|
Name |
Accession |
Description |
Interval |
E-value |
| AllB |
COG0044 |
Dihydroorotase or related cyclic amidohydrolase [Nucleotide transport and metabolism]; ... |
11-429 |
1.06e-156 |
|
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: 449.93 E-value: 1.06e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443493860 11 ITGGTLFDGTGKEIENpgLLIRGGEIAAIGEAAIPAEAAQTLDASGCVISPGFIDLSCNLREPGNGQKGNIASETRAAAH 90
Cdd:COG0044 2 IKNGRVVDPGGLERAD--VLIEDGRIAAIGPDLAAPEAAEVIDATGLLVLPGLIDLHVHLREPGLEHKEDIETGTRAAAA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443493860 91 GGFTTVCASPETSPVNDSSAVTHLIREGADSRGSVRVLPVGAITRGLdGEMLSDMAGLKNAGCVAV-----GNGSRGVRN 165
Cdd:COG0044 80 GGVTTVVDMPNTNPVTDTPEALEFKLARAEEKALVDVGPHGALTKGL-GENLAELGALAEAGAVAFkvfmgSDDGNPVLD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443493860 166 ARILRRCMAYAQTFGLTVMFSPENQALAADGYSHDGQVATRLGLLGIPEVAETAAVMEMLLLAEETGVKLHLSQLSSGRS 245
Cdd:COG0044 159 DGLLRRALEYAAEFGALVAVHAEDPDLIRGGVMNEGKTSPRLGLKGRPAEAEEEAVARDIALAEETGARLHIVHVSTAEA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443493860 246 VQMLADARKRGIQVTADVAMHQLCFTEEALAGFDSRFHVRPPLRSEADRQALVAGVRDGVIDAIVSQHQPHDSAAKQAPL 325
Cdd:COG0044 239 VELIREAKARGLPVTAEVCPHHLTLTDEDLERYGTNFKVNPPLRTEEDREALWEGLADGTIDVIATDHAPHTLEEKELPF 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443493860 326 PATEPGLSSIESVLSLGL-ELVARGELERARLLSALTAGPASVLG--RNARLAEGEAADLCVFAPEQSWQPSVQTLVSAG 402
Cdd:COG0044 319 AEAPNGIPGLETALPLLLtELVHKGRLSLERLVELLSTNPARIFGlpRKGRIAVGADADLVLFDPDAEWTVTAEDLHSKS 398
|
410 420
....*....|....*....|....*..
gi 2443493860 403 RHAPVLDRELPGRVRLTLVAGRTAWAD 429
Cdd:COG0044 399 KNTPFEGRELTGRVVATIVRGRVVYED 425
|
|
| pyrC |
PRK09357 |
dihydroorotase; Validated |
11-429 |
3.07e-154 |
|
dihydroorotase; Validated
Pssm-ID: 236479 [Multi-domain] Cd Length: 423 Bit Score: 443.10 E-value: 3.07e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443493860 11 ITGGTLFDGTGKEiENPGLLIRGGEIAAIGeAAIPAEAAQTLDASGCVISPGFIDLSCNLREPGNGQKGNIASETRAAAH 90
Cdd:PRK09357 5 IKNGRVIDPKGLD-EVADVLIDDGKIAAIG-ENIEAEGAEVIDATGLVVAPGLVDLHVHLREPGQEDKETIETGSRAAAA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443493860 91 GGFTTVCASPETSPVNDSSAVTHLIREGADSRGSVRVLPVGAITRGLDGEMLSDMAGLKNAGCVAVGNGSRGVRNARILR 170
Cdd:PRK09357 83 GGFTTVVAMPNTKPVIDTPEVVEYVLDRAKEAGLVDVLPVGAITKGLAGEELTEFGALKEAGVVAFSDDGIPVQDARLMR 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443493860 171 RCMAYAQTFGLTVMFSPENQALAADGYSHDGQVATRLGLLGIPEVAETAAVMEMLLLAEETGVKLHLSQLSSGRSVQMLA 250
Cdd:PRK09357 163 RALEYAKALDLLIAQHCEDPSLTEGGVMNEGEVSARLGLPGIPAVAEEVMIARDVLLAEATGARVHICHVSTAGSVELIR 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443493860 251 DARKRGIQVTADVAMHQLCFTEEALAGFDSRFHVRPPLRSEADRQALVAGVRDGVIDAIVSQHQPHDSAAKQAPLPATEP 330
Cdd:PRK09357 243 WAKALGIKVTAEVTPHHLLLTDEDLLTYDPNYKVNPPLRTEEDREALIEGLKDGTIDAIATDHAPHAREEKECEFEAAPF 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443493860 331 GLSSIESVLSLGL-ELVARGELERARLLSALTAGPASVLGRNAR-LAEGEAADLCVFAPEQSWQPSVQTLVSAGRHAPVL 408
Cdd:PRK09357 323 GITGLETALSLLYtTLVKTGLLDLEQLLEKMTINPARILGLPAGpLAEGEPADLVIFDPEAEWTVDGEDFASKGKNTPFI 402
|
410 420
....*....|....*....|.
gi 2443493860 409 DRELPGRVRLTLVAGRTAWAD 429
Cdd:PRK09357 403 GMKLKGKVVYTIVDGKIVYQD 423
|
|
| DHOase_IIa |
cd01317 |
Dihydroorotase (DHOase), subgroup IIa; DHOases catalyze the reversible interconversion of ... |
48-419 |
9.45e-142 |
|
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: 409.32 E-value: 9.45e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443493860 48 AAQTLDASGCVISPGFIDLSCNLREPGNGQKGNIASETRAAAHGGFTTVCASPETSPVNDSSAVTHLIREGADSRGSVRV 127
Cdd:cd01317 1 DAEVIDAEGKILAPGLVDLHVHLREPGFEYKETLESGAKAAAAGGFTTVVCMPNTNPVIDNPAVVELLKNRAKDVGIVRV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443493860 128 LPVGAITRGLDGEMLSDMAGLKNAGCVAVGNGSRGVRNARILRRCMAYAQTFGLTVMFSPENQALAADGYSHDGQVATRL 207
Cdd:cd01317 81 LPIGALTKGLKGEELTEIGELLEAGAVGFSDDGKPIQDAELLRRALEYAAMLDLPIIVHPEDPSLAGGGVMNEGKVASRL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443493860 208 GLLGIPEVAETAAVMEMLLLAEETGVKLHLSQLSSGRSVQMLADARKRGIQVTADVAMHQLCFTEEALAGFDSRFHVRPP 287
Cdd:cd01317 161 GLPGIPPEAETIMVARDLELAEATGARVHFQHLSTARSLELIRKAKAKGLPVTAEVTPHHLLLDDEALESYDTNAKVNPP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443493860 288 LRSEADRQALVAGVRDGVIDAIVSQHQPHDSAAKQAPLPATEPGLSSIESVLSLGL-ELVARGELERARLLSALTAGPAS 366
Cdd:cd01317 241 LRSEEDREALIEALKDGTIDAIASDHAPHTDEEKDLPFAEAPPGIIGLETALPLLWtLLVKGGLLTLPDLIRALSTNPAK 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 2443493860 367 VLGRNA-RLAEGEAADLCVFAPEQSWQPSVQTLVSAGRHAPVLDRELPGRVRLT 419
Cdd:cd01317 321 ILGLPPgRLEVGAPADLVLFDPDAEWIVDEETFRSKSKNTPFDGQKLKGRVLAT 374
|
|
| PRK07627 |
PRK07627 |
dihydroorotase; Provisional |
9-430 |
1.74e-129 |
|
dihydroorotase; Provisional
Pssm-ID: 181059 [Multi-domain] Cd Length: 425 Bit Score: 380.18 E-value: 1.74e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443493860 9 LKITGGTLFDGTGKEIENPGLLIRGGEIAAIGEAAIPAEAAQTLDASGCVISPGFIDLSCNLREPGNGQKGNIASETRAA 88
Cdd:PRK07627 3 IHIKGGRLIDPAAGTDRQADLYVAAGKIAAIGQAPAGFNADKTIDASGLIVCPGLVDLSARLREPGYEYKATLESEMAAA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443493860 89 AHGGFTTVCASPETSPVNDSSAVTHLIREGADSRGSVRVLPVGAITRGLDGEMLSDMAGLKNAGCVAVGNGSRGVRNARI 168
Cdd:PRK07627 83 VAGGVTSLVCPPDTDPVLDEPGLVEMLKFRARNLNQAHVYPLGALTVGLKGEVLTEMVELTEAGCVGFSQANVPVVDTQV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443493860 169 LRRCMAYAQTFGLTVMFSPENQALAADGYSHDGQVATRLGLLGIPEVAETAAVMEMLLLAEETGVKLHLSQLSSGRSVQM 248
Cdd:PRK07627 163 LLRALQYASTFGFTVWLRPLDAFLGRGGVAASGAVASRLGLSGVPVAAETIALHTIFELMRVTGARVHLARLSSAAGVAL 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443493860 249 LADARKRGIQVTADVAMHQLCFTEEALAGFDSRFHVRPPLRSEADRQALVAGVRDGVIDAIVSQHQPHDSAAKQAPLPAT 328
Cdd:PRK07627 243 VRAAKAEGLPVTCDVGVNHVHLIDVDIGYFDSQFRLDPPLRSQRDREAIRAALADGTIDAICSDHTPVDDDEKLLPFAEA 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443493860 329 EPGLSSIESVLSLGLELVARGELERARLLSALTAGPASVLGRNA-RLAEGEAADLCVFAPEQSWQPSVQTLVSAGRHAPV 407
Cdd:PRK07627 323 TPGATGLELLLPLTLKWADEAKVPLARALARITSAPARVLGLPAgRLAEGAPADLCVFDPDAHWRVEPRALKSQGKNTPF 402
|
410 420
....*....|....*....|...
gi 2443493860 408 LDRELPGRVRLTLVAGRTAWADP 430
Cdd:PRK07627 403 LGYELPGRVRATLVAGQVAFERR 425
|
|
| pyrC_multi |
TIGR00857 |
dihydroorotase, multifunctional complex type; In contrast to the homodimeric type of ... |
21-429 |
1.27e-97 |
|
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: 298.20 E-value: 1.27e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443493860 21 GKEIENpGLLIRGGEIAAIGEAAIPAEAAqTLDASGCVISPGFIDLSCNLREPGNGQKGNIASETRAAAHGGFTTVCASP 100
Cdd:TIGR00857 1 GKETEV-DILVEGGRIKKIGKLRIPPDAE-VIDAKGLLVLPGFIDLHVHLRDPGEEYKEDIESGSKAAAHGGFTTVADMP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443493860 101 ETSPVNDSSAVTHLIREGADSRGSVRVLPVGAITRGLDGEMLSDMAGLKNAGCVA---VGNGSRgVRNARILRRCMAYAQ 177
Cdd:TIGR00857 79 NTKPPIDTPETLEWKLQRLKKVSLVDVHLYGGVTQGNQGKELTEAYELKEAGAVGrmfTDDGSE-VQDILSMRRALEYAA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443493860 178 TFGLTVMFSPENQALAADGYSHDGQVATRLGLLGIPEVAETAAVMEMLLLAEETGVKLHLSQLSSGRSVQMLADARKRGI 257
Cdd:TIGR00857 158 IAGVPIALHAEDPDLIYGGVMHEGPSAAQLGLPARPPEAEEVAVARLLELAKHAGCPVHICHISTKESLELIVKAKSQGI 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443493860 258 QVTADVAMHQLCFTEEALAGFDSRFHVRPPLRSEADRQALVAGVRDGVIDAIVSQHQPHDSAAKQAPLPATEPGLSSIES 337
Cdd:TIGR00857 238 KITAEVTPHHLLLSEEDVARLDGNGKVNPPLREKEDRLALIEGLKDGIIDIIATDHAPHTLEEKTKEFAAAPPGIPGLET 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443493860 338 VLSLGLELVARGELERARLLSALTAGPASVLGRN--ARLAEGEAADLCVFAPEQSWQPSVQTLVSAGRHAPVLDRELPGR 415
Cdd:TIGR00857 318 ALPLLLQLLVKGLISLKDLIRMLSINPARIFGLPdkGTLEEGNPADITVFDLKKEWTINAETFYSKAKNTPFEGMSLKGK 397
|
410
....*....|....
gi 2443493860 416 VRLTLVAGRTAWAD 429
Cdd:TIGR00857 398 PIATILRGKVVYED 411
|
|
| PRK09059 |
PRK09059 |
dihydroorotase; Validated |
17-425 |
4.28e-92 |
|
dihydroorotase; Validated
Pssm-ID: 181631 [Multi-domain] Cd Length: 429 Bit Score: 284.62 E-value: 4.28e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443493860 17 FDGTGKEIENPGLLIRGGeiAAIGEAAIPaEAAQTLDASGCVISPGFIDLSCNLREPGNGQKGNIASETRAAAHGGFTTV 96
Cdd:PRK09059 19 LDEIGTVLIEDGVIVAAG--KGAGNQGAP-EGAEIVDCAGKAVAPGLVDARVFVGEPGAEHRETIASASRAAAAGGVTSI 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443493860 97 CASPETSPVNDSSAVTHLIREGADSRGSVRVLPVGAITRGLDGEMLSDMAGLKNAGCVAVGNGSRGVRNARILRRCMAYA 176
Cdd:PRK09059 96 IMMPDTDPVIDDVALVEFVKRTARDTAIVNIHPAAAITKGLAGEEMTEFGLLRAAGAVAFTDGRRSVANTQVMRRALTYA 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443493860 177 QTFGLTVMFSPENQALAADGYSHDGQVATRLGLLGIPEVAETAAVMEMLLLAEETGVKLHLSQLSSGRSVQMLADARKRG 256
Cdd:PRK09059 176 RDFDAVIVHETRDPDLGGNGVMNEGLFASWLGLSGIPREAEVIPLERDLRLAALTRGRYHAAQISCAESAEALRRAKDRG 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443493860 257 IQVTADVAMHQLCFTEEALAGFDSRFHVRPPLRSEADRQALVAGVRDGVIDAIVSQHQPHDSAAKQAPLPATEPGLSSIE 336
Cdd:PRK09059 256 LKVTAGVSINHLSLNENDIGEYRTFFKLSPPLRTEDDRVAMVEAVASGTIDIIVSSHDPQDVDTKRLPFSEAAAGAIGLE 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443493860 337 SVLSLGLELVARGELERARLLSALTAGPASVLGRNA-RLAEGEAADLCVFAPEQSWQPSVQTLVSAGRHAPVLDRELPGR 415
Cdd:PRK09059 336 TLLAAALRLYHNGEVPLLRLIEALSTRPAEIFGLPAgTLKPGAPADIIVIDLDEPWVVDPEDLKSRSKNTPFEEARFQGR 415
|
410
....*....|
gi 2443493860 416 VRLTLVAGRT 425
Cdd:PRK09059 416 VVRTIVAGKT 425
|
|
| PRK07369 |
PRK07369 |
dihydroorotase; Provisional |
30-416 |
9.59e-88 |
|
dihydroorotase; Provisional
Pssm-ID: 236002 [Multi-domain] Cd Length: 418 Bit Score: 273.02 E-value: 9.59e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443493860 30 LIRGGEIAAIGE--AAIPAEAaQTLDASGCVISPGFIDLSCNLREPGNGQKGNIASETRAAAHGGFTTVCASPETSPVND 107
Cdd:PRK07369 25 LIEDGKIQAIEPhiDPIPPDT-QIIDASGLILGPGLVDLYSHSGEPGFEERETLASLAAAAAAGGFTRVAILPDTFPPLD 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443493860 108 SSAVTHLIREGADSRGSVRVLPVGAITRGLDGEMLSDMAGLKNAGCVAVGNGsRGVRNARILRRCMAYAQTFGLTVMFSP 187
Cdd:PRK07369 104 NPATLARLQQQAQQIPPVQLHFWGALTLGGQGKQLTELAELAAAGVVGFTDG-QPLENLALLRRLLEYLKPLGKPVALWP 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443493860 188 ENQALAADGYSHDGQVATRLGLLGIPEVAETAAVMEMLLLAEETGVKLHLSQLSSGRSVQMLADARKRGIQVTADVAMHQ 267
Cdd:PRK07369 183 CDRSLAGNGVMREGLLALRLGLPGDPASAETTALAALLELVAAIGTPVHLMRISTARSVELIAQAKARGLPITASTTWMH 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443493860 268 LCFTEEALAGFDSRFHVRPPLRSEADRQALVAGVRDGVIDAIVSQHQPHDSAAKQAPLPATEPGLSSIESVLS-LGLELV 346
Cdd:PRK07369 263 LLLDTEALASYDPNLRLDPPLGNPSDRQALIEGVRTGVIDAIAIDHAPYTYEEKTVAFAEAPPGAIGLELALPlLWQNLV 342
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2443493860 347 ARGELERARLLSALTAGPASVLGRN-ARLAEGEAADLCVFAPEQSWQPSVQTLVSAGRHAPVLDRELPGRV 416
Cdd:PRK07369 343 ETGELSALQLWQALSTNPARCLGQEpPSLAPGQPAELILFDPQKTWTVSAQTLHSLSRNTPWLGQTLKGRV 413
|
|
| L-HYD_ALN |
cd01315 |
L-Hydantoinases (L-HYDs) and Allantoinase (ALN); L-Hydantoinases are a member of the ... |
11-429 |
9.25e-55 |
|
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: 187.88 E-value: 9.25e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443493860 11 ITGGTLFdgTGKEIENPGLLIRGGEIAAIGEAAIPAEAAQTLDASGCVISPGFIDLSCNLREPGNGQKGNIASETRAAAH 90
Cdd:cd01315 4 IKNGRVV--TPDGVREADIAVKGGKIAAIGPDIANTEAEEVIDAGGLVVMPGLIDTHVHINEPGRTEWEGFETGTKAAAA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443493860 91 GGFTTVCASPETSPVNDSSAVTHLIR-EGADSRGSVRVLPVGAITRGLdgemLSDMAGLKNAGCVA-------VGNGSRG 162
Cdd:cd01315 82 GGITTIIDMPLNSIPPTTTVENLEAKlEAAQGKLHVDVGFWGGLVPGN----LDQLRPLDEAGVVGfkcflcpSGVDEFP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443493860 163 VRNARILRRCMAYAQTFGLTVMFSPEN---------QALAADGYSHDGQVATRlgllgiPEVAETAAVMEMLLLAEETGV 233
Cdd:cd01315 158 AVDDEQLEEAMKELAKTGSVLAVHAENpeitealqeQAKAKGKRDYRDYLASR------PVFTEVEAIQRILLLAKETGC 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443493860 234 KLHLSQLSSGRSVQMLADARKRGIQVTADVAMHQLCFTEEALAGFDSRFHVRPPLRSEADRQALVAGVRDGVIDAIVSQH 313
Cdd:cd01315 232 RLHIVHLSSAEAVPLIREARAEGVDVTVETCPHYLTFTAEDVPDGGTEFKCAPPIRDAANQEQLWEALENGDIDMVVSDH 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443493860 314 QPHDSAAKqapLPATE------PGLSSIESVLSLGLEL-VARGELERARLLSALTAGPASVLG---RNARLAEGEAADLC 383
Cdd:cd01315 312 SPCTPELK---LLGKGdffkawGGISGLQLGLPVMLTEaVNKRGLSLEDIARLMCENPAKLFGlshQKGRIAVGYDADFV 388
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 2443493860 384 VFAPEQSWQPSVQTLVSAGRHAPVLDRELPGRVRLTLVAGRTAWAD 429
Cdd:cd01315 389 VWDPEEEFTVDAEDLYYKNKISPYVGRTLKGRVHATILRGTVVYQD 434
|
|
| DHOase_IIb |
cd01318 |
Dihydroorotase (DHOase), subgroup IIb; DHOases catalyze the reversible interconversion of ... |
56-423 |
5.20e-54 |
|
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: 183.69 E-value: 5.20e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443493860 56 GCVISPGFIDLSCNLREPGNGQKGNIASETRAAAHGGFTTVCASPETSP-VNDSSAVTHLIREgADSRGSVRVLPVGAIT 134
Cdd:cd01318 1 GLLILPGVIDIHVHFREPGLTYKEDFVSGSRAAAAGGVTTVMDMPNTKPpTTTAEALYEKLRL-AAAKSVVDYGLYFGVT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443493860 135 RGLDGEMLSDM--AGLKnagcVAVGN--GSRGVRNARILRrcmAYAQTFGLTVmFSPENQAL---AADGYSHDGQVATRL 207
Cdd:cd01318 80 GSEDLEELDKAppAGYK----IFMGDstGDLLDDEETLER---IFAEGSVLVT-FHAEDEDRlreNRKELKGESAHPRIR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443493860 208 gllgiPEVAETAAVMEMLLLAEETGVKLHLSQLSSGRSVQMLADARKRgiqVTADVAMHQLCFTEEALAGFDSRFHVRPP 287
Cdd:cd01318 152 -----DAEAAAVATARALKLARRHGARLHICHVSTPEELKLIKKAKPG---VTVEVTPHHLFLDVEDYDRLGTLGKVNPP 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443493860 288 LRSEADRQALVAGVRDGVIDAIVSQHQPHDSAAKQAPLPATEPGLSSIESVLSLGLELVARGELERARLLSALTAGPASV 367
Cdd:cd01318 224 LRSREDRKALLQALADGRIDVIASDHAPHTLEEKRKGYPAAPSGIPGVETALPLMLTLVNKGILSLSRVVRLTSHNPARI 303
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 2443493860 368 LGRN--ARLAEGEAADLCVFAPEQSWQPSVQTLVSAGRHAPVLDRELPGRVRLTLVAG 423
Cdd:cd01318 304 FGIKnkGRIAEGYDADLTVVDLKEERTIRAEEFHSKAGWTPFEGFEVTGFPVMTIVRG 361
|
|
| PRK08417 |
PRK08417 |
metal-dependent hydrolase; |
29-425 |
7.69e-54 |
|
metal-dependent hydrolase;
Pssm-ID: 236262 [Multi-domain] Cd Length: 386 Bit Score: 184.14 E-value: 7.69e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443493860 29 LLIRGGEIAAIGeAAIPAEaaQTLDASGCVISPGFIDLscNLREPGNGQKG-NIASETRAAAHGGFTTVCASPETSPVND 107
Cdd:PRK08417 1 IRIKDGKITEIG-SDLKGE--EILDAKGKTLLPALVDL--NVSLKNDSLSSkNLKSLENECLKGGVGSIVLYPDSTPAID 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443493860 108 SSAVTHLIREGaDSRGSVRVLPVGAITRglDGEMLSDMAGLKNAGCVAVGNGSrgVRNARILRRCMAYAQTFGLTVMFSP 187
Cdd:PRK08417 76 NEIALELINSA-QRELPMQIFPSIRALD--EDGKLSNIATLLKKGAKALELSS--DLDANLLKVIAQYAKMLDVPIFCRC 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443493860 188 ENQALAADGYSHDGQVATRLGLLGIPEVAETAAVMEMLLLAEETGVKLHLSQLSSGRSVQMLADARKRGIQVTADVAMHQ 267
Cdd:PRK08417 151 EDSSFDDSGVMNDGELSFELGLPGIPSIAETKEVAKMKELAKFYKNKVLFDTLALPRSLELLDKFKSEGEKLLKEVSIHH 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443493860 268 LCFTEEALAGFDSRFHVRPPLRSEADRQALVAGVRDGVIDAIVSQHQPHDSAAKQAPLPATEPGLSSIESVLSLGLELVA 347
Cdd:PRK08417 231 LILDDSACENFNTAAKLNPPLRSKEDRLALLEALKEGKIDFLTSLHSAKSNSKKDLAFDEAAFGIDSICEYFSLCYTYLV 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443493860 348 RGELERARLLSALTA-GPASVLGRN-ARLAEGEAADLCVFAPEQSWQpsVQTLVSagrhaPVLDRELPGRVRLTLVAGRT 425
Cdd:PRK08417 311 KEGIITWSELSRFTSyNPAQFLGLNsGEIEVGKEADLVLFDPNESTI--IDDNFS-----LYSGDELYGKIEAVIIKGKL 383
|
|
| PRK06189 |
PRK06189 |
allantoinase; Provisional |
9-429 |
2.76e-45 |
|
allantoinase; Provisional
Pssm-ID: 235732 [Multi-domain] Cd Length: 451 Bit Score: 162.95 E-value: 2.76e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443493860 9 LKITGGTLFDGTGkeIENPGLLIRGGEIAAIGEAaIPAEAAQTLDASGCVISPGFIDLSCNLREPGNGQKGNIASETRAA 88
Cdd:PRK06189 5 LIIRGGKVVTPEG--VYRADIGIKNGKIAEIAPE-ISSPAREIIDADGLYVFPGMIDVHVHFNEPGRTHWEGFATGSAAL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443493860 89 AHGGFTTVCASPETS--PVNDSsavTHLI--REGADSRGSVRVLPVGAITRGlDGEMLSDMAglkNAGcvAVG------- 157
Cdd:PRK06189 82 AAGGCTTYFDMPLNSipPTVTR---EALDakAELARQKSAVDFALWGGLVPG-NLEHLRELA---EAG--VIGfkafmsn 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443493860 158 NGSRGVRNA--RILRRCMAYAQTFGLTVMFSPENQALA---ADGYSHDGQVATRLGLLGIPEVAETAAVMEMLLLAEETG 232
Cdd:PRK06189 153 SGTDEFRSSddLTLYEGMKEIAALGKILALHAESDALTrhlTTQARQQGKTDVRDYLESRPVVAELEAVQRALLYAQETG 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443493860 233 VKLHLSQLSSGRSVQMLADARKRGIQVTADVAMHQLCFTEEALAGFDSRFHVRPPLRSEADRQALVAGVRDGVIDAIVSQ 312
Cdd:PRK06189 233 CPLHFVHISSGKAVALIAEAKKRGVDVSVETCPHYLLFTEEDFERIGAVAKCAPPLRSRSQKEELWRGLLAGEIDMISSD 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443493860 313 HQP-HDSAAKQAPLPATEPGLSSIESVLSLGLEL--VARG-ELER-ARLLSaltAGPASVLG--RNARLAEGEAADLCVF 385
Cdd:PRK06189 313 HSPcPPELKEGDDFFLVWGGISGGQSTLLVMLTEgyIERGiPLETiARLLA---TNPAKRFGlpQKGRLEVGADADFVLV 389
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 2443493860 386 APEQSWQPSVQTLVSAGRHAPVLDRELPGRVRLTLVAGRTAWAD 429
Cdd:PRK06189 390 DLDETYTLTKEDLFYRHKQSPYEGRTFPGRVVATYLRGQCVYQD 433
|
|
| Cyclic_amidohydrolases |
cd01302 |
Cyclic amidohydrolases, including hydantoinase, dihydropyrimidinase, allantoinase, and ... |
57-419 |
8.81e-44 |
|
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: 156.01 E-value: 8.81e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443493860 57 CVISPGFIDLSCNLREPGNGQ-KGNIASETRAAAHGGFTTVCASPETSPVNDSSAVTHLIREGADSR---------GSVR 126
Cdd:cd01302 1 LLVLPGFIDIHVHLRDPGGTTyKEDFESGSRAAAAGGVTTVIDMPNTGPPPIDLPAIELKIKLAEESsyvdfsfhaGIGP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443493860 127 VLPVGAITRGLDgemlSDMAGLKNAGCVAVGnGSRGVRNARILRRCMAYAqTFGLTVMFspenqalaadgysHdgqvatr 206
Cdd:cd01302 81 GDVTDELKKLFD----AGINSLKVFMNYYFG-ELFDVDDGTLMRTFLEIA-SRGGPVMV-------------H------- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443493860 207 lgllgipevAETAAvmemlLLAEETGVKLHLSQLSSGRSVQMLADARKRGIQVTADVAMHQLCFTEEALAGFDSRFHVRP 286
Cdd:cd01302 135 ---------AERAA-----QLAEEAGANVHIAHVSSGEALELIKFAKNKGVKVTCEVCPHHLFLDESMLRLNGAWGKVNP 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443493860 287 PLRSEADRQALVAGVRDGVIDAIVSQHQPHDSAAKQ--APLPATEPGLSSIESVLSLGLELVARGELERARLLSALTAGP 364
Cdd:cd01302 201 PLRSKEDREALWEGVKNGKIDTIASDHAPHSKEEKEsgKDIWKAPPGFPGLETRLPILLTEGVKRGLSLETLVEILSENP 280
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 2443493860 365 ASVLGRNA--RLAEGEAADLCVFAPEQSWQPSVQTLVSAGRHAPVLDRELPGRVRLT 419
Cdd:cd01302 281 ARIFGLYPkgTIAVGYDADLVIVDPKKEWKVTAEEIESKADWTPFEGMEVTGKPVST 337
|
|
| PRK02382 |
PRK02382 |
dihydroorotase; Provisional |
11-388 |
2.24e-42 |
|
dihydroorotase; Provisional
Pssm-ID: 179417 [Multi-domain] Cd Length: 443 Bit Score: 154.81 E-value: 2.24e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443493860 11 ITGGTLFDG---TGKEIENPGLLIRGGEIAAIGEAAIPAEAAQTLDASGCVISPGFIDLSCNLREPGNGQKGNIASETRA 87
Cdd:PRK02382 1 MRDALLKDGrvyYNNSLQPRDVRIDGGKITAVGKDLDGSSSEEVIDARGMLLLPGGIDVHVHFREPGYTHKETWYTGSRS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443493860 88 AAHGGFTTVCASPETSP--------------VNDSSAVTHLIREGA----DSRGSVRVLPVGAItrgldGEMLsdmaglk 149
Cdd:PRK02382 81 AAAGGVTTVVDQPNTDPptvdgesfdekaelAARKSIVDFGINGGVtgnwDPLESLWERGVFAL-----GEIF------- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443493860 150 nagcVAVGNGSRGVrNARILRRCMAYAQTFGLTVMFSPENQALAADG-YSHDGQV------ATRlgllgiPEVAETAAVM 222
Cdd:PRK02382 149 ----MADSTGGMGI-DEELFEEALAEAARLGVLATVHAEDEDLFDELaKLLKGDAdadawsAYR------PAAAEAAAVE 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443493860 223 EMLLLAEETGVKLHLSQLSSGRSVQMLADARkrgiqVTADVAMHQLCFTEEALAGFDSRFHVRPPLRSEADRQALVAGVR 302
Cdd:PRK02382 218 RALEVASETGARIHIAHISTPEGVDAARREG-----ITCEVTPHHLFLSRRDWERLGTFGKMNPPLRSEKRREALWERLN 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443493860 303 DGVIDAIVSQHQPHDSAAKQAPLPATEPGLSSIESVLSLGLELVARGELERARLLSALTAGPASVLG--RNARLAEGEAA 380
Cdd:PRK02382 293 DGTIDVVASDHAPHTREEKDADIWDAPSGVPGVETMLPLLLAAVRKNRLPLERVRDVTAANPARIFGldGKGRIAEGYDA 372
|
....*...
gi 2443493860 381 DLCVFAPE 388
Cdd:PRK02382 373 DLVLVDPD 380
|
|
| PRK09060 |
PRK09060 |
dihydroorotase; Validated |
9-384 |
3.54e-34 |
|
dihydroorotase; Validated
Pssm-ID: 181632 [Multi-domain] Cd Length: 444 Bit Score: 132.35 E-value: 3.54e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443493860 9 LKITGGTLFDGTGKEIENPGllIRGGEIAAIGEAAiPAEAAQTLDASGCVISPGFIDLSCNLREPGNGQKGNIASETRAA 88
Cdd:PRK09060 7 LILKGGTVVNPDGEGRADIG--IRDGRIAAIGDLS-GASAGEVIDCRGLHVLPGVIDSQVHFREPGLEHKEDLETGSRAA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443493860 89 AHGGFTTVCASPETSPVNDSSAVTHLIREGADSRGSVRV-LPVGAiTRgldgEMLSDMAGLKNA-GC--VAVGNGSR--- 161
Cdd:PRK09060 84 VLGGVTAVFEMPNTNPLTTTAEALADKLARARHRMHCDFaFYVGG-TR----DNADELAELERLpGCagIKVFMGSStgd 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443493860 162 -------GVRN--ARILRRcmayaqtfgltVMFSPENQALAAD--GYSHDGQVATRlgllgiPEV-AETAAVM---EMLL 226
Cdd:PRK09060 159 llveddeGLRRilRNGRRR-----------AAFHSEDEYRLRErkGLRVEGDPSSH------PVWrDEEAALLatrRLVR 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443493860 227 LAEETGVKLHLSQLSSGRSVQMLADARKRgiqVTADVAMHQLCFT-EEALAGFDSRFHVRPPLRSEADRQALVAGVRDGV 305
Cdd:PRK09060 222 LARETGRRIHVLHVSTAEEIDFLADHKDV---ATVEVTPHHLTLAaPECYERLGTLAQMNPPIRDARHRDGLWRGVRQGV 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443493860 306 IDAIVSQHQPHDSAAKQAPLPATEPGLSSIESVLSLGLELVARGELERARLLSALTAGPASVLG--RNARLAEGEAADLC 383
Cdd:PRK09060 299 VDVLGSDHAPHTLEEKAKPYPASPSGMTGVQTLVPIMLDHVNAGRLSLERFVDLTSAGPARIFGiaGKGRIAVGYDADFT 378
|
.
gi 2443493860 384 V 384
Cdd:PRK09060 379 I 379
|
|
| D-HYD |
cd01314 |
D-hydantoinases (D-HYD) also called dihydropyrimidases (DHPase) and related proteins; DHPases ... |
11-429 |
1.89e-33 |
|
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: 130.42 E-value: 1.89e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443493860 11 ITGGTLFdgTGKEIENPGLLIRGGEIAAIGEAAIPAEAAQTLDASGCVISPGFIDLSCNLREP--GNGQKGNIASETRAA 88
Cdd:cd01314 3 IKNGTIV--TADGSFKADILIEDGKIVAIGPNLEAPGGVEVIDATGKYVLPGGIDPHTHLELPfmGTVTADDFESGTRAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443493860 89 AHGGFTTVCasPETSPVNDSS--AVTHLIREGADSRGSVRVLPVGAITRgLDGEMLSDMAGLKNAGCVAVG-----NGSR 161
Cdd:cd01314 81 AAGGTTTII--DFAIPNKGQSllEAVEKWRGKADGKSVIDYGFHMIITD-WTDSVIEELPELVKKGISSFKvfmayKGLL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443493860 162 GVRNARILRrCMAYAQTFGLTVMFSPEN--------QALAADGY-SHDGQVATRlgllgiPEVAETAAVMEMLLLAEETG 232
Cdd:cd01314 158 MVDDEELLD-VLKRAKELGALVMVHAENgdviaelqKKLLAQGKtGPEYHALSR------PPEVEAEATARAIRLAELAG 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443493860 233 VKLHLSQLSSGRSVQMLADARKRGIQVTADVAMHQLCFTEEALA--GFD-SRFHVRPPLRSEADRQALVAGVRDGVIDAI 309
Cdd:cd01314 231 APLYIVHVSSKEAADEIARARKKGLPVYGETCPQYLLLDDSDYWkdWFEgAKYVCSPPLRPKEDQEALWDGLSSGTLQTV 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443493860 310 VSQHQPHDSAAKQAPLPA-TE-P-GLSSIESVLSLGL-ELVARGELERARLLSALTAGPASVLG---RNARLAEGEAADL 382
Cdd:cd01314 311 GSDHCPFNFAQKARGKDDfTKiPnGVPGVETRMPLLWsEGVAKGRITLEKFVELTSTNPAKIFGlypRKGTIAVGSDADL 390
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 2443493860 383 CVFAPEQSWQPSVQTLVSAGRHAPVLDRELPGRVRLTLVAGRTAWAD 429
Cdd:cd01314 391 VIWDPNAEKTISADTHHHNVDYNIFEGMKVKGWPVVTISRGKVVVED 437
|
|
| PRK09236 |
PRK09236 |
dihydroorotase; Reviewed |
14-429 |
2.75e-32 |
|
dihydroorotase; Reviewed
Pssm-ID: 181716 Cd Length: 444 Bit Score: 127.29 E-value: 2.75e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443493860 14 GTLFDGTgkeienpgLLIRGGEIAAIGEAAIPAEAAQTLDASGCVISPGFIDLSCNLREPGNGQKGNIASETRAAAHGGF 93
Cdd:PRK09236 15 GKIFEGD--------VLIENGRIAKIASSISAKSADTVIDAAGRYLLPGMIDDQVHFREPGLTHKGDIASESRAAVAGGI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443493860 94 TTVCASPETSPvndsSAVTHLIREGADSRGSVRVLP-----VGAITRGLDgEML----SDMAGLKnagcVAVGnGSRG-- 162
Cdd:PRK09236 87 TSFMEMPNTNP----PTTTLEALEAKYQIAAQRSLAnysfyFGATNDNLD-EIKrldpKRVCGVK----VFMG-ASTGnm 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443493860 163 -VRNARILRRCMAYAQTFGLTVMFSP----ENQALAADGYSHDgqvatrlgllgIPEVA------ETA-------AVMem 224
Cdd:PRK09236 157 lVDNPETLERIFRDAPTLIATHCEDTptikANLAKYKEKYGDD-----------IPAEMhplirsAEAcykssslAVS-- 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443493860 225 llLAEETGVKLHLSQLSSGRSVQMLADARKRGIQVTADVAMHQLCFTEEALAGFDSRFHVRPPLRSEADRQALVAGVRDG 304
Cdd:PRK09236 224 --LAKKHGTRLHVLHISTAKELSLFENGPLAEKRITAEVCVHHLWFDDSDYARLGNLIKCNPAIKTASDREALRQALADD 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443493860 305 VIDAIVSQHQPHDSAAKQAPLPATEPGLSSIESVLSLGLELVARGELERARLLSALTAGPASVLGRNAR--LAEGEAADL 382
Cdd:PRK09236 302 RIDVIATDHAPHTWEEKQGPYFQAPSGLPLVQHALPALLELVHEGKLSLEKVVEKTSHAPAILFDIKERgfIREGYWADL 381
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 2443493860 383 CVFAPEQSWQPSVQTLVSAGRHAPVLDRELPGRVRLTLVAGRTAWAD 429
Cdd:PRK09236 382 VLVDLNSPWTVTKENILYKCGWSPFEGRTFRSRVATTFVNGQLVYHN 428
|
|
| PRK07575 |
PRK07575 |
dihydroorotase; Provisional |
29-429 |
7.75e-32 |
|
dihydroorotase; Provisional
Pssm-ID: 236055 [Multi-domain] Cd Length: 438 Bit Score: 125.94 E-value: 7.75e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443493860 29 LLIRGGEIAAIGEAAIPAEAAQTLDASGCVISPGFIDLSCNLREPGNGQKGNIASETRAAAHGGFTTVCASPETSPVNDS 108
Cdd:PRK07575 24 VLVEDGKIVAIAPEISATAVDTVIDAEGLTLLPGVIDPQVHFREPGLEHKEDLFTASRACAKGGVTSFLEMPNTKPLTTT 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443493860 109 SAVTHLIREGADSRGSVRV-LPVGAItrgldGEMLSDMAGLKNAGCVAVGNGSRG----VRNARILRRcmayaqtfgltv 183
Cdd:PRK07575 104 QAALDDKLARAAEKCVVNYgFFIGAT-----PDNLPELLTANPTCGIKIFMGSSHgpllVDEEAALER------------ 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443493860 184 MFSPENQALAADGYSHDGQVATRLGLLGIPEVA-------ETAAVMEM---LLLAEETGVKLHLSQLSSGRSVQMLADAR 253
Cdd:PRK07575 167 IFAEGTRLIAVHAEDQARIRARRAEFAGISDPAdhsqiqdEEAALLATrlaLKLSKKYQRRLHILHLSTAIEAELLRQDK 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443493860 254 krGIQVTADVAMHQLCFTEEALAGFDSRFHVRPPLRSEADRQALVAGVRDGVIDAIVSQHQPHDSAAKQAPLPATEPGLS 333
Cdd:PRK07575 247 --PSWVTAEVTPQHLLLNTDAYERIGTLAQMNPPLRSPEDNEALWQALRDGVIDFIATDHAPHTLEEKAQPYPNSPSGMP 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443493860 334 SIESVLSLGLELVARGELERARLLSALTAGPASVLG--RNARLAEGEAADLcvfapeqswqpsvqTLVSAGRHAPVLDRE 411
Cdd:PRK07575 325 GVETSLPLMLTAAMRGKCTVAQVVRWMSTAVARAYGipNKGRIAPGYDADL--------------VLVDLNTYRPVRREE 390
|
410 420 430
....*....|....*....|....*....|..
gi 2443493860 412 LPGRVR--------------LTLVAGRTAWAD 429
Cdd:PRK07575 391 LLTKCGwspfegwnltgwpvTTIVGGQIVFDR 422
|
|
| PLN02795 |
PLN02795 |
allantoinase |
31-425 |
9.71e-30 |
|
allantoinase
Pssm-ID: 178392 [Multi-domain] Cd Length: 505 Bit Score: 120.65 E-value: 9.71e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443493860 31 IRGGEIAAIGE---AAIPAEAAQTLDASGCVISPGFIDLSCNLREPGNGQKGNIASETRAAAHGGFTTVCASPETS-PVN 106
Cdd:PLN02795 66 VEGGRIVSVTKeeeAPKSQKKPHVLDYGNAVVMPGLIDVHVHLNEPGRTEWEGFPTGTKAAAAGGITTLVDMPLNSfPST 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443493860 107 DSSAVTHLIREGADSRGSVRV------LPVGAITRGLDGEMLSDMA-GLKNAGCVAVGNGSRGVRNARI---LRRCMAYA 176
Cdd:PLN02795 146 TSVETLELKIEAAKGKLYVDVgfwgglVPENAHNASVLEELLDAGAlGLKSFMCPSGINDFPMTTATHIkaaLPVLAKYG 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443493860 177 QTFGL--TVMFSPENQA-LAADGYSHDGQVATRlgllgiPEVAETAAVMEMLLLAEET-------GVKLHLSQLS-SGRS 245
Cdd:PLN02795 226 RPLLVhaEVVSPVESDSrLDADPRSYSTYLKSR------PPSWEQEAIRQLLEVAKDTrpggvaeGAHVHIVHLSdAESS 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443493860 246 VQMLADARKRGIQVTADVAMHQLCFTEEALAGFDSRFHVRPPLRSEADRQALVAGVRDGVIDAIVSQHQPHDSAAKqapL 325
Cdd:PLN02795 300 LELIKEAKAKGDSVTVETCPHYLAFSAEEIPDGDTRYKCAPPIRDAANRELLWKALLDGDIDMLSSDHSPSPPDLK---L 376
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443493860 326 PATEP------GLSSIESVL----SLGLelvARGeLERARLLSALTAGPASV--LGRNARLAEGEAADLCVFAPEQSWQP 393
Cdd:PLN02795 377 LEEGNflrawgGISSLQFVLpatwTAGR---AYG-LTLEQLARWWSERPAKLagLDSKGAIAPGKDADIVVWDPEAEFVL 452
|
410 420 430
....*....|....*....|....*....|....*
gi 2443493860 394 SvQTLVSAGRH---APVLDRELPGRVRLTLVAGRT 425
Cdd:PLN02795 453 D-ESYPIYHKHkslSPYLGTKLSGKVIATFVRGNL 486
|
|
| PRK04250 |
PRK04250 |
dihydroorotase; Provisional |
11-424 |
3.94e-29 |
|
dihydroorotase; Provisional
Pssm-ID: 235265 [Multi-domain] Cd Length: 398 Bit Score: 117.56 E-value: 3.94e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443493860 11 ITGGTLFDGtgkEIENPGLLIRGGEIAAIGEAAIPAEaaQTLDASGCVISPGFIDLSCNLREPGNGQKGNIASETRAAAH 90
Cdd:PRK04250 2 LEGKFLLKG---RIVEGGIGIENGRISKISLRDLKGK--EVIKVKGGIILPGLIDVHVHLRDFEESYKETIESGTKAALH 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443493860 91 GGFTTVCASPETSP-VNDSSavTHLIREGADSRGSVRVLPVGAITRGLDGEMLSDMAGLKNAGCVAVGNGsrgvrnaril 169
Cdd:PRK04250 77 GGITLVFDMPNTKPpIMDEK--TYEKRMRIAEKKSYADYALNFLIAGNCEKAEEIKADFYKIFMGASTGG---------- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443493860 170 rrcmAYAQTFGLTVMFSPENQALAADGYSHDGQVATRlgllgiPEVAETAAVMEMLLLAEETGVKLHLSQLSSGRSVQML 249
Cdd:PRK04250 145 ----IFSENFEVDYACAPGIVSVHAEDPELIREFPER------PPEAEVVAIERALEAGKKLKKPLHICHISTKDGLKLI 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443493860 250 ADARKRgiQVTADVAMHQLCFTEEalagfDSR----FHVRPPLRSEADRQALVAGVRDgvIDAIVSQHQPHDSAAKQapl 325
Cdd:PRK04250 215 LKSNLP--WVSFEVTPHHLFLTRK-----DYErnplLKVYPPLRSEEDRKALWENFSK--IPIIASDHAPHTLEDKE--- 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443493860 326 pATEPGLSSIESVLSLGLELVARGELERARLLSALTAGPASVLG-RNARLAEGEAADLCVFAPEQSWQPSVQTLVSAGRH 404
Cdd:PRK04250 283 -AGAAGIPGLETEVPLLLDAANKGMISLFDIVEKMHDNPARIFGiKNYGIEEGNYANFAVFDMKKEWTIKAEELYTKAGW 361
|
410 420
....*....|....*....|
gi 2443493860 405 APVLDRELPGRVRLTLVAGR 424
Cdd:PRK04250 362 TPYEGFKLKGKVIMTILRGE 381
|
|
| PRK08044 |
PRK08044 |
allantoinase AllB; |
31-428 |
5.88e-29 |
|
allantoinase AllB;
Pssm-ID: 169193 [Multi-domain] Cd Length: 449 Bit Score: 118.03 E-value: 5.88e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443493860 31 IRGGEIAAIGEAAipAEAAQTLDASGCVISPGFIDLSCNLREPGNGQKGNIASETRAAAHGGFTTVCASPETS-PVNDSS 109
Cdd:PRK08044 25 VKGGKIAAIGQDL--GDAKEVMDASGLVVSPGMVDAHTHISEPGRSHWEGYETGTRAAAKGGITTMIEMPLNQlPATVDR 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443493860 110 AVTHLIREGADSRGSVRVLPVGA-ITRGLDGEMLSDMAGLKNAGCVAVGNGSRGVRNARI------LRRCMAYAQTFGLT 182
Cdd:PRK08044 103 ASIELKFDAAKGKLTIDAAQLGGlVSYNLDRLHELDEVGVVGFKCFVATCGDRGIDNDFRdvndwqFYKGAQKLGELGQP 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443493860 183 VMFSPENqALAADGY----SHDGQVATRLGLLGIPEVAETAAVMEMLLLAEETGVKLHLSQLSSGRSVQMLADARKRGIQ 258
Cdd:PRK08044 183 VLVHCEN-ALICDELgeeaKREGRVTAHDYVASRPVFTEVEAIRRVLYLAKVAGCRLHVCHISSPEGVEEVTRARQEGQD 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443493860 259 VTADVAMHQLCFTEEALAGFDSRFHVRPPLRSEADRQALVAGVRDGVIDAIVSQHQPHDSAAKQAPLPATEPGLSSIESV 338
Cdd:PRK08044 262 VTCESCPHYFVLDTDQFEEIGTLAKCSPPIRDLENQKGMWEKLFNGEIDCLVSDHSPCPPEMKAGNIMEAWGGIAGLQNC 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443493860 339 LSLGL-ELVARGELERARLLSALTAGPASVLG--RNARLAEGEAADLCVFAPEQSWQPSVQTLVSAGRHAPVLDRELPGR 415
Cdd:PRK08044 342 MDVMFdEAVQKRGMSLPMFGKLMATNAADIFGlqQKGRIAPGKDADFVFIQPNSSYVLKNEDLEYRHKVSPYVGRTIGAR 421
|
410
....*....|...
gi 2443493860 416 VRLTLVAGRTAWA 428
Cdd:PRK08044 422 ITKTILRGDVIYD 434
|
|
| PRK08323 |
PRK08323 |
phenylhydantoinase; Validated |
8-429 |
2.52e-28 |
|
phenylhydantoinase; Validated
Pssm-ID: 236240 [Multi-domain] Cd Length: 459 Bit Score: 116.04 E-value: 2.52e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443493860 8 SLKITGGTLFDGTGkeIENPGLLIRGGEIAAIGeaaiPAEAAQTLDASGCVISPGFIDLSCNLREPGNG--QKGNIASET 85
Cdd:PRK08323 2 STLIKNGTVVTADD--TYKADVLIEDGKIAAIG----ANLGDEVIDATGKYVMPGGIDPHTHMEMPFGGtvSSDDFETGT 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443493860 86 RAAAHGGFTTV---CASPETSPVNDSSAVTHlirEGADSRGSVRVLPVGAITrGLDGEMLSDMAGLknagcVAVG----- 157
Cdd:PRK08323 76 RAAACGGTTTIidfALQPKGQSLREALEAWH---GKAAGKAVIDYGFHMIIT-DWNEVVLDEMPEL-----VEEGitsfk 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443493860 158 -----NGSRGVRNARILRrCMAYAQTFGLTVMFSPEN---------QALAAdgyshdGQVATRLGLLGIPEVAETAAVME 223
Cdd:PRK08323 147 lfmayKGALMLDDDELLR-ALQRAAELGALPMVHAENgdaiaylqaKLLAE------GKTGPEYHALSRPPEVEGEATNR 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443493860 224 MLLLAEETGVKLHLSQLSSGRSVQMLADARKRGIQVTADVAMHQLCFTEEALAGFDS----RFHVRPPLRSEADRQALVA 299
Cdd:PRK08323 220 AIMLAELAGAPLYIVHVSCKEALEAIRRARARGQRVFGETCPQYLLLDESEYDGPDWfegaKYVMSPPLRDKEHQDALWR 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443493860 300 GVRDGVIDAIVSQHQPHdSAAKQAPLPATE----P-GLSSIESVLSLgL--ELVARGELERARLLSALTAGPASVLG--- 369
Cdd:PRK08323 300 GLQDGDLQVVATDHCPF-CFEQKKQLGRGDftkiPnGTPGVEDRMPL-LfsEGVMTGRITLNRFVELTSTNPAKIFGlyp 377
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443493860 370 RNARLAEGEAADLCVFAPEQSWQPSVQTLVSAGRHAPVLDRELPGRVRLTLVAGRTAWAD 429
Cdd:PRK08323 378 RKGTIAVGADADIVIWDPNATKTISASTLHSNVDYNPYEGFEVTGWPVTTLSRGEVVVED 437
|
|
| pyrC |
PRK00369 |
dihydroorotase; Provisional |
56-429 |
1.64e-24 |
|
dihydroorotase; Provisional
Pssm-ID: 234738 [Multi-domain] Cd Length: 392 Bit Score: 104.46 E-value: 1.64e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443493860 56 GCVISPGFIDLSCNLREPGNGQKGNIASETRAAAHGGFTTVCASPETSP-VNDSSAVTHLIREGAD-SRGSVRVLpvGAI 133
Cdd:PRK00369 42 GTLILPGAIDLHVHLRGLKLSYKEDVASGTSEAAYGGVTLVADMPNTIPpLNTPEAITEKLAELEYySRVDYFVY--SGV 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443493860 134 TRGLDGEMLSDMAG-------LKNAGCVavgngsRGVRNARILrrcmayaqtfgltVMFSPEnqalaadgySHDGQVATR 206
Cdd:PRK00369 120 TKDPEKVDKLPIAGykifpedLEREETF------RVLLKSRKL-------------KILHPE---------VPLALKSNR 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443493860 207 LGLLGIpeVAETAAVMEMLLLAeetgvKLHLSQLSSGRSVQMladARKRGIqvTADVAMHQLCFTEEAlagfDSRFHVRP 286
Cdd:PRK00369 172 KLRRNC--WYEIAALYYVKDYQ-----NVHITHASNPRTVRL---AKELGF--TVDITPHHLLVNGEK----DCLTKVNP 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443493860 287 PLRSEADRQALVAGVRDgvIDAIVSQHQPHDSAAKQAPLPATEPGLSSIESVLSLGLELVARGELERARLLSALTAGPAS 366
Cdd:PRK00369 236 PIRDINERLWLLQALSE--VDAIASDHAPHSSFEKLQPYEVCPPGIAALSFTPPFIYTLVSKGILSIDRAVELISTNPAR 313
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2443493860 367 VLGRNAR-LAEGEAADLCVFAPEQsWQPSvqTLVSAGRHAPVLDRELPGRVRLTLVAGRTAWAD 429
Cdd:PRK00369 314 ILGIPYGeIKEGYRANFTVIQFED-WRYS--TKYSKVIETPLDGFELKASVYATIVQGKLAYLE 374
|
|
| CAD_DHOase |
cd01316 |
The eukaryotic CAD protein is a trifunctional enzyme of carbamoylphosphate ... |
58-429 |
9.20e-21 |
|
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: 92.90 E-value: 9.20e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443493860 58 VISPGFIDLSCNLREPGNGQKGNIASETRAAAHGGFTTVCASPETSPV--------------NDSSAVTHLIREGADSRG 123
Cdd:cd01316 3 IRLPGLIDVHVHLREPGATHKEDFASGTKAALAGGFTMVRAMPNTNPSivdvaslklvqslaQAKARCDYAFSIGATSTN 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443493860 124 SVRVlpvgaitrgldGEMLSDMAGLKnagcvavgngsrgvrnarilrrcmayaqtFGLTVMFSPENQALAADGYSHDGQV 203
Cdd:cd01316 83 AATV-----------GELASEAVGLK-----------------------------FYLNETFSTLILDKITAWASHFNAW 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443493860 204 ATRLGLLGIPEVAETAAVmemLLLAEETGVKLHLSQLSSGRSVQMLADARKRGIQVTADVAMHQLCFTEEALAgfDSRFH 283
Cdd:cd01316 123 PSTKPIVTHAKSQTLAAV---LLLASLHNRSIHICHVSSKEEINLIRLAKARGLKVTCEVSPHHLFLSQDDLP--RGQYE 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443493860 284 VRPPLRSEADRQALVAGVrdGVIDAIVSQHQPHDSAAKQAPLPAtePGLSSIESVLSLGLELVARGELERARLLSALTAG 363
Cdd:cd01316 198 VRPFLPTREDQEALWENL--DYIDCFATDHAPHTLAEKTGNKPP--PGFPGVETSLPLLLTAVHEGRLTIEDIVDRLHTN 273
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2443493860 364 PASVLgrnaRLAEGEAADLCVfAPEQSWQPSVQTLVSAGRHAPVLDRELPGRVRLTLVAGRTAWAD 429
Cdd:cd01316 274 PKRIF----NLPPQSDTYVEV-DLDEEWTIPKNPLQSKKGWTPFEGKKVKGKVQRVVLRGETAFID 334
|
|
| PRK13404 |
PRK13404 |
dihydropyrimidinase; Provisional |
11-429 |
8.88e-20 |
|
dihydropyrimidinase; Provisional
Pssm-ID: 184033 [Multi-domain] Cd Length: 477 Bit Score: 91.30 E-value: 8.88e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443493860 11 ITGGTLFDGTGKEIENPGllIRGGEIAAIGEAAipAEAAQTLDASGCVISPGFIDLSCNLREP---GNGQKGNIASETRA 87
Cdd:PRK13404 8 IRGGTVVTATDTFQADIG--IRGGRIAALGEGL--GPGAREIDATGRLVLPGGVDSHCHIDQPsgdGIMMADDFYTGTVS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443493860 88 AAHGGFTTV---CASPETSPVNDS----------SAVT----HLIREGADSRGSVRVLPvGAITRGLDG---EMLSDMAG 147
Cdd:PRK13404 84 AAFGGTTTVipfAAQHRGQSLREAvedyhrraagKAVIdyafHLIVADPTEEVLTEELP-ALIAQGYTSfkvFMTYDDLK 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443493860 148 LKNAGCVAVgngsrgvrnarilrrcMAYAQTFGLTVMFSPENQ---ALAADGYSHDGQVATRLGLLGIPEVAETAAVMEM 224
Cdd:PRK13404 163 LDDRQILDV----------------LAVARRHGAMVMVHAENHdmiAWLTKRLLAAGLTAPKYHAISRPMLAEREATHRA 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443493860 225 LLLAEETGVKLHLSQLSSGRSVQMLADARKRGIQVTADVAMHQLCFTEEAL--AGFD-SRFHVRPPLRSEADRQALVAGV 301
Cdd:PRK13404 227 IALAELVDVPILIVHVSGREAAEQIRRARGRGLKIFAETCPQYLFLTAEDLdrPGMEgAKYICSPPPRDKANQEAIWNGL 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443493860 302 RDGVIDAIVSQHQPH---DSAAK-----QAPLPATEPGLSSIESVLSLGL-ELVARGELERARLLsALTA-GPASVLGRN 371
Cdd:PRK13404 307 ADGTFEVFSSDHAPFrfdDTDGKlaagaNPSFKAIANGIPGIETRLPLLFsEGVVKGRISLNRFV-ALTStNPAKLYGLY 385
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2443493860 372 AR---LAEGEAADLCVfapeqsWQPSVQTLVSAG--RHA----PVLDRELPGRVRLTLVAGRTAWAD 429
Cdd:PRK13404 386 PRkgaIAIGADADIAI------WDPDREVTITNAdlHHAadytPYEGMRVTGWPVTVLSRGRVVVED 446
|
|
| D-aminoacylase |
cd01297 |
D-aminoacylases (N-acyl-D-Amino acid amidohydrolases) catalyze the hydrolysis of ... |
11-389 |
4.93e-13 |
|
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: 70.40 E-value: 4.93e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443493860 11 ITGGTLFDGTGKEIENPGLLIRGGEIAAIGEAAIPaEAAQTLDASGCVISPGFIDL-----SCNLREPGNgqkgniaset 85
Cdd:cd01297 4 IRNGTVVDGTGAPPFTADVGIRDGRIAAIGPILST-SAREVIDAAGLVVAPGFIDVhthydGQVFWDPDL---------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443493860 86 RAAAHGGFTTVCASpetspvNDSSAVTHLIREGADSRGSvRVLPVGAITRGLD------GEMLSDMAGLK---NAGCVAV 156
Cdd:cd01297 73 RPSSRQGVTTVVLG------NCGVSPAPANPDDLARLIM-LMEGLVALGEGLPwgwatfAEYLDALEARPpavNVAALVG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443493860 157 GNGSR----GVRN-----------ARILRRCMAyAQTFGL-TVMFSP--------ENQALAADGYSHDGQVATRLGLLGI 212
Cdd:cd01297 146 HAALRravmGLDAreateeelakmRELLREALE-AGALGIsTGLAYAprlyagtaELVALARVAARYGGVYQTHVRYEGD 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443493860 213 PEVaetAAVMEMLLLAEETGVKLHLSQLSS---------GRSVQMLADARKRGIQVTADVAmhqlcfteealagfdsrfh 283
Cdd:cd01297 225 SIL---EALDELLRLGRETGRPVHISHLKSagapnwgkiDRLLALIEAARAEGLQVTADVY------------------- 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443493860 284 vrP-PLRSEADRQALVagvrdgvidaivsQHQPHDSAAKQAPLPATEPGLSSiESVLSLGLELVARGELERARLLSALTA 362
Cdd:cd01297 283 --PyGAGSEDDVRRIM-------------AHPVVMGGSDGGALGKPHPRSYG-DFTRVLGHYVRERKLLSLEEAVRKMTG 346
|
410 420
....*....|....*....|....*....
gi 2443493860 363 GPASVLGRNAR--LAEGEAADLCVFAPEQ 389
Cdd:cd01297 347 LPARVFGLADRgrIAPGYRADIVVFDPDT 375
|
|
| HutI |
COG1228 |
Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport ... |
5-96 |
3.00e-12 |
|
Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440841 [Multi-domain] Cd Length: 386 Bit Score: 67.68 E-value: 3.00e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443493860 5 QNDSLKITGGTLFDGTGKE-IENPGLLIRGGEIAAIGEAAIPA--EAAQTLDASGCVISPGFIDLSCNL-----REPGNG 76
Cdd:COG1228 6 QAGTLLITNATLVDGTGGGvIENGTVLVEDGKIAAVGPAADLAvpAGAEVIDATGKTVLPGLIDAHTHLglgggRAVEFE 85
|
90 100 110
....*....|....*....|....*....|
gi 2443493860 77 QKGNIASETRAAAH----------GGFTTV 96
Cdd:COG1228 86 AGGGITPTVDLVNPadkrlrralaAGVTTV 115
|
|
| PRK01211 |
PRK01211 |
dihydroorotase; Provisional |
31-385 |
1.21e-11 |
|
dihydroorotase; Provisional
Pssm-ID: 179247 [Multi-domain] Cd Length: 409 Bit Score: 66.03 E-value: 1.21e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443493860 31 IRGGEIAAIgEAAIPAEAAQTLDASgcvISPGFIDLSCNLREPGNGQKGNIASETRAAAHGGFTTVCASPETS-PVNDSS 109
Cdd:PRK01211 20 VEDGKIKSI-KKDAGNIGKKELKGA---ILPAATDIHVHFRTPGETEKEDFSTGTLSAIFGGTTFIMDMPNNNiPIKDYN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443493860 110 AVTHliREGADSRGSVRVLPVGAITRGLDGEMLSD--------MAGLKNAGCVAVGNGS-RGVRNArilrrcmayaqtfG 180
Cdd:PRK01211 96 AFSD--KLGRVAPKAYVDFSLYSMETGNNALILDErsiglkvyMGGTTNTNGTDIEGGEiKKINEA-------------N 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443493860 181 LTVMFSPENQALAADGYSHDGQVatRLGLLGIPEVAETAAVMEMLLLAEETGVKLHLSqlssgrSVQMLADarkrgiqVT 260
Cdd:PRK01211 161 IPVFFHAELSECLRKHQFESKNL--RDHDLARPIECEIKAVKYVKNLDLKTKIIAHVS------SIDVIGR-------FL 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443493860 261 ADVAMHQLCFTEEALAGfdSRFHVRPPLRSEADRQALVAGVRDGVIDAIVSQHQPHdSAAKQAPLPATEPGLSSIESVLS 340
Cdd:PRK01211 226 REVTPHHLLLNDDMPLG--SYGKVNPPLRDRWTQERLLEEYISGRFDILSSDHAPH-TEEDKQEFEYAKSGIIGVETRVP 302
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 2443493860 341 LGLELVARGELERARLLSALTAGPASVLG-RNARLAEGEAADLCVF 385
Cdd:PRK01211 303 LFLALVKKKILPLDVLYKTAIERPASLFGiKKGKIEEGYDADFMAF 348
|
|
| COG3964 |
COG3964 |
Predicted amidohydrolase [General function prediction only]; |
11-66 |
7.38e-11 |
|
Predicted amidohydrolase [General function prediction only];
Pssm-ID: 443164 [Multi-domain] Cd Length: 376 Bit Score: 63.26 E-value: 7.38e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 2443493860 11 ITGGTLFDGTGKEIENPGLLIRGGEIAAIGEAAIPAEAAQTLDASGCVISPGFIDL 66
Cdd:COG3964 4 IKGGRVIDPANGIDGVMDIAIKDGKIAAVAKDIDAAEAKKVIDASGLYVTPGLIDL 59
|
|
| PLN02942 |
PLN02942 |
dihydropyrimidinase |
9-429 |
9.43e-11 |
|
dihydropyrimidinase
Pssm-ID: 178530 Cd Length: 486 Bit Score: 63.32 E-value: 9.43e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443493860 9 LKITGGTLFDGTGKEIENpgLLIRGGEIAAIGEAAIPAEAAQTLDASGCVISPGFIDLSCNLREPGNGQKG--NIASETR 86
Cdd:PLN02942 7 ILIKGGTVVNAHHQELAD--VYVEDGIIVAVAPNLKVPDDVRVIDATGKFVMPGGIDPHTHLAMPFMGTETidDFFSGQA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443493860 87 AAAHGGFTTVCASpeTSPVNDSSAVTHLIREGADSRGSVRVLPVGAITRGLDG-----EMLSDMAGLKNAGCVAVGNGSR 161
Cdd:PLN02942 85 AALAGGTTMHIDF--VIPVNGNLLAGYEAYEKKAEKSCMDYGFHMAITKWDDTvsrdmETLVKEKGINSFKFFMAYKGSL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443493860 162 GVRNARIL---RRCmayaQTFGLTVMFSPENQALAADGYShdgqvatRLGLLGI----------PEVAETAAVMEMLLLA 228
Cdd:PLN02942 163 MVTDELLLegfKRC----KSLGALAMVHAENGDAVFEGQK-------RMIELGItgpeghalsrPPLLEGEATARAIRLA 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443493860 229 EETGVKLHLSQLSSGRSVQMLADARKRGIQVTADVAMHQLCFTEEALAGFD----SRFHVRPPLRSEADRQALVAGVRDG 304
Cdd:PLN02942 232 KFVNTPLYVVHVMSIDAMEEIARARKSGQRVIGEPVVSGLVLDDSKLWDPDftiaSKYVMSPPIRPAGHGKALQAALSSG 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443493860 305 VIDAIVSQHQPHDSAAKQA------PLPAtepGLSSIESVLSLGL-ELVARGEL---ERARLLSALTAGPASVLGRNARL 374
Cdd:PLN02942 312 ILQLVGTDHCPFNSTQKAFgkddfrKIPN---GVNGIEERMHLVWdTMVESGQIsptDYVRVTSTECAKIFNIYPRKGAI 388
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2443493860 375 AEGEAADLCVfapeqsWQPSVQTLVSAGRHAPVLD------RELPGRVRLTLVAGRTAWAD 429
Cdd:PLN02942 389 LAGSDADIII------LNPNSTFTISAKTHHSRIDtnvyegRRGKGKVEVTISQGRVVWEN 443
|
|
| NagA |
COG1820 |
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism]; |
11-69 |
1.49e-08 |
|
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism];
Pssm-ID: 441425 [Multi-domain] Cd Length: 373 Bit Score: 56.26 E-value: 1.49e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 2443493860 11 ITGGTLFDGTGkEIENPGLLIRGGEIAAIGEAAipAEAAQTLDASGCVISPGFIDLSCN 69
Cdd:COG1820 2 ITNARIFTGDG-VLEDGALLIEDGRIAAIGPGA--EPDAEVIDLGGGYLAPGFIDLHVH 57
|
|
| SsnA |
COG0402 |
Cytosine/adenosine deaminase or related metal-dependent hydrolase [Nucleotide transport and ... |
11-66 |
2.99e-07 |
|
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: 52.14 E-value: 2.99e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2443493860 11 ITGGTL--FDGTGKEIENPGLLIRGGEIAAIGEAAIPAE---AAQTLDASGCVISPGFIDL 66
Cdd:COG0402 4 IRGAWVltMDPAGGVLEDGAVLVEDGRIAAVGPGAELPArypAAEVIDAGGKLVLPGLVNT 64
|
|
| PRK09237 |
PRK09237 |
amidohydrolase/deacetylase family metallohydrolase; |
11-66 |
5.11e-07 |
|
amidohydrolase/deacetylase family metallohydrolase;
Pssm-ID: 236423 [Multi-domain] Cd Length: 380 Bit Score: 51.39 E-value: 5.11e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 2443493860 11 ITGGTLFD---GTGKEIEnpgLLIRGGEIAAIGEAAIPAEAAQTLDASGCVISPGFIDL 66
Cdd:PRK09237 3 LRGGRVIDpanGIDGVID---IAIEDGKIAAVAGDIDGSQAKKVIDLSGLYVSPGWIDL 58
|
|
| PRK09061 |
PRK09061 |
D-glutamate deacylase; Validated |
11-262 |
9.80e-07 |
|
D-glutamate deacylase; Validated
Pssm-ID: 236369 [Multi-domain] Cd Length: 509 Bit Score: 50.85 E-value: 9.80e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443493860 11 ITGGTLFD-GTG-KEIENPGllIRGGEIAAIGEAAIpaEAAQTLDASGCVISPGFIDLSCNLREPGNgqkgniaseTRAA 88
Cdd:PRK09061 23 IRNGRVVDpETGlDAVRDVG--IKGGKIAAVGTAAI--EGDRTIDATGLVVAPGFIDLHAHGQSVAA---------YRMQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443493860 89 AHGGFTTVC---------------ASPETSPVNDSSAVTHL-----IREGADSRGSVRVLPVG---------AITRGLDG 139
Cdd:PRK09061 90 AFDGVTTALeleagvlpvarwyaeQAGEGRPLNYGASVGWTpariaVLTGPQAEGTIADFGKAlgdprwqerAATPAELA 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443493860 140 EMLSDMAGLKNAGCVAVGNGsrgvrnarilrrcMAYAQTFGLTvmfspENQALAADGYSHDGQVATRLGLLGIPEVAET- 218
Cdd:PRK09061 170 EILELLEQGLDEGALGIGIG-------------AGYAPGTGHK-----EYLELARLAARAGVPTYTHVRYLSNVDPRSSv 231
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 2443493860 219 AAVMEMLLLAEETGVKLHLSQLSS------GRSVQMLADARKRGIQVTAD 262
Cdd:PRK09061 232 DAYQELIAAAAETGAHMHICHVNStslrdiDRCLALVEKAQAQGLDVTTE 281
|
|
| NagA |
cd00854 |
N-acetylglucosamine-6-phosphate deacetylase, NagA, catalyzes the hydrolysis of the N-acetyl ... |
9-66 |
1.36e-06 |
|
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: 50.27 E-value: 1.36e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 2443493860 9 LKITGGTLFdgTGKEIENPGLLIRGGEIAAIGEAAIPAEAAQTLDASGCVISPGFIDL 66
Cdd:cd00854 1 LIIKNARIL--TPGGLEDGAVLVEDGKIVAIGPEDELEEADEIIDLKGQYLVPGFIDI 56
|
|
| PRK08203 |
PRK08203 |
hydroxydechloroatrazine ethylaminohydrolase; Reviewed |
18-64 |
1.56e-06 |
|
hydroxydechloroatrazine ethylaminohydrolase; Reviewed
Pssm-ID: 236184 [Multi-domain] Cd Length: 451 Bit Score: 50.24 E-value: 1.56e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 2443493860 18 DGTGKEIENPGLLIRGGEIAAIGEA-AIPAEAAQTLDASGCVISPGFI 64
Cdd:PRK08203 15 DAARREIADGGLVVEGGRIVEVGPGgALPQPADEVFDARGHVVTPGLV 62
|
|
| AdeC |
COG1001 |
Adenine deaminase [Nucleotide transport and metabolism]; |
11-65 |
1.75e-06 |
|
Adenine deaminase [Nucleotide transport and metabolism];
Pssm-ID: 440625 [Multi-domain] Cd Length: 559 Bit Score: 50.10 E-value: 1.75e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 2443493860 11 ITGGTLFDGTGKEIENPGLLIRGGEIAAIGEAaiPAEAAQTLDASGCVISPGFID 65
Cdd:COG1001 9 IKNGRLVNVFTGEILEGDIAIAGGRIAGVGDY--IGEATEVIDAAGRYLVPGFID 61
|
|
| ATZ_TRZ_like |
cd01298 |
TRZ/ATZ family contains enzymes from the atrazine degradation pathway and related hydrolases. ... |
11-64 |
3.19e-06 |
|
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: 49.12 E-value: 3.19e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 2443493860 11 ITGGTLF-DGTGKEIENPGLLIRGGEIAAIGEA--AIPAEAAQTLDASGCVISPGFI 64
Cdd:cd01298 3 IRNGTIVtTDPRRVLEDGDVLVEDGRIVAVGPAlpLPAYPADEVIDAKGKVVMPGLV 59
|
|
| Met_dep_hydrolase_B |
cd01307 |
Metallo-dependent hydrolases, subgroup B is part of the superfamily of metallo-dependent ... |
29-66 |
7.81e-06 |
|
Metallo-dependent hydrolases, subgroup B is part of the superfamily of metallo-dependent hydrolases, a large group of proteins that show conservation in their 3-dimensional fold (TIM barrel) and in details of their active site. The vast majority of the members have a conserved metal binding site, involving four histidines and one aspartic acid residue. In the common reaction mechanism, the metal ion (or ions) deprotonate a water molecule for a nucleophilic attack on the substrate. The function of this subgroup is unknown.
Pssm-ID: 238632 [Multi-domain] Cd Length: 338 Bit Score: 47.71 E-value: 7.81e-06
10 20 30
....*....|....*....|....*....|....*...
gi 2443493860 29 LLIRGGEIAAIGEAAIPAEAAQTLDASGCVISPGFIDL 66
Cdd:cd01307 2 VAIENGKIAAVGAALAAPAATQIVDAGGCYVSPGWIDL 39
|
|
| PRK07572 |
PRK07572 |
cytosine deaminase; Validated |
9-65 |
1.68e-05 |
|
cytosine deaminase; Validated
Pssm-ID: 181039 Cd Length: 426 Bit Score: 46.94 E-value: 1.68e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 2443493860 9 LKITGGTLFDG-TGKEIenpglLIRGGEIAAIgEAAIPAEAAQTLDASGCVISPGFID 65
Cdd:PRK07572 4 LIVRNANLPDGrTGIDI-----GIAGGRIAAV-EPGLQAEAAEEIDAAGRLVSPPFVD 55
|
|
| Met_dep_hydrolase_C |
cd01309 |
Metallo-dependent hydrolases, subgroup C is part of the superfamily of metallo-dependent ... |
34-385 |
2.17e-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: 43.07 E-value: 2.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443493860 34 GEIAAIGEAAIPAEAAQTLDASGCVISPGFIDLSCNLrepgngqkgNIASETraaahGGFTTVCASPETSPVN------- 106
Cdd:cd01309 2 GKIVAVGAEITTPADAEVIDAKGKHVTPGLIDAHSHL---------GLDEEG-----GVRETSDANEETDPVTphvraid 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443493860 107 ----DSSAVTHLIREGADsrgSVRVLPVGAITRG-------LDGEMLSDMAGLKNAG-CVAVGNGSRGVRNARILRRCMA 174
Cdd:cd01309 68 ginpDDEAFKRARAGGVT---TVQVLPGSANLIGgqgvvikTDGGTIEDMFIKAPAGlKMALGENPKRVYGGKGKEPATR 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443493860 175 YAQTFGLtvmfspENQALAADGYSHdgqvATRLGLLGIPEVAETAAVMEML--LLAEETGVKLHLSQLSSGRsvQMLADA 252
Cdd:cd01309 145 MGVAALL------RDAFIKAQEYGR----KYDLGKNAKKDPPERDLKLEALlpVLKGEIPVRIHAHRADDIL--TAIRIA 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443493860 253 RKRGIQVTADVAMHQ-LCFTEEALAGF-------DSRFHVRPPLRSEADRQALVAGvRDGVIDAIVSQHqphdSAAKQAP 324
Cdd:cd01309 213 KEFGIKITIEHGAEGyKLADELAKHGIpviygptLTLPKKVEEVNDAIDTNAYLLK-KGGVAFAISSDH----PVLNIRN 287
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2443493860 325 LPaTEPGLSsiesvlslglelVARGeLERARLLSALTAGPASVLG---RNARLAEGEAADLCVF 385
Cdd:cd01309 288 LN-LEAAKA------------VKYG-LSYEEALKAITINPAKILGiedRVGSLEPGKDADLVVW 337
|
|
| PRK07228 |
PRK07228 |
5'-deoxyadenosine deaminase; |
13-64 |
3.79e-04 |
|
5'-deoxyadenosine deaminase;
Pssm-ID: 180895 [Multi-domain] Cd Length: 445 Bit Score: 42.68 E-value: 3.79e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 2443493860 13 GGTLFDGTGKEIENPGLLIRGGEIAAIGEAAIPAEAAQTLDASGCVISPGFI 64
Cdd:PRK07228 8 AGIVTMNAKREIVDGDVLIEDDRIAAVGDRLDLEDYDDHIDATGKVVIPGLI 59
|
|
| PRK08204 |
PRK08204 |
hypothetical protein; Provisional |
11-65 |
4.85e-04 |
|
hypothetical protein; Provisional
Pssm-ID: 181288 [Multi-domain] Cd Length: 449 Bit Score: 42.30 E-value: 4.85e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 2443493860 11 ITGGTL--FDGTGKEIENPGLLIRGGEIAAIGEAaIPAEAAQTLDASGCVISPGFID 65
Cdd:PRK08204 6 IRGGTVltMDPAIGDLPRGDILIEGDRIAAVAPS-IEAPDAEVVDARGMIVMPGLVD 61
|
|
| PRK15446 |
PRK15446 |
phosphonate metabolism protein PhnM; Provisional |
11-68 |
8.37e-04 |
|
phosphonate metabolism protein PhnM; Provisional
Pssm-ID: 237967 [Multi-domain] Cd Length: 383 Bit Score: 41.32 E-value: 8.37e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 2443493860 11 ITGGTLFdgTGKEIENPGLLIRGGEIAAIGEAAIPAEAAqtLDASGCVISPGFIDLSC 68
Cdd:PRK15446 6 LSNARLV--LPDEVVDGSLLIEDGRIAAIDPGASALPGA--IDAEGDYLLPGLVDLHT 59
|
|
| Imidazolone-5PH |
cd01296 |
Imidazolonepropionase/imidazolone-5-propionate hydrolase (Imidazolone-5PH) catalyzes the third ... |
29-65 |
1.21e-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: 40.70 E-value: 1.21e-03
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 2443493860 29 LLIRGGEIAAIGEAA----IPAEAAQTLDASGCVISPGFID 65
Cdd:cd01296 1 IAIRDGRIAAVGPAAslpaPGPAAAEEIDAGGRAVTPGLVD 41
|
|
| SsnA |
COG0402 |
Cytosine/adenosine deaminase or related metal-dependent hydrolase [Nucleotide transport and ... |
354-429 |
3.48e-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: 39.42 E-value: 3.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443493860 354 ARLLSALTAGPASVLGRNA---RLAEGEAADLCVFAPEQ-SWQPS---VQTLVSAGRhapvldrelPGRVRLTLVAGRTA 426
Cdd:COG0402 343 REALEMATLGGARALGLDDeigSLEPGKRADLVVLDLDApHLAPLhdpLSALVYAAD---------GRDVRTVWVAGRVV 413
|
...
gi 2443493860 427 WAD 429
Cdd:COG0402 414 VRD 416
|
|
| FMDH_A |
cd01304 |
Formylmethanofuran dehydrogenase (FMDH) subunit A; Methanogenic bacteria and archea derive ... |
11-65 |
4.49e-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: 39.32 E-value: 4.49e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 2443493860 11 ITGGTLFDGT-GKEIENPGLLIRGGEIAAIGEAAIPAeaaQTLDASGCVISPGFID 65
Cdd:cd01304 1 IKNGTVYDPLnGINGEKMDIFIRDGKIVESSSGAKPA---KVIDASGKVVMAGGVD 53
|
|
| PRK12394 |
PRK12394 |
metallo-dependent hydrolase; |
11-65 |
4.65e-03 |
|
metallo-dependent hydrolase;
Pssm-ID: 183497 [Multi-domain] Cd Length: 379 Bit Score: 38.97 E-value: 4.65e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 2443493860 11 ITGGTLFDGTGKEIENPGLLIRGGEIAAIGEAAIpAEAAQTLDASGCVISPGFID 65
Cdd:PRK12394 7 ITNGHIIDPARNINEINNLRIINDIIVDADKYPV-ASETRIIHADGCIVTPGLID 60
|
|
| PRK05985 |
PRK05985 |
cytosine deaminase; Provisional |
11-92 |
7.07e-03 |
|
cytosine deaminase; Provisional
Pssm-ID: 180337 [Multi-domain] Cd Length: 391 Bit Score: 38.37 E-value: 7.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443493860 11 ITGGTLFDGTGKEIenpglLIRGGEIAAIGEAAIPAEAAQTLDASGCVISPGFIDLSCNL-----------REPGNGQKG 79
Cdd:PRK05985 6 FRNVRPAGGAAVDI-----LIRDGRIAAIGPALAAPPGAEVEDGGGALALPGLVDGHIHLdktfwgdpwypNEPGPSLRE 80
|
90
....*....|...
gi 2443493860 80 NIASETRAAAHGG 92
Cdd:PRK05985 81 RIANERRRRAASG 93
|
|
| nagA |
PRK11170 |
N-acetylglucosamine-6-phosphate deacetylase; Provisional |
11-69 |
8.30e-03 |
|
N-acetylglucosamine-6-phosphate deacetylase; Provisional
Pssm-ID: 183010 Cd Length: 382 Bit Score: 38.03 E-value: 8.30e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2443493860 11 ITGGTLFdgTGKEI-ENPGLLIRGGEIAAI-GEAAIPAEAaQTLDASGCVISPGFIDLSCN 69
Cdd:PRK11170 4 LTNGRIY--TGHEVlDDHAVVIADGLIEAVcPVAELPPGI-EQRDLNGAILSPGFIDLQLN 61
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