|
Name |
Accession |
Description |
Interval |
E-value |
| D-HYD |
cd01314 |
D-hydantoinases (D-HYD) also called dihydropyrimidases (DHPase) and related proteins; DHPases ... |
11-460 |
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: 616.54 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472778 11 ILIKGGRVVNDDVTEEADVYLENGRIQQVGRDLMIPGGAKVIDATGKLVIPGGIDSSVHLHQTFMNAHTQDDFYSGTKAA 90
Cdd:cd01314 1 LIIKNGTIVTADGSFKADILIEDGKIVAIGPNLEAPGGVEVIDATGKYVLPGGIDPHTHLELPFMGTVTADDFESGTRAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472778 91 LLGGSTMLISHVLPDRGASLLDAFEQMRAHADAKACCDYALHVGVTWWGPKVEREMEVLVgERGVNSFQMFMAYKDAMML 170
Cdd:cd01314 81 AAGGTTTIIDFAIPNKGQSLLEAVEKWRGKADGKSVIDYGFHMIITDWTDSVIEELPELV-KKGISSFKVFMAYKGLLMV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472778 171 KDSELYQALNTCKNIGAIARIHAENGELVLEGAKEALDLGISGPEGMEISRPEELEAEATHRAITIGNRAHCPVYLVNVS 250
Cdd:cd01314 160 DDEELLDVLKRAKELGALVMVHAENGDVIAELQKKLLAQGKTGPEYHALSRPPEVEAEATARAIRLAELAGAPLYIVHVS 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472778 251 SMSAADVIGAARMQGKVVQAETTVAHAVLSGmHYYHQDWAHAAAHVIAPPLRlDPNTPDHLIGLLGNDIINVVASDHRAF 330
Cdd:cd01314 240 SKEAADEIARARKKGLPVYGETCPQYLLLDD-SDYWKDWFEGAKYVCSPPLR-PKEDQEALWDGLSSGTLQTVGSDHCPF 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472778 331 STKQKAMGKEDFTKIPHGAPGVEDRMSVIWERGVVSGKMDENRFVAVTSSNAAKIYNLYPRKGRIMPGADADVVVWDPDA 410
Cdd:cd01314 318 NFAQKARGKDDFTKIPNGVPGVETRMPLLWSEGVAKGRITLEKFVELTSTNPAKIFGLYPRKGTIAVGSDADLVIWDPNA 397
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 66472778 411 TRTISASTQAQGGDFNLFEGQRCHGVPLVTISRGRLVCENGVFMCAQGSG 460
Cdd:cd01314 398 EKTISADTHHHNVDYNIFEGMKVKGWPVVTISRGKVVVEDGELVGEKGSG 447
|
|
| PRK08323 |
PRK08323 |
phenylhydantoinase; Validated |
9-469 |
0e+00 |
|
phenylhydantoinase; Validated
Pssm-ID: 236240 [Multi-domain] Cd Length: 459 Bit Score: 558.25 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472778 9 MRILIKGGRVVNDDVTEEADVYLENGRIQQVGRDlmipGGAKVIDATGKLVIPGGIDSSVHLHQTFMNAHTQDDFYSGTK 88
Cdd:PRK08323 1 MSTLIKNGTVVTADDTYKADVLIEDGKIAAIGAN----LGDEVIDATGKYVMPGGIDPHTHMEMPFGGTVSSDDFETGTR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472778 89 AALLGGSTMLISHVLPDRGASLLDAFEQMRAHADAKACCDYALHVGVTWWGPKVEREMEVLVgERGVNSFQMFMAYKDAM 168
Cdd:PRK08323 77 AAACGGTTTIIDFALQPKGQSLREALEAWHGKAAGKAVIDYGFHMIITDWNEVVLDEMPELV-EEGITSFKLFMAYKGAL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472778 169 MLKDSELYQALNTCKNIGAIARIHAENGELVLEGAKEALDLGISGPEGMEISRPEELEAEATHRAITIGNRAHCPVYLVN 248
Cdd:PRK08323 156 MLDDDELLRALQRAAELGALPMVHAENGDAIAYLQAKLLAEGKTGPEYHALSRPPEVEGEATNRAIMLAELAGAPLYIVH 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472778 249 VSSMSAADVIGAARMQGKVVQAETTVAHAVLSGMHYYHQDWAHAAAHVIAPPLRlDPNTPDHLIGLLGNDIINVVASDHR 328
Cdd:PRK08323 236 VSCKEALEAIRRARARGQRVFGETCPQYLLLDESEYDGPDWFEGAKYVMSPPLR-DKEHQDALWRGLQDGDLQVVATDHC 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472778 329 AFSTKQKAM-GKEDFTKIPHGAPGVEDRMSVIWERGVVSGKMDENRFVAVTSSNAAKIYNLYPRKGRIMPGADADVVVWD 407
Cdd:PRK08323 315 PFCFEQKKQlGRGDFTKIPNGTPGVEDRMPLLFSEGVMTGRITLNRFVELTSTNPAKIFGLYPRKGTIAVGADADIVIWD 394
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 66472778 408 PDATRTISASTQAQGGDFNLFEGQRCHGVPLVTISRGRLVCENGVFMCAQGSGKFYPMRAFP 469
Cdd:PRK08323 395 PNATKTISASTLHSNVDYNPYEGFEVTGWPVTTLSRGEVVVEDGEFRGKAGHGRFLKRKPFQ 456
|
|
| D-hydantoinase |
TIGR02033 |
D-hydantoinase; This model represents the D-hydantoinase (dihydropyrimidinase) which primarily ... |
11-464 |
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: 542.75 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472778 11 ILIKGGRVVNDDVTEEADVYLENGRIQQVGRDLMIPGGAKVIDATGKLVIPGGIDSSVHLHQTFMNAHTQDDFYSGTKAA 90
Cdd:TIGR02033 1 LLIKGGTVVNADDVFQADVLIEGGKIVAVGDNLIPPDAVEVIDATGKYVLPGGIDVHTHLEMPFGGTTTADDFFTGTKAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472778 91 LLGGSTMLISHVLPDRGASLLDAFEQMRAHADAKACCDYALHVGVTWWGPKVEREMEVLVGERGVNSFQMFMAYKDAMML 170
Cdd:TIGR02033 81 AAGGTTTIIDFVVPEKGSSLTEALETWHEKAEGKSVIDYGFHMDITHWNDSVLEEHIPEVKEEGINSFKVFMAYKNLLMV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472778 171 KDSELYQALNTCKNIGAIARIHAENGELVLEGAKEALDLGISGPEGMEISRPEELEAEATHRAITIGNRAHCPVYLVNVS 250
Cdd:TIGR02033 161 DDEELFEILKRLKELGALLQVHAENGDIIAELQARMLAQGITGPEYHALSRPPELEAEAVARAITLAALADAPLYVVHVS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472778 251 SMSAADVIGAARMQGKVVQAETTVAHAVLSGmHYYHQDWAHAAAHVIAPPLRlDPNTPDHLIGLLGNDIINVVASDHRAF 330
Cdd:TIGR02033 241 TKDAADEIAQARKKGQPVFGETCPQYLVLDD-THYDKPGFEGAKYVCSPPLR-EPEDQDALWSALSSGALQTVGSDHCTF 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472778 331 STKQK-AMGKEDFTKIPHGAPGVEDRMSVIWERGVVSGKMDENRFVAVTSSNAAKIYNLYPRKGRIMPGADADVVVWDPD 409
Cdd:TIGR02033 319 NFAQKkAIGKDDFTKIPNGGPGVEERMSLLFDEGVAKGRITLEKFVEVTSTNPAKIFNLYPRKGTIAVGSDADIVIWDPN 398
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 66472778 410 ATRTISASTQAQGGDFNLFEGQRCHGVPLVTISRGRLVCENGVFMCAQGSGKFYP 464
Cdd:TIGR02033 399 RTTVISAETHHSNADYNPFEGFKVRGAPVSVLSRGRVVVEDGQLVGTAGAGRFVK 453
|
|
| PLN02942 |
PLN02942 |
dihydropyrimidinase |
5-482 |
2.49e-176 |
|
dihydropyrimidinase
Pssm-ID: 178530 Cd Length: 486 Bit Score: 507.07 E-value: 2.49e-176
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472778 5 GGSSMRILIKGGRVVNDDVTEEADVYLENGRIQQVGRDLMIPGGAKVIDATGKLVIPGGIDSSVHLHQTFMNAHTQDDFY 84
Cdd:PLN02942 1 GASSTKILIKGGTVVNAHHQELADVYVEDGIIVAVAPNLKVPDDVRVIDATGKFVMPGGIDPHTHLAMPFMGTETIDDFF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472778 85 SGTKAALLGGSTMLISHVLPDRGaSLLDAFEQMRAHAdAKACCDYALHVGVTWWGPKVEREMEVLVGERGVNSFQMFMAY 164
Cdd:PLN02942 81 SGQAAALAGGTTMHIDFVIPVNG-NLLAGYEAYEKKA-EKSCMDYGFHMAITKWDDTVSRDMETLVKEKGINSFKFFMAY 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472778 165 KDAMMLKDSELYQALNTCKNIGAIARIHAENGELVLEGAKEALDLGISGPEGMEISRPEELEAEATHRAITIGNRAHCPV 244
Cdd:PLN02942 159 KGSLMVTDELLLEGFKRCKSLGALAMVHAENGDAVFEGQKRMIELGITGPEGHALSRPPLLEGEATARAIRLAKFVNTPL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472778 245 YLVNVSSMSAADVIGAARMQGKVVQAETTVAHAVLSGMHYYHQDWAHAAAHVIAPPLRldpnTPDH---LIGLLGNDIIN 321
Cdd:PLN02942 239 YVVHVMSIDAMEEIARARKSGQRVIGEPVVSGLVLDDSKLWDPDFTIASKYVMSPPIR----PAGHgkaLQAALSSGILQ 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472778 322 VVASDHRAFSTKQKAMGKEDFTKIPHGAPGVEDRMSVIWERGVVSGKMDENRFVAVTSSNAAKIYNLYPRKGRIMPGADA 401
Cdd:PLN02942 315 LVGTDHCPFNSTQKAFGKDDFRKIPNGVNGIEERMHLVWDTMVESGQISPTDYVRVTSTECAKIFNIYPRKGAILAGSDA 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472778 402 DVVVWDPDATRTISASTQAQGGDFNLFEGQRCHGVPLVTISRGRLVCENGVFMCAQGSGKFYPMRAFPdFLYKKLIQREK 481
Cdd:PLN02942 395 DIIILNPNSTFTISAKTHHSRIDTNVYEGRRGKGKVEVTISQGRVVWENGELKVVRGSGRYIEMPPFS-YLFDGIQKADA 473
|
.
gi 66472778 482 T 482
Cdd:PLN02942 474 A 474
|
|
| AllB |
COG0044 |
Dihydroorotase or related cyclic amidohydrolase [Nucleotide transport and metabolism]; ... |
12-462 |
1.49e-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: 388.30 E-value: 1.49e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472778 12 LIKGGRVVNDDVTEEADVYLENGRIQQVGRDLMIPGGAKVIDATGKLVIPGGIDSSVHLHQTFMNahTQDDFYSGTKAAL 91
Cdd:COG0044 1 LIKNGRVVDPGGLERADVLIEDGRIAAIGPDLAAPEAAEVIDATGLLVLPGLIDLHVHLREPGLE--HKEDIETGTRAAA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472778 92 LGGSTMLISHVLPDRGASLLDAFEQMRAHADAKACCDYALHVGVTWWGPKVEREMEVLVgERGVNSFQMFMAYKDA-MML 170
Cdd:COG0044 79 AGGVTTVVDMPNTNPVTDTPEALEFKLARAEEKALVDVGPHGALTKGLGENLAELGALA-EAGAVAFKVFMGSDDGnPVL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472778 171 KDSELYQALNTCKNIGAIARIHAENGELVLEGAKEAldlGISGPEGMEISRPEELEAEATHRAITIGNRAHCPVYLVNVS 250
Cdd:COG0044 158 DDGLLRRALEYAAEFGALVAVHAEDPDLIRGGVMNE---GKTSPRLGLKGRPAEAEEEAVARDIALAEETGARLHIVHVS 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472778 251 SMSAADVIGAARMQGKVVQAETTVAHAVLSGMHYYHQDwahaAAHVIAPPLRlDPNTPDHLIGLLGNDIINVVASDHRAF 330
Cdd:COG0044 235 TAEAVELIREAKARGLPVTAEVCPHHLTLTDEDLERYG----TNFKVNPPLR-TEEDREALWEGLADGTIDVIATDHAPH 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472778 331 STKQKAmgkEDFTKIPHGAPGVEDRMSVIWERGVVSGKMDENRFVAVTSSNAAKIYNLyPRKGRIMPGADADVVVWDPDA 410
Cdd:COG0044 310 TLEEKE---LPFAEAPNGIPGLETALPLLLTELVHKGRLSLERLVELLSTNPARIFGL-PRKGRIAVGADADLVLFDPDA 385
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 66472778 411 TRTISASTQAQGGDFNLFEGQRCHGVPLVTISRGRLVCENGVFmCAQGSGKF 462
Cdd:COG0044 386 EWTVTAEDLHSKSKNTPFEGRELTGRVVATIVRGRVVYEDGEV-VGEPRGRF 436
|
|
| PRK13404 |
PRK13404 |
dihydropyrimidinase; Provisional |
13-470 |
9.73e-117 |
|
dihydropyrimidinase; Provisional
Pssm-ID: 184033 [Multi-domain] Cd Length: 477 Bit Score: 354.39 E-value: 9.73e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472778 13 IKGGRVVNDDVTEEADVYLENGRIQQVGRDLmiPGGAKVIDATGKLVIPGGIDSSVHLHQ-TFMNAHTQDDFYSGTKAAL 91
Cdd:PRK13404 8 IRGGTVVTATDTFQADIGIRGGRIAALGEGL--GPGAREIDATGRLVLPGGVDSHCHIDQpSGDGIMMADDFYTGTVSAA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472778 92 LGGSTMLISHVLPDRGASLLDAFEQMRAHADAKACCDYALHVGVTWWGPKV-EREMEVLVgERGVNSFQMFMAYkDAMML 170
Cdd:PRK13404 86 FGGTTTVIPFAAQHRGQSLREAVEDYHRRAAGKAVIDYAFHLIVADPTEEVlTEELPALI-AQGYTSFKVFMTY-DDLKL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472778 171 KDSELYQALNTCKNIGAIARIHAENGELVLEGAKEALDLGISGPEGMEISRPEELEAEATHRAITIGNRAHCPVYLVNVS 250
Cdd:PRK13404 164 DDRQILDVLAVARRHGAMVMVHAENHDMIAWLTKRLLAAGLTAPKYHAISRPMLAEREATHRAIALAELVDVPILIVHVS 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472778 251 SMSAADVIGAARMQGKVVQAETTVAHAVLSGmHYYHQDWAHAAAHVIAPPLRlDPNTPDHLIGLLGNDIINVVASDHRAF 330
Cdd:PRK13404 244 GREAAEQIRRARGRGLKIFAETCPQYLFLTA-EDLDRPGMEGAKYICSPPPR-DKANQEAIWNGLADGTFEVFSSDHAPF 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472778 331 ---STKQKAMGKED--FTKIPHGAPGVEDRMSVIWERGVVSGKMDENRFVAVTSSNAAKIYNLYPRKGRIMPGADADVVV 405
Cdd:PRK13404 322 rfdDTDGKLAAGANpsFKAIANGIPGIETRLPLLFSEGVVKGRISLNRFVALTSTNPAKLYGLYPRKGAIAIGADADIAI 401
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 66472778 406 WDPDATRTISASTQAQGGDFNLFEGQRCHGVPLVTISRGRLVCENGVFMCAQGSGKFYPmRAFPD 470
Cdd:PRK13404 402 WDPDREVTITNADLHHAADYTPYEGMRVTGWPVTVLSRGRVVVEDGELVAERGSGQFLA-RSLPD 465
|
|
| L-HYD_ALN |
cd01315 |
L-Hydantoinases (L-HYDs) and Allantoinase (ALN); L-Hydantoinases are a member of the ... |
12-451 |
8.73e-67 |
|
L-Hydantoinases (L-HYDs) and Allantoinase (ALN); L-Hydantoinases are a member of the dihydropyrimidinase family, which catalyzes the reversible hydrolytic ring opening of dihydropyrimidines and hydantoins (five-membered cyclic diamides used in biotechnology). But L-HYDs differ by having an L-enantio specificity and by lacking activity on possible natural substrates such as dihydropyrimidines. Allantoinase catalyzes the hydrolytic cleavage of the five-member ring of allantoin (5-ureidohydantoin) to form allantoic acid.
Pssm-ID: 238640 [Multi-domain] Cd Length: 447 Bit Score: 223.71 E-value: 8.73e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472778 12 LIKGGRVVNDDVTEEADVYLENGRIQQVGRDLMIPGGAKVIDATGKLVIPGGIDSSVHLHQtfMNAHTQDDFYSGTKAAL 91
Cdd:cd01315 3 VIKNGRVVTPDGVREADIAVKGGKIAAIGPDIANTEAEEVIDAGGLVVMPGLIDTHVHINE--PGRTEWEGFETGTKAAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472778 92 LGGSTMLISHVLPDRGASLLDA-FEQMRAHADAKACCDYALHVGVTwwgPKVEREMEVLVgERGVNSFQMFMA---YKDA 167
Cdd:cd01315 81 AGGITTIIDMPLNSIPPTTTVEnLEAKLEAAQGKLHVDVGFWGGLV---PGNLDQLRPLD-EAGVVGFKCFLCpsgVDEF 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472778 168 MMLKDSELYQALNTCKNIGAIARIHAENGELVLEGAKEALDLGISGPEGMEISRPEELEAEATHRAITIGNRAHCPVYLV 247
Cdd:cd01315 157 PAVDDEQLEEAMKELAKTGSVLAVHAENPEITEALQEQAKAKGKRDYRDYLASRPVFTEVEAIQRILLLAKETGCRLHIV 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472778 248 NVSSMSAADVIGAARMQGKVVQAETtvahavlsGMHYY---HQDW-AHAAAHVIAPPLRlDPNTPDHLIGLLGNDIINVV 323
Cdd:cd01315 237 HLSSAEAVPLIREARAEGVDVTVET--------CPHYLtftAEDVpDGGTEFKCAPPIR-DAANQEQLWEALENGDIDMV 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472778 324 ASDHRAFSTKQKAMGKEDFTKIPHGAPGVEDRMSVIWERGVVSGKMDENRFVAVTSSNAAKIYNLYPRKGRIMPGADADV 403
Cdd:cd01315 308 VSDHSPCTPELKLLGKGDFFKAWGGISGLQLGLPVMLTEAVNKRGLSLEDIARLMCENPAKLFGLSHQKGRIAVGYDADF 387
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 66472778 404 VVWDPDATRTISASTQAQGGDFNLFEGQRCHGVPLVTISRGRLVCENG 451
Cdd:cd01315 388 VVWDPEEEFTVDAEDLYYKNKISPYVGRTLKGRVHATILRGTVVYQDG 435
|
|
| PRK02382 |
PRK02382 |
dihydroorotase; Provisional |
11-466 |
1.91e-62 |
|
dihydroorotase; Provisional
Pssm-ID: 179417 [Multi-domain] Cd Length: 443 Bit Score: 211.82 E-value: 1.91e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472778 11 ILIKGGRVVNDDVTEEADVYLENGRIQQVGRDLMIPGGAKVIDATGKLVIPGGIDSSVHLHQtfMNAHTQDDFYSGTKAA 90
Cdd:PRK02382 4 ALLKDGRVYYNNSLQPRDVRIDGGKITAVGKDLDGSSSEEVIDARGMLLLPGGIDVHVHFRE--PGYTHKETWYTGSRSA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472778 91 LLGGSTMLISHvlPDRGASLLD--AFEQMRAHADAKACCDYALHVGVT-WWGPkvereMEVLVgERGVNSF-QMFMAYKD 166
Cdd:PRK02382 82 AAGGVTTVVDQ--PNTDPPTVDgeSFDEKAELAARKSIVDFGINGGVTgNWDP-----LESLW-ERGVFALgEIFMADST 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472778 167 AMMLKDSELY-QALNTCKNIGAIARIHAENGELVLEGAKEaLDlGISGPEGMEISRPEELEAEATHRAITIGNRAHCPVY 245
Cdd:PRK02382 154 GGMGIDEELFeEALAEAARLGVLATVHAEDEDLFDELAKL-LK-GDADADAWSAYRPAAAEAAAVERALEVASETGARIH 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472778 246 LVNVSSMSAADVIGAARMqgkvvQAETTVAHAVLSgmhyyHQDWAHAAAHV-IAPPLRLDPNTpDHLIGLLGNDIINVVA 324
Cdd:PRK02382 232 IAHISTPEGVDAARREGI-----TCEVTPHHLFLS-----RRDWERLGTFGkMNPPLRSEKRR-EALWERLNDGTIDVVA 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472778 325 SDHRAFSTKQKAMgkeDFTKIPHGAPGVEDRMSVIWErGVVSGKMDENRFVAVTSSNAAKIYNLyPRKGRIMPGADADVV 404
Cdd:PRK02382 301 SDHAPHTREEKDA---DIWDAPSGVPGVETMLPLLLA-AVRKNRLPLERVRDVTAANPARIFGL-DGKGRIAEGYDADLV 375
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 66472778 405 VWDPDATRTISASTQAQGGDFNLFEGQRchGV-PLVTISRGRLVCENGVFMCAQGSGKFYPMR 466
Cdd:PRK02382 376 LVDPDAAREIRGDDLHSKAGWTPFEGME--GVfPELTMVRGTVVWDGDDINAKRGRGEFLRGR 436
|
|
| allantoinase |
TIGR03178 |
allantoinase; This enzyme carries out the first step in the degradation of allantoin, a ... |
11-453 |
2.43e-56 |
|
allantoinase; This enzyme carries out the first step in the degradation of allantoin, a ring-opening hydrolysis. The seed members of this model are all in the vicinity of other genes involved in the processes of xanthine/urate/allantoin catabolism. Although not included in the seed, many eukaryotic homologs of this family are included above the trusted cutoff. Below the noise cutoff are related hydantoinases.
Pssm-ID: 163175 [Multi-domain] Cd Length: 443 Bit Score: 195.68 E-value: 2.43e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472778 11 ILIKGGRVVNDDVTEEADVYLENGRIQQVGRDlMIPGGAKVIDATGKLVIPGGIDSSVHLhqtfmNAHTQDD---FYSGT 87
Cdd:TIGR03178 2 LIIRGGRVILPNGEREADVGVKGGKIAAIGPD-ILGPAAKIIDAGGLVVFPGVVDTHVHI-----NEPGRTEwegFETGT 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472778 88 KAALLGGSTMLISHVLPDRGASL-LDAFEQMRAHADAKACCDYALhvgvtwWGPKVEREMEVL--VGERGVNSFQMFMAY 164
Cdd:TIGR03178 76 RAAAAGGITTYIDMPLNSIPATTtRASLEAKFEAAKGKLAVDVGF------WGGLVPYNLDDLreLDEAGVVGFKAFLSP 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472778 165 ---KDAMMLKDSELYQALNTCKNIGAIARIHAENGELVLEGAKEALDLGISGPEGMEISRPEELEAEATHRAITIGNRAH 241
Cdd:TIGR03178 150 sgdDEFPHVDDWQLYKGMRELARLGQLLLVHAENPAITSALGEEAPPQGGVGADAYLASRPVFAEVEAIRRTLALAKVTG 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472778 242 CPVYLVNVSSMSAADVIGAARMQGKVVQAEtTVAHAVlsgmHYYHQDWAHAAAHV-IAPPLRlDPNTPDHLIGLLGNDII 320
Cdd:TIGR03178 230 CRVHVVHLSSAEAVELITEAKQEGLDVTVE-TCPHYL----TLTAEEVPDGGTLAkCAPPIR-DLANQEGLWEALLNGLI 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472778 321 NVVASDHRAFSTKQKAMGkeDFTKIPHGAPGVEDRMSVIWERGVVSGKMDENRFVAVTSSNAAKIYNLyPRKGRIMPGAD 400
Cdd:TIGR03178 304 DCVVSDHSPCTPDLKRAG--DFFKAWGGIAGLQSTLDVMFDEAVQKRGLPLEDIARLMATNPAKRFGL-AQKGRIAPGKD 380
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 66472778 401 ADVVVWDPDATRTISASTQAQGGDFNLFEGQRCHGVPLVTISRGRLVCENGVF 453
Cdd:TIGR03178 381 ADFVFVDPDESYTLTPDDLYYRHKVSPYVGRTIGGRVRATYLRGQCIYDDEQF 433
|
|
| pyrC_multi |
TIGR00857 |
dihydroorotase, multifunctional complex type; In contrast to the homodimeric type of ... |
25-450 |
7.52e-55 |
|
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: 190.73 E-value: 7.52e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472778 25 EEADVYLENGRIQQVGRdLMIPGGAKVIDATGKLVIPGGIDSSVHLHQtfMNAHTQDDFYSGTKAALLGGSTMLIShvLP 104
Cdd:TIGR00857 4 TEVDILVEGGRIKKIGK-LRIPPDAEVIDAKGLLVLPGFIDLHVHLRD--PGEEYKEDIESGSKAAAHGGFTTVAD--MP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472778 105 DRGASLLDA--FEQMRAHADAKACCDYALHVGVTW-WGPKVEREMEVL--VGERGVNSFQMFMAYKDAMMLKDSELYQAL 179
Cdd:TIGR00857 79 NTKPPIDTPetLEWKLQRLKKVSLVDVHLYGGVTQgNQGKELTEAYELkeAGAVGRMFTDDGSEVQDILSMRRALEYAAI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472778 180 ntcknIGAIARIHAENGELVLEGAKEaldLGISGPEGMEISRPEELEAEATHRAITIGNRAHCPVYLVNVSSMSAADVIG 259
Cdd:TIGR00857 159 -----AGVPIALHAEDPDLIYGGVMH---EGPSAAQLGLPARPPEAEEVAVARLLELAKHAGCPVHICHISTKESLELIV 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472778 260 AARMQGKVVQAETTVAHAVLSgmhyyHQDWAHAAAHV-IAPPLRlDPNTPDHLIGLLGNDIINVVASDHRAFSTKQKAMG 338
Cdd:TIGR00857 231 KAKSQGIKITAEVTPHHLLLS-----EEDVARLDGNGkVNPPLR-EKEDRLALIEGLKDGIIDIIATDHAPHTLEEKTKE 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472778 339 KEDftkIPHGAPGVEDRMSVIWERgVVSGKMDENRFVAVTSSNAAKIYNLyPRKGRIMPGADADVVVWDPDATRTISAST 418
Cdd:TIGR00857 305 FAA---APPGIPGLETALPLLLQL-LVKGLISLKDLIRMLSINPARIFGL-PDKGTLEEGNPADITVFDLKKEWTINAET 379
|
410 420 430
....*....|....*....|....*....|..
gi 66472778 419 QAQGGDFNLFEGQRCHGVPLVTISRGRLVCEN 450
Cdd:TIGR00857 380 FYSKAKNTPFEGMSLKGKPIATILRGKVVYED 411
|
|
| Cyclic_amidohydrolases |
cd01302 |
Cyclic amidohydrolases, including hydantoinase, dihydropyrimidinase, allantoinase, and ... |
57-440 |
4.50e-54 |
|
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: 186.44 E-value: 4.50e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472778 57 KLVIPGGIDSSVHLHQTFMNAHtQDDFYSGTKAALLGGSTMLISHVLPDRGASLLDAFEQMRAHADAKACCDYALHVGVT 136
Cdd:cd01302 1 LLVLPGFIDIHVHLRDPGGTTY-KEDFESGSRAAAAGGVTTVIDMPNTGPPPIDLPAIELKIKLAEESSYVDFSFHAGIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472778 137 WWGPKVEREmevLVGERGVNSFQMFMAYKDAMMLK--DSELYQALNTCKNIGAIARIHAEngelvlegakealdlgisgp 214
Cdd:cd01302 80 PGDVTDELK---KLFDAGINSLKVFMNYYFGELFDvdDGTLMRTFLEIASRGGPVMVHAE-------------------- 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472778 215 egmeisrpeeleaeathRAITIGNRAHCPVYLVNVSSMSAADVIGAARMQGKVVQAETTVAHAVLSgmhyyHQDWAHAAA 294
Cdd:cd01302 137 -----------------RAAQLAEEAGANVHIAHVSSGEALELIKFAKNKGVKVTCEVCPHHLFLD-----ESMLRLNGA 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472778 295 H-VIAPPLRlDPNTPDHLIGLLGNDIINVVASDHRAFSTKQKAMGKeDFTKIPHGAPGVEDRMS-VIWErgVVSGKMDEN 372
Cdd:cd01302 195 WgKVNPPLR-SKEDREALWEGVKNGKIDTIASDHAPHSKEEKESGK-DIWKAPPGFPGLETRLPiLLTE--GVKRGLSLE 270
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 66472778 373 RFVAVTSSNAAKIYNLYPrKGRIMPGADADVVVWDPDATRTISASTQAQGGDFNLFEGQRCHGVPLVT 440
Cdd:cd01302 271 TLVEILSENPARIFGLYP-KGTIAVGYDADLVIVDPKKEWKVTAEEIESKADWTPFEGMEVTGKPVST 337
|
|
| PRK06189 |
PRK06189 |
allantoinase; Provisional |
11-453 |
1.14e-50 |
|
allantoinase; Provisional
Pssm-ID: 235732 [Multi-domain] Cd Length: 451 Bit Score: 180.67 E-value: 1.14e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472778 11 ILIKGGRVVNDDVTEEADVYLENGRIQQVGRDLMIPGgAKVIDATGKLVIPGGIDSSVHLhqtfmNAHTQDD---FYSGT 87
Cdd:PRK06189 5 LIIRGGKVVTPEGVYRADIGIKNGKIAEIAPEISSPA-REIIDADGLYVFPGMIDVHVHF-----NEPGRTHwegFATGS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472778 88 KAALLGGST----MLISHVLPDRGAsllDAFEQMRAHADAKACCDYALhvgvtwWGPKVEREMEVL--VGERGVNSFQMF 161
Cdd:PRK06189 79 AALAAGGCTtyfdMPLNSIPPTVTR---EALDAKAELARQKSAVDFAL------WGGLVPGNLEHLreLAEAGVIGFKAF 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472778 162 MAY---KDAMMLKDSELYQALNTCKNIGAIARIHAENGELVLEGAKEALDLGISGPEGMEISRPEELEAEATHRAITIGN 238
Cdd:PRK06189 150 MSNsgtDEFRSSDDLTLYEGMKEIAALGKILALHAESDALTRHLTTQARQQGKTDVRDYLESRPVVAELEAVQRALLYAQ 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472778 239 RAHCPVYLVNVSSMSAADVIGAARMQGKVVQAETtVAHAVLsgmhYYHQDWAH-AAAHVIAPPLRlDPNTPDHLIGLLGN 317
Cdd:PRK06189 230 ETGCPLHFVHISSGKAVALIAEAKKRGVDVSVET-CPHYLL----FTEEDFERiGAVAKCAPPLR-SRSQKEELWRGLLA 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472778 318 DIINVVASDHRAFSTKQKAmgKEDFTKIPHGAPGVEDRMSVIWERGVVSGKMDENRFVAVTSSNAAKIYNLyPRKGRIMP 397
Cdd:PRK06189 304 GEIDMISSDHSPCPPELKE--GDDFFLVWGGISGGQSTLLVMLTEGYIERGIPLETIARLLATNPAKRFGL-PQKGRLEV 380
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 66472778 398 GADADVVVWDPDATRTISASTQAQGGDFNLFEGQRCHGVPLVTISRGRLVCENGVF 453
Cdd:PRK06189 381 GADADFVLVDLDETYTLTKEDLFYRHKQSPYEGRTFPGRVVATYLRGQCVYQDGEV 436
|
|
| DHOase_IIa |
cd01317 |
Dihydroorotase (DHOase), subgroup IIa; DHOases catalyze the reversible interconversion of ... |
48-440 |
2.24e-42 |
|
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: 155.86 E-value: 2.24e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472778 48 GAKVIDATGKLVIPGGIDSSVHLHQTfmnAHTQ-DDFYSGTKAALLGGST--MLISHVLPDR-GASLLDaFEQMRAHADA 123
Cdd:cd01317 1 DAEVIDAEGKILAPGLVDLHVHLREP---GFEYkETLESGAKAAAAGGFTtvVCMPNTNPVIdNPAVVE-LLKNRAKDVG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472778 124 KACCdyaLHVGVTWWGPKVER--EMEVLVgERGVNSFQmfmayKDAMMLKDSE-LYQALNTCKNIGAIARIHAENGELVL 200
Cdd:cd01317 77 IVRV---LPIGALTKGLKGEEltEIGELL-EAGAVGFS-----DDGKPIQDAElLRRALEYAAMLDLPIIVHPEDPSLAG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472778 201 EGA----KEALDLGISGpegmeisRPEELEAEATHRAITIGNRAHCPVYLVNVSSMSAADVIGAARMQGKVVQAETTVAH 276
Cdd:cd01317 148 GGVmnegKVASRLGLPG-------IPPEAETIMVARDLELAEATGARVHFQHLSTARSLELIRKAKAKGLPVTAEVTPHH 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472778 277 AVLSGMHYYHQDwahaAAHVIAPPLRlDPNTPDHLIGLLGNDIINVVASDHRAFSTKQKAMGKEDftkIPHGAPGVEDRM 356
Cdd:cd01317 221 LLLDDEALESYD----TNAKVNPPLR-SEEDREALIEALKDGTIDAIASDHAPHTDEEKDLPFAE---APPGIIGLETAL 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472778 357 SVIWERGVVSGKMDENRFVAVTSSNAAKIYNLYPrkGRIMPGADADVVVWDPDATRTISASTQAQGGDFNLFEGQRCHGV 436
Cdd:cd01317 293 PLLWTLLVKGGLLTLPDLIRALSTNPAKILGLPP--GRLEVGAPADLVLFDPDAEWIVDEETFRSKSKNTPFDGQKLKGR 370
|
....
gi 66472778 437 PLVT 440
Cdd:cd01317 371 VLAT 374
|
|
| pyrC |
PRK09357 |
dihydroorotase; Validated |
9-450 |
6.92e-42 |
|
dihydroorotase; Validated
Pssm-ID: 236479 [Multi-domain] Cd Length: 423 Bit Score: 155.74 E-value: 6.92e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472778 9 MRILIKGGRVVNDDVTEE-ADVYLENGRIQQVGRDLmIPGGAKVIDATGKLVIPGGIDSSVHLH---QTFmnahtQDDFY 84
Cdd:PRK09357 1 MMILIKNGRVIDPKGLDEvADVLIDDGKIAAIGENI-EAEGAEVIDATGLVVAPGLVDLHVHLRepgQED-----KETIE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472778 85 SGTKAALLGGSTMLisHVLP--DRGASLLDAFEQMRAHADAKACCDY----ALHVGVTwwgPKVEREMEVLVGERGVnsf 158
Cdd:PRK09357 75 TGSRAAAAGGFTTV--VAMPntKPVIDTPEVVEYVLDRAKEAGLVDVlpvgAITKGLA---GEELTEFGALKEAGVV--- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472778 159 qMF----MAYKDAMMLkdselYQALNTCKNIGAIARIHAE-----NGELVLEGAKEALdLGISGpegmeisRPEELEAEA 229
Cdd:PRK09357 147 -AFsddgIPVQDARLM-----RRALEYAKALDLLIAQHCEdpsltEGGVMNEGEVSAR-LGLPG-------IPAVAEEVM 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472778 230 THRAITIGNRAHCPVYLVNVSSMSAADVIGAARMQGKVVQAETTVAHAVLSGMHYYHQDwahAAAHViAPPLRLDPNTpD 309
Cdd:PRK09357 213 IARDVLLAEATGARVHICHVSTAGSVELIRWAKALGIKVTAEVTPHHLLLTDEDLLTYD---PNYKV-NPPLRTEEDR-E 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472778 310 HLIGLLGNDIINVVASDHRAFSTKQKAmgkEDFTKIPHGAPGVEDRMSVIWERGVVSGKMDENRFVAVTSSNAAKIYNLY 389
Cdd:PRK09357 288 ALIEGLKDGTIDAIATDHAPHAREEKE---CEFEAAPFGITGLETALSLLYTTLVKTGLLDLEQLLEKMTINPARILGLP 364
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 66472778 390 PrkGRIMPGADADVVVWDPDATRTISASTQAQGGDFNLFEGQRCHGVPLVTISRGRLVCEN 450
Cdd:PRK09357 365 A--GPLAEGEPADLVIFDPEAEWTVDGEDFASKGKNTPFIGMKLKGKVVYTIVDGKIVYQD 423
|
|
| DHOase_IIb |
cd01318 |
Dihydroorotase (DHOase), subgroup IIb; DHOases catalyze the reversible interconversion of ... |
56-444 |
3.63e-40 |
|
Dihydroorotase (DHOase), subgroup IIb; DHOases catalyze the reversible interconversion of carbamoyl aspartate to dihydroorotate, a key reaction in pyrimidine biosynthesis. This group contains the archeal members of the DHOase family.
Pssm-ID: 238643 [Multi-domain] Cd Length: 361 Bit Score: 149.79 E-value: 3.63e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472778 56 GKLVIPGGIDSSVHLHQTfmnAHTQ-DDFYSGTKAALLGGstmlISHVL-------PDRGAsllDAFEQMRAHADAKACC 127
Cdd:cd01318 1 GLLILPGVIDIHVHFREP---GLTYkEDFVSGSRAAAAGG----VTTVMdmpntkpPTTTA---EALYEKLRLAAAKSVV 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472778 128 DYALHVGVTwwGPKVEREMEvlvgERGVNSFQMFMAYKDAMMLKDSE-LYQALNTCKnigAIARIHAENGELVLEGAKEA 206
Cdd:cd01318 71 DYGLYFGVT--GSEDLEELD----KAPPAGYKIFMGDSTGDLLDDEEtLERIFAEGS---VLVTFHAEDEDRLRENRKEL 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472778 207 LDLGISgpegmEISRPEELEAEATHRAITIGNRAHCPVYLVNVSSmsaADVIGAARMQGKVVQAETTVAHAVLS-GMHYY 285
Cdd:cd01318 142 KGESAH-----PRIRDAEAAAVATARALKLARRHGARLHICHVST---PEELKLIKKAKPGVTVEVTPHHLFLDvEDYDR 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472778 286 HQDWAHaaahvIAPPLRlDPNTPDHLIGLLGNDIINVVASDHRAFSTKQKAMGKEDftkIPHGAPGVEDRMSVI---WER 362
Cdd:cd01318 214 LGTLGK-----VNPPLR-SREDRKALLQALADGRIDVIASDHAPHTLEEKRKGYPA---APSGIPGVETALPLMltlVNK 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472778 363 GVVSGKmdenRFVAVTSSNAAKIYNLyPRKGRIMPGADADVVVWDPDATRTISASTQAQGGDFNLFEGQRCHGVPLVTIS 442
Cdd:cd01318 285 GILSLS----RVVRLTSHNPARIFGI-KNKGRIAEGYDADLTVVDLKEERTIRAEEFHSKAGWTPFEGFEVTGFPVMTIV 359
|
..
gi 66472778 443 RG 444
Cdd:cd01318 360 RG 361
|
|
| PRK09060 |
PRK09060 |
dihydroorotase; Validated |
12-451 |
1.63e-37 |
|
dihydroorotase; Validated
Pssm-ID: 181632 [Multi-domain] Cd Length: 444 Bit Score: 144.29 E-value: 1.63e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472778 12 LIKGGRVVNDDVTEEADVYLENGRIQQVGrDLMIPGGAKVIDATGKLVIPGGIDSSVHLHQTfMNAHTQdDFYSGTKAAL 91
Cdd:PRK09060 8 ILKGGTVVNPDGEGRADIGIRDGRIAAIG-DLSGASAGEVIDCRGLHVLPGVIDSQVHFREP-GLEHKE-DLETGSRAAV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472778 92 LGGSTMLIShvLPDRGASLLDA--FEQMRAHADAKACCDYALHVGVTWWGPKVEREMEVLVGERGVNSFqMFMAYKDAMM 169
Cdd:PRK09060 85 LGGVTAVFE--MPNTNPLTTTAeaLADKLARARHRMHCDFAFYVGGTRDNADELAELERLPGCAGIKVF-MGSSTGDLLV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472778 170 LKDSELYQALntcKNIGAIARIHAENgELVLegaKEALDLGISG-PEGMEISRPEELEAEATHRAITIGNRAHCPVYLVN 248
Cdd:PRK09060 162 EDDEGLRRIL---RNGRRRAAFHSED-EYRL---RERKGLRVEGdPSSHPVWRDEEAALLATRRLVRLARETGRRIHVLH 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472778 249 VSSMSAADVIGAARmqgKVVQAETTVAHAVLSGMHYYHQDWAHAaahVIAPPLRldpnTPDHLIGL---LGNDIINVVAS 325
Cdd:PRK09060 235 VSTAEEIDFLADHK---DVATVEVTPHHLTLAAPECYERLGTLA---QMNPPIR----DARHRDGLwrgVRQGVVDVLGS 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472778 326 DHRAFSTKQKAmgkEDFTKIPHGAPGVEDRMSVIWERgVVSGKMDENRFVAVTSSNAAKIYNLyPRKGRIMPGADADVVV 405
Cdd:PRK09060 305 DHAPHTLEEKA---KPYPASPSGMTGVQTLVPIMLDH-VNAGRLSLERFVDLTSAGPARIFGI-AGKGRIAVGYDADFTI 379
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 66472778 406 WDPDATRTISASTQAQGGDFNLFEGQRCHGVPLVTISRGRLVCENG 451
Cdd:PRK09060 380 VDLKRRETITNEWIASRCGWTPYDGKEVTGWPVGTIVRGQRVMWDG 425
|
|
| PRK07575 |
PRK07575 |
dihydroorotase; Provisional |
7-453 |
2.19e-31 |
|
dihydroorotase; Provisional
Pssm-ID: 236055 [Multi-domain] Cd Length: 438 Bit Score: 126.71 E-value: 2.19e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472778 7 SSMRILIKGGRVVNDDVT-EEADVYLENGRIQQVGRDLMIPGGAKVIDATGKLVIPGGIDSSVHLHQTfMNAHtQDDFYS 85
Cdd:PRK07575 1 MMMSLLIRNARILLPSGElLLGDVLVEDGKIVAIAPEISATAVDTVIDAEGLTLLPGVIDPQVHFREP-GLEH-KEDLFT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472778 86 GTKAALLGGSTMLIShvLPDRGASLLD--AFEQMRAHADAKACCDYALHVGVTwwgpkvEREMEVLVGERGVNSFQMFMA 163
Cdd:PRK07575 79 ASRACAKGGVTSFLE--MPNTKPLTTTqaALDDKLARAAEKCVVNYGFFIGAT------PDNLPELLTANPTCGIKIFMG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472778 164 YKDAMMLKDSElyqalntckniGAIARI----------HAENGELVLEGAKEAldLGISGPEGMEISRPEELEAEATHRA 233
Cdd:PRK07575 151 SSHGPLLVDEE-----------AALERIfaegtrliavHAEDQARIRARRAEF--AGISDPADHSQIQDEEAALLATRLA 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472778 234 ITIGNRAHCPVYLVNVSSMSAADVIGAARmqGKVVQAETTVAHAVLSGMHYYH-----QdwahaaahvIAPPLRlDPNTP 308
Cdd:PRK07575 218 LKLSKKYQRRLHILHLSTAIEAELLRQDK--PSWVTAEVTPQHLLLNTDAYERigtlaQ---------MNPPLR-SPEDN 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472778 309 DHLIGLLGNDIINVVASDHRAFSTKQKAmgkEDFTKIPHGAPGVEDRMSVIWERgVVSGKMDENRFVAVTSSNAAKIYNL 388
Cdd:PRK07575 286 EALWQALRDGVIDFIATDHAPHTLEEKA---QPYPNSPSGMPGVETSLPLMLTA-AMRGKCTVAQVVRWMSTAVARAYGI 361
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 66472778 389 yPRKGRIMPGADADVVVWDPDATRTISASTQAQGGDFNLFEGQRCHGVPLVTISRGRLVCENGVF 453
Cdd:PRK07575 362 -PNKGRIAPGYDADLVLVDLNTYRPVRREELLTKCGWSPFEGWNLTGWPVTTIVGGQIVFDRGQV 425
|
|
| PRK08044 |
PRK08044 |
allantoinase AllB; |
8-416 |
6.08e-30 |
|
allantoinase AllB;
Pssm-ID: 169193 [Multi-domain] Cd Length: 449 Bit Score: 122.66 E-value: 6.08e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472778 8 SMRILIKGGRVVNDDVTEEADVYLENGRIQQVGRDLmiPGGAKVIDATGKLVIPGGIDSsvHLHQTFMNAHTQDDFYSGT 87
Cdd:PRK08044 2 SFDLIIKNGTVILENEARVVDIAVKGGKIAAIGQDL--GDAKEVMDASGLVVSPGMVDA--HTHISEPGRSHWEGYETGT 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472778 88 KAALLGGSTMLISHVLPDRGASLLDAFEQMRAHAdAKAccdyALHVGVTWWGPKVEREMEVL--VGERGVNSFQMFMAY- 164
Cdd:PRK08044 78 RAAAKGGITTMIEMPLNQLPATVDRASIELKFDA-AKG----KLTIDAAQLGGLVSYNLDRLheLDEVGVVGFKCFVATc 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472778 165 ------KDAMMLKDSELYQALNTCKNIGAIARIHAENGELVLEGAKEALDLGISGPEGMEISRPEELEAEATHRAITIGN 238
Cdd:PRK08044 153 gdrgidNDFRDVNDWQFYKGAQKLGELGQPVLVHCENALICDELGEEAKREGRVTAHDYVASRPVFTEVEAIRRVLYLAK 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472778 239 RAHCPVYLVNVSSMSAADVIGAARMQGKVVQAETTVAHAVLsgmhyYHQDWAHAAAHV-IAPPLRlDPNTPDHLIGLLGN 317
Cdd:PRK08044 233 VAGCRLHVCHISSPEGVEEVTRARQEGQDVTCESCPHYFVL-----DTDQFEEIGTLAkCSPPIR-DLENQKGMWEKLFN 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472778 318 DIINVVASDHRAFSTKQKAmgkEDFTKIPHGAPGVEDRMSVIWERGVVSGKMDENRFVAVTSSNAAKIYNLyPRKGRIMP 397
Cdd:PRK08044 307 GEIDCLVSDHSPCPPEMKA---GNIMEAWGGIAGLQNCMDVMFDEAVQKRGMSLPMFGKLMATNAADIFGL-QQKGRIAP 382
|
410
....*....|....*....
gi 66472778 398 GADADVVVWDPDATRTISA 416
Cdd:PRK08044 383 GKDADFVFIQPNSSYVLKN 401
|
|
| PLN02795 |
PLN02795 |
allantoinase |
16-451 |
2.67e-27 |
|
allantoinase
Pssm-ID: 178392 [Multi-domain] Cd Length: 505 Bit Score: 115.64 E-value: 2.67e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472778 16 GRVVNDDVTEEADVYLENGRIQQVGRDLMIPG---GAKVIDATGKLVIPGGIDSSVHLHQTfmnAHTQ-DDFYSGTKAAL 91
Cdd:PLN02795 51 KRVVTPAGVIPGAVEVEGGRIVSVTKEEEAPKsqkKPHVLDYGNAVVMPGLIDVHVHLNEP---GRTEwEGFPTGTKAAA 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472778 92 LGGSTMLISHVLPDRGASL-LDAFEQMRAHADAKaccdyaLHVGVTWWGPKV------EREMEVLvGERGVNSFQMFM-- 162
Cdd:PLN02795 128 AGGITTLVDMPLNSFPSTTsVETLELKIEAAKGK------LYVDVGFWGGLVpenahnASVLEEL-LDAGALGLKSFMcp 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472778 163 -AYKDAMMLKDSELYQALNTCKNIGAIARIHAENGELVLEGAKEALDLGiSGPEGMEiSRPEELEAEATHRAITI----- 236
Cdd:PLN02795 201 sGINDFPMTTATHIKAALPVLAKYGRPLLVHAEVVSPVESDSRLDADPR-SYSTYLK-SRPPSWEQEAIRQLLEVakdtr 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472778 237 --GNRAHCPVYLVNVS-SMSAADVIGAARMQGKVVQAETTVahavlsgmHYYhqdwAHAAAHV--------IAPPLRLDP 305
Cdd:PLN02795 279 pgGVAEGAHVHIVHLSdAESSLELIKEAKAKGDSVTVETCP--------HYL----AFSAEEIpdgdtrykCAPPIRDAA 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472778 306 NTpDHLIGLLGNDIINVVASDHRAFSTKQKAMGKEDFTKIPHGAPGVEDRMSVIWERGVVSGkMDENRFVAVTSSNAAKI 385
Cdd:PLN02795 347 NR-ELLWKALLDGDIDMLSSDHSPSPPDLKLLEEGNFLRAWGGISSLQFVLPATWTAGRAYG-LTLEQLARWWSERPAKL 424
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 66472778 386 YNLyPRKGRIMPGADADVVVWDPDATRTISASTQAQGGDFNL--FEGQRCHGVPLVTISRGRLVCENG 451
Cdd:PLN02795 425 AGL-DSKGAIAPGKDADIVVWDPEAEFVLDESYPIYHKHKSLspYLGTKLSGKVIATFVRGNLVFLEG 491
|
|
| PRK04250 |
PRK04250 |
dihydroorotase; Provisional |
16-451 |
4.47e-27 |
|
dihydroorotase; Provisional
Pssm-ID: 235265 [Multi-domain] Cd Length: 398 Bit Score: 113.32 E-value: 4.47e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472778 16 GRVVNDDVTEEADVYLENGRIQQVGRDLMipGGAKVIDATGKLVIPGGIDSSVHLhQTFMNAHtQDDFYSGTKAALLGGS 95
Cdd:PRK04250 4 GKFLLKGRIVEGGIGIENGRISKISLRDL--KGKEVIKVKGGIILPGLIDVHVHL-RDFEESY-KETIESGTKAALHGGI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472778 96 TMLIShvLPDRGASLLDA--FEQMRAHADAKACCDYALHVGVTWWGPKVEREMEvlvgergvNSFQMFM-AYKDAMMLKD 172
Cdd:PRK04250 80 TLVFD--MPNTKPPIMDEktYEKRMRIAEKKSYADYALNFLIAGNCEKAEEIKA--------DFYKIFMgASTGGIFSEN 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472778 173 SEL-YqalntcKNIGAIARIHAENGELVLEGakealdlgisgPEgmeisRPEELEAEATHRAITIGNRAHCPVYLVNVSS 251
Cdd:PRK04250 150 FEVdY------ACAPGIVSVHAEDPELIREF-----------PE-----RPPEAEVVAIERALEAGKKLKKPLHICHIST 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472778 252 MSAADVIGAARMQgkVVQAETTVAHAVLSgmhyyHQDWAHAAAHVIAPPLRldpnTPDHLIGLLGN-DIINVVASDHRAF 330
Cdd:PRK04250 208 KDGLKLILKSNLP--WVSFEVTPHHLFLT-----RKDYERNPLLKVYPPLR----SEEDRKALWENfSKIPIIASDHAPH 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472778 331 STKQKAMGKEdftkiphGAPGVEDRMSVIWE---RGVVSGKmdenRFVAVTSSNAAKIYNlYPRKGrIMPGADADVVVWD 407
Cdd:PRK04250 277 TLEDKEAGAA-------GIPGLETEVPLLLDaanKGMISLF----DIVEKMHDNPARIFG-IKNYG-IEEGNYANFAVFD 343
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 66472778 408 PDATRTISASTQAQGGDFNLFEGQRCHGVPLVTISRGRLVCENG 451
Cdd:PRK04250 344 MKKEWTIKAEELYTKAGWTPYEGFKLKGKVIMTILRGEVVMEDD 387
|
|
| PRK09236 |
PRK09236 |
dihydroorotase; Reviewed |
9-451 |
2.46e-24 |
|
dihydroorotase; Reviewed
Pssm-ID: 181716 Cd Length: 444 Bit Score: 105.72 E-value: 2.46e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472778 9 MRILIKGGRVVNDDVTEEADVYLENGRIQQVGRDLMIPGGAKVIDATGKLVIPGGIDSSVHL------HQTfmnahtqdD 82
Cdd:PRK09236 2 KRILIKNARIVNEGKIFEGDVLIENGRIAKIASSISAKSADTVIDAAGRYLLPGMIDDQVHFrepgltHKG--------D 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472778 83 FYSGTKAALLGGST--MLISHVLPDrgASLLDAFEQMRAHADAKACCDYALHVGVTwwgpkvEREMEVL--VGERGVNSF 158
Cdd:PRK09236 74 IASESRAAVAGGITsfMEMPNTNPP--TTTLEALEAKYQIAAQRSLANYSFYFGAT------NDNLDEIkrLDPKRVCGV 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472778 159 QMFMAYKDAMMLKDSElyQAL-NTCKNIGAIARIHAENGELV---LEGAKEAL--DLGISgpEGMEIsRPEELEAEATHR 232
Cdd:PRK09236 146 KVFMGASTGNMLVDNP--ETLeRIFRDAPTLIATHCEDTPTIkanLAKYKEKYgdDIPAE--MHPLI-RSAEACYKSSSL 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472778 233 AITIGNRAHCPVYLVNVSSMSAADVIGAARMQGKVVQAETTVAHavlsgMHYYHQDWAHAAAHVIAPPLRLDPNTPDHLI 312
Cdd:PRK09236 221 AVSLAKKHGTRLHVLHISTAKELSLFENGPLAEKRITAEVCVHH-----LWFDDSDYARLGNLIKCNPAIKTASDREALR 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472778 313 GLLGNDIINVVASDHRAFSTKQKAMGkedFTKIPHGAPGVEDRMSVIWERgVVSGKMDENRFVAVTSSNAAKIYNLyPRK 392
Cdd:PRK09236 296 QALADDRIDVIATDHAPHTWEEKQGP---YFQAPSGLPLVQHALPALLEL-VHEGKLSLEKVVEKTSHAPAILFDI-KER 370
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 66472778 393 GRIMPGADADVVVWDPDATRTISAstqaqggDFNL-------FEGQRCHGVPLVTISRGRLVCENG 451
Cdd:PRK09236 371 GFIREGYWADLVLVDLNSPWTVTK-------ENILykcgwspFEGRTFRSRVATTFVNGQLVYHNG 429
|
|
| PRK01211 |
PRK01211 |
dihydroorotase; Provisional |
25-464 |
1.04e-18 |
|
dihydroorotase; Provisional
Pssm-ID: 179247 [Multi-domain] Cd Length: 409 Bit Score: 88.38 E-value: 1.04e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472778 25 EEADVYLENGRIQQVGRDLmipGGAKVIDATGkLVIPGGIDSSVHLHQTfmNAHTQDDFYSGTKAALLGGSTMLIShvLP 104
Cdd:PRK01211 14 DYLEIEVEDGKIKSIKKDA---GNIGKKELKG-AILPAATDIHVHFRTP--GETEKEDFSTGTLSAIFGGTTFIMD--MP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472778 105 DRGASLLD--AFEQMRAHADAKACCDYALHVGVTwwGPKVEremevLVGERGVnSFQMFMA---YKDAMMLKDSElyqaL 179
Cdd:PRK01211 86 NNNIPIKDynAFSDKLGRVAPKAYVDFSLYSMET--GNNAL-----ILDERSI-GLKVYMGgttNTNGTDIEGGE----I 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472778 180 NTCKNIGAIARIHAENGELVLEGAKEALDLgisgpEGMEISRPEELEAEATHRAITIGNRAHcpvYLVNVSSMsaaDVIG 259
Cdd:PRK01211 154 KKINEANIPVFFHAELSECLRKHQFESKNL-----RDHDLARPIECEIKAVKYVKNLDLKTK---IIAHVSSI---DVIG 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472778 260 AarmqgkvVQAETTVAHAVLsgmhyyHQDWAHAAAHVIAPPLRlDPNTPDHLIGLLGNDIINVVASDHRAFSTKQKAmgk 339
Cdd:PRK01211 223 R-------FLREVTPHHLLL------NDDMPLGSYGKVNPPLR-DRWTQERLLEEYISGRFDILSSDHAPHTEEDKQ--- 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472778 340 eDFTKIPHGAPGVEDRMSVIWERgVVSGKMDENRFVAVTSSNAAKIYNLypRKGRIMPGADADVVVWDPDATRTISASTQ 419
Cdd:PRK01211 286 -EFEYAKSGIIGVETRVPLFLAL-VKKKILPLDVLYKTAIERPASLFGI--KKGKIEEGYDADFMAFDFTNIKKINDKRL 361
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 66472778 420 AQGGDFNLFEGQRCHgVPLVTISRGRLVCENGVFMcAQGSGKFYP 464
Cdd:PRK01211 362 HSKCPVSPFNGFDAI-FPSHVIMRGEVVIDNYELI-SERTGKFVP 404
|
|
| PRK07369 |
PRK07369 |
dihydroorotase; Provisional |
9-418 |
7.00e-18 |
|
dihydroorotase; Provisional
Pssm-ID: 236002 [Multi-domain] Cd Length: 418 Bit Score: 86.19 E-value: 7.00e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472778 9 MRILIKGGRVVnDDVT---EEADVYLENGRIQQVGRDLM-IPGGAKVIDATGKLVIPGGIDSSVHLHQtfMNAHTQDDFY 84
Cdd:PRK07369 2 SNELLQQVRVL-DPVSntdRIADVLIEDGKIQAIEPHIDpIPPDTQIIDASGLILGPGLVDLYSHSGE--PGFEERETLA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472778 85 SGTKAALLGGSTMLIshVLP------DRGASLldAFEQMRAHADAKACCDyalhvgvtWWGP---KVEREMEVLVGE--- 152
Cdd:PRK07369 79 SLAAAAAAGGFTRVA--ILPdtfpplDNPATL--ARLQQQAQQIPPVQLH--------FWGAltlGGQGKQLTELAElaa 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472778 153 RGVNSFQMFMAYKDAMMLKDSELY-QALNtcKNIGAIA--RIHAENGeLVLEGAkEALDLGISGpegmeisRPEELEAEA 229
Cdd:PRK07369 147 AGVVGFTDGQPLENLALLRRLLEYlKPLG--KPVALWPcdRSLAGNG-VMREGL-LALRLGLPG-------DPASAETTA 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472778 230 THRAITIGNRAHCPVYLVNVSSMSAADVIGAARMQGKVVQAETTVAHAVLSGMHYYHQDwahaaahviaPPLRLDP---N 306
Cdd:PRK07369 216 LAALLELVAAIGTPVHLMRISTARSVELIAQAKARGLPITASTTWMHLLLDTEALASYD----------PNLRLDPplgN 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472778 307 TPDH--LIGLLGNDIINVVASDHRAFSTKQKAMGkedFTKIPHGAPGVEDRMSVIWERGVVSGKMDENRFVAVTSSNAAK 384
Cdd:PRK07369 286 PSDRqaLIEGVRTGVIDAIAIDHAPYTYEEKTVA---FAEAPPGAIGLELALPLLWQNLVETGELSALQLWQALSTNPAR 362
|
410 420 430
....*....|....*....|....*....|....
gi 66472778 385 IYNLYPRkgRIMPGADADVVVWDPDATRTISAST 418
Cdd:PRK07369 363 CLGQEPP--SLAPGQPAELILFDPQKTWTVSAQT 394
|
|
| Amidohydro_1 |
pfam01979 |
Amidohydrolase family; This family of enzymes are a a large metal dependent hydrolase ... |
58-447 |
9.50e-16 |
|
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: 78.70 E-value: 9.50e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472778 58 LVIPGGIDSSVHLHQTFM-NAHTQDDFY-----SGTKAALLGGST----MLISHVLPDRGasLLDAFEQMRA--HADAKA 125
Cdd:pfam01979 1 IVLPGLIDAHVHLEMGLLrGIPVPPEFAyealrLGITTMLKSGTTtvldMGATTSTGIEA--LLEAAEELPLglRFLGPG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472778 126 CC---DYALHVGVTWWgPKVEREMEVLVGERGVNSFQMFMAYkDAMMLKDSELYQALNTCKNIGAIARIHAENGELVLEG 202
Cdd:pfam01979 79 CSldtDGELEGRKALR-EKLKAGAEFIKGMADGVVFVGLAPH-GAPTFSDDELKAALEEAKKYGLPVAIHALETKGEVED 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472778 203 AKEAldlgisgpegmeisrpeeleaeathraitIGNRAHCPVYLVNVSSMSAADVIGAARMQG---KVVQAETTVAHAVL 279
Cdd:pfam01979 157 AIAA-----------------------------FGGGIEHGTHLEVAESGGLLDIIKLILAHGvhlSPTEANLLAEHLKG 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472778 280 SGMhyyhqdwahaaAHVIAPPLRLDPNTPDhLIGLLGNDIINVVASDHRAfstkqkaMGkedftkiphGAPGVEDRMSV- 358
Cdd:pfam01979 208 AGV-----------AHCPFSNSKLRSGRIA-LRKALEDGVKVGLGTDGAG-------SG---------NSLNMLEELRLa 259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472778 359 IWERGVVSGKMDENRFVAVTSSNAAKIYNLYPRKGRIMPGADADVVVWDPDATRTISASTQAqggdfnlfegqrchGVPL 438
Cdd:pfam01979 260 LELQFDPEGGLSPLEALRMATINPAKALGLDDKVGSIEVGKDADLVVVDLDPLAAFFGLKPD--------------GNVK 325
|
....*....
gi 66472778 439 VTISRGRLV 447
Cdd:pfam01979 326 KVIVKGKIV 334
|
|
| PRK07627 |
PRK07627 |
dihydroorotase; Provisional |
9-450 |
1.70e-15 |
|
dihydroorotase; Provisional
Pssm-ID: 181059 [Multi-domain] Cd Length: 425 Bit Score: 78.95 E-value: 1.70e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472778 9 MRILIKGGRVVN--DDVTEEADVYLENGRIQQVGRDlmiPGG---AKVIDATGKLVIPGGIDSSVHLHQTFMNahtqddf 83
Cdd:PRK07627 1 MKIHIKGGRLIDpaAGTDRQADLYVAAGKIAAIGQA---PAGfnaDKTIDASGLIVCPGLVDLSARLREPGYE------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472778 84 YSGT-----KAALLGGSTMLIshVLPDRGASL----LDAFEQMRAHADAKAccdYALHVGVTWWGPKVER--EMEVLVgE 152
Cdd:PRK07627 71 YKATlesemAAAVAGGVTSLV--CPPDTDPVLdepgLVEMLKFRARNLNQA---HVYPLGALTVGLKGEVltEMVELT-E 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472778 153 RGVNSFqmfmAYKDAMMLKDSELYQALNTCKNIGAIARIHAENGELVLEGAKE----ALDLGISGPegmeisrPEELEAE 228
Cdd:PRK07627 145 AGCVGF----SQANVPVVDTQVLLRALQYASTFGFTVWLRPLDAFLGRGGVAAsgavASRLGLSGV-------PVAAETI 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472778 229 ATHRAITIGNRAHCPVYLVNVSSMSAADVIGAARMQGKVVQAETTVAHAVLSGMhyyhqDWAHAAAHV-IAPPLRlDPNT 307
Cdd:PRK07627 214 ALHTIFELMRVTGARVHLARLSSAAGVALVRAAKAEGLPVTCDVGVNHVHLIDV-----DIGYFDSQFrLDPPLR-SQRD 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472778 308 PDHLIGLLGNDIINVVASDHRAFSTKQKAMgkeDFTKIPHGAPGVEDRMS--VIWERgvvSGKMDENRFVAVTSSNAAKI 385
Cdd:PRK07627 288 REAIRAALADGTIDAICSDHTPVDDDEKLL---PFAEATPGATGLELLLPltLKWAD---EAKVPLARALARITSAPARV 361
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 66472778 386 YNLypRKGRIMPGADADVVVWDPDATRTISASTQAQGGDFNLFEGQRCHGVPLVTISRGRLVCEN 450
Cdd:PRK07627 362 LGL--PAGRLAEGAPADLCVFDPDAHWRVEPRALKSQGKNTPFLGYELPGRVRATLVAGQVAFER 424
|
|
| HutI |
COG1228 |
Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport ... |
7-70 |
1.22e-12 |
|
Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440841 [Multi-domain] Cd Length: 386 Bit Score: 69.60 E-value: 1.22e-12
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 66472778 7 SSMRILIKGGRVV---NDDVTEEADVYLENGRIQQVGR--DLMIPGGAKVIDATGKLVIPGGIDSSVHL 70
Cdd:COG1228 6 QAGTLLITNATLVdgtGGGVIENGTVLVEDGKIAAVGPaaDLAVPAGAEVIDATGKTVLPGLIDAHTHL 74
|
|
| PRK09059 |
PRK09059 |
dihydroorotase; Validated |
11-449 |
3.87e-12 |
|
dihydroorotase; Validated
Pssm-ID: 181631 [Multi-domain] Cd Length: 429 Bit Score: 68.52 E-value: 3.87e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472778 11 ILIKGGRVVND--DVTEEADVYLENGRIQQVGRDLM---IPGGAKVIDATGKLVIPGGIDSSVHLHQTfmNAHTQDDFYS 85
Cdd:PRK09059 5 ILLANARIIDPsrGLDEIGTVLIEDGVIVAAGKGAGnqgAPEGAEIVDCAGKAVAPGLVDARVFVGEP--GAEHRETIAS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472778 86 GTKAALLGGSTMLIshVLPDRGA----SLLDAFEQMRAHadAKACCDY----ALHVGVTwwgpkvEREM-EV-LVGERGV 155
Cdd:PRK09059 83 ASRAAAAGGVTSII--MMPDTDPviddVALVEFVKRTAR--DTAIVNIhpaaAITKGLA------GEEMtEFgLLRAAGA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472778 156 NSFqmfmaYKDAMMLKDSE-LYQALNTCKNIGAIARIHAENGELVLEGAKE----ALDLGISGPegmeisrPEELEAEAT 230
Cdd:PRK09059 153 VAF-----TDGRRSVANTQvMRRALTYARDFDAVIVHETRDPDLGGNGVMNeglfASWLGLSGI-------PREAEVIPL 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472778 231 HRAITI----GNRAHCpvylVNVSSMSAADVIGAARMQGKVVQAETTVAHAVLSgmhyyHQD-WAHAAAHVIAPPLRldp 305
Cdd:PRK09059 221 ERDLRLaaltRGRYHA----AQISCAESAEALRRAKDRGLKVTAGVSINHLSLN-----ENDiGEYRTFFKLSPPLR--- 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472778 306 nTPDH---LIGLLGNDIINVVASDHRAFSTKQKAMgkeDFTKIPHGAPGVEDRMSVIWeRGVVSGKMDENRFVAVTSSNA 382
Cdd:PRK09059 289 -TEDDrvaMVEAVASGTIDIIVSSHDPQDVDTKRL---PFSEAAAGAIGLETLLAAAL-RLYHNGEVPLLRLIEALSTRP 363
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 66472778 383 AKIYNLypRKGRIMPGADADVVVWDPDATRTISASTQAQGGDFNLFEGQRCHGVPLVTISRGRLVCE 449
Cdd:PRK09059 364 AEIFGL--PAGTLKPGAPADIIVIDLDEPWVVDPEDLKSRSKNTPFEEARFQGRVVRTIVAGKTVYE 428
|
|
| COG3964 |
COG3964 |
Predicted amidohydrolase [General function prediction only]; |
11-69 |
1.51e-11 |
|
Predicted amidohydrolase [General function prediction only];
Pssm-ID: 443164 [Multi-domain] Cd Length: 376 Bit Score: 66.34 E-value: 1.51e-11
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 66472778 11 ILIKGGRVVNDD--VTEEADVYLENGRIQQVGRDLMIPGGAKVIDATGKLVIPGGIDSSVH 69
Cdd:COG3964 2 LLIKGGRVIDPAngIDGVMDIAIKDGKIAAVAKDIDAAEAKKVIDASGLYVTPGLIDLHTH 62
|
|
| PRK09237 |
PRK09237 |
amidohydrolase/deacetylase family metallohydrolase; |
11-69 |
6.12e-11 |
|
amidohydrolase/deacetylase family metallohydrolase;
Pssm-ID: 236423 [Multi-domain] Cd Length: 380 Bit Score: 64.49 E-value: 6.12e-11
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 66472778 11 ILIKGGRVVNDDVTEEA--DVYLENGRIQQVGRDLMIPGGAKVIDATGKLVIPGGIDSSVH 69
Cdd:PRK09237 1 LLLRGGRVIDPANGIDGviDIAIEDGKIAAVAGDIDGSQAKKVIDLSGLYVSPGWIDLHVH 61
|
|
| CAD_DHOase |
cd01316 |
The eukaryotic CAD protein is a trifunctional enzyme of carbamoylphosphate ... |
60-451 |
1.06e-10 |
|
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: 63.24 E-value: 1.06e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472778 60 IPGGIDSSVHLHQtfMNAHTQDDFYSGTKAALLGGSTMLisHVLPDRGASLLD--AFEQMRAHADAKACCDYALHVGVTw 137
Cdd:cd01316 5 LPGLIDVHVHLRE--PGATHKEDFASGTKAALAGGFTMV--RAMPNTNPSIVDvaSLKLVQSLAQAKARCDYAFSIGAT- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472778 138 wgPKVEREMEVLVGErgVNSFQMFMAYKDAMMLKDS-----ELYQALNTCKNIGAiariHAENGEL--VLegakealdlg 210
Cdd:cd01316 80 --STNAATVGELASE--AVGLKFYLNETFSTLILDKitawaSHFNAWPSTKPIVT----HAKSQTLaaVL---------- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472778 211 isgpegmeisrpeeLEAEATHRAITIgnrahcpvylVNVSSMSAADVIGAARMQGKVVQAETTVAHAVLSgmhyyHQDWA 290
Cdd:cd01316 142 --------------LLASLHNRSIHI----------CHVSSKEEINLIRLAKARGLKVTCEVSPHHLFLS-----QDDLP 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472778 291 HAAAHViAPPLrldpNTPDHLIGLLGN-DIINVVASDHrAFSTKQKAMGKedftKIPHGAPGVEDRMSVIWErGVVSGKM 369
Cdd:cd01316 193 RGQYEV-RPFL----PTREDQEALWENlDYIDCFATDH-APHTLAEKTGN----KPPPGFPGVETSLPLLLT-AVHEGRL 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472778 370 DENRFVAVTSSNAAKIYNLYPrkgrimpgaDADVVV-WDPDATRTISASTQAQGGDFNLFEGQRCHGVPLVTISRGRLVC 448
Cdd:cd01316 262 TIEDIVDRLHTNPKRIFNLPP---------QSDTYVeVDLDEEWTIPKNPLQSKKGWTPFEGKKVKGKVQRVVLRGETAF 332
|
...
gi 66472778 449 ENG 451
Cdd:cd01316 333 IDG 335
|
|
| PRK07228 |
PRK07228 |
5'-deoxyadenosine deaminase; |
9-122 |
1.48e-10 |
|
5'-deoxyadenosine deaminase;
Pssm-ID: 180895 [Multi-domain] Cd Length: 445 Bit Score: 63.48 E-value: 1.48e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472778 9 MRILIKGGRVV---NDDVTEEADVYLENGRIQQVGRDLMIPGGAKVIDATGKLVIPGGIDSSVHLHQTFMNAHTQDdfys 85
Cdd:PRK07228 1 MTILIKNAGIVtmnAKREIVDGDVLIEDDRIAAVGDRLDLEDYDDHIDATGKVVIPGLIQGHIHLCQTLFRGIADD---- 76
|
90 100 110
....*....|....*....|....*....|....*..
gi 66472778 86 gtkAALLggsTMLISHVLPDRGAslLDAfEQMRAHAD 122
Cdd:PRK07228 77 ---LELL---DWLKDRIWPLEAA--HDA-ESMYYSAL 104
|
|
| SsnA |
COG0402 |
Cytosine/adenosine deaminase or related metal-dependent hydrolase [Nucleotide transport and ... |
10-131 |
2.33e-10 |
|
Cytosine/adenosine deaminase or related metal-dependent hydrolase [Nucleotide transport and metabolism, General function prediction only]; Cytosine/adenosine deaminase or related metal-dependent hydrolase is part of the Pathway/BioSystem: Pyrimidine salvage
Pssm-ID: 440171 [Multi-domain] Cd Length: 416 Bit Score: 62.54 E-value: 2.33e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472778 10 RILIKGGRVV----NDDVTEEADVYLENGRIQQVGRDLMIP---GGAKVIDATGKLVIPGGIDSSVHLHQTFM------- 75
Cdd:COG0402 1 DLLIRGAWVLtmdpAGGVLEDGAVLVEDGRIAAVGPGAELParyPAAEVIDAGGKLVLPGLVNTHTHLPQTLLrgladdl 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 66472778 76 --------------NAHTQDDFYSGTKAA----LLGGSTML--ISHVLPDRGASLLDAFEQ--MRAHAdAKACCDYAL 131
Cdd:COG0402 81 plldwleeyiwpleARLDPEDVYAGALLAlaemLRSGTTTVadFYYVHPESADALAEAAAEagIRAVL-GRGLMDRGF 157
|
|
| ATZ_TRZ_like |
cd01298 |
TRZ/ATZ family contains enzymes from the atrazine degradation pathway and related hydrolases. ... |
11-121 |
1.58e-09 |
|
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: 59.91 E-value: 1.58e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472778 11 ILIKGGRVV---NDDVTEEADVYLENGRIQQVGRDLMIPG--GAKVIDATGKLVIPGGIDSSVHLHQTFM---------- 75
Cdd:cd01298 1 ILIRNGTIVttdPRRVLEDGDVLVEDGRIVAVGPALPLPAypADEVIDAKGKVVMPGLVNTHTHLAMTLLrgladdlplm 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 66472778 76 -----------NAHTQDDFYSGTKAA----LLGGSTMLISHVLPDRGAsLLDAFEQ--MRAHA 121
Cdd:cd01298 81 ewlkdliwpleRLLTEEDVYLGALLAlaemIRSGTTTFADMYFFYPDA-VAEAAEElgIRAVL 142
|
|
| D-aminoacylase |
cd01297 |
D-aminoacylases (N-acyl-D-Amino acid amidohydrolases) catalyze the hydrolysis of ... |
11-453 |
1.65e-09 |
|
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: 60.00 E-value: 1.65e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472778 11 ILIKGGRVV----NDDVTeeADVYLENGRIQQVGRDLmIPGGAKVIDATGKLVIPGGIDSsvhlhqtfmnaHTQDDfysg 86
Cdd:cd01297 2 LVIRNGTVVdgtgAPPFT--ADVGIRDGRIAAIGPIL-STSAREVIDAAGLVVAPGFIDV-----------HTHYD---- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472778 87 TKAALLGGSTMLISH-----VLPDRGASLLDAFEQMRAhadakaccdyalhvgvtWWGPKVerEMEVLVGERGVNSFQMF 161
Cdd:cd01297 64 GQVFWDPDLRPSSRQgvttvVLGNCGVSPAPANPDDLA-----------------RLIMLM--EGLVALGEGLPWGWATF 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472778 162 MAYKDAMMLKDSelyqALNTCKNIGAIA-RIHA----------ENGELVLEGAKEALD---LGISGpeGMEI-----SRP 222
Cdd:cd01297 125 AEYLDALEARPP----AVNVAALVGHAAlRRAVmgldareateEELAKMRELLREALEagaLGIST--GLAYaprlyAGT 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472778 223 EELEA------------------------EATHRAITIGNRAHCPVYLVNVSSMSAADVigaarmqGKVVQAETTVAHAV 278
Cdd:cd01297 199 AELVAlarvaaryggvyqthvryegdsilEALDELLRLGRETGRPVHISHLKSAGAPNW-------GKIDRLLALIEAAR 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472778 279 LSGmhyyHQDWAHAAAHVIapplrldpNTPDHLIGLLGNDIINvVASDHRAFSTKQ-KAMGkeDFTkiphgapgvedRMS 357
Cdd:cd01297 272 AEG----LQVTADVYPYGA--------GSEDDVRRIMAHPVVM-GGSDGGALGKPHpRSYG--DFT-----------RVL 325
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472778 358 VIW--ERGVVSgkMDENrfVAVTSSNAAKIYNLYPRkGRIMPGADADVVVWDPDatrtisasTQAQGGDFNLFEgQRCHG 435
Cdd:cd01297 326 GHYvrERKLLS--LEEA--VRKMTGLPARVFGLADR-GRIAPGYRADIVVFDPD--------TLADRATFTRPN-QPAEG 391
|
490
....*....|....*...
gi 66472778 436 VPLVTISrGRLVCENGVF 453
Cdd:cd01297 392 IEAVLVN-GVPVVRDGAF 408
|
|
| FwdA |
COG1229 |
Formylmethanofuran dehydrogenase subunit A [Energy production and conversion]; |
9-71 |
9.52e-09 |
|
Formylmethanofuran dehydrogenase subunit A [Energy production and conversion];
Pssm-ID: 440842 Cd Length: 554 Bit Score: 57.89 E-value: 9.52e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472778 9 MRILIKGGRV------VNDDVteeADVYLENGRI-QQVGRdlmiPGGAKVIDATGKLVIPGGIDSsvHLH 71
Cdd:COG1229 1 MELIIKNGRVydpangIDGEV---MDIAIKDGKIvEEPSD----PKDAKVIDASGKVVMAGGVDI--HTH 61
|
|
| PRK08204 |
PRK08204 |
hypothetical protein; Provisional |
9-75 |
1.65e-08 |
|
hypothetical protein; Provisional
Pssm-ID: 181288 [Multi-domain] Cd Length: 449 Bit Score: 56.93 E-value: 1.65e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 66472778 9 MRILIKGGRVVNDDVT----EEADVYLENGRIQQVGRDLMiPGGAKVIDATGKLVIPGGIDSSVHLHQTFM 75
Cdd:PRK08204 2 KRTLIRGGTVLTMDPAigdlPRGDILIEGDRIAAVAPSIE-APDAEVVDARGMIVMPGLVDTHRHTWQSVL 71
|
|
| PRK08393 |
PRK08393 |
N-ethylammeline chlorohydrolase; Provisional |
9-79 |
1.81e-08 |
|
N-ethylammeline chlorohydrolase; Provisional
Pssm-ID: 181411 [Multi-domain] Cd Length: 424 Bit Score: 56.73 E-value: 1.81e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 66472778 9 MRILIKGGRVVNDDVTE--EADVYLENGRIQQVGRDLMIPGGaKVIDATGKLVIPGgidssvhlhqtFMNAHT 79
Cdd:PRK08393 1 MSILIKNGYVIYGENLKviRADVLIEGNKIVEVKRNINKPAD-TVIDASGSVVSPG-----------FINAHT 61
|
|
| NagA |
COG1820 |
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism]; |
12-71 |
3.99e-08 |
|
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism];
Pssm-ID: 441425 [Multi-domain] Cd Length: 373 Bit Score: 55.49 E-value: 3.99e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 66472778 12 LIKGGRVVNDD-VTEEADVYLENGRIQQVGRdlMIPGGAKVIDATGKLVIPGGIDssVHLH 71
Cdd:COG1820 1 AITNARIFTGDgVLEDGALLIEDGRIAAIGP--GAEPDAEVIDLGGGYLAPGFID--LHVH 57
|
|
| NagA |
cd00854 |
N-acetylglucosamine-6-phosphate deacetylase, NagA, catalyzes the hydrolysis of the N-acetyl ... |
11-71 |
1.51e-07 |
|
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: 53.74 E-value: 1.51e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 66472778 11 ILIKGGRVVNDDVTEEADVYLENGRIQQVGRDLMIPGGAKVIDATGKLVIPGGIDssVHLH 71
Cdd:cd00854 1 LIIKNARILTPGGLEDGAVLVEDGKIVAIGPEDELEEADEIIDLKGQYLVPGFID--IHIH 59
|
|
| COG3653 |
COG3653 |
N-acyl-D-aspartate/D-glutamate deacylase [Secondary metabolites biosynthesis, transport and ... |
8-71 |
2.00e-07 |
|
N-acyl-D-aspartate/D-glutamate deacylase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442870 [Multi-domain] Cd Length: 528 Bit Score: 53.64 E-value: 2.00e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 66472778 8 SMRILIKGGRVVndDVTE----EADVYLENGRIQQVGrDLMIPGGAKVIDATGKLVIPGGIDssVHLH 71
Cdd:COG3653 1 MFDLLIRGGTVV--DGTGappfRADVAIKGGRIVAVG-DLAAAEAARVIDATGLVVAPGFID--IHTH 63
|
|
| PRK08203 |
PRK08203 |
hydroxydechloroatrazine ethylaminohydrolase; Reviewed |
9-121 |
2.08e-07 |
|
hydroxydechloroatrazine ethylaminohydrolase; Reviewed
Pssm-ID: 236184 [Multi-domain] Cd Length: 451 Bit Score: 53.70 E-value: 2.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472778 9 MRILIKGGRVV---NDDVTEEAD--VYLENGRIQQVGRDLMIPG-GAKVIDATGKLVIPGGIDSSVHLHQTFMNAH---- 78
Cdd:PRK08203 1 TTLWIKNPLAIvtmDAARREIADggLVVEGGRIVEVGPGGALPQpADEVFDARGHVVTPGLVNTHHHFYQTLTRALpaaq 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 66472778 79 ------------------TQDDFYSGTKAAL----LGGSTMLISH--VLPDRGASLLD----AFEQ--MRAHA 121
Cdd:PRK08203 81 daelfpwlttlypvwarlTPEMVRVATQTALaellLSGCTTSSDHhyLFPNGLRDALDdqieAAREigMRFHA 153
|
|
| pyrC |
PRK00369 |
dihydroorotase; Provisional |
46-462 |
1.03e-06 |
|
dihydroorotase; Provisional
Pssm-ID: 234738 [Multi-domain] Cd Length: 392 Bit Score: 51.30 E-value: 1.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472778 46 PGGAKVIDAT-GKLVIPGGIDSSVHLHQtfMNAHTQDDFYSGTKAALLGGSTMLI---SHVLPDRGASLLDafEQMRAHA 121
Cdd:PRK00369 31 SRCKPDLDLPqGTLILPGAIDLHVHLRG--LKLSYKEDVASGTSEAAYGGVTLVAdmpNTIPPLNTPEAIT--EKLAELE 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472778 122 dAKACCDYALHVGVTwwgpkveREMEVlVGERGVNSFQMFmaykdammlkdSELYQALNTCKNIGAIAR---IHAENGEL 198
Cdd:PRK00369 107 -YYSRVDYFVYSGVT-------KDPEK-VDKLPIAGYKIF-----------PEDLEREETFRVLLKSRKlkiLHPEVPLA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472778 199 VLEGAKEALDLGisgpegMEISRPEEL-EAEATHraITignRAHCPVYLVnvssmsaadvigAARMQGKVVqaETTVAHA 277
Cdd:PRK00369 167 LKSNRKLRRNCW------YEIAALYYVkDYQNVH--IT---HASNPRTVR------------LAKELGFTV--DITPHHL 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472778 278 VLSGMhyyhqdwAHAAAHViAPPLRlDPNTPDHLIGLLGNdiINVVASDHRAFSTKQKAMgkeDFTKIPHGAPGVEDRMS 357
Cdd:PRK00369 222 LVNGE-------KDCLTKV-NPPIR-DINERLWLLQALSE--VDAIASDHAPHSSFEKLQ---PYEVCPPGIAALSFTPP 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472778 358 VIWERgVVSGKMDENRFVAVTSSNAAKIYNLypRKGRIMPGADADVVVWDPDATRTISASTQAQGGDFNLFEGQRChgvP 437
Cdd:PRK00369 288 FIYTL-VSKGILSIDRAVELISTNPARILGI--PYGEIKEGYRANFTVIQFEDWRYSTKYSKVIETPLDGFELKAS---V 361
|
410 420
....*....|....*....|....*
gi 66472778 438 LVTISRGRLVCENGVFMCAQGSGKF 462
Cdd:PRK00369 362 YATIVQGKLAYLEGEVFPVKGINPF 386
|
|
| AdeC |
COG1001 |
Adenine deaminase [Nucleotide transport and metabolism]; |
11-71 |
1.12e-06 |
|
Adenine deaminase [Nucleotide transport and metabolism];
Pssm-ID: 440625 [Multi-domain] Cd Length: 559 Bit Score: 51.25 E-value: 1.12e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 66472778 11 ILIKGGRVVNddV----TEEADVYLENGRIQQVGRDlmIPGGAKVIDATGKLVIPGGIDSsvHLH 71
Cdd:COG1001 7 LVIKNGRLVN--VftgeILEGDIAIAGGRIAGVGDY--IGEATEVIDAAGRYLVPGFIDG--HVH 65
|
|
| PRK09061 |
PRK09061 |
D-glutamate deacylase; Validated |
6-71 |
1.30e-06 |
|
D-glutamate deacylase; Validated
Pssm-ID: 236369 [Multi-domain] Cd Length: 509 Bit Score: 51.23 E-value: 1.30e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 66472778 6 GSSMRILIKGGRVVN-----DDVteeADVYLENGRIQQVGRDLMipGGAKVIDATGKLVIPGGIDssVHLH 71
Cdd:PRK09061 16 MAPYDLVIRNGRVVDpetglDAV---RDVGIKGGKIAAVGTAAI--EGDRTIDATGLVVAPGFID--LHAH 79
|
|
| Met_dep_hydrolase_B |
cd01307 |
Metallo-dependent hydrolases, subgroup B is part of the superfamily of metallo-dependent ... |
28-72 |
2.57e-06 |
|
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: 49.63 E-value: 2.57e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 66472778 28 DVYLENGRIQQVGRDLMIPGGAKVIDATGKLVIPGGIDSSVHLHQ 72
Cdd:cd01307 1 DVAIENGKIAAVGAALAAPAATQIVDAGGCYVSPGWIDLHVHVYQ 45
|
|
| Bact_CD |
cd01293 |
Bacterial cytosine deaminase and related metal-dependent hydrolases. Cytosine deaminases (CDs) ... |
12-119 |
3.66e-06 |
|
Bacterial cytosine deaminase and related metal-dependent hydrolases. Cytosine deaminases (CDs) catalyze the deamination of cytosine, producing uracil and ammonia. They play an important role in pyrimidine salvage. CDs are present in prokaryotes and fungi, but not mammalian cells. The bacterial enzymes, but not the fungal enzymes, are related to the adenosine deaminases (ADA). The bacterial enzymes are iron dependent and hexameric.
Pssm-ID: 238618 [Multi-domain] Cd Length: 398 Bit Score: 49.55 E-value: 3.66e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472778 12 LIKGGRVvNDDVTEEADVYLENGRIQQVGRDLMIPGGAKVIDATGKLVIPGGIDSSVHLHQTF----------------- 74
Cdd:cd01293 1 LLRNARL-ADGGTALVDIAIEDGRIAAIGPALAVPPDAEEVDAKGRLVLPAFVDPHIHLDKTFtggrwpnnsggtlleai 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 66472778 75 ------MNAHTQDDFYS----GTKAALLGGSTMLISHV--LPDRGASLLDAFEQMRA 119
Cdd:cd01293 80 iaweerKLLLTAEDVKEraerALELAIAHGTTAIRTHVdvDPAAGLKALEALLELRE 136
|
|
| PRK06038 |
PRK06038 |
N-ethylammeline chlorohydrolase; Provisional |
11-81 |
6.38e-06 |
|
N-ethylammeline chlorohydrolase; Provisional
Pssm-ID: 180363 [Multi-domain] Cd Length: 430 Bit Score: 48.59 E-value: 6.38e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 66472778 11 ILIKGGRVVNDDVTE--EADVYLENGRIQQVGRDlmIPGGA-KVIDATGKLVIPGGIDSSVHLHQTFMNAHTQD 81
Cdd:PRK06038 4 IIIKNAYVLTMDAGDlkKGSVVIEDGTITEVSES--TPGDAdTVIDAKGSVVMPGLVNTHTHAAMTLFRGYADD 75
|
|
| FMDH_A |
cd01304 |
Formylmethanofuran dehydrogenase (FMDH) subunit A; Methanogenic bacteria and archea derive ... |
13-69 |
7.90e-06 |
|
Formylmethanofuran dehydrogenase (FMDH) subunit A; Methanogenic bacteria and archea derive the energy for autotrophic growth from methanogenesis, the reduction of CO2 with molecular hydrogen as the electron donor. FMDH catalyzes the first step in methanogenesis, the formyl-methanofuran synthesis. In this step, CO2 is bound to methanofuran and subsequently reduced to the formyl state with electrons derived from hydrogen.
Pssm-ID: 238629 [Multi-domain] Cd Length: 541 Bit Score: 48.56 E-value: 7.90e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472778 13 IKGGRVV---NDDVTEEADVYLENGRIQQVGRDlmiPGGAKVIDATGKLVIPGGIDSSVH 69
Cdd:cd01304 1 IKNGTVYdplNGINGEKMDIFIRDGKIVESSSG---AKPAKVIDASGKVVMAGGVDMHSH 57
|
|
| YtcJ |
COG1574 |
Predicted amidohydrolase YtcJ [General function prediction only]; |
2-123 |
8.04e-06 |
|
Predicted amidohydrolase YtcJ [General function prediction only];
Pssm-ID: 441182 [Multi-domain] Cd Length: 535 Bit Score: 48.64 E-value: 8.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472778 2 MSGGGSSMRILIKGGRV--VNDDVTEEADVYLENGRIQQVGRD----LMIPGGAKVIDATGKLVIPGGIDSsvHLHqtfm 75
Cdd:COG1574 1 MKLAAAAADLLLTNGRIytMDPAQPVAEAVAVRDGRIVAVGSDaevrALAGPATEVIDLGGKTVLPGFIDA--HVH---- 74
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 66472778 76 nahtqddfysgtkaaLLGGSTMLISHVLPDrGASLLDAFEQMRAHADA 123
Cdd:COG1574 75 ---------------LLGGGLALLGVDLSG-ARSLDELLARLRAAAAE 106
|
|
| PRK05985 |
PRK05985 |
cytosine deaminase; Provisional |
27-74 |
1.02e-05 |
|
cytosine deaminase; Provisional
Pssm-ID: 180337 [Multi-domain] Cd Length: 391 Bit Score: 48.00 E-value: 1.02e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 66472778 27 ADVYLENGRIQQVGRDLMIPGGAKVIDATGKLVIPGGIDSSVHLHQTF 74
Cdd:PRK05985 17 VDILIRDGRIAAIGPALAAPPGAEVEDGGGALALPGLVDGHIHLDKTF 64
|
|
| Met_dep_hydrolase_C |
cd01309 |
Metallo-dependent hydrolases, subgroup C is part of the superfamily of metallo-dependent ... |
33-70 |
1.71e-05 |
|
Metallo-dependent hydrolases, subgroup C is part of the superfamily of metallo-dependent hydrolases, a large group of proteins that show conservation in their 3-dimensional fold (TIM barrel) and in details of their active site. The vast majority of the members have a conserved metal binding site, involving four histidines and one aspartic acid residue. In the common reaction mechanism, the metal ion (or ions) deprotonate a water molecule for a nucleophilic attack on the substrate. The function of this subgroup is unknown.
Pssm-ID: 238634 [Multi-domain] Cd Length: 359 Bit Score: 47.31 E-value: 1.71e-05
10 20 30
....*....|....*....|....*....|....*...
gi 66472778 33 NGRIQQVGRDLMIPGGAKVIDATGKLVIPGGIDSSVHL 70
Cdd:cd01309 1 DGKIVAVGAEITTPADAEVIDAKGKHVTPGLIDAHSHL 38
|
|
| PRK06380 |
PRK06380 |
metal-dependent hydrolase; Provisional |
9-75 |
2.32e-05 |
|
metal-dependent hydrolase; Provisional
Pssm-ID: 180548 [Multi-domain] Cd Length: 418 Bit Score: 46.80 E-value: 2.32e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472778 9 MRILIKGGRVVNDDVTEE---ADVYLENGRIQQVGRDLmiPGGAKVIDATGKLVIPGGIDSSVHLHQTFM 75
Cdd:PRK06380 1 MSILIKNAWIVTQNEKREilqGNVYIEGNKIVYVGDVN--EEADYIIDATGKVVMPGLINTHAHVGMTAS 68
|
|
| NagA |
COG1820 |
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism]; |
375-409 |
2.61e-05 |
|
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism];
Pssm-ID: 441425 [Multi-domain] Cd Length: 373 Bit Score: 46.63 E-value: 2.61e-05
10 20 30
....*....|....*....|....*....|....*
gi 66472778 375 VAVTSSNAAKIYNLYPRKGRIMPGADADVVVWDPD 409
Cdd:COG1820 328 VRMASLNPARALGLDDRKGSIAPGKDADLVVLDDD 362
|
|
| PRK15446 |
PRK15446 |
phosphonate metabolism protein PhnM; Provisional |
8-71 |
4.71e-05 |
|
phosphonate metabolism protein PhnM; Provisional
Pssm-ID: 237967 [Multi-domain] Cd Length: 383 Bit Score: 45.94 E-value: 4.71e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 66472778 8 SMRILIKGGRVVNDDVTEEADVYLENGRIQQVGRDLMIPGGAkvIDATGKLVIPGGIDssvhLH 71
Cdd:PRK15446 1 MMEMILSNARLVLPDEVVDGSLLIEDGRIAAIDPGASALPGA--IDAEGDYLLPGLVD----LH 58
|
|
| Isoaspartyl-dipeptidase |
cd01308 |
Isoaspartyl dipeptidase hydrolyzes the beta-L-isoaspartyl linkages in dipeptides, as part of ... |
12-70 |
9.24e-05 |
|
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: 45.07 E-value: 9.24e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 66472778 12 LIKGGRVVNDDVTEEADVYLENGRIQQVGRDLMIPGGAK--VIDATGKLVIPGGIDSSVHL 70
Cdd:cd01308 3 LIKNAEVYAPEYLGKKDILIAGGKILAIEDQLNLPGYENvtVVDLHGKILVPGFIDQHVHI 63
|
|
| NagA |
cd00854 |
N-acetylglucosamine-6-phosphate deacetylase, NagA, catalyzes the hydrolysis of the N-acetyl ... |
375-409 |
1.40e-04 |
|
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: 44.49 E-value: 1.40e-04
10 20 30
....*....|....*....|....*....|....*
gi 66472778 375 VAVTSSNAAKIYNLYPRKGRIMPGADADVVVWDPD 409
Cdd:cd00854 330 VRMASLNPAKLLGLDDRKGSLKPGKDADLVVLDDD 364
|
|
| PRK09228 |
PRK09228 |
guanine deaminase; Provisional |
31-75 |
1.48e-04 |
|
guanine deaminase; Provisional
Pssm-ID: 236419 [Multi-domain] Cd Length: 433 Bit Score: 44.41 E-value: 1.48e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 66472778 31 LENGRIQQVG--RDLM--IPGGAKVIDATGKLVIPGGIDSSVHLHQTFM 75
Cdd:PRK09228 36 VEDGRIVAAGpyAELRaqLPADAEVTDYRGKLILPGFIDTHIHYPQTDM 84
|
|
| PRK07203 |
PRK07203 |
putative aminohydrolase SsnA; |
11-74 |
2.65e-04 |
|
putative aminohydrolase SsnA;
Pssm-ID: 235963 [Multi-domain] Cd Length: 442 Bit Score: 43.77 E-value: 2.65e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 66472778 11 ILIKGGRVVNDD----VTEEADVYLENGRIQQVGRDLMIPG---GAKVIDATGKLVIPGGIDSSVHLHQTF 74
Cdd:PRK07203 2 LLIGNGTAITRDpakpVIEDGAIAIEGNVIVEIGTTDELKAkypDAEFIDAKGKLIMPGLINSHNHIYSGL 72
|
|
| Amidohydro_3 |
pfam07969 |
Amidohydrolase family; |
356-412 |
8.53e-04 |
|
Amidohydrolase family;
Pssm-ID: 400360 [Multi-domain] Cd Length: 464 Bit Score: 42.13 E-value: 8.53e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 66472778 356 MSVIWERGVVSGKMDENRF---VAVTSSNAAKIYNLYPRKGRIMPGADADVVVWDPDATR 412
Cdd:pfam07969 383 MRQTAGGGEVLGPDEELSLeeaLALYTSGPAKALGLEDRKGTLGVGKDADLVVLDDDPLT 442
|
|
| Imidazolone-5PH |
cd01296 |
Imidazolonepropionase/imidazolone-5-propionate hydrolase (Imidazolone-5PH) catalyzes the third ... |
29-70 |
1.26e-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: 1.26e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 66472778 29 VYLENGRIQQVGR--DLMIPGGA--KVIDATGKLVIPGGIDSSVHL 70
Cdd:cd01296 1 IAIRDGRIAAVGPaaSLPAPGPAaaEEIDAGGRAVTPGLVDCHTHL 46
|
|
| Isoaspartyl-dipeptidase |
cd01308 |
Isoaspartyl dipeptidase hydrolyzes the beta-L-isoaspartyl linkages in dipeptides, as part of ... |
377-409 |
1.38e-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: 41.22 E-value: 1.38e-03
10 20 30
....*....|....*....|....*....|...
gi 66472778 377 VTSSNAAKIYNLYPrKGRIMPGADADVVVWDPD 409
Cdd:cd01308 330 VITSNVARILKLRK-KGEIQPGFDADLVILDKD 361
|
|
| ureC |
PRK13207 |
urease subunit alpha; Reviewed |
27-70 |
3.35e-03 |
|
urease subunit alpha; Reviewed
Pssm-ID: 237305 [Multi-domain] Cd Length: 568 Bit Score: 40.16 E-value: 3.35e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 66472778 27 ADVYLENGRIQQVGR----------DLMIPGGAKVIDATGKLVIPGGIDSSVHL 70
Cdd:PRK13207 85 ADIGIKDGRIVAIGKagnpdiqdgvDIIIGPGTEVIAGEGLIVTAGGIDTHIHF 138
|
|
| Amidohydro_3 |
pfam07969 |
Amidohydrolase family; |
50-82 |
4.16e-03 |
|
Amidohydrolase family;
Pssm-ID: 400360 [Multi-domain] Cd Length: 464 Bit Score: 39.82 E-value: 4.16e-03
10 20 30
....*....|....*....|....*....|...
gi 66472778 50 KVIDATGKLVIPGGIDSSVHLHQTFMNAHTQDD 82
Cdd:pfam07969 1 EVIDAKGRLVLPGFVDPHTHLDGGGLNLRELRL 33
|
|
| FwdA |
COG1229 |
Formylmethanofuran dehydrogenase subunit A [Energy production and conversion]; |
377-451 |
4.29e-03 |
|
Formylmethanofuran dehydrogenase subunit A [Energy production and conversion];
Pssm-ID: 440842 Cd Length: 554 Bit Score: 39.79 E-value: 4.29e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 66472778 377 VTSSNAAKIYNLyPRKGRIMPGADADVVVWDPDATRTISASTQAqggdfnLFEGqrchgvPLVTISRGRLVCENG 451
Cdd:COG1229 437 MTRAGPAKALGL-ADRGHLGVGADADIAIYDINPDDKDYEDIEK------MFSK------PAYVIKDGEVVVKDG 498
|
|
| YtcJ_like |
cd01300 |
YtcJ_like metal dependent amidohydrolases. YtcJ is a Bacillus subtilis ORF of unknown function. ... |
28-73 |
9.92e-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: 38.83 E-value: 9.92e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 66472778 28 DVYLENGRIQQVGRD----LMIPGGAKVIDATGKLVIPGGIDSSVHLHQT 73
Cdd:cd01300 1 AVAVRDGRIVAVGSDaeakALKGPATEVIDLKGKTVLPGFIDSHSHLLLG 50
|
|
| |
