|
Name |
Accession |
Description |
Interval |
E-value |
| D-HYD |
cd01314 |
D-hydantoinases (D-HYD) also called dihydropyrimidases (DHPase) and related proteins; DHPases ... |
1-403 |
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: 646.20 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952364 1 MVLPGGVDVHTRLQMPVMGMTPADDFCQGTKAALAGGTTMILDHVFPDAGVSLLAAYEQWRERADSAACCDYSLHVDIPR 80
Cdd:cd01314 48 YVLPGGIDPHTHLELPFMGTVTADDFESGTRAAAAGGTTTIIDFAIPNKGQSLLEAVEKWRGKADGKSVIDYGFHMIITD 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952364 81 WHESTKEELEALVrDKGVNSFLVFMAYKDRCQCTDGQIYEIFSLIRDLGAVAQVHAENGDIVEEEQKRLLEQGITGPEGH 160
Cdd:cd01314 128 WTDSVIEELPELV-KKGISSFKVFMAYKGLLMVDDEELLDVLKRAKELGALVMVHAENGDVIAELQKKLLAQGKTGPEYH 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952364 161 VLSHPEEVEAEAVYRAVTIAKQANCPLYVTKVMSKGAADMVAQAKRRGVVVFGEPITASLGTDGSHYWsKNWAKAAAFVT 240
Cdd:cd01314 207 ALSRPPEVEAEATARAIRLAELAGAPLYIVHVSSKEAADEIARARKKGLPVYGETCPQYLLLDDSDYW-KDWFEGAKYVC 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952364 241 SPPINPDpTTADHLTSLLSSGDLQVTGSAHCTFTTAQKAVGKDNFTLIPEGVNGIEERMSVVWEKCVASGKMDENEFVAV 320
Cdd:cd01314 286 SPPLRPK-EDQEALWDGLSSGTLQTVGSDHCPFNFAQKARGKDDFTKIPNGVPGVETRMPLLWSEGVAKGRITLEKFVEL 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952364 321 TSTNAAKIFNFYPRKGRVAVGSDADLVIWNPRATKVISAKSHNLNVEYNIFEGVECRGVPTVVISQGRVVLEDGNLLVTP 400
Cdd:cd01314 365 TSTNPAKIFGLYPRKGTIAVGSDADLVIWDPNAEKTISADTHHHNVDYNIFEGMKVKGWPVVTISRGKVVVEDGELVGEK 444
|
...
gi 568952364 401 GAG 403
Cdd:cd01314 445 GSG 447
|
|
| D-hydantoinase |
TIGR02033 |
D-hydantoinase; This model represents the D-hydantoinase (dihydropyrimidinase) which primarily ... |
1-408 |
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: 589.36 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952364 1 MVLPGGVDVHTRLQMPVMGMTPADDFCQGTKAALAGGTTMILDHVFPDAGVSLLAAYEQWRERADSAACCDYSLHVDIPR 80
Cdd:TIGR02033 48 YVLPGGIDVHTHLEMPFGGTTTADDFFTGTKAAAAGGTTTIIDFVVPEKGSSLTEALETWHEKAEGKSVIDYGFHMDITH 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952364 81 WHESTKEELEALVRDKGVNSFLVFMAYKDRCQCTDGQIYEIFSLIRDLGAVAQVHAENGDIVEEEQKRLLEQGITGPEGH 160
Cdd:TIGR02033 128 WNDSVLEEHIPEVKEEGINSFKVFMAYKNLLMVDDEELFEILKRLKELGALLQVHAENGDIIAELQARMLAQGITGPEYH 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952364 161 VLSHPEEVEAEAVYRAVTIAKQANCPLYVTKVMSKGAADMVAQAKRRGVVVFGEPITASLGTDGSHYWsKNWAKAAAFVT 240
Cdd:TIGR02033 208 ALSRPPELEAEAVARAITLAALADAPLYVVHVSTKDAADEIAQARKKGQPVFGETCPQYLVLDDTHYD-KPGFEGAKYVC 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952364 241 SPPINpDPTTADHLTSLLSSGDLQVTGSAHCTFTTAQK-AVGKDNFTLIPEGVNGIEERMSVVWEKCVASGKMDENEFVA 319
Cdd:TIGR02033 287 SPPLR-EPEDQDALWSALSSGALQTVGSDHCTFNFAQKkAIGKDDFTKIPNGGPGVEERMSLLFDEGVAKGRITLEKFVE 365
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952364 320 VTSTNAAKIFNFYPRKGRVAVGSDADLVIWNPRATKVISAKSHNLNVEYNIFEGVECRGVPTVVISQGRVVLEDGNLLVT 399
Cdd:TIGR02033 366 VTSTNPAKIFNLYPRKGTIAVGSDADIVIWDPNRTTVISAETHHSNADYNPFEGFKVRGAPVSVLSRGRVVVEDGQLVGT 445
|
....*....
gi 568952364 400 PGAGRFIPR 408
Cdd:TIGR02033 446 AGAGRFVKR 454
|
|
| PRK08323 |
PRK08323 |
phenylhydantoinase; Validated |
2-412 |
1.72e-180 |
|
phenylhydantoinase; Validated
Pssm-ID: 236240 [Multi-domain] Cd Length: 459 Bit Score: 514.34 E-value: 1.72e-180
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952364 2 VLPGGVDVHTRLQMPVMGMTPADDFCQGTKAALAGGTTMILDHVFPDAGVSLLAAYEQWRERADSAACCDYSLHVDIPRW 81
Cdd:PRK08323 47 VMPGGIDPHTHMEMPFGGTVSSDDFETGTRAAACGGTTTIIDFALQPKGQSLREALEAWHGKAAGKAVIDYGFHMIITDW 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952364 82 HESTKEELEALVrDKGVNSFLVFMAYKDRCQCTDGQIYEIFSLIRDLGAVAQVHAENGDIVEEEQKRLLEQGITGPEGHV 161
Cdd:PRK08323 127 NEVVLDEMPELV-EEGITSFKLFMAYKGALMLDDDELLRALQRAAELGALPMVHAENGDAIAYLQAKLLAEGKTGPEYHA 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952364 162 LSHPEEVEAEAVYRAVTIAKQANCPLYVTKVMSKGAADMVAQAKRRGVVVFGEPITASLGTDGSHYWSKNWAKAAAFVTS 241
Cdd:PRK08323 206 LSRPPEVEGEATNRAIMLAELAGAPLYIVHVSCKEALEAIRRARARGQRVFGETCPQYLLLDESEYDGPDWFEGAKYVMS 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952364 242 PPINPdPTTADHLTSLLSSGDLQVTGSAHCTFTTAQKA-VGKDNFTLIPEGVNGIEERMSVVWEKCVASGKMDENEFVAV 320
Cdd:PRK08323 286 PPLRD-KEHQDALWRGLQDGDLQVVATDHCPFCFEQKKqLGRGDFTKIPNGTPGVEDRMPLLFSEGVMTGRITLNRFVEL 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952364 321 TSTNAAKIFNFYPRKGRVAVGSDADLVIWNPRATKVISAKSHNLNVEYNIFEGVECRGVPTVVISQGRVVLEDGNLLVTP 400
Cdd:PRK08323 365 TSTNPAKIFGLYPRKGTIAVGADADIVIWDPNATKTISASTLHSNVDYNPYEGFEVTGWPVTTLSRGEVVVEDGEFRGKA 444
|
410
....*....|..
gi 568952364 401 GAGRFIPRKTFP 412
Cdd:PRK08323 445 GHGRFLKRKPFQ 456
|
|
| PLN02942 |
PLN02942 |
dihydropyrimidinase |
2-423 |
1.52e-169 |
|
dihydropyrimidinase
Pssm-ID: 178530 Cd Length: 486 Bit Score: 487.43 E-value: 1.52e-169
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952364 2 VLPGGVDVHTRLQMPVMGMTPADDFCQGTKAALAGGTTMILDHVFPDAGvSLLAAYEQWRERADSAaCCDYSLHVDIPRW 81
Cdd:PLN02942 55 VMPGGIDPHTHLAMPFMGTETIDDFFSGQAAALAGGTTMHIDFVIPVNG-NLLAGYEAYEKKAEKS-CMDYGFHMAITKW 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952364 82 HESTKEELEALVRDKGVNSFLVFMAYKDRCQCTDGQIYEIFSLIRDLGAVAQVHAENGDIVEEEQKRLLEQGITGPEGHV 161
Cdd:PLN02942 133 DDTVSRDMETLVKEKGINSFKFFMAYKGSLMVTDELLLEGFKRCKSLGALAMVHAENGDAVFEGQKRMIELGITGPEGHA 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952364 162 LSHPEEVEAEAVYRAVTIAKQANCPLYVTKVMSKGAADMVAQAKRRGVVVFGEPITASLGTDGSHYWSKNWAKAAAFVTS 241
Cdd:PLN02942 213 LSRPPLLEGEATARAIRLAKFVNTPLYVVHVMSIDAMEEIARARKSGQRVIGEPVVSGLVLDDSKLWDPDFTIASKYVMS 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952364 242 PPINPdpttADH---LTSLLSSGDLQVTGSAHCTFTTAQKAVGKDNFTLIPEGVNGIEERMSVVWEKCVASGKMDENEFV 318
Cdd:PLN02942 293 PPIRP----AGHgkaLQAALSSGILQLVGTDHCPFNSTQKAFGKDDFRKIPNGVNGIEERMHLVWDTMVESGQISPTDYV 368
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952364 319 AVTSTNAAKIFNFYPRKGRVAVGSDADLVIWNPRATKVISAKSHNLNVEYNIFEGVECRGVPTVVISQGRVVLEDGNLLV 398
Cdd:PLN02942 369 RVTSTECAKIFNIYPRKGAILAGSDADIIILNPNSTFTISAKTHHSRIDTNVYEGRRGKGKVEVTISQGRVVWENGELKV 448
|
410 420
....*....|....*....|....*
gi 568952364 399 TPGAGRFIPRKTFPdFVYKRIKARN 423
Cdd:PLN02942 449 VRGSGRYIEMPPFS-YLFDGIQKAD 472
|
|
| AllB |
COG0044 |
Dihydroorotase or related cyclic amidohydrolase [Nucleotide transport and metabolism]; ... |
2-408 |
1.22e-106 |
|
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: 325.12 E-value: 1.22e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952364 2 VLPGGVDVHTRLQMPvmGMTPADDFCQGTKAALAGGTTMILDHVFPDAGVSLLAAYEQWRERADSAACCDYSLHVDIPRW 81
Cdd:COG0044 48 VLPGLIDLHVHLREP--GLEHKEDIETGTRAAAAGGVTTVVDMPNTNPVTDTPEALEFKLARAEEKALVDVGPHGALTKG 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952364 82 HESTKEELEALVrDKGVNSFLVFMAYKD-RCQCTDGQIYEIFSLIRDLGAVAQVHAENGDIVEEeqkRLLEQGITGPEGH 160
Cdd:COG0044 126 LGENLAELGALA-EAGAVAFKVFMGSDDgNPVLDDGLLRRALEYAAEFGALVAVHAEDPDLIRG---GVMNEGKTSPRLG 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952364 161 VLSHPEEVEAEAVYRAVTIAKQANCPLYVTKVMSKGAADMVAQAKRRGVVVFGE--P----ITAS-LGTDGSHYwsknwa 233
Cdd:COG0044 202 LKGRPAEAEEEAVARDIALAEETGARLHIVHVSTAEAVELIREAKARGLPVTAEvcPhhltLTDEdLERYGTNF------ 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952364 234 kaaafVTSPPINpdptTADHLTSL---LSSGDLQVTGSAHCTFTTAQKAvgkDNFTLIPEGVNGIEERMSVVWEKCVASG 310
Cdd:COG0044 276 -----KVNPPLR----TEEDREALwegLADGTIDVIATDHAPHTLEEKE---LPFAEAPNGIPGLETALPLLLTELVHKG 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952364 311 KMDENEFVAVTSTNAAKIFNFyPRKGRVAVGSDADLVIWNPRATKVISAKSHNLNVEYNIFEGVECRGVPTVVISQGRVV 390
Cdd:COG0044 344 RLSLERLVELLSTNPARIFGL-PRKGRIAVGADADLVLFDPDAEWTVTAEDLHSKSKNTPFEGRELTGRVVATIVRGRVV 422
|
410
....*....|....*...
gi 568952364 391 LEDGNLLVTPgAGRFIPR 408
Cdd:COG0044 423 YEDGEVVGEP-RGRFLRR 439
|
|
| PRK13404 |
PRK13404 |
dihydropyrimidinase; Provisional |
1-408 |
1.25e-102 |
|
dihydropyrimidinase; Provisional
Pssm-ID: 184033 [Multi-domain] Cd Length: 477 Bit Score: 316.25 E-value: 1.25e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952364 1 MVLPGGVDVHTRLQMPV-MGMTPADDFCQGTKAALAGGTTMILDHVFPDAGVSLLAAYEQWRERADSAACCDYSLHVDIP 79
Cdd:PRK13404 51 LVLPGGVDSHCHIDQPSgDGIMMADDFYTGTVSAAFGGTTTVIPFAAQHRGQSLREAVEDYHRRAAGKAVIDYAFHLIVA 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952364 80 RWHEST-KEELEALVRDkGVNSFLVFMAYkDRCQCTDGQIYEIFSLIRDLGAVAQVHAENGDIVEEEQKRLLEQGITGPE 158
Cdd:PRK13404 131 DPTEEVlTEELPALIAQ-GYTSFKVFMTY-DDLKLDDRQILDVLAVARRHGAMVMVHAENHDMIAWLTKRLLAAGLTAPK 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952364 159 GHVLSHPEEVEAEAVYRAVTIAKQANCPLYVTKVMSKGAADMVAQAKRRGVVVFGEP------ITAS-LGTDGSHywskn 231
Cdd:PRK13404 209 YHAISRPMLAEREATHRAIALAELVDVPILIVHVSGREAAEQIRRARGRGLKIFAETcpqylfLTAEdLDRPGME----- 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952364 232 wakAAAFVTSPPinpdPTTADHLTSL---LSSGDLQVTGSAHCTF---TTAQKAVGKDN--FTLIPEGVNGIEERMSVVW 303
Cdd:PRK13404 284 ---GAKYICSPP----PRDKANQEAIwngLADGTFEVFSSDHAPFrfdDTDGKLAAGANpsFKAIANGIPGIETRLPLLF 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952364 304 EKCVASGKMDENEFVAVTSTNAAKIFNFYPRKGRVAVGSDADLVIWNPRATKVISAKSHNLNVEYNIFEGVECRGVPTVV 383
Cdd:PRK13404 357 SEGVVKGRISLNRFVALTSTNPAKLYGLYPRKGAIAIGADADIAIWDPDREVTITNADLHHAADYTPYEGMRVTGWPVTV 436
|
410 420
....*....|....*....|....*
gi 568952364 384 ISQGRVVLEDGNLLVTPGAGRFIPR 408
Cdd:PRK13404 437 LSRGRVVVEDGELVAERGSGQFLAR 461
|
|
| Cyclic_amidohydrolases |
cd01302 |
Cyclic amidohydrolases, including hydantoinase, dihydropyrimidinase, allantoinase, and ... |
2-380 |
4.31e-56 |
|
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: 190.68 E-value: 4.31e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952364 2 VLPGGVDVHTRLQMPVMGMTpADDFCQGTKAALAGGTTMILDHVFPDAGVSLLAAYEQWRERADSAACCDYSLHVDIprW 81
Cdd:cd01302 3 VLPGFIDIHVHLRDPGGTTY-KEDFESGSRAAAAGGVTTVIDMPNTGPPPIDLPAIELKIKLAEESSYVDFSFHAGI--G 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952364 82 HESTKEELEaLVRDKGVNSFLVFMAYK--DRCQCTDGQIYEIFSLIRDLGAVAQVHAEngdiveeeqkrlleqgitgpeg 159
Cdd:cd01302 80 PGDVTDELK-KLFDAGINSLKVFMNYYfgELFDVDDGTLMRTFLEIASRGGPVMVHAE---------------------- 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952364 160 hvlshpeeveaeavyRAVTIAKQANCPLYVTKVMSKGAADMVAQAKRRGVVVFGEPITASLGTDGShYWSKNWAKaaaFV 239
Cdd:cd01302 137 ---------------RAAQLAEEAGANVHIAHVSSGEALELIKFAKNKGVKVTCEVCPHHLFLDES-MLRLNGAW---GK 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952364 240 TSPPINPdPTTADHLTSLLSSGDLQVTGSAHCTFTTAQKAVGKDnFTLIPEGVNGIEERMSVVWEKcVASGKMDENEFVA 319
Cdd:cd01302 198 VNPPLRS-KEDREALWEGVKNGKIDTIASDHAPHSKEEKESGKD-IWKAPPGFPGLETRLPILLTE-GVKRGLSLETLVE 274
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568952364 320 VTSTNAAKIFNFYPrKGRVAVGSDADLVIWNPRATKVISAKSHNLNVEYNIFEGVECRGVP 380
Cdd:cd01302 275 ILSENPARIFGLYP-KGTIAVGYDADLVIVDPKKEWKVTAEEIESKADWTPFEGMEVTGKP 334
|
|
| L-HYD_ALN |
cd01315 |
L-Hydantoinases (L-HYDs) and Allantoinase (ALN); L-Hydantoinases are a member of the ... |
1-406 |
4.46e-51 |
|
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: 180.18 E-value: 4.46e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952364 1 MVLPGGVDVHTRLQMPvmGMTPADDFCQGTKAALAGGTTMILD---HVFPDA--GVSLLAAYEQWRERadsaaccdysLH 75
Cdd:cd01315 49 VVMPGLIDTHVHINEP--GRTEWEGFETGTKAAAAGGITTIIDmplNSIPPTttVENLEAKLEAAQGK----------LH 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952364 76 VDIPRWHESTK---EELEALVrDKGVNSFLVFMA---YKDRCQCTDGQIYEIFSLIRDLGAVAQVHAENGDIVEEEQKRL 149
Cdd:cd01315 117 VDVGFWGGLVPgnlDQLRPLD-EAGVVGFKCFLCpsgVDEFPAVDDEQLEEAMKELAKTGSVLAVHAENPEITEALQEQA 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952364 150 LEQGITGPEGHVLSHPEEVEAEAVYRAVTIAKQANCPLYVTKVMSKGAADMVAQAKRRGVVVFGEPITaslgtdgsHYWS 229
Cdd:cd01315 196 KAKGKRDYRDYLASRPVFTEVEAIQRILLLAKETGCRLHIVHLSSAEAVPLIREARAEGVDVTVETCP--------HYLT 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952364 230 -------KNwakAAAFVTSPPINpDPTTADHLTSLLSSGDLQVTGSAHCTFTTAQKAVGKDNFTLIPEGVNGIEERMSVV 302
Cdd:cd01315 268 ftaedvpDG---GTEFKCAPPIR-DAANQEQLWEALENGDIDMVVSDHSPCTPELKLLGKGDFFKAWGGISGLQLGLPVM 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952364 303 WEKCVASGKMDENEFVAVTSTNAAKIFNFYPRKGRVAVGSDADLVIWNPRATKVISAKSHNLNVEYNIFEGVECRGVPTV 382
Cdd:cd01315 344 LTEAVNKRGLSLEDIARLMCENPAKLFGLSHQKGRIAVGYDADFVVWDPEEEFTVDAEDLYYKNKISPYVGRTLKGRVHA 423
|
410 420
....*....|....*....|....
gi 568952364 383 VISQGRVVLEDGNLLVTPgAGRFI 406
Cdd:cd01315 424 TILRGTVVYQDGEVVGEP-LGQLL 446
|
|
| PRK02382 |
PRK02382 |
dihydroorotase; Provisional |
2-409 |
2.92e-36 |
|
dihydroorotase; Provisional
Pssm-ID: 179417 [Multi-domain] Cd Length: 443 Bit Score: 139.79 E-value: 2.92e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952364 2 VLPGGVDVHTRLQMPvmGMTPADDFCQGTKAALAGGTTMILDHVFPDAGVSLLAAYEQWRERADSAACCDYSLHVDI-PR 80
Cdd:PRK02382 52 LLPGGIDVHVHFREP--GYTHKETWYTGSRSAAAGGVTTVVDQPNTDPPTVDGESFDEKAELAARKSIVDFGINGGVtGN 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952364 81 WhestkEELEALVRdKGVNSF-LVFMAYKDRCQCTDGQIY-EIFSLIRDLGAVAQVHAENGDIVEEEQKRLleQGITGPE 158
Cdd:PRK02382 130 W-----DPLESLWE-RGVFALgEIFMADSTGGMGIDEELFeEALAEAARLGVLATVHAEDEDLFDELAKLL--KGDADAD 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952364 159 GHVLSHPEEVEAEAVYRAVTIAKQANCPLYVTKVMSKGAADMvaqAKRRGVVVFGEPITASLGTDgshywskNWAKAAAF 238
Cdd:PRK02382 202 AWSAYRPAAAEAAAVERALEVASETGARIHIAHISTPEGVDA---ARREGITCEVTPHHLFLSRR-------DWERLGTF 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952364 239 V-TSPPINPDPTTaDHLTSLLSSGDLQVTGSAHCTFTTAQKAVG-KDnftlIPEGVNGIEERMSVVWEKcVASGKMDENE 316
Cdd:PRK02382 272 GkMNPPLRSEKRR-EALWERLNDGTIDVVASDHAPHTREEKDADiWD----APSGVPGVETMLPLLLAA-VRKNRLPLER 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952364 317 FVAVTSTNAAKIFNFyPRKGRVAVGSDADLVIWNPRATKVISAKSHNLNVEYNIFEGVEcrGV-PTVVISQGRVVLEDGN 395
Cdd:PRK02382 346 VRDVTAANPARIFGL-DGKGRIAEGYDADLVLVDPDAAREIRGDDLHSKAGWTPFEGME--GVfPELTMVRGTVVWDGDD 422
|
410
....*....|....
gi 568952364 396 LLVTPGAGRFIPRK 409
Cdd:PRK02382 423 INAKRGRGEFLRGR 436
|
|
| pyrC_multi |
TIGR00857 |
dihydroorotase, multifunctional complex type; In contrast to the homodimeric type of ... |
1-393 |
1.12e-35 |
|
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: 137.57 E-value: 1.12e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952364 1 MVLPGGVDVHTRLQMPvmGMTPADDFCQGTKAALAGGTTMILDHVFPDAGVSLLAAYEQWRERADSAACCDYSLHVDIPR 80
Cdd:TIGR00857 36 LVLPGFIDLHVHLRDP--GEEYKEDIESGSKAAAHGGFTTVADMPNTKPPIDTPETLEWKLQRLKKVSLVDVHLYGGVTQ 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952364 81 wHESTKEELEAlvrdkgvnSFLVFMAYKDRCQCTDG-QIYEIFSLIRDLGAVAQ------VHAENGDIVEEEQKRlleQG 153
Cdd:TIGR00857 114 -GNQGKELTEA--------YELKEAGAVGRMFTDDGsEVQDILSMRRALEYAAIagvpiaLHAEDPDLIYGGVMH---EG 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952364 154 ITGPEGHVLSHPEEVEAEAVYRAVTIAKQANCPLYVTKVMSKGAADMVAQAKRRGVvvfgePITAS------LGTDGSHY 227
Cdd:TIGR00857 182 PSAAQLGLPARPPEAEEVAVARLLELAKHAGCPVHICHISTKESLELIVKAKSQGI-----KITAEvtphhlLLSEEDVA 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952364 228 WSKNWAKaaafvTSPPINPdPTTADHLTSLLSSGDLQVTGSAHCTFTTAQKAVgkdNFTLIPEGVNGIEERMSVVWEKCV 307
Cdd:TIGR00857 257 RLDGNGK-----VNPPLRE-KEDRLALIEGLKDGIIDIIATDHAPHTLEEKTK---EFAAAPPGIPGLETALPLLLQLLV 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952364 308 AsGKMDENEFVAVTSTNAAKIFNFyPRKGRVAVGSDADLVIWNPRATKVISAKSHNLNVEYNIFEGVECRGVPTVVISQG 387
Cdd:TIGR00857 328 K-GLISLKDLIRMLSINPARIFGL-PDKGTLEEGNPADITVFDLKKEWTINAETFYSKAKNTPFEGMSLKGKPIATILRG 405
|
....*.
gi 568952364 388 RVVLED 393
Cdd:TIGR00857 406 KVVYED 411
|
|
| PRK06189 |
PRK06189 |
allantoinase; Provisional |
2-406 |
4.64e-35 |
|
allantoinase; Provisional
Pssm-ID: 235732 [Multi-domain] Cd Length: 451 Bit Score: 136.37 E-value: 4.64e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952364 2 VLPGGVDVHTRLQMPvmGMTPADDFCQGTKAALAGGTT----MILDHVFPdagVSLLAAYEQWRERADSAACCDYSLhvd 77
Cdd:PRK06189 52 VFPGMIDVHVHFNEP--GRTHWEGFATGSAALAAGGCTtyfdMPLNSIPP---TVTREALDAKAELARQKSAVDFAL--- 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952364 78 iprWHESTKEELEAL--VRDKGVNSFLVFMAYK--DRCQ-CTDGQIYEIFSLIRDLGAVAQVHAENGDIVEEEQKRLLEQ 152
Cdd:PRK06189 124 ---WGGLVPGNLEHLreLAEAGVIGFKAFMSNSgtDEFRsSDDLTLYEGMKEIAALGKILALHAESDALTRHLTTQARQQ 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952364 153 GITGPEGHVLSHPEEVEAEAVYRAVTIAKQANCPLYVTKVMSKGAADMVAQAKRRGVVV----------FGEPITASLGT 222
Cdd:PRK06189 201 GKTDVRDYLESRPVVAELEAVQRALLYAQETGCPLHFVHISSGKAVALIAEAKKRGVDVsvetcphyllFTEEDFERIGA 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952364 223 dgshywsknWAKAAafvtsPPINpDPTTADHLTSLLSSGDLQVTGSAHCTFTTAQKAvgKDNFTLIPEGVNGIEERMSVV 302
Cdd:PRK06189 281 ---------VAKCA-----PPLR-SRSQKEELWRGLLAGEIDMISSDHSPCPPELKE--GDDFFLVWGGISGGQSTLLVM 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952364 303 WEKCVASGKMDENEFVAVTSTNAAKIFNFyPRKGRVAVGSDADLVIWNPRATKVISAKSHNLNVEYNIFEGVECRGVPTV 382
Cdd:PRK06189 344 LTEGYIERGIPLETIARLLATNPAKRFGL-PQKGRLEVGADADFVLVDLDETYTLTKEDLFYRHKQSPYEGRTFPGRVVA 422
|
410 420
....*....|....*....|....
gi 568952364 383 VISQGRVVLEDGNlLVTPGAGRFI 406
Cdd:PRK06189 423 TYLRGQCVYQDGE-VFPPPRGQLL 445
|
|
| DHOase_IIb |
cd01318 |
Dihydroorotase (DHOase), subgroup IIb; DHOases catalyze the reversible interconversion of ... |
2-387 |
3.27e-31 |
|
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: 123.98 E-value: 3.27e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952364 2 VLPGGVDVHTRLQMPvmGMTPADDFCQGTKAALAGGTTMILD---HVFPdagVSLLAAYEQWRERADSAACCDYSLHVDI 78
Cdd:cd01318 4 ILPGVIDIHVHFREP--GLTYKEDFVSGSRAAAAGGVTTVMDmpnTKPP---TTTAEALYEKLRLAAAKSVVDYGLYFGV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952364 79 PRwhESTKEELEALvrdkGVNSFLVFMAykdrcQCT-DGQIYE--IFSLIRDLGAVAQVHAENGDIVEEEQKRLLEQGIt 155
Cdd:cd01318 79 TG--SEDLEELDKA----PPAGYKIFMG-----DSTgDLLDDEetLERIFAEGSVLVTFHAEDEDRLRENRKELKGESA- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952364 156 gpegHVLSHPEEVEAEAVYRAVTIAKQANCPLYVTKVMSKGAADMVAQAKRRGVV-------VFGEPITASLGTdgshyw 228
Cdd:cd01318 147 ----HPRIRDAEAAAVATARALKLARRHGARLHICHVSTPEELKLIKKAKPGVTVevtphhlFLDVEDYDRLGT------ 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952364 229 sknWAKaaafvTSPPINpDPTTADHLTSLLSSGDLQVTGSAHCTFTTAQKAVGKDNftlIPEGVNGIEERMSVVWEKcVA 308
Cdd:cd01318 217 ---LGK-----VNPPLR-SREDRKALLQALADGRIDVIASDHAPHTLEEKRKGYPA---APSGIPGVETALPLMLTL-VN 283
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568952364 309 SGKMDENEFVAVTSTNAAKIFNFyPRKGRVAVGSDADLVIWNPRATKVISAKSHNLNVEYNIFEGVECRGVPTVVISQG 387
Cdd:cd01318 284 KGILSLSRVVRLTSHNPARIFGI-KNKGRIAEGYDADLTVVDLKEERTIRAEEFHSKAGWTPFEGFEVTGFPVMTIVRG 361
|
|
| DHOase_IIa |
cd01317 |
Dihydroorotase (DHOase), subgroup IIa; DHOases catalyze the reversible interconversion of ... |
2-381 |
1.18e-25 |
|
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: 108.09 E-value: 1.18e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952364 2 VLPGGVDVHTRLQMPvmGMTPADDFCQGTKAALAGGTT--MILDHVFPDagVSLLAAYEQWRERADsaaccDYSLHVDIP 79
Cdd:cd01317 12 LAPGLVDLHVHLREP--GFEYKETLESGAKAAAAGGFTtvVCMPNTNPV--IDNPAVVELLKNRAK-----DVGIVRVLP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952364 80 rWHESTK----EELE--ALVRDKGVNSFlvfmaYKDRCQCTDGQI-YEIFSLIRDLGAVAQVHAENgdiveeeqKRLLEQ 152
Cdd:cd01317 83 -IGALTKglkgEELTeiGELLEAGAVGF-----SDDGKPIQDAELlRRALEYAAMLDLPIIVHPED--------PSLAGG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952364 153 GIT--GPEGHVL---SHPEEVEAEAVYRAVTIAKQANCPLYVTKVMSKGAADMVAQAKRRGVvvfgePITASLGtdgSHY 227
Cdd:cd01317 149 GVMneGKVASRLglpGIPPEAETIMVARDLELAEATGARVHFQHLSTARSLELIRKAKAKGL-----PVTAEVT---PHH 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952364 228 WSKNWAKAAAFVTSPPINP---DPTTADHLTSLLSSGDLQVTGSAHCTFTTAQKAVGkdnFTLIPEGVNGIEERMSVVWE 304
Cdd:cd01317 221 LLLDDEALESYDTNAKVNPplrSEEDREALIEALKDGTIDAIASDHAPHTDEEKDLP---FAEAPPGIIGLETALPLLWT 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952364 305 KCVASGKMDENEFVAVTSTNAAKIFNFYPrkGRVAVGSDADLVIWNPRATKVISA-----KSHNlnveyNIFEGVECRGV 379
Cdd:cd01317 298 LLVKGGLLTLPDLIRALSTNPAKILGLPP--GRLEVGAPADLVLFDPDAEWIVDEetfrsKSKN-----TPFDGQKLKGR 370
|
..
gi 568952364 380 PT 381
Cdd:cd01317 371 VL 372
|
|
| Amidohydro_1 |
pfam01979 |
Amidohydrolase family; This family of enzymes are a a large metal dependent hydrolase ... |
1-390 |
1.61e-25 |
|
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: 107.20 E-value: 1.61e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952364 1 MVLPGGVDVHTRLQMPVMGMTPADDFC------QGTKAALAGGTTMILDHVF--PDAGVSLLAAYEQWRE--RADSAACC 70
Cdd:pfam01979 1 IVLPGLIDAHVHLEMGLLRGIPVPPEFayealrLGITTMLKSGTTTVLDMGAttSTGIEALLEAAEELPLglRFLGPGCS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952364 71 ---DYSLHVDIPRWHEStKEELEALVRDKGVNSFLVFMAYKDRcQCTDGQIYEIFSLIRDLGAVAQVHAENGDiveEEQK 147
Cdd:pfam01979 81 ldtDGELEGRKALREKL-KAGAEFIKGMADGVVFVGLAPHGAP-TFSDDELKAALEEAKKYGLPVAIHALETK---GEVE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952364 148 RLLEQGITGPEghVLSHPEEVEAEAVYRAVTIAKQANCPLYVTkvmskGAADMVAQAKRRGVVvfgepitasLGTDGSHY 227
Cdd:pfam01979 156 DAIAAFGGGIE--HGTHLEVAESGGLLDIIKLILAHGVHLSPT-----EANLLAEHLKGAGVA---------HCPFSNSK 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952364 228 WSKNWAKAAAfvtsppinpdpttadhltsLLSSGDLQVTGSAHCtfttaqkaVGKDNFTLIPEGVNGIEERMsvvwekcV 307
Cdd:pfam01979 220 LRSGRIALRK-------------------ALEDGVKVGLGTDGA--------GSGNSLNMLEELRLALELQF-------D 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952364 308 ASGKMDENEFVAVTSTNAAKIFNFYPRKGRVAVGSDADLVIWNPRatkvisakshnlnvEYNIFEGVECRGVPTVVISQG 387
Cdd:pfam01979 266 PEGGLSPLEALRMATINPAKALGLDDKVGSIEVGKDADLVVVDLD--------------PLAAFFGLKPDGNVKKVIVKG 331
|
...
gi 568952364 388 RVV 390
Cdd:pfam01979 332 KIV 334
|
|
| PRK08044 |
PRK08044 |
allantoinase AllB; |
1-407 |
2.87e-23 |
|
allantoinase AllB;
Pssm-ID: 169193 [Multi-domain] Cd Length: 449 Bit Score: 102.24 E-value: 2.87e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952364 1 MVLPGGVDVHTRLQMPvmGMTPADDFCQGTKAALAGG-TTMIldhVFPDAGVSLLAAYEQWRERADSAaccDYSLHVDIP 79
Cdd:PRK08044 50 VVSPGMVDAHTHISEP--GRSHWEGYETGTRAAAKGGiTTMI---EMPLNQLPATVDRASIELKFDAA---KGKLTIDAA 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952364 80 RWHESTKEELEAL--VRDKGVNSFLVFMAY-------KDRCQCTDGQIYEIFSLIRDLGAVAQVHAENGDIVEEEQKRLL 150
Cdd:PRK08044 122 QLGGLVSYNLDRLheLDEVGVVGFKCFVATcgdrgidNDFRDVNDWQFYKGAQKLGELGQPVLVHCENALICDELGEEAK 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952364 151 EQGITGPEGHVLSHPEEVEAEAVYRAVTIAKQANCPLYVTKVMSKGAADMVAQAKRRGVVVFGEPITaslgtdgsHYWSK 230
Cdd:PRK08044 202 REGRVTAHDYVASRPVFTEVEAIRRVLYLAKVAGCRLHVCHISSPEGVEEVTRARQEGQDVTCESCP--------HYFVL 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952364 231 NWAKAAAFVT----SPPINpDPTTADHLTSLLSSGDLQVTGSAHCTFTTAQKAvgkDNFTLIPEGVNGIEERMSVVWEKC 306
Cdd:PRK08044 274 DTDQFEEIGTlakcSPPIR-DLENQKGMWEKLFNGEIDCLVSDHSPCPPEMKA---GNIMEAWGGIAGLQNCMDVMFDEA 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952364 307 VASGKMDENEFVAVTSTNAAKIFNFyPRKGRVAVGSDADLVIWNPRATKVISAKSHNLNVEYNIFEGVECRGVPTVVISQ 386
Cdd:PRK08044 350 VQKRGMSLPMFGKLMATNAADIFGL-QQKGRIAPGKDADFVFIQPNSSYVLKNEDLEYRHKVSPYVGRTIGARITKTILR 428
|
410 420
....*....|....*....|.
gi 568952364 387 GRVVLEDGNLLVTPGAGRFIP 407
Cdd:PRK08044 429 GDVIYDIEQGFPVAPKGQFIL 449
|
|
| PLN02795 |
PLN02795 |
allantoinase |
1-395 |
7.47e-21 |
|
allantoinase
Pssm-ID: 178392 [Multi-domain] Cd Length: 505 Bit Score: 95.61 E-value: 7.47e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952364 1 MVLPGGVDVHTRLQMPvmGMTPADDFCQGTKAALAGGTTMILDhvFPDAGVSLLAAYEQWRERADSAAccdYSLHVDIPR 80
Cdd:PLN02795 96 VVMPGLIDVHVHLNEP--GRTEWEGFPTGTKAAAAGGITTLVD--MPLNSFPSTTSVETLELKIEAAK---GKLYVDVGF 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952364 81 WHESTKE------ELEALVrDKGVNSFLVFM---AYKDRCQCTDGQIYEIFSLIRDLGAVAQVHAENGDIVEEEQKrlLE 151
Cdd:PLN02795 169 WGGLVPEnahnasVLEELL-DAGALGLKSFMcpsGINDFPMTTATHIKAALPVLAKYGRPLLVHAEVVSPVESDSR--LD 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952364 152 QGITGPEGHVLSHPEEVEAEAVYRAVTIAKQAN-------CPLYVTKVM-SKGAADMVAQAKRRGVVVFGEPITaslgtd 223
Cdd:PLN02795 246 ADPRSYSTYLKSRPPSWEQEAIRQLLEVAKDTRpggvaegAHVHIVHLSdAESSLELIKEAKAKGDSVTVETCP------ 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952364 224 gsHYWsknwAKAAA--------FVTSPPINpDPTTADHLTSLLSSGDLQVTGSAHCTFTTAQKAVGKDNFTLIPEGVNGI 295
Cdd:PLN02795 320 --HYL----AFSAEeipdgdtrYKCAPPIR-DAANRELLWKALLDGDIDMLSSDHSPSPPDLKLLEEGNFLRAWGGISSL 392
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952364 296 EERMSVVWEKCVASGkMDENEFVAVTSTNAAKIFNFyPRKGRVAVGSDADLVIWNPRATKVISA------KSHNLNVeyn 369
Cdd:PLN02795 393 QFVLPATWTAGRAYG-LTLEQLARWWSERPAKLAGL-DSKGAIAPGKDADIVVWDPEAEFVLDEsypiyhKHKSLSP--- 467
|
410 420
....*....|....*....|....*.
gi 568952364 370 iFEGVECRGVPTVVISQGRVVLEDGN 395
Cdd:PLN02795 468 -YLGTKLSGKVIATFVRGNLVFLEGK 492
|
|
| pyrC |
PRK09357 |
dihydroorotase; Validated |
2-393 |
8.21e-20 |
|
dihydroorotase; Validated
Pssm-ID: 236479 [Multi-domain] Cd Length: 423 Bit Score: 91.80 E-value: 8.21e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952364 2 VLPGGVDVHTRLQMPvmGMTPADDFCQGTKAALAGG---------TTMILDhvfpDAGVsllaaYEQWRERADSAACCDy 72
Cdd:PRK09357 51 VAPGLVDLHVHLREP--GQEDKETIETGSRAAAAGGfttvvampnTKPVID----TPEV-----VEYVLDRAKEAGLVD- 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952364 73 sLHVDIPRWHESTKEEL---EALvRDKGVNSFlvfmaykdrcqCTDGQIYEIFSLIRdlGAVAQVHAENGDIVE-EEQKR 148
Cdd:PRK09357 119 -VLPVGAITKGLAGEELtefGAL-KEAGVVAF-----------SDDGIPVQDARLMR--RALEYAKALDLLIAQhCEDPS 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952364 149 LLEQGITGpEGHVLSH------PEEVEAEAVYRAVTIAKQANCPLYVTKVMSKGAADMVAQAKRRGVvvfgePITA---- 218
Cdd:PRK09357 184 LTEGGVMN-EGEVSARlglpgiPAVAEEVMIARDVLLAEATGARVHICHVSTAGSVELIRWAKALGI-----KVTAevtp 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952364 219 --------SLGTDGSHYwsknwaKaaafvtsppINPdP--TTADHLTSL--LSSGDLQVTGSAHCTFTTAQKAVGkdnFT 286
Cdd:PRK09357 258 hhllltdeDLLTYDPNY------K---------VNP-PlrTEEDREALIegLKDGTIDAIATDHAPHAREEKECE---FE 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952364 287 LIPEGVNGIEERMSVVWEKCVASGKMDENEFVAVTSTNAAKIFNFYPrkGRVAVGSDADLVIWNPRATKVISA-----KS 361
Cdd:PRK09357 319 AAPFGITGLETALSLLYTTLVKTGLLDLEQLLEKMTINPARILGLPA--GPLAEGEPADLVIFDPEAEWTVDGedfasKG 396
|
410 420 430
....*....|....*....|....*....|..
gi 568952364 362 HNlnveyNIFEGVECRGVPTVVISQGRVVLED 393
Cdd:PRK09357 397 KN-----TPFIGMKLKGKVVYTIVDGKIVYQD 423
|
|
| PRK01211 |
PRK01211 |
dihydroorotase; Provisional |
2-408 |
1.56e-18 |
|
dihydroorotase; Provisional
Pssm-ID: 179247 [Multi-domain] Cd Length: 409 Bit Score: 87.61 E-value: 1.56e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952364 2 VLPGGVDVHTRLQMPvmGMTPADDFCQGTKAALAGGTTMILDHVFPDAGVSLLAAYEQWRERADSAACCDYSLHvdiprw 81
Cdd:PRK01211 44 ILPAATDIHVHFRTP--GETEKEDFSTGTLSAIFGGTTFIMDMPNNNIPIKDYNAFSDKLGRVAPKAYVDFSLY------ 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952364 82 heSTKEELEALVRDKGVNSFLVFMAYKDRCQCTDGQIYEIfSLIRDLGAVAQVHAENGDIVEE---EQKRLLEqgitgpe 158
Cdd:PRK01211 116 --SMETGNNALILDERSIGLKVYMGGTTNTNGTDIEGGEI-KKINEANIPVFFHAELSECLRKhqfESKNLRD------- 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952364 159 gHVLSHPEEVEAEAVYRAVTIAKQANCPLYVTKVMSKGaaDMVAQAKRRGVVVFGEpitASLGTDGShywsknwakaaaf 238
Cdd:PRK01211 186 -HDLARPIECEIKAVKYVKNLDLKTKIIAHVSSIDVIG--RFLREVTPHHLLLNDD---MPLGSYGK------------- 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952364 239 vTSPPINpDPTTADHLTSLLSSGDLQVTGSAHCTFTTAQKAvgkdNFTLIPEGVNGIEERMSVVWeKCVASGKMDENEFV 318
Cdd:PRK01211 247 -VNPPLR-DRWTQERLLEEYISGRFDILSSDHAPHTEEDKQ----EFEYAKSGIIGVETRVPLFL-ALVKKKILPLDVLY 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952364 319 AVTSTNAAKIFNFypRKGRVAVGSDADLVIWNPRATKVISAKSHNLNVEYNIFEGVECRgVPTVVISQGRVVLEDGNLLV 398
Cdd:PRK01211 320 KTAIERPASLFGI--KKGKIEEGYDADFMAFDFTNIKKINDKRLHSKCPVSPFNGFDAI-FPSHVIMRGEVVIDNYELIS 396
|
410
....*....|
gi 568952364 399 TPgAGRFIPR 408
Cdd:PRK01211 397 ER-TGKFVPK 405
|
|
| PRK04250 |
PRK04250 |
dihydroorotase; Provisional |
1-400 |
2.63e-18 |
|
dihydroorotase; Provisional
Pssm-ID: 235265 [Multi-domain] Cd Length: 398 Bit Score: 86.75 E-value: 2.63e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952364 1 MVLPGGVDVHTRLQmpvmgmtpadDFCQ--------GTKAALAGGTTMILDHVFPDAGVSLLAAYEQWRERADSAACCDY 72
Cdd:PRK04250 44 IILPGLIDVHVHLR----------DFEEsyketiesGTKAALHGGITLVFDMPNTKPPIMDEKTYEKRMRIAEKKSYADY 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952364 73 SLHVDIprwhESTKEELEALVRDkgvnsflvfmAYKDRCQCTDGQIY-EIFSL-IRDLGAVAQVHAENGDIVEEEQKRll 150
Cdd:PRK04250 114 ALNFLI----AGNCEKAEEIKAD----------FYKIFMGASTGGIFsENFEVdYACAPGIVSVHAEDPELIREFPER-- 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952364 151 eqgitgpeghvlshPEEVEAEAVYRAVTIAKQANCPLYVTKVMSKGAADMVAQAKRRGVVVFGEPitaslgtdgSH--YW 228
Cdd:PRK04250 178 --------------PPEAEVVAIERALEAGKKLKKPLHICHISTKDGLKLILKSNLPWVSFEVTP---------HHlfLT 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952364 229 SKNWAKAAAFVTSPPINpdptTADHLTSLLSSGD-LQVTGSAHCTFTTAQKAVGKdnftlipEGVNGIEERMSVVWEkCV 307
Cdd:PRK04250 235 RKDYERNPLLKVYPPLR----SEEDRKALWENFSkIPIIASDHAPHTLEDKEAGA-------AGIPGLETEVPLLLD-AA 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952364 308 ASGKMDENEFVAVTSTNAAKIFNFyPRKGrVAVGSDADLVIWNPRATKVISAKSHNLNVEYNIFEGVECRGVPTVVISQG 387
Cdd:PRK04250 303 NKGMISLFDIVEKMHDNPARIFGI-KNYG-IEEGNYANFAVFDMKKEWTIKAEELYTKAGWTPYEGFKLKGKVIMTILRG 380
|
410
....*....|...
gi 568952364 388 RVVLEDGNLLVTP 400
Cdd:PRK04250 381 EVVMEDDEIIGKP 393
|
|
| PRK09060 |
PRK09060 |
dihydroorotase; Validated |
2-404 |
1.61e-16 |
|
dihydroorotase; Validated
Pssm-ID: 181632 [Multi-domain] Cd Length: 444 Bit Score: 81.89 E-value: 1.61e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952364 2 VLPGGVDVHTRLQMPvmGMTPADDFCQGTKAALAGGTTMILDhvFPDAGVSLL--AAYEQWRERADSAACCDYSLHVDip 79
Cdd:PRK09060 54 VLPGVIDSQVHFREP--GLEHKEDLETGSRAAVLGGVTAVFE--MPNTNPLTTtaEALADKLARARHRMHCDFAFYVG-- 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952364 80 rwheSTKE---ELEALVRDKGVNSFLVFMA-------YKDrcqctDGQIYEIFSLIRdlgAVAQVHAEngdivEEEqkRL 149
Cdd:PRK09060 128 ----GTRDnadELAELERLPGCAGIKVFMGsstgdllVED-----DEGLRRILRNGR---RRAAFHSE-----DEY--RL 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952364 150 LEQGITGPEGHVLSHP----EEVEAEAVYRAVTIAKQANCPLYVTKVMSKGAADMVAQAKRRGVV--------VFGEPIT 217
Cdd:PRK09060 189 RERKGLRVEGDPSSHPvwrdEEAALLATRRLVRLARETGRRIHVLHVSTAEEIDFLADHKDVATVevtphhltLAAPECY 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952364 218 ASLGTdgshYWSKNwakaaafvtsPPINpDPTTADHLTSLLSSGDLQVTGSAHCTFTTAQKAvgkDNFTLIPEGVNGIEE 297
Cdd:PRK09060 269 ERLGT----LAQMN----------PPIR-DARHRDGLWRGVRQGVVDVLGSDHAPHTLEEKA---KPYPASPSGMTGVQT 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952364 298 RMSVVWEKcVASGKMDENEFVAVTSTNAAKIFNFyPRKGRVAVGSDADLVIWNPRATKVISAKSHNLNVEYNIFEGVECR 377
Cdd:PRK09060 331 LVPIMLDH-VNAGRLSLERFVDLTSAGPARIFGI-AGKGRIAVGYDADFTIVDLKRRETITNEWIASRCGWTPYDGKEVT 408
|
410 420
....*....|....*....|....*..
gi 568952364 378 GVPTVVISQGRVVLEDGNlLVTPGAGR 404
Cdd:PRK09060 409 GWPVGTIVRGQRVMWDGE-LVGPPTGE 434
|
|
| PRK07575 |
PRK07575 |
dihydroorotase; Provisional |
1-396 |
1.49e-13 |
|
dihydroorotase; Provisional
Pssm-ID: 236055 [Multi-domain] Cd Length: 438 Bit Score: 72.40 E-value: 1.49e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952364 1 MVLPGGVD--VHTRlqMPvmGMTPADDFCQGTKAALAGGTTMILDHVFPDAGVSLLAAYEQWRERADSAACCDYSLHVDi 78
Cdd:PRK07575 53 TLLPGVIDpqVHFR--EP--GLEHKEDLFTASRACAKGGVTSFLEMPNTKPLTTTQAALDDKLARAAEKCVVNYGFFIG- 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952364 79 prwheSTKEELEALVRDKGVNSFLVFM--AYKDRCQCTDGQIYEIFSLIRDLGAVaqvHAENGDIVEEEQKRLleQGITG 156
Cdd:PRK07575 128 -----ATPDNLPELLTANPTCGIKIFMgsSHGPLLVDEEAALERIFAEGTRLIAV---HAEDQARIRARRAEF--AGISD 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952364 157 PEGHVLSHPEEVEAEAVYRAVTIAKQANCPLYVTKVMSKGAADMVAQAKRRGVVVFGEPITASLGTDgshywskNWAKAA 236
Cdd:PRK07575 198 PADHSQIQDEEAALLATRLALKLSKKYQRRLHILHLSTAIEAELLRQDKPSWVTAEVTPQHLLLNTD-------AYERIG 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952364 237 AFVT-SPPINpDPTTADHLTSLLSSGDLQVTGSAHCTFTTAQKAVGKDNftlIPEGVNGIEERMSVVWEKCVAsGKMDEN 315
Cdd:PRK07575 271 TLAQmNPPLR-SPEDNEALWQALRDGVIDFIATDHAPHTLEEKAQPYPN---SPSGMPGVETSLPLMLTAAMR-GKCTVA 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952364 316 EFVAVTSTNAAKIFNFyPRKGRVAVGSDADLVIWNPRATKVISAKSHNLNVEYNIFEGVECRGVPTVVISQGRVVLEDGN 395
Cdd:PRK07575 346 QVVRWMSTAVARAYGI-PNKGRIAPGYDADLVLVDLNTYRPVRREELLTKCGWSPFEGWNLTGWPVTTIVGGQIVFDRGQ 424
|
.
gi 568952364 396 L 396
Cdd:PRK07575 425 V 425
|
|
| CAD_DHOase |
cd01316 |
The eukaryotic CAD protein is a trifunctional enzyme of carbamoylphosphate ... |
3-403 |
2.36e-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: 59.00 E-value: 2.36e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952364 3 LPGGVDVHTRLQMPvmGMTPADDFCQGTKAALAGGTTMILdhVFPDAGVSLL--AAYEQWRERADSAACCDYSLHVDIPR 80
Cdd:cd01316 5 LPGLIDVHVHLREP--GATHKEDFASGTKAALAGGFTMVR--AMPNTNPSIVdvASLKLVQSLAQAKARCDYAFSIGATS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952364 81 WHESTKEELEalvrDKGVNSFLvfmaykdrcqctdgqiyeifslirdlgavaqvhaengdIVEEEQKRLLEQGITGPEGH 160
Cdd:cd01316 81 TNAATVGELA----SEAVGLKF--------------------------------------YLNETFSTLILDKITAWASH 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952364 161 VLSHPEE----VEAEAVYRAVTI--AKQANCPLYVTKVMSKGAADMVAQAKRRGVVVFGEPITASLgtdgshYWSKNWAK 234
Cdd:cd01316 119 FNAWPSTkpivTHAKSQTLAAVLllASLHNRSIHICHVSSKEEINLIRLAKARGLKVTCEVSPHHL------FLSQDDLP 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952364 235 AAAFvtspPINPDPTTADHLTSL---LSSGDLQVTGSAhcTFTTAQKAVGKdnftlIPEGVNGIEERMSVVWeKCVASGK 311
Cdd:cd01316 193 RGQY----EVRPFLPTREDQEALwenLDYIDCFATDHA--PHTLAEKTGNK-----PPPGFPGVETSLPLLL-TAVHEGR 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952364 312 MDENEFVAVTSTNAAKIFNFYPRKGrVAVGSDADlVIWNPRATKVISAKShnlnveYNIFEGVECRGVPTVVISQGRVVL 391
Cdd:cd01316 261 LTIEDIVDRLHTNPKRIFNLPPQSD-TYVEVDLD-EEWTIPKNPLQSKKG------WTPFEGKKVKGKVQRVVLRGETAF 332
|
410
....*....|..
gi 568952364 392 EDGNLLVTPGAG 403
Cdd:cd01316 333 IDGEIVAPPGFG 344
|
|
| pyrC |
PRK00369 |
dihydroorotase; Provisional |
1-403 |
1.02e-07 |
|
dihydroorotase; Provisional
Pssm-ID: 234738 [Multi-domain] Cd Length: 392 Bit Score: 54.00 E-value: 1.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952364 1 MVLPGGVDVHTRLQMpvMGMTPADDFCQGTKAALAGGTTMILDhvFPDAgVSLLAAYEQWRERADSAAC---CDYSLHVD 77
Cdd:PRK00369 44 LILPGAIDLHVHLRG--LKLSYKEDVASGTSEAAYGGVTLVAD--MPNT-IPPLNTPEAITEKLAELEYysrVDYFVYSG 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952364 78 IPRwhesTKEELEALvrdkGVNSFLVFMAykdrcqctdgqiyeifslirdlgavaqvhaengDIVEEEQKRLLEqgitgp 157
Cdd:PRK00369 119 VTK----DPEKVDKL----PIAGYKIFPE---------------------------------DLEREETFRVLL------ 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952364 158 EGHVLS--HPEEVEAEAVYRAVtiakQANCPLYVTKVMS-KGAADM----------VAQAKRRGvvvFGEPITAS-LGTD 223
Cdd:PRK00369 152 KSRKLKilHPEVPLALKSNRKL----RRNCWYEIAALYYvKDYQNVhithasnprtVRLAKELG---FTVDITPHhLLVN 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952364 224 G-SHYWSKnwakaaafvTSPPINpDPTTADHLTSLLSSGDLQVtgSAHCTFTTAQKavgKDNFTLIPEGVNGIEERMSVV 302
Cdd:PRK00369 225 GeKDCLTK---------VNPPIR-DINERLWLLQALSEVDAIA--SDHAPHSSFEK---LQPYEVCPPGIAALSFTPPFI 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952364 303 WeKCVASGKMDENEFVAVTSTNAAKIFNFypRKGRVAVGSDADLVIWNPRATKVISAKShnlNVEYNIFEGVECRGVPTV 382
Cdd:PRK00369 290 Y-TLVSKGILSIDRAVELISTNPARILGI--PYGEIKEGYRANFTVIQFEDWRYSTKYS---KVIETPLDGFELKASVYA 363
|
410 420
....*....|....*....|.
gi 568952364 383 VISQGRVVLEDGNllVTPGAG 403
Cdd:PRK00369 364 TIVQGKLAYLEGE--VFPVKG 382
|
|
| Amidohydro_3 |
pfam07969 |
Amidohydrolase family; |
1-374 |
1.14e-07 |
|
Amidohydrolase family;
Pssm-ID: 400360 [Multi-domain] Cd Length: 464 Bit Score: 54.07 E-value: 1.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952364 1 MVLPGGVDVHT---RLQMPVMGMTPADDFCQGTKAALAG------------------------GTTMILDHVFPDAGVSL 53
Cdd:pfam07969 9 LVLPGFVDPHThldGGGLNLRELRLPDVLPNAVVKGQAGrtpkgrwlvgegwdeaqfaetrfpYALADLDEVAPDGPVLL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952364 54 LAA--YEQWRERA--DSAaccDYSLHVDIPR----WHESTKEELEALVRDK---------------GVNSFLVFMAyKDR 110
Cdd:pfam07969 89 RALhtHAAVANSAalDLA---GITKATEDPPggeiARDANGEGLTGLLREGayalppllareaeaaAVAAALAALP-GFG 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952364 111 CQCTDGQIYEIFSLIrDLGAVAQVHAENGDIveEEQKRLLEQGITGPEGHV-------------------LSHP------ 165
Cdd:pfam07969 165 ITSVDGGGGNVHSLD-DYEPLRELTAAEKLK--ELLDAPERLGLPHSIYELrigamklfadgvlgsrtaaLTEPyfdapg 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952364 166 ---EEVEAEAVYRAVTIAKQANCPLYV-----TKVMSK-GAADMVAQAK-RRGVVVFG-------------EPITASLGT 222
Cdd:pfam07969 242 tgwPDFEDEALAELVAAARERGLDVAIhaigdATIDTAlDAFEAVAEKLgNQGRVRIEhaqgvvpytysqiERVAALGGA 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952364 223 DGSHYWSknWAKAAAFVTSPPINPDPTTADHLTSLLSSGDLQVTGS-AHCTFTTAQKAVGkDNFTLIPEG---VNGIEER 298
Cdd:pfam07969 322 AGVQPVF--DPLWGDWLQDRLGAERARGLTPVKELLNAGVKVALGSdAPVGPFDPWPRIG-AAVMRQTAGggeVLGPDEE 398
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568952364 299 MSVvwekcvasgkmdeNEFVAVTSTNAAKIFNFYPRKGRVAVGSDADLVIWNPRATKVISAKSHNLNVEYNIFEGV 374
Cdd:pfam07969 399 LSL-------------EEALALYTSGPAKALGLEDRKGTLGVGKDADLVVLDDDPLTVDPPAIADIRVRLTVVDGR 461
|
|
| PRK07369 |
PRK07369 |
dihydroorotase; Provisional |
165-361 |
8.35e-06 |
|
dihydroorotase; Provisional
Pssm-ID: 236002 [Multi-domain] Cd Length: 418 Bit Score: 48.06 E-value: 8.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952364 165 PEEVEAEAVYRAVTIAKQANCPLYVTKVMSKGAADMVAQAKRRGVvvfgePITAS-------LGT-DGSHYwSKNWAKAa 236
Cdd:PRK07369 208 PASAETTALAALLELVAAIGTPVHLMRISTARSVELIAQAKARGL-----PITASttwmhllLDTeALASY-DPNLRLD- 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952364 237 afvtsPPI-NPDPTTAdhLTSLLSSGDLQVTGSAHCTFTTAQKAVGkdnFTLIPEGVNGIEERMSVVWEKCVASGKMDEN 315
Cdd:PRK07369 281 -----PPLgNPSDRQA--LIEGVRTGVIDAIAIDHAPYTYEEKTVA---FAEAPPGAIGLELALPLLWQNLVETGELSAL 350
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 568952364 316 EFVAVTSTNAAKIFNFYPRkgRVAVGSDADLVIWNPRATKVISAKS 361
Cdd:PRK07369 351 QLWQALSTNPARCLGQEPP--SLAPGQPAELILFDPQKTWTVSAQT 394
|
|
| NagA |
cd00854 |
N-acetylglucosamine-6-phosphate deacetylase, NagA, catalyzes the hydrolysis of the N-acetyl ... |
318-373 |
2.28e-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: 43.34 E-value: 2.28e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 568952364 318 VAVTSTNAAKIFNFYPRKGRVAVGSDADLVIWNPratkvisakshNLNVEYNIFEG 373
Cdd:cd00854 330 VRMASLNPAKLLGLDDRKGSLKPGKDADLVVLDD-----------DLNVKATWING 374
|
|
| Met_dep_hydrolase_C |
cd01309 |
Metallo-dependent hydrolases, subgroup C is part of the superfamily of metallo-dependent ... |
305-350 |
9.79e-04 |
|
Metallo-dependent hydrolases, subgroup C is part of the superfamily of metallo-dependent hydrolases, a large group of proteins that show conservation in their 3-dimensional fold (TIM barrel) and in details of their active site. The vast majority of the members have a conserved metal binding site, involving four histidines and one aspartic acid residue. In the common reaction mechanism, the metal ion (or ions) deprotonate a water molecule for a nucleophilic attack on the substrate. The function of this subgroup is unknown.
Pssm-ID: 238634 [Multi-domain] Cd Length: 359 Bit Score: 41.53 E-value: 9.79e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 568952364 305 KCVASGKMDENEFVAVTStNAAKIFNFYPRKGRVAVGSDADLVIWN 350
Cdd:cd01309 294 KAVKYGLSYEEALKAITI-NPAKILGIEDRVGSLEPGKDADLVVWN 338
|
|
| SsnA |
COG0402 |
Cytosine/adenosine deaminase or related metal-dependent hydrolase [Nucleotide transport and ... |
2-225 |
1.06e-03 |
|
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: 41.35 E-value: 1.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952364 2 VLPGGVDVHTRL-QMPVMGMTPADDFCQ--------------------GTKAA----LAGGTTMILDH--VFPDAGVSLL 54
Cdd:COG0402 57 VLPGLVNTHTHLpQTLLRGLADDLPLLDwleeyiwplearldpedvyaGALLAlaemLRSGTTTVADFyyVHPESADALA 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952364 55 AAYEQWRERADSA-ACCDYSLHVDIPRWHESTKEELEALVRDkgvnsflVFMAYKDRCQ----------CTDGQIYEIFS 123
Cdd:COG0402 137 EAAAEAGIRAVLGrGLMDRGFPDGLREDADEGLADSERLIER-------WHGAADGRIRvalaphapytVSPELLRAAAA 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952364 124 LIRDLGAVAQVH-----AENGDIVEEEQKR----LLEQGITGPeGHVLSH-----PEEVE--AEavyRAVTIakqANCP- 186
Cdd:COG0402 210 LARELGLPLHTHlaetrDEVEWVLELYGKRpveyLDELGLLGP-RTLLAHcvhltDEEIAllAE---TGASV---AHCPt 282
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 568952364 187 --LYvtkvMSKGAADmVAQAKRRGVVVfgepitaSLGTDGS 225
Cdd:COG0402 283 snLK----LGSGIAP-VPRLLAAGVRV-------GLGTDGA 311
|
|
| Met_dep_hydrolase_B |
cd01307 |
Metallo-dependent hydrolases, subgroup B is part of the superfamily of metallo-dependent ... |
267-363 |
3.64e-03 |
|
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: 39.62 E-value: 3.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952364 267 GSAHCTFTTAQKAVGKDnftLIPE----------GVNGIEERMSVVWEKCVASGkMDENEFVAVTSTNAAKIFNFyPRKG 336
Cdd:cd01307 226 GTASFSFRVARAAIAAG---LLPDtissdihgrnRTNGPVYALATTLSKLLALG-MPLEEVIEAVTANPARMLGL-AEIG 300
|
90 100
....*....|....*....|....*..
gi 568952364 337 RVAVGSDADLVIWNPRATKVISAKSHN 363
Cdd:cd01307 301 TLAVGYDADLTVFDLKDGRVELVDSEG 327
|
|
| PRK09061 |
PRK09061 |
D-glutamate deacylase; Validated |
333-408 |
8.30e-03 |
|
D-glutamate deacylase; Validated
Pssm-ID: 236369 [Multi-domain] Cd Length: 509 Bit Score: 38.91 E-value: 8.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568952364 333 PRKGRVAVGSDADLVIWNP-----RATKVISAK-SHnlnveynifegvecrGVPTVVISqGRVVLEDGNLLVTPGAGRFI 406
Cdd:PRK09061 441 RRKGRLQAGADADIVVFDPetitdRATFEDPNRpSE---------------GVRHVLVN-GVPVVSNGELVRDARPGRPV 504
|
..
gi 568952364 407 PR 408
Cdd:PRK09061 505 RR 506
|
|
| HutI |
COG1228 |
Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport ... |
319-374 |
8.46e-03 |
|
Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440841 [Multi-domain] Cd Length: 386 Bit Score: 38.40 E-value: 8.46e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 568952364 319 AVTStNAAKIFNFYPRKGRVAVGSDADLVIWNPRATKVISAkshNLNVEYNIFEGV 374
Cdd:COG1228 330 AATI-NAAKALGLDDDVGSLEPGKLADLVLLDGDPLEDIAY---LEDVRAVMKDGR 381
|
|
| Imidazolone-5PH |
cd01296 |
Imidazolonepropionase/imidazolone-5-propionate hydrolase (Imidazolone-5PH) catalyzes the third ... |
311-350 |
9.75e-03 |
|
Imidazolonepropionase/imidazolone-5-propionate hydrolase (Imidazolone-5PH) catalyzes the third step in the histidine degradation pathway, the hydrolysis of (S)-3-(5-oxo-4,5-dihydro-3H-imidazol-4-yl)propanoate to N-formimidoyl-L-glutamate. In bacteria, the enzyme is part of histidine utilization (hut) operon.
Pssm-ID: 238621 [Multi-domain] Cd Length: 371 Bit Score: 38.39 E-value: 9.75e-03
10 20 30 40
....*....|....*....|....*....|....*....|
gi 568952364 311 KMDENEFVAVTSTNAAKIFNFYPRKGRVAVGSDADLVIWN 350
Cdd:cd01296 309 RMTPEEALTAATINAAAALGLGETVGSLEVGKQADLVILD 348
|
|
| |
