|
Name |
Accession |
Description |
Interval |
E-value |
| D-HYD |
cd01314 |
D-hydantoinases (D-HYD) also called dihydropyrimidases (DHPase) and related proteins; DHPases ... |
17-436 |
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: 656.21 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119569521 17 LLIRGGRIVNDDQSFYADVHVEDGLIKQIGENLIVPGGIKTIDAHGLMVLPGGVDVHTRLQMPVLGMTPADDFCQGTKAA 96
Cdd:cd01314 1 LIIKNGTIVTADGSFKADILIEDGKIVAIGPNLEAPGGVEVIDATGKYVLPGGIDPHTHLELPFMGTVTADDFESGTRAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119569521 97 LAGGTTMILDHVFPDTGVSLLAAYEQWRERADSAACCDYSLHVDITRWHESIKEELEALVKeKGVNSFLVFMAYKDRCQC 176
Cdd:cd01314 81 AAGGTTTIIDFAIPNKGQSLLEAVEKWRGKADGKSVIDYGFHMIITDWTDSVIEELPELVK-KGISSFKVFMAYKGLLMV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119569521 177 SDSQMYEIFSIIRDLGALAQVHAENGDIVEEEQKRLLELGITGPEGHVLSHPEEVEAEAVYRAVTIAKQANCPLYVTKVM 256
Cdd:cd01314 160 DDEELLDVLKRAKELGALVMVHAENGDVIAELQKKLLAQGKTGPEYHALSRPPEVEAEATARAIRLAELAGAPLYIVHVS 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119569521 257 SKGAADAIAQAKRRGVVVFGEPITASLGTDGSHYWsKNWAKAAAFVTSPPVNPDpTTADHLTCLLSSGDLQVTGSAHCTF 336
Cdd:cd01314 240 SKEAADEIARARKKGLPVYGETCPQYLLLDDSDYW-KDWFEGAKYVCSPPLRPK-EDQEALWDGLSSGTLQTVGSDHCPF 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119569521 337 TTAQKAVGKDNFALIPEGTNGIEERMSMVWEKCVASGKMDENEFVAVTSTNAAKIFNFYPRKGRVAVGSDADLVIWNPKA 416
Cdd:cd01314 318 NFAQKARGKDDFTKIPNGVPGVETRMPLLWSEGVAKGRITLEKFVELTSTNPAKIFGLYPRKGTIAVGSDADLVIWDPNA 397
|
410 420
....*....|....*....|....*...
gi 119569521 417 TKIISAKTHNLLA--------EIHGVPR 436
Cdd:cd01314 398 EKTISADTHHHNVdynifegmKVKGWPV 425
|
|
| D-hydantoinase |
TIGR02033 |
D-hydantoinase; This model represents the D-hydantoinase (dihydropyrimidinase) which primarily ... |
17-430 |
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: 587.05 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119569521 17 LLIRGGRIVNDDQSFYADVHVEDGLIKQIGENLIVPGGIKTIDAHGLMVLPGGVDVHTRLQMPVLGMTPADDFCQGTKAA 96
Cdd:TIGR02033 1 LLIKGGTVVNADDVFQADVLIEGGKIVAVGDNLIPPDAVEVIDATGKYVLPGGIDVHTHLEMPFGGTTTADDFFTGTKAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119569521 97 LAGGTTMILDHVFPDTGVSLLAAYEQWRERADSAACCDYSLHVDITRWHESIKEELEALVKEKGVNSFLVFMAYKDRCQC 176
Cdd:TIGR02033 81 AAGGTTTIIDFVVPEKGSSLTEALETWHEKAEGKSVIDYGFHMDITHWNDSVLEEHIPEVKEEGINSFKVFMAYKNLLMV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119569521 177 SDSQMYEIFSIIRDLGALAQVHAENGDIVEEEQKRLLELGITGPEGHVLSHPEEVEAEAVYRAVTIAKQANCPLYVTKVM 256
Cdd:TIGR02033 161 DDEELFEILKRLKELGALLQVHAENGDIIAELQARMLAQGITGPEYHALSRPPELEAEAVARAITLAALADAPLYVVHVS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119569521 257 SKGAADAIAQAKRRGVVVFGEPITASLGTDGSHYWsKNWAKAAAFVTSPPVNpDPTTADHLTCLLSSGDLQVTGSAHCTF 336
Cdd:TIGR02033 241 TKDAADEIAQARKKGQPVFGETCPQYLVLDDTHYD-KPGFEGAKYVCSPPLR-EPEDQDALWSALSSGALQTVGSDHCTF 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119569521 337 TTAQK-AVGKDNFALIPEGTNGIEERMSMVWEKCVASGKMDENEFVAVTSTNAAKIFNFYPRKGRVAVGSDADLVIWNPK 415
Cdd:TIGR02033 319 NFAQKkAIGKDDFTKIPNGGPGVEERMSLLFDEGVAKGRITLEKFVEVTSTNPAKIFNLYPRKGTIAVGSDADIVIWDPN 398
|
410
....*....|....*
gi 119569521 416 ATKIISAKTHNLLAE 430
Cdd:TIGR02033 399 RTTVISAETHHSNAD 413
|
|
| PRK08323 |
PRK08323 |
phenylhydantoinase; Validated |
16-425 |
3.52e-174 |
|
phenylhydantoinase; Validated
Pssm-ID: 236240 [Multi-domain] Cd Length: 459 Bit Score: 498.54 E-value: 3.52e-174
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119569521 16 RLLIRGGRIVNDDQSFYADVHVEDGLIKQIGENlivpGGIKTIDAHGLMVLPGGVDVHTRLQMPVLGMTPADDFCQGTKA 95
Cdd:PRK08323 2 STLIKNGTVVTADDTYKADVLIEDGKIAAIGAN----LGDEVIDATGKYVMPGGIDPHTHMEMPFGGTVSSDDFETGTRA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119569521 96 ALAGGTTMILDHVFPDTGVSLLAAYEQWRERADSAACCDYSLHVDITRWHESIKEELEALVKEkGVNSFLVFMAYKDRCQ 175
Cdd:PRK08323 78 AACGGTTTIIDFALQPKGQSLREALEAWHGKAAGKAVIDYGFHMIITDWNEVVLDEMPELVEE-GITSFKLFMAYKGALM 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119569521 176 CSDSQMYEIFSIIRDLGALAQVHAENGDIVEEEQKRLLELGITGPEGHVLSHPEEVEAEAVYRAVTIAKQANCPLYVTKV 255
Cdd:PRK08323 157 LDDDELLRALQRAAELGALPMVHAENGDAIAYLQAKLLAEGKTGPEYHALSRPPEVEGEATNRAIMLAELAGAPLYIVHV 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119569521 256 MSKGAADAIAQAKRRGVVVFGEPITASLGTDGSHYWSKNWAKAAAFVTSPPVNpDPTTADHLTCLLSSGDLQVTGSAHCT 335
Cdd:PRK08323 237 SCKEALEAIRRARARGQRVFGETCPQYLLLDESEYDGPDWFEGAKYVMSPPLR-DKEHQDALWRGLQDGDLQVVATDHCP 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119569521 336 FTTAQKA-VGKDNFALIPEGTNGIEERMSMVWEKCVASGKMDENEFVAVTSTNAAKIFNFYPRKGRVAVGSDADLVIWNP 414
Cdd:PRK08323 316 FCFEQKKqLGRGDFTKIPNGTPGVEDRMPLLFSEGVMTGRITLNRFVELTSTNPAKIFGLYPRKGTIAVGADADIVIWDP 395
|
410
....*....|.
gi 119569521 415 KATKIISAKTH 425
Cdd:PRK08323 396 NATKTISASTL 406
|
|
| PLN02942 |
PLN02942 |
dihydropyrimidinase |
12-425 |
7.17e-174 |
|
dihydropyrimidinase
Pssm-ID: 178530 Cd Length: 486 Bit Score: 498.60 E-value: 7.17e-174
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119569521 12 ITSDRLLIRGGRIVNDDQSFYADVHVEDGLIKQIGENLIVPGGIKTIDAHGLMVLPGGVDVHTRLQMPVLGMTPADDFCQ 91
Cdd:PLN02942 2 ASSTKILIKGGTVVNAHHQELADVYVEDGIIVAVAPNLKVPDDVRVIDATGKFVMPGGIDPHTHLAMPFMGTETIDDFFS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119569521 92 GTKAALAGGTTMILDHVFPDTGvSLLAAYEQWRERADSAaCCDYSLHVDITRWHESIKEELEALVKEKGVNSFLVFMAYK 171
Cdd:PLN02942 82 GQAAALAGGTTMHIDFVIPVNG-NLLAGYEAYEKKAEKS-CMDYGFHMAITKWDDTVSRDMETLVKEKGINSFKFFMAYK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119569521 172 DRCQCSDSQMYEIFSIIRDLGALAQVHAENGDIVEEEQKRLLELGITGPEGHVLSHPEEVEAEAVYRAVTIAKQANCPLY 251
Cdd:PLN02942 160 GSLMVTDELLLEGFKRCKSLGALAMVHAENGDAVFEGQKRMIELGITGPEGHALSRPPLLEGEATARAIRLAKFVNTPLY 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119569521 252 VTKVMSKGAADAIAQAKRRGVVVFGEPITASLGTDGSHYWSKNWAKAAAFVTSPPVNPdpttADH---LTCLLSSGDLQV 328
Cdd:PLN02942 240 VVHVMSIDAMEEIARARKSGQRVIGEPVVSGLVLDDSKLWDPDFTIASKYVMSPPIRP----AGHgkaLQAALSSGILQL 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119569521 329 TGSAHCTFTTAQKAVGKDNFALIPEGTNGIEERMSMVWEKCVASGKMDENEFVAVTSTNAAKIFNFYPRKGRVAVGSDAD 408
Cdd:PLN02942 316 VGTDHCPFNSTQKAFGKDDFRKIPNGVNGIEERMHLVWDTMVESGQISPTDYVRVTSTECAKIFNIYPRKGAILAGSDAD 395
|
410
....*....|....*..
gi 119569521 409 LVIWNPKATKIISAKTH 425
Cdd:PLN02942 396 IIILNPNSTFTISAKTH 412
|
|
| AllB |
COG0044 |
Dihydroorotase or related cyclic amidohydrolase [Nucleotide transport and metabolism]; ... |
18-425 |
1.01e-113 |
|
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: 343.23 E-value: 1.01e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119569521 18 LIRGGRIVNDDQSFYADVHVEDGLIKQIGENLIVPGGIKTIDAHGLMVLPGGVDVHTRLQMPvlGMTPADDFCQGTKAAL 97
Cdd:COG0044 1 LIKNGRVVDPGGLERADVLIEDGRIAAIGPDLAAPEAAEVIDATGLLVLPGLIDLHVHLREP--GLEHKEDIETGTRAAA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119569521 98 AGGTTMILDhvFPDT--GVSLLAAYEQWRERADSAACCDYSLHVDITRWHESIKEELEALVkEKGVNSFLVFMAYKD-RC 174
Cdd:COG0044 79 AGGVTTVVD--MPNTnpVTDTPEALEFKLARAEEKALVDVGPHGALTKGLGENLAELGALA-EAGAVAFKVFMGSDDgNP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119569521 175 QCSDSQMYEIFSIIRDLGALAQVHAENGDIVEEeqkRLLELGITGPEGHVLSHPEEVEAEAVYRAVTIAKQANCPLYVTK 254
Cdd:COG0044 156 VLDDGLLRRALEYAAEFGALVAVHAEDPDLIRG---GVMNEGKTSPRLGLKGRPAEAEEEAVARDIALAEETGARLHIVH 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119569521 255 VMSKGAADAIAQAKRRGVVVFGE--P----ITAS-LGTDGSHYwsknwakaaafVTSPPVNpdpTTADHLTCL--LSSGD 325
Cdd:COG0044 233 VSTAEAVELIREAKARGLPVTAEvcPhhltLTDEdLERYGTNF-----------KVNPPLR---TEEDREALWegLADGT 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119569521 326 LQVTGSAHCTFTTAQKAvgkDNFALIPEGTNGIEERMSMVWEKCVASGKMDENEFVAVTSTNAAKIFNFyPRKGRVAVGS 405
Cdd:COG0044 299 IDVIATDHAPHTLEEKE---LPFAEAPNGIPGLETALPLLLTELVHKGRLSLERLVELLSTNPARIFGL-PRKGRIAVGA 374
|
410 420
....*....|....*....|
gi 119569521 406 DADLVIWNPKATKIISAKTH 425
Cdd:COG0044 375 DADLVLFDPDAEWTVTAEDL 394
|
|
| PRK13404 |
PRK13404 |
dihydropyrimidinase; Provisional |
17-422 |
7.17e-101 |
|
dihydropyrimidinase; Provisional
Pssm-ID: 184033 [Multi-domain] Cd Length: 477 Bit Score: 311.63 E-value: 7.17e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119569521 17 LLIRGGRIVNDDQSFYADVHVEDGLIKQIGENLivPGGIKTIDAHGLMVLPGGVDVHTRLQMPV-LGMTPADDFCQGTKA 95
Cdd:PRK13404 6 LVIRGGTVVTATDTFQADIGIRGGRIAALGEGL--GPGAREIDATGRLVLPGGVDSHCHIDQPSgDGIMMADDFYTGTVS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119569521 96 ALAGGTTMILDHVFPDTGVSLLAAYEQWRERADSAACCDYSLHV---DITRwhESIKEELEALVKEkGVNSFLVFMAYkD 172
Cdd:PRK13404 84 AAFGGTTTVIPFAAQHRGQSLREAVEDYHRRAAGKAVIDYAFHLivaDPTE--EVLTEELPALIAQ-GYTSFKVFMTY-D 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119569521 173 RCQCSDSQMYEIFSIIRDLGALAQVHAENGDIVEEEQKRLLELGITGPEGHVLSHPEEVEAEAVYRAVTIAKQANCPLYV 252
Cdd:PRK13404 160 DLKLDDRQILDVLAVARRHGAMVMVHAENHDMIAWLTKRLLAAGLTAPKYHAISRPMLAEREATHRAIALAELVDVPILI 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119569521 253 TKVMSKGAADAIAQAKRRGVVVFGEP------ITAS-LGTDGSHywsknwakAAAFVTSPPvnpdPTTADHLTCL---LS 322
Cdd:PRK13404 240 VHVSGREAAEQIRRARGRGLKIFAETcpqylfLTAEdLDRPGME--------GAKYICSPP----PRDKANQEAIwngLA 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119569521 323 SGDLQVTGSAHCTF---TTAQKAVGKDN--FALIPEGTNGIEERMSMVWEKCVASGKMDENEFVAVTSTNAAKIFNFYPR 397
Cdd:PRK13404 308 DGTFEVFSSDHAPFrfdDTDGKLAAGANpsFKAIANGIPGIETRLPLLFSEGVVKGRISLNRFVALTSTNPAKLYGLYPR 387
|
410 420
....*....|....*....|....*
gi 119569521 398 KGRVAVGSDADLVIWNPKATKIISA 422
Cdd:PRK13404 388 KGAIAIGADADIAIWDPDREVTITN 412
|
|
| L-HYD_ALN |
cd01315 |
L-Hydantoinases (L-HYDs) and Allantoinase (ALN); L-Hydantoinases are a member of the ... |
17-422 |
2.85e-56 |
|
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: 194.43 E-value: 2.85e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119569521 17 LLIRGGRIVNDDQSFYADVHVEDGLIKQIGENLIVPGGIKTIDAHGLMVLPGGVDVHTRLQMPvlGMTPADDFCQGTKAA 96
Cdd:cd01315 2 LVIKNGRVVTPDGVREADIAVKGGKIAAIGPDIANTEAEEVIDAGGLVVMPGLIDTHVHINEP--GRTEWEGFETGTKAA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119569521 97 LAGGTTMILD---HVFPDT--GVSLLAAYEQWRERadsaaccdysLHVDITRWHESIK---EELEALVkEKGVNSFLVFM 168
Cdd:cd01315 80 AAGGITTIIDmplNSIPPTttVENLEAKLEAAQGK----------LHVDVGFWGGLVPgnlDQLRPLD-EAGVVGFKCFL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119569521 169 A---YKDRCQCSDSQMYEIFSIIRDLGALAQVHAENGDIVEEEQKRLLELGITGPEGHVLSHPEEVEAEAVYRAVTIAKQ 245
Cdd:cd01315 149 CpsgVDEFPAVDDEQLEEAMKELAKTGSVLAVHAENPEITEALQEQAKAKGKRDYRDYLASRPVFTEVEAIQRILLLAKE 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119569521 246 ANCPLYVTKVMSKGAADAIAQAKRRGVVVFGEPITaslgtdgsHYWS-------KNwakAAAFVTSPPVNpDPTTADHLT 318
Cdd:cd01315 229 TGCRLHIVHLSSAEAVPLIREARAEGVDVTVETCP--------HYLTftaedvpDG---GTEFKCAPPIR-DAANQEQLW 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119569521 319 CLLSSGDLQVTGSAHCTFTTAQKAVGKDNFALIPEGTNGIEERMSMVWEKCVASGKMDENEFVAVTSTNAAKIFNFYPRK 398
Cdd:cd01315 297 EALENGDIDMVVSDHSPCTPELKLLGKGDFFKAWGGISGLQLGLPVMLTEAVNKRGLSLEDIARLMCENPAKLFGLSHQK 376
|
410 420
....*....|....*....|....
gi 119569521 399 GRVAVGSDADLVIWNPKATKIISA 422
Cdd:cd01315 377 GRIAVGYDADFVVWDPEEEFTVDA 400
|
|
| Cyclic_amidohydrolases |
cd01302 |
Cyclic amidohydrolases, including hydantoinase, dihydropyrimidinase, allantoinase, and ... |
63-425 |
8.28e-51 |
|
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: 176.81 E-value: 8.28e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119569521 63 LMVLPGGVDVHTRLQMPVLGMTpADDFCQGTKAALAGGTTMILDHVFPDTGVSLLAAYEQWRERADSAACCDYSLHVDIT 142
Cdd:cd01302 1 LLVLPGFIDIHVHLRDPGGTTY-KEDFESGSRAAAAGGVTTVIDMPNTGPPPIDLPAIELKIKLAEESSYVDFSFHAGIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119569521 143 RwhESIKEELEaLVKEKGVNSFLVFMAYK--DRCQCSDSQMYEIFSIIRDLGALAQVHAEngdiveeeqkrllelgitgp 220
Cdd:cd01302 80 P--GDVTDELK-KLFDAGINSLKVFMNYYfgELFDVDDGTLMRTFLEIASRGGPVMVHAE-------------------- 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119569521 221 eghvlshpeeveaeavyRAVTIAKQANCPLYVTKVMSKGAADAIAQAKRRGVVVFGEPITASLGTDGShYWSKNWAKaaa 300
Cdd:cd01302 137 -----------------RAAQLAEEAGANVHIAHVSSGEALELIKFAKNKGVKVTCEVCPHHLFLDES-MLRLNGAW--- 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119569521 301 FVTSPPVNPdPTTADHLTCLLSSGDLQVTGSAHCTFTTAQKAVGKDnFALIPEGTNGIEERMSMVWEKcVASGKMDENEF 380
Cdd:cd01302 196 GKVNPPLRS-KEDREALWEGVKNGKIDTIASDHAPHSKEEKESGKD-IWKAPPGFPGLETRLPILLTE-GVKRGLSLETL 272
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 119569521 381 VAVTSTNAAKIFNFYPrKGRVAVGSDADLVIWNPKATKIISAKTH 425
Cdd:cd01302 273 VEILSENPARIFGLYP-KGTIAVGYDADLVIVDPKKEWKVTAEEI 316
|
|
| PRK06189 |
PRK06189 |
allantoinase; Provisional |
17-417 |
2.59e-40 |
|
allantoinase; Provisional
Pssm-ID: 235732 [Multi-domain] Cd Length: 451 Bit Score: 151.01 E-value: 2.59e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119569521 17 LLIRGGRIVNDDQSFYADVHVEDGLIKQIGENLIVPGGiKTIDAHGLMVLPGGVDVHTRLQMPvlGMTPADDFCQGTKAA 96
Cdd:PRK06189 5 LIIRGGKVVTPEGVYRADIGIKNGKIAEIAPEISSPAR-EIIDADGLYVFPGMIDVHVHFNEP--GRTHWEGFATGSAAL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119569521 97 LAGGTTMILDHVFPDTGVSLLA-AYEQWRERADSAACCDYSLHVDITRWHesiKEELEALVkEKGVNSFLVFMAYK--DR 173
Cdd:PRK06189 82 AAGGCTTYFDMPLNSIPPTVTReALDAKAELARQKSAVDFALWGGLVPGN---LEHLRELA-EAGVIGFKAFMSNSgtDE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119569521 174 CQ-CSDSQMYEIFSIIRDLGALAQVHAENGDIVEEEQKRLLELGITGPEGHVLSHPEEVEAEAVYRAVTIAKQANCPLYV 252
Cdd:PRK06189 158 FRsSDDLTLYEGMKEIAALGKILALHAESDALTRHLTTQARQQGKTDVRDYLESRPVVAELEAVQRALLYAQETGCPLHF 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119569521 253 TKVMSKGAADAIAQAKRRGVVV----------FGEPITASLGTdgshywsknWAKAAafvtsPPVNpDPTTADHLTCLLS 322
Cdd:PRK06189 238 VHISSGKAVALIAEAKKRGVDVsvetcphyllFTEEDFERIGA---------VAKCA-----PPLR-SRSQKEELWRGLL 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119569521 323 SGDLQVTGSAHCTFTTAQKAvgKDNFALIPEGTNGIEERMSMVWEKCVASGKMDENEFVAVTSTNAAKIFNFyPRKGRVA 402
Cdd:PRK06189 303 AGEIDMISSDHSPCPPELKE--GDDFFLVWGGISGGQSTLLVMLTEGYIERGIPLETIARLLATNPAKRFGL-PQKGRLE 379
|
410
....*....|....*
gi 119569521 403 VGSDADLVIWNPKAT 417
Cdd:PRK06189 380 VGADADFVLVDLDET 394
|
|
| pyrC_multi |
TIGR00857 |
dihydroorotase, multifunctional complex type; In contrast to the homodimeric type of ... |
33-424 |
1.25e-39 |
|
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: 148.36 E-value: 1.25e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119569521 33 ADVHVEDGLIKQIGENLIVPGGiKTIDAHGLMVLPGGVDVHTRLQMPvlGMTPADDFCQGTKAALAGGTTMILDhvFPDT 112
Cdd:TIGR00857 6 VDILVEGGRIKKIGKLRIPPDA-EVIDAKGLLVLPGFIDLHVHLRDP--GEEYKEDIESGSKAAAHGGFTTVAD--MPNT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119569521 113 GVSLLAAYE-QWR-ERADSAACCDYSLHVDITRwHESIKEELEAlvkekgvnSFLVFMA-----YKDRCQC--SDSQMYE 183
Cdd:TIGR00857 81 KPPIDTPETlEWKlQRLKKVSLVDVHLYGGVTQ-GNQGKELTEA--------YELKEAGavgrmFTDDGSEvqDILSMRR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119569521 184 IFSIIRDLGALAQVHAENGDIVEEEQKRLLELgitGPEGHVLSHPEEVEAEAVYRAVTIAKQANCPLYVTKVMSKGAADA 263
Cdd:TIGR00857 152 ALEYAAIAGVPIALHAEDPDLIYGGVMHEGPS---AAQLGLPARPPEAEEVAVARLLELAKHAGCPVHICHISTKESLEL 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119569521 264 IAQAKRRGVvvfgePITAS------LGTDGSHYWSKNWAKaaafvTSPPVNPdPTTADHLTCLLSSGDLQVTGSAHCTFT 337
Cdd:TIGR00857 229 IVKAKSQGI-----KITAEvtphhlLLSEEDVARLDGNGK-----VNPPLRE-KEDRLALIEGLKDGIIDIIATDHAPHT 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119569521 338 TAQKAVgkdNFALIPEGTNGIEERMSMVWEKCVAsGKMDENEFVAVTSTNAAKIFNFyPRKGRVAVGSDADLVIWNPKAT 417
Cdd:TIGR00857 298 LEEKTK---EFAAAPPGIPGLETALPLLLQLLVK-GLISLKDLIRMLSINPARIFGL-PDKGTLEEGNPADITVFDLKKE 372
|
....*..
gi 119569521 418 KIISAKT 424
Cdd:TIGR00857 373 WTINAET 379
|
|
| PRK02382 |
PRK02382 |
dihydroorotase; Provisional |
17-422 |
1.12e-37 |
|
dihydroorotase; Provisional
Pssm-ID: 179417 [Multi-domain] Cd Length: 443 Bit Score: 143.64 E-value: 1.12e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119569521 17 LLIRGGRIVNDDQSFYADVHVEDGLIKQIGENLIVPGGIKTIDAHGLMVLPGGVDVHTRLQMPvlGMTPADDFCQGTKAA 96
Cdd:PRK02382 4 ALLKDGRVYYNNSLQPRDVRIDGGKITAVGKDLDGSSSEEVIDARGMLLLPGGIDVHVHFREP--GYTHKETWYTGSRSA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119569521 97 LAGGTTMILDHVFPDTGVSLLAAYEQWRERADSAACCDYSLHVDITRWHESIKEELealvkEKGVNSF-LVFMAYKDRCQ 175
Cdd:PRK02382 82 AAGGVTTVVDQPNTDPPTVDGESFDEKAELAARKSIVDFGINGGVTGNWDPLESLW-----ERGVFALgEIFMADSTGGM 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119569521 176 CSDSQMY-EIFSIIRDLGALAQVHAENGDIVeEEQKRLLElGITGPEGHVLSHPEEVEAEAVYRAVTIAKQANCPLYVTK 254
Cdd:PRK02382 157 GIDEELFeEALAEAARLGVLATVHAEDEDLF-DELAKLLK-GDADADAWSAYRPAAAEAAAVERALEVASETGARIHIAH 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119569521 255 VMSkgaADAIAQAKRRGVVVFGEPITASLGTDgshywskNWAKAAAFV-TSPPVNPDPTTaDHLTCLLSSGDLQVTGSAH 333
Cdd:PRK02382 235 IST---PEGVDAARREGITCEVTPHHLFLSRR-------DWERLGTFGkMNPPLRSEKRR-EALWERLNDGTIDVVASDH 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119569521 334 CTFTTAQKAVG-KDnfalIPEGTNGIEERMSMVWEKcVASGKMDENEFVAVTSTNAAKIFNFyPRKGRVAVGSDADLVIW 412
Cdd:PRK02382 304 APHTREEKDADiWD----APSGVPGVETMLPLLLAA-VRKNRLPLERVRDVTAANPARIFGL-DGKGRIAEGYDADLVLV 377
|
410
....*....|
gi 119569521 413 NPKATKIISA 422
Cdd:PRK02382 378 DPDAAREIRG 387
|
|
| pyrC |
PRK09357 |
dihydroorotase; Validated |
16-424 |
2.87e-31 |
|
dihydroorotase; Validated
Pssm-ID: 236479 [Multi-domain] Cd Length: 423 Bit Score: 125.31 E-value: 2.87e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119569521 16 RLLIRGGRIVNDDQSFY-ADVHVEDGLIKQIGENLIVPGGiKTIDAHGLMVLPGGVDVHTRLQMPvlGMTPADDFCQGTK 94
Cdd:PRK09357 2 MILIKNGRVIDPKGLDEvADVLIDDGKIAAIGENIEAEGA-EVIDATGLVVAPGLVDLHVHLREP--GQEDKETIETGSR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119569521 95 AALAGGTTMIldHVFPDTG--VSLLAAYEQWRERADSAACCDysLHV--DITRWHESiKE--ELEALVKEKgvnsflVFM 168
Cdd:PRK09357 79 AAAAGGFTTV--VAMPNTKpvIDTPEVVEYVLDRAKEAGLVD--VLPvgAITKGLAG-EEltEFGALKEAG------VVA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119569521 169 AYKDRCQCSDSQ-MYEIFSIIRDLGALAQVHAENGDIVEE----EQKRLLELGITGpeghvlsHPEEVEAEAVYRAVTIA 243
Cdd:PRK09357 148 FSDDGIPVQDARlMRRALEYAKALDLLIAQHCEDPSLTEGgvmnEGEVSARLGLPG-------IPAVAEEVMIARDVLLA 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119569521 244 KQANCPLYVTKVMSKGAADAIAQAKRRGVvvfgePITA------------SLGTDGSHYwsKnwakaaafvtsppVNPdP 311
Cdd:PRK09357 221 EATGARVHICHVSTAGSVELIRWAKALGI-----KVTAevtphhllltdeDLLTYDPNY--K-------------VNP-P 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119569521 312 --TTADHLTCL--LSSGDLQVTGSAHCTFTTAQKAVGkdnFALIPEGTNGIEERMSMVWEKCVASGKMDENEFVAVTSTN 387
Cdd:PRK09357 280 lrTEEDREALIegLKDGTIDAIATDHAPHAREEKECE---FEAAPFGITGLETALSLLYTTLVKTGLLDLEQLLEKMTIN 356
|
410 420 430
....*....|....*....|....*....|....*..
gi 119569521 388 AAKIFNFYPrkGRVAVGSDADLVIWNPKATKIISAKT 424
Cdd:PRK09357 357 PARILGLPA--GPLAEGEPADLVIFDPEAEWTVDGED 391
|
|
| PRK08044 |
PRK08044 |
allantoinase AllB; |
17-422 |
5.28e-31 |
|
allantoinase AllB;
Pssm-ID: 169193 [Multi-domain] Cd Length: 449 Bit Score: 124.97 E-value: 5.28e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119569521 17 LLIRGGRIVNDDQSFYADVHVEDGLIKQIGENLivPGGIKTIDAHGLMVLPGGVDVHTRLQMPvlGMTPADDFCQGTKAA 96
Cdd:PRK08044 5 LIIKNGTVILENEARVVDIAVKGGKIAAIGQDL--GDAKEVMDASGLVVSPGMVDAHTHISEP--GRSHWEGYETGTRAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119569521 97 LAGG-TTMIldhVFPDTGVSLLAAYEQWRERADSAaccDYSLHVDITRWHESIKEELEAL--VKEKGVNSFLVFMAY--- 170
Cdd:PRK08044 81 AKGGiTTMI---EMPLNQLPATVDRASIELKFDAA---KGKLTIDAAQLGGLVSYNLDRLheLDEVGVVGFKCFVATcgd 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119569521 171 ----KDRCQCSDSQMYEIFSIIRDLGALAQVHAENGDIVEEEQKRLLELGITGPEGHVLSHPEEVEAEAVYRAVTIAKQA 246
Cdd:PRK08044 155 rgidNDFRDVNDWQFYKGAQKLGELGQPVLVHCENALICDELGEEAKREGRVTAHDYVASRPVFTEVEAIRRVLYLAKVA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119569521 247 NCPLYVTKVMSKGAADAIAQAKRRGVVVFGEPITaslgtdgsHYWSKNWAKAAAFVT----SPPVNpDPTTADHLTCLLS 322
Cdd:PRK08044 235 GCRLHVCHISSPEGVEEVTRARQEGQDVTCESCP--------HYFVLDTDQFEEIGTlakcSPPIR-DLENQKGMWEKLF 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119569521 323 SGDLQVTGSAHCTFTTAQKAvgkDNFALIPEGTNGIEERMSMVWEKCVASGKMDENEFVAVTSTNAAKIFNFyPRKGRVA 402
Cdd:PRK08044 306 NGEIDCLVSDHSPCPPEMKA---GNIMEAWGGIAGLQNCMDVMFDEAVQKRGMSLPMFGKLMATNAADIFGL-QQKGRIA 381
|
410 420
....*....|....*....|
gi 119569521 403 VGSDADLVIWNPKATKIISA 422
Cdd:PRK08044 382 PGKDADFVFIQPNSSYVLKN 401
|
|
| DHOase_IIa |
cd01317 |
Dihydroorotase (DHOase), subgroup IIa; DHOases catalyze the reversible interconversion of ... |
54-424 |
1.55e-30 |
|
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: 122.35 E-value: 1.55e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119569521 54 GIKTIDAHGLMVLPGGVDVHTRLQMPvlGMTPADDFCQGTKAALAGGTTMILdhVFPDTGVSL--LAAYEQWRERADSAA 131
Cdd:cd01317 1 DAEVIDAEGKILAPGLVDLHVHLREP--GFEYKETLESGAKAAAAGGFTTVV--CMPNTNPVIdnPAVVELLKNRAKDVG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119569521 132 CCDYSLHVDITRwhESIKEELE--ALVKEKGVNSFlvfmAYKDRCQCSDSQMYEIFSIIRDLGALAQVHAENGDIVEE-- 207
Cdd:cd01317 77 IVRVLPIGALTK--GLKGEELTeiGELLEAGAVGF----SDDGKPIQDAELLRRALEYAAMLDLPIIVHPEDPSLAGGgv 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119569521 208 --EQKRLLELGITGpeghvlsHPEEVEAEAVYRAVTIAKQANCPLYVTKVMSKGAADAIAQAKRRGVvvfgePITASLGt 285
Cdd:cd01317 151 mnEGKVASRLGLPG-------IPPEAETIMVARDLELAEATGARVHFQHLSTARSLELIRKAKAKGL-----PVTAEVT- 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119569521 286 dgSHYWSKNWAKAAAFVTSPPVNP---DPTTADHLTCLLSSGDLQVTGSAHCTFTTAQKAVGkdnFALIPEGTNGIEERM 362
Cdd:cd01317 218 --PHHLLLDDEALESYDTNAKVNPplrSEEDREALIEALKDGTIDAIASDHAPHTDEEKDLP---FAEAPPGIIGLETAL 292
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 119569521 363 SMVWEKCVASGKMDENEFVAVTSTNAAKIFNFYPrkGRVAVGSDADLVIWNPKATKIISAKT 424
Cdd:cd01317 293 PLLWTLLVKGGLLTLPDLIRALSTNPAKILGLPP--GRLEVGAPADLVLFDPDAEWIVDEET 352
|
|
| DHOase_IIb |
cd01318 |
Dihydroorotase (DHOase), subgroup IIb; DHOases catalyze the reversible interconversion of ... |
62-422 |
1.01e-29 |
|
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: 119.75 E-value: 1.01e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119569521 62 GLMVLPGGVDVHTRLQMPvlGMTPADDFCQGTKAALAGGTTMILDhvFPDTG--VSLLAAYEQWRERADSAACCDYSLHV 139
Cdd:cd01318 1 GLLILPGVIDIHVHFREP--GLTYKEDFVSGSRAAAAGGVTTVMD--MPNTKppTTTAEALYEKLRLAAAKSVVDYGLYF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119569521 140 DITRwhESIKEELEALvkekGVNSFLVFMAYkdrcqcSDSQMYE----IFSIIRDLGALAQVHAENGDIVEEEQKRLLEL 215
Cdd:cd01318 77 GVTG--SEDLEELDKA----PPAGYKIFMGD------STGDLLDdeetLERIFAEGSVLVTFHAEDEDRLRENRKELKGE 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119569521 216 GItgpegHVLSHPEEVEAEAVYRAVTIAKQANCPLYVTKVMSKGAADAIAQAKRRGVV-------VFGEPITASLGTdgs 288
Cdd:cd01318 145 SA-----HPRIRDAEAAAVATARALKLARRHGARLHICHVSTPEELKLIKKAKPGVTVevtphhlFLDVEDYDRLGT--- 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119569521 289 hywsknWAKaaafvtsppVNP---DPTTADHLTCLLSSGDLQVTGSAHCTFTTAQKAVGKDNfalIPEGTNGIEERMS-M 364
Cdd:cd01318 217 ------LGK---------VNPplrSREDRKALLQALADGRIDVIASDHAPHTLEEKRKGYPA---APSGIPGVETALPlM 278
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 119569521 365 VWekCVASGKMDENEFVAVTSTNAAKIFNFyPRKGRVAVGSDADLVIWNPKATKIISA 422
Cdd:cd01318 279 LT--LVNKGILSLSRVVRLTSHNPARIFGI-KNKGRIAEGYDADLTVVDLKEERTIRA 333
|
|
| PRK09060 |
PRK09060 |
dihydroorotase; Validated |
17-459 |
1.23e-23 |
|
dihydroorotase; Validated
Pssm-ID: 181632 [Multi-domain] Cd Length: 444 Bit Score: 103.46 E-value: 1.23e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119569521 17 LLIRGGRIVNDDQSFYADVHVEDGLIKQIGENLIVPGGiKTIDAHGLMVLPGGVDVHTRLQMPvlGMTPADDFCQGTKAA 96
Cdd:PRK09060 7 LILKGGTVVNPDGEGRADIGIRDGRIAAIGDLSGASAG-EVIDCRGLHVLPGVIDSQVHFREP--GLEHKEDLETGSRAA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119569521 97 LAGGTTMILDhvFPDTGVSLL--AAYEQWRERADSAACCDYSLHVDITrwHESIkEELEALVKEKGVNSFLVFM--AYKD 172
Cdd:PRK09060 84 VLGGVTAVFE--MPNTNPLTTtaEALADKLARARHRMHCDFAFYVGGT--RDNA-DELAELERLPGCAGIKVFMgsSTGD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119569521 173 RCQCSDSQMYEIFSIIRDLGAlaqVHAEngdivEEEqkRLLELGITGPEGHVLSHP----EEVEAEAVYRAVTIAKQANC 248
Cdd:PRK09060 159 LLVEDDEGLRRILRNGRRRAA---FHSE-----DEY--RLRERKGLRVEGDPSSHPvwrdEEAALLATRRLVRLARETGR 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119569521 249 PLYVTKVMSKGAADAIAQAKRRGVV--------VFGEPITASLGTdgshYWSKNwakaaafvtsPPVNpDPTTADHLTCL 320
Cdd:PRK09060 229 RIHVLHVSTAEEIDFLADHKDVATVevtphhltLAAPECYERLGT----LAQMN----------PPIR-DARHRDGLWRG 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119569521 321 LSSGDLQVTGSAHCTFTTAQKAvgkDNFALIPEGTNGIEERMSMVWEKcVASGKMDENEFVAVTSTNAAKIFNFyPRKGR 400
Cdd:PRK09060 294 VRQGVVDVLGSDHAPHTLEEKA---KPYPASPSGMTGVQTLVPIMLDH-VNAGRLSLERFVDLTSAGPARIFGI-AGKGR 368
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 119569521 401 VAVGSDADLVIWNPKATKIIsakTHNLLAEIHG-VPrglYDG------PV------HEVMVPAK---PGSGAPAR 459
Cdd:PRK09060 369 IAVGYDADFTIVDLKRRETI---TNEWIASRCGwTP---YDGkevtgwPVgtivrgQRVMWDGElvgPPTGEPVR 437
|
|
| Amidohydro_1 |
pfam01979 |
Amidohydrolase family; This family of enzymes are a a large metal dependent hydrolase ... |
64-420 |
1.52e-23 |
|
Amidohydrolase family; This family of enzymes are a a large metal dependent hydrolase superfamily. The family includes Adenine deaminase EC:3.5.4.2 that hydrolyses adenine to form hypoxanthine and ammonia. Adenine deaminases reaction is important for adenine utilization as a purine and also as a nitrogen source. This family also includes dihydroorotase and N-acetylglucosamine-6-phosphate deacetylases, EC:3.5.1.25 These enzymes catalyze the reaction N-acetyl-D-glucosamine 6-phosphate + H2O <=> D-glucosamine 6-phosphate + acetate. This family includes the catalytic domain of urease alpha subunit. Dihydroorotases (EC:3.5.2.3) are also included.
Pssm-ID: 460401 [Multi-domain] Cd Length: 334 Bit Score: 101.42 E-value: 1.52e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119569521 64 MVLPGGVDVHTRLQMPVLGMTPADDFC------QGTKAALAGGTTMILDHVFPD-TGVSLL--AAYEQWRE-RADSAACC 133
Cdd:pfam01979 1 IVLPGLIDAHVHLEMGLLRGIPVPPEFayealrLGITTMLKSGTTTVLDMGATTsTGIEALleAAEELPLGlRFLGPGCS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119569521 134 ---DYSLHVDITRWHEsIKEELEALVKEKGVNSFLVFMAYKDRcQCSDSQMYEIFSIIRDLGALAQVHAENGDiveEEQK 210
Cdd:pfam01979 81 ldtDGELEGRKALREK-LKAGAEFIKGMADGVVFVGLAPHGAP-TFSDDELKAALEEAKKYGLPVAIHALETK---GEVE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119569521 211 RLLELGITGPEghVLSHPEEVEAEAVYRAVTIAKQANCPLYVTkvmskGAADAIAQAKRRGVVvfgepitasLGTDGSHY 290
Cdd:pfam01979 156 DAIAAFGGGIE--HGTHLEVAESGGLLDIIKLILAHGVHLSPT-----EANLLAEHLKGAGVA---------HCPFSNSK 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119569521 291 WSKNWAKAAAfvtsppvnpdpttadhltcLLSSGDLQVTGSAHCtfttaqkaVGKDNFALIPEGTNGIEERMsmvwekcV 370
Cdd:pfam01979 220 LRSGRIALRK-------------------ALEDGVKVGLGTDGA--------GSGNSLNMLEELRLALELQF-------D 265
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 119569521 371 ASGKMDENEFVAVTSTNAAKIFNFYPRKGRVAVGSDADLVIWNPKATKII 420
Cdd:pfam01979 266 PEGGLSPLEALRMATINPAKALGLDDKVGSIEVGKDADLVVVDLDPLAAF 315
|
|
| PRK07575 |
PRK07575 |
dihydroorotase; Provisional |
14-411 |
1.48e-22 |
|
dihydroorotase; Provisional
Pssm-ID: 236055 [Multi-domain] Cd Length: 438 Bit Score: 100.13 E-value: 1.48e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119569521 14 SDRLLIRGGRIVNDDQSFY-ADVHVEDGLIKQIGENLIVPGGIKTIDAHGLMVLPGGVD--VHTRlqMPvlGMTPADDFC 90
Cdd:PRK07575 2 MMSLLIRNARILLPSGELLlGDVLVEDGKIVAIAPEISATAVDTVIDAEGLTLLPGVIDpqVHFR--EP--GLEHKEDLF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119569521 91 QGTKAALAGGTTMILDhvFPDTG--VSLLAAYEQWRERADSAACCDYSLHVDITrwhesiKEELEALVKEKGVNSFLVFM 168
Cdd:PRK07575 78 TASRACAKGGVTSFLE--MPNTKplTTTQAALDDKLARAAEKCVVNYGFFIGAT------PDNLPELLTANPTCGIKIFM 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119569521 169 --AYKDRCQCSDSQMYEIFSIIRDLGAlaqVHAENGDIVEEEQKRLleLGITGPEGHVLSHPEEVEAEAVYRAVTIAKQA 246
Cdd:PRK07575 150 gsSHGPLLVDEEAALERIFAEGTRLIA---VHAEDQARIRARRAEF--AGISDPADHSQIQDEEAALLATRLALKLSKKY 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119569521 247 NCPLYVTKVMSKGAADAIAQAKRRGVVVFGEPitaslgtdgsHYWSKNWAKAAAFVTSPPVNPDPTTADHLTCL---LSS 323
Cdd:PRK07575 225 QRRLHILHLSTAIEAELLRQDKPSWVTAEVTP----------QHLLLNTDAYERIGTLAQMNPPLRSPEDNEALwqaLRD 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119569521 324 GDLQVTGSAHCTFTTAQKAVGkdnFALIPEGTNGIEERMSMVWEKCVAsGKMDENEFVAVTSTNAAKIFNFyPRKGRVAV 403
Cdd:PRK07575 295 GVIDFIATDHAPHTLEEKAQP---YPNSPSGMPGVETSLPLMLTAAMR-GKCTVAQVVRWMSTAVARAYGI-PNKGRIAP 369
|
....*...
gi 119569521 404 GSDADLVI 411
Cdd:PRK07575 370 GYDADLVL 377
|
|
| PLN02795 |
PLN02795 |
allantoinase |
12-417 |
3.22e-21 |
|
allantoinase
Pssm-ID: 178392 [Multi-domain] Cd Length: 505 Bit Score: 96.77 E-value: 3.22e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119569521 12 ITSDRLLIRGGRIVNDdqsfyadVHVEDGLIKQIGENLIVPG---GIKTIDAHGLMVLPGGVDVHTRLQMPvlGMTPADD 88
Cdd:PLN02795 48 LYSKRVVTPAGVIPGA-------VEVEGGRIVSVTKEEEAPKsqkKPHVLDYGNAVVMPGLIDVHVHLNEP--GRTEWEG 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119569521 89 FCQGTKAALAGGTTMILD---HVFPDTgvsllAAYEQWRERADSAAccdYSLHVDITRWHESIKE------ELEALVkEK 159
Cdd:PLN02795 119 FPTGTKAAAAGGITTLVDmplNSFPST-----TSVETLELKIEAAK---GKLYVDVGFWGGLVPEnahnasVLEELL-DA 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119569521 160 GVNSFLVFM---AYKDRCQCSDSQMYEIFSIIRDLGALAQVHAENGDIVEEEQKrlLELGITGPEGHVLSHPEEVEAEAV 236
Cdd:PLN02795 190 GALGLKSFMcpsGINDFPMTTATHIKAALPVLAKYGRPLLVHAEVVSPVESDSR--LDADPRSYSTYLKSRPPSWEQEAI 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119569521 237 YRAVTIAKQAN-------CPLYVTKVM-SKGAADAIAQAKRRGVVVFGEPITaslgtdgsHYWsknwAKAAA-------- 300
Cdd:PLN02795 268 RQLLEVAKDTRpggvaegAHVHIVHLSdAESSLELIKEAKAKGDSVTVETCP--------HYL----AFSAEeipdgdtr 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119569521 301 FVTSPPVNpDPTTADHLTCLLSSGDLQVTGSAHCTFTTAQKAVGKDNFALIPEGTNGIEERMSMVWEKCVASGkMDENEF 380
Cdd:PLN02795 336 YKCAPPIR-DAANRELLWKALLDGDIDMLSSDHSPSPPDLKLLEEGNFLRAWGGISSLQFVLPATWTAGRAYG-LTLEQL 413
|
410 420 430
....*....|....*....|....*....|....*..
gi 119569521 381 VAVTSTNAAKIFNFyPRKGRVAVGSDADLVIWNPKAT 417
Cdd:PLN02795 414 ARWWSERPAKLAGL-DSKGAIAPGKDADIVVWDPEAE 449
|
|
| PRK04250 |
PRK04250 |
dihydroorotase; Provisional |
22-423 |
3.89e-18 |
|
dihydroorotase; Provisional
Pssm-ID: 235265 [Multi-domain] Cd Length: 398 Bit Score: 86.36 E-value: 3.89e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119569521 22 GRIVNDDQSFYADVHVEDGLIKQIGENLIvpGGIKTIDAHGLMVLPGGVDVHTRLQmpvlgmtpadDFCQ--------GT 93
Cdd:PRK04250 4 GKFLLKGRIVEGGIGIENGRISKISLRDL--KGKEVIKVKGGIILPGLIDVHVHLR----------DFEEsyketiesGT 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119569521 94 KAALAGGTTMILDHvfPDTGVSLLAA--YEQWRERADSAACCDYSLHVDITRWHESIKEELEALVKEkgvnsflvFMAyk 171
Cdd:PRK04250 72 KAALHGGITLVFDM--PNTKPPIMDEktYEKRMRIAEKKSYADYALNFLIAGNCEKAEEIKADFYKI--------FMG-- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119569521 172 drcqcsdSQMYEIFS------IIRDLGALAqVHAENGDIVEEEQKRllelgitgpeghvlshPEEVEAEAVYRAVTIAKQ 245
Cdd:PRK04250 140 -------ASTGGIFSenfevdYACAPGIVS-VHAEDPELIREFPER----------------PPEAEVVAIERALEAGKK 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119569521 246 ANCPLYVTKVMSKGAADAIAQAKRRGVVVFGEPitaslgtdgSH--YWSKNWAKAAAFVTSPPVNpdptTADHLTCLLSS 323
Cdd:PRK04250 196 LKKPLHICHISTKDGLKLILKSNLPWVSFEVTP---------HHlfLTRKDYERNPLLKVYPPLR----SEEDRKALWEN 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119569521 324 GD-LQVTGSAHCTFTTAQKAVGKdnfALIPegtnGIEERMSMVWEkCVASGKMDENEFVAVTSTNAAKIFNFyPRKGrVA 402
Cdd:PRK04250 263 FSkIPIIASDHAPHTLEDKEAGA---AGIP----GLETEVPLLLD-AANKGMISLFDIVEKMHDNPARIFGI-KNYG-IE 332
|
410 420
....*....|....*....|.
gi 119569521 403 VGSDADLVIWNPKATKIISAK 423
Cdd:PRK04250 333 EGNYANFAVFDMKKEWTIKAE 353
|
|
| PRK01211 |
PRK01211 |
dihydroorotase; Provisional |
32-423 |
5.52e-18 |
|
dihydroorotase; Provisional
Pssm-ID: 179247 [Multi-domain] Cd Length: 409 Bit Score: 86.06 E-value: 5.52e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119569521 32 YADVHVEDGLIKQIGENLivpGGIKTIDAHGLmVLPGGVDVHTRLQMPvlGMTPADDFCQGTKAALAGGTTMILDhvFPD 111
Cdd:PRK01211 15 YLEIEVEDGKIKSIKKDA---GNIGKKELKGA-ILPAATDIHVHFRTP--GETEKEDFSTGTLSAIFGGTTFIMD--MPN 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119569521 112 TGVSL--LAAYEQWRERADSAACCDYSLHvditrwheSIKEELEALVKEKGVNSFLVFMAYKDRCQCSDSQMYEIfSIIR 189
Cdd:PRK01211 87 NNIPIkdYNAFSDKLGRVAPKAYVDFSLY--------SMETGNNALILDERSIGLKVYMGGTTNTNGTDIEGGEI-KKIN 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119569521 190 DLGALAQVHAENGDIVEE---EQKRLLElgitgpegHVLSHPEEVEAEAVYRAVTIAKQANCPLYVTKVMSKGaaDAIAQ 266
Cdd:PRK01211 158 EANIPVFFHAELSECLRKhqfESKNLRD--------HDLARPIECEIKAVKYVKNLDLKTKIIAHVSSIDVIG--RFLRE 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119569521 267 AKRRGVVVFGEpitASLGTDGShywsknwakaaafvTSPPVNpDPTTADHLTCLLSSGDLQVTGSAHCTFTTAQKAvgkd 346
Cdd:PRK01211 228 VTPHHLLLNDD---MPLGSYGK--------------VNPPLR-DRWTQERLLEEYISGRFDILSSDHAPHTEEDKQ---- 285
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 119569521 347 NFALIPEGTNGIEERMSMVWeKCVASGKMDENEFVAVTSTNAAKIFNFypRKGRVAVGSDADLVIWNPKATKIISAK 423
Cdd:PRK01211 286 EFEYAKSGIIGVETRVPLFL-ALVKKKILPLDVLYKTAIERPASLFGI--KKGKIEEGYDADFMAFDFTNIKKINDK 359
|
|
| PRK09236 |
PRK09236 |
dihydroorotase; Reviewed |
15-252 |
7.51e-17 |
|
dihydroorotase; Reviewed
Pssm-ID: 181716 Cd Length: 444 Bit Score: 82.61 E-value: 7.51e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119569521 15 DRLLIRGGRIVNDDQSFYADVHVEDGLIKQIGENLIVPGGIKTIDAHGLMVLPGGVD--VHTRlqMPvlGMTPADDFCQG 92
Cdd:PRK09236 2 KRILIKNARIVNEGKIFEGDVLIENGRIAKIASSISAKSADTVIDAAGRYLLPGMIDdqVHFR--EP--GLTHKGDIASE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119569521 93 TKAALAGGTTMILD--HVFPDTgvSLLAAYEQWRERADSAACCDYSLHVDITrwHESIkEELEALVKEK--GVNsflVFM 168
Cdd:PRK09236 78 SRAAVAGGITSFMEmpNTNPPT--TTLEALEAKYQIAAQRSLANYSFYFGAT--NDNL-DEIKRLDPKRvcGVK---VFM 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119569521 169 AykdrcqCSDSQMY--------EIFsiiRDLGALAQVHAENGDIVEEEQKRLLEL-GITGPEGHvlsHPEEVEAEAVYR- 238
Cdd:PRK09236 150 G------ASTGNMLvdnpetleRIF---RDAPTLIATHCEDTPTIKANLAKYKEKyGDDIPAEM---HPLIRSAEACYKs 217
|
250
....*....|....*..
gi 119569521 239 ---AVTIAKQANCPLYV 252
Cdd:PRK09236 218 sslAVSLAKKHGTRLHV 234
|
|
| SsnA |
COG0402 |
Cytosine/adenosine deaminase or related metal-dependent hydrolase [Nucleotide transport and ... |
16-288 |
7.95e-14 |
|
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: 73.32 E-value: 7.95e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119569521 16 RLLIRGGRIV--NDDQSFYAD--VHVEDGLIKQIGENLIVP---GGIKTIDAHGLMVLPGGVDVHTRL-QMPVLGMTPAD 87
Cdd:COG0402 1 DLLIRGAWVLtmDPAGGVLEDgaVLVEDGRIAAVGPGAELParyPAAEVIDAGGKLVLPGLVNTHTHLpQTLLRGLADDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119569521 88 DFCQ--------------------GTKAA----LAGGTTMILDH--VFPDTGVSLLAAYEQWRERADSA-ACCDYSLHVD 140
Cdd:COG0402 81 PLLDwleeyiwplearldpedvyaGALLAlaemLRSGTTTVADFyyVHPESADALAEAAAEAGIRAVLGrGLMDRGFPDG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119569521 141 ITRWHESIKEELEALVKEkgvnsflVFMAYKDRCQ----------CSDSQMYEIFSIIRDLGALAQVH-----AENGDIV 205
Cdd:COG0402 161 LREDADEGLADSERLIER-------WHGAADGRIRvalaphapytVSPELLRAAAALARELGLPLHTHlaetrDEVEWVL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119569521 206 EEEQKR----LLELGITGPeGHVLSH-----PEEVE--AEavyRAVTIakqANCP---LYvtkvMSKGAADaIAQAKRRG 271
Cdd:COG0402 234 ELYGKRpveyLDELGLLGP-RTLLAHcvhltDEEIAllAE---TGASV---AHCPtsnLK----LGSGIAP-VPRLLAAG 301
|
330
....*....|....*..
gi 119569521 272 VVVfgepitaSLGTDGS 288
Cdd:COG0402 302 VRV-------GLGTDGA 311
|
|
| HutI |
COG1228 |
Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport ... |
13-413 |
5.18e-12 |
|
Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440841 [Multi-domain] Cd Length: 386 Bit Score: 67.29 E-value: 5.18e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119569521 13 TSDRLLIRGGRIVNDDQSFY---ADVHVEDGLIKQIGEN--LIVPGGIKTIDAHGLMVLPGGVDVHTRLqmpVLGMTPAD 87
Cdd:COG1228 6 QAGTLLITNATLVDGTGGGVienGTVLVEDGKIAAVGPAadLAVPAGAEVIDATGKTVLPGLIDAHTHL---GLGGGRAV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119569521 88 DFCQGT----------------KAALAGGTTMILDHVFPDTGVS------LLAAYEQWR-ERADSAACCDYSLHvdiTRW 144
Cdd:COG1228 83 EFEAGGgitptvdlvnpadkrlRRALAAGVTTVRDLPGGPLGLRdaiiagESKLLPGPRvLAAGPALSLTGGAH---ARG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119569521 145 HESIKEELEALVKEkGVNsFLVFMAYKDRCQCSDSQMYEIFSIIRDLGALAQVHAENGDIVeeeqKRLLELGITGPEgHV 224
Cdd:COG1228 160 PEEARAALRELLAE-GAD-YIKVFAEGGAPDFSLEELRAILEAAHALGLPVAAHAHQADDI----RLAVEAGVDSIE-HG 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119569521 225 LSHPEEVeaeavyravtiakqancplyvtkvmskgaadaIAQAKRRGVVVFGePiTASLGTDGSHYWSKNWAKAAAFVts 304
Cdd:COG1228 233 TYLDDEV--------------------------------ADLLAEAGTVVLV-P-TLSLFLALLEGAAAPVAAKARKV-- 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119569521 305 ppvnpdpttadhltcllssGDLQVTgsahcTFTTAQKA-----VGKDNFALIPEGTNgieerMSMVWEKCVASGkMDENE 379
Cdd:COG1228 277 -------------------REAALA-----NARRLHDAgvpvaLGTDAGVGVPPGRS-----LHRELALAVEAG-LTPEE 326
|
410 420 430
....*....|....*....|....*....|....*
gi 119569521 380 -FVAVTStNAAKIFNFYPRKGRVAVGSDADLVIWN 413
Cdd:COG1228 327 aLRAATI-NAAKALGLDDDVGSLEPGKLADLVLLD 360
|
|
| PRK15446 |
PRK15446 |
phosphonate metabolism protein PhnM; Provisional |
16-243 |
1.97e-11 |
|
phosphonate metabolism protein PhnM; Provisional
Pssm-ID: 237967 [Multi-domain] Cd Length: 383 Bit Score: 65.59 E-value: 1.97e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119569521 16 RLLIRGGRIVNDDQSFYADVHVEDGLIKQIGENLIVPGGIktIDAHGLMVLPGGVDVHT----RLQMPVLG-MTPADDFC 90
Cdd:PRK15446 3 EMILSNARLVLPDEVVDGSLLIEDGRIAAIDPGASALPGA--IDAEGDYLLPGLVDLHTdnleKHLAPRPGvDWPADAAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119569521 91 QGTKAALAG-GTTMILDHVF----PDTGV-------SLLAAYEQWRERadSAACCDYSLH--VDITrwHESIKEELEALV 156
Cdd:PRK15446 81 AAHDAQLAAaGITTVFDALSvgdeEDGGLrsrdlarKLIDAIEEARAR--GLLRADHRLHlrCELT--NPDALELFEALL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119569521 157 KEKGVnSFLVFMaykDRcqcSDSQMYEifsiiRDLGALAQVHAENGDIVEEEQKRLLELGITGPEGHVLSHPEEVEAEAV 236
Cdd:PRK15446 157 AHPRV-DLVSLM---DH---TPGQRQF-----RDLEKYREYYAGKYGLSDEEFDAFVEERIALSARYAPPNRRAIAALAR 224
|
....*..
gi 119569521 237 YRAVTIA 243
Cdd:PRK15446 225 ARGIPLA 231
|
|
| PRK07369 |
PRK07369 |
dihydroorotase; Provisional |
33-424 |
3.81e-11 |
|
dihydroorotase; Provisional
Pssm-ID: 236002 [Multi-domain] Cd Length: 418 Bit Score: 65.01 E-value: 3.81e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119569521 33 ADVHVEDGLIKQIGENLI-VPGGIKTIDAHGLMVLPGGVDVHTRLQMPvlGMTPADDFCQGTKAALAGGTTM--ILDHVF 109
Cdd:PRK07369 22 ADVLIEDGKIQAIEPHIDpIPPDTQIIDASGLILGPGLVDLYSHSGEP--GFEERETLASLAAAAAAGGFTRvaILPDTF 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119569521 110 P--DTGvSLLAAYEQWRERADSaaccdyslhvdiTRWHE----SIKEELEALVK-----EKGVNSFlvfmaykdrcqcSD 178
Cdd:PRK07369 100 PplDNP-ATLARLQQQAQQIPP------------VQLHFwgalTLGGQGKQLTElaelaAAGVVGF------------TD 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119569521 179 SQMYEIFSIIRDLGALAQVH-------------AENGdiVEEEQKRLLELGITGpeghvlsHPEEVEAEAVYRAVTIAKQ 245
Cdd:PRK07369 155 GQPLENLALLRRLLEYLKPLgkpvalwpcdrslAGNG--VMREGLLALRLGLPG-------DPASAETTALAALLELVAA 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119569521 246 ANCPLYVTKVMSKGAADAIAQAKRRGVvvfgePITAS-------LGT-DGSHYwSKNWAKAaafvtsPPV-NPDPTTAdh 316
Cdd:PRK07369 226 IGTPVHLMRISTARSVELIAQAKARGL-----PITASttwmhllLDTeALASY-DPNLRLD------PPLgNPSDRQA-- 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119569521 317 LTCLLSSGDLQVTGSAHCTFTTAQKAVGkdnFALIPEGTNGIEERMSMVWEKCVASGKMDENEFVAVTSTNAAKIFNFYP 396
Cdd:PRK07369 292 LIEGVRTGVIDAIAIDHAPYTYEEKTVA---FAEAPPGAIGLELALPLLWQNLVETGELSALQLWQALSTNPARCLGQEP 368
|
410 420
....*....|....*....|....*...
gi 119569521 397 RkgRVAVGSDADLVIWNPKATKIISAKT 424
Cdd:PRK07369 369 P--SLAPGQPAELILFDPQKTWTVSAQT 394
|
|
| ATZ_TRZ_like |
cd01298 |
TRZ/ATZ family contains enzymes from the atrazine degradation pathway and related hydrolases. ... |
17-448 |
6.87e-11 |
|
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: 64.15 E-value: 6.87e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119569521 17 LLIRGGRIVNDDQS---FYADVHVEDGLIKQIGENLIVPGGI--KTIDAHGLMVLPGGVDVHTRLQM------------- 78
Cdd:cd01298 1 ILIRNGTIVTTDPRrvlEDGDVLVEDGRIVAVGPALPLPAYPadEVIDAKGKVVMPGLVNTHTHLAMtllrgladdlplm 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119569521 79 --------PVLGMTPADDFCQGTKAALA----GGTTMILDHVFPDTGVSLLAAYEQ-WReradsaACCDYSLHVDITRWH 145
Cdd:cd01298 81 ewlkdliwPLERLLTEEDVYLGALLALAemirSGTTTFADMYFFYPDAVAEAAEELgIR------AVLGRGIMDLGTEDV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119569521 146 ESIKEEL---EALVKEkgvnsflvfmaYKDRCQ--------------CSDSQMYEIFSIIRDLGALAQVH-AENGDIVEE 207
Cdd:cd01298 155 EETEEALaeaERLIRE-----------WHGAADgrirvalaphapytCSDELLREVAELAREYGVPLHIHlAETEDEVEE 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119569521 208 EQKR--------LLELGITGPEGhVLSH-----PEEVE--AEavyRAVTIakqANCPLYVTKVMSkGAADaIAQAKRRGV 272
Cdd:cd01298 224 SLEKygkrpveyLEELGLLGPDV-VLAHcvwltDEEIEllAE---TGTGV---AHNPASNMKLAS-GIAP-VPEMLEAGV 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119569521 273 VVfgepitaSLGTDGSHywSKNwakaaafvtsppvNPDPTTADHLTCLLssgdlqvtgsahctfttaQKAVGKDNFALIP 352
Cdd:cd01298 295 NV-------GLGTDGAA--SNN-------------NLDMFEEMRLAALL------------------QKLAHGDPTALPA 334
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119569521 353 EgtngieermsmvwekcvasgkmdenEFVAVTSTNAAKIFNFyPRKGRVAVGSDADLVIWNPkaTKIISAKTHNLLAEIh 432
Cdd:cd01298 335 E-------------------------EALEMATIGGAKALGL-DEIGSLEVGKKADLILIDL--DGPHLLPVHDPISHL- 385
|
490
....*....|....*.
gi 119569521 433 gvPRGLYDGPVHEVMV 448
Cdd:cd01298 386 --VYSANGGDVDTVIV 399
|
|
| COG3964 |
COG3964 |
Predicted amidohydrolase [General function prediction only]; |
17-106 |
2.83e-10 |
|
Predicted amidohydrolase [General function prediction only];
Pssm-ID: 443164 [Multi-domain] Cd Length: 376 Bit Score: 62.11 E-value: 2.83e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119569521 17 LLIRGGRIVNDDQSFYA--DVHVEDGLIKQIGENLIVPGGIKTIDAHGLMVLPGGVDVHTRL--QMPVLGMtPADDFCqg 92
Cdd:COG3964 2 LLIKGGRVIDPANGIDGvmDIAIKDGKIAAVAKDIDAAEAKKVIDASGLYVTPGLIDLHTHVfpGGTDYGV-DPDGVG-- 78
|
90
....*....|....
gi 119569521 93 tkaaLAGGTTMILD 106
Cdd:COG3964 79 ----VRSGVTTVVD 88
|
|
| COG3653 |
COG3653 |
N-acyl-D-aspartate/D-glutamate deacylase [Secondary metabolites biosynthesis, transport and ... |
17-74 |
4.21e-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: 4.21e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 119569521 17 LLIRGGRIVN--DDQSFYADVHVEDGLIKQIGeNLIVPGGIKTIDAHGLMVLPGGVDVHT 74
Cdd:COG3653 4 LLIRGGTVVDgtGAPPFRADVAIKGGRIVAVG-DLAAAEAARVIDATGLVVAPGFIDIHT 62
|
|
| D-aminoacylase |
cd01297 |
D-aminoacylases (N-acyl-D-Amino acid amidohydrolases) catalyze the hydrolysis of ... |
17-219 |
4.67e-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: 61.54 E-value: 4.67e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119569521 17 LLIRGGRIVndDQS----FYADVHVEDGLIKQIGENLIVPGGiKTIDAHGLMVLPGGVDVHTRLQMPVL---GMTPaddf 89
Cdd:cd01297 2 LVIRNGTVV--DGTgappFTADVGIRDGRIAAIGPILSTSAR-EVIDAAGLVVAPGFIDVHTHYDGQVFwdpDLRP---- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119569521 90 cqgtkAALAGGTTMILDH-------VFPD----------TGVSLL----------AAYEQWRERADSA--ACCDYSlHVD 140
Cdd:cd01297 75 -----SSRQGVTTVVLGNcgvspapANPDdlarlimlmeGLVALGeglpwgwatfAEYLDALEARPPAvnVAALVG-HAA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119569521 141 ITRWH------ESIKEELEALVK--EKGVNS----FLVFMAYKDRCQCSDSQMYEIFSIIRDLGALAQVHAEN-GDIVEE 207
Cdd:cd01297 149 LRRAVmgldarEATEEELAKMREllREALEAgalgISTGLAYAPRLYAGTAELVALARVAARYGGVYQTHVRYeGDSILE 228
|
250
....*....|...
gi 119569521 208 EQKRLLELG-ITG 219
Cdd:cd01297 229 ALDELLRLGrETG 241
|
|
| CAD_DHOase |
cd01316 |
The eukaryotic CAD protein is a trifunctional enzyme of carbamoylphosphate ... |
63-139 |
9.69e-09 |
|
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: 57.08 E-value: 9.69e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 119569521 63 LMVLPGGVDVHTRLqmPVLGMTPADDFCQGTKAALAGGTTMILdhVFPDTGVSLL--AAYEQWRERADSAACCDYSLHV 139
Cdd:cd01316 2 TIRLPGLIDVHVHL--REPGATHKEDFASGTKAALAGGFTMVR--AMPNTNPSIVdvASLKLVQSLAQAKARCDYAFSI 76
|
|
| PRK09237 |
PRK09237 |
amidohydrolase/deacetylase family metallohydrolase; |
17-74 |
9.71e-09 |
|
amidohydrolase/deacetylase family metallohydrolase;
Pssm-ID: 236423 [Multi-domain] Cd Length: 380 Bit Score: 57.17 E-value: 9.71e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 119569521 17 LLIRGGRIVNDDQSFYA--DVHVEDGLIKQIGENLIVPGGIKTIDAHGLMVLPGGVDVHT 74
Cdd:PRK09237 1 LLLRGGRVIDPANGIDGviDIAIEDGKIAAVAGDIDGSQAKKVIDLSGLYVSPGWIDLHV 60
|
|
| Bact_CD |
cd01293 |
Bacterial cytosine deaminase and related metal-dependent hydrolases. Cytosine deaminases (CDs) ... |
18-411 |
1.08e-08 |
|
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: 57.26 E-value: 1.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119569521 18 LIRGGRIVNDDQSFYaDVHVEDGLIKQIGENLIVPGGIKTIDAHGLMVLPGGVDVHTRL-QMPVLGMTPADDFCQGTKAA 96
Cdd:cd01293 1 LLRNARLADGGTALV-DIAIEDGRIAAIGPALAVPPDAEEVDAKGRLVLPAFVDPHIHLdKTFTGGRWPNNSGGTLLEAI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119569521 97 LAGGTTMiLDHVFPDTgvsllaayeqwRERADSAACCDYS-------LHVDItrwHESIKEE-LEAL--VKEKgvnsflv 166
Cdd:cd01293 80 IAWEERK-LLLTAEDV-----------KERAERALELAIAhgttairTHVDV---DPAAGLKaLEALleLREE------- 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119569521 167 fmaYKDRCQCsdsqmyeifsiirDLGALAQVHAENGDIVEEEQKRLLELGitgpeGHVLS---HPEEVEA--EAVYRAVT 241
Cdd:cd01293 138 ---WADLIDL-------------QIVAFPQHGLLSTPGGEELMREALKMG-----ADVVGgipPAEIDEDgeESLDTLFE 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119569521 242 IAKQANCPL-----YVTKVMSKGAADAIAQAKRRGvvvFGEPITAS----LGTDGSHYWSKNWAKAAA----FVTSPPVN 308
Cdd:cd01293 197 LAQEHGLDIdlhldETDDPGSRTLEELAEEAERRG---MQGRVTCShataLGSLPEAEVSRLADLLAEagisVVSLPPIN 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119569521 309 PDpttadhltcLLSSGDlqvTGSAHCTFTTAQK--------AVGKDNF--ALIPEGTNGIEERMSMVWEKCvasGKMDEN 378
Cdd:cd01293 274 LY---------LQGRED---TTPKRRGVTPVKElraagvnvALGSDNVrdPWYPFGSGDMLEVANLAAHIA---QLGTPE 338
|
410 420 430
....*....|....*....|....*....|....*.
gi 119569521 379 EF---VAVTSTNAAKIFNFypRKGRVAVGSDADLVI 411
Cdd:cd01293 339 DLalaLDLITGNAARALGL--EDYGIKVGCPADLVL 372
|
|
| PRK07228 |
PRK07228 |
5'-deoxyadenosine deaminase; |
16-287 |
2.76e-08 |
|
5'-deoxyadenosine deaminase;
Pssm-ID: 180895 [Multi-domain] Cd Length: 445 Bit Score: 56.16 E-value: 2.76e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119569521 16 RLLIRGGRIVNDDQS---FYADVHVEDGLIKQIGENLIVPGGIKTIDAHGLMVLPGGVDVHTRLqMPVLGMTPADDF--- 89
Cdd:PRK07228 2 TILIKNAGIVTMNAKreiVDGDVLIEDDRIAAVGDRLDLEDYDDHIDATGKVVIPGLIQGHIHL-CQTLFRGIADDLell 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119569521 90 -----------------------CQGTKAALAGGTTMILDHVFPDTGVSLLAAYEQWRERADSAACC-DYSLHVDIT--- 142
Cdd:PRK07228 81 dwlkdriwpleaahdaesmyysaLLGIGELIESGTTTIVDMESVHHTDSAFEAAGESGIRAVLGKVMmDYGDDVPEGlqe 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119569521 143 RWHESIKEELEALVKEKGVNSFLVFMAYKDRCQCSDSQmyEIFSIIRDL----GALAQVHA-ENGD---IVEEEQKR--- 211
Cdd:PRK07228 161 DTEASLAESVRLLEKWHGADNGRIRYAFTPRFAVSCTE--ELLRGVRDLadeyGVRIHTHAsENRGeieTVEEETGMrni 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119569521 212 --LLELGITGpEGHVLSH---PEEVEAEAVyrAVTIAKQANCPLYVTKVMSkGAADaIAQAKRRGVVVfgepitaSLGTD 286
Cdd:PRK07228 239 hyLDEVGLTG-EDLILAHcvwLDEEEREIL--AETGTHVTHCPSSNLKLAS-GIAP-VPDLLERGINV-------ALGAD 306
|
.
gi 119569521 287 G 287
Cdd:PRK07228 307 G 307
|
|
| NagA |
cd00854 |
N-acetylglucosamine-6-phosphate deacetylase, NagA, catalyzes the hydrolysis of the N-acetyl ... |
17-415 |
3.87e-08 |
|
N-acetylglucosamine-6-phosphate deacetylase, NagA, catalyzes the hydrolysis of the N-acetyl group of N-acetyl-glucosamine-6-phosphate (GlcNAc-6-P) to glucosamine 6-phosphate and acetate. This is the first committed step in the biosynthetic pathway to amino-sugar-nucleotides, which is needed for cell wall peptidoglycan and teichoic acid biosynthesis. Deacetylation of N-acetylglucosamine is also important in lipopolysaccharide synthesis and cell wall recycling.
Pssm-ID: 238434 [Multi-domain] Cd Length: 374 Bit Score: 55.28 E-value: 3.87e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119569521 17 LLIRGGRIVNDDQSFYADVHVEDGLIKQIGENLIVPGGIKTIDAHGLMVLPGGVDVHTRlqmpvlgmtpaddfcqgtkaa 96
Cdd:cd00854 1 LIIKNARILTPGGLEDGAVLVEDGKIVAIGPEDELEEADEIIDLKGQYLVPGFIDIHIH--------------------- 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119569521 97 laGGttmiLDHVFPDTGvsllaayeqwreradsaaccdyslhvditrwHESIKEELEALVKEkGVNSFLV-FMAykdrcq 175
Cdd:cd00854 60 --GG----GGADFMDGT-------------------------------AEALKTIAEALAKH-GTTSFLPtTVT------ 95
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119569521 176 CSDSQMYEIFSIIRDL-----GA-LAQVHAEnGDIVEEEQKrllelgitG--PEGHVLS-HPEEVE-----AEAVYRAVT 241
Cdd:cd00854 96 APPEEIAKALAAIAEAiaegqGAeILGIHLE-GPFISPEKK--------GahPPEYLRApDPEELKkwleaAGGLIKLVT 166
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119569521 242 IAKQancplyvtkvmSKGAADAIAQAKRRGVVVfgepitaSLG-TDGSHYWSKNWAKAAA-FVT------SPPVNPDP-- 311
Cdd:cd00854 167 LAPE-----------LDGALELIRYLVERGIIV-------SIGhSDATYEQAVAAFEAGAtHVThlfnamSPLHHREPgv 228
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119569521 312 ----TTADHLTCLLSSGDLQVTGSAhctFTTAQKAVGKDNFALI---------PEGTNGIEERMSMVWEKCV--ASG--- 373
Cdd:cd00854 229 vgaaLSDDDVYAELIADGIHVHPAA---VRLAYRAKGADKIVLVtdamaaaglPDGEYELGGQTVTVKDGVArlADGtla 305
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 119569521 374 ----KMDE-------------NEFVAVTSTNAAKIFNFYPRKGRVAVGSDADLVIWNPK 415
Cdd:cd00854 306 gstlTMDQavrnmvkwggcplEEAVRMASLNPAKLLGLDDRKGSLKPGKDADLVVLDDD 364
|
|
| PRK09061 |
PRK09061 |
D-glutamate deacylase; Validated |
16-104 |
5.50e-08 |
|
D-glutamate deacylase; Validated
Pssm-ID: 236369 [Multi-domain] Cd Length: 509 Bit Score: 55.09 E-value: 5.50e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119569521 16 RLLIRGGRIVNDDQSFYA--DVHVEDGLIKQIGENLIvpGGIKTIDAHGLMVLPGGVDVHTRlqmpvlGMTPADDFCQgt 93
Cdd:PRK09061 20 DLVIRNGRVVDPETGLDAvrDVGIKGGKIAAVGTAAI--EGDRTIDATGLVVAPGFIDLHAH------GQSVAAYRMQ-- 89
|
90
....*....|.
gi 119569521 94 kaALAGGTTMI 104
Cdd:PRK09061 90 --AFDGVTTAL 98
|
|
| PRK07627 |
PRK07627 |
dihydroorotase; Provisional |
16-112 |
7.00e-08 |
|
dihydroorotase; Provisional
Pssm-ID: 181059 [Multi-domain] Cd Length: 425 Bit Score: 54.68 E-value: 7.00e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119569521 16 RLLIRGGRIVN-----DDQsfyADVHVEDGLIKQIGEnliVPGGI---KTIDAHGLMVLPGGVDVHTRLQMPvlGMTPAD 87
Cdd:PRK07627 2 KIHIKGGRLIDpaagtDRQ---ADLYVAAGKIAAIGQ---APAGFnadKTIDASGLIVCPGLVDLSARLREP--GYEYKA 73
|
90 100
....*....|....*....|....*
gi 119569521 88 DFCQGTKAALAGGTTMILdhVFPDT 112
Cdd:PRK07627 74 TLESEMAAAVAGGVTSLV--CPPDT 96
|
|
| NagA |
COG1820 |
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism]; |
18-74 |
1.17e-07 |
|
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism];
Pssm-ID: 441425 [Multi-domain] Cd Length: 373 Bit Score: 53.95 E-value: 1.17e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 119569521 18 LIRGGRIVNDDQSFY-ADVHVEDGLIKQIGENliVPGGIKTIDAHGLMVLPGGVDVHT 74
Cdd:COG1820 1 AITNARIFTGDGVLEdGALLIEDGRIAAIGPG--AEPDAEVIDLGGGYLAPGFIDLHV 56
|
|
| Amidohydro_3 |
pfam07969 |
Amidohydrolase family; |
56-430 |
4.58e-07 |
|
Amidohydrolase family;
Pssm-ID: 400360 [Multi-domain] Cd Length: 464 Bit Score: 52.15 E-value: 4.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119569521 56 KTIDAHGLMVLPGGVDVHT---RLQMPVLGMTPADDFCQGTKAALAG------------------------GTTMILDHV 108
Cdd:pfam07969 1 EVIDAKGRLVLPGFVDPHThldGGGLNLRELRLPDVLPNAVVKGQAGrtpkgrwlvgegwdeaqfaetrfpYALADLDEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119569521 109 FPDTGVSLLA-----------AYEQWRERADSAACCDYSLHVDITRWH------ESIKEELEALVKEKGVNSFLVFMAYK 171
Cdd:pfam07969 81 APDGPVLLRAlhthaavansaALDLAGITKATEDPPGGEIARDANGEGltgllrEGAYALPPLLAREAEAAAVAAALAAL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119569521 172 DR--CQCSDSQMYEIFSIIrDLGALAQVHAENGDIveEEQKRLLELGITGPEGHV-------------------LSHP-- 228
Cdd:pfam07969 161 PGfgITSVDGGGGNVHSLD-DYEPLRELTAAEKLK--ELLDAPERLGLPHSIYELrigamklfadgvlgsrtaaLTEPyf 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119569521 229 -------EEVEAEAVYRAVTIAKQANCPLYV-----TKVMSkgAADAIAQAKRR-------------GVVVFG----EPI 279
Cdd:pfam07969 238 dapgtgwPDFEDEALAELVAAARERGLDVAIhaigdATIDT--ALDAFEAVAEKlgnqgrvriehaqGVVPYTysqiERV 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119569521 280 TASLGTDGSHYWSknWAKAAAFVTSPPVNPDPTTADHLTCLLSSGDLQVTGS-AHCTFTTAQKAVGkDNFALIPEGTN-- 356
Cdd:pfam07969 316 AALGGAAGVQPVF--DPLWGDWLQDRLGAERARGLTPVKELLNAGVKVALGSdAPVGPFDPWPRIG-AAVMRQTAGGGev 392
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 119569521 357 -GIEERMSMvwekcvasgkmdeNEFVAVTSTNAAKIFNFYPRKGRVAVGSDADLVIWNPKATKIISAKTHNLLAE 430
Cdd:pfam07969 393 lGPDEELSL-------------EEALALYTSGPAKALGLEDRKGTLGVGKDADLVVLDDDPLTVDPPAIADIRVR 454
|
|
| PRK05985 |
PRK05985 |
cytosine deaminase; Provisional |
17-128 |
1.22e-06 |
|
cytosine deaminase; Provisional
Pssm-ID: 180337 [Multi-domain] Cd Length: 391 Bit Score: 50.70 E-value: 1.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119569521 17 LLIRGGRIVNDDQsfyADVHVEDGLIKQIGENLIVPGGIKTIDAHGLMVLPGGVDVHTRLQMPVLGM------------- 83
Cdd:PRK05985 4 LLFRNVRPAGGAA---VDILIRDGRIAAIGPALAAPPGAEVEDGGGALALPGLVDGHIHLDKTFWGDpwypnepgpslre 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 119569521 84 -------------TPADDfcQGTK---AALAGGTTMILDHVFPDTGVSL------LAAYEQWRERAD 128
Cdd:PRK05985 81 rianerrrraasgHPAAE--RALAlarAAAAAGTTAMRSHVDVDPDAGLrhleavLAARETLRGLID 145
|
|
| PRK08204 |
PRK08204 |
hypothetical protein; Provisional |
15-106 |
1.67e-06 |
|
hypothetical protein; Provisional
Pssm-ID: 181288 [Multi-domain] Cd Length: 449 Bit Score: 50.39 E-value: 1.67e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119569521 15 DRLLIRGGRIVNDDQSF----YADVHVEDGLIKQIGENlIVPGGIKTIDAHGLMVLPGGVDVH---------------TR 75
Cdd:PRK08204 2 KRTLIRGGTVLTMDPAIgdlpRGDILIEGDRIAAVAPS-IEAPDAEVVDARGMIVMPGLVDTHrhtwqsvlrgigadwTL 80
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 119569521 76 LQ--MPVLG-----MTPADDFCQ---GTKAALAGGTTMILD 106
Cdd:PRK08204 81 QTyfREIHGnlgpmFRPEDVYIAnllGALEALDAGVTTLLD 121
|
|
| Met_dep_hydrolase_C |
cd01309 |
Metallo-dependent hydrolases, subgroup C is part of the superfamily of metallo-dependent ... |
39-413 |
9.17e-06 |
|
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: 47.69 E-value: 9.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119569521 39 DGLIKQIGENLIVPGGIKTIDAHGLMVLPGGVDVHTRLQM-----------------PVL-------GMTPADdfcQGTK 94
Cdd:cd01309 1 DGKIVAVGAEITTPADAEVIDAKGKHVTPGLIDAHSHLGLdeeggvretsdaneetdPVTphvraidGINPDD---EAFK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119569521 95 AALAGGTTMIldHVFPDTG------VSLLAAYeqWRERADSAACCDYSLHVditRWHESIKEELEALVKEKgvnsflvfm 168
Cdd:cd01309 78 RARAGGVTTV--QVLPGSAnliggqGVVIKTD--GGTIEDMFIKAPAGLKM---ALGENPKRVYGGKGKEP--------- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119569521 169 aykdrcqcsdSQMYEIFSIIRDLGALAQVHAENGDIVEEEQKrllelgitgpeghvLSHPEEVEAEAVYRAVTIAKQANC 248
Cdd:cd01309 142 ----------ATRMGVAALLRDAFIKAQEYGRKYDLGKNAKK--------------DPPERDLKLEALLPVLKGEIPVRI 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119569521 249 PLYVtkvmskgaADAIAQAKRRgVVVFGEPITASLGTDGsHYWSKNWAKAAAFVTSPPV-----------NPDPTTAdhl 317
Cdd:cd01309 198 HAHR--------ADDILTAIRI-AKEFGIKITIEHGAEG-YKLADELAKHGIPVIYGPTltlpkkveevnDAIDTNA--- 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119569521 318 tCLLSSGDLqvtgsahctfttaqkavgkdNFALIPEGTNGIEERMSMVWEKCVASGKMDENEFVAVTStNAAKIFNFYPR 397
Cdd:cd01309 265 -YLLKKGGV--------------------AFAISSDHPVLNIRNLNLEAAKAVKYGLSYEEALKAITI-NPAKILGIEDR 322
|
410
....*....|....*.
gi 119569521 398 KGRVAVGSDADLVIWN 413
Cdd:cd01309 323 VGSLEPGKDADLVVWN 338
|
|
| Met_dep_hydrolase_B |
cd01307 |
Metallo-dependent hydrolases, subgroup B is part of the superfamily of metallo-dependent ... |
34-411 |
2.48e-05 |
|
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: 46.55 E-value: 2.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119569521 34 DVHVEDGLIKQIGENLIVPGGIKTIDAHGLMVLPGGVDVHTRL--QMPVLGMTPadDFCqgtkaALAGGTTMILDHVFPD 111
Cdd:cd01307 1 DVAIENGKIAAVGAALAAPAATQIVDAGGCYVSPGWIDLHVHVyqGGTRYGDRP--DMI-----GVKSGVTTVVDAGSAG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119569521 112 TGvSLLAAYEQWRERAdsaaccdyslhvditrwhesiKEELEALvkekgVNSFLVFMAYKDrcqcsdsQMYEIFSIirDL 191
Cdd:cd01307 74 AD-NIDGFRYTVIERS---------------------ATRVYAF-----LNISRVGLVAQD-------ELPDPDNI--DE 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119569521 192 GALAQVHAENGDIVEEEQKRlLELGITGPEGhvlshpeeveAEAVYRAVTIAKQANCPLYVTKVMSKGAADAIAQAKRRG 271
Cdd:cd01307 118 DAVVAAAREYPDVIVGLKAR-ASKSVVGEWG----------IKPLELAKKIAKEADLPLMVHIGSPPPILDEVVPLLRRG 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119569521 272 VVVfgepitaslgtdgSHYWSknwAKAAAFVTSP-PVNPDPTTADHLTCLLSSGDlqvtGSAHCTFTTAQKAVGKDnfaL 350
Cdd:cd01307 187 DVL-------------THCFN---GKPNGIVDEEgEVLPLVRRARERGVIFDVGH----GTASFSFRVARAAIAAG---L 243
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 119569521 351 IPE----------GTNGIEERMSMVWEKCVASGkMDENEFVAVTSTNAAKIFNFyPRKGRVAVGSDADLVI 411
Cdd:cd01307 244 LPDtissdihgrnRTNGPVYALATTLSKLLALG-MPLEEVIEAVTANPARMLGL-AEIGTLAVGYDADLTV 312
|
|
| FwdA |
COG1229 |
Formylmethanofuran dehydrogenase subunit A [Energy production and conversion]; |
17-74 |
2.76e-05 |
|
Formylmethanofuran dehydrogenase subunit A [Energy production and conversion];
Pssm-ID: 440842 Cd Length: 554 Bit Score: 46.72 E-value: 2.76e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 119569521 17 LLIRGGRI------VNDDQsfyADVHVEDGlikQIGENLIVPGGIKTIDAHGLMVLPGGVDVHT 74
Cdd:COG1229 3 LIIKNGRVydpangIDGEV---MDIAIKDG---KIVEEPSDPKDAKVIDASGKVVMAGGVDIHT 60
|
|
| pyrC |
PRK00369 |
dihydroorotase; Provisional |
62-411 |
3.72e-04 |
|
dihydroorotase; Provisional
Pssm-ID: 234738 [Multi-domain] Cd Length: 392 Bit Score: 42.83 E-value: 3.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119569521 62 GLMVLPGGVDVHTRLQMpvLGMTPADDFCQGTKAALAGGTTMILDhvFPDTgVSLLAAYEQWRERADSAAC---CDYSLH 138
Cdd:PRK00369 42 GTLILPGAIDLHVHLRG--LKLSYKEDVASGTSEAAYGGVTLVAD--MPNT-IPPLNTPEAITEKLAELEYysrVDYFVY 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119569521 139 VDITRWHESIKEelealvkekgvnsfLVFMAYKdrcqcsdsqmyeifsiirdlgalaqVHAEngDIVEEEQKRLLElgit 218
Cdd:PRK00369 117 SGVTKDPEKVDK--------------LPIAGYK-------------------------IFPE--DLEREETFRVLL---- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119569521 219 gpEGHVLS--HPEEVEAEAVYRAVtiakQANCPLYVTKVMS-KGAADA-IAQAKRRGVVVFGEPITASlgTDGS-HYWSK 293
Cdd:PRK00369 152 --KSRKLKilHPEVPLALKSNRKL----RRNCWYEIAALYYvKDYQNVhITHASNPRTVRLAKELGFT--VDITpHHLLV 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119569521 294 NWAKAAAFVTSPPVNpDPTTADHLTCLLSSGDLQVtgSAHCTFTTAQKavgKDNFALIPEGTNGIEERMSMVWeKCVASG 373
Cdd:PRK00369 224 NGEKDCLTKVNPPIR-DINERLWLLQALSEVDAIA--SDHAPHSSFEK---LQPYEVCPPGIAALSFTPPFIY-TLVSKG 296
|
330 340 350
....*....|....*....|....*....|....*...
gi 119569521 374 KMDENEFVAVTSTNAAKIFNFypRKGRVAVGSDADLVI 411
Cdd:PRK00369 297 ILSIDRAVELISTNPARILGI--PYGEIKEGYRANFTV 332
|
|
| YtcJ |
COG1574 |
Predicted amidohydrolase YtcJ [General function prediction only]; |
17-74 |
5.86e-04 |
|
Predicted amidohydrolase YtcJ [General function prediction only];
Pssm-ID: 441182 [Multi-domain] Cd Length: 535 Bit Score: 42.48 E-value: 5.86e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 119569521 17 LLIRGGRI--VNDDQSFYADVHVEDGLIKQIGEN----LIVPGGIKTIDAHGLMVLPGGVDVHT 74
Cdd:COG1574 10 LLLTNGRIytMDPAQPVAEAVAVRDGRIVAVGSDaevrALAGPATEVIDLGGKTVLPGFIDAHV 73
|
|
| ureC |
PRK13308 |
urease subunit alpha; Reviewed |
33-104 |
7.29e-04 |
|
urease subunit alpha; Reviewed
Pssm-ID: 183965 [Multi-domain] Cd Length: 569 Bit Score: 42.00 E-value: 7.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119569521 33 ADVHVEDGLIKQIG------------ENLIVPGGIKTIDAHGLMVLPGGVDVHTRLQMPvlgmtpaddfcQGTKAALAGG 100
Cdd:PRK13308 87 GDIGIRDGRIVGIGkagnpdimdgvdPRLVVGPGTDVRPAEGLIATPGAIDVHVHFDSA-----------QLVDHALASG 155
|
....*
gi 119569521 101 -TTMI 104
Cdd:PRK13308 156 iTTML 160
|
|
| PRK08393 |
PRK08393 |
N-ethylammeline chlorohydrolase; Provisional |
17-88 |
9.65e-04 |
|
N-ethylammeline chlorohydrolase; Provisional
Pssm-ID: 181411 [Multi-domain] Cd Length: 424 Bit Score: 41.71 E-value: 9.65e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 119569521 17 LLIRGGRIVNDD--QSFYADVHVEDGLIKQIGENLIVPGGiKTIDAHGLMVLPGGVDVHTRLQMPVL-GMtpADD 88
Cdd:PRK08393 3 ILIKNGYVIYGEnlKVIRADVLIEGNKIVEVKRNINKPAD-TVIDASGSVVSPGFINAHTHSPMVLLrGL--ADD 74
|
|
| AdeC |
COG1001 |
Adenine deaminase [Nucleotide transport and metabolism]; |
17-102 |
1.19e-03 |
|
Adenine deaminase [Nucleotide transport and metabolism];
Pssm-ID: 440625 [Multi-domain] Cd Length: 559 Bit Score: 41.62 E-value: 1.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119569521 17 LLIRGGRIVN--DDQSFYADVHVEDGLIKQIGEnlIVPGGIKTIDAHGLMVLPGGVDVHTRL--QMpvlgMTPAdDFCqg 92
Cdd:COG1001 7 LVIKNGRLVNvfTGEILEGDIAIAGGRIAGVGD--YIGEATEVIDAAGRYLVPGFIDGHVHIesSM----VTPA-EFA-- 77
|
90
....*....|
gi 119569521 93 tKAALAGGTT 102
Cdd:COG1001 78 -RAVLPHGTT 86
|
|
| FMDH_A |
cd01304 |
Formylmethanofuran dehydrogenase (FMDH) subunit A; Methanogenic bacteria and archea derive ... |
34-74 |
2.57e-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: 40.47 E-value: 2.57e-03
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 119569521 34 DVHVEDGlikQIGENLIVPGGIKTIDAHGLMVLPGGVDVHT 74
Cdd:cd01304 19 DIFIRDG---KIVESSSGAKPAKVIDASGKVVMAGGVDMHS 56
|
|
| PRK07583 |
PRK07583 |
cytosine deaminase; |
33-76 |
2.92e-03 |
|
cytosine deaminase;
Pssm-ID: 236062 Cd Length: 438 Bit Score: 39.97 E-value: 2.92e-03
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 119569521 33 ADVHVEDGLIKQIGENLIVPGGIKTIDAHGLMVLPGGVDVHTRL 76
Cdd:PRK07583 41 VDIEIADGKIAAILPAGGAPDELPAVDLKGRMVWPCFVDMHTHL 84
|
|
| PRK08203 |
PRK08203 |
hydroxydechloroatrazine ethylaminohydrolase; Reviewed |
16-119 |
4.09e-03 |
|
hydroxydechloroatrazine ethylaminohydrolase; Reviewed
Pssm-ID: 236184 [Multi-domain] Cd Length: 451 Bit Score: 39.45 E-value: 4.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119569521 16 RLLIRGGRIV---NDDQSFYADVH--VEDGLIKQIGENLIVPGGI-KTIDAHGLMVLPGGVDVH-------TRLQMPVL- 81
Cdd:PRK08203 2 TLWIKNPLAIvtmDAARREIADGGlvVEGGRIVEVGPGGALPQPAdEVFDARGHVVTPGLVNTHhhfyqtlTRALPAAQd 81
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 119569521 82 ---------------GMTPaDDFCQGTKAALA----GGTTMILDH--VFPDTGVSLLAA 119
Cdd:PRK08203 82 aelfpwlttlypvwaRLTP-EMVRVATQTALAelllSGCTTSSDHhyLFPNGLRDALDD 139
|
|
| Imidazolone-5PH |
cd01296 |
Imidazolonepropionase/imidazolone-5-propionate hydrolase (Imidazolone-5PH) catalyzes the third ... |
35-76 |
4.40e-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: 39.55 E-value: 4.40e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 119569521 35 VHVEDGLIKQIGE----NLIVPGGIKTIDAHGLMVLPGGVDVHTRL 76
Cdd:cd01296 1 IAIRDGRIAAVGPaaslPAPGPAAAEEIDAGGRAVTPGLVDCHTHL 46
|
|
| PRK06038 |
PRK06038 |
N-ethylammeline chlorohydrolase; Provisional |
17-89 |
4.58e-03 |
|
N-ethylammeline chlorohydrolase; Provisional
Pssm-ID: 180363 [Multi-domain] Cd Length: 430 Bit Score: 39.35 E-value: 4.58e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 119569521 17 LLIRGGRIVNDDQSFY--ADVHVEDGLIKQIGENliVPGGIKT-IDAHGLMVLPGGVDVHTRLQMPVL-GMtpADDF 89
Cdd:PRK06038 4 IIIKNAYVLTMDAGDLkkGSVVIEDGTITEVSES--TPGDADTvIDAKGSVVMPGLVNTHTHAAMTLFrGY--ADDL 76
|
|
| Urease_alpha |
cd00375 |
Urease alpha-subunit; Urease is a nickel-dependent metalloenzyme that catalyzes the hydrolysis ... |
33-104 |
5.44e-03 |
|
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: 39.23 E-value: 5.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119569521 33 ADVHVEDGLIKQIG------------ENLIVPGGIKTIDAHGLMVLPGGVDVHTRLQMPvlgmtpaddfcQGTKAALAGG 100
Cdd:cd00375 83 ADIGIKDGRIVAIGkagnpdimdgvtPNMIVGPSTEVIAGEGKIVTAGGIDTHVHFICP-----------QQIEEALASG 151
|
....*
gi 119569521 101 -TTMI 104
Cdd:cd00375 152 iTTMI 156
|
|
| |
