|
Name |
Accession |
Description |
Interval |
E-value |
| D-hydantoinase |
TIGR02033 |
D-hydantoinase; This model represents the D-hydantoinase (dihydropyrimidinase) which primarily ... |
15-469 |
0e+00 |
|
D-hydantoinase; This model represents the D-hydantoinase (dihydropyrimidinase) which primarily converts 5,6-dihydrouracil to 3-ureidopropanoate but also acts on dihydrothymine and hydantoin. The enzyme is a metalloenzyme.
Pssm-ID: 273937 [Multi-domain] Cd Length: 454 Bit Score: 764.24 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564393312 15 LLIKGGRIVNDDQSFYADIYMEDGLIKQIGDNLIVPGGVKTIEANGKMVMPGGIDVHTHFQMPYKGMTTVDDFFQGTKAA 94
Cdd:TIGR02033 1 LLIKGGTVVNADDVFQADVLIEGGKIVAVGDNLIPPDAVEVIDATGKYVLPGGIDVHTHLEMPFGGTTTADDFFTGTKAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564393312 95 LAGGTTMIIDHVVPEPESSLTEAYEKWREWADGKSCCDYALHVDITHWNDSVKQEVQNLSKEKGVNSFMVYMAYKDLYQV 174
Cdd:TIGR02033 81 AAGGTTTIIDFVVPEKGSSLTEALETWHEKAEGKSVIDYGFHMDITHWNDSVLEEHIPEVKEEGINSFKVFMAYKNLLMV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564393312 175 SNTELYEIFTCLGELGAIAQVHAENGDIIAQEQARMLEMGITGPEGHVLSRPEELEAEAVFRAITVASQTNCPLYVTKVM 254
Cdd:TIGR02033 161 DDEELFEILKRLKELGALLQVHAENGDIIAELQARMLAQGITGPEYHALSRPPELEAEAVARAITLAALADAPLYVVHVS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564393312 255 SKSAADLISQARKKGNVVFGEPITASLGIDGTHYWsKNWAKAAAFVTSPPLSpDPTTPDYINSLLASGDLQLSGSAHCTF 334
Cdd:TIGR02033 241 TKDAADEIAQARKKGQPVFGETCPQYLVLDDTHYD-KPGFEGAKYVCSPPLR-EPEDQDALWSALSSGALQTVGSDHCTF 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564393312 335 STAQK-AIGKDNFTAIPEGTNGVEERMSVIWDKAVATGKMDENQFVAVTSTNAAKIFNLYPRKGRIAVGSDSDLVIWDPD 413
Cdd:TIGR02033 319 NFAQKkAIGKDDFTKIPNGGPGVEERMSLLFDEGVAKGRITLEKFVEVTSTNPAKIFNLYPRKGTIAVGSDADIVIWDPN 398
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 564393312 414 AVKIVSAKNHQSVAEYNIFEGMELRGAPLVVICQGKIMLEDGNLHVTQGAGRFIPC 469
Cdd:TIGR02033 399 RTTVISAETHHSNADYNPFEGFKVRGAPVSVLSRGRVVVEDGQLVGTAGAGRFVKR 454
|
|
| D-HYD |
cd01314 |
D-hydantoinases (D-HYD) also called dihydropyrimidases (DHPase) and related proteins; DHPases ... |
15-464 |
0e+00 |
|
D-hydantoinases (D-HYD) also called dihydropyrimidases (DHPase) and related proteins; DHPases are a family of enzymes that catalyze the reversible hydrolytic ring opening of the amide bond in five- or six-membered cyclic diamides, like dihydropyrimidine or hydantoin. The hydrolysis of dihydropyrimidines is the second step of reductive catabolism of pyrimidines in human. The hydrolysis of 5-substituted hydantoins in microorganisms leads to enantiomerically pure N-carbamyl amino acids, which are used for the production of antibiotics, peptide hormones, pyrethroids, and pesticides. HYDs are classified depending on their stereoselectivity. This family also includes collapsin response regulators (CRMPs), cytosolic proteins involved in neuronal differentiation and axonal guidance which have strong homology to DHPases, but lack most of the active site residues.
Pssm-ID: 238639 [Multi-domain] Cd Length: 447 Bit Score: 737.10 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564393312 15 LLIKGGRIVNDDQSFYADIYMEDGLIKQIGDNLIVPGGVKTIEANGKMVMPGGIDVHTHFQMPYKGMTTVDDFFQGTKAA 94
Cdd:cd01314 1 LIIKNGTIVTADGSFKADILIEDGKIVAIGPNLEAPGGVEVIDATGKYVLPGGIDPHTHLELPFMGTVTADDFESGTRAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564393312 95 LAGGTTMIIDHVVPEPESSLTEAYEKWREWADGKSCCDYALHVDITHWNDSVKQEVQNLSKeKGVNSFMVYMAYKDLYQV 174
Cdd:cd01314 81 AAGGTTTIIDFAIPNKGQSLLEAVEKWRGKADGKSVIDYGFHMIITDWTDSVIEELPELVK-KGISSFKVFMAYKGLLMV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564393312 175 SNTELYEIFTCLGELGAIAQVHAENGDIIAQEQARMLEMGITGPEGHVLSRPEELEAEAVFRAITVASQTNCPLYVTKVM 254
Cdd:cd01314 160 DDEELLDVLKRAKELGALVMVHAENGDVIAELQKKLLAQGKTGPEYHALSRPPEVEAEATARAIRLAELAGAPLYIVHVS 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564393312 255 SKSAADLISQARKKGNVVFGEPITASLGIDGTHYWsKNWAKAAAFVTSPPLSPDpTTPDYINSLLASGDLQLSGSAHCTF 334
Cdd:cd01314 240 SKEAADEIARARKKGLPVYGETCPQYLLLDDSDYW-KDWFEGAKYVCSPPLRPK-EDQEALWDGLSSGTLQTVGSDHCPF 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564393312 335 STAQKAIGKDNFTAIPEGTNGVEERMSVIWDKAVATGKMDENQFVAVTSTNAAKIFNLYPRKGRIAVGSDSDLVIWDPDA 414
Cdd:cd01314 318 NFAQKARGKDDFTKIPNGVPGVETRMPLLWSEGVAKGRITLEKFVELTSTNPAKIFGLYPRKGTIAVGSDADLVIWDPNA 397
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 564393312 415 VKIVSAKNHQSVAEYNIFEGMELRGAPLVVICQGKIMLEDGNLHVTQGAG 464
Cdd:cd01314 398 EKTISADTHHHNVDYNIFEGMKVKGWPVVTISRGKVVVEDGELVGEKGSG 447
|
|
| PRK08323 |
PRK08323 |
phenylhydantoinase; Validated |
14-473 |
0e+00 |
|
phenylhydantoinase; Validated
Pssm-ID: 236240 [Multi-domain] Cd Length: 459 Bit Score: 569.42 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564393312 14 RLLIKGGRIVNDDQSFYADIYMEDGLIKQIGDNlivpGGVKTIEANGKMVMPGGIDVHTHFQMPYKGMTTVDDFFQGTKA 93
Cdd:PRK08323 2 STLIKNGTVVTADDTYKADVLIEDGKIAAIGAN----LGDEVIDATGKYVMPGGIDPHTHMEMPFGGTVSSDDFETGTRA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564393312 94 ALAGGTTMIIDHVVPEPESSLTEAYEKWREWADGKSCCDYALHVDITHWNDSVKQEVQNLSKEkGVNSFMVYMAYKDLYQ 173
Cdd:PRK08323 78 AACGGTTTIIDFALQPKGQSLREALEAWHGKAAGKAVIDYGFHMIITDWNEVVLDEMPELVEE-GITSFKLFMAYKGALM 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564393312 174 VSNTELYEIFTCLGELGAIAQVHAENGDIIAQEQARMLEMGITGPEGHVLSRPEELEAEAVFRAITVASQTNCPLYVTKV 253
Cdd:PRK08323 157 LDDDELLRALQRAAELGALPMVHAENGDAIAYLQAKLLAEGKTGPEYHALSRPPEVEGEATNRAIMLAELAGAPLYIVHV 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564393312 254 MSKSAADLISQARKKGNVVFGEPITASLGIDGTHYWSKNWAKAAAFVTSPPLSPdpttPDYINSL---LASGDLQLSGSA 330
Cdd:PRK08323 237 SCKEALEAIRRARARGQRVFGETCPQYLLLDESEYDGPDWFEGAKYVMSPPLRD----KEHQDALwrgLQDGDLQVVATD 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564393312 331 HCTFSTAQKA-IGKDNFTAIPEGTNGVEERMSVIWDKAVATGKMDENQFVAVTSTNAAKIFNLYPRKGRIAVGSDSDLVI 409
Cdd:PRK08323 313 HCPFCFEQKKqLGRGDFTKIPNGTPGVEDRMPLLFSEGVMTGRITLNRFVELTSTNPAKIFGLYPRKGTIAVGADADIVI 392
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 564393312 410 WDPDAVKIVSAKNHQSVAEYNIFEGMELRGAPLVVICQGKIMLEDGNLHVTQGAGRFIPCSPFS 473
Cdd:PRK08323 393 WDPNATKTISASTLHSNVDYNPYEGFEVTGWPVTTLSRGEVVVEDGEFRGKAGHGRFLKRKPFQ 456
|
|
| PLN02942 |
PLN02942 |
dihydropyrimidinase |
12-483 |
0e+00 |
|
dihydropyrimidinase
Pssm-ID: 178530 Cd Length: 486 Bit Score: 550.22 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564393312 12 SDRLLIKGGRIVNDDQSFYADIYMEDGLIKQIGDNLIVPGGVKTIEANGKMVMPGGIDVHTHFQMPYKGMTTVDDFFQGT 91
Cdd:PLN02942 4 STKILIKGGTVVNAHHQELADVYVEDGIIVAVAPNLKVPDDVRVIDATGKFVMPGGIDPHTHLAMPFMGTETIDDFFSGQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564393312 92 KAALAGGTTMIIDHVVPePESSLTEAYEKWREWADgKSCCDYALHVDITHWNDSVKQEVQNLSKEKGVNSFMVYMAYKDL 171
Cdd:PLN02942 84 AAALAGGTTMHIDFVIP-VNGNLLAGYEAYEKKAE-KSCMDYGFHMAITKWDDTVSRDMETLVKEKGINSFKFFMAYKGS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564393312 172 YQVSNTELYEIFTCLGELGAIAQVHAENGDIIAQEQARMLEMGITGPEGHVLSRPEELEAEAVFRAITVASQTNCPLYVT 251
Cdd:PLN02942 162 LMVTDELLLEGFKRCKSLGALAMVHAENGDAVFEGQKRMIELGITGPEGHALSRPPLLEGEATARAIRLAKFVNTPLYVV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564393312 252 KVMSKSAADLISQARKKGNVVFGEPITASLGIDGTHYWSKNWAKAAAFVTSPPLSPdPTTPDYINSLLASGDLQLSGSAH 331
Cdd:PLN02942 242 HVMSIDAMEEIARARKSGQRVIGEPVVSGLVLDDSKLWDPDFTIASKYVMSPPIRP-AGHGKALQAALSSGILQLVGTDH 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564393312 332 CTFSTAQKAIGKDNFTAIPEGTNGVEERMSVIWDKAVATGKMDENQFVAVTSTNAAKIFNLYPRKGRIAVGSDSDLVIWD 411
Cdd:PLN02942 321 CPFNSTQKAFGKDDFRKIPNGVNGIEERMHLVWDTMVESGQISPTDYVRVTSTECAKIFNIYPRKGAILAGSDADIIILN 400
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 564393312 412 PDAVKIVSAKNHQSVAEYNIFEGMELRGAPLVVICQGKIMLEDGNLHVTQGAGRFIPCSPFSdYVYKRIKAR 483
Cdd:PLN02942 401 PNSTFTISAKTHHSRIDTNVYEGRRGKGKVEVTISQGRVVWENGELKVVRGSGRYIEMPPFS-YLFDGIQKA 471
|
|
| AllB |
COG0044 |
Dihydroorotase or related cyclic amidohydrolase [Nucleotide transport and metabolism]; ... |
16-468 |
7.94e-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: 381.36 E-value: 7.94e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564393312 16 LIKGGRIVNDDQSFYADIYMEDGLIKQIGDNLIVPGGVKTIEANGKMVMPGGIDVHTHFQMPykGMTTVDDFFQGTKAAL 95
Cdd:COG0044 1 LIKNGRVVDPGGLERADVLIEDGRIAAIGPDLAAPEAAEVIDATGLLVLPGLIDLHVHLREP--GLEHKEDIETGTRAAA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564393312 96 AGGTTMIIDHVVPEPESSLTEAYEKWREWADGKSCCDYALHVDITHWNDSVKQEVQNLsKEKGVNSFMVYMAYKDLYQVS 175
Cdd:COG0044 79 AGGVTTVVDMPNTNPVTDTPEALEFKLARAEEKALVDVGPHGALTKGLGENLAELGAL-AEAGAVAFKVFMGSDDGNPVL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564393312 176 NTE-LYEIFTCLGELGAIAQVHAENGDIIAqeqARMLEMGITGPEGHVLSRPEELEAEAVFRAITVASQTNCPLYVTKVM 254
Cdd:COG0044 158 DDGlLRRALEYAAEFGALVAVHAEDPDLIR---GGVMNEGKTSPRLGLKGRPAEAEEEAVARDIALAEETGARLHIVHVS 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564393312 255 SKSAADLISQARKKGNVVFGE--P----ITAS-LGIDGTHYwsknwakaaafVTSPPLSpdptTPDYINSL---LASGDL 324
Cdd:COG0044 235 TAEAVELIREAKARGLPVTAEvcPhhltLTDEdLERYGTNF-----------KVNPPLR----TEEDREALwegLADGTI 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564393312 325 QLSGSAHCTFSTAQKAigkDNFTAIPEGTNGVEERMSVIWDKAVATGKMDENQFVAVTSTNAAKIFNLyPRKGRIAVGSD 404
Cdd:COG0044 300 DVIATDHAPHTLEEKE---LPFAEAPNGIPGLETALPLLLTELVHKGRLSLERLVELLSTNPARIFGL-PRKGRIAVGAD 375
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 564393312 405 SDLVIWDPDAVKIVSAKNHQSVAEYNIFEGMELRGAPLVVICQGKIMLEDGNLhVTQGAGRFIP 468
Cdd:COG0044 376 ADLVLFDPDAEWTVTAEDLHSKSKNTPFEGRELTGRVVATIVRGRVVYEDGEV-VGEPRGRFLR 438
|
|
| PRK13404 |
PRK13404 |
dihydropyrimidinase; Provisional |
15-471 |
2.43e-116 |
|
dihydropyrimidinase; Provisional
Pssm-ID: 184033 [Multi-domain] Cd Length: 477 Bit Score: 353.62 E-value: 2.43e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564393312 15 LLIKGGRIVNDDQSFYADIYMEDGLIKQIGDNLivPGGVKTIEANGKMVMPGGIDVHTHFQMPY-KGMTTVDDFFQGTKA 93
Cdd:PRK13404 6 LVIRGGTVVTATDTFQADIGIRGGRIAALGEGL--GPGAREIDATGRLVLPGGVDSHCHIDQPSgDGIMMADDFYTGTVS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564393312 94 ALAGGTTMIIDHVVPEPESSLTEAYEKWREWADGKSCCDYALHVDITHWNDSV-KQEVQNLSKEkGVNSFMVYMAYKDLy 172
Cdd:PRK13404 84 AAFGGTTTVIPFAAQHRGQSLREAVEDYHRRAAGKAVIDYAFHLIVADPTEEVlTEELPALIAQ-GYTSFKVFMTYDDL- 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564393312 173 QVSNTELYEIFTCLGELGAIAQVHAENGDIIAQEQARMLEMGITGPEGHVLSRPEELEAEAVFRAITVASQTNCPLYVTK 252
Cdd:PRK13404 162 KLDDRQILDVLAVARRHGAMVMVHAENHDMIAWLTKRLLAAGLTAPKYHAISRPMLAEREATHRAIALAELVDVPILIVH 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564393312 253 VMSKSAADLISQARKKGNVVFGEP------ITAS-LGIDGTHywsknwakAAAFVTSPPLSpDPTTPDYINSLLASGDLQ 325
Cdd:PRK13404 242 VSGREAAEQIRRARGRGLKIFAETcpqylfLTAEdLDRPGME--------GAKYICSPPPR-DKANQEAIWNGLADGTFE 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564393312 326 LSGSAHCTF---STAQKAIGKDN--FTAIPEGTNGVEERMSVIWDKAVATGKMDENQFVAVTSTNAAKIFNLYPRKGRIA 400
Cdd:PRK13404 313 VFSSDHAPFrfdDTDGKLAAGANpsFKAIANGIPGIETRLPLLFSEGVVKGRISLNRFVALTSTNPAKLYGLYPRKGAIA 392
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 564393312 401 VGSDSDLVIWDPDAVKIVSAKNHQSVAEYNIFEGMELRGAPLVVICQGKIMLEDGNLHVTQGAGRFIPCSP 471
Cdd:PRK13404 393 IGADADIAIWDPDREVTITNADLHHAADYTPYEGMRVTGWPVTVLSRGRVVVEDGELVAERGSGQFLARSL 463
|
|
| L-HYD_ALN |
cd01315 |
L-Hydantoinases (L-HYDs) and Allantoinase (ALN); L-Hydantoinases are a member of the ... |
15-467 |
1.08e-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: 1.08e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564393312 15 LLIKGGRIVNDDQSFYADIYMEDGLIKQIGDNLIVPGGVKTIEANGKMVMPGGIDVHTHFQMPykGMTTVDDFFQGTKAA 94
Cdd:cd01315 2 LVIKNGRVVTPDGVREADIAVKGGKIAAIGPDIANTEAEEVIDAGGLVVMPGLIDTHVHINEP--GRTEWEGFETGTKAA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564393312 95 LAGGTTMIIDhvVP---EPESSLTEAYEKWREWADGKSCCDYALhvdithWNDSVKQEVQNLSK--EKGV---NSFMVYM 166
Cdd:cd01315 80 AAGGITTIID--MPlnsIPPTTTVENLEAKLEAAQGKLHVDVGF------WGGLVPGNLDQLRPldEAGVvgfKCFLCPS 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564393312 167 AYKDLYQVSNTELYEIFTCLGELGAIAQVHAENGDIIAQEQARMLEMGITGPEGHVLSRPEELEAEAVFRAITVASQTNC 246
Cdd:cd01315 152 GVDEFPAVDDEQLEEAMKELAKTGSVLAVHAENPEITEALQEQAKAKGKRDYRDYLASRPVFTEVEAIQRILLLAKETGC 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564393312 247 PLYVTKVMSKSAADLISQARKKGNVVFGEPITASLGI------DGthywsknwakAAAFVTSPPLSpDPTTPDYINSLLA 320
Cdd:cd01315 232 RLHIVHLSSAEAVPLIREARAEGVDVTVETCPHYLTFtaedvpDG----------GTEFKCAPPIR-DAANQEQLWEALE 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564393312 321 SGDLQLSGSAHCTFSTAQKAIGKDNFTAIPEGTNGVEERMSVIWDKAVATGKMDENQFVAVTSTNAAKIFNLYPRKGRIA 400
Cdd:cd01315 301 NGDIDMVVSDHSPCTPELKLLGKGDFFKAWGGISGLQLGLPVMLTEAVNKRGLSLEDIARLMCENPAKLFGLSHQKGRIA 380
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 564393312 401 VGSDSDLVIWDPDAVKIVSAKNHQSVAEYNIFEGMELRGAPLVVICQGKIMLEDGNlHVTQGAGRFI 467
Cdd:cd01315 381 VGYDADFVVWDPEEEFTVDAEDLYYKNKISPYVGRTLKGRVHATILRGTVVYQDGE-VVGEPLGQLL 446
|
|
| Cyclic_amidohydrolases |
cd01302 |
Cyclic amidohydrolases, including hydantoinase, dihydropyrimidinase, allantoinase, and ... |
61-441 |
6.55e-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: 6.55e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564393312 61 KMVMPGGIDVHTHFQMPYKGmTTVDDFFQGTKAALAGGTTMIIDHVVPEPESSLTEAYEKWREWADGKSCCDYALHVDIt 140
Cdd:cd01302 1 LLVLPGFIDIHVHLRDPGGT-TYKEDFESGSRAAAAGGVTTVIDMPNTGPPPIDLPAIELKIKLAEESSYVDFSFHAGI- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564393312 141 hwndSVKQEVQNLSK--EKGVNSFMVYMAYK--DLYQVSNTELYEIFTCLGELGAIAQVHAEngdiiaqeqarmlemgit 216
Cdd:cd01302 79 ----GPGDVTDELKKlfDAGINSLKVFMNYYfgELFDVDDGTLMRTFLEIASRGGPVMVHAE------------------ 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564393312 217 gpeghvlsrpeeleaeavfRAITVASQTNCPLYVTKVMSKSAADLISQARKKGNVVFGEPITASLGIDgTHYWSKNWAKa 296
Cdd:cd01302 137 -------------------RAAQLAEEAGANVHIAHVSSGEALELIKFAKNKGVKVTCEVCPHHLFLD-ESMLRLNGAW- 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564393312 297 aaFVTSPPLSPdPTTPDYINSLLASGDLQLSGSAHCTFSTAQKAIGKDnFTAIPEGTNGVEERMSVIWdKAVATGKMDEN 376
Cdd:cd01302 196 --GKVNPPLRS-KEDREALWEGVKNGKIDTIASDHAPHSKEEKESGKD-IWKAPPGFPGLETRLPILL-TEGVKRGLSLE 270
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 564393312 377 QFVAVTSTNAAKIFNLYPrKGRIAVGSDSDLVIWDPDAVKIVSAKNHQSVAEYNIFEGMELRGAP 441
Cdd:cd01302 271 TLVEILSENPARIFGLYP-KGTIAVGYDADLVIVDPKKEWKVTAEEIESKADWTPFEGMEVTGKP 334
|
|
| allantoinase |
TIGR03178 |
allantoinase; This enzyme carries out the first step in the degradation of allantoin, a ... |
15-468 |
1.50e-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: 1.50e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564393312 15 LLIKGGRIVNDDQSFYADIYMEDGLIKQIGDNlIVPGGVKTIEANGKMVMPGGIDVHTHFQMPykGMTTVDDFFQGTKAA 94
Cdd:TIGR03178 2 LIIRGGRVILPNGEREADVGVKGGKIAAIGPD-ILGPAAKIIDAGGLVVFPGVVDTHVHINEP--GRTEWEGFETGTRAA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564393312 95 LAGGTTMIIDHVVPEPESSLT-EAYEKWREWADGKsccdyaLHVDITHWNDSVKQEVQNLSK--EKGVNSFMVYMAY--- 168
Cdd:TIGR03178 79 AAGGITTYIDMPLNSIPATTTrASLEAKFEAAKGK------LAVDVGFWGGLVPYNLDDLREldEAGVVGFKAFLSPsgd 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564393312 169 KDLYQVSNTELYEIFTCLGELGAIAQVHAENGDIIAQEQARMLEMGITGPEGHVLSRPEELEAEAVFRAITVASQTNCPL 248
Cdd:TIGR03178 153 DEFPHVDDWQLYKGMRELARLGQLLLVHAENPAITSALGEEAPPQGGVGADAYLASRPVFAEVEAIRRTLALAKVTGCRV 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564393312 249 YVTKVMSKSAADLISQARKKGNVVFGEPItaslgidgTHYWSKNWAK----AAAFVTSPPLSPDPTTPDYINSLLAsGDL 324
Cdd:TIGR03178 233 HVVHLSSAEAVELITEAKQEGLDVTVETC--------PHYLTLTAEEvpdgGTLAKCAPPIRDLANQEGLWEALLN-GLI 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564393312 325 QLSGSAHCTFSTAQKAigKDNFTAIPEGTNGVEERMSVIWDKAVATGKMDENQFVAVTSTNAAKIFNLyPRKGRIAVGSD 404
Cdd:TIGR03178 304 DCVVSDHSPCTPDLKR--AGDFFKAWGGIAGLQSTLDVMFDEAVQKRGLPLEDIARLMATNPAKRFGL-AQKGRIAPGKD 380
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 564393312 405 SDLVIWDPDAVKIVSAKNHQSVAEYNIFEGMELRGAPLVVICQGKIMLEDGNLhVTQGAGRFIP 468
Cdd:TIGR03178 381 ADFVFVDPDESYTLTPDDLYYRHKVSPYVGRTIGGRVRATYLRGQCIYDDEQF-IGAPKGQLLL 443
|
|
| PRK06189 |
PRK06189 |
allantoinase; Provisional |
15-458 |
2.42e-54 |
|
allantoinase; Provisional
Pssm-ID: 235732 [Multi-domain] Cd Length: 451 Bit Score: 190.68 E-value: 2.42e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564393312 15 LLIKGGRIVNDDQSFYADIYMEDGLIKQIGDNLIVPGGvKTIEANGKMVMPGGIDVHTHFQMPykGMTTVDDFFQGTKAA 94
Cdd:PRK06189 5 LIIRGGKVVTPEGVYRADIGIKNGKIAEIAPEISSPAR-EIIDADGLYVFPGMIDVHVHFNEP--GRTHWEGFATGSAAL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564393312 95 LAGGTTMIIDHVVPEPESSLT-EAYEKWREWADGKSCCDYALhvdithWNDSVKQEVQNLSK--EKGVNSFMVYMAYK-- 169
Cdd:PRK06189 82 AAGGCTTYFDMPLNSIPPTVTrEALDAKAELARQKSAVDFAL------WGGLVPGNLEHLRElaEAGVIGFKAFMSNSgt 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564393312 170 DLYQVSNTE-LYEIFTCLGELGAIAQVHAENGDIIAQEQARMLEMGITGPEGHVLSRPEELEAEAVFRAITVASQTNCPL 248
Cdd:PRK06189 156 DEFRSSDDLtLYEGMKEIAALGKILALHAESDALTRHLTTQARQQGKTDVRDYLESRPVVAELEAVQRALLYAQETGCPL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564393312 249 YVTKVMSKSAADLISQARKKG-NV---------VFGEPITASLGIdgthywsknWAKAAafvtsPPLSPDPTTPDYINSL 318
Cdd:PRK06189 236 HFVHISSGKAVALIAEAKKRGvDVsvetcphylLFTEEDFERIGA---------VAKCA-----PPLRSRSQKEELWRGL 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564393312 319 LAsGDLQLSGSAH--CTFSTAQKaigkDNFTAIPEGTNGVEERMSVIWDKAVATGKMDENQFVAVTSTNAAKIFNLyPRK 396
Cdd:PRK06189 302 LA-GEIDMISSDHspCPPELKEG----DDFFLVWGGISGGQSTLLVMLTEGYIERGIPLETIARLLATNPAKRFGL-PQK 375
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 564393312 397 GRIAVGSDSDLVIWDPDAVKIVSAKNHQSVAEYNIFEGMELRGAPLVVICQGKIMLEDGNLH 458
Cdd:PRK06189 376 GRLEVGADADFVLVDLDETYTLTKEDLFYRHKQSPYEGRTFPGRVVATYLRGQCVYQDGEVF 437
|
|
| PRK02382 |
PRK02382 |
dihydroorotase; Provisional |
15-468 |
3.60e-54 |
|
dihydroorotase; Provisional
Pssm-ID: 179417 [Multi-domain] Cd Length: 443 Bit Score: 189.86 E-value: 3.60e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564393312 15 LLIKGGRIVNDDQSFYADIYMEDGLIKQIGDNLIVPGGVKTIEANGKMVMPGGIDVHTHFQMPykGMTTVDDFFQGTKAA 94
Cdd:PRK02382 4 ALLKDGRVYYNNSLQPRDVRIDGGKITAVGKDLDGSSSEEVIDARGMLLLPGGIDVHVHFREP--GYTHKETWYTGSRSA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564393312 95 LAGGTTMIIDHVVPEPESSLTEAYEKWREWADGKSCCDYALhvdithwNDSVKQEVQNLSK--EKGVNSF-MVYMA--YK 169
Cdd:PRK02382 82 AAGGVTTVVDQPNTDPPTVDGESFDEKAELAARKSIVDFGI-------NGGVTGNWDPLESlwERGVFALgEIFMAdsTG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564393312 170 DLyQVSNTELYEIFTCLGELGAIAQVHAENGDIIAqEQARMLEmGITGPEGHVLSRPEELEAEAVFRAITVASQTNCPLY 249
Cdd:PRK02382 155 GM-GIDEELFEEALAEAARLGVLATVHAEDEDLFD-ELAKLLK-GDADADAWSAYRPAAAEAAAVERALEVASETGARIH 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564393312 250 VTKVMSKSAADLISqarkkgnvvfGEPITAslgiDGT-HYW---SKNWAKAAAFV-TSPPLSPDPTTPDYINSLlASGDL 324
Cdd:PRK02382 232 IAHISTPEGVDAAR----------REGITC----EVTpHHLflsRRDWERLGTFGkMNPPLRSEKRREALWERL-NDGTI 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564393312 325 QLSGSAHCTFSTAQKAigkDNFTAIPEGTNGVEERMSVIWdKAVATGKMDENQFVAVTSTNAAKIFNLyPRKGRIAVGSD 404
Cdd:PRK02382 297 DVVASDHAPHTREEKD---ADIWDAPSGVPGVETMLPLLL-AAVRKNRLPLERVRDVTAANPARIFGL-DGKGRIAEGYD 371
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 564393312 405 SDLVIWDPDAVKIVSAKNHQSVAEYNIFEGMElrGA-PLVVICQGKIMLEDGNLHVTQGAGRFIP 468
Cdd:PRK02382 372 ADLVLVDPDAAREIRGDDLHSKAGWTPFEGME--GVfPELTMVRGTVVWDGDDINAKRGRGEFLR 434
|
|
| DHOase_IIb |
cd01318 |
Dihydroorotase (DHOase), subgroup IIb; DHOases catalyze the reversible interconversion of ... |
60-448 |
9.41e-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: 9.41e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564393312 60 GKMVMPGGIDVHTHFQMPykGMTTVDDFFQGTKAALAGGTTMIID--HVVPEPESSltEAYEKWREWADGKSCCDYALHV 137
Cdd:cd01318 1 GLLILPGVIDIHVHFREP--GLTYKEDFVSGSRAAAAGGVTTVMDmpNTKPPTTTA--EALYEKLRLAAAKSVVDYGLYF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564393312 138 DIThwndsvKQEVQNLSKEKGVNSFMVYMA--YKDLYQVSNTeLYEIFtclGELGAIAQVHAENGDIIAQEQARMLEMGI 215
Cdd:cd01318 77 GVT------GSEDLEELDKAPPAGYKIFMGdsTGDLLDDEET-LERIF---AEGSVLVTFHAEDEDRLRENRKELKGESA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564393312 216 tgpegHVLSRPEELEAEAVFRAITVASQTNCPLYVTKVMSKSAADLISQARKKGNV-------VFGEPITASLGidgthy 288
Cdd:cd01318 147 -----HPRIRDAEAAAVATARALKLARRHGARLHICHVSTPEELKLIKKAKPGVTVevtphhlFLDVEDYDRLG------ 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564393312 289 wskNWAKaaafvTSPPLSpDPTTPDYINSLLASGDLQLSGSAHCTFSTAQKAIGkdnFTAIPEGTNGVEERMSVIWDkAV 368
Cdd:cd01318 216 ---TLGK-----VNPPLR-SREDRKALLQALADGRIDVIASDHAPHTLEEKRKG---YPAAPSGIPGVETALPLMLT-LV 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564393312 369 ATGKMDENQFVAVTSTNAAKIFNLyPRKGRIAVGSDSDLVIWDPDAVKIVSAKNHQSVAEYNIFEGMELRGAPLVVICQG 448
Cdd:cd01318 283 NKGILSLSRVVRLTSHNPARIFGI-KNKGRIAEGYDADLTVVDLKEERTIRAEEFHSKAGWTPFEGFEVTGFPVMTIVRG 361
|
|
| PRK08044 |
PRK08044 |
allantoinase AllB; |
15-422 |
2.85e-36 |
|
allantoinase AllB;
Pssm-ID: 169193 [Multi-domain] Cd Length: 449 Bit Score: 140.76 E-value: 2.85e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564393312 15 LLIKGGRIVNDDQSFYADIYMEDGLIKQIGDNLivPGGVKTIEANGKMVMPGGIDVHTHFQMPykGMTTVDDFFQGTKAA 94
Cdd:PRK08044 5 LIIKNGTVILENEARVVDIAVKGGKIAAIGQDL--GDAKEVMDASGLVVSPGMVDAHTHISEP--GRSHWEGYETGTRAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564393312 95 LAGGTTMIIDHVVPE-PESSLTEAYEKWREWADGKSCCDYALHVDITHWNDSVKQEVQnlskEKGVNSFMVYMAY----- 168
Cdd:PRK08044 81 AKGGITTMIEMPLNQlPATVDRASIELKFDAAKGKLTIDAAQLGGLVSYNLDRLHELD----EVGVVGFKCFVATcgdrg 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564393312 169 --KDLYQVSNTELYEIFTCLGELGAIAQVHAENGDIIAQEQARMLEMGITGPEGHVLSRPEELEAEAVFRAITVASQTNC 246
Cdd:PRK08044 157 idNDFRDVNDWQFYKGAQKLGELGQPVLVHCENALICDELGEEAKREGRVTAHDYVASRPVFTEVEAIRRVLYLAKVAGC 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564393312 247 PLYVTKVMSKSAADLISQARKKGNVVFGEPItaslgidgTHYWSKNWAKAAAFVT----SPPLSPDPTTPDYINSLLaSG 322
Cdd:PRK08044 237 RLHVCHISSPEGVEEVTRARQEGQDVTCESC--------PHYFVLDTDQFEEIGTlakcSPPIRDLENQKGMWEKLF-NG 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564393312 323 DLQLSGSAHCTFSTAQKAigkDNFTAIPEGTNGVEERMSVIWDKAVATGKMDENQFVAVTSTNAAKIFNLyPRKGRIAVG 402
Cdd:PRK08044 308 EIDCLVSDHSPCPPEMKA---GNIMEAWGGIAGLQNCMDVMFDEAVQKRGMSLPMFGKLMATNAADIFGL-QQKGRIAPG 383
|
410 420
....*....|....*....|
gi 564393312 403 SDSDLVIWDPDAVKIVSAKN 422
Cdd:PRK08044 384 KDADFVFIQPNSSYVLKNED 403
|
|
| pyrC |
PRK09357 |
dihydroorotase; Validated |
14-454 |
1.59e-35 |
|
dihydroorotase; Validated
Pssm-ID: 236479 [Multi-domain] Cd Length: 423 Bit Score: 138.02 E-value: 1.59e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564393312 14 RLLIKGGRIVNDDQSFY-ADIYMEDGLIKQIGDNLIVPGgVKTIEANGKMVMPGGIDVHTHFQMPykGMTTVDDFFQGTK 92
Cdd:PRK09357 2 MILIKNGRVIDPKGLDEvADVLIDDGKIAAIGENIEAEG-AEVIDATGLVVAPGLVDLHVHLREP--GQEDKETIETGSR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564393312 93 AALAGGTTMiidhVV------PEPESSLTEAYEKWRewADGKSCCDyaLHV--DIThwndsVKQEVQNLS-----KEKGV 159
Cdd:PRK09357 79 AAAAGGFTT----VVampntkPVIDTPEVVEYVLDR--AKEAGLVD--VLPvgAIT-----KGLAGEELTefgalKEAGV 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564393312 160 NSFMvymayKDLYQVSNTEL-YEIFTCLGELG-AIAQvHAE----NGDIIAQEQARMLEMGITGpeghvlsRPEELEAEA 233
Cdd:PRK09357 146 VAFS-----DDGIPVQDARLmRRALEYAKALDlLIAQ-HCEdpslTEGGVMNEGEVSARLGLPG-------IPAVAEEVM 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564393312 234 VFRAITVASQTNCPLYVTKVMSKSAADLISQARKKGnvvfgEPITA------------SLGIDGTHYwsknwaKAAafvt 301
Cdd:PRK09357 213 IARDVLLAEATGARVHICHVSTAGSVELIRWAKALG-----IKVTAevtphhllltdeDLLTYDPNY------KVN---- 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564393312 302 sPPLSpdptTPDYINSL---LASGDLQLSGSAHCTFSTAQKAIGkdnFTAIPEGTNGVEERMSVIWDKAVATGKMDENQF 378
Cdd:PRK09357 278 -PPLR----TEEDREALiegLKDGTIDAIATDHAPHAREEKECE---FEAAPFGITGLETALSLLYTTLVKTGLLDLEQL 349
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 564393312 379 VAVTSTNAAKIFNLYPrkGRIAVGSDSDLVIWDPDAVKIVSAKNHQSVAEYNIFEGMELRGAPLVVICQGKIMLED 454
Cdd:PRK09357 350 LEKMTINPARILGLPA--GPLAEGEPADLVIFDPEAEWTVDGEDFASKGKNTPFIGMKLKGKVVYTIVDGKIVYQD 423
|
|
| PRK07575 |
PRK07575 |
dihydroorotase; Provisional |
12-457 |
1.93e-31 |
|
dihydroorotase; Provisional
Pssm-ID: 236055 [Multi-domain] Cd Length: 438 Bit Score: 126.71 E-value: 1.93e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564393312 12 SDRLLIKGGRIVNDDQSFY-ADIYMEDGLIKQIGDNLIVPGGVKTIEANGKMVMPGGIDVHTHFQMPykGMTTVDDFFQG 90
Cdd:PRK07575 2 MMSLLIRNARILLPSGELLlGDVLVEDGKIVAIAPEISATAVDTVIDAEGLTLLPGVIDPQVHFREP--GLEHKEDLFTA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564393312 91 TKAALAGGTTMIIDHVVPEPESSLTEAYEKWREWADGKSCCDYALHVDITHWNDSVKQEVQNLSkekGVNSFMVYMaYKD 170
Cdd:PRK07575 80 SRACAKGGVTSFLEMPNTKPLTTTQAALDDKLARAAEKCVVNYGFFIGATPDNLPELLTANPTC---GIKIFMGSS-HGP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564393312 171 LYQVSNTELYEIFTCLGELgaIAqVHAENGDIIAQEQARMleMGITGPEGHVLSRPEELEAEAVFRAITVASQTNCPLYV 250
Cdd:PRK07575 156 LLVDEEAALERIFAEGTRL--IA-VHAEDQARIRARRAEF--AGISDPADHSQIQDEEAALLATRLALKLSKKYQRRLHI 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564393312 251 TKVMSKSAADLISQArkKGNVVFGEPITASLGIDGTHYwsknwAKAAAFV-TSPPLSpDPTTPDYINSLLASGDLQLSGS 329
Cdd:PRK07575 231 LHLSTAIEAELLRQD--KPSWVTAEVTPQHLLLNTDAY-----ERIGTLAqMNPPLR-SPEDNEALWQALRDGVIDFIAT 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564393312 330 AHCTFSTAQKAIGKDNftaIPEGTNGVEERMSVIWDKAVAtGKMDENQFVAVTSTNAAKIFNLyPRKGRIAVGSDSDLVI 409
Cdd:PRK07575 303 DHAPHTLEEKAQPYPN---SPSGMPGVETSLPLMLTAAMR-GKCTVAQVVRWMSTAVARAYGI-PNKGRIAPGYDADLVL 377
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 564393312 410 WDPDAVKIVSAKNHQSVAEYNIFEGMELRGAPLVVICQGKIMLEDGNL 457
Cdd:PRK07575 378 VDLNTYRPVRREELLTKCGWSPFEGWNLTGWPVTTIVGGQIVFDRGQV 425
|
|
| DHOase_IIa |
cd01317 |
Dihydroorotase (DHOase), subgroup IIa; DHOases catalyze the reversible interconversion of ... |
52-442 |
1.94e-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: 1.94e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564393312 52 GVKTIEANGKMVMPGGIDVHTHFQMPykGMTTVDDFFQGTKAALAGGTTmiidHVVPEPESslteayekwREWADgkscc 131
Cdd:cd01317 1 DAEVIDAEGKILAPGLVDLHVHLREP--GFEYKETLESGAKAAAAGGFT----TVVCMPNT---------NPVID----- 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564393312 132 dyalhvdithwNDSVKQEVQNLSKEKGVNSFMVYMAY-KDLYQVSNTELYEiftcLGELGAIA----QVHAENGDIIAQ- 205
Cdd:cd01317 61 -----------NPAVVELLKNRAKDVGIVRVLPIGALtKGLKGEELTEIGE----LLEAGAVGfsddGKPIQDAELLRRa 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564393312 206 -EQARMLEMGIT----------------GPEGHVL---SRPEELEAEAVFRAITVASQTNCPLYVTKVMSKSAADLISQA 265
Cdd:cd01317 126 lEYAAMLDLPIIvhpedpslagggvmneGKVASRLglpGIPPEAETIMVARDLELAEATGARVHFQHLSTARSLELIRKA 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564393312 266 RKKGnvvfgEPITASLGIdgtHYWS------KNWAkaAAFVTSPPLSpDPTTPDYINSLLASGDLQLSGSAHCTFSTAQK 339
Cdd:cd01317 206 KAKG-----LPVTAEVTP---HHLLlddealESYD--TNAKVNPPLR-SEEDREALIEALKDGTIDAIASDHAPHTDEEK 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564393312 340 AIGkdnFTAIPEGTNGVEERMSVIWDKAVATGKMDENQFVAVTSTNAAKIFNLYPrkGRIAVGSDSDLVIWDPDAVKIVS 419
Cdd:cd01317 275 DLP---FAEAPPGIIGLETALPLLWTLLVKGGLLTLPDLIRALSTNPAKILGLPP--GRLEVGAPADLVLFDPDAEWIVD 349
|
410 420
....*....|....*....|...
gi 564393312 420 AKNHQSVAEYNIFEGMELRGAPL 442
Cdd:cd01317 350 EETFRSKSKNTPFDGQKLKGRVL 372
|
|
| PRK09060 |
PRK09060 |
dihydroorotase; Validated |
15-465 |
2.32e-30 |
|
dihydroorotase; Validated
Pssm-ID: 181632 [Multi-domain] Cd Length: 444 Bit Score: 123.88 E-value: 2.32e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564393312 15 LLIKGGRIVNDDQSFYADIYMEDGLIKQIGDNLIVPGGvKTIEANGKMVMPGGIDVHTHFQMPykGMTTVDDFFQGTKAA 94
Cdd:PRK09060 7 LILKGGTVVNPDGEGRADIGIRDGRIAAIGDLSGASAG-EVIDCRGLHVLPGVIDSQVHFREP--GLEHKEDLETGSRAA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564393312 95 LAGGTTMIIDHVVPEPESSLTEAYEKWREWADGKSCCDYALHVDITHWNdsvKQEVQNLSKEKGVNSFMVYM--AYKDLY 172
Cdd:PRK09060 84 VLGGVTAVFEMPNTNPLTTTAEALADKLARARHRMHCDFAFYVGGTRDN---ADELAELERLPGCAGIKVFMgsSTGDLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564393312 173 QVSNTELYEIftclgeLGAI---AQVHAEngdiiaqEQARMLEMGITGPEGHVLSRPEELEAEAVFRA----ITVASQTN 245
Cdd:PRK09060 161 VEDDEGLRRI------LRNGrrrAAFHSE-------DEYRLRERKGLRVEGDPSSHPVWRDEEAALLAtrrlVRLARETG 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564393312 246 CPLYVTKVMSKSAADLISQARkkgNVVFGEPITASLGIDGTHYWSKNWAKAaafVTSPPLSpDPTTPDYINSLLASGDLQ 325
Cdd:PRK09060 228 RRIHVLHVSTAEEIDFLADHK---DVATVEVTPHHLTLAAPECYERLGTLA---QMNPPIR-DARHRDGLWRGVRQGVVD 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564393312 326 LSGSAHCTFSTAQKAigkDNFTAIPEGTNGVEERMSVIWDKaVATGKMDENQFVAVTSTNAAKIFNLyPRKGRIAVGSDS 405
Cdd:PRK09060 301 VLGSDHAPHTLEEKA---KPYPASPSGMTGVQTLVPIMLDH-VNAGRLSLERFVDLTSAGPARIFGI-AGKGRIAVGYDA 375
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 564393312 406 DLVIWDPDAVKIVSAKNHQSVAEYNIFEGMELRGAPLVVICQGKIMLEDGNLhVTQGAGR 465
Cdd:PRK09060 376 DFTIVDLKRRETITNEWIASRCGWTPYDGKEVTGWPVGTIVRGQRVMWDGEL-VGPPTGE 434
|
|
| PLN02795 |
PLN02795 |
allantoinase |
1-467 |
1.15e-29 |
|
allantoinase
Pssm-ID: 178392 [Multi-domain] Cd Length: 505 Bit Score: 122.58 E-value: 1.15e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564393312 1 MYSPARNKVRQSDRLLIK-------GGRIVNDDQSFYADIYMEDGLIKQIGDNLIVPG---GVKTIEANGKMVMPGGIDV 70
Cdd:PLN02795 25 LFAPALPLQGRDRCSLLPwphfvlySKRVVTPAGVIPGAVEVEGGRIVSVTKEEEAPKsqkKPHVLDYGNAVVMPGLIDV 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564393312 71 HTHFQMPykGMTTVDDFFQGTKAALAGGTTMIIDhvVP---EPESSLTEAYEKWREWADGKsccdyaLHVDITHWNDSVK 147
Cdd:PLN02795 105 HVHLNEP--GRTEWEGFPTGTKAAAAGGITTLVD--MPlnsFPSTTSVETLELKIEAAKGK------LYVDVGFWGGLVP 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564393312 148 QEVQNLSKEK--------GVNSFMVYMAYKDLYQVSNTELYEIFTCLGELGAIAQVHAENGDIIAQEQarMLEMGITGPE 219
Cdd:PLN02795 175 ENAHNASVLEelldagalGLKSFMCPSGINDFPMTTATHIKAALPVLAKYGRPLLVHAEVVSPVESDS--RLDADPRSYS 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564393312 220 GHVLSRPEELEAEAVFRAITVASQTN-------CPLYVTKVM-SKSAADLISQARKKGNVVFGEPITASLGI------DG 285
Cdd:PLN02795 253 TYLKSRPPSWEQEAIRQLLEVAKDTRpggvaegAHVHIVHLSdAESSLELIKEAKAKGDSVTVETCPHYLAFsaeeipDG 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564393312 286 thywsknwakAAAFVTSPPLSpDPTTPDYINSLLASGDLQLSGSAHCTFSTAQKAIGKDNFTAIPEGTNGVEERMSVIWD 365
Cdd:PLN02795 333 ----------DTRYKCAPPIR-DAANRELLWKALLDGDIDMLSSDHSPSPPDLKLLEEGNFLRAWGGISSLQFVLPATWT 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564393312 366 KAVATGkMDENQFVAVTSTNAAKIFNLyPRKGRIAVGSDSDLVIWDPDAVKIVSAK-----NHQSVAEYnifEGMELRGA 440
Cdd:PLN02795 402 AGRAYG-LTLEQLARWWSERPAKLAGL-DSKGAIAPGKDADIVVWDPEAEFVLDESypiyhKHKSLSPY---LGTKLSGK 476
|
490 500
....*....|....*....|....*..
gi 564393312 441 PLVVICQGKIMLEDGNlHVTQGAGRFI 467
Cdd:PLN02795 477 VIATFVRGNLVFLEGK-HAKQACGSPI 502
|
|
| PRK04250 |
PRK04250 |
dihydroorotase; Provisional |
20-455 |
2.16e-29 |
|
dihydroorotase; Provisional
Pssm-ID: 235265 [Multi-domain] Cd Length: 398 Bit Score: 120.26 E-value: 2.16e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564393312 20 GRIVNDDQSFYADIYMEDGLIKQIGDNLIvpGGVKTIEANGKMVMPGGIDVHTH---FQMPYKgmTTVDdffQGTKAALA 96
Cdd:PRK04250 4 GKFLLKGRIVEGGIGIENGRISKISLRDL--KGKEVIKVKGGIILPGLIDVHVHlrdFEESYK--ETIE---SGTKAALH 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564393312 97 GGTTMIIDHVVPEPESSLTEAYEKWREWADGKSCCDYALHVDITHWNDSVKQEVQNLSKEkgvnsFMVyMAYKDLYQVSN 176
Cdd:PRK04250 77 GGITLVFDMPNTKPPIMDEKTYEKRMRIAEKKSYADYALNFLIAGNCEKAEEIKADFYKI-----FMG-ASTGGIFSENF 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564393312 177 TELYEiftclgELGAIAQVHAENGDIIAQEqarmlemgitgPEghvlsRPEELEAEAVFRAITVASQTNCPLYVTKVMSK 256
Cdd:PRK04250 151 EVDYA------CAPGIVSVHAEDPELIREF-----------PE-----RPPEAEVVAIERALEAGKKLKKPLHICHISTK 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564393312 257 SAADLISQARKkgnvvfgEPITASLGIDGTHYWSKNWAKAAAFVTSPPLSpdpTTPDYINSLLASGDLQLSGSAHCTFST 336
Cdd:PRK04250 209 DGLKLILKSNL-------PWVSFEVTPHHLFLTRKDYERNPLLKVYPPLR---SEEDRKALWENFSKIPIIASDHAPHTL 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564393312 337 AQKAIGKdnfTAIPegtnGVEERMSVIWDkAVATGKMDENQFVAVTSTNAAKIFNlYPRKGrIAVGSDSDLVIWDPDAVK 416
Cdd:PRK04250 279 EDKEAGA---AGIP----GLETEVPLLLD-AANKGMISLFDIVEKMHDNPARIFG-IKNYG-IEEGNYANFAVFDMKKEW 348
|
410 420 430
....*....|....*....|....*....|....*....
gi 564393312 417 IVSAKNHQSVAEYNIFEGMELRGAPLVVICQGKIMLEDG 455
Cdd:PRK04250 349 TIKAEELYTKAGWTPYEGFKLKGKVIMTILRGEVVMEDD 387
|
|
| PRK01211 |
PRK01211 |
dihydroorotase; Provisional |
30-468 |
1.50e-23 |
|
dihydroorotase; Provisional
Pssm-ID: 179247 [Multi-domain] Cd Length: 409 Bit Score: 103.01 E-value: 1.50e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564393312 30 YADIYMEDGLIKQIGDNLivpGGVKTIEANGkMVMPGGIDVHTHFQMPykGMTTVDDFFQGTKAALAGGTTMIIDHVVPE 109
Cdd:PRK01211 15 YLEIEVEDGKIKSIKKDA---GNIGKKELKG-AILPAATDIHVHFRTP--GETEKEDFSTGTLSAIFGGTTFIMDMPNNN 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564393312 110 PESSLTEAYEKWREWADGKSCCDYALHVDITHWNDSVKQEVQnlskekgvNSFMVYMAYKDLYQVSNTELYEIfTCLGEL 189
Cdd:PRK01211 89 IPIKDYNAFSDKLGRVAPKAYVDFSLYSMETGNNALILDERS--------IGLKVYMGGTTNTNGTDIEGGEI-KKINEA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564393312 190 GAIAQVHAENGDIIAQEQARMLEMgitgpEGHVLSRPEELEAEAVFRAITVASQtncplyvTKVMS-KSAADLISQarkk 268
Cdd:PRK01211 160 NIPVFFHAELSECLRKHQFESKNL-----RDHDLARPIECEIKAVKYVKNLDLK-------TKIIAhVSSIDVIGR---- 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564393312 269 gnvvFGEPITASlgidgtHYWSKNWAKAAAF-VTSPPLSPDPTTPDYINSLLaSGDLQLSGSAHCTFSTAQKAigkdNFT 347
Cdd:PRK01211 224 ----FLREVTPH------HLLLNDDMPLGSYgKVNPPLRDRWTQERLLEEYI-SGRFDILSSDHAPHTEEDKQ----EFE 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564393312 348 AIPEGTNGVEERMSVIWdKAVATGKMDENQFVAVTSTNAAKIFNLypRKGRIAVGSDSDLVIWDPDAVKIVSAKNHQSVA 427
Cdd:PRK01211 289 YAKSGIIGVETRVPLFL-ALVKKKILPLDVLYKTAIERPASLFGI--KKGKIEEGYDADFMAFDFTNIKKINDKRLHSKC 365
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 564393312 428 EYNIFEGMELRgAPLVVICQGKIMLEDGNLhVTQGAGRFIP 468
Cdd:PRK01211 366 PVSPFNGFDAI-FPSHVIMRGEVVIDNYEL-ISERTGKFVP 404
|
|
| Amidohydro_1 |
pfam01979 |
Amidohydrolase family; This family of enzymes are a a large metal dependent hydrolase ... |
62-451 |
5.71e-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: 100.27 E-value: 5.71e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564393312 62 MVMPGGIDVHTHFQM------PYKGMTTVDDFFQGTKAALAGGTTMIIDHVVPEPESSLT--EAYEKWRE--WADGKSCC 131
Cdd:pfam01979 1 IVLPGLIDAHVHLEMgllrgiPVPPEFAYEALRLGITTMLKSGTTTVLDMGATTSTGIEAllEAAEELPLglRFLGPGCS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564393312 132 ---DYALHVDIThwndSVKQEVQNLSKEKGVNSFMVYMAYKD--LYQVSNTELYEIFTCLGELGAIAQVHAENGDIiaqE 206
Cdd:pfam01979 81 ldtDGELEGRKA----LREKLKAGAEFIKGMADGVVFVGLAPhgAPTFSDDELKAALEEAKKYGLPVAIHALETKG---E 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564393312 207 QARMLEMGITGPEghVLSRPEELEAEAVFRAITVASQTNCPLYVTkvmskSAADLISQARKKGNVvfgepitasLGIDGT 286
Cdd:pfam01979 154 VEDAIAAFGGGIE--HGTHLEVAESGGLLDIIKLILAHGVHLSPT-----EANLLAEHLKGAGVA---------HCPFSN 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564393312 287 HYWSKNWAKAAAfvtspplspdpttpdyinsLLASGDLQLSGSAHCtfstaqkaIGKDNFTAIPEGTNGVEERmsviwdk 366
Cdd:pfam01979 218 SKLRSGRIALRK-------------------ALEDGVKVGLGTDGA--------GSGNSLNMLEELRLALELQ------- 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564393312 367 AVATGKMDENQFVAVTSTNAAKIFNLYPRKGRIAVGSDSDLVIWDPDavkivsaknhqsvaEYNIFEGMELRGAPLVVIC 446
Cdd:pfam01979 264 FDPEGGLSPLEALRMATINPAKALGLDDKVGSIEVGKDADLVVVDLD--------------PLAAFFGLKPDGNVKKVIV 329
|
....*
gi 564393312 447 QGKIM 451
Cdd:pfam01979 330 KGKIV 334
|
|
| PRK09236 |
PRK09236 |
dihydroorotase; Reviewed |
13-458 |
9.77e-22 |
|
dihydroorotase; Reviewed
Pssm-ID: 181716 Cd Length: 444 Bit Score: 98.02 E-value: 9.77e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564393312 13 DRLLIKGGRIVNDDQSFYADIYMEDGLIKQIGDNLIVPGGVKTIEANGKMVMPGGIDVHTHFQMPykGMTTVDDFFQGTK 92
Cdd:PRK09236 2 KRILIKNARIVNEGKIFEGDVLIENGRIAKIASSISAKSADTVIDAAGRYLLPGMIDDQVHFREP--GLTHKGDIASESR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564393312 93 AALAGGTTMIID--HVVPepeSSLT-EAYEKWREWADGKSCCDYALHVDIThwNDSVkQEVQNLSKEK--GVNSFM---- 163
Cdd:PRK09236 80 AAVAGGITSFMEmpNTNP---PTTTlEALEAKYQIAAQRSLANYSFYFGAT--NDNL-DEIKRLDPKRvcGVKVFMgast 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564393312 164 ----VymaykDLYQVsnteLYEIFTCLGELgaIAqVHAENGDIIAQEQARMLEM---GITgPEGHVLSRpeelEAEAVFR 236
Cdd:PRK09236 154 gnmlV-----DNPET----LERIFRDAPTL--IA-THCEDTPTIKANLAKYKEKygdDIP-AEMHPLIR----SAEACYK 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564393312 237 ----AITVASQTNCPLYVTKVMSKSAADLISQ---ARKKgnvvfgepITASLGIDGTHYWSKNWAKAAAFVTSPPLSPDP 309
Cdd:PRK09236 217 ssslAVSLAKKHGTRLHVLHISTAKELSLFENgplAEKR--------ITAEVCVHHLWFDDSDYARLGNLIKCNPAIKTA 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564393312 310 TTPDYINSLLASGDLQLSGSAHCTFSTAQKaigKDNFTAIPEGTNGVEERMSVIWDKaVATGKMDENQFVAVTSTNAAKI 389
Cdd:PRK09236 289 SDREALRQALADDRIDVIATDHAPHTWEEK---QGPYFQAPSGLPLVQHALPALLEL-VHEGKLSLEKVVEKTSHAPAIL 364
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 564393312 390 FNLyPRKGRIAVGSDSDLVIWDPDAVKIVSAKNHQSVAEYNIFEGMELRGAPLVVICQGKIMLEDGNLH 458
Cdd:PRK09236 365 FDI-KERGFIREGYWADLVLVDLNSPWTVTKENILYKCGWSPFEGRTFRSRVATTFVNGQLVYHNGQLV 432
|
|
| HutI |
COG1228 |
Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport ... |
6-420 |
4.99e-14 |
|
Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440841 [Multi-domain] Cd Length: 386 Bit Score: 73.84 E-value: 4.99e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564393312 6 RNKVRQSDRLLIKGGRIVNDDQSFY---ADIYMEDGLIKQIGDN--LIVPGGVKTIEANGKMVMPGGIDVHTHFQMPYKG 80
Cdd:COG1228 1 KKAPAQAGTLLITNATLVDGTGGGVienGTVLVEDGKIAAVGPAadLAVPAGAEVIDATGKTVLPGLIDAHTHLGLGGGR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564393312 81 MT----------TVDDFFQGTK---AALAGGTTMIIDH------VVPEPESSLTEAYEKWREWADGKS-CCDYALHvdiT 140
Cdd:COG1228 81 AVefeagggitpTVDLVNPADKrlrRALAAGVTTVRDLpggplgLRDAIIAGESKLLPGPRVLAAGPAlSLTGGAH---A 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564393312 141 HWNDSVKQEVQNLsKEKGVNSFMVYMAYKDlYQVSNTELYEIFTCLGELGAIAQVHAENGDIIaqeqARMLEMGITGPEg 220
Cdd:COG1228 158 RGPEEARAALREL-LAEGADYIKVFAEGGA-PDFSLEELRAILEAAHALGLPVAAHAHQADDI----RLAVEAGVDSIE- 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564393312 221 HVLSRPEEleaeavfraitvasqtncplyvtkvmsksAADLIsqaRKKGNVVfgepitaslgidgthywsknwakaaafv 300
Cdd:COG1228 231 HGTYLDDE-----------------------------VADLL---AEAGTVV---------------------------- 250
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564393312 301 tsppLSPDPTTPDYINSLLASGDLQLSGSAHC-TFSTAQK--------AIGKDNFTAIPEGTNGVEErmsvIWdKAVATG 371
Cdd:COG1228 251 ----LVPTLSLFLALLEGAAAPVAAKARKVREaALANARRlhdagvpvALGTDAGVGVPPGRSLHRE----LA-LAVEAG 321
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 564393312 372 kMDENQ-FVAVTStNAAKIFNLYPRKGRIAVGSDSDLVIWDPDAVKIVSA 420
Cdd:COG1228 322 -LTPEEaLRAATI-NAAKALGLDDDVGSLEPGKLADLVLLDGDPLEDIAY 369
|
|
| ATZ_TRZ_like |
cd01298 |
TRZ/ATZ family contains enzymes from the atrazine degradation pathway and related hydrolases. ... |
15-120 |
1.50e-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: 1.50e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564393312 15 LLIKGGRIVNDDQS---FYADIYMEDGLIKQIGDNLIVPG--GVKTIEANGKMVMPGGIDVHTHFQM------------- 76
Cdd:cd01298 1 ILIRNGTIVTTDPRrvlEDGDVLVEDGRIVAVGPALPLPAypADEVIDAKGKVVMPGLVNTHTHLAMtllrgladdlplm 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 564393312 77 --------PYKGMTTVDDFFQGTKAALA----GGTTMIIDHVVPEPEsSLTEAYEK 120
Cdd:cd01298 81 ewlkdliwPLERLLTEEDVYLGALLALAemirSGTTTFADMYFFYPD-AVAEAAEE 135
|
|
| pyrC |
PRK00369 |
dihydroorotase; Provisional |
32-466 |
3.67e-12 |
|
dihydroorotase; Provisional
Pssm-ID: 234738 [Multi-domain] Cd Length: 392 Bit Score: 68.25 E-value: 3.67e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564393312 32 DIYMEDGlIKQIGDNLIVpgGVKTIEANGK---------MVMPGGIDVHTHF---QMPYKgmttvDDFFQGTKAALAGGT 99
Cdd:PRK00369 8 KAYLGKE-IKEICINFDR--RIKEIKSRCKpdldlpqgtLILPGAIDLHVHLrglKLSYK-----EDVASGTSEAAYGGV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564393312 100 TMIIDHVVPEPESSLTEAY-EKWREWADGkSCCDYALHVDIThwnDSVKqEVQNLskekGVNSFMVYMayKDLyqvsntE 178
Cdd:PRK00369 80 TLVADMPNTIPPLNTPEAItEKLAELEYY-SRVDYFVYSGVT---KDPE-KVDKL----PIAGYKIFP--EDL------E 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564393312 179 LYEIFTCLGELGAIAQVHAEngdiiaqeqarmLEMGITGPEGhvLSRPEELEAEAVFRAITVASqtncpLYVTKVmskSA 258
Cdd:PRK00369 143 REETFRVLLKSRKLKILHPE------------VPLALKSNRK--LRRNCWYEIAALYYVKDYQN-----VHITHA---SN 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564393312 259 ADLISQARKKGnvvFGEPITAS-LGIDG-THYWSKnwakaaafvTSPPLSpDPTTPDYINSLLASGDLQLSGsaHCTFST 336
Cdd:PRK00369 201 PRTVRLAKELG---FTVDITPHhLLVNGeKDCLTK---------VNPPIR-DINERLWLLQALSEVDAIASD--HAPHSS 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564393312 337 AQKaigKDNFTAIPEGTNGVEERMSVIWdKAVATGKMDENQFVAVTSTNAAKIFNLypRKGRIAVGSDSDLVIwdpdaVK 416
Cdd:PRK00369 266 FEK---LQPYEVCPPGIAALSFTPPFIY-TLVSKGILSIDRAVELISTNPARILGI--PYGEIKEGYRANFTV-----IQ 334
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 564393312 417 IVSAKNHQ--SVAEYNIFEGMELRGAPLVVICQGKIMLEDGNLHVTQGAGRF 466
Cdd:PRK00369 335 FEDWRYSTkySKVIETPLDGFELKASVYATIVQGKLAYLEGEVFPVKGINPF 386
|
|
| D-aminoacylase |
cd01297 |
D-aminoacylases (N-acyl-D-Amino acid amidohydrolases) catalyze the hydrolysis of ... |
15-465 |
2.07e-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: 66.17 E-value: 2.07e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564393312 15 LLIKGGRIVndDQS----FYADIYMEDGLIKQIGDNLIVPGgVKTIEANGKMVMPGGIDVHTHfqmpYKGMTTVDDFFqg 90
Cdd:cd01297 2 LVIRNGTVV--DGTgappFTADVGIRDGRIAAIGPILSTSA-REVIDAAGLVVAPGFIDVHTH----YDGQVFWDPDL-- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564393312 91 TKAALAGGTTMIIDH-------VVPEPESSLTEAYEKWREWADGK-----SCCDYALHVD------------------IT 140
Cdd:cd01297 73 RPSSRQGVTTVVLGNcgvspapANPDDLARLIMLMEGLVALGEGLpwgwaTFAEYLDALEarppavnvaalvghaalrRA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564393312 141 HWNDSVKQ----EVQNLSK--EKGVNS----FMVYMAYKDLYQVSNTELYEIFTCLGELGAIAQVHAEN-GDIIAQEQAR 209
Cdd:cd01297 153 VMGLDAREateeELAKMREllREALEAgalgISTGLAYAPRLYAGTAELVALARVAARYGGVYQTHVRYeGDSILEALDE 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564393312 210 MLEMGitgpeghvlsrpEELEAEAVFRAITVASQTNCPLYvtkvmsKSAADLISQARKKGNVVFGE--PITASLGidgth 287
Cdd:cd01297 233 LLRLG------------RETGRPVHISHLKSAGAPNWGKI------DRLLALIEAARAEGLQVTADvyPYGAGSE----- 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564393312 288 ywsknwAKAAAFVTSPPlspdpttpdyinsLLASGDLQLSGSAH----CTFStaqKAIGKdnftaipegtnGVEERMSVI 363
Cdd:cd01297 290 ------DDVRRIMAHPV-------------VMGGSDGGALGKPHprsyGDFT---RVLGH-----------YVRERKLLS 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564393312 364 WDKAVAtgKMdenqfvavtSTNAAKIFNLYPRkGRIAVGSDSDLVIWDPDAVKIVS---AKNHQSvaeynifEGMELrga 440
Cdd:cd01297 337 LEEAVR--KM---------TGLPARVFGLADR-GRIAPGYRADIVVFDPDTLADRAtftRPNQPA-------EGIEA--- 394
|
490 500
....*....|....*....|....*
gi 564393312 441 plvVICQGKIMLEDGnLHVTQGAGR 465
Cdd:cd01297 395 ---VLVNGVPVVRDG-AFTGARPGR 415
|
|
| CAD_DHOase |
cd01316 |
The eukaryotic CAD protein is a trifunctional enzyme of carbamoylphosphate ... |
64-464 |
3.80e-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: 3.80e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564393312 64 MPGGIDVHTHFQMPykGMTTVDDFFQGTKAALAGGTTMIidHVVPEPESSL--TEAYEKWREWADGKSCCDYALHVDITH 141
Cdd:cd01316 5 LPGLIDVHVHLREP--GATHKEDFASGTKAALAGGFTMV--RAMPNTNPSIvdVASLKLVQSLAQAKARCDYAFSIGATS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564393312 142 WNDSvkqEVQNLSKEKGVNSFMVYMAYKDLYQVSNTELYEIFTCLGELGAIAqVHAENGDIIAqeqarmlemgitgpegh 221
Cdd:cd01316 81 TNAA---TVGELASEAVGLKFYLNETFSTLILDKITAWASHFNAWPSTKPIV-THAKSQTLAA----------------- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564393312 222 vlsrpeeleaeavfrAITVASQTNCPLYVTKVMSKSAADLISQARKKGNVVFGEPITASLGI---DGTHYWSknwakaaa 298
Cdd:cd01316 140 ---------------VLLLASLHNRSIHICHVSSKEEINLIRLAKARGLKVTCEVSPHHLFLsqdDLPRGQY-------- 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564393312 299 fvtspPLSPDPTTPDYINSL---LASGDLQLSGSAHCTFstAQKAIGKdnftaIPEGTNGVEERMSVIWdKAVATGKMDE 375
Cdd:cd01316 197 -----EVRPFLPTREDQEALwenLDYIDCFATDHAPHTL--AEKTGNK-----PPPGFPGVETSLPLLL-TAVHEGRLTI 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564393312 376 NQFVAVTSTNAAKIFNLYPRkgriavgSDSDLVIwDPDAVKIVSAKNHQSVAEYNIFEGMELRGAPLVVICQGKIMLEDG 455
Cdd:cd01316 264 EDIVDRLHTNPKRIFNLPPQ-------SDTYVEV-DLDEEWTIPKNPLQSKKGWTPFEGKKVKGKVQRVVLRGETAFIDG 335
|
....*....
gi 564393312 456 NLHVTQGAG 464
Cdd:cd01316 336 EIVAPPGFG 344
|
|
| COG3653 |
COG3653 |
N-acyl-D-aspartate/D-glutamate deacylase [Secondary metabolites biosynthesis, transport and ... |
15-73 |
3.06e-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: 3.06e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 564393312 15 LLIKGGRIVN--DDQSFYADIYMEDGLIKQIGDnLIVPGGVKTIEANGKMVMPGGIDVHTH 73
Cdd:COG3653 4 LLIRGGTVVDgtGAPPFRADVAIKGGRIVAVGD-LAAAEAARVIDATGLVVAPGFIDIHTH 63
|
|
| SsnA |
COG0402 |
Cytosine/adenosine deaminase or related metal-dependent hydrolase [Nucleotide transport and ... |
14-120 |
8.67e-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: 8.67e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564393312 14 RLLIKGGRIV--NDDQSFYAD--IYMEDGLIKQIGDNLIVP---GGVKTIEANGKMVMPGGIDVHTH-FQMPYKGMT--- 82
Cdd:COG0402 1 DLLIRGAWVLtmDPAGGVLEDgaVLVEDGRIAAVGPGAELParyPAAEVIDAGGKLVLPGLVNTHTHlPQTLLRGLAddl 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 564393312 83 -----------------TVDDFFQGTKAA----LAGGTTMIIDH--VVPEPESSLTEAYEK 120
Cdd:COG0402 81 plldwleeyiwplearlDPEDVYAGALLAlaemLRSGTTTVADFyyVHPESADALAEAAAE 141
|
|
| PRK09237 |
PRK09237 |
amidohydrolase/deacetylase family metallohydrolase; |
15-411 |
3.83e-09 |
|
amidohydrolase/deacetylase family metallohydrolase;
Pssm-ID: 236423 [Multi-domain] Cd Length: 380 Bit Score: 58.71 E-value: 3.83e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564393312 15 LLIKGGRIVNDDQSFYA--DIYMEDGLIKQIGDNLIVPGGVKTIEANGKMVMPGGIDVHTHFqmpYKGMTtvDDFFQGTK 92
Cdd:PRK09237 1 LLLRGGRVIDPANGIDGviDIAIEDGKIAAVAGDIDGSQAKKVIDLSGLYVSPGWIDLHVHV---YPGST--PYGDEPDE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564393312 93 AALAGGTTMIIDhvvpepesslteayekwrewADGKSCCDYalhvdithwnDSVKQEVQNLSKEKgvnsfmVYmAYKDLY 172
Cdd:PRK09237 76 VGVRSGVTTVVD--------------------AGSAGADNF----------DDFRKLTIEASKTR------VL-AFLNIS 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564393312 173 QV---SNTELYEIFTClgELGAIAQVHAENGDIIAQEQARMlEMGITGPEGhvlSRPEEleaeavfRAITVASQTNCPLY 249
Cdd:PRK09237 119 RIgllAQDELADLEDI--DADAVAEAVKRNPDFIVGIKARM-SSSVVGDNG---IEPLE-------LAKAIAAEANLPLM 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564393312 250 VTKVMSKSAADLISQARKKGNVVfgepitaslgidgTHYWSKnwaKAAAFVTspplsPDPTTPDYINSLLASGdLQLS-- 327
Cdd:PRK09237 186 VHIGNPPPSLEEILELLRPGDIL-------------THCFNG---KPNRILD-----EDGELRPSVLEALERG-VRLDvg 243
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564393312 328 -GSAHCTFSTAQKAIGKD-NFTAIpeGT--------NGVEERMSVIWDKAVATGkMDENQFVAVTSTNAAKIFNLyPRKG 397
Cdd:PRK09237 244 hGTASFSFKVAEAAIAAGiLPDTI--STdiycrnriNGPVYSLATVMSKFLALG-MPLEEVIAAVTKNAADALRL-PELG 319
|
410
....*....|....
gi 564393312 398 RIAVGSDSDLVIWD 411
Cdd:PRK09237 320 RLQVGSDADLTLFT 333
|
|
| FwdA |
COG1229 |
Formylmethanofuran dehydrogenase subunit A [Energy production and conversion]; |
15-73 |
4.10e-09 |
|
Formylmethanofuran dehydrogenase subunit A [Energy production and conversion];
Pssm-ID: 440842 Cd Length: 554 Bit Score: 59.05 E-value: 4.10e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 564393312 15 LLIKGGRI------VNDDQsfyADIYMEDGlikQIGDNLIVPGGVKTIEANGKMVMPGGIDVHTH 73
Cdd:COG1229 3 LIIKNGRVydpangIDGEV---MDIAIKDG---KIVEEPSDPKDAKVIDASGKVVMAGGVDIHTH 61
|
|
| NagA |
cd00854 |
N-acetylglucosamine-6-phosphate deacetylase, NagA, catalyzes the hydrolysis of the N-acetyl ... |
15-73 |
4.93e-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: 4.93e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 564393312 15 LLIKGGRIVNDDQSFYADIYMEDGLIKQIGDNLIVPGGVKTIEANGKMVMPGGIDVHTH 73
Cdd:cd00854 1 LIIKNARILTPGGLEDGAVLVEDGKIVAIGPEDELEEADEIIDLKGQYLVPGFIDIHIH 59
|
|
| PRK09061 |
PRK09061 |
D-glutamate deacylase; Validated |
5-102 |
6.18e-08 |
|
D-glutamate deacylase; Validated
Pssm-ID: 236369 [Multi-domain] Cd Length: 509 Bit Score: 55.47 E-value: 6.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564393312 5 ARNKVRQSDRLLIKGGRIVNDDQSFYA--DIYMEDGLIKQIGDNLIvpGGVKTIEANGKMVMPGGIDVHTHfqmpykGMT 82
Cdd:PRK09061 11 LMPASMAPYDLVIRNGRVVDPETGLDAvrDVGIKGGKIAAVGTAAI--EGDRTIDATGLVVAPGFIDLHAH------GQS 82
|
90 100
....*....|....*....|
gi 564393312 83 TVDDFFQgtkaALAGGTTMI 102
Cdd:PRK09061 83 VAAYRMQ----AFDGVTTAL 98
|
|
| PRK07228 |
PRK07228 |
5'-deoxyadenosine deaminase; |
14-218 |
6.80e-08 |
|
5'-deoxyadenosine deaminase;
Pssm-ID: 180895 [Multi-domain] Cd Length: 445 Bit Score: 55.01 E-value: 6.80e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564393312 14 RLLIKGGRIVNDDQS---FYADIYMEDGLIKQIGDNLIVPGGVKTIEANGKMVMPGGIDVHTHF-QMPYKGMTtvDDF-- 87
Cdd:PRK07228 2 TILIKNAGIVTMNAKreiVDGDVLIEDDRIAAVGDRLDLEDYDDHIDATGKVVIPGLIQGHIHLcQTLFRGIA--DDLel 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564393312 88 ----------FQGTKAA--------------LAGGTTMIIDHV-VPEPESSLTEAYEKWREWADGKSCCDYALHVDIT-- 140
Cdd:PRK07228 80 ldwlkdriwpLEAAHDAesmyysallgigelIESGTTTIVDMEsVHHTDSAFEAAGESGIRAVLGKVMMDYGDDVPEGlq 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564393312 141 -HWNDSVKQEVQNLSKEKGVNSFMVYMAYKDLYQVSNTElyeifTCLGELGAIAQ-------VHA-EN-GDIIAQEQARM 210
Cdd:PRK07228 160 eDTEASLAESVRLLEKWHGADNGRIRYAFTPRFAVSCTE-----ELLRGVRDLADeygvrihTHAsENrGEIETVEEETG 234
|
250
....*....|....*
gi 564393312 211 L-------EMGITGP 218
Cdd:PRK07228 235 MrnihyldEVGLTGE 249
|
|
| PRK07627 |
PRK07627 |
dihydroorotase; Provisional |
14-454 |
9.84e-08 |
|
dihydroorotase; Provisional
Pssm-ID: 181059 [Multi-domain] Cd Length: 425 Bit Score: 54.30 E-value: 9.84e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564393312 14 RLLIKGGRIVN-----DDQsfyADIYMEDGLIKQIGDnliVPGGV---KTIEANGKMVMPGGIDVHTHFQMP-YKGMTTV 84
Cdd:PRK07627 2 KIHIKGGRLIDpaagtDRQ---ADLYVAAGKIAAIGQ---APAGFnadKTIDASGLIVCPGLVDLSARLREPgYEYKATL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564393312 85 DDFFQgtkAALAGGTTMII-----DHVVPEPEssLTEAyekwrewadgksccdyalhvdithwndsVKQEVQNLSKEK-- 157
Cdd:PRK07627 76 ESEMA---AAVAGGVTSLVcppdtDPVLDEPG--LVEM----------------------------LKFRARNLNQAHvy 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564393312 158 GVNSFMVYMAYKDLyqvsnTELYEiftcLGELGAIAQVHAENGDIIAQEQARMLEMGIT-------------------GP 218
Cdd:PRK07627 123 PLGALTVGLKGEVL-----TEMVE----LTEAGCVGFSQANVPVVDTQVLLRALQYASTfgftvwlrpldaflgrggvAA 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564393312 219 EGHVLSR------PEELEAEAVFRAITVASQTNCPLYVTKVMSKSAADLISQARKKgnvvfGEPITASLGIDGTH----- 287
Cdd:PRK07627 194 SGAVASRlglsgvPVAAETIALHTIFELMRVTGARVHLARLSSAAGVALVRAAKAE-----GLPVTCDVGVNHVHlidvd 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564393312 288 --YWSKNwakaaaFVTSPPLSpDPTTPDYINSLLASGDLQLSGSAHCTFSTAQKAIgkdNFTAIPEGTNGVEERMSVIWD 365
Cdd:PRK07627 269 igYFDSQ------FRLDPPLR-SQRDREAIRAALADGTIDAICSDHTPVDDDEKLL---PFAEATPGATGLELLLPLTLK 338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564393312 366 KAVATgKMDENQFVAVTSTNAAKIFNLypRKGRIAVGSDSDLVIWDPDAVKIVSAKNHQSVAEYNIFEGMELRGAPLVVI 445
Cdd:PRK07627 339 WADEA-KVPLARALARITSAPARVLGL--PAGRLAEGAPADLCVFDPDAHWRVEPRALKSQGKNTPFLGYELPGRVRATL 415
|
....*....
gi 564393312 446 CQGKIMLED 454
Cdd:PRK07627 416 VAGQVAFER 424
|
|
| Met_dep_hydrolase_B |
cd01307 |
Metallo-dependent hydrolases, subgroup B is part of the superfamily of metallo-dependent ... |
32-428 |
1.33e-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: 1.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564393312 32 DIYMEDGLIKQIGDNLIVPGGVKTIEANGKMVMPGGIDVHTHFqmpYKGMTTVDDffQGTKAALAGGTTMIIDhvvpepe 111
Cdd:cd01307 1 DVAIENGKIAAVGAALAAPAATQIVDAGGCYVSPGWIDLHVHV---YQGGTRYGD--RPDMIGVKSGVTTVVD------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564393312 112 sslteayekwrewADGKSCCDYalhvdithwnDSVKQEVQNLSKEKgvnsfmVYmAYKDLY---QVSNTELYEIFTClgE 188
Cdd:cd01307 69 -------------AGSAGADNI----------DGFRYTVIERSATR------VY-AFLNISrvgLVAQDELPDPDNI--D 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564393312 189 LGAIAQVHAENGDIIAQEQARMlEMGITGPEGhvlSRPEELEAEAvfraitvASQTNCPLYvtkVMSKSAADLISQA--- 265
Cdd:cd01307 117 EDAVVAAAREYPDVIVGLKARA-SKSVVGEWG---IKPLELAKKI-------AKEADLPLM---VHIGSPPPILDEVvpl 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564393312 266 RKKGNVVfgepitaslgidgTHYWSknwAKAAAFVTspplsPDPTTPDYINSLLASG---DLQlSGSAHCTFSTAQKAIG 342
Cdd:cd01307 183 LRRGDVL-------------THCFN---GKPNGIVD-----EEGEVLPLVRRARERGvifDVG-HGTASFSFRVARAAIA 240
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564393312 343 KD-NFTAI------PEGTNGVEERMSVIWDKAVATGkMDENQFVAVTSTNAAKIFNLyPRKGRIAVGSDSDLVIWD--PD 413
Cdd:cd01307 241 AGlLPDTIssdihgRNRTNGPVYALATTLSKLLALG-MPLEEVIEAVTANPARMLGL-AEIGTLAVGYDADLTVFDlkDG 318
|
410
....*....|....*
gi 564393312 414 AVKIVSAKNHQSVAE 428
Cdd:cd01307 319 RVELVDSEGDTLIAE 333
|
|
| NagA |
COG1820 |
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism]; |
16-73 |
1.38e-07 |
|
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism];
Pssm-ID: 441425 [Multi-domain] Cd Length: 373 Bit Score: 53.95 E-value: 1.38e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 564393312 16 LIKGGRIVNDDQSFY-ADIYMEDGLIKQIGDNliVPGGVKTIEANGKMVMPGGIDVHTH 73
Cdd:COG1820 1 AITNARIFTGDGVLEdGALLIEDGRIAAIGPG--AEPDAEVIDLGGGYLAPGFIDLHVH 57
|
|
| AdeC |
COG1001 |
Adenine deaminase [Nucleotide transport and metabolism]; |
15-104 |
3.22e-07 |
|
Adenine deaminase [Nucleotide transport and metabolism];
Pssm-ID: 440625 [Multi-domain] Cd Length: 559 Bit Score: 53.18 E-value: 3.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564393312 15 LLIKGGRIVN--DDQSFYADIYMEDGLIKQIGDnlIVPGGVKTIEANGKMVMPGGIDVHTHFQmpyKGMTTVDDFfqgTK 92
Cdd:COG1001 7 LVIKNGRLVNvfTGEILEGDIAIAGGRIAGVGD--YIGEATEVIDAAGRYLVPGFIDGHVHIE---SSMVTPAEF---AR 78
|
90
....*....|...
gi 564393312 93 AALAGGTT-MIID 104
Cdd:COG1001 79 AVLPHGTTtVIAD 91
|
|
| metallo-dependent_hydrolases |
cd01292 |
Superfamily of metallo-dependent hydrolases (also called amidohydrolase superfamily) is a ... |
68-274 |
3.57e-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: 3.57e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564393312 68 IDVHTHFQMP----------------YKGMTTVDDFFQGTKAALAGGTTMIIDHVVPEPESSLTEAYEKWREWADGKSCC 131
Cdd:cd01292 2 IDTHVHLDGSalrgtrlnlelkeaeeLSPEDLYEDTLRALEALLAGGVTTVVDMGSTPPPTTTKAAIEAVAEAARASAGI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564393312 132 DYALHVDITH--------WNDSVKQEVQnLSKEKGVNSFMVYMAYKDlYQVSNTELYEIFTCLGELGAIAQVHAENGDII 203
Cdd:cd01292 82 RVVLGLGIPGvpaavdedAEALLLELLR-RGLELGAVGLKLAGPYTA-TGLSDESLRRVLEEARKLGLPVVIHAGELPDP 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 564393312 204 AQEQARMLEMGITGPE---GHVLSRPEELEAEAVFRAITVASqTNCPLYVTKVMSKSAADLISQARKKGNVVFG 274
Cdd:cd01292 160 TRALEDLVALLRLGGRvviGHVSHLDPELLELLKEAGVSLEV-CPLSNYLLGRDGEGAEALRRLLELGIRVTLG 232
|
|
| PRK08204 |
PRK08204 |
hypothetical protein; Provisional |
13-111 |
4.84e-07 |
|
hypothetical protein; Provisional
Pssm-ID: 181288 [Multi-domain] Cd Length: 449 Bit Score: 52.31 E-value: 4.84e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564393312 13 DRLLIKGGRIVNDDQSF----YADIYMEDGLIKQIGDNlIVPGGVKTIEANGKMVMPGGIDVHTH--------------- 73
Cdd:PRK08204 2 KRTLIRGGTVLTMDPAIgdlpRGDILIEGDRIAAVAPS-IEAPDAEVVDARGMIVMPGLVDTHRHtwqsvlrgigadwtl 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 564393312 74 ---FQMPYKGMTTV---DDFFQGTKA----ALAGGTTMIID--HVVPEPE 111
Cdd:PRK08204 81 qtyFREIHGNLGPMfrpEDVYIANLLgaleALDAGVTTLLDwsHINNSPE 130
|
|
| Amidohydro_3 |
pfam07969 |
Amidohydrolase family; |
379-434 |
1.09e-06 |
|
Amidohydrolase family;
Pssm-ID: 400360 [Multi-domain] Cd Length: 464 Bit Score: 51.38 E-value: 1.09e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 564393312 379 VAVTSTNAAKIFNLYPRKGRIAVGSDSDLVIWDPDAVKIVSAKNHQSVAEYNIFEG 434
Cdd:pfam07969 405 LALYTSGPAKALGLEDRKGTLGVGKDADLVVLDDDPLTVDPPAIADIRVRLTVVDG 460
|
|
| FMDH_A |
cd01304 |
Formylmethanofuran dehydrogenase (FMDH) subunit A; Methanogenic bacteria and archea derive ... |
17-73 |
2.00e-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: 2.00e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 564393312 17 IKGGRIVNDDQSFYA---DIYMEDGlikQIGDNLIVPGGVKTIEANGKMVMPGGIDVHTH 73
Cdd:cd01304 1 IKNGTVYDPLNGINGekmDIFIRDG---KIVESSSGAKPAKVIDASGKVVMAGGVDMHSH 57
|
|
| PRK07369 |
PRK07369 |
dihydroorotase; Provisional |
31-439 |
2.07e-06 |
|
dihydroorotase; Provisional
Pssm-ID: 236002 [Multi-domain] Cd Length: 418 Bit Score: 50.37 E-value: 2.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564393312 31 ADIYMEDGLIKQIGDNLI-VPGGVKTIEANGKMVMPGGIDVHTHFQMPykGMTTVDDFFQGTKAALAGGTTMI------- 102
Cdd:PRK07369 22 ADVLIEDGKIQAIEPHIDpIPPDTQIIDASGLILGPGLVDLYSHSGEP--GFEERETLASLAAAAAAGGFTRVailpdtf 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564393312 103 --IDHvvPEPESSL-----TEAYEKWREWADgksccdyalhvdITHwNDSVKQ--EVQNLSkEKGVNSFMVYMAYKDLYQ 173
Cdd:PRK07369 100 ppLDN--PATLARLqqqaqQIPPVQLHFWGA------------LTL-GGQGKQltELAELA-AAGVVGFTDGQPLENLAL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564393312 174 VSNTELYeiftcLGELGAIAQVHAEN----GDIIAQEQARMLEMGITGpeghvlsRPEELEAEAVFRAITVASQTNCPLY 249
Cdd:PRK07369 164 LRRLLEY-----LKPLGKPVALWPCDrslaGNGVMREGLLALRLGLPG-------DPASAETTALAALLELVAAIGTPVH 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564393312 250 VTKVMSKSAADLISQARKKGnvvfgEPITASlgidgTHYWSKNWAKAAAFVTSPPLSPDPT--TPDYINSLLA---SGDL 324
Cdd:PRK07369 232 LMRISTARSVELIAQAKARG-----LPITAS-----TTWMHLLLDTEALASYDPNLRLDPPlgNPSDRQALIEgvrTGVI 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564393312 325 QLSGSAHCTFSTAQKAIGkdnFTAIPEGTNGVEERMSVIWDKAVATGKMDENQFVAVTSTNAAKIFNLYPRkgRIAVGSD 404
Cdd:PRK07369 302 DAIAIDHAPYTYEEKTVA---FAEAPPGAIGLELALPLLWQNLVETGELSALQLWQALSTNPARCLGQEPP--SLAPGQP 376
|
410 420 430
....*....|....*....|....*....|....*
gi 564393312 405 SDLVIWDPDAVKIVSAKNHQSVAEYNIFEGMELRG 439
Cdd:PRK07369 377 AELILFDPQKTWTVSAQTLHSLSRNTPWLGQTLKG 411
|
|
| Urease_alpha |
cd00375 |
Urease alpha-subunit; Urease is a nickel-dependent metalloenzyme that catalyzes the hydrolysis ... |
31-103 |
3.87e-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: 3.87e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564393312 31 ADIYMEDGLIKQIG------------DNLIVPGGVKTIEANGKMVMPGGIDVHTHFQMPykgmttvddffQGTKAALAGG 98
Cdd:cd00375 83 ADIGIKDGRIVAIGkagnpdimdgvtPNMIVGPSTEVIAGEGKIVTAGGIDTHVHFICP-----------QQIEEALASG 151
|
....*
gi 564393312 99 TTMII 103
Cdd:cd00375 152 ITTMI 156
|
|
| YtcJ |
COG1574 |
Predicted amidohydrolase YtcJ [General function prediction only]; |
15-74 |
4.38e-06 |
|
Predicted amidohydrolase YtcJ [General function prediction only];
Pssm-ID: 441182 [Multi-domain] Cd Length: 535 Bit Score: 49.41 E-value: 4.38e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 564393312 15 LLIKGGRI--VNDDQSFYADIYMEDGLIKQIGDN----LIVPGGVKTIEANGKMVMPGGIDVHTHF 74
Cdd:COG1574 10 LLLTNGRIytMDPAQPVAEAVAVRDGRIVAVGSDaevrALAGPATEVIDLGGKTVLPGFIDAHVHL 75
|
|
| NagA |
COG1820 |
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism]; |
379-413 |
4.92e-06 |
|
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism];
Pssm-ID: 441425 [Multi-domain] Cd Length: 373 Bit Score: 48.94 E-value: 4.92e-06
10 20 30
....*....|....*....|....*....|....*
gi 564393312 379 VAVTSTNAAKIFNLYPRKGRIAVGSDSDLVIWDPD 413
Cdd:COG1820 328 VRMASLNPARALGLDDRKGSIAPGKDADLVVLDDD 362
|
|
| PRK06380 |
PRK06380 |
metal-dependent hydrolase; Provisional |
15-91 |
5.26e-06 |
|
metal-dependent hydrolase; Provisional
Pssm-ID: 180548 [Multi-domain] Cd Length: 418 Bit Score: 49.11 E-value: 5.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564393312 15 LLIKGGRIVNDDQS---FYADIYMEDGLIKQIGDnlIVPGGVKTIEANGKMVMPGGIDVHTHFQMP-YKGM---TTVDDF 87
Cdd:PRK06380 3 ILIKNAWIVTQNEKreiLQGNVYIEGNKIVYVGD--VNEEADYIIDATGKVVMPGLINTHAHVGMTaSKGLfddVDLEEF 80
|
....
gi 564393312 88 FQGT 91
Cdd:PRK06380 81 LMKT 84
|
|
| PRK07203 |
PRK07203 |
putative aminohydrolase SsnA; |
15-74 |
5.32e-06 |
|
putative aminohydrolase SsnA;
Pssm-ID: 235963 [Multi-domain] Cd Length: 442 Bit Score: 49.16 E-value: 5.32e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 564393312 15 LLIKGGRIV-NDDQSFY---ADIYMEDGLIKQIGDNlivpGGVKT-------IEANGKMVMPGGIDVHTHF 74
Cdd:PRK07203 2 LLIGNGTAItRDPAKPViedGAIAIEGNVIVEIGTT----DELKAkypdaefIDAKGKLIMPGLINSHNHI 68
|
|
| Bact_CD |
cd01293 |
Bacterial cytosine deaminase and related metal-dependent hydrolases. Cytosine deaminases (CDs) ... |
31-126 |
6.08e-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: 48.78 E-value: 6.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564393312 31 ADIYMEDGLIKQIGDNLIVPGGVKTIEANGKMVMPGGIDVHTH------FQMP-----------------YKGMTTVDDF 87
Cdd:cd01293 15 VDIAIEDGRIAAIGPALAVPPDAEEVDAKGRLVLPAFVDPHIHldktftGGRWpnnsggtlleaiiaweeRKLLLTAEDV 94
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 564393312 88 FQ----GTKAALAGGTTMIIDHVVPEPESSLT------EAYEKWREWAD 126
Cdd:cd01293 95 KEraerALELAIAHGTTAIRTHVDVDPAAGLKaleallELREEWADLID 143
|
|
| PRK15446 |
PRK15446 |
phosphonate metabolism protein PhnM; Provisional |
14-72 |
7.16e-06 |
|
phosphonate metabolism protein PhnM; Provisional
Pssm-ID: 237967 [Multi-domain] Cd Length: 383 Bit Score: 48.64 E-value: 7.16e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 564393312 14 RLLIKGGRIVNDDQSFYADIYMEDGLIKQIGDNLIVPGGvkTIEANGKMVMPGGIDVHT 72
Cdd:PRK15446 3 EMILSNARLVLPDEVVDGSLLIEDGRIAAIDPGASALPG--AIDAEGDYLLPGLVDLHT 59
|
|
| ureC |
PRK13308 |
urease subunit alpha; Reviewed |
31-102 |
1.02e-05 |
|
urease subunit alpha; Reviewed
Pssm-ID: 183965 [Multi-domain] Cd Length: 569 Bit Score: 48.16 E-value: 1.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564393312 31 ADIYMEDGLIKQIG------------DNLIVPGGVKTIEANGKMVMPGGIDVHTHFQMPykgmttvddffQGTKAALAGG 98
Cdd:PRK13308 87 GDIGIRDGRIVGIGkagnpdimdgvdPRLVVGPGTDVRPAEGLIATPGAIDVHVHFDSA-----------QLVDHALASG 155
|
....*
gi 564393312 99 -TTMI 102
Cdd:PRK13308 156 iTTML 160
|
|
| PRK08393 |
PRK08393 |
N-ethylammeline chlorohydrolase; Provisional |
15-76 |
4.04e-05 |
|
N-ethylammeline chlorohydrolase; Provisional
Pssm-ID: 181411 [Multi-domain] Cd Length: 424 Bit Score: 46.33 E-value: 4.04e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 564393312 15 LLIKGGRIVNDD--QSFYADIYMEDGLIKQIGDNLIVPGGvKTIEANGKMVMPGGIDVHTHFQM 76
Cdd:PRK08393 3 ILIKNGYVIYGEnlKVIRADVLIEGNKIVEVKRNINKPAD-TVIDASGSVVSPGFINAHTHSPM 65
|
|
| Met_dep_hydrolase_C |
cd01309 |
Metallo-dependent hydrolases, subgroup C is part of the superfamily of metallo-dependent ... |
37-73 |
7.77e-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: 7.77e-05
10 20 30
....*....|....*....|....*....|....*..
gi 564393312 37 DGLIKQIGDNLIVPGGVKTIEANGKMVMPGGIDVHTH 73
Cdd:cd01309 1 DGKIVAVGAEITTPADAEVIDAKGKHVTPGLIDAHSH 37
|
|
| ureC |
PRK13206 |
urease subunit alpha; Reviewed |
31-103 |
1.13e-04 |
|
urease subunit alpha; Reviewed
Pssm-ID: 237304 [Multi-domain] Cd Length: 573 Bit Score: 45.09 E-value: 1.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564393312 31 ADIYMEDGLIKQIG------------DNLIVPGGVKTIEANGKMVMPGGIDVHTHFQMPykgmttvddffQGTKAALAGG 98
Cdd:PRK13206 89 ADVGIRDGRIVAIGkagnpdimdgvhPDLVIGPSTEIIAGNGRILTAGAIDCHVHFICP-----------QIVDEALAAG 157
|
....*
gi 564393312 99 TTMII 103
Cdd:PRK13206 158 ITTLI 162
|
|
| ureC |
PRK13207 |
urease subunit alpha; Reviewed |
31-102 |
1.53e-04 |
|
urease subunit alpha; Reviewed
Pssm-ID: 237305 [Multi-domain] Cd Length: 568 Bit Score: 44.40 E-value: 1.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564393312 31 ADIYMEDGLIKQIG--------DN--LIVPGGVKTIEANGKMVMPGGIDVHTHFQMPykgmttvddffQGTKAALAGG-T 99
Cdd:PRK13207 85 ADIGIKDGRIVAIGkagnpdiqDGvdIIIGPGTEVIAGEGLIVTAGGIDTHIHFICP-----------QQIEEALASGvT 153
|
...
gi 564393312 100 TMI 102
Cdd:PRK13207 154 TMI 156
|
|
| Imidazolone-5PH |
cd01296 |
Imidazolonepropionase/imidazolone-5-propionate hydrolase (Imidazolone-5PH) catalyzes the third ... |
33-74 |
1.84e-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: 43.79 E-value: 1.84e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 564393312 33 IYMEDGLIKQIGD----NLIVPGGVKTIEANGKMVMPGGIDVHTHF 74
Cdd:cd01296 1 IAIRDGRIAAVGPaaslPAPGPAAAEEIDAGGRAVTPGLVDCHTHL 46
|
|
| ureB |
PRK13985 |
urease subunit alpha; |
17-99 |
2.03e-04 |
|
urease subunit alpha;
Pssm-ID: 184438 [Multi-domain] Cd Length: 568 Bit Score: 44.12 E-value: 2.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564393312 17 IKGGRIVNDDQSFYADiyMEDGlikqIGDNLIVPGGVKTIEANGKMVMPGGIDVHTHFQMPYKGMTTvddFFQGTKAALA 96
Cdd:PRK13985 87 IKDGKIAGIGKGGNKD--MQDG----VKNNLSVGPATEALAGEGLIVTAGGIDTHIHFISPQQIPTA---FASGVTTMIG 157
|
...
gi 564393312 97 GGT 99
Cdd:PRK13985 158 GGT 160
|
|
| PRK05985 |
PRK05985 |
cytosine deaminase; Provisional |
31-126 |
6.24e-04 |
|
cytosine deaminase; Provisional
Pssm-ID: 180337 [Multi-domain] Cd Length: 391 Bit Score: 42.23 E-value: 6.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564393312 31 ADIYMEDGLIKQIGDNLIVPGGVKTIEANGKMVMPGGIDVHTHFQMPYKGM--------TTVDDFFQGTK---------- 92
Cdd:PRK05985 17 VDILIRDGRIAAIGPALAAPPGAEVEDGGGALALPGLVDGHIHLDKTFWGDpwypnepgPSLRERIANERrrraasghpa 96
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 564393312 93 ---------AALAGGTTMIIDHVVPEPESSLT------EAYEKWREWAD 126
Cdd:PRK05985 97 aeralalarAAAAAGTTAMRSHVDVDPDAGLRhleavlAARETLRGLID 145
|
|
| PRK09059 |
PRK09059 |
dihydroorotase; Validated |
15-103 |
7.51e-04 |
|
dihydroorotase; Validated
Pssm-ID: 181631 [Multi-domain] Cd Length: 429 Bit Score: 42.33 E-value: 7.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564393312 15 LLIKGGRIVNDDQSF--YADIYMEDGLIKQIGD---NLIVPGGVKTIEANGKMVMPGGIDVHTHFQMPykGMTTVDDFFQ 89
Cdd:PRK09059 5 ILLANARIIDPSRGLdeIGTVLIEDGVIVAAGKgagNQGAPEGAEIVDCAGKAVAPGLVDARVFVGEP--GAEHRETIAS 82
|
90
....*....|....
gi 564393312 90 GTKAALAGGTTMII 103
Cdd:PRK09059 83 ASRAAAAGGVTSII 96
|
|
| PRK07583 |
PRK07583 |
cytosine deaminase; |
31-73 |
1.66e-03 |
|
cytosine deaminase;
Pssm-ID: 236062 Cd Length: 438 Bit Score: 41.12 E-value: 1.66e-03
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 564393312 31 ADIYMEDGLIKQIGDNLIVPGGVKTIEANGKMVMPGGIDVHTH 73
Cdd:PRK07583 41 VDIEIADGKIAAILPAGGAPDELPAVDLKGRMVWPCFVDMHTH 83
|
|
| Isoaspartyl-dipeptidase |
cd01308 |
Isoaspartyl dipeptidase hydrolyzes the beta-L-isoaspartyl linkages in dipeptides, as part of ... |
381-460 |
1.75e-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: 1.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564393312 381 VTSTNAAKIFNLYPrKGRIAVGSDSDLVIWDPDavkivsaknhqsvaeYNIFEgmelrgaplvVICQGKIMLEDGNLHVT 460
Cdd:cd01308 330 VITSNVARILKLRK-KGEIQPGFDADLVILDKD---------------LDINS----------VIAKGQIMVRNGKLLVK 383
|
|
| PRK06038 |
PRK06038 |
N-ethylammeline chlorohydrolase; Provisional |
15-87 |
2.37e-03 |
|
N-ethylammeline chlorohydrolase; Provisional
Pssm-ID: 180363 [Multi-domain] Cd Length: 430 Bit Score: 40.50 E-value: 2.37e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 564393312 15 LLIKGGRIVNDDQSFY--ADIYMEDGLIKQIGDNliVPGGVKT-IEANGKMVMPGGIDVHTHFQMP-YKGMTtvDDF 87
Cdd:PRK06038 4 IIIKNAYVLTMDAGDLkkGSVVIEDGTITEVSES--TPGDADTvIDAKGSVVMPGLVNTHTHAAMTlFRGYA--DDL 76
|
|
| YtcJ_like |
cd01300 |
YtcJ_like metal dependent amidohydrolases. YtcJ is a Bacillus subtilis ORF of unknown function. ... |
32-74 |
3.58e-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: 3.58e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 564393312 32 DIYMEDGLIKQIGDN----LIVPGGVKTIEANGKMVMPGGIDVHTHF 74
Cdd:cd01300 1 AVAVRDGRIVAVGSDaeakALKGPATEVIDLKGKTVLPGFIDSHSHL 47
|
|
| PRK08203 |
PRK08203 |
hydroxydechloroatrazine ethylaminohydrolase; Reviewed |
14-74 |
3.70e-03 |
|
hydroxydechloroatrazine ethylaminohydrolase; Reviewed
Pssm-ID: 236184 [Multi-domain] Cd Length: 451 Bit Score: 39.84 E-value: 3.70e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 564393312 14 RLLIKGGRIV---NDDQSFYAD--IYMEDGLIKQIGDNLIVPG-GVKTIEANGKMVMPGGIDVHTHF 74
Cdd:PRK08203 2 TLWIKNPLAIvtmDAARREIADggLVVEGGRIVEVGPGGALPQpADEVFDARGHVVTPGLVNTHHHF 68
|
|
| Imidazolone-5PH |
cd01296 |
Imidazolonepropionase/imidazolone-5-propionate hydrolase (Imidazolone-5PH) catalyzes the third ... |
367-411 |
7.95e-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: 7.95e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 564393312 367 AVATGKMDENQFVAVTSTNAAKIFNLYPRKGRIAVGSDSDLVIWD 411
Cdd:cd01296 304 ACRLMRMTPEEALTAATINAAAALGLGETVGSLEVGKQADLVILD 348
|
|
| PLN02303 |
PLN02303 |
urease |
29-102 |
9.83e-03 |
|
urease
Pssm-ID: 215172 [Multi-domain] Cd Length: 837 Bit Score: 38.96 E-value: 9.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564393312 29 FYADIYMEDGLIKQIG------------DNLIVpgGVKT--IEANGKMVMPGGIDVHTHFQMPYkgmttvddffQGTKAA 94
Cdd:PLN02303 350 YKADIGIKDGLIVGIGkagnpdvmdgvtSNMIV--GVNTevIAGEGMIVTAGGIDCHVHFICPQ----------LATEAI 417
|
....*...
gi 564393312 95 LAGGTTMI 102
Cdd:PLN02303 418 ASGITTLV 425
|
|
| |
