|
Name |
Accession |
Description |
Interval |
E-value |
| pyrC |
PRK09357 |
dihydroorotase; Validated |
1-379 |
0e+00 |
|
dihydroorotase; Validated
Pssm-ID: 236479 [Multi-domain] Cd Length: 423 Bit Score: 605.27 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232993981 1 MVALPGLVDLHTHLREPGYEASETVLSGTRAAAAGGFTAVFAMPNTSPVADSAGVVEQELALGEAAGYATVQPIGAVTVG 80
Cdd:PRK09357 49 LVVAPGLVDLHVHLREPGQEDKETIETGSRAAAAGGFTTVVAMPNTKPVIDTPEVVEYVLDRAKEAGLVDVLPVGAITKG 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232993981 81 QKGERLAELGAMASsrANVRVFSDDGFCVWDPLIMRRALEYVKAFDGVIAQHAQDPRLTEGAQLNEGAVSAELGLTGWPA 160
Cdd:PRK09357 129 LAGEELTEFGALKE--AGVVAFSDDGIPVQDARLMRRALEYAKALDLLIAQHCEDPSLTEGGVMNEGEVSARLGLPGIPA 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232993981 161 VAEESIIARDILLAEHVGSRLHVCHLSTAGSVELIRWAKKRGVAVTAEVTPHHLLLTDELARGYDARFKVNPPLRTQEDV 240
Cdd:PRK09357 207 VAEEVMIARDVLLAEATGARVHICHVSTAGSVELIRWAKALGIKVTAEVTPHHLLLTDEDLLTYDPNYKVNPPLRTEEDR 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232993981 241 LAVREGLADGTIDIVATDHAPHPSEAKACEWQAAANGMVGLESALRVVHQSMVQTGLLDWTDVARVMSSAPARIGSLPGH 320
Cdd:PRK09357 287 EALIEGLKDGTIDAIATDHAPHAREEKECEFEAAPFGITGLETALSLLYTTLVKTGLLDLEQLLEKMTINPARILGLPAG 366
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 1232993981 321 gtPIAAGQPAEFTLYDADAVGVFAESDLHGQSTNSPYLGRDLPGKVLWTVHHGYTTLED 379
Cdd:PRK09357 367 --PLAEGEPADLVIFDPEAEWTVDGEDFASKGKNTPFIGMKLKGKVVYTIVDGKIVYQD 423
|
|
| AllB |
COG0044 |
Dihydroorotase or related cyclic amidohydrolase [Nucleotide transport and metabolism]; ... |
1-385 |
1.40e-179 |
|
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: 506.17 E-value: 1.40e-179
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232993981 1 MVALPGLVDLHTHLREPGYEASETVLSGTRAAAAGGFTAVFAMPNTSPVADSAGVVEQELALGEAAGYATVQPIGAVTVG 80
Cdd:COG0044 46 LLVLPGLIDLHVHLREPGLEHKEDIETGTRAAAAGGVTTVVDMPNTNPVTDTPEALEFKLARAEEKALVDVGPHGALTKG 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232993981 81 QkGERLAELGAMAssRANVRVF-----SDDGFCVWDPLIMRRALEYVKAFDGVIAQHAQDPRLTEGAQLNEGAVSAELGL 155
Cdd:COG0044 126 L-GENLAELGALA--EAGAVAFkvfmgSDDGNPVLDDGLLRRALEYAAEFGALVAVHAEDPDLIRGGVMNEGKTSPRLGL 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232993981 156 TGWPAVAEESIIARDILLAEHVGSRLHVCHLSTAGSVELIRWAKKRGVAVTAEVTPHHLLLTDELARGYDARFKVNPPLR 235
Cdd:COG0044 203 KGRPAEAEEEAVARDIALAEETGARLHIVHVSTAEAVELIREAKARGLPVTAEVCPHHLTLTDEDLERYGTNFKVNPPLR 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232993981 236 TQEDVLAVREGLADGTIDIVATDHAPHPSEAKACEWQAAANGMVGLESALRVVHQSMVQTGLLDWTDVARVMSSAPARIG 315
Cdd:COG0044 283 TEEDREALWEGLADGTIDVIATDHAPHTLEEKELPFAEAPNGIPGLETALPLLLTELVHKGRLSLERLVELLSTNPARIF 362
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232993981 316 SLPGHGTpIAAGQPAEFTLYDADAVGVFAESDLHGQSTNSPYLGRDLPGKVLWTVHHGYTTLEDGVLAER 385
Cdd:COG0044 363 GLPRKGR-IAVGADADLVLFDPDAEWTVTAEDLHSKSKNTPFEGRELTGRVVATIVRGRVVYEDGEVVGE 431
|
|
| DHOase_IIa |
cd01317 |
Dihydroorotase (DHOase), subgroup IIa; DHOases catalyze the reversible interconversion of ... |
1-369 |
1.98e-152 |
|
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: 435.13 E-value: 1.98e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232993981 1 MVALPGLVDLHTHLREPGYEASETVLSGTRAAAAGGFTAVFAMPNTSPVADSAGVVEQELALGEAAGYATVQPIGAVTVG 80
Cdd:cd01317 10 KILAPGLVDLHVHLREPGFEYKETLESGAKAAAAGGFTTVVCMPNTNPVIDNPAVVELLKNRAKDVGIVRVLPIGALTKG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232993981 81 QKGERLAELGAMASsrANVRVFSDDGFCVWDPLIMRRALEYVKAFDGVIAQHAQDPRLTEGAQLNEGAVSAELGLTGWPA 160
Cdd:cd01317 90 LKGEELTEIGELLE--AGAVGFSDDGKPIQDAELLRRALEYAAMLDLPIIVHPEDPSLAGGGVMNEGKVASRLGLPGIPP 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232993981 161 VAEESIIARDILLAEHVGSRLHVCHLSTAGSVELIRWAKKRGVAVTAEVTPHHLLLTDELARGYDARFKVNPPLRTQEDV 240
Cdd:cd01317 168 EAETIMVARDLELAEATGARVHFQHLSTARSLELIRKAKAKGLPVTAEVTPHHLLLDDEALESYDTNAKVNPPLRSEEDR 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232993981 241 LAVREGLADGTIDIVATDHAPHPSEAKACEWQAAANGMVGLESALRVVHQSMVQTGLLDWTDVARVMSSAPARIGSLPgh 320
Cdd:cd01317 248 EALIEALKDGTIDAIASDHAPHTDEEKDLPFAEAPPGIIGLETALPLLWTLLVKGGLLTLPDLIRALSTNPAKILGLP-- 325
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 1232993981 321 GTPIAAGQPAEFTLYDADAVGVFAESDLHGQSTNSPYLGRDLPGKVLWT 369
Cdd:cd01317 326 PGRLEVGAPADLVLFDPDAEWIVDEETFRSKSKNTPFDGQKLKGRVLAT 374
|
|
| pyrC_multi |
TIGR00857 |
dihydroorotase, multifunctional complex type; In contrast to the homodimeric type of ... |
2-379 |
1.44e-139 |
|
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: 403.75 E-value: 1.44e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232993981 2 VALPGLVDLHTHLREPGYEASETVLSGTRAAAAGGFTAVFAMPNTSPVADSAGVVEQELALGEAAGYATVQPIGAVTVGQ 81
Cdd:TIGR00857 36 LVLPGFIDLHVHLRDPGEEYKEDIESGSKAAAHGGFTTVADMPNTKPPIDTPETLEWKLQRLKKVSLVDVHLYGGVTQGN 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232993981 82 KGERLAELGAMASSRANVRVFSDDGFCVWDPLIMRRALEYVKAFDGVIAQHAQDPRLTEGAQLNEGAVSAELGLTGWPAV 161
Cdd:TIGR00857 116 QGKELTEAYELKEAGAVGRMFTDDGSEVQDILSMRRALEYAAIAGVPIALHAEDPDLIYGGVMHEGPSAAQLGLPARPPE 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232993981 162 AEESIIARDILLAEHVGSRLHVCHLSTAGSVELIRWAKKRGVAVTAEVTPHHLLLTDELARGYDARFKVNPPLRTQEDVL 241
Cdd:TIGR00857 196 AEEVAVARLLELAKHAGCPVHICHISTKESLELIVKAKSQGIKITAEVTPHHLLLSEEDVARLDGNGKVNPPLREKEDRL 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232993981 242 AVREGLADGTIDIVATDHAPHPSEAKACEWQAAANGMVGLESALRVVHQSMVQtGLLDWTDVARVMSSAPARIGSLPGHG 321
Cdd:TIGR00857 276 ALIEGLKDGIIDIIATDHAPHTLEEKTKEFAAAPPGIPGLETALPLLLQLLVK-GLISLKDLIRMLSINPARIFGLPDKG 354
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 1232993981 322 TpIAAGQPAEFTLYDADAVGVFAESDLHGQSTNSPYLGRDLPGKVLWTVHHGYTTLED 379
Cdd:TIGR00857 355 T-LEEGNPADITVFDLKKEWTINAETFYSKAKNTPFEGMSLKGKPIATILRGKVVYED 411
|
|
| PRK07369 |
PRK07369 |
dihydroorotase; Provisional |
5-367 |
8.55e-86 |
|
dihydroorotase; Provisional
Pssm-ID: 236002 [Multi-domain] Cd Length: 418 Bit Score: 266.47 E-value: 8.55e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232993981 5 PGLVDLHTHLREPGYEASETVLSGTRAAAAGGFTAVFAMPNTSPVADSAGVVEQELALGEAAGYATVQPIGAVTVGQKGE 84
Cdd:PRK07369 57 PGLVDLYSHSGEPGFEERETLASLAAAAAAGGFTRVAILPDTFPPLDNPATLARLQQQAQQIPPVQLHFWGALTLGGQGK 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232993981 85 RLAELGAMAssRANVRVFSDdGFCVWDPLIMRRALEYVKAFDGVIAQHAQDPRLTEGAQLNEGAVSAELGLTGWPAVAEE 164
Cdd:PRK07369 137 QLTELAELA--AAGVVGFTD-GQPLENLALLRRLLEYLKPLGKPVALWPCDRSLAGNGVMREGLLALRLGLPGDPASAET 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232993981 165 SIIARDILLAEHVGSRLHVCHLSTAGSVELIRWAKKRGVAVTAEVTPHHLLLTDELARGYDARFKVNPPLRTQEDVLAVR 244
Cdd:PRK07369 214 TALAALLELVAAIGTPVHLMRISTARSVELIAQAKARGLPITASTTWMHLLLDTEALASYDPNLRLDPPLGNPSDRQALI 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232993981 245 EGLADGTIDIVATDHAPHPSEAKACEWQAAANGMVGLESALRVVHQSMVQTGLLDWTDVARVMSSAPARIGSLPghGTPI 324
Cdd:PRK07369 294 EGVRTGVIDAIAIDHAPYTYEEKTVAFAEAPPGAIGLELALPLLWQNLVETGELSALQLWQALSTNPARCLGQE--PPSL 371
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 1232993981 325 AAGQPAEFTLYDADAVGVFAESDLHGQSTNSPYLGRDLPGKVL 367
Cdd:PRK07369 372 APGQPAELILFDPQKTWTVSAQTLHSLSRNTPWLGQTLKGRVL 414
|
|
| PRK09059 |
PRK09059 |
dihydroorotase; Validated |
1-378 |
4.00e-85 |
|
dihydroorotase; Validated
Pssm-ID: 181631 [Multi-domain] Cd Length: 429 Bit Score: 265.36 E-value: 4.00e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232993981 1 MVALPGLVDLHTHLREPGYEASETVLSGTRAAAAGGFTAVFAMPNTSPVADSAGVVEQELALGEAAGYATVQPIGAVTVG 80
Cdd:PRK09059 56 KAVAPGLVDARVFVGEPGAEHRETIASASRAAAAGGVTSIIMMPDTDPVIDDVALVEFVKRTARDTAIVNIHPAAAITKG 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232993981 81 QKGERLAELGAMASsrANVRVFSDDGFCVWDPLIMRRALEYVKAFDGVIAQHAQDPRLTEGAQLNEGAVSAELGLTGWPA 160
Cdd:PRK09059 136 LAGEEMTEFGLLRA--AGAVAFTDGRRSVANTQVMRRALTYARDFDAVIVHETRDPDLGGNGVMNEGLFASWLGLSGIPR 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232993981 161 VAEESIIARDILLAEHVGSRLHVCHLSTAGSVELIRWAKKRGVAVTAEVTPHHLLLTDELARGYDARFKVNPPLRTQEDV 240
Cdd:PRK09059 214 EAEVIPLERDLRLAALTRGRYHAAQISCAESAEALRRAKDRGLKVTAGVSINHLSLNENDIGEYRTFFKLSPPLRTEDDR 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232993981 241 LAVREGLADGTIDIVATDHAPHPSEAKACEWQAAANGMVGLES----ALRVVHqsmvqTGLLDWTDVARVMSSAPARIGS 316
Cdd:PRK09059 294 VAMVEAVASGTIDIIVSSHDPQDVDTKRLPFSEAAAGAIGLETllaaALRLYH-----NGEVPLLRLIEALSTRPAEIFG 368
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1232993981 317 LPGhGTpIAAGQPAEFTLYDADAVGVFAESDLHGQSTNSPYLGRDLPGKVLWTVHHGYTTLE 378
Cdd:PRK09059 369 LPA-GT-LKPGAPADIIVIDLDEPWVVDPEDLKSRSKNTPFEEARFQGRVVRTIVAGKTVYE 428
|
|
| DHOase_IIb |
cd01318 |
Dihydroorotase (DHOase), subgroup IIb; DHOases catalyze the reversible interconversion of ... |
2-370 |
1.05e-80 |
|
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: 251.48 E-value: 1.05e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232993981 2 VALPGLVDLHTHLREPGYEASETVLSGTRAAAAGGFTAVFAMPNTSPVADSAGVVEQELALGEAAGYATVQPIGAVTVGQ 81
Cdd:cd01318 3 LILPGVIDIHVHFREPGLTYKEDFVSGSRAAAAGGVTTVMDMPNTKPPTTTAEALYEKLRLAAAKSVVDYGLYFGVTGSE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232993981 82 KGERLAELGAmassrANVRVFSDDGfcVWDPLIMRRALEYV-KAFDGVIAQHAQDP-RLTEGAQLNEGAVSAELGLtgwP 159
Cdd:cd01318 83 DLEELDKAPP-----AGYKIFMGDS--TGDLLDDEETLERIfAEGSVLVTFHAEDEdRLRENRKELKGESAHPRIR---D 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232993981 160 AVAEESIIARDILLAEHVGSRLHVCHLSTAGSVELIRWAKKRgvaVTAEVTPHHLLLTDELARGYDARFKVNPPLRTQED 239
Cdd:cd01318 153 AEAAAVATARALKLARRHGARLHICHVSTPEELKLIKKAKPG---VTVEVTPHHLFLDVEDYDRLGTLGKVNPPLRSRED 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232993981 240 VLAVREGLADGTIDIVATDHAPHPSEAKACEWQAAANGMVGLESALRVVhQSMVQTGLLDWTDVARVMSSAPARIGSLPG 319
Cdd:cd01318 230 RKALLQALADGRIDVIASDHAPHTLEEKRKGYPAAPSGIPGVETALPLM-LTLVNKGILSLSRVVRLTSHNPARIFGIKN 308
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 1232993981 320 HGTpIAAGQPAEFTLYDADAVGVFAESDLHGQSTNSPYLGRDLPGKVLWTV 370
Cdd:cd01318 309 KGR-IAEGYDADLTVVDLKEERTIRAEEFHSKAGWTPFEGFEVTGFPVMTI 358
|
|
| PRK07627 |
PRK07627 |
dihydroorotase; Provisional |
1-379 |
3.09e-79 |
|
dihydroorotase; Provisional
Pssm-ID: 181059 [Multi-domain] Cd Length: 425 Bit Score: 249.98 E-value: 3.09e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232993981 1 MVALPGLVDLHTHLREPGYEASETVLSGTRAAAAGGFTAVFAMPNTSPVADSAGVVEQELALGEAAGYATVQPIGAVTVG 80
Cdd:PRK07627 51 LIVCPGLVDLSARLREPGYEYKATLESEMAAAVAGGVTSLVCPPDTDPVLDEPGLVEMLKFRARNLNQAHVYPLGALTVG 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232993981 81 QKGERLAELGAMAssRANVRVFSDDGFCVWDPLIMRRALEYVKAFDGVIAQHAQDPRLTEGAQLNEGAVSAELGLTGWPA 160
Cdd:PRK07627 131 LKGEVLTEMVELT--EAGCVGFSQANVPVVDTQVLLRALQYASTFGFTVWLRPLDAFLGRGGVAASGAVASRLGLSGVPV 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232993981 161 VAEESIIARDILLAEHVGSRLHVCHLSTAGSVELIRWAKKRGVAVTAEVTPHHLLLTDELARGYDARFKVNPPLRTQEDV 240
Cdd:PRK07627 209 AAETIALHTIFELMRVTGARVHLARLSSAAGVALVRAAKAEGLPVTCDVGVNHVHLIDVDIGYFDSQFRLDPPLRSQRDR 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232993981 241 LAVREGLADGTIDIVATDHAPHPSEAKACEWQAAANGMVGLESALRVVhqsmvqtglLDWTDVARV--------MSSAPA 312
Cdd:PRK07627 289 EAIRAALADGTIDAICSDHTPVDDDEKLLPFAEATPGATGLELLLPLT---------LKWADEAKVplaralarITSAPA 359
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1232993981 313 RIGSLP-GHgtpIAAGQPAEFTLYDADAVGVFAESDLHGQSTNSPYLGRDLPGKVLWTVHHGYTTLED 379
Cdd:PRK07627 360 RVLGLPaGR---LAEGAPADLCVFDPDAHWRVEPRALKSQGKNTPFLGYELPGRVRATLVAGQVAFER 424
|
|
| L-HYD_ALN |
cd01315 |
L-Hydantoinases (L-HYDs) and Allantoinase (ALN); L-Hydantoinases are a member of the ... |
2-380 |
2.92e-68 |
|
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: 222.16 E-value: 2.92e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232993981 2 VALPGLVDLHTHLREPGYEASETVLSGTRAAAAGGFTAVFAMP-NTSPVADSAGVVEQELALGEAAGYATVQPIGAVTVG 80
Cdd:cd01315 49 VVMPGLIDTHVHINEPGRTEWEGFETGTKAAAAGGITTIIDMPlNSIPPTTTVENLEAKLEAAQGKLHVDVGFWGGLVPG 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232993981 81 QkGERLAELGAmassrANVRVF-------SDDGFCVWDPLIMRRALEYVKAFDGVIAQHAQDPRLTEgaqlNEGAVSAEL 153
Cdd:cd01315 129 N-LDQLRPLDE-----AGVVGFkcflcpsGVDEFPAVDDEQLEEAMKELAKTGSVLAVHAENPEITE----ALQEQAKAK 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232993981 154 GLTGW-------PAVAEESIIARDILLAEHVGSRLHVCHLSTAGSVELIRWAKKRGVAVTAEVTPHHLLLTDELARGYDA 226
Cdd:cd01315 199 GKRDYrdylasrPVFTEVEAIQRILLLAKETGCRLHIVHLSSAEAVPLIREARAEGVDVTVETCPHYLTFTAEDVPDGGT 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232993981 227 RFKVNPPLRTQEDVLAVREGLADGTIDIVATDHAPHPSEAKACEWQ---AAANGMVGLESALRVVHQSMVQTGLLDWTDV 303
Cdd:cd01315 279 EFKCAPPIRDAANQEQLWEALENGDIDMVVSDHSPCTPELKLLGKGdffKAWGGISGLQLGLPVMLTEAVNKRGLSLEDI 358
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1232993981 304 ARVMSSAPARIGSLPGHGTPIAAGQPAEFTLYDADAVGVFAESDLHGQSTNSPYLGRDLPGKVLWTVHHGYTTLEDG 380
Cdd:cd01315 359 ARLMCENPAKLFGLSHQKGRIAVGYDADFVVWDPEEEFTVDAEDLYYKNKISPYVGRTLKGRVHATILRGTVVYQDG 435
|
|
| Cyclic_amidohydrolases |
cd01302 |
Cyclic amidohydrolases, including hydantoinase, dihydropyrimidinase, allantoinase, and ... |
2-366 |
1.03e-63 |
|
Cyclic amidohydrolases, including hydantoinase, dihydropyrimidinase, allantoinase, and dihydroorotase, are involved in the metabolism of pyrimidines and purines, sharing the property of hydrolyzing the cyclic amide bond of each substrate to the corresponding N-carbamyl amino acids. Allantoinases catalyze the degradation of purines, while dihydropyrimidinases and hydantoinases, a microbial counterpart of dihydropyrimidinase, are involved in pyrimidine degradation. Dihydroorotase participates in the de novo synthesis of pyrimidines.
Pssm-ID: 238627 [Multi-domain] Cd Length: 337 Bit Score: 206.86 E-value: 1.03e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232993981 2 VALPGLVDLHTHLREPG-YEASETVLSGTRAAAAGGFTAVFAMPNTSPvaDSAGVVEQELALGEAAGYATVQ---PIGAV 77
Cdd:cd01302 2 LVLPGFIDIHVHLRDPGgTTYKEDFESGSRAAAAGGVTTVIDMPNTGP--PPIDLPAIELKIKLAEESSYVDfsfHAGIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232993981 78 TVGQKGE--RLAELGA------MASSrANVRVFSDDGfcvwdpLIMRRALEYvKAFDGVIAQHAQdprltegaqlnegav 149
Cdd:cd01302 80 PGDVTDElkKLFDAGInslkvfMNYY-FGELFDVDDG------TLMRTFLEI-ASRGGPVMVHAE--------------- 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232993981 150 saelgltgwpavaeesiiaRDILLAEHVGSRLHVCHLSTAGSVELIRWAKKRGVAVTAEVTPHHLLLTDELARGYDARFK 229
Cdd:cd01302 137 -------------------RAAQLAEEAGANVHIAHVSSGEALELIKFAKNKGVKVTCEVCPHHLFLDESMLRLNGAWGK 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232993981 230 VNPPLRTQEDVLAVREGLADGTIDIVATDHAPHPSEAK--ACEWQAAANGMVGLESALRVVHQSMVQTGLLdWTDVARVM 307
Cdd:cd01302 198 VNPPLRSKEDREALWEGVKNGKIDTIASDHAPHSKEEKesGKDIWKAPPGFPGLETRLPILLTEGVKRGLS-LETLVEIL 276
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 1232993981 308 SSAPARIGSLPGHGTpIAAGQPAEFTLYDADAVGVFAESDLHGQSTNSPYLGRDLPGKV 366
Cdd:cd01302 277 SENPARIFGLYPKGT-IAVGYDADLVIVDPKKEWKVTAEEIESKADWTPFEGMEVTGKP 334
|
|
| PRK02382 |
PRK02382 |
dihydroorotase; Provisional |
1-368 |
8.12e-63 |
|
dihydroorotase; Provisional
Pssm-ID: 179417 [Multi-domain] Cd Length: 443 Bit Score: 207.97 E-value: 8.12e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232993981 1 MVALPGLVDLHTHLREPGYEASETVLSGTRAAAAGGFTAVFAMPNTSPVADSAGVVEQELALGEAAGYATVQPIGAVTVG 80
Cdd:PRK02382 50 MLLLPGGIDVHVHFREPGYTHKETWYTGSRSAAAGGVTTVVDQPNTDPPTVDGESFDEKAELAARKSIVDFGINGGVTGN 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232993981 81 -QKGERLAELGA-------MASSRANVRVFSDDgfcvwdpliMRRALEYVKAFDGVIAQHAQDP-RLTEGAQLNEGAVSA 151
Cdd:PRK02382 130 wDPLESLWERGVfalgeifMADSTGGMGIDEEL---------FEEALAEAARLGVLATVHAEDEdLFDELAKLLKGDADA 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232993981 152 ELGLTGWPAVAEESIIARDILLAEHVGSRLHVCHLSTAGSVELIRWAKkrgvaVTAEVTPHHLLLTDELARGYDARFKVN 231
Cdd:PRK02382 201 DAWSAYRPAAAEAAAVERALEVASETGARIHIAHISTPEGVDAARREG-----ITCEVTPHHLFLSRRDWERLGTFGKMN 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232993981 232 PPLRTQEDVLAVREGLADGTIDIVATDHAPHPSEAKACEWQAAANGMVGLESALRVVHQSmVQTGLLDWTDVARVMSSAP 311
Cdd:PRK02382 276 PPLRSEKRREALWERLNDGTIDVVASDHAPHTREEKDADIWDAPSGVPGVETMLPLLLAA-VRKNRLPLERVRDVTAANP 354
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1232993981 312 ARIGSLPGHGTpIAAGQPAEFTLYDADAVGVFAESDLHGQSTNSPYLGRD--------LPGKVLW 368
Cdd:PRK02382 355 ARIFGLDGKGR-IAEGYDADLVLVDPDAAREIRGDDLHSKAGWTPFEGMEgvfpeltmVRGTVVW 418
|
|
| allantoinase |
TIGR03178 |
allantoinase; This enzyme carries out the first step in the degradation of allantoin, a ... |
2-380 |
1.21e-58 |
|
allantoinase; This enzyme carries out the first step in the degradation of allantoin, a ring-opening hydrolysis. The seed members of this model are all in the vicinity of other genes involved in the processes of xanthine/urate/allantoin catabolism. Although not included in the seed, many eukaryotic homologs of this family are included above the trusted cutoff. Below the noise cutoff are related hydantoinases.
Pssm-ID: 163175 [Multi-domain] Cd Length: 443 Bit Score: 196.84 E-value: 1.21e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232993981 2 VALPGLVDLHTHLREPGYEASETVLSGTRAAAAGGFTAVFAMP-NTSPVADSAGVVEQELALGEAAGYATVQPIGAVTVG 80
Cdd:TIGR03178 48 VVFPGVVDTHVHINEPGRTEWEGFETGTRAAAAGGITTYIDMPlNSIPATTTRASLEAKFEAAKGKLAVDVGFWGGLVPY 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232993981 81 QkgerLAELGAMASS-----RANVRVFSDDGFCVWDPLIMRRALEYVKAFDGVIAQHAQDP----RLTEGAQlNEGAVSA 151
Cdd:TIGR03178 128 N----LDDLRELDEAgvvgfKAFLSPSGDDEFPHVDDWQLYKGMRELARLGQLLLVHAENPaitsALGEEAP-PQGGVGA 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232993981 152 ELGLTGWPAVAEESIIARDILLAEHVGSRLHVCHLSTAGSVELIRWAKKRGVAVTAEVTPHHLLLT-DELARGyDARFKV 230
Cdd:TIGR03178 203 DAYLASRPVFAEVEAIRRTLALAKVTGCRVHVVHLSSAEAVELITEAKQEGLDVTVETCPHYLTLTaEEVPDG-GTLAKC 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232993981 231 NPPLRTQEDVLAVREGLADGTIDIVATDHAPHPSEAKACEWQAAA-NGMVGLESALRVVHQSMVQTGLLDWTDVARVMSS 309
Cdd:TIGR03178 282 APPIRDLANQEGLWEALLNGLIDCVVSDHSPCTPDLKRAGDFFKAwGGIAGLQSTLDVMFDEAVQKRGLPLEDIARLMAT 361
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1232993981 310 APARIGSLPGHGTpIAAGQPAEFTLYDADAVGVFAESDLHGQSTNSPYLGRDLPGKVLWTVHHGYTTLEDG 380
Cdd:TIGR03178 362 NPAKRFGLAQKGR-IAPGKDADFVFVDPDESYTLTPDDLYYRHKVSPYVGRTIGGRVRATYLRGQCIYDDE 431
|
|
| PRK06189 |
PRK06189 |
allantoinase; Provisional |
4-380 |
1.39e-57 |
|
allantoinase; Provisional
Pssm-ID: 235732 [Multi-domain] Cd Length: 451 Bit Score: 194.15 E-value: 1.39e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232993981 4 LPGLVDLHTHLREPGYEASETVLSGTRAAAAGGFTAVFAMP-NTSPVADSAGVVEQELALGEAAGYATVQPIGAVTVGQK 82
Cdd:PRK06189 53 FPGMIDVHVHFNEPGRTHWEGFATGSAALAAGGCTTYFDMPlNSIPPTVTREALDAKAELARQKSAVDFALWGGLVPGNL 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232993981 83 GE--RLAELGA------MASSRANVRVFSDDgfcvwdpLIMRRALEYVKAFDGVIAQHAQDPRLTEGAQ---LNEGAVSA 151
Cdd:PRK06189 133 EHlrELAEAGVigfkafMSNSGTDEFRSSDD-------LTLYEGMKEIAALGKILALHAESDALTRHLTtqaRQQGKTDV 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232993981 152 ELGLTGWPAVAEESIIARDILLAEHVGSRLHVCHLSTAGSVELIRWAKKRGVAVTAEVTPHHLLLTDELARGYDARFKVN 231
Cdd:PRK06189 206 RDYLESRPVVAELEAVQRALLYAQETGCPLHFVHISSGKAVALIAEAKKRGVDVSVETCPHYLLFTEEDFERIGAVAKCA 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232993981 232 PPLRTQEDVLAVREGLADGTIDIVATDHAPHPSEAKACE-WQAAANGMVGLESALRVVHQSMVQTGLLDWTDVARVMSSA 310
Cdd:PRK06189 286 PPLRSRSQKEELWRGLLAGEIDMISSDHSPCPPELKEGDdFFLVWGGISGGQSTLLVMLTEGYIERGIPLETIARLLATN 365
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232993981 311 PARIGSLPGHGTpIAAGQPAEFTLYDADAVGVFAESDLHGQSTNSPYLGRDLPGKVLWTVHHGYTTLEDG 380
Cdd:PRK06189 366 PAKRFGLPQKGR-LEVGADADFVLVDLDETYTLTKEDLFYRHKQSPYEGRTFPGRVVATYLRGQCVYQDG 434
|
|
| PRK04250 |
PRK04250 |
dihydroorotase; Provisional |
2-388 |
6.34e-57 |
|
dihydroorotase; Provisional
Pssm-ID: 235265 [Multi-domain] Cd Length: 398 Bit Score: 191.14 E-value: 6.34e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232993981 2 VALPGLVDLHTHLREPGYEASETVLSGTRAAAAGGFTAVFAMPNTSPVADSAGVVEQELALGEAAGYATVQpIGAVTVGQ 81
Cdd:PRK04250 44 IILPGLIDVHVHLRDFEESYKETIESGTKAALHGGITLVFDMPNTKPPIMDEKTYEKRMRIAEKKSYADYA-LNFLIAGN 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232993981 82 KGE------RLAELGAMASSRAnvrVFSDDgFCVwdplimrralEYVKAfDGVIAQHAQDPRLTEGAQLNegavsaelgl 155
Cdd:PRK04250 123 CEKaeeikaDFYKIFMGASTGG---IFSEN-FEV----------DYACA-PGIVSVHAEDPELIREFPER---------- 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232993981 156 tgwPAVAEESIIARDILLAEHVGSRLHVCHLSTAGSVELIRwaKKRGVAVTAEVTPHHLLLTDELARgYDARFKVNPPLR 235
Cdd:PRK04250 178 ---PPEAEVVAIERALEAGKKLKKPLHICHISTKDGLKLIL--KSNLPWVSFEVTPHHLFLTRKDYE-RNPLLKVYPPLR 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232993981 236 TQEDVLAVREGLAdgTIDIVATDHAPHPSEAKacewQAAANGMVGLESALRVVhQSMVQTGLLDWTDVARVMSSAPARIG 315
Cdd:PRK04250 252 SEEDRKALWENFS--KIPIIASDHAPHTLEDK----EAGAAGIPGLETEVPLL-LDAANKGMISLFDIVEKMHDNPARIF 324
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1232993981 316 SLPGHGtpIAAGQPAEFTLYDADAVGVFAESDLHGQSTNSPYLGRDLPGKVLWTVHHGYTTLEDGVLAE--RGAR 388
Cdd:PRK04250 325 GIKNYG--IEEGNYANFAVFDMKKEWTIKAEELYTKAGWTPYEGFKLKGKVIMTILRGEVVMEDDEIIGkpRGVR 397
|
|
| PRK07575 |
PRK07575 |
dihydroorotase; Provisional |
4-380 |
2.04e-53 |
|
dihydroorotase; Provisional
Pssm-ID: 236055 [Multi-domain] Cd Length: 438 Bit Score: 182.95 E-value: 2.04e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232993981 4 LPGLVDLHTHLREPGYEASETVLSGTRAAAAGGFTAVFAMPNTSPVADSAGVVEQELALgeAAGYATVQPigAVTVGQKG 83
Cdd:PRK07575 55 LPGVIDPQVHFREPGLEHKEDLFTASRACAKGGVTSFLEMPNTKPLTTTQAALDDKLAR--AAEKCVVNY--GFFIGATP 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232993981 84 ERLAELGA----------MASSRANVRVfsdDGFCVWDPLIMRRALeyvkafdgVIAQHAQD-PRLTEGAQLnegavsae 152
Cdd:PRK07575 131 DNLPELLTanptcgikifMGSSHGPLLV---DEEAALERIFAEGTR--------LIAVHAEDqARIRARRAE-------- 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232993981 153 lgLTGWPAVAEESII----------ARDILLAEHVGSRLHVCHLSTAGSVELIRWAKkrGVAVTAEVTPHHLLL-TDELA 221
Cdd:PRK07575 192 --FAGISDPADHSQIqdeeaallatRLALKLSKKYQRRLHILHLSTAIEAELLRQDK--PSWVTAEVTPQHLLLnTDAYE 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232993981 222 RgYDARFKVNPPLRTQEDVLAVREGLADGTIDIVATDHAPHPSEAKACEWQAAANGMVGLESALRVVHQSMVQtGLLDWT 301
Cdd:PRK07575 268 R-IGTLAQMNPPLRSPEDNEALWQALRDGVIDFIATDHAPHTLEEKAQPYPNSPSGMPGVETSLPLMLTAAMR-GKCTVA 345
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1232993981 302 DVARVMSSAPARIGSLPGHGTpIAAGQPAEFTLYDADAVGVFAESDLHGQSTNSPYLGRDLPGKVLWTVHHGYTTLEDG 380
Cdd:PRK07575 346 QVVRWMSTAVARAYGIPNKGR-IAPGYDADLVLVDLNTYRPVRREELLTKCGWSPFEGWNLTGWPVTTIVGGQIVFDRG 423
|
|
| D-HYD |
cd01314 |
D-hydantoinases (D-HYD) also called dihydropyrimidases (DHPase) and related proteins; DHPases ... |
4-387 |
2.55e-51 |
|
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: 177.79 E-value: 2.55e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232993981 4 LPGLVDLHTHLREP--GYEASETVLSGTRAAAAGGFTAVFAMPNTSPVADSAGVVEQ--ELALGEAA---GYAtvqpiGA 76
Cdd:cd01314 50 LPGGIDPHTHLELPfmGTVTADDFESGTRAAAAGGTTTIIDFAIPNKGQSLLEAVEKwrGKADGKSVidyGFH-----MI 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232993981 77 VT-----VGQKGERLAELGA------MASsrANVRVFSDDGFCvwdpLIMRRALEYvkafdGVIAQ-HAQDPRLTegAQL 144
Cdd:cd01314 125 ITdwtdsVIEELPELVKKGIssfkvfMAY--KGLLMVDDEELL----DVLKRAKEL-----GALVMvHAENGDVI--AEL 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232993981 145 NEGAVSAelGLTGW-------PAVAEESIIARDILLAEHVGSRLHVCHLSTAGSVELIRWAKKRGVAVTAEVTPHHLLLT 217
Cdd:cd01314 192 QKKLLAQ--GKTGPeyhalsrPPEVEAEATARAIRLAELAGAPLYIVHVSSKEAADEIARARKKGLPVYGETCPQYLLLD 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232993981 218 DELARGYD---ARFKVNPPLRTQEDVLAVREGLADGTIDIVATDHAPHPSEAKA---CEWQAAANGMVGLESALRVVHQS 291
Cdd:cd01314 270 DSDYWKDWfegAKYVCSPPLRPKEDQEALWDGLSSGTLQTVGSDHCPFNFAQKArgkDDFTKIPNGVPGVETRMPLLWSE 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232993981 292 MVQTGLLDWTDVARVMSSAPARI-GSLPGHGTpIAAGQPAEFTLYDADAVGVFAESDLHGQSTNSPYLGRDLPGKVLWTV 370
Cdd:cd01314 350 GVAKGRITLEKFVELTSTNPAKIfGLYPRKGT-IAVGSDADLVIWDPNAEKTISADTHHHNVDYNIFEGMKVKGWPVVTI 428
|
410
....*....|....*...
gi 1232993981 371 HHGYTTLEDG-VLAERGA 387
Cdd:cd01314 429 SRGKVVVEDGeLVGEKGS 446
|
|
| PRK09060 |
PRK09060 |
dihydroorotase; Validated |
4-383 |
8.47e-47 |
|
dihydroorotase; Validated
Pssm-ID: 181632 [Multi-domain] Cd Length: 444 Bit Score: 165.48 E-value: 8.47e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232993981 4 LPGLVDLHTHLREPGYEASETVLSGTRAAAAGGFTAVFAMPNTSPVADSAGVVEQELALGEAAGYATVqpigAVTVG--- 80
Cdd:PRK09060 55 LPGVIDSQVHFREPGLEHKEDLETGSRAAVLGGVTAVFEMPNTNPLTTTAEALADKLARARHRMHCDF----AFYVGgtr 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232993981 81 QKGERLAEL----GA------MASSRANVRVFSDDGFCVWDPLIMRRAleyvkAFdgviaqHAQD-PRLTEGAQL-NEGA 148
Cdd:PRK09060 131 DNADELAELerlpGCagikvfMGSSTGDLLVEDDEGLRRILRNGRRRA-----AF------HSEDeYRLRERKGLrVEGD 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232993981 149 VSAElgltgwPAV--AEESIIA--RDILLAEHVGSRLHVCHLSTAGSVELIRWAKKRgvaVTAEVTPHHLLLTDELArgY 224
Cdd:PRK09060 200 PSSH------PVWrdEEAALLAtrRLVRLARETGRRIHVLHVSTAEEIDFLADHKDV---ATVEVTPHHLTLAAPEC--Y 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232993981 225 D---ARFKVNPPLRTQEDVLAVREGLADGTIDIVATDHAPHPSEAKACEWQAAANGMVGLESALRVV--HqsmVQTGLLD 299
Cdd:PRK09060 269 ErlgTLAQMNPPIRDARHRDGLWRGVRQGVVDVLGSDHAPHTLEEKAKPYPASPSGMTGVQTLVPIMldH---VNAGRLS 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232993981 300 WTDVARVMSSAPARIGSLPGHGTpIAAGQPAEFTLYDADAVGVFAESDLHGQSTNSPYLGRDLPGKVLWTVHHGYTTLED 379
Cdd:PRK09060 346 LERFVDLTSAGPARIFGIAGKGR-IAVGYDADFTIVDLKRRETITNEWIASRCGWTPYDGKEVTGWPVGTIVRGQRVMWD 424
|
....
gi 1232993981 380 GVLA 383
Cdd:PRK09060 425 GELV 428
|
|
| PLN02795 |
PLN02795 |
allantoinase |
2-385 |
2.78e-45 |
|
allantoinase
Pssm-ID: 178392 [Multi-domain] Cd Length: 505 Bit Score: 163.02 E-value: 2.78e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232993981 2 VALPGLVDLHTHLREPGYEASETVLSGTRAAAAGGFTAVFAMP-NTSPVADSAGVVEQELALGEAAGYATVQPIGAVTVG 80
Cdd:PLN02795 96 VVMPGLIDVHVHLNEPGRTEWEGFPTGTKAAAAGGITTLVDMPlNSFPSTTSVETLELKIEAAKGKLYVDVGFWGGLVPE 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232993981 81 QKG-----ERLAELGA------MASSRANvrvfsddGFCVWDPLIMRRALEYVKAFDGVIAQHAQDPRLTE-GAQLNEGA 148
Cdd:PLN02795 176 NAHnasvlEELLDAGAlglksfMCPSGIN-------DFPMTTATHIKAALPVLAKYGRPLLVHAEVVSPVEsDSRLDADP 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232993981 149 VSAELGLTGWPAVAEESIIARDILLAEHV-------GSRLHVCHLSTAG-SVELIRWAKKRGVAVTAEVTPHHLLLT-DE 219
Cdd:PLN02795 249 RSYSTYLKSRPPSWEQEAIRQLLEVAKDTrpggvaeGAHVHIVHLSDAEsSLELIKEAKAKGDSVTVETCPHYLAFSaEE 328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232993981 220 LARGyDARFKVNPPLRTQEDVLAVREGLADGTIDIVATDHAPHPSEAKACE---WQAAANGMVGLESALRVVHQSMVQTG 296
Cdd:PLN02795 329 IPDG-DTRYKCAPPIRDAANRELLWKALLDGDIDMLSSDHSPSPPDLKLLEegnFLRAWGGISSLQFVLPATWTAGRAYG 407
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232993981 297 lLDWTDVARVMSSAPARIGSLPGHGTpIAAGQPAEFTLYDADAVGVFAES--DLHGQSTNSPYLGRDLPGKVLWTVHHGY 374
Cdd:PLN02795 408 -LTLEQLARWWSERPAKLAGLDSKGA-IAPGKDADIVVWDPEAEFVLDESypIYHKHKSLSPYLGTKLSGKVIATFVRGN 485
|
410
....*....|.
gi 1232993981 375 TTLEDGVLAER 385
Cdd:PLN02795 486 LVFLEGKHAKQ 496
|
|
| PRK08417 |
PRK08417 |
metal-dependent hydrolase; |
4-366 |
1.25e-44 |
|
metal-dependent hydrolase;
Pssm-ID: 236262 [Multi-domain] Cd Length: 386 Bit Score: 158.33 E-value: 1.25e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232993981 4 LPGLVDLHTHLREPGYEASeTVLSGTRAAAAGGFTAVFAMPNTSPVADSAGVVE-QELALGEAAGyatvQPIGAVTVGQK 82
Cdd:PRK08417 29 LPALVDLNVSLKNDSLSSK-NLKSLENECLKGGVGSIVLYPDSTPAIDNEIALElINSAQRELPM----QIFPSIRALDE 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232993981 83 GERLAELGAMASSRANVRVFSDDgfcvWDPLIMRRALEYVKAFDGVIAQHAQDPRLTEGAQLNEGAVSAELGLTGWPAVA 162
Cdd:PRK08417 104 DGKLSNIATLLKKGAKALELSSD----LDANLLKVIAQYAKMLDVPIFCRCEDSSFDDSGVMNDGELSFELGLPGIPSIA 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232993981 163 EESIIARDILLAEHVGSRLHVCHLSTAGSVELIRWAKKRGVAVTAEVTPHHLLLTDELARGYDARFKVNPPLRTQEDVLA 242
Cdd:PRK08417 180 ETKEVAKMKELAKFYKNKVLFDTLALPRSLELLDKFKSEGEKLLKEVSIHHLILDDSACENFNTAAKLNPPLRSKEDRLA 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232993981 243 VREGLADGTIDIVATDHAPHPSEAKACEWQAAANGMVGLESALRVVHQSMVQTGLLDWTDVARVMSSAPARIGSLPghGT 322
Cdd:PRK08417 260 LLEALKEGKIDFLTSLHSAKSNSKKDLAFDEAAFGIDSICEYFSLCYTYLVKEGIITWSELSRFTSYNPAQFLGLN--SG 337
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 1232993981 323 PIAAGQPAEFTLYDadavgvfAESDLHGQSTNSPYLGRDLPGKV 366
Cdd:PRK08417 338 EIEVGKEADLVLFD-------PNESTIIDDNFSLYSGDELYGKI 374
|
|
| D-hydantoinase |
TIGR02033 |
D-hydantoinase; This model represents the D-hydantoinase (dihydropyrimidinase) which primarily ... |
4-387 |
1.15e-41 |
|
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: 152.15 E-value: 1.15e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232993981 4 LPGLVDLHTHLREP--GYEASETVLSGTRAAAAGGFTAV--FAMPNTSPVADSAGVVEQELALGEAA-GYATVQPIGAVT 78
Cdd:TIGR02033 50 LPGGIDVHTHLEMPfgGTTTADDFFTGTKAAAAGGTTTIidFVVPEKGSSLTEALETWHEKAEGKSViDYGFHMDITHWN 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232993981 79 VGQKGERLAELGAMASSRANVRVFSDDGFCVWDPLIMRrALEYVKAFDGVIAQHAQDprlteGAQLNEGAVSA-ELGLTG 157
Cdd:TIGR02033 130 DSVLEEHIPEVKEEGINSFKVFMAYKNLLMVDDEELFE-ILKRLKELGALLQVHAEN-----GDIIAELQARMlAQGITG 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232993981 158 -------WPAVAEESIIARDILLAEHVGSRLHVCHLSTAGSVELIRWAKKRGVAVTAEVTPHHLLLTDELargYD----- 225
Cdd:TIGR02033 204 peyhalsRPPELEAEAVARAITLAALADAPLYVVHVSTKDAADEIAQARKKGQPVFGETCPQYLVLDDTH---YDkpgfe 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232993981 226 -ARFKVNPPLRTQEDVLAVREGLADGTIDIVATDHAPHPSEAK----ACEWQAAANGMVGLESALRVVHQSMVQTGLLDW 300
Cdd:TIGR02033 281 gAKYVCSPPLREPEDQDALWSALSSGALQTVGSDHCTFNFAQKkaigKDDFTKIPNGGPGVEERMSLLFDEGVAKGRITL 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232993981 301 TDVARVMSSAPARIGSL-PGHGTpIAAGQPAEFTLYDADAVGVFAESDLHGQSTNSPYLGRDLPGKVLWTVHHGYTTLED 379
Cdd:TIGR02033 361 EKFVEVTSTNPAKIFNLyPRKGT-IAVGSDADIVIWDPNRTTVISAETHHSNADYNPFEGFKVRGAPVSVLSRGRVVVED 439
|
....*....
gi 1232993981 380 G-VLAERGA 387
Cdd:TIGR02033 440 GqLVGTAGA 448
|
|
| PRK08044 |
PRK08044 |
allantoinase AllB; |
1-373 |
3.40e-41 |
|
allantoinase AllB;
Pssm-ID: 169193 [Multi-domain] Cd Length: 449 Bit Score: 150.78 E-value: 3.40e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232993981 1 MVALPGLVDLHTHLREPGYEASETVLSGTRAAAAGGFTAVFAMP-NTSPVADSAGVVEQELALGEAAGYATVQPIGAVtV 79
Cdd:PRK08044 49 LVVSPGMVDAHTHISEPGRSHWEGYETGTRAAAKGGITTMIEMPlNQLPATVDRASIELKFDAAKGKLTIDAAQLGGL-V 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232993981 80 GQKGERLAEL--GAMASSRANVRVFSDDG----FCVWDPLIMRRALEYVKAFDGVIAQHAQDPRLTE--GAQL-NEGAVS 150
Cdd:PRK08044 128 SYNLDRLHELdeVGVVGFKCFVATCGDRGidndFRDVNDWQFYKGAQKLGELGQPVLVHCENALICDelGEEAkREGRVT 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232993981 151 AELGLTGWPAVAEESIIARDILLAEHVGSRLHVCHLSTAGSVELIRWAKKRGVAVTAEVTPHHLLLTDELARGYDARFKV 230
Cdd:PRK08044 208 AHDYVASRPVFTEVEAIRRVLYLAKVAGCRLHVCHISSPEGVEEVTRARQEGQDVTCESCPHYFVLDTDQFEEIGTLAKC 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232993981 231 NPPLRTQEDVLAVREGLADGTIDIVATDHAPHPSEAKACEWQAAANGMVGLESALRVVHQSMVQTGLLDWTDVARVMSSA 310
Cdd:PRK08044 288 SPPIRDLENQKGMWEKLFNGEIDCLVSDHSPCPPEMKAGNIMEAWGGIAGLQNCMDVMFDEAVQKRGMSLPMFGKLMATN 367
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1232993981 311 PARIGSLPGHGTpIAAGQPAEFTLYDADAVGVFAESDLHGQSTNSPYLGRDLPGKVLWTVHHG 373
Cdd:PRK08044 368 AADIFGLQQKGR-IAPGKDADFVFIQPNSSYVLKNEDLEYRHKVSPYVGRTIGARITKTILRG 429
|
|
| CAD_DHOase |
cd01316 |
The eukaryotic CAD protein is a trifunctional enzyme of carbamoylphosphate ... |
2-386 |
3.68e-41 |
|
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: 148.37 E-value: 3.68e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232993981 2 VALPGLVDLHTHLREPGYEASETVLSGTRAAAAGGFTAVFAMPNTSPVADSAGVVEQELALGEAAGYATVqpigAVTVGQ 81
Cdd:cd01316 3 IRLPGLIDVHVHLREPGATHKEDFASGTKAALAGGFTMVRAMPNTNPSIVDVASLKLVQSLAQAKARCDY----AFSIGA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232993981 82 KGERLAELGAMASSRANVRVFSDDGFcvwDPLIMRRAleyvkafdGVIAQHaqdprltegaqlnegavsaelgLTGWPAV 161
Cdd:cd01316 79 TSTNAATVGELASEAVGLKFYLNETF---STLILDKI--------TAWASH----------------------FNAWPST 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232993981 162 ------AEESIIARDILLAEHVGSRLHVCHLSTAGSVELIRWAKKRGVAVTAEVTPHHLLL-TDELARGydaRFKVNPPL 234
Cdd:cd01316 126 kpivthAKSQTLAAVLLLASLHNRSIHICHVSSKEEINLIRLAKARGLKVTCEVSPHHLFLsQDDLPRG---QYEVRPFL 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232993981 235 RTQEDVLAVREGLAdgTIDIVATDHAPHPSEAKACEwqAAANGMVGLESALRVVHQSmVQTGLLDWTDVARVMSSAPARI 314
Cdd:cd01316 203 PTREDQEALWENLD--YIDCFATDHAPHTLAEKTGN--KPPPGFPGVETSLPLLLTA-VHEGRLTIEDIVDRLHTNPKRI 277
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1232993981 315 GSLPghgtpiaaGQPAEFTLYDADAVGVFAESDLHGQSTNSPYLGRDLPGKVLWTVHHGYTTLEDG-VLAERG 386
Cdd:cd01316 278 FNLP--------PQSDTYVEVDLDEEWTIPKNPLQSKKGWTPFEGKKVKGKVQRVVLRGETAFIDGeIVAPPG 342
|
|
| PRK08323 |
PRK08323 |
phenylhydantoinase; Validated |
4-387 |
1.06e-37 |
|
phenylhydantoinase; Validated
Pssm-ID: 236240 [Multi-domain] Cd Length: 459 Bit Score: 141.46 E-value: 1.06e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232993981 4 LPGLVDLHTHLREP--GYEASETVLSGTRAAAAGGFTAV--FAMPNTSPVADSAGVVEQELALGEAAG-YATVQPIGAVT 78
Cdd:PRK08323 48 MPGGIDPHTHMEMPfgGTVSSDDFETGTRAAACGGTTTIidFALQPKGQSLREALEAWHGKAAGKAVIdYGFHMIITDWN 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232993981 79 VgqkgERLAELGAMA----SSranVRVF--------SDDGfcvwdplIMRRALEYVKAFDGVIAQHAqdprltEG----A 142
Cdd:PRK08323 128 E----VVLDEMPELVeegiTS---FKLFmaykgalmLDDD-------ELLRALQRAAELGALPMVHA------ENgdaiA 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232993981 143 QLNEGAVSAelGLTG-------WPAVAEESIIARDILLAEHVGSRLHVCHLSTAGSVELIRWAKKRGVAVTAEVTPHHLL 215
Cdd:PRK08323 188 YLQAKLLAE--GKTGpeyhalsRPPEVEGEATNRAIMLAELAGAPLYIVHVSCKEALEAIRRARARGQRVFGETCPQYLL 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232993981 216 LTDELARGYD----ARFKVNPPLRTQEDVLAVREGLADGTIDIVATDHAPHPSEAKA---------CewqaaANGMVGLE 282
Cdd:PRK08323 266 LDESEYDGPDwfegAKYVMSPPLRDKEHQDALWRGLQDGDLQVVATDHCPFCFEQKKqlgrgdftkI-----PNGTPGVE 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232993981 283 SALRVVHQSMVQTGLLDWTDVARVMSSAPARIGSL-PGHGTpIAAGQPAEFTLYDADAVGVFAESDLHGQSTNSPYLGRD 361
Cdd:PRK08323 341 DRMPLLFSEGVMTGRITLNRFVELTSTNPAKIFGLyPRKGT-IAVGADADIVIWDPNATKTISASTLHSNVDYNPYEGFE 419
|
410 420
....*....|....*....|....*..
gi 1232993981 362 LPGKVLWTVHHGYTTLEDG-VLAERGA 387
Cdd:PRK08323 420 VTGWPVTTLSRGEVVVEDGeFRGKAGH 446
|
|
| PRK09236 |
PRK09236 |
dihydroorotase; Reviewed |
4-314 |
7.07e-37 |
|
dihydroorotase; Reviewed
Pssm-ID: 181716 Cd Length: 444 Bit Score: 138.85 E-value: 7.07e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232993981 4 LPGLVDLHTHLREPGYEASETVLSGTRAAAAGGFTAVFAMPNTSPVADSAGVVEQELALGEAAGYATVqpigAVTVGQKG 83
Cdd:PRK09236 53 LPGMIDDQVHFREPGLTHKGDIASESRAAVAGGITSFMEMPNTNPPTTTLEALEAKYQIAAQRSLANY----SFYFGATN 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232993981 84 ERLAELGAMASSR-ANVRVF---SDDGFCVWDPLIMRRALEYVKAfdgVIAQHAQDprlTEGAQLNEGAVSAELG--LTg 157
Cdd:PRK09236 129 DNLDEIKRLDPKRvCGVKVFmgaSTGNMLVDNPETLERIFRDAPT---LIATHCED---TPTIKANLAKYKEKYGddIP- 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232993981 158 wpaVAEESIIaRD-----------ILLAEHVGSRLHVCHLSTAGSVELIRWAKKRGVAVTAEVTPHHLLLTDELARGYDA 226
Cdd:PRK09236 202 ---AEMHPLI-RSaeacykssslaVSLAKKHGTRLHVLHISTAKELSLFENGPLAEKRITAEVCVHHLWFDDSDYARLGN 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232993981 227 RFKVNPPLRTQEDVLAVREGLADGTIDIVATDHAPHPSEAKACE-WQAAANG-MV--GLESALRVVHQsmvqtGLLDWTD 302
Cdd:PRK09236 278 LIKCNPAIKTASDREALRQALADDRIDVIATDHAPHTWEEKQGPyFQAPSGLpLVqhALPALLELVHE-----GKLSLEK 352
|
330
....*....|..
gi 1232993981 303 VARVMSSAPARI 314
Cdd:PRK09236 353 VVEKTSHAPAIL 364
|
|
| PRK13404 |
PRK13404 |
dihydropyrimidinase; Provisional |
1-386 |
6.02e-34 |
|
dihydropyrimidinase; Provisional
Pssm-ID: 184033 [Multi-domain] Cd Length: 477 Bit Score: 131.36 E-value: 6.02e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232993981 1 MVALPGLVDLHTHLREP---GYEASETVLSGTRAAAAGGFTAV--FAMPNTSPVADSAGVVEQELALGEAA-GYATVQPI 74
Cdd:PRK13404 50 RLVLPGGVDSHCHIDQPsgdGIMMADDFYTGTVSAAFGGTTTVipFAAQHRGQSLREAVEDYHRRAAGKAViDYAFHLIV 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232993981 75 GAVTVGQKGERLAELgaMASSRANVRVF-SDDGFCVWDPLIMRrALEYVKAFDGVIAQHAQdprltegaqlNEGAVS--- 150
Cdd:PRK13404 130 ADPTEEVLTEELPAL--IAQGYTSFKVFmTYDDLKLDDRQILD-VLAVARRHGAMVMVHAE----------NHDMIAwlt 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232993981 151 ---AELGLTG-------WPAVAEESIIARDILLAEHVGSRLHVCHLSTAGSVELIRWAKKRGVAVTAEVTPHHLLLT-DE 219
Cdd:PRK13404 197 krlLAAGLTApkyhaisRPMLAEREATHRAIALAELVDVPILIVHVSGREAAEQIRRARGRGLKIFAETCPQYLFLTaED 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232993981 220 LAR-GYD-ARFKVNPPLRTQEDVLAVREGLADGTIDIVATDHAPHPSEAKACE--------WQAAANGMVGLESALRVVH 289
Cdd:PRK13404 277 LDRpGMEgAKYICSPPPRDKANQEAIWNGLADGTFEVFSSDHAPFRFDDTDGKlaaganpsFKAIANGIPGIETRLPLLF 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232993981 290 QSMVQTGLLDWTDVARVMSSAPARI-GSLPGHGTpIAAGQPAEFTLYDADAVGVFAESDLHGQSTNSPYLGRDLPGKVLW 368
Cdd:PRK13404 357 SEGVVKGRISLNRFVALTSTNPAKLyGLYPRKGA-IAIGADADIAIWDPDREVTITNADLHHAADYTPYEGMRVTGWPVT 435
|
410
....*....|....*....
gi 1232993981 369 TVHHGYTTLEDGVL-AERG 386
Cdd:PRK13404 436 VLSRGRVVVEDGELvAERG 454
|
|
| pyrC |
PRK00369 |
dihydroorotase; Provisional |
2-334 |
6.97e-32 |
|
dihydroorotase; Provisional
Pssm-ID: 234738 [Multi-domain] Cd Length: 392 Bit Score: 124.10 E-value: 6.97e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232993981 2 VALPGLVDLHTHLRepGYEAS--ETVLSGTRAAAAGGFTAVFAMPNTSPVADSAGVVEQELAlgEAAGYATVQPIGAVTV 79
Cdd:PRK00369 44 LILPGAIDLHVHLR--GLKLSykEDVASGTSEAAYGGVTLVADMPNTIPPLNTPEAITEKLA--ELEYYSRVDYFVYSGV 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232993981 80 GQKGERLAELGAmassrANVRVFSDDgfcvwdpLIMRRALEYVKAFDGVIAQHAQDPRLTEGAQLNEGAVSAELGltgwp 159
Cdd:PRK00369 120 TKDPEKVDKLPI-----AGYKIFPED-------LEREETFRVLLKSRKLKILHPEVPLALKSNRKLRRNCWYEIA----- 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232993981 160 avaeesiiardILLAEHVGSRLHVCHLSTAGSVeliRWAKKRGVavTAEVTPHHLLLtdelARGYDARFKVNPPLRTQED 239
Cdd:PRK00369 183 -----------ALYYVKDYQNVHITHASNPRTV---RLAKELGF--TVDITPHHLLV----NGEKDCLTKVNPPIRDINE 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232993981 240 VLAVREGLADgtIDIVATDHAPHPSEAKACEWQAAANGMVGLESALRVVHqSMVQTGLLDWTDVARVMSSAPARIGSLPg 319
Cdd:PRK00369 243 RLWLLQALSE--VDAIASDHAPHSSFEKLQPYEVCPPGIAALSFTPPFIY-TLVSKGILSIDRAVELISTNPARILGIP- 318
|
330
....*....|....*
gi 1232993981 320 hGTPIAAGQPAEFTL 334
Cdd:PRK00369 319 -YGEIKEGYRANFTV 332
|
|
| PLN02942 |
PLN02942 |
dihydropyrimidinase |
4-382 |
2.79e-30 |
|
dihydropyrimidinase
Pssm-ID: 178530 Cd Length: 486 Bit Score: 121.10 E-value: 2.79e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232993981 4 LPGLVDLHTHLREP--GYEASETVLSGTRAAAAGGFTAV--FAMPntspvadsagvVEQELAlgeaAGYATVqpigavtv 79
Cdd:PLN02942 56 MPGGIDPHTHLAMPfmGTETIDDFFSGQAAALAGGTTMHidFVIP-----------VNGNLL----AGYEAY-------- 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232993981 80 gqkgERLAELGAMassranvrvfsDDGFCV----WDPLIMRRALEYVK-----------AFDGVIAqhAQDPRLTEG-AQ 143
Cdd:PLN02942 113 ----EKKAEKSCM-----------DYGFHMaitkWDDTVSRDMETLVKekginsfkffmAYKGSLM--VTDELLLEGfKR 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232993981 144 LNE-GAVSA-----------------ELGLTG-------WPAVAEESIIARDILLAEHVGSRLHVCHLSTAGSVELIRWA 198
Cdd:PLN02942 176 CKSlGALAMvhaengdavfegqkrmiELGITGpeghalsRPPLLEGEATARAIRLAKFVNTPLYVVHVMSIDAMEEIARA 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232993981 199 KKRGVAVTAEVTPHHLLLTDELARGYD----ARFKVNPPLRTQEDVLAVREGLADGTIDIVATDHAPHPSEAKAC---EW 271
Cdd:PLN02942 256 RKSGQRVIGEPVVSGLVLDDSKLWDPDftiaSKYVMSPPIRPAGHGKALQAALSSGILQLVGTDHCPFNSTQKAFgkdDF 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232993981 272 QAAANGMVGLESALRVVHQSMVQTGLLDWTDVARVMSSAPARIGSLPGHGTPIAAGQPAEFTLYDADAVGVFAESDLHGQ 351
Cdd:PLN02942 336 RKIPNGVNGIEERMHLVWDTMVESGQISPTDYVRVTSTECAKIFNIYPRKGAILAGSDADIIILNPNSTFTISAKTHHSR 415
|
410 420 430
....*....|....*....|....*....|.
gi 1232993981 352 STNSPYLGRDLPGKVLWTVHHGYTTLEDGVL 382
Cdd:PLN02942 416 IDTNVYEGRRGKGKVEVTISQGRVVWENGEL 446
|
|
| PRK01211 |
PRK01211 |
dihydroorotase; Provisional |
4-361 |
5.69e-27 |
|
dihydroorotase; Provisional
Pssm-ID: 179247 [Multi-domain] Cd Length: 409 Bit Score: 110.72 E-value: 5.69e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232993981 4 LPGLVDLHTHLREPGYEASETVLSGTRAAAAGGFTAVFAMPNTSPVADSAGVVEQELALGEAAGYATVQpIGAVTVGQKG 83
Cdd:PRK01211 45 LPAATDIHVHFRTPGETEKEDFSTGTLSAIFGGTTFIMDMPNNNIPIKDYNAFSDKLGRVAPKAYVDFS-LYSMETGNNA 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232993981 84 ERLAELGAmassraNVRVFSDDGFCVWDPLIMRRALEYVKAFDGVIAQHAQDPRLTEGAQLNEGAVsaelgltgwpavaE 163
Cdd:PRK01211 124 LILDERSI------GLKVYMGGTTNTNGTDIEGGEIKKINEANIPVFFHAELSECLRKHQFESKNL-------------R 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232993981 164 ESIIAR----DILLAEHVGS----RLHVCHLStagSVELIRwakkrgvAVTAEVTPHHLLLTDELARGydARFKVNPPLR 235
Cdd:PRK01211 185 DHDLARpiecEIKAVKYVKNldlkTKIIAHVS---SIDVIG-------RFLREVTPHHLLLNDDMPLG--SYGKVNPPLR 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232993981 236 ---TQEDVLavrEGLADGTIDIVATDHAPHPSEAKAcEWQAAANGMVGLESalRV-VHQSMVQTGLLDWTDVARVMSSAP 311
Cdd:PRK01211 253 drwTQERLL---EEYISGRFDILSSDHAPHTEEDKQ-EFEYAKSGIIGVET--RVpLFLALVKKKILPLDVLYKTAIERP 326
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 1232993981 312 ARI-GSLPGHgtpIAAGQPAEFTLYDADAVGVFAESDLHGQSTNSPYLGRD 361
Cdd:PRK01211 327 ASLfGIKKGK---IEEGYDADFMAFDFTNIKKINDKRLHSKCPVSPFNGFD 374
|
|
| Amidohydro_1 |
pfam01979 |
Amidohydrolase family; This family of enzymes are a a large metal dependent hydrolase ... |
2-346 |
3.03e-12 |
|
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: 67.14 E-value: 3.03e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232993981 2 VALPGLVDLHTHLR--------EPGYEASETVLSGTRAAAAGGFTAVFAMPNTSPVADSA---GVVEQELALGEAAGYAT 70
Cdd:pfam01979 1 IVLPGLIDAHVHLEmgllrgipVPPEFAYEALRLGITTMLKSGTTTVLDMGATTSTGIEAlleAAEELPLGLRFLGPGCS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232993981 71 VQPIG----AVTVGQKGERLAE-LGAMASSRANVRV-------FSDDGfcvwdpliMRRALEYVKAFDGVIAQHAQDPRL 138
Cdd:pfam01979 81 LDTDGelegRKALREKLKAGAEfIKGMADGVVFVGLaphgaptFSDDE--------LKAALEEAKKYGLPVAIHALETKG 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232993981 139 TEGAQLNEGAVSAELGltGWPAVAEESIIARDILLAEHvgsrlHVCHLSTAGSVELIRWAKKRGVAvtaevtphHLLLTD 218
Cdd:pfam01979 153 EVEDAIAAFGGGIEHG--THLEVAESGGLLDIIKLILA-----HGVHLSPTEANLLAEHLKGAGVA--------HCPFSN 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232993981 219 ELARgydarfkvnpplrtqEDVLAVREGLADGTIDIVATDHaphpseakacewqAAANGMVGLESALRV-VHQSMVQTGL 297
Cdd:pfam01979 218 SKLR---------------SGRIALRKALEDGVKVGLGTDG-------------AGSGNSLNMLEELRLaLELQFDPEGG 269
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 1232993981 298 LDWTDVARVMSSAPARIGSLPGHGTPIAAGQPAEFTLYDADAVGVFAES 346
Cdd:pfam01979 270 LSPLEALRMATINPAKALGLDDKVGSIEVGKDADLVVVDLDPLAAFFGL 318
|
|
| DHOase |
pfam12890 |
Dihydro-orotase-like; This is a small family of dihydro-orotase-like proteins from various ... |
2-188 |
7.66e-10 |
|
Dihydro-orotase-like; This is a small family of dihydro-orotase-like proteins from various bacteria.
Pssm-ID: 315550 [Multi-domain] Cd Length: 142 Bit Score: 56.80 E-value: 7.66e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232993981 2 VALPGLVDLHTHLREPGYEASETVLsgtraaaaggfTAVFAMPNTSPVAdsagvveqelalgeaagyatvqpiGAVTVGQ 81
Cdd:pfam12890 3 LIVPGLAFLHVHLTAPSGEAQELKE-----------TTWAAYGVTFKAP------------------------AGITVED 47
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232993981 82 KGERlaelgamassranVRVFSDDGFCVWDPLIMRRALEYvKAFDGVIAQHAQDPRLTEGAQLNEGAVSAELGlTGWPAV 161
Cdd:pfam12890 48 DSEE-------------GFIFTNDTYYITIQLLEGEGMKK-SELDQELKAIATDDEVTNQSAVQDFELPQFYG-TQLKGN 112
|
170 180
....*....|....*....|....*..
gi 1232993981 162 AEESIIARDILLAEHVGSRLHVCHLST 188
Cdd:pfam12890 113 CETEHCVYSYLLAKAAGCGFYVSIIYT 139
|
|
| DHOase |
cd01294 |
Dihydroorotase (DHOase) catalyzes the reversible interconversion of carbamoyl aspartate to ... |
185-275 |
2.00e-07 |
|
Dihydroorotase (DHOase) catalyzes the reversible interconversion of carbamoyl aspartate to dihydroorotate, a key reaction in the pyrimidine biosynthesis. In contrast to the large polyfunctional CAD proteins of higher organisms, this group of DHOases is monofunctional and mainly dimeric.
Pssm-ID: 238619 Cd Length: 335 Bit Score: 52.29 E-value: 2.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232993981 185 HLSTAGSVELIRWAKKRgvaVTAEVTPHHLLLT-DELARGydarfKVNP-----P-LRTQEDVLAVREGLADGTIDI-VA 256
Cdd:cd01294 169 HITTADAVEYVKSCNEN---VAATITPHHLLLTrDDLLGG-----GLNPhlyckPvAKRPEDREALRKAATSGHPKFfLG 240
|
90
....*....|....*....
gi 1232993981 257 TDHAPHPSEAKACEWQAAA 275
Cdd:cd01294 241 SDSAPHPKSNKESSCGCAG 259
|
|
| metallo-dependent_hydrolases |
cd01292 |
Superfamily of metallo-dependent hydrolases (also called amidohydrolase superfamily) is a ... |
7-266 |
2.80e-07 |
|
Superfamily of metallo-dependent hydrolases (also called amidohydrolase superfamily) is a large group of proteins that show conservation in their 3-dimensional fold (TIM barrel) and in details of their active site. The vast majority of the members have a conserved metal binding site, involving four histidines and one aspartic acid residue. In the common reaction mechanism, the metal ion (or ions) deprotonate a water molecule for a nucleophilic attack on the substrate. The family includes urease alpha, adenosine deaminase, phosphotriesterase dihydroorotases, allantoinases, hydantoinases, AMP-, adenine and cytosine deaminases, imidazolonepropionase, aryldialkylphosphatase, chlorohydrolases, formylmethanofuran dehydrogenases and others.
Pssm-ID: 238617 [Multi-domain] Cd Length: 275 Bit Score: 51.57 E-value: 2.80e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232993981 7 LVDLHTHLREPGYE------------------ASETVLSGTRAAAAGGFTAVFAMPNTSPVADSAGVVEQ------ELAL 62
Cdd:cd01292 1 FIDTHVHLDGSALRgtrlnlelkeaeelspedLYEDTLRALEALLAGGVTTVVDMGSTPPPTTTKAAIEAvaeaarASAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232993981 63 GEAAGYATVQPIGAVTVGQKGE-RLAELGAMASSRAN-VRVFSDDGFCVWDPLIMRRALEYVKAFDGVIAQHAqdprlte 140
Cdd:cd01292 81 IRVVLGLGIPGVPAAVDEDAEAlLLELLRRGLELGAVgLKLAGPYTATGLSDESLRRVLEEARKLGLPVVIHA------- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232993981 141 gaqlnegavsaelGLTGWPAVAEESIIARDillaeHVGSRLHVCHlSTAGSVELIRWAKKRGVAVtaEVTPHHLLLTDel 220
Cdd:cd01292 154 -------------GELPDPTRALEDLVALL-----RLGGRVVIGH-VSHLDPELLELLKEAGVSL--EVCPLSNYLLG-- 210
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1232993981 221 argydarfkvnpplRTQEDVLAVREGLADGTIDIVATDHAPHPSEA 266
Cdd:cd01292 211 --------------RDGEGAEALRRLLELGIRVTLGTDGPPHPLGT 242
|
|
| PRK09061 |
PRK09061 |
D-glutamate deacylase; Validated |
1-212 |
1.40e-03 |
|
D-glutamate deacylase; Validated
Pssm-ID: 236369 [Multi-domain] Cd Length: 509 Bit Score: 40.45 E-value: 1.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232993981 1 MVALPGLVDLHTHLREPGyeasetvlsGTRAAAAGGFTAVFAMP-NTSPVA---DSAGVVEQELALGEAAGYATVQPIGA 76
Cdd:PRK09061 67 LVVAPGFIDLHAHGQSVA---------AYRMQAFDGVTTALELEaGVLPVArwyAEQAGEGRPLNYGASVGWTPARIAVL 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232993981 77 VTVGQKGERLAELGAMASSRANVRVFSDDGFCVWDPLImRRALEYVKAFDGVIAQHAqdPRLTEGAQLNEGAVSAELGLT 156
Cdd:PRK09061 138 TGPQAEGTIADFGKALGDPRWQERAATPAELAEILELL-EQGLDEGALGIGIGAGYA--PGTGHKEYLELARLAARAGVP 214
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1232993981 157 GWPAVAEESII---------ARDILLAEHVGSRLHVCHL-STAGS-----VELIRWAKKRGVAVTAEVTPH 212
Cdd:PRK09061 215 TYTHVRYLSNVdprssvdayQELIAAAAETGAHMHICHVnSTSLRdidrcLALVEKAQAQGLDVTTEAYPY 285
|
|
| PLN02599 |
PLN02599 |
dihydroorotase |
172-299 |
4.29e-03 |
|
dihydroorotase
Pssm-ID: 178209 [Multi-domain] Cd Length: 364 Bit Score: 38.96 E-value: 4.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232993981 172 LLAEHVGSRLHVCHLSTAGSVELIRWAKKRGVAVTaeVTPHHLLLTDE--LARGYDARFKVNPPLRTQEDVLAVREGLAD 249
Cdd:PLN02599 180 LVQKLPQLKIVMEHITTMDAVEFVESCGDGNVAAT--VTPQHLLLNRNalFQGGLQPHNYCLPVLKREIHREALVKAATS 257
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1232993981 250 GTI-DIVATDHAPHPSEAKACEWQAAanGMVGLESALRVVHQSMVQTGLLD 299
Cdd:PLN02599 258 GSKkFFLGTDSAPHPKRAKEASCGCA--GIYSAPVALSLYAKAFEEAGALD 306
|
|
| |
