|
Name |
Accession |
Description |
Interval |
E-value |
| D-HYD |
cd01314 |
D-hydantoinases (D-HYD) also called dihydropyrimidases (DHPase) and related proteins; DHPases ... |
17-466 |
0e+00 |
|
D-hydantoinases (D-HYD) also called dihydropyrimidases (DHPase) and related proteins; DHPases are a family of enzymes that catalyze the reversible hydrolytic ring opening of the amide bond in five- or six-membered cyclic diamides, like dihydropyrimidine or hydantoin. The hydrolysis of dihydropyrimidines is the second step of reductive catabolism of pyrimidines in human. The hydrolysis of 5-substituted hydantoins in microorganisms leads to enantiomerically pure N-carbamyl amino acids, which are used for the production of antibiotics, peptide hormones, pyrethroids, and pesticides. HYDs are classified depending on their stereoselectivity. This family also includes collapsin response regulators (CRMPs), cytosolic proteins involved in neuronal differentiation and axonal guidance which have strong homology to DHPases, but lack most of the active site residues.
Pssm-ID: 238639 [Multi-domain] Cd Length: 447 Bit Score: 720.16 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472750 17 LLIKGGRIVNDDQSFYADIYMEDGVIKQIGDNLIVPGGVKTIEANGKMVIPGGIDIHTHLQMPFRGTTTADDFTQGTKAA 96
Cdd:cd01314 1 LIIKNGTIVTADGSFKADILIEDGKIVAIGPNLEAPGGVEVIDATGKYVLPGGIDPHTHLELPFMGTVTADDFESGTRAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472750 97 LAGGTTMIVDHVIPEPGCSLLEAFDRWSKWADEKACCDYSLHVDITHWNDSVKQEVETLIKeKGVNSFQVYMAFKDLYQM 176
Cdd:cd01314 81 AAGGTTTIIDFAIPNKGQSLLEAVEKWRGKADGKSVIDYGFHMIITDWTDSVIEELPELVK-KGISSFKVFMAYKGLLMV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472750 177 SNTELYEVFTFLGEHGGIAQVHAENGEIIAEEQARMLEMGITGPEGHVLSRPEELEAEAVFRAVTIASQTNCPLYVTRVM 256
Cdd:cd01314 160 DDEELLDVLKRAKELGALVMVHAENGDVIAELQKKLLAQGKTGPEYHALSRPPEVEAEATARAIRLAELAGAPLYIVHVS 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472750 257 SKSAADIISQARKKGNVVFGEPITASLGTDGTHYWsKNWAKAASFVTSPPLSPDpTTPDYLNTLLASGDLSVVGSAHCTF 336
Cdd:cd01314 240 SKEAADEIARARKKGLPVYGETCPQYLLLDDSDYW-KDWFEGAKYVCSPPLRPK-EDQEALWDGLSSGTLQTVGSDHCPF 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472750 337 SVAQKAIGKDDFTQIPEGVNGAEERMSIIWDKAVVTGKMDENMFVAVTSTNAAKILNLYPRKGRIAVGSDSDLVIWDTDA 416
Cdd:cd01314 318 NFAQKARGKDDFTKIPNGVPGVETRMPLLWSEGVAKGRITLEKFVELTSTNPAKIFGLYPRKGTIAVGSDADLVIWDPNA 397
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 66472750 417 VRTITAKTHHSAAEYNVFEGMELRGAPMLVVCQGKIVLEDGNLHATSGTG 466
Cdd:cd01314 398 EKTISADTHHHNVDYNIFEGMKVKGWPVVTISRGKVVVEDGELVGEKGSG 447
|
|
| D-hydantoinase |
TIGR02033 |
D-hydantoinase; This model represents the D-hydantoinase (dihydropyrimidinase) which primarily ... |
17-471 |
0e+00 |
|
D-hydantoinase; This model represents the D-hydantoinase (dihydropyrimidinase) which primarily converts 5,6-dihydrouracil to 3-ureidopropanoate but also acts on dihydrothymine and hydantoin. The enzyme is a metalloenzyme.
Pssm-ID: 273937 [Multi-domain] Cd Length: 454 Bit Score: 703.76 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472750 17 LLIKGGRIVNDDQSFYADIYMEDGVIKQIGDNLIVPGGVKTIEANGKMVIPGGIDIHTHLQMPFRGTTTADDFTQGTKAA 96
Cdd:TIGR02033 1 LLIKGGTVVNADDVFQADVLIEGGKIVAVGDNLIPPDAVEVIDATGKYVLPGGIDVHTHLEMPFGGTTTADDFFTGTKAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472750 97 LAGGTTMIVDHVIPEPGCSLLEAFDRWSKWADEKACCDYSLHVDITHWNDSVKQEVETLIKEKGVNSFQVYMAFKDLYQM 176
Cdd:TIGR02033 81 AAGGTTTIIDFVVPEKGSSLTEALETWHEKAEGKSVIDYGFHMDITHWNDSVLEEHIPEVKEEGINSFKVFMAYKNLLMV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472750 177 SNTELYEVFTFLGEHGGIAQVHAENGEIIAEEQARMLEMGITGPEGHVLSRPEELEAEAVFRAVTIASQTNCPLYVTRVM 256
Cdd:TIGR02033 161 DDEELFEILKRLKELGALLQVHAENGDIIAELQARMLAQGITGPEYHALSRPPELEAEAVARAITLAALADAPLYVVHVS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472750 257 SKSAADIISQARKKGNVVFGEPITASLGTDGTHYWsKNWAKAASFVTSPPLSpDPTTPDYLNTLLASGDLSVVGSAHCTF 336
Cdd:TIGR02033 241 TKDAADEIAQARKKGQPVFGETCPQYLVLDDTHYD-KPGFEGAKYVCSPPLR-EPEDQDALWSALSSGALQTVGSDHCTF 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472750 337 SVAQK-AIGKDDFTQIPEGVNGAEERMSIIWDKAVVTGKMDENMFVAVTSTNAAKILNLYPRKGRIAVGSDSDLVIWDTD 415
Cdd:TIGR02033 319 NFAQKkAIGKDDFTKIPNGGPGVEERMSLLFDEGVAKGRITLEKFVEVTSTNPAKIFNLYPRKGTIAVGSDADIVIWDPN 398
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 66472750 416 AVRTITAKTHHSAAEYNVFEGMELRGAPMLVVCQGKIVLEDGNLHATSGTGRFIPC 471
Cdd:TIGR02033 399 RTTVISAETHHSNADYNPFEGFKVRGAPVSVLSRGRVVVEDGQLVGTAGAGRFVKR 454
|
|
| PRK08323 |
PRK08323 |
phenylhydantoinase; Validated |
16-475 |
0e+00 |
|
phenylhydantoinase; Validated
Pssm-ID: 236240 [Multi-domain] Cd Length: 459 Bit Score: 577.89 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472750 16 RLLIKGGRIVNDDQSFYADIYMEDGVIKQIGDNlivpGGVKTIEANGKMVIPGGIDIHTHLQMPFRGTTTADDFTQGTKA 95
Cdd:PRK08323 2 STLIKNGTVVTADDTYKADVLIEDGKIAAIGAN----LGDEVIDATGKYVMPGGIDPHTHMEMPFGGTVSSDDFETGTRA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472750 96 ALAGGTTMIVDHVIPEPGCSLLEAFDRWSKWADEKACCDYSLHVDITHWNDSVKQEVETLIKEkGVNSFQVYMAFKDLYQ 175
Cdd:PRK08323 78 AACGGTTTIIDFALQPKGQSLREALEAWHGKAAGKAVIDYGFHMIITDWNEVVLDEMPELVEE-GITSFKLFMAYKGALM 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472750 176 MSNTELYEVFTFLGEHGGIAQVHAENGEIIAEEQARMLEMGITGPEGHVLSRPEELEAEAVFRAVTIASQTNCPLYVTRV 255
Cdd:PRK08323 157 LDDDELLRALQRAAELGALPMVHAENGDAIAYLQAKLLAEGKTGPEYHALSRPPEVEGEATNRAIMLAELAGAPLYIVHV 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472750 256 MSKSAADIISQARKKGNVVFGEPITASLGTDGTHYWSKNWAKAASFVTSPPLSPdPTTPDYLNTLLASGDLSVVGSAHCT 335
Cdd:PRK08323 237 SCKEALEAIRRARARGQRVFGETCPQYLLLDESEYDGPDWFEGAKYVMSPPLRD-KEHQDALWRGLQDGDLQVVATDHCP 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472750 336 FSVAQKA-IGKDDFTQIPEGVNGAEERMSIIWDKAVVTGKMDENMFVAVTSTNAAKILNLYPRKGRIAVGSDSDLVIWDT 414
Cdd:PRK08323 316 FCFEQKKqLGRGDFTKIPNGTPGVEDRMPLLFSEGVMTGRITLNRFVELTSTNPAKIFGLYPRKGTIAVGADADIVIWDP 395
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 66472750 415 DAVRTITAKTHHSAAEYNVFEGMELRGAPMLVVCQGKIVLEDGNLHATSGTGRFIPCSPFP 475
Cdd:PRK08323 396 NATKTISASTLHSNVDYNPYEGFEVTGWPVTTLSRGEVVVEDGEFRGKAGHGRFLKRKPFQ 456
|
|
| PLN02942 |
PLN02942 |
dihydropyrimidinase |
12-475 |
0e+00 |
|
dihydropyrimidinase
Pssm-ID: 178530 Cd Length: 486 Bit Score: 540.97 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472750 12 ITSERLLIKGGRIVNDDQSFYADIYMEDGVIKQIGDNLIVPGGVKTIEANGKMVIPGGIDIHTHLQMPFRGTTTADDFTQ 91
Cdd:PLN02942 2 ASSTKILIKGGTVVNAHHQELADVYVEDGIIVAVAPNLKVPDDVRVIDATGKFVMPGGIDPHTHLAMPFMGTETIDDFFS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472750 92 GTKAALAGGTTMIVDHVIPEPGcSLLEAFDRWSKWAdEKACCDYSLHVDITHWNDSVKQEVETLIKEKGVNSFQVYMAFK 171
Cdd:PLN02942 82 GQAAALAGGTTMHIDFVIPVNG-NLLAGYEAYEKKA-EKSCMDYGFHMAITKWDDTVSRDMETLVKEKGINSFKFFMAYK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472750 172 DLYQMSNTELYEVFTFLGEHGGIAQVHAENGEIIAEEQARMLEMGITGPEGHVLSRPEELEAEAVFRAVTIASQTNCPLY 251
Cdd:PLN02942 160 GSLMVTDELLLEGFKRCKSLGALAMVHAENGDAVFEGQKRMIELGITGPEGHALSRPPLLEGEATARAIRLAKFVNTPLY 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472750 252 VTRVMSKSAADIISQARKKGNVVFGEPITASLGTDGTHYWSKNWAKAASFVTSPPLSPdPTTPDYLNTLLASGDLSVVGS 331
Cdd:PLN02942 240 VVHVMSIDAMEEIARARKSGQRVIGEPVVSGLVLDDSKLWDPDFTIASKYVMSPPIRP-AGHGKALQAALSSGILQLVGT 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472750 332 AHCTFSVAQKAIGKDDFTQIPEGVNGAEERMSIIWDKAVVTGKMDENMFVAVTSTNAAKILNLYPRKGRIAVGSDSDLVI 411
Cdd:PLN02942 319 DHCPFNSTQKAFGKDDFRKIPNGVNGIEERMHLVWDTMVESGQISPTDYVRVTSTECAKIFNIYPRKGAILAGSDADIII 398
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 66472750 412 WDTDAVRTITAKTHHSAAEYNVFEGMELRGAPMLVVCQGKIVLEDGNLHATSGTGRFIPCSPFP 475
Cdd:PLN02942 399 LNPNSTFTISAKTHHSRIDTNVYEGRRGKGKVEVTISQGRVVWENGELKVVRGSGRYIEMPPFS 462
|
|
| AllB |
COG0044 |
Dihydroorotase or related cyclic amidohydrolase [Nucleotide transport and metabolism]; ... |
18-470 |
8.17e-130 |
|
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: 386.37 E-value: 8.17e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472750 18 LIKGGRIVNDDQSFYADIYMEDGVIKQIGDNLIVPGGVKTIEANGKMVIPGGIDIHTHLQMPFRgtTTADDFTQGTKAAL 97
Cdd:COG0044 1 LIKNGRVVDPGGLERADVLIEDGRIAAIGPDLAAPEAAEVIDATGLLVLPGLIDLHVHLREPGL--EHKEDIETGTRAAA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472750 98 AGGTTMIVDHVIPEPGCSLLEAFDRWSKWADEKACCDYSLHVDITHWNDSVKQEVETLiKEKGVNSFQVYMAFKDLYQMS 177
Cdd:COG0044 79 AGGVTTVVDMPNTNPVTDTPEALEFKLARAEEKALVDVGPHGALTKGLGENLAELGAL-AEAGAVAFKVFMGSDDGNPVL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472750 178 NTE-LYEVFTFLGEHGGIAQVHAENGEIIAEeqaRMLEMGITGPEGHVLSRPEELEAEAVFRAVTIASQTNCPLYVTRVM 256
Cdd:COG0044 158 DDGlLRRALEYAAEFGALVAVHAEDPDLIRG---GVMNEGKTSPRLGLKGRPAEAEEEAVARDIALAEETGARLHIVHVS 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472750 257 SKSAADIISQARKKGNVVFGE--P----ITAS-LGTDGTHYwsknwakaasfVTSPPLsPDPTTPDYLNTLLASGDLSVV 329
Cdd:COG0044 235 TAEAVELIREAKARGLPVTAEvcPhhltLTDEdLERYGTNF-----------KVNPPL-RTEEDREALWEGLADGTIDVI 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472750 330 GSAHCTFSVAQKAigkDDFTQIPEGVNGAEERMSIIWDKAVVTGKMDENMFVAVTSTNAAKILNLyPRKGRIAVGSDSDL 409
Cdd:COG0044 303 ATDHAPHTLEEKE---LPFAEAPNGIPGLETALPLLLTELVHKGRLSLERLVELLSTNPARIFGL-PRKGRIAVGADADL 378
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 66472750 410 VIWDTDAVRTITAKTHHSAAEYNVFEGMELRGAPMLVVCQGKIVLEDGNLHAtSGTGRFIP 470
Cdd:COG0044 379 VLFDPDAEWTVTAEDLHSKSKNTPFEGRELTGRVVATIVRGRVVYEDGEVVG-EPRGRFLR 438
|
|
| PRK13404 |
PRK13404 |
dihydropyrimidinase; Provisional |
17-478 |
1.04e-115 |
|
dihydropyrimidinase; Provisional
Pssm-ID: 184033 [Multi-domain] Cd Length: 477 Bit Score: 351.69 E-value: 1.04e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472750 17 LLIKGGRIVNDDQSFYADIYMEDGVIKQIGDNLivPGGVKTIEANGKMVIPGGIDIHTHLQMPF-RGTTTADDFTQGTKA 95
Cdd:PRK13404 6 LVIRGGTVVTATDTFQADIGIRGGRIAALGEGL--GPGAREIDATGRLVLPGGVDSHCHIDQPSgDGIMMADDFYTGTVS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472750 96 ALAGGTTMIVDHVIPEPGCSLLEAFDRWSKWADEKACCDYSLHVDITHWNDSV-KQEVETLIKEkGVNSFQVYMAFKDLy 174
Cdd:PRK13404 84 AAFGGTTTVIPFAAQHRGQSLREAVEDYHRRAAGKAVIDYAFHLIVADPTEEVlTEELPALIAQ-GYTSFKVFMTYDDL- 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472750 175 QMSNTELYEVFTFLGEHGGIAQVHAENGEIIAEEQARMLEMGITGPEGHVLSRPEELEAEAVFRAVTIASQTNCPLYVTR 254
Cdd:PRK13404 162 KLDDRQILDVLAVARRHGAMVMVHAENHDMIAWLTKRLLAAGLTAPKYHAISRPMLAEREATHRAIALAELVDVPILIVH 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472750 255 VMSKSAADIISQARKKGNVVFGEP------ITAS-LGTDGTHywsknwakAASFVTSPPLSpDPTTPDYLNTLLASGDLS 327
Cdd:PRK13404 242 VSGREAAEQIRRARGRGLKIFAETcpqylfLTAEdLDRPGME--------GAKYICSPPPR-DKANQEAIWNGLADGTFE 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472750 328 VVGSAHCTFSVaQKAIGKD------DFTQIPEGVNGAEERMSIIWDKAVVTGKMDENMFVAVTSTNAAKILNLYPRKGRI 401
Cdd:PRK13404 313 VFSSDHAPFRF-DDTDGKLaaganpSFKAIANGIPGIETRLPLLFSEGVVKGRISLNRFVALTSTNPAKLYGLYPRKGAI 391
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 66472750 402 AVGSDSDLVIWDTDAVRTITAKTHHSAAEYNVFEGMELRGAPMLVVCQGKIVLEDGNLHATSGTGRFIPCSPfPDFA 478
Cdd:PRK13404 392 AIGADADIAIWDPDREVTITNADLHHAADYTPYEGMRVTGWPVTVLSRGRVVVEDGELVAERGSGQFLARSL-PDRA 467
|
|
| L-HYD_ALN |
cd01315 |
L-Hydantoinases (L-HYDs) and Allantoinase (ALN); L-Hydantoinases are a member of the ... |
17-457 |
2.17e-65 |
|
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: 219.85 E-value: 2.17e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472750 17 LLIKGGRIVNDDQSFYADIYMEDGVIKQIGDNLIVPGGVKTIEANGKMVIPGGIDIHTHLQMPfrGTTTADDFTQGTKAA 96
Cdd:cd01315 2 LVIKNGRVVTPDGVREADIAVKGGKIAAIGPDIANTEAEEVIDAGGLVVMPGLIDTHVHINEP--GRTEWEGFETGTKAA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472750 97 LAGGTTMIVDhvIP---EPGCSLLEAFDRWSKWADEKaccdysLHVDITHWNDSVKQEVETLIK--EKGVNSFQVYMA-- 169
Cdd:cd01315 80 AAGGITTIID--MPlnsIPPTTTVENLEAKLEAAQGK------LHVDVGFWGGLVPGNLDQLRPldEAGVVGFKCFLCps 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472750 170 -FKDLYQMSNTELYEVFTFLGEHGGIAQVHAENGEIIAEEQARMLEMGITGPEGHVLSRPEELEAEAVFRAVTIASQTNC 248
Cdd:cd01315 152 gVDEFPAVDDEQLEEAMKELAKTGSVLAVHAENPEITEALQEQAKAKGKRDYRDYLASRPVFTEVEAIQRILLLAKETGC 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472750 249 PLYVTRVMSKSAADIISQARKKGNVVFGEpitaslgtDGTHYW---SKNWAKAAS-FVTSPPLSpDPTTPDYLNTLLASG 324
Cdd:cd01315 232 RLHIVHLSSAEAVPLIREARAEGVDVTVE--------TCPHYLtftAEDVPDGGTeFKCAPPIR-DAANQEQLWEALENG 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472750 325 DLSVVGSAHCTFSVAQKAIGKDDFTQIPEGVNGAEERMSIIWDKAVVTGKMDENMFVAVTSTNAAKILNLYPRKGRIAVG 404
Cdd:cd01315 303 DIDMVVSDHSPCTPELKLLGKGDFFKAWGGISGLQLGLPVMLTEAVNKRGLSLEDIARLMCENPAKLFGLSHQKGRIAVG 382
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 66472750 405 SDSDLVIWDTDAVRTITAKTHHSAAEYNVFEGMELRGAPMLVVCQGKIVLEDG 457
Cdd:cd01315 383 YDADFVVWDPEEEFTVDAEDLYYKNKISPYVGRTLKGRVHATILRGTVVYQDG 435
|
|
| Cyclic_amidohydrolases |
cd01302 |
Cyclic amidohydrolases, including hydantoinase, dihydropyrimidinase, allantoinase, and ... |
63-446 |
2.01e-61 |
|
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: 206.09 E-value: 2.01e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472750 63 KMVIPGGIDIHTHLQMPFrGTTTADDFTQGTKAALAGGTTMIVDHVIPEPGCSLLEAFDRWSKWADEKACCDYSLHVDIt 142
Cdd:cd01302 1 LLVLPGFIDIHVHLRDPG-GTTYKEDFESGSRAAAAGGVTTVIDMPNTGPPPIDLPAIELKIKLAEESSYVDFSFHAGI- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472750 143 hWNDSVKQEVETLIkEKGVNSFQVYMAFK--DLYQMSNTELYEVFTFLGEHGGIAQVHAEngeiiaeeqarmlemgitgp 220
Cdd:cd01302 79 -GPGDVTDELKKLF-DAGINSLKVFMNYYfgELFDVDDGTLMRTFLEIASRGGPVMVHAE-------------------- 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472750 221 eghvlsrpeeleaeavfRAVTIASQTNCPLYVTRVMSKSAADIISQARKKGNVVFGEPITASLGTDgTHYWSKNWAKaas 300
Cdd:cd01302 137 -----------------RAAQLAEEAGANVHIAHVSSGEALELIKFAKNKGVKVTCEVCPHHLFLD-ESMLRLNGAW--- 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472750 301 FVTSPPLSPdPTTPDYLNTLLASGDLSVVGSAHCTFSVAQKAIGKDdFTQIPEGVNGAEERMSIIWdKAVVTGKMDENMF 380
Cdd:cd01302 196 GKVNPPLRS-KEDREALWEGVKNGKIDTIASDHAPHSKEEKESGKD-IWKAPPGFPGLETRLPILL-TEGVKRGLSLETL 272
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 66472750 381 VAVTSTNAAKILNLYPrKGRIAVGSDSDLVIWDTDAVRTITAKTHHSAAEYNVFEGMELRGAPMLV 446
Cdd:cd01302 273 VEILSENPARIFGLYP-KGTIAVGYDADLVIVDPKKEWKVTAEEIESKADWTPFEGMEVTGKPVST 337
|
|
| PRK02382 |
PRK02382 |
dihydroorotase; Provisional |
17-470 |
4.84e-55 |
|
dihydroorotase; Provisional
Pssm-ID: 179417 [Multi-domain] Cd Length: 443 Bit Score: 192.17 E-value: 4.84e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472750 17 LLIKGGRIVNDDQSFYADIYMEDGVIKQIGDNLIVPGGVKTIEANGKMVIPGGIDIHTHLQMPfrGTTTADDFTQGTKAA 96
Cdd:PRK02382 4 ALLKDGRVYYNNSLQPRDVRIDGGKITAVGKDLDGSSSEEVIDARGMLLLPGGIDVHVHFREP--GYTHKETWYTGSRSA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472750 97 LAGGTTMIVDHVIPEPGCSLLEAFDRWSKWADEKACCDYSLhvdithwNDSVKQEVETL--IKEKGVNSF-QVYMAfKDL 173
Cdd:PRK02382 82 AAGGVTTVVDQPNTDPPTVDGESFDEKAELAARKSIVDFGI-------NGGVTGNWDPLesLWERGVFALgEIFMA-DST 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472750 174 YQMS-NTELY-EVFTFLGEHGGIAQVHAENGEIIaEEQARMLEmGITGPEGHVLSRPEELEAEAVFRAVTIASQTNCPLY 251
Cdd:PRK02382 154 GGMGiDEELFeEALAEAARLGVLATVHAEDEDLF-DELAKLLK-GDADADAWSAYRPAAAEAAAVERALEVASETGARIH 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472750 252 VTRVMSKSAADIISqarkkgnvvfGEPITaslgTDGT-HYW---SKNWAKAASFV-TSPPLSPDPTTPDYLNTLlASGDL 326
Cdd:PRK02382 232 IAHISTPEGVDAAR----------REGIT----CEVTpHHLflsRRDWERLGTFGkMNPPLRSEKRREALWERL-NDGTI 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472750 327 SVVGSAHCTFSVAQKAigkDDFTQIPEGVNGAEERMSIIWdKAVVTGKMDENMFVAVTSTNAAKILNLyPRKGRIAVGSD 406
Cdd:PRK02382 297 DVVASDHAPHTREEKD---ADIWDAPSGVPGVETMLPLLL-AAVRKNRLPLERVRDVTAANPARIFGL-DGKGRIAEGYD 371
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 66472750 407 SDLVIWDTDAVRTITAKTHHSAAEYNVFEGMElrGA-PMLVVCQGKIVLEDGNLHATSGTGRFIP 470
Cdd:PRK02382 372 ADLVLVDPDAAREIRGDDLHSKAGWTPFEGME--GVfPELTMVRGTVVWDGDDINAKRGRGEFLR 434
|
|
| allantoinase |
TIGR03178 |
allantoinase; This enzyme carries out the first step in the degradation of allantoin, a ... |
17-470 |
1.00e-51 |
|
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: 183.35 E-value: 1.00e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472750 17 LLIKGGRIVNDDQSFYADIYMEDGVIKQIGDNlIVPGGVKTIEANGKMVIPGGIDIHTHLQMPfrGTTTADDFTQGTKAA 96
Cdd:TIGR03178 2 LIIRGGRVILPNGEREADVGVKGGKIAAIGPD-ILGPAAKIIDAGGLVVFPGVVDTHVHINEP--GRTEWEGFETGTRAA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472750 97 LAGGTTMIVDhvIP---EPGCSLLEAFDRWSKWADEKaccdysLHVDITHWNDSVKQEVETL--IKEKGVNSFQVYMA-- 169
Cdd:TIGR03178 79 AAGGITTYID--MPlnsIPATTTRASLEAKFEAAKGK------LAVDVGFWGGLVPYNLDDLreLDEAGVVGFKAFLSps 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472750 170 -FKDLYQMSNTELYEVFTFLGEHGGIAQVHAENGEIIAEEQARMLEMGITGPEGHVLSRPEELEAEAVFRAVTIASQTNC 248
Cdd:TIGR03178 151 gDDEFPHVDDWQLYKGMRELARLGQLLLVHAENPAITSALGEEAPPQGGVGADAYLASRPVFAEVEAIRRTLALAKVTGC 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472750 249 PLYVTRVMSKSAADIISQARKKgnvvfGEPITASLGTDGTHYWSKNWAKAAS-FVTSPPLSpDPTTPDYLNTLLASGDLS 327
Cdd:TIGR03178 231 RVHVVHLSSAEAVELITEAKQE-----GLDVTVETCPHYLTLTAEEVPDGGTlAKCAPPIR-DLANQEGLWEALLNGLID 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472750 328 VVGSAH--CTFSVAQkaigKDDFTQIPEGVNGAEERMSIIWDKAVVTGKMDENMFVAVTSTNAAKILNLyPRKGRIAVGS 405
Cdd:TIGR03178 305 CVVSDHspCTPDLKR----AGDFFKAWGGIAGLQSTLDVMFDEAVQKRGLPLEDIARLMATNPAKRFGL-AQKGRIAPGK 379
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 66472750 406 DSDLVIWDTDAVRTITAKTHHSAAEYNVFEGMELRGAPMLVVCQGKIVLEDGNLhATSGTGRFIP 470
Cdd:TIGR03178 380 DADFVFVDPDESYTLTPDDLYYRHKVSPYVGRTIGGRVRATYLRGQCIYDDEQF-IGAPKGQLLL 443
|
|
| PRK06189 |
PRK06189 |
allantoinase; Provisional |
17-460 |
1.72e-51 |
|
allantoinase; Provisional
Pssm-ID: 235732 [Multi-domain] Cd Length: 451 Bit Score: 182.98 E-value: 1.72e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472750 17 LLIKGGRIVNDDQSFYADIYMEDGVIKQIGDNLIVPGGvKTIEANGKMVIPGGIDIHTHLQMPfrGTTTADDFTQGTKAA 96
Cdd:PRK06189 5 LIIRGGKVVTPEGVYRADIGIKNGKIAEIAPEISSPAR-EIIDADGLYVFPGMIDVHVHFNEP--GRTHWEGFATGSAAL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472750 97 LAGGTTMIVDHVIPEPGCSLL-EAFDRWSKWADEKACCDYSLhvdithWNDSVKQEVETLIK--EKGVNSFQVYMAFK-- 171
Cdd:PRK06189 82 AAGGCTTYFDMPLNSIPPTVTrEALDAKAELARQKSAVDFAL------WGGLVPGNLEHLRElaEAGVIGFKAFMSNSgt 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472750 172 DLYQMSNTE-LYEVFTFLGEHGGIAQVHAENGEIIAEEQARMLEMGITGPEGHVLSRPEELEAEAVFRAVTIASQTNCPL 250
Cdd:PRK06189 156 DEFRSSDDLtLYEGMKEIAALGKILALHAESDALTRHLTTQARQQGKTDVRDYLESRPVVAELEAVQRALLYAQETGCPL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472750 251 YVTRVMSKSAADIISQARKKG-NV---------VFGEPITASLGTdgthywsknWAKAAsfvtsPPLSpDPTTPDYLNTL 320
Cdd:PRK06189 236 HFVHISSGKAVALIAEAKKRGvDVsvetcphylLFTEEDFERIGA---------VAKCA-----PPLR-SRSQKEELWRG 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472750 321 LASGDLSVVGSAH--CTFSVAQkaigKDDFTQIPEGVNGAEERMSIIWDKAVVTGKMDENMFVAVTSTNAAKILNLyPRK 398
Cdd:PRK06189 301 LLAGEIDMISSDHspCPPELKE----GDDFFLVWGGISGGQSTLLVMLTEGYIERGIPLETIARLLATNPAKRFGL-PQK 375
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 66472750 399 GRIAVGSDSDLVIWDTDAVRTITAKTHHSAAEYNVFEGMELRGAPMLVVCQGKIVLEDGNLH 460
Cdd:PRK06189 376 GRLEVGADADFVLVDLDETYTLTKEDLFYRHKQSPYEGRTFPGRVVATYLRGQCVYQDGEVF 437
|
|
| pyrC_multi |
TIGR00857 |
dihydroorotase, multifunctional complex type; In contrast to the homodimeric type of ... |
33-456 |
1.21e-49 |
|
dihydroorotase, multifunctional complex type; In contrast to the homodimeric type of dihydroorotase found in E. coli, this class tends to appear in a large, multifunctional complex with aspartate transcarbamoylase. Homologous domains appear in multifunctional proteins of higher eukaryotes. In some species, including Pseudomonas putida and P. aeruginosa, this protein is inactive but is required as a non-catalytic subunit of aspartate transcarbamoylase (ATCase). In these species, a second, active dihydroorotase is also present. The seed for this model does not include any example of the dihydroorotase domain of eukaryotic multidomain pyrimidine synthesis proteins. All proteins described by this model should represent active and inactive dihydroorotase per se and functionally equivalent domains of multifunctional proteins from higher eukaryotes, but exclude related proteins such as allantoinase. [Purines, pyrimidines, nucleosides, and nucleotides, Pyrimidine ribonucleotide biosynthesis]
Pssm-ID: 273302 [Multi-domain] Cd Length: 411 Bit Score: 176.86 E-value: 1.21e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472750 33 ADIYMEDGVIKQIGDNLIVPGgVKTIEANGKMVIPGGIDIHTHLQMPfrGTTTADDFTQGTKAALAGGTTMIVDHVIPEP 112
Cdd:TIGR00857 6 VDILVEGGRIKKIGKLRIPPD-AEVIDAKGLLVLPGFIDLHVHLRDP--GEEYKEDIESGSKAAAHGGFTTVADMPNTKP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472750 113 GCSLLEAFDRWSKWADEKACCDYSLHVDITHWNDsVKQEVE-TLIKEKGVNSFQVYMAFKDLYQMSNteLYEVFTFLGEH 191
Cdd:TIGR00857 83 PIDTPETLEWKLQRLKKVSLVDVHLYGGVTQGNQ-GKELTEaYELKEAGAVGRMFTDDGSEVQDILS--MRRALEYAAIA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472750 192 GGIAQVHAENGEIIAEEQARMLEMgitGPEGHVLSRPEELEAEAVFRAVTIASQTNCPLYVTRVMSKSAADIISQARKKg 271
Cdd:TIGR00857 160 GVPIALHAEDPDLIYGGVMHEGPS---AAQLGLPARPPEAEEVAVARLLELAKHAGCPVHICHISTKESLELIVKAKSQ- 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472750 272 nvvfGEPITAS------LGTDGTHYWSKNWAKaasfvTSPPLSPdPTTPDYLNTLLASGDLSVVGSAHCTFSVAQKAIGk 345
Cdd:TIGR00857 236 ----GIKITAEvtphhlLLSEEDVARLDGNGK-----VNPPLRE-KEDRLALIEGLKDGIIDIIATDHAPHTLEEKTKE- 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472750 346 ddFTQIPEGVNGAEERMSIIWDkAVVTGKMDENMFVAVTSTNAAKILNLyPRKGRIAVGSDSDLVIWDTDAVRTITAKTH 425
Cdd:TIGR00857 305 --FAAAPPGIPGLETALPLLLQ-LLVKGLISLKDLIRMLSINPARIFGL-PDKGTLEEGNPADITVFDLKKEWTINAETF 380
|
410 420 430
....*....|....*....|....*....|.
gi 66472750 426 HSAAEYNVFEGMELRGAPMLVVCQGKIVLED 456
Cdd:TIGR00857 381 YSKAKNTPFEGMSLKGKPIATILRGKVVYED 411
|
|
| pyrC |
PRK09357 |
dihydroorotase; Validated |
16-456 |
3.94e-43 |
|
dihydroorotase; Validated
Pssm-ID: 236479 [Multi-domain] Cd Length: 423 Bit Score: 159.21 E-value: 3.94e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472750 16 RLLIKGGRIVNDDQSFY-ADIYMEDGVIKQIGDNLIVPGgVKTIEANGKMVIPGGIDIHTHLQMPfrGTTTADDFTQGTK 94
Cdd:PRK09357 2 MILIKNGRVIDPKGLDEvADVLIDDGKIAAIGENIEAEG-AEVIDATGLVVAPGLVDLHVHLREP--GQEDKETIETGSR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472750 95 AALAGGTTMIV-----DHVIPEPGcsLLEAFdrWSKwADEKACCDysLHV--DIThwndsVKQEVETL-----IKEKGVn 162
Cdd:PRK09357 79 AAAAGGFTTVVampntKPVIDTPE--VVEYV--LDR-AKEAGLVD--VLPvgAIT-----KGLAGEELtefgaLKEAGV- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472750 163 sfqvyMAFKD--LYQMSNTELYEVFTFLGEHGGIAQVHAE----NGEIIAEEQARMLEMGITGpeghvlsRPEELEAEAV 236
Cdd:PRK09357 146 -----VAFSDdgIPVQDARLMRRALEYAKALDLLIAQHCEdpslTEGGVMNEGEVSARLGLPG-------IPAVAEEVMI 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472750 237 FRAVTIASQTNCPLYVTRVMSKSAADIISQARKKGnvvfgEPITA------------SLGTDGTHYwsknwaKAAsfvts 304
Cdd:PRK09357 214 ARDVLLAEATGARVHICHVSTAGSVELIRWAKALG-----IKVTAevtphhllltdeDLLTYDPNY------KVN----- 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472750 305 PPLSpDPTTPDYLNTLLASGDLSVVGSAHCTFSVAQKAIgkdDFTQIPEGVNGAEERMSIIWDKAVVTGKMDENMFVAVT 384
Cdd:PRK09357 278 PPLR-TEEDREALIEGLKDGTIDAIATDHAPHAREEKEC---EFEAAPFGITGLETALSLLYTTLVKTGLLDLEQLLEKM 353
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 66472750 385 STNAAKILNLYPrkGRIAVGSDSDLVIWDTDAVRTITAKTHHSAAEYNVFEGMELRGAPMLVVCQGKIVLED 456
Cdd:PRK09357 354 TINPARILGLPA--GPLAEGEPADLVIFDPEAEWTVDGEDFASKGKNTPFIGMKLKGKVVYTIVDGKIVYQD 423
|
|
| DHOase_IIb |
cd01318 |
Dihydroorotase (DHOase), subgroup IIb; DHOases catalyze the reversible interconversion of ... |
62-450 |
7.25e-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: 143.24 E-value: 7.25e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472750 62 GKMVIPGGIDIHTHLQMPfrGTTTADDFTQGTKAALAGGTTMIVDHVIPEPGCSLLEAFDRWSKWADEKACCDYSLHVDI 141
Cdd:cd01318 1 GLLILPGVIDIHVHFREP--GLTYKEDFVSGSRAAAAGGVTTVMDMPNTKPPTTTAEALYEKLRLAAAKSVVDYGLYFGV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472750 142 ThwNDSVKQEVETLikekGVNSFQVYMA--FKDLYQMSNT------ELYEVFTFlgehggiaqvHAENGEIIAEEQARML 213
Cdd:cd01318 79 T--GSEDLEELDKA----PPAGYKIFMGdsTGDLLDDEETlerifaEGSVLVTF----------HAEDEDRLRENRKELK 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472750 214 EMGItgpegHVLSRPEELEAEAVFRAVTIASQTNCPLYVTRVMSKSAADIISQARKKGNV-------VFGEPITASLGTd 286
Cdd:cd01318 143 GESA-----HPRIRDAEAAAVATARALKLARRHGARLHICHVSTPEELKLIKKAKPGVTVevtphhlFLDVEDYDRLGT- 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472750 287 gthywsknWAKaasfvTSPPLSpDPTTPDYLNTLLASGDLSVVGSAHCTFSVAQKAigkDDFTQIPEGVNGAEERMSII- 365
Cdd:cd01318 217 --------LGK-----VNPPLR-SREDRKALLQALADGRIDVIASDHAPHTLEEKR---KGYPAAPSGIPGVETALPLMl 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472750 366 --WDKAVVTGKMdenmFVAVTSTNAAKILNLyPRKGRIAVGSDSDLVIWDTDAVRTITAKTHHSAAEYNVFEGMELRGAP 443
Cdd:cd01318 280 tlVNKGILSLSR----VVRLTSHNPARIFGI-KNKGRIAEGYDADLTVVDLKEERTIRAEEFHSKAGWTPFEGFEVTGFP 354
|
....*..
gi 66472750 444 MLVVCQG 450
Cdd:cd01318 355 VMTIVRG 361
|
|
| DHOase_IIa |
cd01317 |
Dihydroorotase (DHOase), subgroup IIa; DHOases catalyze the reversible interconversion of ... |
54-446 |
1.18e-34 |
|
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: 134.67 E-value: 1.18e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472750 54 GVKTIEANGKMVIPGGIDIHTHLQMPfrGTTTADDFTQGTKAALAGGTTMIVDHVIPEPGCSLLEAFDR-WSKWADEKAC 132
Cdd:cd01317 1 DAEVIDAEGKILAPGLVDLHVHLREP--GFEYKETLESGAKAAAAGGFTTVVCMPNTNPVIDNPAVVELlKNRAKDVGIV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472750 133 CDY---SLhvdithwndSVKQEVETL-----IKEKGVNSFqvymaFKDLYQMSNTE-LYEVFTFLGEHGGIAQVHAENGE 203
Cdd:cd01317 79 RVLpigAL---------TKGLKGEELteigeLLEAGAVGF-----SDDGKPIQDAElLRRALEYAAMLDLPIIVHPEDPS 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472750 204 IIAEeqARMLEMGITGPEGhVLSRPEELEAEAVFRAVTIASQTNCPLYVTRVMSKSAADIISQARKKGnvvfgEPITASL 283
Cdd:cd01317 145 LAGG--GVMNEGKVASRLG-LPGIPPEAETIMVARDLELAEATGARVHFQHLSTARSLELIRKAKAKG-----LPVTAEV 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472750 284 GTdgtHYWSKNWAKAASFVT----SPPLSpDPTTPDYLNTLLASGDLSVVGSAHCTFSVAQKAIgkdDFTQIPEGVNGAE 359
Cdd:cd01317 217 TP---HHLLLDDEALESYDTnakvNPPLR-SEEDREALIEALKDGTIDAIASDHAPHTDEEKDL---PFAEAPPGIIGLE 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472750 360 ERMSIIWDKAVVTGKMDENMFVAVTSTNAAKILNLYPrkGRIAVGSDSDLVIWDTDAVRTITAKTHHSAAEYNVFEGMEL 439
Cdd:cd01317 290 TALPLLWTLLVKGGLLTLPDLIRALSTNPAKILGLPP--GRLEVGAPADLVLFDPDAEWIVDEETFRSKSKNTPFDGQKL 367
|
....*..
gi 66472750 440 RGAPMLV 446
Cdd:cd01317 368 KGRVLAT 374
|
|
| PRK08044 |
PRK08044 |
allantoinase AllB; |
17-422 |
1.67e-32 |
|
allantoinase AllB;
Pssm-ID: 169193 [Multi-domain] Cd Length: 449 Bit Score: 129.98 E-value: 1.67e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472750 17 LLIKGGRIVNDDQSFYADIYMEDGVIKQIGDNLivPGGVKTIEANGKMVIPGGIDIHTHLQMPfrGTTTADDFTQGTKAA 96
Cdd:PRK08044 5 LIIKNGTVILENEARVVDIAVKGGKIAAIGQDL--GDAKEVMDASGLVVSPGMVDAHTHISEP--GRSHWEGYETGTRAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472750 97 LAGG-TTMIvdhviPEPGCSLLEAFDRWSKWADEKACcDYSLHVDITHWNDSVKQEVETL--IKEKGVNSFQVYMAF--- 170
Cdd:PRK08044 81 AKGGiTTMI-----EMPLNQLPATVDRASIELKFDAA-KGKLTIDAAQLGGLVSYNLDRLheLDEVGVVGFKCFVATcgd 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472750 171 ----KDLYQMSNTELYEVFTFLGEHGGIAQVHAENGEIIAEEQARMLEMGITGPEGHVLSRPEELEAEAVFRAVTIASQT 246
Cdd:PRK08044 155 rgidNDFRDVNDWQFYKGAQKLGELGQPVLVHCENALICDELGEEAKREGRVTAHDYVASRPVFTEVEAIRRVLYLAKVA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472750 247 NCPLYVTRVMSKSAADIISQARKKGNVVFGEPItaslgtdgTHYW---SKNWAKAASFVT-SPPLSPDPTTPDYLNTLLa 322
Cdd:PRK08044 235 GCRLHVCHISSPEGVEEVTRARQEGQDVTCESC--------PHYFvldTDQFEEIGTLAKcSPPIRDLENQKGMWEKLF- 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472750 323 SGDLSVVGSAHCTFSVAQKAigkDDFTQIPEGVNGAEERMSIIWDKAVVTGKMDENMFVAVTSTNAAKILNLyPRKGRIA 402
Cdd:PRK08044 306 NGEIDCLVSDHSPCPPEMKA---GNIMEAWGGIAGLQNCMDVMFDEAVQKRGMSLPMFGKLMATNAADIFGL-QQKGRIA 381
|
410 420
....*....|....*....|
gi 66472750 403 VGSDSDLVIWDTDAVRTITA 422
Cdd:PRK08044 382 PGKDADFVFIQPNSSYVLKN 401
|
|
| PRK09060 |
PRK09060 |
dihydroorotase; Validated |
17-467 |
4.46e-29 |
|
dihydroorotase; Validated
Pssm-ID: 181632 [Multi-domain] Cd Length: 444 Bit Score: 120.02 E-value: 4.46e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472750 17 LLIKGGRIVNDDQSFYADIYMEDGVIKQIGDNLIVPGGvKTIEANGKMVIPGGIDIHTHLQMPfrGTTTADDFTQGTKAA 96
Cdd:PRK09060 7 LILKGGTVVNPDGEGRADIGIRDGRIAAIGDLSGASAG-EVIDCRGLHVLPGVIDSQVHFREP--GLEHKEDLETGSRAA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472750 97 LAGGTTMIVDHVIPEPGCSLLEAFDRWSKWADEKACCDYSLHVDITHWNdsvKQEVETLIKEKGVNSFQVYM--AFKDLY 174
Cdd:PRK09060 84 VLGGVTAVFEMPNTNPLTTTAEALADKLARARHRMHCDFAFYVGGTRDN---ADELAELERLPGCAGIKVFMgsSTGDLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472750 175 QMSNTELYEVFtflgEHGG-IAQVHAEngeiiaeEQARMLEMGITGPEGHVLSRPEELEAEAVFRA----VTIASQTNCP 249
Cdd:PRK09060 161 VEDDEGLRRIL----RNGRrRAAFHSE-------DEYRLRERKGLRVEGDPSSHPVWRDEEAALLAtrrlVRLARETGRR 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472750 250 LYVTRVMSKSAADIISQARKKGNV--------VFGEPITASLGTdgthYWSKNwakaasfvtsPPLSpDPTTPDYLNTLL 321
Cdd:PRK09060 230 IHVLHVSTAEEIDFLADHKDVATVevtphhltLAAPECYERLGT----LAQMN----------PPIR-DARHRDGLWRGV 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472750 322 ASGDLSVVGSAHCTFSVAQKAigkDDFTQIPEGVNGAEERMSIIWDKaVVTGKMDENMFVAVTSTNAAKILNLyPRKGRI 401
Cdd:PRK09060 295 RQGVVDVLGSDHAPHTLEEKA---KPYPASPSGMTGVQTLVPIMLDH-VNAGRLSLERFVDLTSAGPARIFGI-AGKGRI 369
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 66472750 402 AVGSDSDLVIWDTDAVRTITAKTHHSAAEYNVFEGMELRGAPMLVVCQGKIVLEDGNLhATSGTGR 467
Cdd:PRK09060 370 AVGYDADFTIVDLKRRETITNEWIASRCGWTPYDGKEVTGWPVGTIVRGQRVMWDGEL-VGPPTGE 434
|
|
| PRK04250 |
PRK04250 |
dihydroorotase; Provisional |
22-457 |
4.70e-27 |
|
dihydroorotase; Provisional
Pssm-ID: 235265 [Multi-domain] Cd Length: 398 Bit Score: 113.32 E-value: 4.70e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472750 22 GRIVNDDQSFYADIYMEDGVIKQIGDNLIvpGGVKTIEANGKMVIPGGIDIHTHLQmpfrgtttadDFTQ--------GT 93
Cdd:PRK04250 4 GKFLLKGRIVEGGIGIENGRISKISLRDL--KGKEVIKVKGGIILPGLIDVHVHLR----------DFEEsyketiesGT 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472750 94 KAALAGGTTMIVDHVIPEPGCSLLEAFDRWSKWADEKACCDYSLHVdITHWNDSVKQEVETLIKEKGVNSfqvymAFKDL 173
Cdd:PRK04250 72 KAALHGGITLVFDMPNTKPPIMDEKTYEKRMRIAEKKSYADYALNF-LIAGNCEKAEEIKADFYKIFMGA-----STGGI 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472750 174 YQMSNTELYEvftflgEHGGIAQVHAENGEIIAEEqarmlemgitgPEghvlsRPEELEAEAVFRAVTIASQTNCPLYVT 253
Cdd:PRK04250 146 FSENFEVDYA------CAPGIVSVHAEDPELIREF-----------PE-----RPPEAEVVAIERALEAGKKLKKPLHIC 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472750 254 RVMSKSAADIISQARKkgnvvfgEPITASLGTDGTHYWSKNWAKAASFVTSPPLSpDPTTPDYLNTLLASGDlsVVGSAH 333
Cdd:PRK04250 204 HISTKDGLKLILKSNL-------PWVSFEVTPHHLFLTRKDYERNPLLKVYPPLR-SEEDRKALWENFSKIP--IIASDH 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472750 334 CTFSVAQKAIGKDDF----TQIPEGVNGAEERMSIIWDkavVTGKMdenmfvavtSTNAAKILNlYPRKGrIAVGSDSDL 409
Cdd:PRK04250 274 APHTLEDKEAGAAGIpgleTEVPLLLDAANKGMISLFD---IVEKM---------HDNPARIFG-IKNYG-IEEGNYANF 339
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 66472750 410 VIWDTDAVRTITAKTHHSAAEYNVFEGMELRGAPMLVVCQGKIVLEDG 457
Cdd:PRK04250 340 AVFDMKKEWTIKAEELYTKAGWTPYEGFKLKGKVIMTILRGEVVMEDD 387
|
|
| PRK07575 |
PRK07575 |
dihydroorotase; Provisional |
14-459 |
1.55e-26 |
|
dihydroorotase; Provisional
Pssm-ID: 236055 [Multi-domain] Cd Length: 438 Bit Score: 112.46 E-value: 1.55e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472750 14 SERLLIKGGRIVNDDQSFY-ADIYMEDGVIKQIGDNLIVPGGVKTIEANGKMVIPGGIDIHTHLQMPfrGTTTADDFTQG 92
Cdd:PRK07575 2 MMSLLIRNARILLPSGELLlGDVLVEDGKIVAIAPEISATAVDTVIDAEGLTLLPGVIDPQVHFREP--GLEHKEDLFTA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472750 93 TKAALAGGTTMIVDHVIPEPGCSLLEAFDRWSKWADEKACCDYSLHVDITHWNdsvkqeVETLIKEKGVNSFQVYM--AF 170
Cdd:PRK07575 80 SRACAKGGVTSFLEMPNTKPLTTTQAALDDKLARAAEKCVVNYGFFIGATPDN------LPELLTANPTCGIKIFMgsSH 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472750 171 KDLYQMSNTELYEVF---TFLgehggIAqVHAENGEIIAEEQARMleMGITGPEGHVLSRPEELEAEAVFRAVTIASQTN 247
Cdd:PRK07575 154 GPLLVDEEAALERIFaegTRL-----IA-VHAEDQARIRARRAEF--AGISDPADHSQIQDEEAALLATRLALKLSKKYQ 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472750 248 CPLYVTRVMSKSAADIISQArkKGNVVFGE--PITASLGTDgthywskNWAKAASFVT-SPPLSpDPTTPDYLNTLLASG 324
Cdd:PRK07575 226 RRLHILHLSTAIEAELLRQD--KPSWVTAEvtPQHLLLNTD-------AYERIGTLAQmNPPLR-SPEDNEALWQALRDG 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472750 325 DLSVVGSAHCTFSVAQKAIGkddFTQIPEGVNGAEERMSIIWDKAVvTGKMDENMFVAVTSTNAAKILNLyPRKGRIAVG 404
Cdd:PRK07575 296 VIDFIATDHAPHTLEEKAQP---YPNSPSGMPGVETSLPLMLTAAM-RGKCTVAQVVRWMSTAVARAYGI-PNKGRIAPG 370
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 66472750 405 SDSDLVIWDTDAVRTITAKTHHSAAEYNVFEGMELRGAPMLVVCQGKIVLEDGNL 459
Cdd:PRK07575 371 YDADLVLVDLNTYRPVRREELLTKCGWSPFEGWNLTGWPVTTIVGGQIVFDRGQV 425
|
|
| PRK01211 |
PRK01211 |
dihydroorotase; Provisional |
32-470 |
8.71e-26 |
|
dihydroorotase; Provisional
Pssm-ID: 179247 [Multi-domain] Cd Length: 409 Bit Score: 109.56 E-value: 8.71e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472750 32 YADIYMEDGVIKQIGDNLivpGGVKTIEANGkMVIPGGIDIHTHLQMPfrGTTTADDFTQGTKAALAGGTTMIVDHVIPE 111
Cdd:PRK01211 15 YLEIEVEDGKIKSIKKDA---GNIGKKELKG-AILPAATDIHVHFRTP--GETEKEDFSTGTLSAIFGGTTFIMDMPNNN 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472750 112 PGCSLLEAFDRWSKWADEKACCDYSLHVDITHWNDSVKQEVETLIKekgvnsfqVYMAfkdlyQMSNTELYEVftflgEH 191
Cdd:PRK01211 89 IPIKDYNAFSDKLGRVAPKAYVDFSLYSMETGNNALILDERSIGLK--------VYMG-----GTTNTNGTDI-----EG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472750 192 GGIAQV---------HAENGEIIAEEQARMLEMgitgpEGHVLSRPEELEAEAVFRAVTIASQTNCPLYVTRVmsKSAAD 262
Cdd:PRK01211 151 GEIKKIneanipvffHAELSECLRKHQFESKNL-----RDHDLARPIECEIKAVKYVKNLDLKTKIIAHVSSI--DVIGR 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472750 263 IISQARKKGNVVFGEpitASLGTDGThywsknwakaasfvTSPPLSPDPTTPDYLNTLLaSGDLSVVGSAHCTFSVAQKA 342
Cdd:PRK01211 224 FLREVTPHHLLLNDD---MPLGSYGK--------------VNPPLRDRWTQERLLEEYI-SGRFDILSSDHAPHTEEDKQ 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472750 343 igkdDFTQIPEGVNGAEERMSIIWdKAVVTGKMDENMFVAVTSTNAAKILNLypRKGRIAVGSDSDLVIWDTDAVRTITA 422
Cdd:PRK01211 286 ----EFEYAKSGIIGVETRVPLFL-ALVKKKILPLDVLYKTAIERPASLFGI--KKGKIEEGYDADFMAFDFTNIKKIND 358
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 66472750 423 KTHHSAAEYNVFEGMELRgAPMLVVCQGKIVLEDGNLhATSGTGRFIP 470
Cdd:PRK01211 359 KRLHSKCPVSPFNGFDAI-FPSHVIMRGEVVIDNYEL-ISERTGKFVP 404
|
|
| PLN02795 |
PLN02795 |
allantoinase |
22-469 |
3.90e-25 |
|
allantoinase
Pssm-ID: 178392 [Multi-domain] Cd Length: 505 Bit Score: 109.09 E-value: 3.90e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472750 22 GRIVNDDQSFYADIYMEDGVIKQIGDNLIVPG---GVKTIEANGKMVIPGGIDIHTHLQMPfrGTTTADDFTQGTKAALA 98
Cdd:PLN02795 51 KRVVTPAGVIPGAVEVEGGRIVSVTKEEEAPKsqkKPHVLDYGNAVVMPGLIDVHVHLNEP--GRTEWEGFPTGTKAAAA 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472750 99 GGTTMIVDhvIP---EPGCSLLEAFDRWSKWADEKaccdysLHVDITHWNDSVKQ------EVETLIkEKGVNSFQVYM- 168
Cdd:PLN02795 129 GGITTLVD--MPlnsFPSTTSVETLELKIEAAKGK------LYVDVGFWGGLVPEnahnasVLEELL-DAGALGLKSFMc 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472750 169 --AFKDLYQMSNTELYEVFTFLGEHGGIAQVHAEngEIIAEEQARMLEMGITGPEGHVLSRPEELEAEAVFRAVTIASQT 246
Cdd:PLN02795 200 psGINDFPMTTATHIKAALPVLAKYGRPLLVHAE--VVSPVESDSRLDADPRSYSTYLKSRPPSWEQEAIRQLLEVAKDT 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472750 247 N-------CPLYVTRVM-SKSAADIISQARKKGNVVFGEPITaslgtdgtHYWsknwAKAAS--------FVTSPPLSpD 310
Cdd:PLN02795 278 RpggvaegAHVHIVHLSdAESSLELIKEAKAKGDSVTVETCP--------HYL----AFSAEeipdgdtrYKCAPPIR-D 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472750 311 PTTPDYLNTLLASGDLSVVGSAHCTFSVAQKAIGKDDFTQIPEGVNGAEERMSIIWDKAVVTGkMDENMFVAVTSTNAAK 390
Cdd:PLN02795 345 AANRELLWKALLDGDIDMLSSDHSPSPPDLKLLEEGNFLRAWGGISSLQFVLPATWTAGRAYG-LTLEQLARWWSERPAK 423
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472750 391 ILNLyPRKGRIAVGSDSDLVIWDTDAVRTI--TAKTHHSAAEYNVFEGMELRGAPMLVVCQGKIVLEDGNlHATSGTGRF 468
Cdd:PLN02795 424 LAGL-DSKGAIAPGKDADIVVWDPEAEFVLdeSYPIYHKHKSLSPYLGTKLSGKVIATFVRGNLVFLEGK-HAKQACGSP 501
|
.
gi 66472750 469 I 469
Cdd:PLN02795 502 I 502
|
|
| Amidohydro_1 |
pfam01979 |
Amidohydrolase family; This family of enzymes are a a large metal dependent hydrolase ... |
64-453 |
2.68e-21 |
|
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: 95.26 E-value: 2.68e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472750 64 MVIPGGIDIHTHLQM-PFRGTTTADDF-----TQGTKAALAGGTTMIVDHVIPEPGC--SLLEAFDR-------WSKWAD 128
Cdd:pfam01979 1 IVLPGLIDAHVHLEMgLLRGIPVPPEFayealRLGITTMLKSGTTTVLDMGATTSTGieALLEAAEElplglrfLGPGCS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472750 129 EKAccDYSLHVDITHWNDSVKQEVETLIKEKGVnsFQVYMAFKDLYQMSNTELYEVFTFLGEHGGIAQVHAenGEIIAEE 208
Cdd:pfam01979 81 LDT--DGELEGRKALREKLKAGAEFIKGMADGV--VFVGLAPHGAPTFSDDELKAALEEAKKYGLPVAIHA--LETKGEV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472750 209 QARMLEMGITGPEGHVLSRPEELeaeAVFRAVTIASQTNCPLYVTrvmskSAADIISQARKKGNVvfgepitasLGTDGT 288
Cdd:pfam01979 155 EDAIAAFGGGIEHGTHLEVAESG---GLLDIIKLILAHGVHLSPT-----EANLLAEHLKGAGVA---------HCPFSN 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472750 289 HYWSKNWAKAASfvtspplspdpttpdylntLLASGDLSVVGSAHCtfsvaqkaIGKDDFTQIPEGVNGAEERmsiiwdk 368
Cdd:pfam01979 218 SKLRSGRIALRK-------------------ALEDGVKVGLGTDGA--------GSGNSLNMLEELRLALELQ------- 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472750 369 AVVTGKMDENMFVAVTSTNAAKILNLYPRKGRIAVGSDSDLVIWDTDavrtitakthhsaaEYNVFEGMELRGAPMLVVC 448
Cdd:pfam01979 264 FDPEGGLSPLEALRMATINPAKALGLDDKVGSIEVGKDADLVVVDLD--------------PLAAFFGLKPDGNVKKVIV 329
|
....*
gi 66472750 449 QGKIV 453
Cdd:pfam01979 330 KGKIV 334
|
|
| PRK09236 |
PRK09236 |
dihydroorotase; Reviewed |
16-106 |
2.19e-16 |
|
dihydroorotase; Reviewed
Pssm-ID: 181716 Cd Length: 444 Bit Score: 81.84 E-value: 2.19e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472750 16 RLLIKGGRIVNDDQSFYADIYMEDGVIKQIGDNLIVPGGVKTIEANGKMVIPGGIDIHTHlqmpFR--GTTTADDFTQGT 93
Cdd:PRK09236 3 RILIKNARIVNEGKIFEGDVLIENGRIAKIASSISAKSADTVIDAAGRYLLPGMIDDQVH----FRepGLTHKGDIASES 78
|
90
....*....|...
gi 66472750 94 KAALAGGTTMIVD 106
Cdd:PRK09236 79 RAAVAGGITSFME 91
|
|
| HutI |
COG1228 |
Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport ... |
13-422 |
1.30e-13 |
|
Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440841 [Multi-domain] Cd Length: 386 Bit Score: 72.69 E-value: 1.30e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472750 13 TSERLLIKGGRIVNDDQSFY---ADIYMEDGVIKQIGDN--LIVPGGVKTIEANGKMVIPGGIDIHTHLQMPFRG----- 82
Cdd:COG1228 6 QAGTLLITNATLVDGTGGGVienGTVLVEDGKIAAVGPAadLAVPAGAEVIDATGKTVLPGLIDAHTHLGLGGGRavefe 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472750 83 -----TTTADDFTQGTK---AALAGGTTMIVDHvipePGCSL----------LEAFDRWSKWADEKA-CCDYSLHvdiTH 143
Cdd:COG1228 86 agggiTPTVDLVNPADKrlrRALAAGVTTVRDL----PGGPLglrdaiiageSKLLPGPRVLAAGPAlSLTGGAH---AR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472750 144 WNDSVKQEVETLIKEkGVNSFQVYMAFKDlYQMSNTELYEVFTFLGEHGGIAQVHAENGEIIaeeqARMLEMGITGPEgH 223
Cdd:COG1228 159 GPEEARAALRELLAE-GADYIKVFAEGGA-PDFSLEELRAILEAAHALGLPVAAHAHQADDI----RLAVEAGVDSIE-H 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472750 224 VLSRPEEleaeavfravtiasqtncplyvtrvmsksaadIISQARKKGNVVFGePiTASLGTDGTHYWSKNWAKAASFVt 303
Cdd:COG1228 232 GTYLDDE--------------------------------VADLLAEAGTVVLV-P-TLSLFLALLEGAAAPVAAKARKV- 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472750 304 spplspDPTTPDYLNTLLASGdlsvvgsahCTFsvaqkAIGKDDFTQIPEGVNGAEErMSIiwdkaVVTGKMD-ENMFVA 382
Cdd:COG1228 277 ------REAALANARRLHDAG---------VPV-----ALGTDAGVGVPPGRSLHRE-LAL-----AVEAGLTpEEALRA 330
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 66472750 383 VTStNAAKILNLYPRKGRIAVGSDSDLVIWDTDAVRTITA 422
Cdd:COG1228 331 ATI-NAAKALGLDDDVGSLEPGKLADLVLLDGDPLEDIAY 369
|
|
| SsnA |
COG0402 |
Cytosine/adenosine deaminase or related metal-dependent hydrolase [Nucleotide transport and ... |
16-456 |
3.06e-13 |
|
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: 71.78 E-value: 3.06e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472750 16 RLLIKGGRIV--NDDQSFYAD--IYMEDGVIKQIGDNLIVP---GGVKTIEANGKMVIPGGIDIHTHL-QMPFRGTT--- 84
Cdd:COG0402 1 DLLIRGAWVLtmDPAGGVLEDgaVLVEDGRIAAVGPGAELParyPAAEVIDAGGKLVLPGLVNTHTHLpQTLLRGLAddl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472750 85 -----------------TADDFTQGTKAA----LAGGTTMIVDHvipepGCSLLEAFDRWSKWADE--------KACCDY 135
Cdd:COG0402 81 plldwleeyiwplearlDPEDVYAGALLAlaemLRSGTTTVADF-----YYVHPESADALAEAAAEagiravlgRGLMDR 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472750 136 SLHVDITHWNDSVKQEVETLIKE-KGVNS--FQVYMAFKDLYQMSNTELYEVFTFLGEHGGIAQVH-----AENGEIIAE 207
Cdd:COG0402 156 GFPDGLREDADEGLADSERLIERwHGAADgrIRVALAPHAPYTVSPELLRAAAALARELGLPLHTHlaetrDEVEWVLEL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472750 208 EQAR----MLEMGITGPE---GH-VLSRPEELE--AEavfRAVTIASqtnCPlyvtrvMS--KSAADI--ISQARKKGnv 273
Cdd:COG0402 236 YGKRpveyLDELGLLGPRtllAHcVHLTDEEIAllAE---TGASVAH---CP------TSnlKLGSGIapVPRLLAAG-- 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472750 274 vfgepITASLGTDGthywsknwakAASfvtspplspdpttpdylntllaSGDLSVVGSAHcTFSVAQKAIGKDdftqiPE 353
Cdd:COG0402 302 -----VRVGLGTDG----------AAS----------------------NNSLDMFEEMR-LAALLQRLRGGD-----PT 338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472750 354 GVNGAEermsiiwdkavvtgkmdenMFVAVTsTNAAKILNLYPRKGRIAVGSDSDLVIWDTDAVRTITAkthHSAAEYNV 433
Cdd:COG0402 339 ALSARE-------------------ALEMAT-LGGARALGLDDEIGSLEPGKRADLVVLDLDAPHLAPL---HDPLSALV 395
|
490 500
....*....|....*....|...
gi 66472750 434 FEGMelRGAPMLVVCQGKIVLED 456
Cdd:COG0402 396 YAAD--GRDVRTVWVAGRVVVRD 416
|
|
| ATZ_TRZ_like |
cd01298 |
TRZ/ATZ family contains enzymes from the atrazine degradation pathway and related hydrolases. ... |
17-459 |
3.79e-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: 71.46 E-value: 3.79e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472750 17 LLIKGGRIVNDDQS---FYADIYMEDGVIKQIGDNLIVPG--GVKTIEANGKMVIPGGIDIHTHLQM------------- 78
Cdd:cd01298 1 ILIRNGTIVTTDPRrvlEDGDVLVEDGRIVAVGPALPLPAypADEVIDAKGKVVMPGLVNTHTHLAMtllrgladdlplm 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472750 79 --------PFRGTTTADDFTQGTKAALA----GGTTMIVDHVIPEP-------------GCSLLEAFDRWSKWADEkacc 133
Cdd:cd01298 81 ewlkdliwPLERLLTEEDVYLGALLALAemirSGTTTFADMYFFYPdavaeaaeelgirAVLGRGIMDLGTEDVEE---- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472750 134 dyslhvdithwNDSVKQEVETLIKE-KGVNS--FQVYMAFKDLYQMSNTELYEVFTFLGEHGGIAQVH-AENGEIIAEEQ 209
Cdd:cd01298 157 -----------TEEALAEAERLIREwHGAADgrIRVALAPHAPYTCSDELLREVAELAREYGVPLHIHlAETEDEVEESL 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472750 210 AR--------MLEMGITGPE---GH-VLSRPEELE--AEavfRAVTIASqtnCPlyvTRVMsKSAADI--ISQARKKGnv 273
Cdd:cd01298 226 EKygkrpveyLEELGLLGPDvvlAHcVWLTDEEIEllAE---TGTGVAH---NP---ASNM-KLASGIapVPEMLEAG-- 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472750 274 vfgepITASLGTDGThywsknwakaasfvtspplspdpttpdylntllASGD-LSVVGSAHcTFSVAQKAIGKDDfTQIP 352
Cdd:cd01298 294 -----VNVGLGTDGA---------------------------------ASNNnLDMFEEMR-LAALLQKLAHGDP-TALP 333
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472750 353 egvngAEErmsiiwdkavvtgkmdenmFVAVTSTNAAKILNLyPRKGRIAVGSDSDLVIWDTDAVRTITAKTHHSAAEYN 432
Cdd:cd01298 334 -----AEE-------------------ALEMATIGGAKALGL-DEIGSLEVGKKADLILIDLDGPHLLPVHDPISHLVYS 388
|
490 500
....*....|....*....|....*..
gi 66472750 433 VFEGmELRgapmLVVCQGKIVLEDGNL 459
Cdd:cd01298 389 ANGG-DVD----TVIVNGRVVMEDGEL 410
|
|
| COG3964 |
COG3964 |
Predicted amidohydrolase [General function prediction only]; |
17-106 |
1.10e-12 |
|
Predicted amidohydrolase [General function prediction only];
Pssm-ID: 443164 [Multi-domain] Cd Length: 376 Bit Score: 69.81 E-value: 1.10e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472750 17 LLIKGGRIVNDDQSFYA--DIYMEDGVIKQIGDNLIVPGGVKTIEANGKMVIPGGIDIHTHLqmpFRGTTT----ADDFT 90
Cdd:COG3964 2 LLIKGGRVIDPANGIDGvmDIAIKDGKIAAVAKDIDAAEAKKVIDASGLYVTPGLIDLHTHV---FPGGTDygvdPDGVG 78
|
90
....*....|....*.
gi 66472750 91 qgtkaaLAGGTTMIVD 106
Cdd:COG3964 79 ------VRSGVTTVVD 88
|
|
| CAD_DHOase |
cd01316 |
The eukaryotic CAD protein is a trifunctional enzyme of carbamoylphosphate ... |
66-466 |
5.30e-12 |
|
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: 67.48 E-value: 5.30e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472750 66 IPGGIDIHTHLQMPfrGTTTADDFTQGTKAALAGGTTMIvdHVIPEPGCSLL--EAFDRWSKWADEKACCDYSLHVDITH 143
Cdd:cd01316 5 LPGLIDVHVHLREP--GATHKEDFASGTKAALAGGFTMV--RAMPNTNPSIVdvASLKLVQSLAQAKARCDYAFSIGATS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472750 144 WNDSvkqEVETLIKEKGVNSFQVYMAFKDLYQMSNTELYEVFTFLGEHGGIAqVHAENGEIIAeeqarmlemgitgpegh 223
Cdd:cd01316 81 TNAA---TVGELASEAVGLKFYLNETFSTLILDKITAWASHFNAWPSTKPIV-THAKSQTLAA----------------- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472750 224 VLsrpeeleaeavfravTIASQTNCPLYVTRVMSKSAADIISQARKKGNVVFGEPITASLgtdgthYWSKNWAKAASFvt 303
Cdd:cd01316 140 VL---------------LLASLHNRSIHICHVSSKEEINLIRLAKARGLKVTCEVSPHHL------FLSQDDLPRGQY-- 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472750 304 spPLSPDPTTPDYLNTL---LASGDLSVVGSAHCTFsvAQKAIGKddftqIPEGVNGAEERMSIIWdKAVVTGKMDENMF 380
Cdd:cd01316 197 --EVRPFLPTREDQEALwenLDYIDCFATDHAPHTL--AEKTGNK-----PPPGFPGVETSLPLLL-TAVHEGRLTIEDI 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472750 381 VAVTSTNAAKILNLYPRkgriavgSDSDLVIwDTDAVRTITAKTHHSAAEYNVFEGMELRGAPMLVVCQGKIVLEDGNLH 460
Cdd:cd01316 267 VDRLHTNPKRIFNLPPQ-------SDTYVEV-DLDEEWTIPKNPLQSKKGWTPFEGKKVKGKVQRVVLRGETAFIDGEIV 338
|
....*.
gi 66472750 461 ATSGTG 466
Cdd:cd01316 339 APPGFG 344
|
|
| pyrC |
PRK00369 |
dihydroorotase; Provisional |
34-468 |
6.48e-12 |
|
dihydroorotase; Provisional
Pssm-ID: 234738 [Multi-domain] Cd Length: 392 Bit Score: 67.48 E-value: 6.48e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472750 34 DIYMEDGvIKQIGDNLIVpgGVKTIEANGK---------MVIPGGIDIHTHLqmpfRGTTTA--DDFTQGTKAALAGGTT 102
Cdd:PRK00369 8 KAYLGKE-IKEICINFDR--RIKEIKSRCKpdldlpqgtLILPGAIDLHVHL----RGLKLSykEDVASGTSEAAYGGVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472750 103 MIVDHVIPEPGCSLLEAFDRWSKWADEKACCDYSLHVDIThwnDSVKqEVETLikekGVNSFQVYMafKDLyqmsntELY 182
Cdd:PRK00369 81 LVADMPNTIPPLNTPEAITEKLAELEYYSRVDYFVYSGVT---KDPE-KVDKL----PIAGYKIFP--EDL------ERE 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472750 183 EVFTFLGEHGGIAQVHAEngeiiaeeqarmLEMGITGPEGhvLSRPEELEAEAVFRAVTIASqtncpLYVTRVmskSAAD 262
Cdd:PRK00369 145 ETFRVLLKSRKLKILHPE------------VPLALKSNRK--LRRNCWYEIAALYYVKDYQN-----VHITHA---SNPR 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472750 263 IISQARKKGnvvFGEPITAS-LGTDG-THYWSKnwakaasfvTSPPLSpDPTTPDYLNTLLASGDlsVVGSAHCTFSVAQ 340
Cdd:PRK00369 203 TVRLAKELG---FTVDITPHhLLVNGeKDCLTK---------VNPPIR-DINERLWLLQALSEVD--AIASDHAPHSSFE 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472750 341 KaigKDDFTQIPEGVNGAEERMSIIWdKAVVTGKMDENMFVAVTSTNAAKILNLypRKGRIAVGSDSDLVIWDTDAVRTi 420
Cdd:PRK00369 268 K---LQPYEVCPPGIAALSFTPPFIY-TLVSKGILSIDRAVELISTNPARILGI--PYGEIKEGYRANFTVIQFEDWRY- 340
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 66472750 421 taKTHHSAAEYNVFEGMELRGAPMLVVCQGKIVLEDGNLHATSGTGRF 468
Cdd:PRK00369 341 --STKYSKVIETPLDGFELKASVYATIVQGKLAYLEGEVFPVKGINPF 386
|
|
| PRK09237 |
PRK09237 |
amidohydrolase/deacetylase family metallohydrolase; |
17-106 |
7.36e-11 |
|
amidohydrolase/deacetylase family metallohydrolase;
Pssm-ID: 236423 [Multi-domain] Cd Length: 380 Bit Score: 64.10 E-value: 7.36e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472750 17 LLIKGGRIVNDDQSFYA--DIYMEDGVIKQIGDNLIVPGGVKTIEANGKMVIPGGIDIHTHLqmpFRGTTT----ADDFT 90
Cdd:PRK09237 1 LLLRGGRVIDPANGIDGviDIAIEDGKIAAVAGDIDGSQAKKVIDLSGLYVSPGWIDLHVHV---YPGSTPygdePDEVG 77
|
90
....*....|....*.
gi 66472750 91 QGTkaalagGTTMIVD 106
Cdd:PRK09237 78 VRS------GVTTVVD 87
|
|
| PRK07228 |
PRK07228 |
5'-deoxyadenosine deaminase; |
16-107 |
1.07e-10 |
|
5'-deoxyadenosine deaminase;
Pssm-ID: 180895 [Multi-domain] Cd Length: 445 Bit Score: 63.87 E-value: 1.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472750 16 RLLIKGGRIVNDDQS---FYADIYMEDGVIKQIGDNLIVPGGVKTIEANGKMVIPGGIDIHTHL-QMPFRGttTADDFT- 90
Cdd:PRK07228 2 TILIKNAGIVTMNAKreiVDGDVLIEDDRIAAVGDRLDLEDYDDHIDATGKVVIPGLIQGHIHLcQTLFRG--IADDLEl 79
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 66472750 91 -----------------QGTKAA--------LAGGTTMIVDH 107
Cdd:PRK07228 80 ldwlkdriwpleaahdaESMYYSallgigelIESGTTTIVDM 121
|
|
| PRK07627 |
PRK07627 |
dihydroorotase; Provisional |
16-456 |
1.76e-10 |
|
dihydroorotase; Provisional
Pssm-ID: 181059 [Multi-domain] Cd Length: 425 Bit Score: 63.16 E-value: 1.76e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472750 16 RLLIKGGRIVN-----DDQsfyADIYMEDGVIKQIGDnliVPGGV---KTIEANGKMVIPGGIDIHTHLQMP---FRGTT 84
Cdd:PRK07627 2 KIHIKGGRLIDpaagtDRQ---ADLYVAAGKIAAIGQ---APAGFnadKTIDASGLIVCPGLVDLSARLREPgyeYKATL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472750 85 TADdftqgTKAALAGGTTMIV-----DHVIPEPGcsLLEAFDRWSKWADEKaccdyslHV-DITHWNDSVKQEVET---L 155
Cdd:PRK07627 76 ESE-----MAAAVAGGVTSLVcppdtDPVLDEPG--LVEMLKFRARNLNQA-------HVyPLGALTVGLKGEVLTemvE 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472750 156 IKEKGVNSF-QVYMAFKDL------YQMSNTELYEVF-----TFLGEHGgiaqvHAENGEIIAeeqarmlEMGITGPegh 223
Cdd:PRK07627 142 LTEAGCVGFsQANVPVVDTqvllraLQYASTFGFTVWlrpldAFLGRGG-----VAASGAVAS-------RLGLSGV--- 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472750 224 vlsrPEELEAEAVFRAVTIASQTNCPLYVTRVMSKSAADIISQARKKgnvvfGEPITASLGTDGTH-------YWSKNwa 296
Cdd:PRK07627 207 ----PVAAETIALHTIFELMRVTGARVHLARLSSAAGVALVRAAKAE-----GLPVTCDVGVNHVHlidvdigYFDSQ-- 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472750 297 kaasFVTSPPLSpDPTTPDYLNTLLASGDLSVVGSAHctfsvaqKAIGKDD----FTQIPEGVNGAEERMSIIWDKAVVT 372
Cdd:PRK07627 276 ----FRLDPPLR-SQRDREAIRAALADGTIDAICSDH-------TPVDDDEkllpFAEATPGATGLELLLPLTLKWADEA 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472750 373 GKMDENMFVAVTStNAAKILNLypRKGRIAVGSDSDLVIWDTDAVRTITAKTHHSAAEYNVFEGMELRGAPMLVVCQGKI 452
Cdd:PRK07627 344 KVPLARALARITS-APARVLGL--PAGRLAEGAPADLCVFDPDAHWRVEPRALKSQGKNTPFLGYELPGRVRATLVAGQV 420
|
....
gi 66472750 453 VLED 456
Cdd:PRK07627 421 AFER 424
|
|
| COG3653 |
COG3653 |
N-acyl-D-aspartate/D-glutamate deacylase [Secondary metabolites biosynthesis, transport and ... |
17-75 |
4.37e-10 |
|
N-acyl-D-aspartate/D-glutamate deacylase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442870 [Multi-domain] Cd Length: 528 Bit Score: 62.11 E-value: 4.37e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 66472750 17 LLIKGGRIVN--DDQSFYADIYMEDGVIKQIGDnLIVPGGVKTIEANGKMVIPGGIDIHTH 75
Cdd:COG3653 4 LLIRGGTVVDgtGAPPFRADVAIKGGRIVAVGD-LAAAEAARVIDATGLVVAPGFIDIHTH 63
|
|
| NagA |
cd00854 |
N-acetylglucosamine-6-phosphate deacetylase, NagA, catalyzes the hydrolysis of the N-acetyl ... |
17-415 |
7.47e-10 |
|
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: 61.06 E-value: 7.47e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472750 17 LLIKGGRIVNDDQSFYADIYMEDGVIKQIGDNLIVPGGVKTIEANGKMVIPGGIDIHTHlqmpfrGTTTAdDFTQGTkaa 96
Cdd:cd00854 1 LIIKNARILTPGGLEDGAVLVEDGKIVAIGPEDELEEADEIIDLKGQYLVPGFIDIHIH------GGGGA-DFMDGT--- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472750 97 laggttmivdhvipepgcslLEAFDRWSkwadekaccdyslhvdithwndsvkqevETLIKEkGVNSFqvymaFKDLYQM 176
Cdd:cd00854 71 --------------------AEALKTIA----------------------------EALAKH-GTTSF-----LPTTVTA 96
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472750 177 SNTELYEVFTFLGEHG------GIAQVHAEnGEIIAEEQArmlemgitG--PEGHVLS-RPEELE-----AEAVFRAVTI 242
Cdd:cd00854 97 PPEEIAKALAAIAEAIaegqgaEILGIHLE-GPFISPEKK--------GahPPEYLRApDPEELKkwleaAGGLIKLVTL 167
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472750 243 ASQTncplyvtrvmsKSAADIISQARKKGnvvfgepITASLG-TDGTHYWSKNWAKA-ASFVT------SPPLSPDPTtp 314
Cdd:cd00854 168 APEL-----------DGALELIRYLVERG-------IIVSIGhSDATYEQAVAAFEAgATHVThlfnamSPLHHREPG-- 227
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472750 315 dYLNTLLASGDLSV------VGSAHCTFSVAQKAIGKDDFTQI---------PEGVNGAEERMSIIWDKAVV-------- 371
Cdd:cd00854 228 -VVGAALSDDDVYAeliadgIHVHPAAVRLAYRAKGADKIVLVtdamaaaglPDGEYELGGQTVTVKDGVARladgtlag 306
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 66472750 372 -TGKMDE---NMF----------VAVTSTNAAKILNLYPRKGRIAVGSDSDLVIWDTD 415
Cdd:cd00854 307 sTLTMDQavrNMVkwggcpleeaVRMASLNPAKLLGLDDRKGSLKPGKDADLVVLDDD 364
|
|
| D-aminoacylase |
cd01297 |
D-aminoacylases (N-acyl-D-Amino acid amidohydrolases) catalyze the hydrolysis of ... |
17-457 |
9.94e-10 |
|
D-aminoacylases (N-acyl-D-Amino acid amidohydrolases) catalyze the hydrolysis of N-acyl-D-amino acids to produce the corresponding D-amino acids, which are used as intermediates in the synthesis of pesticides, bioactive peptides, and antibiotics.
Pssm-ID: 238622 [Multi-domain] Cd Length: 415 Bit Score: 60.77 E-value: 9.94e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472750 17 LLIKGGRIVndDQS----FYADIYMEDGVIKQIGDNLIVPGgVKTIEANGKMVIPGGIDIHTHLQMPFrgtttaddFTQG 92
Cdd:cd01297 2 LVIRNGTVV--DGTgappFTADVGIRDGRIAAIGPILSTSA-REVIDAAGLVVAPGFIDVHTHYDGQV--------FWDP 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472750 93 TKAALA--GGTTMIV----------DHVIPEPGCSLLEAFD--------RWSKWAD-----EKA--CCDYSLHV-----D 140
Cdd:cd01297 71 DLRPSSrqGVTTVVLgncgvspapaNPDDLARLIMLMEGLValgeglpwGWATFAEyldalEARppAVNVAALVghaalR 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472750 141 ITHWNDSVKQ----EVETLIK--EKGVNS----FQVYMAFKDLYQMSNTELYEVFTFLGEHGGIAQVHAEN-GEIIAEEQ 209
Cdd:cd01297 151 RAVMGLDAREateeELAKMREllREALEAgalgISTGLAYAPRLYAGTAELVALARVAARYGGVYQTHVRYeGDSILEAL 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472750 210 ARMLEMG-ITGpeghvlsrpeeleaeavfRAVTIASQTNCPLYVTRVMSKSAADIISQARKKGNVVFGE-PITASLGTDg 287
Cdd:cd01297 231 DELLRLGrETG------------------RPVHISHLKSAGAPNWGKIDRLLALIEAARAEGLQVTADVyPYGAGSEDD- 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472750 288 thywsknwakAASFVTSPplspdpttpdylnTLLASGDLSVVGSAHC------TFSVAQKAIGKDDFTqIPEGVngaeER 361
Cdd:cd01297 292 ----------VRRIMAHP-------------VVMGGSDGGALGKPHPrsygdfTRVLGHYVRERKLLS-LEEAV----RK 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472750 362 MsiiwdkavvTGKmdenmfvavtstnAAKILNLYPRkGRIAVGSDSDLVIWDTDAVR---TITAKTHHSaaeynvfEGME 438
Cdd:cd01297 344 M---------TGL-------------PARVFGLADR-GRIAPGYRADIVVFDPDTLAdraTFTRPNQPA-------EGIE 393
|
490
....*....|....*....
gi 66472750 439 lrgapmLVVCQGKIVLEDG 457
Cdd:cd01297 394 ------AVLVNGVPVVRDG 406
|
|
| PRK09061 |
PRK09061 |
D-glutamate deacylase; Validated |
16-467 |
1.37e-09 |
|
D-glutamate deacylase; Validated
Pssm-ID: 236369 [Multi-domain] Cd Length: 509 Bit Score: 60.48 E-value: 1.37e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472750 16 RLLIKGGRIVNDDQSFYA--DIYMEDGVIKQIGDNLIvpGGVKTIEANGKMVIPGGIDIHTHLQMP-------FRGTTTA 86
Cdd:PRK09061 20 DLVIRNGRVVDPETGLDAvrDVGIKGGKIAAVGTAAI--EGDRTIDATGLVVAPGFIDLHAHGQSVaayrmqaFDGVTTA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472750 87 DDFTQGT--------KAALAG-----GTT-------MIVDHVIPEPGC--SLLEAFDRwSKWADEKAccdyslhvdithw 144
Cdd:PRK09061 98 LELEAGVlpvarwyaEQAGEGrplnyGASvgwtparIAVLTGPQAEGTiaDFGKALGD-PRWQERAA------------- 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472750 145 NDSVKQEVETLIkEKGVNSFQVYMAFKDLY--QMSNTELYEVFTFLGEHGGIAQVHAEngeiiaeeqarmlEMGITGPEG 222
Cdd:PRK09061 164 TPAELAEILELL-EQGLDEGALGIGIGAGYapGTGHKEYLELARLAARAGVPTYTHVR-------------YLSNVDPRS 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472750 223 HVlsrpeeleaEAVFRAVTIASQTNCPLYVTRVMSKSAADI------ISQARKKGNVVFGE--PITAS---LGTD----- 286
Cdd:PRK09061 230 SV---------DAYQELIAAAAETGAHMHICHVNSTSLRDIdrclalVEKAQAQGLDVTTEayPYGAGstvVGAAffdpg 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472750 287 -----GTHYWSKNWAKA------------------ASFVTSPPLSPD-PTTPDYLNTLLASGDLSVVGSAHCTFSVAQKA 342
Cdd:PRK09061 301 wlermGLGYGSLQWVETgerlltreelaklrandpGGLVLIHFLDEDnPRDRALLDRSVLFPGAAIASDAMPWTWSDGTV 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472750 343 IGKDDFTQIPEGV-----NGA---------EERMSIIWDKAVvtGKMdenmfvavtSTNAAKILNLY----PRKGRIAVG 404
Cdd:PRK09061 381 YEGDAWPLPEDAVshprsAGTfarflreyvRERKALSLLEAI--RKC---------TLMPAQILEDSvpamRRKGRLQAG 449
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 66472750 405 SDSDLVIWDTDAVR---TITAKTHHSAaeynvfegmelrGAPMLVVcQGKIVLEDGNLHATSGTGR 467
Cdd:PRK09061 450 ADADIVVFDPETITdraTFEDPNRPSE------------GVRHVLV-NGVPVVSNGELVRDARPGR 502
|
|
| PRK07369 |
PRK07369 |
dihydroorotase; Provisional |
33-441 |
8.11e-09 |
|
dihydroorotase; Provisional
Pssm-ID: 236002 [Multi-domain] Cd Length: 418 Bit Score: 57.69 E-value: 8.11e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472750 33 ADIYMEDGVIKQIGDNLI-VPGGVKTIEANGKMVIPGGIDIHTHLQMPfrGTTTADDFTQGTKAALAGGTTMIVdhVIP- 110
Cdd:PRK07369 22 ADVLIEDGKIQAIEPHIDpIPPDTQIIDASGLILGPGLVDLYSHSGEP--GFEERETLASLAAAAAAGGFTRVA--ILPd 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472750 111 -EPGCSLLEAFDRWSKWADEKAccdySLHVD----ITHwNDSVKQ--EVETLIkEKGVNSFQVYMAFKDLyqmsnTELYE 183
Cdd:PRK07369 98 tFPPLDNPATLARLQQQAQQIP----PVQLHfwgaLTL-GGQGKQltELAELA-AAGVVGFTDGQPLENL-----ALLRR 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472750 184 VFTFLGEHGGIAQVHAEN----GEIIAEEQARMLEMGITGpeghvlsRPEELEAEAVFRAVTIASQTNCPLYVTRVMSKS 259
Cdd:PRK07369 167 LLEYLKPLGKPVALWPCDrslaGNGVMREGLLALRLGLPG-------DPASAETTALAALLELVAAIGTPVHLMRISTAR 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472750 260 AADIISQARKKGnvvfgEPITAS-------LGTDGTHYWSKNWAKAasfvtsPPLSpdptTPDYLNTLLA---SGDLSVV 329
Cdd:PRK07369 240 SVELIAQAKARG-----LPITASttwmhllLDTEALASYDPNLRLD------PPLG----NPSDRQALIEgvrTGVIDAI 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472750 330 GSAHCTFSVAQKAIGkddFTQIPEGVNGAEERMSIIWDKAVVTGKMDENMFVAVTSTNAAKILNLYPRkgRIAVGSDSDL 409
Cdd:PRK07369 305 AIDHAPYTYEEKTVA---FAEAPPGAIGLELALPLLWQNLVETGELSALQLWQALSTNPARCLGQEPP--SLAPGQPAEL 379
|
410 420 430
....*....|....*....|....*....|..
gi 66472750 410 VIWDTDAVRTITAKTHHSAAEYNVFEGMELRG 441
Cdd:PRK07369 380 ILFDPQKTWTVSAQTLHSLSRNTPWLGQTLKG 411
|
|
| metallo-dependent_hydrolases |
cd01292 |
Superfamily of metallo-dependent hydrolases (also called amidohydrolase superfamily) is a ... |
70-287 |
8.76e-09 |
|
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: 56.96 E-value: 8.76e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472750 70 IDIHTHLQMP----------------FRGTTTADDFTQGTKAALAGGTTMIVDHVIPEPGCSLLEAFDRWSKWADEKACC 133
Cdd:cd01292 2 IDTHVHLDGSalrgtrlnlelkeaeeLSPEDLYEDTLRALEALLAGGVTTVVDMGSTPPPTTTKAAIEAVAEAARASAGI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472750 134 DYSLHVDITHWNDSVKQEVETLIKE---KGVNSFQVYMAFKDLYQMSNT---ELYEVFTFLGEHGGIAQVHAENGEIIAE 207
Cdd:cd01292 82 RVVLGLGIPGVPAAVDEDAEALLLEllrRGLELGAVGLKLAGPYTATGLsdeSLRRVLEEARKLGLPVVIHAGELPDPTR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472750 208 EQARMLEMGITGPE---GHVLSRPEELEAEAVFRAVTIASqtnCPLYVTRVMSKS-AADIISQARKKGNVVfgepitaSL 283
Cdd:cd01292 162 ALEDLVALLRLGGRvviGHVSHLDPELLELLKEAGVSLEV---CPLSNYLLGRDGeGAEALRRLLELGIRV-------TL 231
|
....
gi 66472750 284 GTDG 287
Cdd:cd01292 232 GTDG 235
|
|
| FwdA |
COG1229 |
Formylmethanofuran dehydrogenase subunit A [Energy production and conversion]; |
17-75 |
4.53e-08 |
|
Formylmethanofuran dehydrogenase subunit A [Energy production and conversion];
Pssm-ID: 440842 Cd Length: 554 Bit Score: 55.97 E-value: 4.53e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 66472750 17 LLIKGGRI------VNDDQsfyADIYMEDGvikQIGDNLIVPGGVKTIEANGKMVIPGGIDIHTH 75
Cdd:COG1229 3 LIIKNGRVydpangIDGEV---MDIAIKDG---KIVEEPSDPKDAKVIDASGKVVMAGGVDIHTH 61
|
|
| NagA |
COG1820 |
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism]; |
18-75 |
4.92e-08 |
|
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism];
Pssm-ID: 441425 [Multi-domain] Cd Length: 373 Bit Score: 55.11 E-value: 4.92e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 66472750 18 LIKGGRIVNDDQSFY-ADIYMEDGVIKQIGDNliVPGGVKTIEANGKMVIPGGIDIHTH 75
Cdd:COG1820 1 AITNARIFTGDGVLEdGALLIEDGRIAAIGPG--AEPDAEVIDLGGGYLAPGFIDLHVH 57
|
|
| Met_dep_hydrolase_B |
cd01307 |
Metallo-dependent hydrolases, subgroup B is part of the superfamily of metallo-dependent ... |
34-414 |
8.47e-08 |
|
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: 54.26 E-value: 8.47e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472750 34 DIYMEDGVIKQIGDNLIVPGGVKTIEANGKMVIPGGIDIHTHLQmpFRGTTTADDFTQgtkAALAGGTTMIVDHviPEPG 113
Cdd:cd01307 1 DVAIENGKIAAVGAALAAPAATQIVDAGGCYVSPGWIDLHVHVY--QGGTRYGDRPDM---IGVKSGVTTVVDA--GSAG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472750 114 CSLLEAFDRWskwadekaccdyslhvdITHwndSVKQEVETLIKEkgvnSFQVYMAFKDLYQMSNTELYEVFTFLgehgg 193
Cdd:cd01307 74 ADNIDGFRYT-----------------VIE---RSATRVYAFLNI----SRVGLVAQDELPDPDNIDEDAVVAAA----- 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472750 194 iaqvhAENGEIIAEEQARMlEMGITGPEGhvlSRPEELEAEavfravtIASQTNCPLYvtrVMSKSAADIISQA---RKK 270
Cdd:cd01307 125 -----REYPDVIVGLKARA-SKSVVGEWG---IKPLELAKK-------IAKEADLPLM---VHIGSPPPILDEVvplLRR 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472750 271 GNVVfgepitaslgtdgTHYWSknwAKAASFVTSpplspdptTPDYLNTLLASGDLSVV-----GSAHCTFSVAQKAIGK 345
Cdd:cd01307 186 GDVL-------------THCFN---GKPNGIVDE--------EGEVLPLVRRARERGVIfdvghGTASFSFRVARAAIAA 241
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 66472750 346 DDFTQI-------PEGVNGAEERMSIIWDKAVVTGKMDENMFVAVTsTNAAKILNLyPRKGRIAVGSDSDLVIWDT 414
Cdd:cd01307 242 GLLPDTissdihgRNRTNGPVYALATTLSKLLALGMPLEEVIEAVT-ANPARMLGL-AEIGTLAVGYDADLTVFDL 315
|
|
| PRK08417 |
PRK08417 |
metal-dependent hydrolase; |
35-455 |
2.73e-07 |
|
metal-dependent hydrolase;
Pssm-ID: 236262 [Multi-domain] Cd Length: 386 Bit Score: 52.78 E-value: 2.73e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472750 35 IYMEDGVIKQIGDNLivpGGVKTIEANGKMVIPGGIDIHTHlqmPFRGTTTADDFTQGTKAALAGGttmiVDHVIPEPGC 114
Cdd:PRK08417 1 IRIKDGKITEIGSDL---KGEEILDAKGKTLLPALVDLNVS---LKNDSLSSKNLKSLENECLKGG----VGSIVLYPDS 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472750 115 slleafdrwskwadEKACCD-YSLHVDithwndsvkqevETLIKEKGVNSFQVYMAFKDlyqmsNTELYEVFTFLgEHGG 193
Cdd:PRK08417 71 --------------TPAIDNeIALELI------------NSAQRELPMQIFPSIRALDE-----DGKLSNIATLL-KKGA 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472750 194 IAqVHAE-----NGEIIAEEQARMLEM-------------------GITGPEGHVLSRPEELEAEAVFRAVTIASQTNCP 249
Cdd:PRK08417 119 KA-LELSsdldaNLLKVIAQYAKMLDVpifcrcedssfddsgvmndGELSFELGLPGIPSIAETKEVAKMKELAKFYKNK 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472750 250 LYVTRVMSKSAADIISQARKKGNVVFGEPITASLGTDGTHywSKNWAKAASFvtSPPLSpDPTTPDYLNTLLASGDLSVV 329
Cdd:PRK08417 198 VLFDTLALPRSLELLDKFKSEGEKLLKEVSIHHLILDDSA--CENFNTAAKL--NPPLR-SKEDRLALLEALKEGKIDFL 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472750 330 GSAHCTFSVAQKAIGkddFTQIPEGVNGAEERMSIIWDKAVVTGKMDENMFVAVTSTNAAKILNLypRKGRIAVGSDSDL 409
Cdd:PRK08417 273 TSLHSAKSNSKKDLA---FDEAAFGIDSICEYFSLCYTYLVKEGIITWSELSRFTSYNPAQFLGL--NSGEIEVGKEADL 347
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 66472750 410 VIWDTDAvRTITAKThhsaaeYNVFEGMELRGAPMLVVCQGKIVLE 455
Cdd:PRK08417 348 VLFDPNE-STIIDDN------FSLYSGDELYGKIEAVIIKGKLYLE 386
|
|
| Bact_CD |
cd01293 |
Bacterial cytosine deaminase and related metal-dependent hydrolases. Cytosine deaminases (CDs) ... |
12-128 |
3.16e-07 |
|
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: 52.63 E-value: 3.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472750 12 ITSERLLIKGGRIVnddqsfyaDIYMEDGVIKQIGDNLIVPGGVKTIEANGKMVIPGGIDIHTHL--------QMPFRGT 83
Cdd:cd01293 2 LRNARLADGGTALV--------DIAIEDGRIAAIGPALAVPPDAEEVDAKGRLVLPAFVDPHIHLdktftggrWPNNSGG 73
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472750 84 T---------------TADDFTQ----GTKAALAGGTTMI-----VDHVIPEPGCS-LLEAFDRWSKWAD 128
Cdd:cd01293 74 TlleaiiaweerklllTAEDVKEraerALELAIAHGTTAIrthvdVDPAAGLKALEaLLELREEWADLID 143
|
|
| PRK08393 |
PRK08393 |
N-ethylammeline chlorohydrolase; Provisional |
17-88 |
9.46e-07 |
|
N-ethylammeline chlorohydrolase; Provisional
Pssm-ID: 181411 [Multi-domain] Cd Length: 424 Bit Score: 51.34 E-value: 9.46e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 66472750 17 LLIKGGRIVNDD--QSFYADIYMEDGVIKQIGDNLIVPGGvKTIEANGKMVIPGGIDIHTHLQMP-FRGttTADD 88
Cdd:PRK08393 3 ILIKNGYVIYGEnlKVIRADVLIEGNKIVEVKRNINKPAD-TVIDASGSVVSPGFINAHTHSPMVlLRG--LADD 74
|
|
| PRK08204 |
PRK08204 |
hypothetical protein; Provisional |
15-112 |
1.15e-06 |
|
hypothetical protein; Provisional
Pssm-ID: 181288 [Multi-domain] Cd Length: 449 Bit Score: 51.16 E-value: 1.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472750 15 ERLLIKGGRIVNDDQSF----YADIYMEDGVIKQIGDNlIVPGGVKTIEANGKMVIPGGIDIHTHL-QMPFRGTTTADDF 89
Cdd:PRK08204 2 KRTLIRGGTVLTMDPAIgdlpRGDILIEGDRIAAVAPS-IEAPDAEVVDARGMIVMPGLVDTHRHTwQSVLRGIGADWTL 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 66472750 90 TQ------------------------GTKAALAGGTTMIVD--HVIPEP 112
Cdd:PRK08204 81 QTyfreihgnlgpmfrpedvyianllGALEALDAGVTTLLDwsHINNSP 129
|
|
| PRK15446 |
PRK15446 |
phosphonate metabolism protein PhnM; Provisional |
16-244 |
3.83e-06 |
|
phosphonate metabolism protein PhnM; Provisional
Pssm-ID: 237967 [Multi-domain] Cd Length: 383 Bit Score: 49.41 E-value: 3.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472750 16 RLLIKGGRIVNDDQSFYADIYMEDGVIKQIGDNLIVPGGvkTIEANGKMVIPGGIDIHT-----HLQ------MPFRGTT 84
Cdd:PRK15446 3 EMILSNARLVLPDEVVDGSLLIEDGRIAAIDPGASALPG--AIDAEGDYLLPGLVDLHTdnlekHLAprpgvdWPADAAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472750 85 TADDftqgTKAALAGGTTM----------IVDHVIPEPGCSLLEAFDRWSkwADEKACCDYSLH--VDITHwnDSVKQEV 152
Cdd:PRK15446 81 AAHD----AQLAAAGITTVfdalsvgdeeDGGLRSRDLARKLIDAIEEAR--ARGLLRADHRLHlrCELTN--PDALELF 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472750 153 ETLIKEKGVNsfqvYMAFKD----LYQMSNTELYEvfTFLGEHGGIAqvHAENGEIIAEEQARMlemgitgpEGHVLSRP 228
Cdd:PRK15446 153 EALLAHPRVD----LVSLMDhtpgQRQFRDLEKYR--EYYAGKYGLS--DEEFDAFVEERIALS--------ARYAPPNR 216
|
250
....*....|....*.
gi 66472750 229 EELEAEAVFRAVTIAS 244
Cdd:PRK15446 217 RAIAALARARGIPLAS 232
|
|
| NagA |
COG1820 |
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism]; |
381-415 |
5.91e-06 |
|
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism];
Pssm-ID: 441425 [Multi-domain] Cd Length: 373 Bit Score: 48.56 E-value: 5.91e-06
10 20 30
....*....|....*....|....*....|....*
gi 66472750 381 VAVTSTNAAKILNLYPRKGRIAVGSDSDLVIWDTD 415
Cdd:COG1820 328 VRMASLNPARALGLDDRKGSIAPGKDADLVVLDDD 362
|
|
| AdeC |
COG1001 |
Adenine deaminase [Nucleotide transport and metabolism]; |
17-86 |
1.05e-05 |
|
Adenine deaminase [Nucleotide transport and metabolism];
Pssm-ID: 440625 [Multi-domain] Cd Length: 559 Bit Score: 48.17 E-value: 1.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472750 17 LLIKGGRIVN--DDQSFYADIYMEDGVIKQIGDnlIVPGGVKTIEANGKMVIPGGIDIHTHL--QM--PF--------RG 82
Cdd:COG1001 7 LVIKNGRLVNvfTGEILEGDIAIAGGRIAGVGD--YIGEATEVIDAAGRYLVPGFIDGHVHIesSMvtPAefaravlpHG 84
|
....
gi 66472750 83 TTTA 86
Cdd:COG1001 85 TTTV 88
|
|
| YtcJ |
COG1574 |
Predicted amidohydrolase YtcJ [General function prediction only]; |
17-89 |
1.23e-05 |
|
Predicted amidohydrolase YtcJ [General function prediction only];
Pssm-ID: 441182 [Multi-domain] Cd Length: 535 Bit Score: 47.87 E-value: 1.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472750 17 LLIKGGRI--VNDDQSFYADIYMEDGVIKQIGDN----LIVPGGVKTIEANGKMVIPGGIDIHTHLQM--------PFRG 82
Cdd:COG1574 10 LLLTNGRIytMDPAQPVAEAVAVRDGRIVAVGSDaevrALAGPATEVIDLGGKTVLPGFIDAHVHLLGgglallgvDLSG 89
|
....*..
gi 66472750 83 TTTADDF 89
Cdd:COG1574 90 ARSLDEL 96
|
|
| Amidohydro_3 |
pfam07969 |
Amidohydrolase family; |
381-436 |
1.78e-05 |
|
Amidohydrolase family;
Pssm-ID: 400360 [Multi-domain] Cd Length: 464 Bit Score: 47.53 E-value: 1.78e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 66472750 381 VAVTSTNAAKILNLYPRKGRIAVGSDSDLVIWDTDAVRTITAKTHHSAAEYNVFEG 436
Cdd:pfam07969 405 LALYTSGPAKALGLEDRKGTLGVGKDADLVVLDDDPLTVDPPAIADIRVRLTVVDG 460
|
|
| FMDH_A |
cd01304 |
Formylmethanofuran dehydrogenase (FMDH) subunit A; Methanogenic bacteria and archea derive ... |
19-75 |
2.26e-05 |
|
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: 47.02 E-value: 2.26e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472750 19 IKGGRIVNDDQSFYA---DIYMEDGvikQIGDNLIVPGGVKTIEANGKMVIPGGIDIHTH 75
Cdd:cd01304 1 IKNGTVYDPLNGINGekmDIFIRDG---KIVESSSGAKPAKVIDASGKVVMAGGVDMHSH 57
|
|
| ureC |
PRK13308 |
urease subunit alpha; Reviewed |
19-104 |
4.25e-05 |
|
urease subunit alpha; Reviewed
Pssm-ID: 183965 [Multi-domain] Cd Length: 569 Bit Score: 46.24 E-value: 4.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472750 19 IKGGRIVNDDQSFYADIyMeDGVikqiGDNLIVPGGVKTIEANGKMVIPGGIDIHTHLQMPfrgtttaddftQGTKAALA 98
Cdd:PRK13308 91 IRDGRIVGIGKAGNPDI-M-DGV----DPRLVVGPGTDVRPAEGLIATPGAIDVHVHFDSA-----------QLVDHALA 153
|
....*..
gi 66472750 99 GG-TTMI 104
Cdd:PRK13308 154 SGiTTML 160
|
|
| PRK06380 |
PRK06380 |
metal-dependent hydrolase; Provisional |
17-88 |
4.26e-05 |
|
metal-dependent hydrolase; Provisional
Pssm-ID: 180548 [Multi-domain] Cd Length: 418 Bit Score: 46.03 E-value: 4.26e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 66472750 17 LLIKGGRIVNDDQS---FYADIYMEDGVIKQIGDnlIVPGGVKTIEANGKMVIPGGIDIHTHLQMP-FRGttTADD 88
Cdd:PRK06380 3 ILIKNAWIVTQNEKreiLQGNVYIEGNKIVYVGD--VNEEADYIIDATGKVVMPGLINTHAHVGMTaSKG--LFDD 74
|
|
| PRK07583 |
PRK07583 |
cytosine deaminase; |
33-76 |
4.39e-05 |
|
cytosine deaminase;
Pssm-ID: 236062 Cd Length: 438 Bit Score: 46.13 E-value: 4.39e-05
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 66472750 33 ADIYMEDGVIKQIGDNLIVPGGVKTIEANGKMVIPGGIDIHTHL 76
Cdd:PRK07583 41 VDIEIADGKIAAILPAGGAPDELPAVDLKGRMVWPCFVDMHTHL 84
|
|
| Urease_alpha |
cd00375 |
Urease alpha-subunit; Urease is a nickel-dependent metalloenzyme that catalyzes the hydrolysis ... |
33-104 |
4.65e-05 |
|
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: 46.17 E-value: 4.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472750 33 ADIYMEDGVIKQIG------------DNLIVPGGVKTIEANGKMVIPGGIDIHTHLQMPfrgtttaddftQGTKAALAGG 100
Cdd:cd00375 83 ADIGIKDGRIVAIGkagnpdimdgvtPNMIVGPSTEVIAGEGKIVTAGGIDTHVHFICP-----------QQIEEALASG 151
|
....*
gi 66472750 101 -TTMI 104
Cdd:cd00375 152 iTTMI 156
|
|
| PRK05985 |
PRK05985 |
cytosine deaminase; Provisional |
33-119 |
8.89e-05 |
|
cytosine deaminase; Provisional
Pssm-ID: 180337 [Multi-domain] Cd Length: 391 Bit Score: 44.92 E-value: 8.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472750 33 ADIYMEDGVIKQIGDNLIVPGGVKTIEANGKMVIPGGIDIHTHLQ-----MPFRGTTTADDFTQGT-------------- 93
Cdd:PRK05985 17 VDILIRDGRIAAIGPALAAPPGAEVEDGGGALALPGLVDGHIHLDktfwgDPWYPNEPGPSLRERIanerrrraasghpa 96
|
90 100 110
....*....|....*....|....*....|....*.
gi 66472750 94 --------KAALAGGTTMIVDHVI--PEPGCSLLEA 119
Cdd:PRK05985 97 aeralalaRAAAAAGTTAMRSHVDvdPDAGLRHLEA 132
|
|
| PRK09059 |
PRK09059 |
dihydroorotase; Validated |
17-105 |
9.30e-05 |
|
dihydroorotase; Validated
Pssm-ID: 181631 [Multi-domain] Cd Length: 429 Bit Score: 45.03 E-value: 9.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472750 17 LLIKGGRIVNDDQSF--YADIYMEDGVIKQIGD---NLIVPGGVKTIEANGKMVIPGGIDIHTHLQMPfrGTTTADDFTQ 91
Cdd:PRK09059 5 ILLANARIIDPSRGLdeIGTVLIEDGVIVAAGKgagNQGAPEGAEIVDCAGKAVAPGLVDARVFVGEP--GAEHRETIAS 82
|
90
....*....|....
gi 66472750 92 GTKAALAGGTTMIV 105
Cdd:PRK09059 83 ASRAAAAGGVTSII 96
|
|
| PRK06038 |
PRK06038 |
N-ethylammeline chlorohydrolase; Provisional |
15-89 |
9.98e-05 |
|
N-ethylammeline chlorohydrolase; Provisional
Pssm-ID: 180363 [Multi-domain] Cd Length: 430 Bit Score: 45.13 E-value: 9.98e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 66472750 15 ERLLIKGGRIVNDDQSFY--ADIYMEDGVIKQIGDNliVPGGVKT-IEANGKMVIPGGIDIHTHLQMP-FRGttTADDF 89
Cdd:PRK06038 2 ADIIIKNAYVLTMDAGDLkkGSVVIEDGTITEVSES--TPGDADTvIDAKGSVVMPGLVNTHTHAAMTlFRG--YADDL 76
|
|
| Imidazolone-5PH |
cd01296 |
Imidazolonepropionase/imidazolone-5-propionate hydrolase (Imidazolone-5PH) catalyzes the third ... |
35-76 |
1.80e-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: 1.80e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 66472750 35 IYMEDGVIKQIGD----NLIVPGGVKTIEANGKMVIPGGIDIHTHL 76
Cdd:cd01296 1 IAIRDGRIAAVGPaaslPAPGPAAAEEIDAGGRAVTPGLVDCHTHL 46
|
|
| Met_dep_hydrolase_C |
cd01309 |
Metallo-dependent hydrolases, subgroup C is part of the superfamily of metallo-dependent ... |
368-415 |
6.82e-04 |
|
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: 42.30 E-value: 6.82e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 66472750 368 KAVVTGKMDENMFVAVTStNAAKILNLYPRKGRIAVGSDSDLVIWDTD 415
Cdd:cd01309 294 KAVKYGLSYEEALKAITI-NPAKILGIEDRVGSLEPGKDADLVVWNGD 340
|
|
| PRK07203 |
PRK07203 |
putative aminohydrolase SsnA; |
17-76 |
7.04e-04 |
|
putative aminohydrolase SsnA;
Pssm-ID: 235963 [Multi-domain] Cd Length: 442 Bit Score: 42.23 E-value: 7.04e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 66472750 17 LLIKGGRIV-NDDQSFY---ADIYMEDGVIKQIGDNlivpGGVKT-------IEANGKMVIPGGIDIHTHL 76
Cdd:PRK07203 2 LLIGNGTAItRDPAKPViedGAIAIEGNVIVEIGTT----DELKAkypdaefIDAKGKLIMPGLINSHNHI 68
|
|
| Met_dep_hydrolase_C |
cd01309 |
Metallo-dependent hydrolases, subgroup C is part of the superfamily of metallo-dependent ... |
39-78 |
7.45e-04 |
|
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: 41.91 E-value: 7.45e-04
10 20 30 40
....*....|....*....|....*....|....*....|
gi 66472750 39 DGVIKQIGDNLIVPGGVKTIEANGKMVIPGGIDIHTHLQM 78
Cdd:cd01309 1 DGKIVAVGAEITTPADAEVIDAKGKHVTPGLIDAHSHLGL 40
|
|
| Amidohydro_3 |
pfam07969 |
Amidohydrolase family; |
56-76 |
7.54e-04 |
|
Amidohydrolase family;
Pssm-ID: 400360 [Multi-domain] Cd Length: 464 Bit Score: 42.13 E-value: 7.54e-04
|
| ureB |
PRK13985 |
urease subunit alpha; |
5-104 |
7.84e-04 |
|
urease subunit alpha;
Pssm-ID: 184438 [Multi-domain] Cd Length: 568 Bit Score: 42.19 E-value: 7.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472750 5 GKKNIPKITSERLLIKGGRIVNDDQSFYADIYMEDGVIKQIG------------DNLIVPGGVKTIEANGKMVIPGGIDI 72
Cdd:PRK13985 55 SQSNNPSKEELDLIITNALIIDYTGIYKADIGIKDGKIAGIGkggnkdmqdgvkNNLSVGPATEALAGEGLIVTAGGIDT 134
|
90 100 110
....*....|....*....|....*....|..
gi 66472750 73 HTHLQMPfrgtttaddfTQGTKAALAGGTTMI 104
Cdd:PRK13985 135 HIHFISP----------QQIPTAFASGVTTMI 156
|
|
| Imidazolone-5PH |
cd01296 |
Imidazolonepropionase/imidazolone-5-propionate hydrolase (Imidazolone-5PH) catalyzes the third ... |
369-415 |
1.06e-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: 41.47 E-value: 1.06e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 66472750 369 AVVTGKMDENMFVAVTSTNAAKILNLYPRKGRIAVGSDSDLVIWDTD 415
Cdd:cd01296 304 ACRLMRMTPEEALTAATINAAAALGLGETVGSLEVGKQADLVILDAP 350
|
|
| ureC |
PRK13206 |
urease subunit alpha; Reviewed |
33-105 |
1.77e-03 |
|
urease subunit alpha; Reviewed
Pssm-ID: 237304 [Multi-domain] Cd Length: 573 Bit Score: 41.23 E-value: 1.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472750 33 ADIYMEDGVIKQIG------------DNLIVPGGVKTIEANGKMVIPGGIDIHTHLQMPfrgtttaddftQGTKAALAGG 100
Cdd:PRK13206 89 ADVGIRDGRIVAIGkagnpdimdgvhPDLVIGPSTEIIAGNGRILTAGAIDCHVHFICP-----------QIVDEALAAG 157
|
....*
gi 66472750 101 TTMIV 105
Cdd:PRK13206 158 ITTLI 162
|
|
| ureC |
PRK13207 |
urease subunit alpha; Reviewed |
33-104 |
2.17e-03 |
|
urease subunit alpha; Reviewed
Pssm-ID: 237305 [Multi-domain] Cd Length: 568 Bit Score: 40.93 E-value: 2.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472750 33 ADIYMEDGVIKQIG--------DN--LIVPGGVKTIEANGKMVIPGGIDIHTHLQMPfrgtttaddftQGTKAALAGG-T 101
Cdd:PRK13207 85 ADIGIKDGRIVAIGkagnpdiqDGvdIIIGPGTEVIAGEGLIVTAGGIDTHIHFICP-----------QQIEEALASGvT 153
|
...
gi 66472750 102 TMI 104
Cdd:PRK13207 154 TMI 156
|
|
| YtcJ_like |
cd01300 |
YtcJ_like metal dependent amidohydrolases. YtcJ is a Bacillus subtilis ORF of unknown function. ... |
34-76 |
3.36e-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: 3.36e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 66472750 34 DIYMEDGVIKQIGDN----LIVPGGVKTIEANGKMVIPGGIDIHTHL 76
Cdd:cd01300 1 AVAVRDGRIVAVGSDaeakALKGPATEVIDLKGKTVLPGFIDSHSHL 47
|
|
| PRK06846 |
PRK06846 |
putative deaminase; Validated |
34-82 |
3.65e-03 |
|
putative deaminase; Validated
Pssm-ID: 235873 [Multi-domain] Cd Length: 410 Bit Score: 39.99 E-value: 3.65e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 66472750 34 DIYMEDGVIKQIGDNLIVP-GGVKTIEANGKMVIPGGIDIHTHLQMPFRG 82
Cdd:PRK06846 33 TLEIQDGKIVAIRPNKQVPdATLPTYDANGLLMLPAFREMHIHLDKTYYG 82
|
|
| Isoaspartyl-dipeptidase |
cd01308 |
Isoaspartyl dipeptidase hydrolyzes the beta-L-isoaspartyl linkages in dipeptides, as part of ... |
377-415 |
3.76e-03 |
|
Isoaspartyl dipeptidase hydrolyzes the beta-L-isoaspartyl linkages in dipeptides, as part of the degradative pathway to eliminate proteins with beta-L-isoaspartyl peptide bonds, bonds whereby the beta-group of an aspartate forms the peptide link with the amino group of the following amino acid. Formation of this bond is a spontaneous nonenzymatic reaction in nature and can profoundly effect the function of the protein. Isoaspartyl dipeptidase is an octameric enzyme that contains a binuclear zinc center in the active site of each subunit and shows a strong preference of hydrolyzing Asp-Leu dipeptides.
Pssm-ID: 238633 [Multi-domain] Cd Length: 387 Bit Score: 39.68 E-value: 3.76e-03
10 20 30
....*....|....*....|....*....|....*....
gi 66472750 377 ENMFVAVTStNAAKILNLYPrKGRIAVGSDSDLVIWDTD 415
Cdd:cd01308 325 EVALRVITS-NVARILKLRK-KGEIQPGFDADLVILDKD 361
|
|
| PRK08203 |
PRK08203 |
hydroxydechloroatrazine ethylaminohydrolase; Reviewed |
16-107 |
4.27e-03 |
|
hydroxydechloroatrazine ethylaminohydrolase; Reviewed
Pssm-ID: 236184 [Multi-domain] Cd Length: 451 Bit Score: 39.84 E-value: 4.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472750 16 RLLIKGGRIV---NDDQSFYAD--IYMEDGVIKQIGDNLIVPG-GVKTIEANGKMVIPGGIDIHTHL-QMPFRG------ 82
Cdd:PRK08203 2 TLWIKNPLAIvtmDAARREIADggLVVEGGRIVEVGPGGALPQpADEVFDARGHVVTPGLVNTHHHFyQTLTRAlpaaqd 81
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 66472750 83 -------TT--------TADDFTQGTKAALA----GGTTMIVDH 107
Cdd:PRK08203 82 aelfpwlTTlypvwarlTPEMVRVATQTALAelllSGCTTSSDH 125
|
|
| PRK12394 |
PRK12394 |
metallo-dependent hydrolase; |
17-106 |
6.66e-03 |
|
metallo-dependent hydrolase;
Pssm-ID: 183497 [Multi-domain] Cd Length: 379 Bit Score: 38.97 E-value: 6.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472750 17 LLIKGGRIvnddqsfyADIYMEDGVIKQIG--DNLIVP-------GGVKTIEANGKMVIPGGIDIHTHLqmPFRGTttaD 87
Cdd:PRK12394 5 ILITNGHI--------IDPARNINEINNLRiiNDIIVDadkypvaSETRIIHADGCIVTPGLIDYHAHV--FYDGT---E 71
|
90
....*....|....*....
gi 66472750 88 DFTQGTKAALAGGTTMIVD 106
Cdd:PRK12394 72 GGVRPDMYMPPNGVTTVVD 90
|
|
| FMDH_A |
cd01304 |
Formylmethanofuran dehydrogenase (FMDH) subunit A; Methanogenic bacteria and archea derive ... |
383-462 |
8.84e-03 |
|
Formylmethanofuran dehydrogenase (FMDH) subunit A; Methanogenic bacteria and archea derive the energy for autotrophic growth from methanogenesis, the reduction of CO2 with molecular hydrogen as the electron donor. FMDH catalyzes the first step in methanogenesis, the formyl-methanofuran synthesis. In this step, CO2 is bound to methanofuran and subsequently reduced to the formyl state with electrons derived from hydrogen.
Pssm-ID: 238629 [Multi-domain] Cd Length: 541 Bit Score: 38.93 E-value: 8.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472750 383 VTSTNAAKILNLyPRKGRIAVGSDSDLVIWDTDAvrtITAKTHHSAAEYNVFEGmelrgaPMLVVCQGKIVLEDGNLHAT 462
Cdd:cd01304 435 MTRAGPAKLLGL-SDKGHLGVGADADIAIYDDDP---DQVDPSDYEKVEKAFSR------AAYVLKDGEIVVKDGEVVAE 504
|
|
| |
