAIMLAELAGAPLYIVHV 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25742568 256 MSKSAADLISQARKKGNVVFGEPITASLGIDGTHYWSKNWAKAAAFVTSPPLSPdpttPDYINSL---LASGDLQLSGSA 332
Cdd:PRK08323 237 SCKEALEAIRRARARGQRVFGETCPQYLLLDESEYDGPDWFEGAKYVMSPPLRD----KEHQDALwrgLQDGDLQVVATD 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25742568 333 HCTFSTAQKA-IGKDNFTAIPEGTNGVEERMSVIWDKAVATGKMDENQFVAVTSTNAAKIFNLYPRKGRIAVGSDSDLVI 411
Cdd:PRK08323 313 HCPFCFEQKKqLGRGDFTKIPNGTPGVEDRMPLLFSEGVMTGRITLNRFVELTSTNPAKIFGLYPRKGTIAVGADADIVI 392
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 25742568 412 WDPDAVKIVSAKNHQSVAEYNIFEGMELRGAPLVVICQGKIMLEDGNLHVTQGAGRFIPCSPFS 475
Cdd:PRK08323 393 WDPNATKTISASTLHSNVDYNPYEGFEVTGWPVTTLSRGEVVVEDGEFRGKAGHGRFLKRKPFQ 456
|
|
| PLN02942 |
PLN02942 |
dihydropyrimidinase |
12-485 |
0e+00 |
|
dihydropyrimidinase
Pssm-ID: 178530 Cd Length: 486 Bit Score: 550.99 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25742568 12 ITSDRLLIKGGRIVNDDQSFYADIYMEDGLIKQIGDNLIVPGGVKTIEANGKMVMPGGIDVHTHFQMPYKGMTTVDDFFQ 91
Cdd:PLN02942 2 ASSTKILIKGGTVVNAHHQELADVYVEDGIIVAVAPNLKVPDDVRVIDATGKFVMPGGIDPHTHLAMPFMGTETIDDFFS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25742568 92 GTKAALAGGTTMIIDHVVPePESSLTEAYEKWREWADgKSCCDYALHVDITHWNDSVKQEVQNLSKEKGVNSFMVYMAYK 171
Cdd:PLN02942 82 GQAAALAGGTTMHIDFVIP-VNGNLLAGYEAYEKKAE-KSCMDYGFHMAITKWDDTVSRDMETLVKEKGINSFKFFMAYK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25742568 172 DLYQVSNTELYEIFTCLGELGAIAQVHAENGDIIAQEQARMLEMGITGPEGHVLSRPEELEAEAVFRAITVASQTNCPLY 251
Cdd:PLN02942 160 GSLMVTDELLLEGFKRCKSLGALAMVHAENGDAVFEGQKRMIELGITGPEGHALSRPPLLEGEATARAIRLAKFVNTPLY 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25742568 252 VTKVMSKSAADLISQARKKGNVVFGEPITASLGIDGTHYWSKNWAKAAAFVTSPPLSPdPTTPDYINSLLASGDLQLSGS 331
Cdd:PLN02942 240 VVHVMSIDAMEEIARARKSGQRVIGEPVVSGLVLDDSKLWDPDFTIASKYVMSPPIRP-AGHGKALQAALSSGILQLVGT 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25742568 332 AHCTFSTAQKAIGKDNFTAIPEGTNGVEERMSVIWDKAVATGKMDENQFVAVTSTNAAKIFNLYPRKGRIAVGSDSDLVI 411
Cdd:PLN02942 319 DHCPFNSTQKAFGKDDFRKIPNGVNGIEERMHLVWDTMVESGQISPTDYVRVTSTECAKIFNIYPRKGAILAGSDADIII 398
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 25742568 412 WDPDAVKIVSAKNHQSVAEYNIFEGMELRGAPLVVICQGKIMLEDGNLHVTQGAGRFIPCSPFSdYVYKRIKAR 485
Cdd:PLN02942 399 LNPNSTFTISAKTHHSRIDTNVYEGRRGKGKVEVTISQGRVVWENGELKVVRGSGRYIEMPPFS-YLFDGIQKA 471
|
|
| AllB |
COG0044 |
Dihydroorotase or related cyclic amidohydrolase [Nucleotide transport and metabolism]; ... |
18-470 |
5.55e-128 |
|
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: 382.13 E-value: 5.55e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25742568 18 LIKGGRIVNDDQSFYADIYMEDGLIKQIGDNLIVPGGVKTIEANGKMVMPGGIDVHTHFQMPykGMTTVDDFFQGTKAAL 97
Cdd:COG0044 1 LIKNGRVVDPGGLERADVLIEDGRIAAIGPDLAAPEAAEVIDATGLLVLPGLIDLHVHLREP--GLEHKEDIETGTRAAA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25742568 98 AGGTTMIIDHVVPEPESSLTEAYEKWREWADGKSCCDYALHVDITHWNDSVKQEVQNLsKEKGVNSFMVYMAYKDLYQVS 177
Cdd:COG0044 79 AGGVTTVVDMPNTNPVTDTPEALEFKLARAEEKALVDVGPHGALTKGLGENLAELGAL-AEAGAVAFKVFMGSDDGNPVL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25742568 178 NTE-LYEIFTCLGELGAIAQVHAENGDIIAqeqARMLEMGITGPEGHVLSRPEELEAEAVFRAITVASQTNCPLYVTKVM 256
Cdd:COG0044 158 DDGlLRRALEYAAEFGALVAVHAEDPDLIR---GGVMNEGKTSPRLGLKGRPAEAEEEAVARDIALAEETGARLHIVHVS 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25742568 257 SKSAADLISQARKKGNVVFGE--P----ITAS-LGIDGTHYwsknwakaaafVTSPPLSpdptTPDYINSL---LASGDL 326
Cdd:COG0044 235 TAEAVELIREAKARGLPVTAEvcPhhltLTDEdLERYGTNF-----------KVNPPLR----TEEDREALwegLADGTI 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25742568 327 QLSGSAHCTFSTAQKAigkDNFTAIPEGTNGVEERMSVIWDKAVATGKMDENQFVAVTSTNAAKIFNLyPRKGRIAVGSD 406
Cdd:COG0044 300 DVIATDHAPHTLEEKE---LPFAEAPNGIPGLETALPLLLTELVHKGRLSLERLVELLSTNPARIFGL-PRKGRIAVGAD 375
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 25742568 407 SDLVIWDPDAVKIVSAKNHQSVAEYNIFEGMELRGAPLVVICQGKIMLEDGNLhVTQGAGRFIP 470
Cdd:COG0044 376 ADLVLFDPDAEWTVTAEDLHSKSKNTPFEGRELTGRVVATIVRGRVVYEDGEV-VGEPRGRFLR 438
|
|
| PRK13404 |
PRK13404 |
dihydropyrimidinase; Provisional |
17-473 |
2.18e-116 |
|
dihydropyrimidinase; Provisional
Pssm-ID: 184033 [Multi-domain] Cd Length: 477 Bit Score: 353.62 E-value: 2.18e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25742568 17 LLIKGGRIVNDDQSFYADIYMEDGLIKQIGDNLivPGGVKTIEANGKMVMPGGIDVHTHFQMPY-KGMTTVDDFFQGTKA 95
Cdd:PRK13404 6 LVIRGGTVVTATDTFQADIGIRGGRIAALGEGL--GPGAREIDATGRLVLPGGVDSHCHIDQPSgDGIMMADDFYTGTVS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25742568 96 ALAGGTTMIIDHVVPEPESSLTEAYEKWREWADGKSCCDYALHVDITHWNDSV-KQEVQNLSKEkGVNSFMVYMAYKDLy 174
Cdd:PRK13404 84 AAFGGTTTVIPFAAQHRGQSLREAVEDYHRRAAGKAVIDYAFHLIVADPTEEVlTEELPALIAQ-GYTSFKVFMTYDDL- 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25742568 175 QVSNTELYEIFTCLGELGAIAQVHAENGDIIAQEQARMLEMGITGPEGHVLSRPEELEAEAVFRAITVASQTNCPLYVTK 254
Cdd:PRK13404 162 KLDDRQILDVLAVARRHGAMVMVHAENHDMIAWLTKRLLAAGLTAPKYHAISRPMLAEREATHRAIALAELVDVPILIVH 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25742568 255 VMSKSAADLISQARKKGNVVFGEP------ITAS-LGIDGTHywsknwakAAAFVTSPPLSpDPTTPDYINSLLASGDLQ 327
Cdd:PRK13404 242 VSGREAAEQIRRARGRGLKIFAETcpqylfLTAEdLDRPGME--------GAKYICSPPPR-DKANQEAIWNGLADGTFE 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25742568 328 LSGSAHCTF---STAQKAIGKDN--FTAIPEGTNGVEERMSVIWDKAVATGKMDENQFVAVTSTNAAKIFNLYPRKGRIA 402
Cdd:PRK13404 313 VFSSDHAPFrfdDTDGKLAAGANpsFKAIANGIPGIETRLPLLFSEGVVKGRISLNRFVALTSTNPAKLYGLYPRKGAIA 392
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 25742568 403 VGSDSDLVIWDPDAVKIVSAKNHQSVAEYNIFEGMELRGAPLVVICQGKIMLEDGNLHVTQGAGRFIPCSP 473
Cdd:PRK13404 393 IGADADIAIWDPDREVTITNADLHHAADYTPYEGMRVTGWPVTVLSRGRVVVEDGELVAERGSGQFLARSL 463
|
|
| L-HYD_ALN |
cd01315 |
L-Hydantoinases (L-HYDs) and Allantoinase (ALN); L-Hydantoinases are a member of the ... |
17-469 |
1.13e-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: 231.41 E-value: 1.13e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25742568 17 LLIKGGRIVNDDQSFYADIYMEDGLIKQIGDNLIVPGGVKTIEANGKMVMPGGIDVHTHFQMPykGMTTVDDFFQGTKAA 96
Cdd:cd01315 2 LVIKNGRVVTPDGVREADIAVKGGKIAAIGPDIANTEAEEVIDAGGLVVMPGLIDTHVHINEP--GRTEWEGFETGTKAA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25742568 97 LAGGTTMIIDhvVP---EPESSLTEAYEKWREWADGKSCCDYALhvdithWNDSVKQEVQNLSK--EKGV---NSFMVYM 168
Cdd:cd01315 80 AAGGITTIID--MPlnsIPPTTTVENLEAKLEAAQGKLHVDVGF------WGGLVPGNLDQLRPldEAGVvgfKCFLCPS 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25742568 169 AYKDLYQVSNTELYEIFTCLGELGAIAQVHAENGDIIAQEQARMLEMGITGPEGHVLSRPEELEAEAVFRAITVASQTNC 248
Cdd:cd01315 152 GVDEFPAVDDEQLEEAMKELAKTGSVLAVHAENPEITEALQEQAKAKGKRDYRDYLASRPVFTEVEAIQRILLLAKETGC 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25742568 249 PLYVTKVMSKSAADLISQARKKGNVVFGEPITASLGI------DGthywsknwakAAAFVTSPPLSpDPTTPDYINSLLA 322
Cdd:cd01315 232 RLHIVHLSSAEAVPLIREARAEGVDVTVETCPHYLTFtaedvpDG----------GTEFKCAPPIR-DAANQEQLWEALE 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25742568 323 SGDLQLSGSAHCTFSTAQKAIGKDNFTAIPEGTNGVEERMSVIWDKAVATGKMDENQFVAVTSTNAAKIFNLYPRKGRIA 402
Cdd:cd01315 301 NGDIDMVVSDHSPCTPELKLLGKGDFFKAWGGISGLQLGLPVMLTEAVNKRGLSLEDIARLMCENPAKLFGLSHQKGRIA 380
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 25742568 403 VGSDSDLVIWDPDAVKIVSAKNHQSVAEYNIFEGMELRGAPLVVICQGKIMLEDGNlHVTQGAGRFI 469
Cdd:cd01315 381 VGYDADFVVWDPEEEFTVDAEDLYYKNKISPYVGRTLKGRVHATILRGTVVYQDGE-VVGEPLGQLL 446
|
|
| Cyclic_amidohydrolases |
cd01302 |
Cyclic amidohydrolases, including hydantoinase, dihydropyrimidinase, allantoinase, and ... |
63-443 |
6.84e-63 |
|
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: 209.94 E-value: 6.84e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25742568 63 KMVMPGGIDVHTHFQMPYKGmTTVDDFFQGTKAALAGGTTMIIDHVVPEPESSLTEAYEKWREWADGKSCCDYALHVDIt 142
Cdd:cd01302 1 LLVLPGFIDIHVHLRDPGGT-TYKEDFESGSRAAAAGGVTTVIDMPNTGPPPIDLPAIELKIKLAEESSYVDFSFHAGI- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25742568 143 hwndSVKQEVQNLSK--EKGVNSFMVYMAYK--DLYQVSNTELYEIFTCLGELGAIAQVHAEngdiiaqeqarmlemgit 218
Cdd:cd01302 79 ----GPGDVTDELKKlfDAGINSLKVFMNYYfgELFDVDDGTLMRTFLEIASRGGPVMVHAE------------------ 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25742568 219 gpeghvlsrpeeleaeavfRAITVASQTNCPLYVTKVMSKSAADLISQARKKGNVVFGEPITASLGIDgTHYWSKNWAKa 298
Cdd:cd01302 137 -------------------RAAQLAEEAGANVHIAHVSSGEALELIKFAKNKGVKVTCEVCPHHLFLD-ESMLRLNGAW- 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25742568 299 aaFVTSPPLSPdPTTPDYINSLLASGDLQLSGSAHCTFSTAQKAIGKDnFTAIPEGTNGVEERMSVIWdKAVATGKMDEN 378
Cdd:cd01302 196 --GKVNPPLRS-KEDREALWEGVKNGKIDTIASDHAPHSKEEKESGKD-IWKAPPGFPGLETRLPILL-TEGVKRGLSLE 270
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 25742568 379 QFVAVTSTNAAKIFNLYPrKGRIAVGSDSDLVIWDPDAVKIVSAKNHQSVAEYNIFEGMELRGAP 443
Cdd:cd01302 271 TLVEILSENPARIFGLYP-KGTIAVGYDADLVIVDPKKEWKVTAEEIESKADWTPFEGMEVTGKP 334
|
|
| allantoinase |
TIGR03178 |
allantoinase; This enzyme carries out the first step in the degradation of allantoin, a ... |
17-470 |
1.35e-55 |
|
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: 193.75 E-value: 1.35e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25742568 17 LLIKGGRIVNDDQSFYADIYMEDGLIKQIGDNlIVPGGVKTIEANGKMVMPGGIDVHTHFQMPykGMTTVDDFFQGTKAA 96
Cdd:TIGR03178 2 LIIRGGRVILPNGEREADVGVKGGKIAAIGPD-ILGPAAKIIDAGGLVVFPGVVDTHVHINEP--GRTEWEGFETGTRAA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25742568 97 LAGGTTMIIDHVVPEPESSLT-EAYEKWREWADGKsccdyaLHVDITHWNDSVKQEVQNLSK--EKGVNSFMVYMAY--- 170
Cdd:TIGR03178 79 AAGGITTYIDMPLNSIPATTTrASLEAKFEAAKGK------LAVDVGFWGGLVPYNLDDLREldEAGVVGFKAFLSPsgd 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25742568 171 KDLYQVSNTELYEIFTCLGELGAIAQVHAENGDIIAQEQARMLEMGITGPEGHVLSRPEELEAEAVFRAITVASQTNCPL 250
Cdd:TIGR03178 153 DEFPHVDDWQLYKGMRELARLGQLLLVHAENPAITSALGEEAPPQGGVGADAYLASRPVFAEVEAIRRTLALAKVTGCRV 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25742568 251 YVTKVMSKSAADLISQARKKGNVVFGEPItaslgidgTHYWSKNWAK----AAAFVTSPPLSPDPTTPDYINSLLAsGDL 326
Cdd:TIGR03178 233 HVVHLSSAEAVELITEAKQEGLDVTVETC--------PHYLTLTAEEvpdgGTLAKCAPPIRDLANQEGLWEALLN-GLI 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25742568 327 QLSGSAHCTFSTAQKAigKDNFTAIPEGTNGVEERMSVIWDKAVATGKMDENQFVAVTSTNAAKIFNLyPRKGRIAVGSD 406
Cdd:TIGR03178 304 DCVVSDHSPCTPDLKR--AGDFFKAWGGIAGLQSTLDVMFDEAVQKRGLPLEDIARLMATNPAKRFGL-AQKGRIAPGKD 380
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 25742568 407 SDLVIWDPDAVKIVSAKNHQSVAEYNIFEGMELRGAPLVVICQGKIMLEDGNLhVTQGAGRFIP 470
Cdd:TIGR03178 381 ADFVFVDPDESYTLTPDDLYYRHKVSPYVGRTIGGRVRATYLRGQCIYDDEQF-IGAPKGQLLL 443
|
|
| PRK06189 |
PRK06189 |
allantoinase; Provisional |
17-460 |
2.20e-54 |
|
allantoinase; Provisional
Pssm-ID: 235732 [Multi-domain] Cd Length: 451 Bit Score: 190.68 E-value: 2.20e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25742568 17 LLIKGGRIVNDDQSFYADIYMEDGLIKQIGDNLIVPGGvKTIEANGKMVMPGGIDVHTHFQMPykGMTTVDDFFQGTKAA 96
Cdd:PRK06189 5 LIIRGGKVVTPEGVYRADIGIKNGKIAEIAPEISSPAR-EIIDADGLYVFPGMIDVHVHFNEP--GRTHWEGFATGSAAL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25742568 97 LAGGTTMIIDHVVPEPESSLT-EAYEKWREWADGKSCCDYALhvdithWNDSVKQEVQNLSK--EKGVNSFMVYMAYK-- 171
Cdd:PRK06189 82 AAGGCTTYFDMPLNSIPPTVTrEALDAKAELARQKSAVDFAL------WGGLVPGNLEHLRElaEAGVIGFKAFMSNSgt 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25742568 172 DLYQVSNTE-LYEIFTCLGELGAIAQVHAENGDIIAQEQARMLEMGITGPEGHVLSRPEELEAEAVFRAITVASQTNCPL 250
Cdd:PRK06189 156 DEFRSSDDLtLYEGMKEIAALGKILALHAESDALTRHLTTQARQQGKTDVRDYLESRPVVAELEAVQRALLYAQETGCPL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25742568 251 YVTKVMSKSAADLISQARKKG-NV---------VFGEPITASLGIdgthywsknWAKAAafvtsPPLSPDPTTPDYINSL 320
Cdd:PRK06189 236 HFVHISSGKAVALIAEAKKRGvDVsvetcphylLFTEEDFERIGA---------VAKCA-----PPLRSRSQKEELWRGL 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25742568 321 LAsGDLQLSGSAH--CTFSTAQKaigkDNFTAIPEGTNGVEERMSVIWDKAVATGKMDENQFVAVTSTNAAKIFNLyPRK 398
Cdd:PRK06189 302 LA-GEIDMISSDHspCPPELKEG----DDFFLVWGGISGGQSTLLVMLTEGYIERGIPLETIARLLATNPAKRFGL-PQK 375
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 25742568 399 GRIAVGSDSDLVIWDPDAVKIVSAKNHQSVAEYNIFEGMELRGAPLVVICQGKIMLEDGNLH 460
Cdd:PRK06189 376 GRLEVGADADFVLVDLDETYTLTKEDLFYRHKQSPYEGRTFPGRVVATYLRGQCVYQDGEVF 437
|
|
| PRK02382 |
PRK02382 |
dihydroorotase; Provisional |
17-470 |
2.67e-54 |
|
dihydroorotase; Provisional
Pssm-ID: 179417 [Multi-domain] Cd Length: 443 Bit Score: 190.25 E-value: 2.67e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25742568 17 LLIKGGRIVNDDQSFYADIYMEDGLIKQIGDNLIVPGGVKTIEANGKMVMPGGIDVHTHFQMPykGMTTVDDFFQGTKAA 96
Cdd:PRK02382 4 ALLKDGRVYYNNSLQPRDVRIDGGKITAVGKDLDGSSSEEVIDARGMLLLPGGIDVHVHFREP--GYTHKETWYTGSRSA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25742568 97 LAGGTTMIIDHVVPEPESSLTEAYEKWREWADGKSCCDYALhvdithwNDSVKQEVQNLSK--EKGVNSF-MVYMA--YK 171
Cdd:PRK02382 82 AAGGVTTVVDQPNTDPPTVDGESFDEKAELAARKSIVDFGI-------NGGVTGNWDPLESlwERGVFALgEIFMAdsTG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25742568 172 DLyQVSNTELYEIFTCLGELGAIAQVHAENGDIIAqEQARMLEmGITGPEGHVLSRPEELEAEAVFRAITVASQTNCPLY 251
Cdd:PRK02382 155 GM-GIDEELFEEALAEAARLGVLATVHAEDEDLFD-ELAKLLK-GDADADAWSAYRPAAAEAAAVERALEVASETGARIH 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25742568 252 VTKVMSKSAADLISqarkkgnvvfGEPITAslgiDGT-HYW---SKNWAKAAAFV-TSPPLSPDPTTPDYINSLlASGDL 326
Cdd:PRK02382 232 IAHISTPEGVDAAR----------REGITC----EVTpHHLflsRRDWERLGTFGkMNPPLRSEKRREALWERL-NDGTI 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25742568 327 QLSGSAHCTFSTAQKAigkDNFTAIPEGTNGVEERMSVIWdKAVATGKMDENQFVAVTSTNAAKIFNLyPRKGRIAVGSD 406
Cdd:PRK02382 297 DVVASDHAPHTREEKD---ADIWDAPSGVPGVETMLPLLL-AAVRKNRLPLERVRDVTAANPARIFGL-DGKGRIAEGYD 371
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 25742568 407 SDLVIWDPDAVKIVSAKNHQSVAEYNIFEGMElrGA-PLVVICQGKIMLEDGNLHVTQGAGRFIP 470
Cdd:PRK02382 372 ADLVLVDPDAAREIRGDDLHSKAGWTPFEGME--GVfPELTMVRGTVVWDGDDINAKRGRGEFLR 434
|
|
| DHOase_IIb |
cd01318 |
Dihydroorotase (DHOase), subgroup IIb; DHOases catalyze the reversible interconversion of ... |
62-450 |
9.63e-38 |
|
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: 142.86 E-value: 9.63e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25742568 62 GKMVMPGGIDVHTHFQMPykGMTTVDDFFQGTKAALAGGTTMIID--HVVPEPESSltEAYEKWREWADGKSCCDYALHV 139
Cdd:cd01318 1 GLLILPGVIDIHVHFREP--GLTYKEDFVSGSRAAAAGGVTTVMDmpNTKPPTTTA--EALYEKLRLAAAKSVVDYGLYF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25742568 140 DIThwndsvKQEVQNLSKEKGVNSFMVYMA--YKDLYQVSNTeLYEIFtclGELGAIAQVHAENGDIIAQEQARMLEMGI 217
Cdd:cd01318 77 GVT------GSEDLEELDKAPPAGYKIFMGdsTGDLLDDEET-LERIF---AEGSVLVTFHAEDEDRLRENRKELKGESA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25742568 218 tgpegHVLSRPEELEAEAVFRAITVASQTNCPLYVTKVMSKSAADLISQARKKGNV-------VFGEPITASLGidgthy 290
Cdd:cd01318 147 -----HPRIRDAEAAAVATARALKLARRHGARLHICHVSTPEELKLIKKAKPGVTVevtphhlFLDVEDYDRLG------ 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25742568 291 wskNWAKaaafvTSPPLSpDPTTPDYINSLLASGDLQLSGSAHCTFSTAQKAIGkdnFTAIPEGTNGVEERMSVIWDkAV 370
Cdd:cd01318 216 ---TLGK-----VNPPLR-SREDRKALLQALADGRIDVIASDHAPHTLEEKRKG---YPAAPSGIPGVETALPLMLT-LV 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25742568 371 ATGKMDENQFVAVTSTNAAKIFNLyPRKGRIAVGSDSDLVIWDPDAVKIVSAKNHQSVAEYNIFEGMELRGAPLVVICQG 450
Cdd:cd01318 283 NKGILSLSRVVRLTSHNPARIFGI-KNKGRIAEGYDADLTVVDLKEERTIRAEEFHSKAGWTPFEGFEVTGFPVMTIVRG 361
|
|
| PRK08044 |
PRK08044 |
allantoinase AllB; |
17-424 |
3.19e-36 |
|
allantoinase AllB;
Pssm-ID: 169193 [Multi-domain] Cd Length: 449 Bit Score: 140.76 E-value: 3.19e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25742568 17 LLIKGGRIVNDDQSFYADIYMEDGLIKQIGDNLivPGGVKTIEANGKMVMPGGIDVHTHFQMPykGMTTVDDFFQGTKAA 96
Cdd:PRK08044 5 LIIKNGTVILENEARVVDIAVKGGKIAAIGQDL--GDAKEVMDASGLVVSPGMVDAHTHISEP--GRSHWEGYETGTRAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25742568 97 LAGGTTMIIDHVVPE-PESSLTEAYEKWREWADGKSCCDYALHVDITHWNDSVKQEVQnlskEKGVNSFMVYMAY----- 170
Cdd:PRK08044 81 AKGGITTMIEMPLNQlPATVDRASIELKFDAAKGKLTIDAAQLGGLVSYNLDRLHELD----EVGVVGFKCFVATcgdrg 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25742568 171 --KDLYQVSNTELYEIFTCLGELGAIAQVHAENGDIIAQEQARMLEMGITGPEGHVLSRPEELEAEAVFRAITVASQTNC 248
Cdd:PRK08044 157 idNDFRDVNDWQFYKGAQKLGELGQPVLVHCENALICDELGEEAKREGRVTAHDYVASRPVFTEVEAIRRVLYLAKVAGC 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25742568 249 PLYVTKVMSKSAADLISQARKKGNVVFGEPItaslgidgTHYWSKNWAKAAAFVT----SPPLSPDPTTPDYINSLLaSG 324
Cdd:PRK08044 237 RLHVCHISSPEGVEEVTRARQEGQDVTCESC--------PHYFVLDTDQFEEIGTlakcSPPIRDLENQKGMWEKLF-NG 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25742568 325 DLQLSGSAHCTFSTAQKAigkDNFTAIPEGTNGVEERMSVIWDKAVATGKMDENQFVAVTSTNAAKIFNLyPRKGRIAVG 404
Cdd:PRK08044 308 EIDCLVSDHSPCPPEMKA---GNIMEAWGGIAGLQNCMDVMFDEAVQKRGMSLPMFGKLMATNAADIFGL-QQKGRIAPG 383
|
410 420
....*....|....*....|
gi 25742568 405 SDSDLVIWDPDAVKIVSAKN 424
Cdd:PRK08044 384 KDADFVFIQPNSSYVLKNED 403
|
|
| pyrC |
PRK09357 |
dihydroorotase; Validated |
16-456 |
1.53e-35 |
|
dihydroorotase; Validated
Pssm-ID: 236479 [Multi-domain] Cd Length: 423 Bit Score: 138.02 E-value: 1.53e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25742568 16 RLLIKGGRIVNDDQSFY-ADIYMEDGLIKQIGDNLIVPGgVKTIEANGKMVMPGGIDVHTHFQMPykGMTTVDDFFQGTK 94
Cdd:PRK09357 2 MILIKNGRVIDPKGLDEvADVLIDDGKIAAIGENIEAEG-AEVIDATGLVVAPGLVDLHVHLREP--GQEDKETIETGSR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25742568 95 AALAGGTTMiidhVV------PEPESSLTEAYEKWRewADGKSCCDyaLHV--DIThwndsVKQEVQNLS-----KEKGV 161
Cdd:PRK09357 79 AAAAGGFTT----VVampntkPVIDTPEVVEYVLDR--AKEAGLVD--VLPvgAIT-----KGLAGEELTefgalKEAGV 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25742568 162 NSFMvymayKDLYQVSNTEL-YEIFTCLGELG-AIAQvHAE----NGDIIAQEQARMLEMGITGpeghvlsRPEELEAEA 235
Cdd:PRK09357 146 VAFS-----DDGIPVQDARLmRRALEYAKALDlLIAQ-HCEdpslTEGGVMNEGEVSARLGLPG-------IPAVAEEVM 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25742568 236 VFRAITVASQTNCPLYVTKVMSKSAADLISQARKKGnvvfgEPITA------------SLGIDGTHYwsknwaKAAafvt 303
Cdd:PRK09357 213 IARDVLLAEATGARVHICHVSTAGSVELIRWAKALG-----IKVTAevtphhllltdeDLLTYDPNY------KVN---- 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25742568 304 sPPLSpdptTPDYINSL---LASGDLQLSGSAHCTFSTAQKAIGkdnFTAIPEGTNGVEERMSVIWDKAVATGKMDENQF 380
Cdd:PRK09357 278 -PPLR----TEEDREALiegLKDGTIDAIATDHAPHAREEKECE---FEAAPFGITGLETALSLLYTTLVKTGLLDLEQL 349
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 25742568 381 VAVTSTNAAKIFNLYPrkGRIAVGSDSDLVIWDPDAVKIVSAKNHQSVAEYNIFEGMELRGAPLVVICQGKIMLED 456
Cdd:PRK09357 350 LEKMTINPARILGLPA--GPLAEGEPADLVIFDPEAEWTVDGEDFASKGKNTPFIGMKLKGKVVYTIVDGKIVYQD 423
|
|
| DHOase_IIa |
cd01317 |
Dihydroorotase (DHOase), subgroup IIa; DHOases catalyze the reversible interconversion of ... |
54-444 |
1.88e-31 |
|
Dihydroorotase (DHOase), subgroup IIa; DHOases catalyze the reversible interconversion of carbamoyl aspartate to dihydroorotate, a key reaction in pyrimidine biosynthesis. This subgroup also contains proteins that lack the active site, like unc-33, a C.elegans protein involved in axon growth.
Pssm-ID: 238642 [Multi-domain] Cd Length: 374 Bit Score: 125.43 E-value: 1.88e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25742568 54 GVKTIEANGKMVMPGGIDVHTHFQMPykGMTTVDDFFQGTKAALAGGTTmiidHVVPEPESslteayekwREWADgkscc 133
Cdd:cd01317 1 DAEVIDAEGKILAPGLVDLHVHLREP--GFEYKETLESGAKAAAAGGFT----TVVCMPNT---------NPVID----- 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25742568 134 dyalhvdithwNDSVKQEVQNLSKEKGVNSFMVYMAY-KDLYQVSNTELYEiftcLGELGAIA----QVHAENGDIIAQ- 207
Cdd:cd01317 61 -----------NPAVVELLKNRAKDVGIVRVLPIGALtKGLKGEELTEIGE----LLEAGAVGfsddGKPIQDAELLRRa 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25742568 208 -EQARMLEMGIT----------------GPEGHVL---SRPEELEAEAVFRAITVASQTNCPLYVTKVMSKSAADLISQA 267
Cdd:cd01317 126 lEYAAMLDLPIIvhpedpslagggvmneGKVASRLglpGIPPEAETIMVARDLELAEATGARVHFQHLSTARSLELIRKA 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25742568 268 RKKGnvvfgEPITASLGIdgtHYWS------KNWAkaAAFVTSPPLSpDPTTPDYINSLLASGDLQLSGSAHCTFSTAQK 341
Cdd:cd01317 206 KAKG-----LPVTAEVTP---HHLLlddealESYD--TNAKVNPPLR-SEEDREALIEALKDGTIDAIASDHAPHTDEEK 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25742568 342 AIGkdnFTAIPEGTNGVEERMSVIWDKAVATGKMDENQFVAVTSTNAAKIFNLYPrkGRIAVGSDSDLVIWDPDAVKIVS 421
Cdd:cd01317 275 DLP---FAEAPPGIIGLETALPLLWTLLVKGGLLTLPDLIRALSTNPAKILGLPP--GRLEVGAPADLVLFDPDAEWIVD 349
|
410 420
....*....|....*....|...
gi 25742568 422 AKNHQSVAEYNIFEGMELRGAPL 444
Cdd:cd01317 350 EETFRSKSKNTPFDGQKLKGRVL 372
|
|
| PRK07575 |
PRK07575 |
dihydroorotase; Provisional |
14-459 |
1.97e-31 |
|
dihydroorotase; Provisional
Pssm-ID: 236055 [Multi-domain] Cd Length: 438 Bit Score: 126.71 E-value: 1.97e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25742568 14 SDRLLIKGGRIVNDDQSFY-ADIYMEDGLIKQIGDNLIVPGGVKTIEANGKMVMPGGIDVHTHFQMPykGMTTVDDFFQG 92
Cdd:PRK07575 2 MMSLLIRNARILLPSGELLlGDVLVEDGKIVAIAPEISATAVDTVIDAEGLTLLPGVIDPQVHFREP--GLEHKEDLFTA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25742568 93 TKAALAGGTTMIIDHVVPEPESSLTEAYEKWREWADGKSCCDYALHVDITHWNDSVKQEVQNLSkekGVNSFMVYMaYKD 172
Cdd:PRK07575 80 SRACAKGGVTSFLEMPNTKPLTTTQAALDDKLARAAEKCVVNYGFFIGATPDNLPELLTANPTC---GIKIFMGSS-HGP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25742568 173 LYQVSNTELYEIFTCLGELgaIAqVHAENGDIIAQEQARMleMGITGPEGHVLSRPEELEAEAVFRAITVASQTNCPLYV 252
Cdd:PRK07575 156 LLVDEEAALERIFAEGTRL--IA-VHAEDQARIRARRAEF--AGISDPADHSQIQDEEAALLATRLALKLSKKYQRRLHI 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25742568 253 TKVMSKSAADLISQArkKGNVVFGEPITASLGIDGTHYwsknwAKAAAFV-TSPPLSpDPTTPDYINSLLASGDLQLSGS 331
Cdd:PRK07575 231 LHLSTAIEAELLRQD--KPSWVTAEVTPQHLLLNTDAY-----ERIGTLAqMNPPLR-SPEDNEALWQALRDGVIDFIAT 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25742568 332 AHCTFSTAQKAIGKDNftaIPEGTNGVEERMSVIWDKAVAtGKMDENQFVAVTSTNAAKIFNLyPRKGRIAVGSDSDLVI 411
Cdd:PRK07575 303 DHAPHTLEEKAQPYPN---SPSGMPGVETSLPLMLTAAMR-GKCTVAQVVRWMSTAVARAYGI-PNKGRIAPGYDADLVL 377
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 25742568 412 WDPDAVKIVSAKNHQSVAEYNIFEGMELRGAPLVVICQGKIMLEDGNL 459
Cdd:PRK07575 378 VDLNTYRPVRREELLTKCGWSPFEGWNLTGWPVTTIVGGQIVFDRGQV 425
|
|
| PRK09060 |
PRK09060 |
dihydroorotase; Validated |
17-467 |
2.14e-30 |
|
dihydroorotase; Validated
Pssm-ID: 181632 [Multi-domain] Cd Length: 444 Bit Score: 123.88 E-value: 2.14e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25742568 17 LLIKGGRIVNDDQSFYADIYMEDGLIKQIGDNLIVPGGvKTIEANGKMVMPGGIDVHTHFQMPykGMTTVDDFFQGTKAA 96
Cdd:PRK09060 7 LILKGGTVVNPDGEGRADIGIRDGRIAAIGDLSGASAG-EVIDCRGLHVLPGVIDSQVHFREP--GLEHKEDLETGSRAA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25742568 97 LAGGTTMIIDHVVPEPESSLTEAYEKWREWADGKSCCDYALHVDITHWNdsvKQEVQNLSKEKGVNSFMVYM--AYKDLY 174
Cdd:PRK09060 84 VLGGVTAVFEMPNTNPLTTTAEALADKLARARHRMHCDFAFYVGGTRDN---ADELAELERLPGCAGIKVFMgsSTGDLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25742568 175 QVSNTELYEIftclgeLGAI---AQVHAEngdiiaqEQARMLEMGITGPEGHVLSRPEELEAEAVFRA----ITVASQTN 247
Cdd:PRK09060 161 VEDDEGLRRI------LRNGrrrAAFHSE-------DEYRLRERKGLRVEGDPSSHPVWRDEEAALLAtrrlVRLARETG 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25742568 248 CPLYVTKVMSKSAADLISQARkkgNVVFGEPITASLGIDGTHYWSKNWAKAaafVTSPPLSpDPTTPDYINSLLASGDLQ 327
Cdd:PRK09060 228 RRIHVLHVSTAEEIDFLADHK---DVATVEVTPHHLTLAAPECYERLGTLA---QMNPPIR-DARHRDGLWRGVRQGVVD 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25742568 328 LSGSAHCTFSTAQKAigkDNFTAIPEGTNGVEERMSVIWDKaVATGKMDENQFVAVTSTNAAKIFNLyPRKGRIAVGSDS 407
Cdd:PRK09060 301 VLGSDHAPHTLEEKA---KPYPASPSGMTGVQTLVPIMLDH-VNAGRLSLERFVDLTSAGPARIFGI-AGKGRIAVGYDA 375
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 25742568 408 DLVIWDPDAVKIVSAKNHQSVAEYNIFEGMELRGAPLVVICQGKIMLEDGNLhVTQGAGR 467
Cdd:PRK09060 376 DFTIVDLKRRETITNEWIASRCGWTPYDGKEVTGWPVGTIVRGQRVMWDGEL-VGPPTGE 434
|
|
| PLN02795 |
PLN02795 |
allantoinase |
12-469 |
6.57e-30 |
|
allantoinase
Pssm-ID: 178392 [Multi-domain] Cd Length: 505 Bit Score: 123.35 E-value: 6.57e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25742568 12 ITSDRLLIKGGRIVNDdqsfyadIYMEDGLIKQIGDNLIVPG---GVKTIEANGKMVMPGGIDVHTHFQMPykGMTTVDD 88
Cdd:PLN02795 48 LYSKRVVTPAGVIPGA-------VEVEGGRIVSVTKEEEAPKsqkKPHVLDYGNAVVMPGLIDVHVHLNEP--GRTEWEG 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25742568 89 FFQGTKAALAGGTTMIIDhvVP---EPESSLTEAYEKWREWADGKsccdyaLHVDITHWNDSVKQEVQNLSKEK------ 159
Cdd:PLN02795 119 FPTGTKAAAAGGITTLVD--MPlnsFPSTTSVETLELKIEAAKGK------LYVDVGFWGGLVPENAHNASVLEelldag 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25742568 160 --GVNSFMVYMAYKDLYQVSNTELYEIFTCLGELGAIAQVHAENGDIIAQEQarMLEMGITGPEGHVLSRPEELEAEAVF 237
Cdd:PLN02795 191 alGLKSFMCPSGINDFPMTTATHIKAALPVLAKYGRPLLVHAEVVSPVESDS--RLDADPRSYSTYLKSRPPSWEQEAIR 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25742568 238 RAITVASQTN-------CPLYVTKVM-SKSAADLISQARKKGNVVFGEPITASLGI------DGthywsknwakAAAFVT 303
Cdd:PLN02795 269 QLLEVAKDTRpggvaegAHVHIVHLSdAESSLELIKEAKAKGDSVTVETCPHYLAFsaeeipDG----------DTRYKC 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25742568 304 SPPLSpDPTTPDYINSLLASGDLQLSGSAHCTFSTAQKAIGKDNFTAIPEGTNGVEERMSVIWDKAVATGkMDENQFVAV 383
Cdd:PLN02795 339 APPIR-DAANRELLWKALLDGDIDMLSSDHSPSPPDLKLLEEGNFLRAWGGISSLQFVLPATWTAGRAYG-LTLEQLARW 416
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25742568 384 TSTNAAKIFNLyPRKGRIAVGSDSDLVIWDPDAVKIVSAK-----NHQSVAEYnifEGMELRGAPLVVICQGKIMLEDGN 458
Cdd:PLN02795 417 WSERPAKLAGL-DSKGAIAPGKDADIVVWDPEAEFVLDESypiyhKHKSLSPY---LGTKLSGKVIATFVRGNLVFLEGK 492
|
490
....*....|.
gi 25742568 459 lHVTQGAGRFI 469
Cdd:PLN02795 493 -HAKQACGSPI 502
|
|
| PRK04250 |
PRK04250 |
dihydroorotase; Provisional |
22-457 |
2.19e-29 |
|
dihydroorotase; Provisional
Pssm-ID: 235265 [Multi-domain] Cd Length: 398 Bit Score: 120.26 E-value: 2.19e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25742568 22 GRIVNDDQSFYADIYMEDGLIKQIGDNLIvpGGVKTIEANGKMVMPGGIDVHTH---FQMPYKgmTTVDdffQGTKAALA 98
Cdd:PRK04250 4 GKFLLKGRIVEGGIGIENGRISKISLRDL--KGKEVIKVKGGIILPGLIDVHVHlrdFEESYK--ETIE---SGTKAALH 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25742568 99 GGTTMIIDHVVPEPESSLTEAYEKWREWADGKSCCDYALHVDITHWNDSVKQEVQNLSKEkgvnsFMVyMAYKDLYQVSN 178
Cdd:PRK04250 77 GGITLVFDMPNTKPPIMDEKTYEKRMRIAEKKSYADYALNFLIAGNCEKAEEIKADFYKI-----FMG-ASTGGIFSENF 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25742568 179 TELYEiftclgELGAIAQVHAENGDIIAQEqarmlemgitgPEghvlsRPEELEAEAVFRAITVASQTNCPLYVTKVMSK 258
Cdd:PRK04250 151 EVDYA------CAPGIVSVHAEDPELIREF-----------PE-----RPPEAEVVAIERALEAGKKLKKPLHICHISTK 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25742568 259 SAADLISQARKkgnvvfgEPITASLGIDGTHYWSKNWAKAAAFVTSPPLSpdpTTPDYINSLLASGDLQLSGSAHCTFST 338
Cdd:PRK04250 209 DGLKLILKSNL-------PWVSFEVTPHHLFLTRKDYERNPLLKVYPPLR---SEEDRKALWENFSKIPIIASDHAPHTL 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25742568 339 AQKAIGKdnfTAIPegtnGVEERMSVIWDkAVATGKMDENQFVAVTSTNAAKIFNlYPRKGrIAVGSDSDLVIWDPDAVK 418
Cdd:PRK04250 279 EDKEAGA---AGIP----GLETEVPLLLD-AANKGMISLFDIVEKMHDNPARIFG-IKNYG-IEEGNYANFAVFDMKKEW 348
|
410 420 430
....*....|....*....|....*....|....*....
gi 25742568 419 IVSAKNHQSVAEYNIFEGMELRGAPLVVICQGKIMLEDG 457
Cdd:PRK04250 349 TIKAEELYTKAGWTPYEGFKLKGKVIMTILRGEVVMEDD 387
|
|
| PRK01211 |
PRK01211 |
dihydroorotase; Provisional |
32-470 |
1.95e-23 |
|
dihydroorotase; Provisional
Pssm-ID: 179247 [Multi-domain] Cd Length: 409 Bit Score: 102.63 E-value: 1.95e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25742568 32 YADIYMEDGLIKQIGDNLivpGGVKTIEANGkMVMPGGIDVHTHFQMPykGMTTVDDFFQGTKAALAGGTTMIIDHVVPE 111
Cdd:PRK01211 15 YLEIEVEDGKIKSIKKDA---GNIGKKELKG-AILPAATDIHVHFRTP--GETEKEDFSTGTLSAIFGGTTFIMDMPNNN 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25742568 112 PESSLTEAYEKWREWADGKSCCDYALHVDITHWNDSVKQEVQnlskekgvNSFMVYMAYKDLYQVSNTELYEIfTCLGEL 191
Cdd:PRK01211 89 IPIKDYNAFSDKLGRVAPKAYVDFSLYSMETGNNALILDERS--------IGLKVYMGGTTNTNGTDIEGGEI-KKINEA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25742568 192 GAIAQVHAENGDIIAQEQARMLEMgitgpEGHVLSRPEELEAEAVFRAITVASQtncplyvTKVMS-KSAADLISQarkk 270
Cdd:PRK01211 160 NIPVFFHAELSECLRKHQFESKNL-----RDHDLARPIECEIKAVKYVKNLDLK-------TKIIAhVSSIDVIGR---- 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25742568 271 gnvvFGEPITASlgidgtHYWSKNWAKAAAF-VTSPPLSPDPTTPDYINSLLaSGDLQLSGSAHCTFSTAQKAigkdNFT 349
Cdd:PRK01211 224 ----FLREVTPH------HLLLNDDMPLGSYgKVNPPLRDRWTQERLLEEYI-SGRFDILSSDHAPHTEEDKQ----EFE 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25742568 350 AIPEGTNGVEERMSVIWdKAVATGKMDENQFVAVTSTNAAKIFNLypRKGRIAVGSDSDLVIWDPDAVKIVSAKNHQSVA 429
Cdd:PRK01211 289 YAKSGIIGVETRVPLFL-ALVKKKILPLDVLYKTAIERPASLFGI--KKGKIEEGYDADFMAFDFTNIKKINDKRLHSKC 365
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 25742568 430 EYNIFEGMELRgAPLVVICQGKIMLEDGNLhVTQGAGRFIP 470
Cdd:PRK01211 366 PVSPFNGFDAI-FPSHVIMRGEVVIDNYEL-ISERTGKFVP 404
|
|
| Amidohydro_1 |
pfam01979 |
Amidohydrolase family; This family of enzymes are a a large metal dependent hydrolase ... |
64-453 |
6.95e-23 |
|
Amidohydrolase family; This family of enzymes are a a large metal dependent hydrolase superfamily. The family includes Adenine deaminase EC:3.5.4.2 that hydrolyses adenine to form hypoxanthine and ammonia. Adenine deaminases reaction is important for adenine utilization as a purine and also as a nitrogen source. This family also includes dihydroorotase and N-acetylglucosamine-6-phosphate deacetylases, EC:3.5.1.25 These enzymes catalyze the reaction N-acetyl-D-glucosamine 6-phosphate + H2O <=> D-glucosamine 6-phosphate + acetate. This family includes the catalytic domain of urease alpha subunit. Dihydroorotases (EC:3.5.2.3) are also included.
Pssm-ID: 460401 [Multi-domain] Cd Length: 334 Bit Score: 99.88 E-value: 6.95e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25742568 64 MVMPGGIDVHTHFQM------PYKGMTTVDDFFQGTKAALAGGTTMIIDHVVPEPESSLT--EAYEKWRE--WADGKSCC 133
Cdd:pfam01979 1 IVLPGLIDAHVHLEMgllrgiPVPPEFAYEALRLGITTMLKSGTTTVLDMGATTSTGIEAllEAAEELPLglRFLGPGCS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25742568 134 ---DYALHVDIThwndSVKQEVQNLSKEKGVNSFMVYMAYKD--LYQVSNTELYEIFTCLGELGAIAQVHAENGDIiaqE 208
Cdd:pfam01979 81 ldtDGELEGRKA----LREKLKAGAEFIKGMADGVVFVGLAPhgAPTFSDDELKAALEEAKKYGLPVAIHALETKG---E 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25742568 209 QARMLEMGITGPEghVLSRPEELEAEAVFRAITVASQTNCPLYVTkvmskSAADLISQARKKGNVvfgepitasLGIDGT 288
Cdd:pfam01979 154 VEDAIAAFGGGIE--HGTHLEVAESGGLLDIIKLILAHGVHLSPT-----EANLLAEHLKGAGVA---------HCPFSN 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25742568 289 HYWSKNWAKAAAfvtspplspdpttpdyinsLLASGDLQLSGSAHCtfstaqkaIGKDNFTAIPEGTNGVEERmsviwdk 368
Cdd:pfam01979 218 SKLRSGRIALRK-------------------ALEDGVKVGLGTDGA--------GSGNSLNMLEELRLALELQ------- 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25742568 369 AVATGKMDENQFVAVTSTNAAKIFNLYPRKGRIAVGSDSDLVIWDPDavkivsaknhqsvaEYNIFEGMELRGAPLVVIC 448
Cdd:pfam01979 264 FDPEGGLSPLEALRMATINPAKALGLDDKVGSIEVGKDADLVVVDLD--------------PLAAFFGLKPDGNVKKVIV 329
|
....*
gi 25742568 449 QGKIM 453
Cdd:pfam01979 330 KGKIV 334
|
|
| PRK09236 |
PRK09236 |
dihydroorotase; Reviewed |
15-460 |
9.86e-22 |
|
dihydroorotase; Reviewed
Pssm-ID: 181716 Cd Length: 444 Bit Score: 98.02 E-value: 9.86e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25742568 15 DRLLIKGGRIVNDDQSFYADIYMEDGLIKQIGDNLIVPGGVKTIEANGKMVMPGGIDVHTHFQMPykGMTTVDDFFQGTK 94
Cdd:PRK09236 2 KRILIKNARIVNEGKIFEGDVLIENGRIAKIASSISAKSADTVIDAAGRYLLPGMIDDQVHFREP--GLTHKGDIASESR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25742568 95 AALAGGTTMIID--HVVPepeSSLT-EAYEKWREWADGKSCCDYALHVDIThwNDSVkQEVQNLSKEK--GVNSFM---- 165
Cdd:PRK09236 80 AAVAGGITSFMEmpNTNP---PTTTlEALEAKYQIAAQRSLANYSFYFGAT--NDNL-DEIKRLDPKRvcGVKVFMgast 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25742568 166 ----VymaykDLYQVsnteLYEIFTCLGELgaIAqVHAENGDIIAQEQARMLEM---GITgPEGHVLSRpeelEAEAVFR 238
Cdd:PRK09236 154 gnmlV-----DNPET----LERIFRDAPTL--IA-THCEDTPTIKANLAKYKEKygdDIP-AEMHPLIR----SAEACYK 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25742568 239 ----AITVASQTNCPLYVTKVMSKSAADLISQ---ARKKgnvvfgepITASLGIDGTHYWSKNWAKAAAFVTSPPLSPDP 311
Cdd:PRK09236 217 ssslAVSLAKKHGTRLHVLHISTAKELSLFENgplAEKR--------ITAEVCVHHLWFDDSDYARLGNLIKCNPAIKTA 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25742568 312 TTPDYINSLLASGDLQLSGSAHCTFSTAQKaigKDNFTAIPEGTNGVEERMSVIWDKaVATGKMDENQFVAVTSTNAAKI 391
Cdd:PRK09236 289 SDREALRQALADDRIDVIATDHAPHTWEEK---QGPYFQAPSGLPLVQHALPALLEL-VHEGKLSLEKVVEKTSHAPAIL 364
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 25742568 392 FNLyPRKGRIAVGSDSDLVIWDPDAVKIVSAKNHQSVAEYNIFEGMELRGAPLVVICQGKIMLEDGNLH 460
Cdd:PRK09236 365 FDI-KERGFIREGYWADLVLVDLNSPWTVTKENILYKCGWSPFEGRTFRSRVATTFVNGQLVYHNGQLV 432
|
|
| ATZ_TRZ_like |
cd01298 |
TRZ/ATZ family contains enzymes from the atrazine degradation pathway and related hydrolases. ... |
17-122 |
1.41e-13 |
|
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: 72.62 E-value: 1.41e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25742568 17 LLIKGGRIVNDDQS---FYADIYMEDGLIKQIGDNLIVPG--GVKTIEANGKMVMPGGIDVHTHFQM------------- 78
Cdd:cd01298 1 ILIRNGTIVTTDPRrvlEDGDVLVEDGRIVAVGPALPLPAypADEVIDAKGKVVMPGLVNTHTHLAMtllrgladdlplm 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 25742568 79 --------PYKGMTTVDDFFQGTKAALA----GGTTMIIDHVVPEPEsSLTEAYEK 122
Cdd:cd01298 81 ewlkdliwPLERLLTEEDVYLGALLALAemirSGTTTFADMYFFYPD-AVAEAAEE 135
|
|
| HutI |
COG1228 |
Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport ... |
13-422 |
1.62e-13 |
|
Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440841 [Multi-domain] Cd Length: 386 Bit Score: 72.30 E-value: 1.62e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25742568 13 TSDRLLIKGGRIVNDDQSFY---ADIYMEDGLIKQIGDN--LIVPGGVKTIEANGKMVMPGGIDVHTHFQMPYKGMT--- 84
Cdd:COG1228 6 QAGTLLITNATLVDGTGGGVienGTVLVEDGKIAAVGPAadLAVPAGAEVIDATGKTVLPGLIDAHTHLGLGGGRAVefe 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25742568 85 -------TVDDFFQGTK---AALAGGTTMIIDH------VVPEPESSLTEAYEKWREWADGKS-CCDYALHvdiTHWNDS 147
Cdd:COG1228 86 agggitpTVDLVNPADKrlrRALAAGVTTVRDLpggplgLRDAIIAGESKLLPGPRVLAAGPAlSLTGGAH---ARGPEE 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25742568 148 VKQEVQNLsKEKGVNSFMVYMAYKDlYQVSNTELYEIFTCLGELGAIAQVHAENGDIIaqeqARMLEMGITGPEgHVLSR 227
Cdd:COG1228 163 ARAALREL-LAEGADYIKVFAEGGA-PDFSLEELRAILEAAHALGLPVAAHAHQADDI----RLAVEAGVDSIE-HGTYL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25742568 228 PEEleaeavfraitvasqtncplyvtkvmsksAADLIsqaRKKGNVVfgepitaslgidgthywsknwakaaafvtsppL 307
Cdd:COG1228 236 DDE-----------------------------VADLL---AEAGTVV--------------------------------L 251
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25742568 308 SPDPTTPDYINSLLASGDLQLSGSAHC-TFSTAQK--------AIGKDNFTAIPEGTNGVEErmsvIWdKAVATGkMDEN 378
Cdd:COG1228 252 VPTLSLFLALLEGAAAPVAAKARKVREaALANARRlhdagvpvALGTDAGVGVPPGRSLHRE----LA-LAVEAG-LTPE 325
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 25742568 379 Q-FVAVTStNAAKIFNLYPRKGRIAVGSDSDLVIWDPDAVKIVSA 422
Cdd:COG1228 326 EaLRAATI-NAAKALGLDDDVGSLEPGKLADLVLLDGDPLEDIAY 369
|
|
| pyrC |
PRK00369 |
dihydroorotase; Provisional |
34-468 |
3.69e-12 |
|
dihydroorotase; Provisional
Pssm-ID: 234738 [Multi-domain] Cd Length: 392 Bit Score: 68.25 E-value: 3.69e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25742568 34 DIYMEDGlIKQIGDNLIVpgGVKTIEANGK---------MVMPGGIDVHTHF---QMPYKgmttvDDFFQGTKAALAGGT 101
Cdd:PRK00369 8 KAYLGKE-IKEICINFDR--RIKEIKSRCKpdldlpqgtLILPGAIDLHVHLrglKLSYK-----EDVASGTSEAAYGGV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25742568 102 TMIIDHVVPEPESSLTEAY-EKWREWADGkSCCDYALHVDIThwnDSVKqEVQNLskekGVNSFMVYMayKDLyqvsntE 180
Cdd:PRK00369 80 TLVADMPNTIPPLNTPEAItEKLAELEYY-SRVDYFVYSGVT---KDPE-KVDKL----PIAGYKIFP--EDL------E 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25742568 181 LYEIFTCLGELGAIAQVHAEngdiiaqeqarmLEMGITGPEGhvLSRPEELEAEAVFRAITVASqtncpLYVTKVmskSA 260
Cdd:PRK00369 143 REETFRVLLKSRKLKILHPE------------VPLALKSNRK--LRRNCWYEIAALYYVKDYQN-----VHITHA---SN 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25742568 261 ADLISQARKKGnvvFGEPITAS-LGIDG-THYWSKnwakaaafvTSPPLSpDPTTPDYINSLLASGDLQLSGsaHCTFST 338
Cdd:PRK00369 201 PRTVRLAKELG---FTVDITPHhLLVNGeKDCLTK---------VNPPIR-DINERLWLLQALSEVDAIASD--HAPHSS 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25742568 339 AQKaigKDNFTAIPEGTNGVEERMSVIWdKAVATGKMDENQFVAVTSTNAAKIFNLypRKGRIAVGSDSDLVIwdpdaVK 418
Cdd:PRK00369 266 FEK---LQPYEVCPPGIAALSFTPPFIY-TLVSKGILSIDRAVELISTNPARILGI--PYGEIKEGYRANFTV-----IQ 334
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 25742568 419 IVSAKNHQ--SVAEYNIFEGMELRGAPLVVICQGKIMLEDGNLHVTQGAGRF 468
Cdd:PRK00369 335 FEDWRYSTkySKVIETPLDGFELKASVYATIVQGKLAYLEGEVFPVKGINPF 386
|
|
| D-aminoacylase |
cd01297 |
D-aminoacylases (N-acyl-D-Amino acid amidohydrolases) catalyze the hydrolysis of ... |
17-467 |
1.46e-11 |
|
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: 66.55 E-value: 1.46e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25742568 17 LLIKGGRIVndDQS----FYADIYMEDGLIKQIGDNLIVPGgVKTIEANGKMVMPGGIDVHTHfqmpYKGMTTVDDFFqg 92
Cdd:cd01297 2 LVIRNGTVV--DGTgappFTADVGIRDGRIAAIGPILSTSA-REVIDAAGLVVAPGFIDVHTH----YDGQVFWDPDL-- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25742568 93 TKAALAGGTTMIIDH-------VVPEPESSLTEAYEKWREWADGK-----SCCDYALHVD------------------IT 142
Cdd:cd01297 73 RPSSRQGVTTVVLGNcgvspapANPDDLARLIMLMEGLVALGEGLpwgwaTFAEYLDALEarppavnvaalvghaalrRA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25742568 143 HWNDSVKQ----EVQNLSK--EKGVNS----FMVYMAYKDLYQVSNTELYEIFTCLGELGAIAQVHAEN-GDIIAQEQAR 211
Cdd:cd01297 153 VMGLDAREateeELAKMREllREALEAgalgISTGLAYAPRLYAGTAELVALARVAARYGGVYQTHVRYeGDSILEALDE 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25742568 212 MLEMGitgpeghvlsrpEELEAEAVFRAITVASQTNCPLYvtkvmsKSAADLISQARKKGNVVFGE--PITASLGidgth 289
Cdd:cd01297 233 LLRLG------------RETGRPVHISHLKSAGAPNWGKI------DRLLALIEAARAEGLQVTADvyPYGAGSE----- 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25742568 290 ywsknwAKAAAFVTSPPlspdpttpdyinsLLASGDLQLSGSAH----CTFStaqKAIGKdnftaipegtnGVEERMSVI 365
Cdd:cd01297 290 ------DDVRRIMAHPV-------------VMGGSDGGALGKPHprsyGDFT---RVLGH-----------YVRERKLLS 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25742568 366 WDKAVAtgKMdenqfvavtSTNAAKIFNLYPRkGRIAVGSDSDLVIWDPDAVKIVS---AKNHQSvaeynifEGMELrga 442
Cdd:cd01297 337 LEEAVR--KM---------TGLPARVFGLADR-GRIAPGYRADIVVFDPDTLADRAtftRPNQPA-------EGIEA--- 394
|
490 500
....*....|....*....|....*
gi 25742568 443 plvVICQGKIMLEDGnLHVTQGAGR 467
Cdd:cd01297 395 ---VLVNGVPVVRDG-AFTGARPGR 415
|
|
| CAD_DHOase |
cd01316 |
The eukaryotic CAD protein is a trifunctional enzyme of carbamoylphosphate ... |
66-466 |
3.82e-11 |
|
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: 64.78 E-value: 3.82e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25742568 66 MPGGIDVHTHFQMPykGMTTVDDFFQGTKAALAGGTTMIidHVVPEPESSL--TEAYEKWREWADGKSCCDYALHVDITH 143
Cdd:cd01316 5 LPGLIDVHVHLREP--GATHKEDFASGTKAALAGGFTMV--RAMPNTNPSIvdVASLKLVQSLAQAKARCDYAFSIGATS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25742568 144 WNDSvkqEVQNLSKEKGVNSFMVYMAYKDLYQVSNTELYEIFTCLGELGAIAqVHAENGDIIAqeqarmlemgitgpegh 223
Cdd:cd01316 81 TNAA---TVGELASEAVGLKFYLNETFSTLILDKITAWASHFNAWPSTKPIV-THAKSQTLAA----------------- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25742568 224 vlsrpeeleaeavfrAITVASQTNCPLYVTKVMSKSAADLISQARKKGNVVFGEPITASLGI---DGTHYWSknwakaaa 300
Cdd:cd01316 140 ---------------VLLLASLHNRSIHICHVSSKEEINLIRLAKARGLKVTCEVSPHHLFLsqdDLPRGQY-------- 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25742568 301 fvtspPLSPDPTTPDYINSL---LASGDLQLSGSAHCTFstAQKAIGKdnftaIPEGTNGVEERMSVIWdKAVATGKMDE 377
Cdd:cd01316 197 -----EVRPFLPTREDQEALwenLDYIDCFATDHAPHTL--AEKTGNK-----PPPGFPGVETSLPLLL-TAVHEGRLTI 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25742568 378 NQFVAVTSTNAAKIFNLYPRkgriavgSDSDLVIwDPDAVKIVSAKNHQSVAEYNIFEGMELRGAPLVVICQGKIMLEDG 457
Cdd:cd01316 264 EDIVDRLHTNPKRIFNLPPQ-------SDTYVEV-DLDEEWTIPKNPLQSKKGWTPFEGKKVKGKVQRVVLRGETAFIDG 335
|
....*....
gi 25742568 458 NLHVTQGAG 466
Cdd:cd01316 336 EIVAPPGFG 344
|
|
| COG3653 |
COG3653 |
N-acyl-D-aspartate/D-glutamate deacylase [Secondary metabolites biosynthesis, transport and ... |
17-75 |
2.88e-10 |
|
N-acyl-D-aspartate/D-glutamate deacylase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442870 [Multi-domain] Cd Length: 528 Bit Score: 62.88 E-value: 2.88e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 25742568 17 LLIKGGRIVN--DDQSFYADIYMEDGLIKQIGDnLIVPGGVKTIEANGKMVMPGGIDVHTH 75
Cdd:COG3653 4 LLIRGGTVVDgtGAPPFRADVAIKGGRIVAVGD-LAAAEAARVIDATGLVVAPGFIDIHTH 63
|
|
| SsnA |
COG0402 |
Cytosine/adenosine deaminase or related metal-dependent hydrolase [Nucleotide transport and ... |
16-122 |
8.13e-10 |
|
Cytosine/adenosine deaminase or related metal-dependent hydrolase [Nucleotide transport and metabolism, General function prediction only]; Cytosine/adenosine deaminase or related metal-dependent hydrolase is part of the Pathway/BioSystem: Pyrimidine salvage
Pssm-ID: 440171 [Multi-domain] Cd Length: 416 Bit Score: 61.00 E-value: 8.13e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25742568 16 RLLIKGGRIV--NDDQSFYAD--IYMEDGLIKQIGDNLIVP---GGVKTIEANGKMVMPGGIDVHTH-FQMPYKGMT--- 84
Cdd:COG0402 1 DLLIRGAWVLtmDPAGGVLEDgaVLVEDGRIAAVGPGAELParyPAAEVIDAGGKLVLPGLVNTHTHlPQTLLRGLAddl 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 25742568 85 -----------------TVDDFFQGTKAA----LAGGTTMIIDH--VVPEPESSLTEAYEK 122
Cdd:COG0402 81 plldwleeyiwplearlDPEDVYAGALLAlaemLRSGTTTVADFyyVHPESADALAEAAAE 141
|
|
| PRK09237 |
PRK09237 |
amidohydrolase/deacetylase family metallohydrolase; |
17-413 |
4.06e-09 |
|
amidohydrolase/deacetylase family metallohydrolase;
Pssm-ID: 236423 [Multi-domain] Cd Length: 380 Bit Score: 58.71 E-value: 4.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25742568 17 LLIKGGRIVNDDQSFYA--DIYMEDGLIKQIGDNLIVPGGVKTIEANGKMVMPGGIDVHTHFqmpYKGMTtvDDFFQGTK 94
Cdd:PRK09237 1 LLLRGGRVIDPANGIDGviDIAIEDGKIAAVAGDIDGSQAKKVIDLSGLYVSPGWIDLHVHV---YPGST--PYGDEPDE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25742568 95 AALAGGTTMIIDhvvpepesslteayekwrewADGKSCCDYalhvdithwnDSVKQEVQNLSKEKgvnsfmVYmAYKDLY 174
Cdd:PRK09237 76 VGVRSGVTTVVD--------------------AGSAGADNF----------DDFRKLTIEASKTR------VL-AFLNIS 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25742568 175 QV---SNTELYEIFTClgELGAIAQVHAENGDIIAQEQARMlEMGITGPEGhvlSRPEEleaeavfRAITVASQTNCPLY 251
Cdd:PRK09237 119 RIgllAQDELADLEDI--DADAVAEAVKRNPDFIVGIKARM-SSSVVGDNG---IEPLE-------LAKAIAAEANLPLM 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25742568 252 VTKVMSKSAADLISQARKKGNVVfgepitaslgidgTHYWSKnwaKAAAFVTspplsPDPTTPDYINSLLASGdLQLS-- 329
Cdd:PRK09237 186 VHIGNPPPSLEEILELLRPGDIL-------------THCFNG---KPNRILD-----EDGELRPSVLEALERG-VRLDvg 243
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25742568 330 -GSAHCTFSTAQKAIGKD-NFTAIpeGT--------NGVEERMSVIWDKAVATGkMDENQFVAVTSTNAAKIFNLyPRKG 399
Cdd:PRK09237 244 hGTASFSFKVAEAAIAAGiLPDTI--STdiycrnriNGPVYSLATVMSKFLALG-MPLEEVIAAVTKNAADALRL-PELG 319
|
410
....*....|....
gi 25742568 400 RIAVGSDSDLVIWD 413
Cdd:PRK09237 320 RLQVGSDADLTLFT 333
|
|
| FwdA |
COG1229 |
Formylmethanofuran dehydrogenase subunit A [Energy production and conversion]; |
17-75 |
4.19e-09 |
|
Formylmethanofuran dehydrogenase subunit A [Energy production and conversion];
Pssm-ID: 440842 Cd Length: 554 Bit Score: 59.05 E-value: 4.19e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 25742568 17 LLIKGGRI------VNDDQsfyADIYMEDGlikQIGDNLIVPGGVKTIEANGKMVMPGGIDVHTH 75
Cdd:COG1229 3 LIIKNGRVydpangIDGEV---MDIAIKDG---KIVEEPSDPKDAKVIDASGKVVMAGGVDIHTH 61
|
|
| NagA |
cd00854 |
N-acetylglucosamine-6-phosphate deacetylase, NagA, catalyzes the hydrolysis of the N-acetyl ... |
17-75 |
5.00e-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: 55.28 E-value: 5.00e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 25742568 17 LLIKGGRIVNDDQSFYADIYMEDGLIKQIGDNLIVPGGVKTIEANGKMVMPGGIDVHTH 75
Cdd:cd00854 1 LIIKNARILTPGGLEDGAVLVEDGKIVAIGPEDELEEADEIIDLKGQYLVPGFIDIHIH 59
|
|
| PRK09061 |
PRK09061 |
D-glutamate deacylase; Validated |
16-467 |
5.70e-08 |
|
D-glutamate deacylase; Validated
Pssm-ID: 236369 [Multi-domain] Cd Length: 509 Bit Score: 55.47 E-value: 5.70e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25742568 16 RLLIKGGRIVNDDQSFYA--DIYMEDGLIKQIGDNLIvpGGVKTIEANGKMVMPGGIDVHTHFQMP-------YKGMTTV 86
Cdd:PRK09061 20 DLVIRNGRVVDPETGLDAvrDVGIKGGKIAAVGTAAI--EGDRTIDATGLVVAPGFIDLHAHGQSVaayrmqaFDGVTTA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25742568 87 DDFFQGT--------KAALAG-----GTTM------IIDHVVPEPESSLtEAYEKW---REWADgksccDYALHVDITHW 144
Cdd:PRK09061 98 LELEAGVlpvarwyaEQAGEGrplnyGASVgwtparIAVLTGPQAEGTI-ADFGKAlgdPRWQE-----RAATPAELAEI 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25742568 145 NDSVKQEVQNLSKEKGVNsfmvyMAYkdLYQVSNTELYEIFTCLGELGAIAQVHAEngdiiaqeqarmlEMGITGPEGHV 224
Cdd:PRK09061 172 LELLEQGLDEGALGIGIG-----AGY--APGTGHKEYLELARLAARAGVPTYTHVR-------------YLSNVDPRSSV 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25742568 225 lsrpeeleaEAVFRAITVASQTNCPLYVTKVMSKS------AADLISQARKKGNVVFGE--P-ITASLGID--------- 286
Cdd:PRK09061 232 ---------DAYQELIAAAAETGAHMHICHVNSTSlrdidrCLALVEKAQAQGLDVTTEayPyGAGSTVVGaaffdpgwl 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25742568 287 ---GTHYWSKNW----------AKAAAFVTSPPLSP---------DPTTPDYINSLLASGDLQLSGSAHCTFSTAQKAIG 344
Cdd:PRK09061 303 ermGLGYGSLQWvetgerlltrEELAKLRANDPGGLvlihfldedNPRDRALLDRSVLFPGAAIASDAMPWTWSDGTVYE 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25742568 345 KDNFTAIPEG-----TNG---------VEERMSVIWDKAVAtgKMdenqfvavtSTNAAKIFNLY----PRKGRIAVGSD 406
Cdd:PRK09061 383 GDAWPLPEDAvshprSAGtfarflreyVRERKALSLLEAIR--KC---------TLMPAQILEDSvpamRRKGRLQAGAD 451
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 25742568 407 SDLVIWDPDAVKIVS---AKNHQSvaeynifEGMELrgaplvVICQGKIMLEDGNLHVTQGAGR 467
Cdd:PRK09061 452 ADIVVFDPETITDRAtfeDPNRPS-------EGVRH------VLVNGVPVVSNGELVRDARPGR 502
|
|
| PRK07228 |
PRK07228 |
5'-deoxyadenosine deaminase; |
16-220 |
6.32e-08 |
|
5'-deoxyadenosine deaminase;
Pssm-ID: 180895 [Multi-domain] Cd Length: 445 Bit Score: 55.01 E-value: 6.32e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25742568 16 RLLIKGGRIVNDDQS---FYADIYMEDGLIKQIGDNLIVPGGVKTIEANGKMVMPGGIDVHTHF-QMPYKGMTtvDDF-- 89
Cdd:PRK07228 2 TILIKNAGIVTMNAKreiVDGDVLIEDDRIAAVGDRLDLEDYDDHIDATGKVVIPGLIQGHIHLcQTLFRGIA--DDLel 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25742568 90 ----------FQGTKAA--------------LAGGTTMIIDHV-VPEPESSLTEAYEKWREWADGKSCCDYALHVDIT-- 142
Cdd:PRK07228 80 ldwlkdriwpLEAAHDAesmyysallgigelIESGTTTIVDMEsVHHTDSAFEAAGESGIRAVLGKVMMDYGDDVPEGlq 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25742568 143 -HWNDSVKQEVQNLSKEKGVNSFMVYMAYKDLYQVSNTElyeifTCLGELGAIAQ-------VHA-EN-GDIIAQEQARM 212
Cdd:PRK07228 160 eDTEASLAESVRLLEKWHGADNGRIRYAFTPRFAVSCTE-----ELLRGVRDLADeygvrihTHAsENrGEIETVEEETG 234
|
250
....*....|....*
gi 25742568 213 L-------EMGITGP 220
Cdd:PRK07228 235 MrnihyldEVGLTGE 249
|
|
| PRK07627 |
PRK07627 |
dihydroorotase; Provisional |
16-456 |
9.14e-08 |
|
dihydroorotase; Provisional
Pssm-ID: 181059 [Multi-domain] Cd Length: 425 Bit Score: 54.68 E-value: 9.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25742568 16 RLLIKGGRIVN-----DDQsfyADIYMEDGLIKQIGDnliVPGGV---KTIEANGKMVMPGGIDVHTHFQMP-YKGMTTV 86
Cdd:PRK07627 2 KIHIKGGRLIDpaagtDRQ---ADLYVAAGKIAAIGQ---APAGFnadKTIDASGLIVCPGLVDLSARLREPgYEYKATL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25742568 87 DDFFQgtkAALAGGTTMII-----DHVVPEPEssLTEAyekwrewadgksccdyalhvdithwndsVKQEVQNLSKEK-- 159
Cdd:PRK07627 76 ESEMA---AAVAGGVTSLVcppdtDPVLDEPG--LVEM----------------------------LKFRARNLNQAHvy 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25742568 160 GVNSFMVYMAYKDLyqvsnTELYEiftcLGELGAIAQVHAENGDIIAQEQARMLEMGIT-------------------GP 220
Cdd:PRK07627 123 PLGALTVGLKGEVL-----TEMVE----LTEAGCVGFSQANVPVVDTQVLLRALQYASTfgftvwlrpldaflgrggvAA 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25742568 221 EGHVLSR------PEELEAEAVFRAITVASQTNCPLYVTKVMSKSAADLISQARKKgnvvfGEPITASLGIDGTH----- 289
Cdd:PRK07627 194 SGAVASRlglsgvPVAAETIALHTIFELMRVTGARVHLARLSSAAGVALVRAAKAE-----GLPVTCDVGVNHVHlidvd 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25742568 290 --YWSKNwakaaaFVTSPPLSpDPTTPDYINSLLASGDLQLSGSAHCTFSTAQKAIgkdNFTAIPEGTNGVEERMSVIWD 367
Cdd:PRK07627 269 igYFDSQ------FRLDPPLR-SQRDREAIRAALADGTIDAICSDHTPVDDDEKLL---PFAEATPGATGLELLLPLTLK 338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25742568 368 KAVATgKMDENQFVAVTSTNAAKIFNLypRKGRIAVGSDSDLVIWDPDAVKIVSAKNHQSVAEYNIFEGMELRGAPLVVI 447
Cdd:PRK07627 339 WADEA-KVPLARALARITSAPARVLGL--PAGRLAEGAPADLCVFDPDAHWRVEPRALKSQGKNTPFLGYELPGRVRATL 415
|
....*....
gi 25742568 448 CQGKIMLED 456
Cdd:PRK07627 416 VAGQVAFER 424
|
|
| Met_dep_hydrolase_B |
cd01307 |
Metallo-dependent hydrolases, subgroup B is part of the superfamily of metallo-dependent ... |
34-430 |
1.26e-07 |
|
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: 53.87 E-value: 1.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25742568 34 DIYMEDGLIKQIGDNLIVPGGVKTIEANGKMVMPGGIDVHTHFqmpYKGMTTVDDffQGTKAALAGGTTMIIDhvvpepe 113
Cdd:cd01307 1 DVAIENGKIAAVGAALAAPAATQIVDAGGCYVSPGWIDLHVHV---YQGGTRYGD--RPDMIGVKSGVTTVVD------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25742568 114 sslteayekwrewADGKSCCDYalhvdithwnDSVKQEVQNLSKEKgvnsfmVYmAYKDLY---QVSNTELYEIFTClgE 190
Cdd:cd01307 69 -------------AGSAGADNI----------DGFRYTVIERSATR------VY-AFLNISrvgLVAQDELPDPDNI--D 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25742568 191 LGAIAQVHAENGDIIAQEQARMlEMGITGPEGhvlSRPEELEAEAvfraitvASQTNCPLYvtkVMSKSAADLISQA--- 267
Cdd:cd01307 117 EDAVVAAAREYPDVIVGLKARA-SKSVVGEWG---IKPLELAKKI-------AKEADLPLM---VHIGSPPPILDEVvpl 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25742568 268 RKKGNVVfgepitaslgidgTHYWSknwAKAAAFVTspplsPDPTTPDYINSLLASG---DLQlSGSAHCTFSTAQKAIG 344
Cdd:cd01307 183 LRRGDVL-------------THCFN---GKPNGIVD-----EEGEVLPLVRRARERGvifDVG-HGTASFSFRVARAAIA 240
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25742568 345 KD-NFTAI------PEGTNGVEERMSVIWDKAVATGkMDENQFVAVTSTNAAKIFNLyPRKGRIAVGSDSDLVIWD--PD 415
Cdd:cd01307 241 AGlLPDTIssdihgRNRTNGPVYALATTLSKLLALG-MPLEEVIEAVTANPARMLGL-AEIGTLAVGYDADLTVFDlkDG 318
|
410
....*....|....*
gi 25742568 416 AVKIVSAKNHQSVAE 430
Cdd:cd01307 319 RVELVDSEGDTLIAE 333
|
|
| NagA |
COG1820 |
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism]; |
18-75 |
1.36e-07 |
|
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism];
Pssm-ID: 441425 [Multi-domain] Cd Length: 373 Bit Score: 53.95 E-value: 1.36e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 25742568 18 LIKGGRIVNDDQSFY-ADIYMEDGLIKQIGDNliVPGGVKTIEANGKMVMPGGIDVHTH 75
Cdd:COG1820 1 AITNARIFTGDGVLEdGALLIEDGRIAAIGPG--AEPDAEVIDLGGGYLAPGFIDLHVH 57
|
|
| AdeC |
COG1001 |
Adenine deaminase [Nucleotide transport and metabolism]; |
17-106 |
3.18e-07 |
|
Adenine deaminase [Nucleotide transport and metabolism];
Pssm-ID: 440625 [Multi-domain] Cd Length: 559 Bit Score: 53.18 E-value: 3.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25742568 17 LLIKGGRIVN--DDQSFYADIYMEDGLIKQIGDnlIVPGGVKTIEANGKMVMPGGIDVHTHFQmpyKGMTTVDDFfqgTK 94
Cdd:COG1001 7 LVIKNGRLVNvfTGEILEGDIAIAGGRIAGVGD--YIGEATEVIDAAGRYLVPGFIDGHVHIE---SSMVTPAEF---AR 78
|
90
....*....|...
gi 25742568 95 AALAGGTT-MIID 106
Cdd:COG1001 79 AVLPHGTTtVIAD 91
|
|
| metallo-dependent_hydrolases |
cd01292 |
Superfamily of metallo-dependent hydrolases (also called amidohydrolase superfamily) is a ... |
70-276 |
3.58e-07 |
|
Superfamily of metallo-dependent hydrolases (also called amidohydrolase superfamily) is a large group of proteins that show conservation in their 3-dimensional fold (TIM barrel) and in details of their active site. The vast majority of the members have a conserved metal binding site, involving four histidines and one aspartic acid residue. In the common reaction mechanism, the metal ion (or ions) deprotonate a water molecule for a nucleophilic attack on the substrate. The family includes urease alpha, adenosine deaminase, phosphotriesterase dihydroorotases, allantoinases, hydantoinases, AMP-, adenine and cytosine deaminases, imidazolonepropionase, aryldialkylphosphatase, chlorohydrolases, formylmethanofuran dehydrogenases and others.
Pssm-ID: 238617 [Multi-domain] Cd Length: 275 Bit Score: 51.95 E-value: 3.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25742568 70 IDVHTHFQMP----------------YKGMTTVDDFFQGTKAALAGGTTMIIDHVVPEPESSLTEAYEKWREWADGKSCC 133
Cdd:cd01292 2 IDTHVHLDGSalrgtrlnlelkeaeeLSPEDLYEDTLRALEALLAGGVTTVVDMGSTPPPTTTKAAIEAVAEAARASAGI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25742568 134 DYALHVDITH--------WNDSVKQEVQnLSKEKGVNSFMVYMAYKDlYQVSNTELYEIFTCLGELGAIAQVHAENGDII 205
Cdd:cd01292 82 RVVLGLGIPGvpaavdedAEALLLELLR-RGLELGAVGLKLAGPYTA-TGLSDESLRRVLEEARKLGLPVVIHAGELPDP 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 25742568 206 AQEQARMLEMGITGPE---GHVLSRPEELEAEAVFRAITVASqTNCPLYVTKVMSKSAADLISQARKKGNVVFG 276
Cdd:cd01292 160 TRALEDLVALLRLGGRvviGHVSHLDPELLELLKEAGVSLEV-CPLSNYLLGRDGEGAEALRRLLELGIRVTLG 232
|
|
| PRK08204 |
PRK08204 |
hypothetical protein; Provisional |
15-113 |
4.34e-07 |
|
hypothetical protein; Provisional
Pssm-ID: 181288 [Multi-domain] Cd Length: 449 Bit Score: 52.70 E-value: 4.34e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25742568 15 DRLLIKGGRIVNDDQSF----YADIYMEDGLIKQIGDNlIVPGGVKTIEANGKMVMPGGIDVHTH--------------- 75
Cdd:PRK08204 2 KRTLIRGGTVLTMDPAIgdlpRGDILIEGDRIAAVAPS-IEAPDAEVVDARGMIVMPGLVDTHRHtwqsvlrgigadwtl 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 25742568 76 ---FQMPYKGMTTV---DDFFQGTKA----ALAGGTTMIID--HVVPEPE 113
Cdd:PRK08204 81 qtyFREIHGNLGPMfrpEDVYIANLLgaleALDAGVTTLLDwsHINNSPE 130
|
|
| Amidohydro_3 |
pfam07969 |
Amidohydrolase family; |
381-436 |
1.01e-06 |
|
Amidohydrolase family;
Pssm-ID: 400360 [Multi-domain] Cd Length: 464 Bit Score: 51.38 E-value: 1.01e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 25742568 381 VAVTSTNAAKIFNLYPRKGRIAVGSDSDLVIWDPDAVKIVSAKNHQSVAEYNIFEG 436
Cdd:pfam07969 405 LALYTSGPAKALGLEDRKGTLGVGKDADLVVLDDDPLTVDPPAIADIRVRLTVVDG 460
|
|
| FMDH_A |
cd01304 |
Formylmethanofuran dehydrogenase (FMDH) subunit A; Methanogenic bacteria and archea derive ... |
19-75 |
2.02e-06 |
|
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: 50.49 E-value: 2.02e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 25742568 19 IKGGRIVNDDQSFYA---DIYMEDGlikQIGDNLIVPGGVKTIEANGKMVMPGGIDVHTH 75
Cdd:cd01304 1 IKNGTVYDPLNGINGekmDIFIRDG---KIVESSSGAKPAKVIDASGKVVMAGGVDMHSH 57
|
|
| PRK07369 |
PRK07369 |
dihydroorotase; Provisional |
33-441 |
2.08e-06 |
|
dihydroorotase; Provisional
Pssm-ID: 236002 [Multi-domain] Cd Length: 418 Bit Score: 50.37 E-value: 2.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25742568 33 ADIYMEDGLIKQIGDNLI-VPGGVKTIEANGKMVMPGGIDVHTHFQMPykGMTTVDDFFQGTKAALAGGTTMI------- 104
Cdd:PRK07369 22 ADVLIEDGKIQAIEPHIDpIPPDTQIIDASGLILGPGLVDLYSHSGEP--GFEERETLASLAAAAAAGGFTRVailpdtf 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25742568 105 --IDHvvPEPESSL-----TEAYEKWREWADgksccdyalhvdITHwNDSVKQ--EVQNLSkEKGVNSFMVYMAYKDLYQ 175
Cdd:PRK07369 100 ppLDN--PATLARLqqqaqQIPPVQLHFWGA------------LTL-GGQGKQltELAELA-AAGVVGFTDGQPLENLAL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25742568 176 VSNTELYeiftcLGELGAIAQVHAEN----GDIIAQEQARMLEMGITGpeghvlsRPEELEAEAVFRAITVASQTNCPLY 251
Cdd:PRK07369 164 LRRLLEY-----LKPLGKPVALWPCDrslaGNGVMREGLLALRLGLPG-------DPASAETTALAALLELVAAIGTPVH 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25742568 252 VTKVMSKSAADLISQARKKGnvvfgEPITASlgidgTHYWSKNWAKAAAFVTSPPLSPDPT--TPDYINSLLA---SGDL 326
Cdd:PRK07369 232 LMRISTARSVELIAQAKARG-----LPITAS-----TTWMHLLLDTEALASYDPNLRLDPPlgNPSDRQALIEgvrTGVI 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25742568 327 QLSGSAHCTFSTAQKAIGkdnFTAIPEGTNGVEERMSVIWDKAVATGKMDENQFVAVTSTNAAKIFNLYPRkgRIAVGSD 406
Cdd:PRK07369 302 DAIAIDHAPYTYEEKTVA---FAEAPPGAIGLELALPLLWQNLVETGELSALQLWQALSTNPARCLGQEPP--SLAPGQP 376
|
410 420 430
....*....|....*....|....*....|....*
gi 25742568 407 SDLVIWDPDAVKIVSAKNHQSVAEYNIFEGMELRG 441
Cdd:PRK07369 377 AELILFDPQKTWTVSAQTLHSLSRNTPWLGQTLKG 411
|
|
| Bact_CD |
cd01293 |
Bacterial cytosine deaminase and related metal-dependent hydrolases. Cytosine deaminases (CDs) ... |
12-128 |
2.61e-06 |
|
Bacterial cytosine deaminase and related metal-dependent hydrolases. Cytosine deaminases (CDs) catalyze the deamination of cytosine, producing uracil and ammonia. They play an important role in pyrimidine salvage. CDs are present in prokaryotes and fungi, but not mammalian cells. The bacterial enzymes, but not the fungal enzymes, are related to the adenosine deaminases (ADA). The bacterial enzymes are iron dependent and hexameric.
Pssm-ID: 238618 [Multi-domain] Cd Length: 398 Bit Score: 49.94 E-value: 2.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25742568 12 ITSDRLLIKGGRIVnddqsfyaDIYMEDGLIKQIGDNLIVPGGVKTIEANGKMVMPGGIDVHTH------FQMP------ 79
Cdd:cd01293 2 LRNARLADGGTALV--------DIAIEDGRIAAIGPALAVPPDAEEVDAKGRLVLPAFVDPHIHldktftGGRWpnnsgg 73
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25742568 80 -----------YKGMTTVDDFFQ----GTKAALAGGTTMIIDHVVPEPESSLT------EAYEKWREWAD 128
Cdd:cd01293 74 tlleaiiaweeRKLLLTAEDVKEraerALELAIAHGTTAIRTHVDVDPAAGLKaleallELREEWADLID 143
|
|
| Urease_alpha |
cd00375 |
Urease alpha-subunit; Urease is a nickel-dependent metalloenzyme that catalyzes the hydrolysis ... |
33-105 |
4.00e-06 |
|
Urease alpha-subunit; Urease is a nickel-dependent metalloenzyme that catalyzes the hydrolysis of urea to form ammonia and carbon dioxide. Nickel-dependent ureases are found in bacteria, fungi and plants. Their primary role is to allow the use of external and internally generated urea as a nitrogen source. The enzyme consists of 3 subunits, alpha, beta and gamma, which can be fused and present on a single protein chain and which in turn forms multimers, mainly trimers. The large alpha subunit is the catalytic domain containing an active site with a bi-nickel center complexed by a carbamylated lysine. The beta and gamma subunits play a role in subunit association to form the higher order trimers.
Pssm-ID: 238221 [Multi-domain] Cd Length: 567 Bit Score: 49.63 E-value: 4.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25742568 33 ADIYMEDGLIKQIG------------DNLIVPGGVKTIEANGKMVMPGGIDVHTHFQMPykgmttvddffQGTKAALAGG 100
Cdd:cd00375 83 ADIGIKDGRIVAIGkagnpdimdgvtPNMIVGPSTEVIAGEGKIVTAGGIDTHVHFICP-----------QQIEEALASG 151
|
....*
gi 25742568 101 TTMII 105
Cdd:cd00375 152 ITTMI 156
|
|
| YtcJ |
COG1574 |
Predicted amidohydrolase YtcJ [General function prediction only]; |
17-76 |
4.01e-06 |
|
Predicted amidohydrolase YtcJ [General function prediction only];
Pssm-ID: 441182 [Multi-domain] Cd Length: 535 Bit Score: 49.41 E-value: 4.01e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 25742568 17 LLIKGGRI--VNDDQSFYADIYMEDGLIKQIGDN----LIVPGGVKTIEANGKMVMPGGIDVHTHF 76
Cdd:COG1574 10 LLLTNGRIytMDPAQPVAEAVAVRDGRIVAVGSDaevrALAGPATEVIDLGGKTVLPGFIDAHVHL 75
|
|
| NagA |
COG1820 |
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism]; |
381-415 |
4.86e-06 |
|
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism];
Pssm-ID: 441425 [Multi-domain] Cd Length: 373 Bit Score: 48.94 E-value: 4.86e-06
10 20 30
....*....|....*....|....*....|....*
gi 25742568 381 VAVTSTNAAKIFNLYPRKGRIAVGSDSDLVIWDPD 415
Cdd:COG1820 328 VRMASLNPARALGLDDRKGSIAPGKDADLVVLDDD 362
|
|
| PRK06380 |
PRK06380 |
metal-dependent hydrolase; Provisional |
17-93 |
5.53e-06 |
|
metal-dependent hydrolase; Provisional
Pssm-ID: 180548 [Multi-domain] Cd Length: 418 Bit Score: 49.11 E-value: 5.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25742568 17 LLIKGGRIVNDDQS---FYADIYMEDGLIKQIGDnlIVPGGVKTIEANGKMVMPGGIDVHTHFQMP-YKGM---TTVDDF 89
Cdd:PRK06380 3 ILIKNAWIVTQNEKreiLQGNVYIEGNKIVYVGD--VNEEADYIIDATGKVVMPGLINTHAHVGMTaSKGLfddVDLEEF 80
|
....
gi 25742568 90 FQGT 93
Cdd:PRK06380 81 LMKT 84
|
|
| PRK07203 |
PRK07203 |
putative aminohydrolase SsnA; |
17-76 |
5.54e-06 |
|
putative aminohydrolase SsnA;
Pssm-ID: 235963 [Multi-domain] Cd Length: 442 Bit Score: 49.16 E-value: 5.54e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 25742568 17 LLIKGGRIV-NDDQSFY---ADIYMEDGLIKQIGDNlivpGGVKT-------IEANGKMVMPGGIDVHTHF 76
Cdd:PRK07203 2 LLIGNGTAItRDPAKPViedGAIAIEGNVIVEIGTT----DELKAkypdaefIDAKGKLIMPGLINSHNHI 68
|
|
| PRK15446 |
PRK15446 |
phosphonate metabolism protein PhnM; Provisional |
16-74 |
6.42e-06 |
|
phosphonate metabolism protein PhnM; Provisional
Pssm-ID: 237967 [Multi-domain] Cd Length: 383 Bit Score: 48.64 E-value: 6.42e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 25742568 16 RLLIKGGRIVNDDQSFYADIYMEDGLIKQIGDNLIVPGGvkTIEANGKMVMPGGIDVHT 74
Cdd:PRK15446 3 EMILSNARLVLPDEVVDGSLLIEDGRIAAIDPGASALPG--AIDAEGDYLLPGLVDLHT 59
|
|
| ureC |
PRK13308 |
urease subunit alpha; Reviewed |
33-104 |
1.03e-05 |
|
urease subunit alpha; Reviewed
Pssm-ID: 183965 [Multi-domain] Cd Length: 569 Bit Score: 48.16 E-value: 1.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25742568 33 ADIYMEDGLIKQIG------------DNLIVPGGVKTIEANGKMVMPGGIDVHTHFQMPykgmttvddffQGTKAALAGG 100
Cdd:PRK13308 87 GDIGIRDGRIVGIGkagnpdimdgvdPRLVVGPGTDVRPAEGLIATPGAIDVHVHFDSA-----------QLVDHALASG 155
|
....*
gi 25742568 101 -TTMI 104
Cdd:PRK13308 156 iTTML 160
|
|
| PRK08393 |
PRK08393 |
N-ethylammeline chlorohydrolase; Provisional |
17-78 |
4.25e-05 |
|
N-ethylammeline chlorohydrolase; Provisional
Pssm-ID: 181411 [Multi-domain] Cd Length: 424 Bit Score: 45.95 E-value: 4.25e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 25742568 17 LLIKGGRIVNDD--QSFYADIYMEDGLIKQIGDNLIVPGGvKTIEANGKMVMPGGIDVHTHFQM 78
Cdd:PRK08393 3 ILIKNGYVIYGEnlKVIRADVLIEGNKIVEVKRNINKPAD-TVIDASGSVVSPGFINAHTHSPM 65
|
|
| Met_dep_hydrolase_C |
cd01309 |
Metallo-dependent hydrolases, subgroup C is part of the superfamily of metallo-dependent ... |
39-75 |
8.02e-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: 44.99 E-value: 8.02e-05
10 20 30
....*....|....*....|....*....|....*..
gi 25742568 39 DGLIKQIGDNLIVPGGVKTIEANGKMVMPGGIDVHTH 75
Cdd:cd01309 1 DGKIVAVGAEITTPADAEVIDAKGKHVTPGLIDAHSH 37
|
|
| ureC |
PRK13206 |
urease subunit alpha; Reviewed |
33-105 |
1.09e-04 |
|
urease subunit alpha; Reviewed
Pssm-ID: 237304 [Multi-domain] Cd Length: 573 Bit Score: 45.09 E-value: 1.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25742568 33 ADIYMEDGLIKQIG------------DNLIVPGGVKTIEANGKMVMPGGIDVHTHFQMPykgmttvddffQGTKAALAGG 100
Cdd:PRK13206 89 ADVGIRDGRIVAIGkagnpdimdgvhPDLVIGPSTEIIAGNGRILTAGAIDCHVHFICP-----------QIVDEALAAG 157
|
....*
gi 25742568 101 TTMII 105
Cdd:PRK13206 158 ITTLI 162
|
|
| ureB |
PRK13985 |
urease subunit alpha; |
5-101 |
1.52e-04 |
|
urease subunit alpha;
Pssm-ID: 184438 [Multi-domain] Cd Length: 568 Bit Score: 44.50 E-value: 1.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25742568 5 GKKNIPRITSDRLLIKGGRIVNDDQSFYADIYMEDGLIKQIG------------DNLIVPGGVKTIEANGKMVMPGGIDV 72
Cdd:PRK13985 55 SQSNNPSKEELDLIITNALIIDYTGIYKADIGIKDGKIAGIGkggnkdmqdgvkNNLSVGPATEALAGEGLIVTAGGIDT 134
|
90 100
....*....|....*....|....*....
gi 25742568 73 HTHFQMPYKGMTTvddFFQGTKAALAGGT 101
Cdd:PRK13985 135 HIHFISPQQIPTA---FASGVTTMIGGGT 160
|
|
| ureC |
PRK13207 |
urease subunit alpha; Reviewed |
33-104 |
1.62e-04 |
|
urease subunit alpha; Reviewed
Pssm-ID: 237305 [Multi-domain] Cd Length: 568 Bit Score: 44.40 E-value: 1.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25742568 33 ADIYMEDGLIKQIG--------DNLIVPGGVKT--IEANGKMVMPGGIDVHTHFQMPykgmttvddffQGTKAALAGG-T 101
Cdd:PRK13207 85 ADIGIKDGRIVAIGkagnpdiqDGVDIIIGPGTevIAGEGLIVTAGGIDTHIHFICP-----------QQIEEALASGvT 153
|
...
gi 25742568 102 TMI 104
Cdd:PRK13207 154 TMI 156
|
|
| Imidazolone-5PH |
cd01296 |
Imidazolonepropionase/imidazolone-5-propionate hydrolase (Imidazolone-5PH) catalyzes the third ... |
35-76 |
1.77e-04 |
|
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: 44.17 E-value: 1.77e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 25742568 35 IYMEDGLIKQIGD----NLIVPGGVKTIEANGKMVMPGGIDVHTHF 76
Cdd:cd01296 1 IAIRDGRIAAVGPaaslPAPGPAAAEEIDAGGRAVTPGLVDCHTHL 46
|
|
| PRK05985 |
PRK05985 |
cytosine deaminase; Provisional |
33-128 |
5.36e-04 |
|
cytosine deaminase; Provisional
Pssm-ID: 180337 [Multi-domain] Cd Length: 391 Bit Score: 42.61 E-value: 5.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25742568 33 ADIYMEDGLIKQIGDNLIVPGGVKTIEANGKMVMPGGIDVHTHFQMPYKGM--------TTVDDFFQGTK---------- 94
Cdd:PRK05985 17 VDILIRDGRIAAIGPALAAPPGAEVEDGGGALALPGLVDGHIHLDKTFWGDpwypnepgPSLRERIANERrrraasghpa 96
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 25742568 95 ---------AALAGGTTMIIDHVVPEPESSLT------EAYEKWREWAD 128
Cdd:PRK05985 97 aeralalarAAAAAGTTAMRSHVDVDPDAGLRhleavlAARETLRGLID 145
|
|
| PRK09059 |
PRK09059 |
dihydroorotase; Validated |
17-105 |
7.23e-04 |
|
dihydroorotase; Validated
Pssm-ID: 181631 [Multi-domain] Cd Length: 429 Bit Score: 42.33 E-value: 7.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25742568 17 LLIKGGRIVNDDQSF--YADIYMEDGLIKQIGD---NLIVPGGVKTIEANGKMVMPGGIDVHTHFQMPykGMTTVDDFFQ 91
Cdd:PRK09059 5 ILLANARIIDPSRGLdeIGTVLIEDGVIVAAGKgagNQGAPEGAEIVDCAGKAVAPGLVDARVFVGEP--GAEHRETIAS 82
|
90
....*....|....
gi 25742568 92 GTKAALAGGTTMII 105
Cdd:PRK09059 83 ASRAAAAGGVTSII 96
|
|
| PRK07583 |
PRK07583 |
cytosine deaminase; |
33-75 |
1.67e-03 |
|
cytosine deaminase;
Pssm-ID: 236062 Cd Length: 438 Bit Score: 41.12 E-value: 1.67e-03
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 25742568 33 ADIYMEDGLIKQIGDNLIVPGGVKTIEANGKMVMPGGIDVHTH 75
Cdd:PRK07583 41 VDIEIADGKIAAILPAGGAPDELPAVDLKGRMVWPCFVDMHTH 83
|
|
| Isoaspartyl-dipeptidase |
cd01308 |
Isoaspartyl dipeptidase hydrolyzes the beta-L-isoaspartyl linkages in dipeptides, as part of ... |
383-462 |
1.95e-03 |
|
Isoaspartyl dipeptidase hydrolyzes the beta-L-isoaspartyl linkages in dipeptides, as part of the degradative pathway to eliminate proteins with beta-L-isoaspartyl peptide bonds, bonds whereby the beta-group of an aspartate forms the peptide link with the amino group of the following amino acid. Formation of this bond is a spontaneous nonenzymatic reaction in nature and can profoundly effect the function of the protein. Isoaspartyl dipeptidase is an octameric enzyme that contains a binuclear zinc center in the active site of each subunit and shows a strong preference of hydrolyzing Asp-Leu dipeptides.
Pssm-ID: 238633 [Multi-domain] Cd Length: 387 Bit Score: 40.84 E-value: 1.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25742568 383 VTSTNAAKIFNLYPrKGRIAVGSDSDLVIWDPDavkivsaknhqsvaeYNIFEgmelrgaplvVICQGKIMLEDGNLHVT 462
Cdd:cd01308 330 VITSNVARILKLRK-KGEIQPGFDADLVILDKD---------------LDINS----------VIAKGQIMVRNGKLLVK 383
|
|
| PRK06038 |
PRK06038 |
N-ethylammeline chlorohydrolase; Provisional |
17-89 |
2.38e-03 |
|
N-ethylammeline chlorohydrolase; Provisional
Pssm-ID: 180363 [Multi-domain] Cd Length: 430 Bit Score: 40.50 E-value: 2.38e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 25742568 17 LLIKGGRIVNDDQSFY--ADIYMEDGLIKQIGDNliVPGGVKT-IEANGKMVMPGGIDVHTHFQMP-YKGMTtvDDF 89
Cdd:PRK06038 4 IIIKNAYVLTMDAGDLkkGSVVIEDGTITEVSES--TPGDADTvIDAKGSVVMPGLVNTHTHAAMTlFRGYA--DDL 76
|
|
| PRK08203 |
PRK08203 |
hydroxydechloroatrazine ethylaminohydrolase; Reviewed |
16-76 |
3.41e-03 |
|
hydroxydechloroatrazine ethylaminohydrolase; Reviewed
Pssm-ID: 236184 [Multi-domain] Cd Length: 451 Bit Score: 40.22 E-value: 3.41e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 25742568 16 RLLIKGGRIV---NDDQSFYAD--IYMEDGLIKQIGDNLIVPG-GVKTIEANGKMVMPGGIDVHTHF 76
Cdd:PRK08203 2 TLWIKNPLAIvtmDAARREIADggLVVEGGRIVEVGPGGALPQpADEVFDARGHVVTPGLVNTHHHF 68
|
|
| YtcJ_like |
cd01300 |
YtcJ_like metal dependent amidohydrolases. YtcJ is a Bacillus subtilis ORF of unknown function. ... |
34-76 |
3.41e-03 |
|
YtcJ_like metal dependent amidohydrolases. YtcJ is a Bacillus subtilis ORF of unknown function. The Arabidopsis homolog LAF3 has been identified as a factor required for phytochrome A signalling.
Pssm-ID: 238625 [Multi-domain] Cd Length: 479 Bit Score: 39.98 E-value: 3.41e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 25742568 34 DIYMEDGLIKQIGDN----LIVPGGVKTIEANGKMVMPGGIDVHTHF 76
Cdd:cd01300 1 AVAVRDGRIVAVGSDaeakALKGPATEVIDLKGKTVLPGFIDSHSHL 47
|
|
| Imidazolone-5PH |
cd01296 |
Imidazolonepropionase/imidazolone-5-propionate hydrolase (Imidazolone-5PH) catalyzes the third ... |
369-413 |
7.92e-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: 38.78 E-value: 7.92e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 25742568 369 AVATGKMDENQFVAVTSTNAAKIFNLYPRKGRIAVGSDSDLVIWD 413
Cdd:cd01296 304 ACRLMRMTPEEALTAATINAAAALGLGETVGSLEVGKQADLVILD 348
|
|
| |
