|
Name |
Accession |
Description |
Interval |
E-value |
| pyrC |
PRK09357 |
dihydroorotase; Validated |
18-438 |
0e+00 |
|
dihydroorotase; Validated
Pssm-ID: 236479 [Multi-domain] Cd Length: 423 Bit Score: 665.36 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765312 18 LLIKNIRLY---GEGEPTNVLIRGGVIDSIGPEVQADGAaETIDGGGNVLLPGLVDMHVHLREPGREDTETIESGSKAAA 94
Cdd:PRK09357 3 ILIKNGRVIdpkGLDEVADVLIDDGKIAAIGENIEAEGA-EVIDATGLVVAPGLVDLHVHLREPGQEDKETIETGSRAAA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765312 95 KGGFTAVFTMANTTPVTDQPIIAESVWAKSQALGLCDVHPVGSITKGLEGKSLTEFGMMArsDAKVRMFSDDGKCVQNPQ 174
Cdd:PRK09357 82 AGGFTTVVAMPNTKPVIDTPEVVEYVLDRAKEAGLVDVLPVGAITKGLAGEELTEFGALK--EAGVVAFSDDGIPVQDAR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765312 175 LMRRALEYAKGMDVLLAQHAEDDRMTGGSSAHEGENAARLGLRGWPRVAEESIVARDALLARDYGNRVHICHASTQGTVE 254
Cdd:PRK09357 160 LMRRALEYAKALDLLIAQHCEDPSLTEGGVMNEGEVSARLGLPGIPAVAEEVMIARDVLLAEATGARVHICHVSTAGSVE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765312 255 LLQWAKEHDIPLTAEVTPHHLLMTDDKLRTYDGLFRVNPPLREQRDTEALRQALLDGTIDCVATDHAPHGSEDKCVEFEN 334
Cdd:PRK09357 240 LIRWAKALGIKVTAEVTPHHLLLTDEDLLTYDPNYKVNPPLRTEEDREALIEGLKDGTIDAIATDHAPHAREEKECEFEA 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765312 335 ARPGMLGLESSLAVITKLFVETGLADWRFIARVMSERPAEITRLPghGRPLEVGEPANLTIVDPQHHWVSDSAQLASKSQ 414
Cdd:PRK09357 320 APFGITGLETALSLLYTTLVKTGLLDLEQLLEKMTINPARILGLP--AGPLAEGEPADLVIFDPEAEWTVDGEDFASKGK 397
|
410 420
....*....|....*....|....
gi 552765312 415 NNPYAGEEFGARVTHTILRGSVTF 438
Cdd:PRK09357 398 NTPFIGMKLKGKVVYTIVDGKIVY 421
|
|
| AllB |
COG0044 |
Dihydroorotase or related cyclic amidohydrolase [Nucleotide transport and metabolism]; ... |
19-439 |
0e+00 |
|
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: 538.91 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765312 19 LIKNIRLYGEG--EPTNVLIRGGVIDSIGPEVQADGAAETIDGGGNVLLPGLVDMHVHLREPGREDTETIESGSKAAAKG 96
Cdd:COG0044 1 LIKNGRVVDPGglERADVLIEDGRIAAIGPDLAAPEAAEVIDATGLLVLPGLIDLHVHLREPGLEHKEDIETGTRAAAAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765312 97 GFTAVFTMANTTPVTDQPIIAESVWAKSQALGLCDVHPVGSITKGLeGKSLTEFGMMARSDA---KVRMFSDDGKCVQNP 173
Cdd:COG0044 81 GVTTVVDMPNTNPVTDTPEALEFKLARAEEKALVDVGPHGALTKGL-GENLAELGALAEAGAvafKVFMGSDDGNPVLDD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765312 174 QLMRRALEYAKGMDVLLAQHAEDDRMTGGSSAHEGENAARLGLRGWPRVAEESIVARDALLARDYGNRVHICHASTQGTV 253
Cdd:COG0044 160 GLLRRALEYAAEFGALVAVHAEDPDLIRGGVMNEGKTSPRLGLKGRPAEAEEEAVARDIALAEETGARLHIVHVSTAEAV 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765312 254 ELLQWAKEHDIPLTAEVTPHHLLMTDDKLRTYDGLFRVNPPLREQRDTEALRQALLDGTIDCVATDHAPHGSEDKCVEFE 333
Cdd:COG0044 240 ELIREAKARGLPVTAEVCPHHLTLTDEDLERYGTNFKVNPPLRTEEDREALWEGLADGTIDVIATDHAPHTLEEKELPFA 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765312 334 NARPGMLGLESSLAVITKLFVETGLADWRFIARVMSERPAEITRLPGHGRpLEVGEPANLTIVDPQHHWVSDSAQLASKS 413
Cdd:COG0044 320 EAPNGIPGLETALPLLLTELVHKGRLSLERLVELLSTNPARIFGLPRKGR-IAVGADADLVLFDPDAEWTVTAEDLHSKS 398
|
410 420
....*....|....*....|....*.
gi 552765312 414 QNNPYAGEEFGARVTHTILRGSVTFD 439
Cdd:COG0044 399 KNTPFEGRELTGRVVATIVRGRVVYE 424
|
|
| pyrC_multi |
TIGR00857 |
dihydroorotase, multifunctional complex type; In contrast to the homodimeric type of ... |
27-437 |
1.88e-163 |
|
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: 466.53 E-value: 1.88e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765312 27 GEGEPTNVLIRGGVIDSIGpEVQADGAAETIDGGGNVLLPGLVDMHVHLREPGREDTETIESGSKAAAKGGFTAVFTMAN 106
Cdd:TIGR00857 1 GKETEVDILVEGGRIKKIG-KLRIPPDAEVIDAKGLLVLPGFIDLHVHLRDPGEEYKEDIESGSKAAAHGGFTTVADMPN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765312 107 TTPVTDQPIIAESVWAKSQALGLCDVHPVGSITKGLEGKSLTEFGMMARSDAKVRMFSDDGKCVQNPQLMRRALEYAKGM 186
Cdd:TIGR00857 80 TKPPIDTPETLEWKLQRLKKVSLVDVHLYGGVTQGNQGKELTEAYELKEAGAVGRMFTDDGSEVQDILSMRRALEYAAIA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765312 187 DVLLAQHAEDDRMTGGSSAHEGENAARLGLRGWPRVAEESIVARDALLARDYGNRVHICHASTQGTVELLQWAKEHDIPL 266
Cdd:TIGR00857 160 GVPIALHAEDPDLIYGGVMHEGPSAAQLGLPARPPEAEEVAVARLLELAKHAGCPVHICHISTKESLELIVKAKSQGIKI 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765312 267 TAEVTPHHLLMTDDKLRTYDGLFRVNPPLREQRDTEALRQALLDGTIDCVATDHAPHGSEDKCVEFENARPGMLGLESSL 346
Cdd:TIGR00857 240 TAEVTPHHLLLSEEDVARLDGNGKVNPPLREKEDRLALIEGLKDGIIDIIATDHAPHTLEEKTKEFAAAPPGIPGLETAL 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765312 347 AVITKLFVEtGLADWRFIARVMSERPAEITRLPGHGrPLEVGEPANLTIVDPQHHWVSDSAQLASKSQNNPYAGEEFGAR 426
Cdd:TIGR00857 320 PLLLQLLVK-GLISLKDLIRMLSINPARIFGLPDKG-TLEEGNPADITVFDLKKEWTINAETFYSKAKNTPFEGMSLKGK 397
|
410
....*....|.
gi 552765312 427 VTHTILRGSVT 437
Cdd:TIGR00857 398 PIATILRGKVV 408
|
|
| DHOase_IIa |
cd01317 |
Dihydroorotase (DHOase), subgroup IIa; DHOases catalyze the reversible interconversion of ... |
53-430 |
3.57e-161 |
|
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: 459.40 E-value: 3.57e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765312 53 AAETIDGGGNVLLPGLVDMHVHLREPGREDTETIESGSKAAAKGGFTAVFTMANTTPVTDQPIIAESVWAKSQALGLCDV 132
Cdd:cd01317 1 DAEVIDAEGKILAPGLVDLHVHLREPGFEYKETLESGAKAAAAGGFTTVVCMPNTNPVIDNPAVVELLKNRAKDVGIVRV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765312 133 HPVGSITKGLEGKSLTEFGMMArsDAKVRMFSDDGKCVQNPQLMRRALEYAKGMDVLLAQHAEDDRMTGGSSAHEGENAA 212
Cdd:cd01317 81 LPIGALTKGLKGEELTEIGELL--EAGAVGFSDDGKPIQDAELLRRALEYAAMLDLPIIVHPEDPSLAGGGVMNEGKVAS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765312 213 RLGLRGWPRVAEESIVARDALLARDYGNRVHICHASTQGTVELLQWAKEHDIPLTAEVTPHHLLMTDDKLRTYDGLFRVN 292
Cdd:cd01317 159 RLGLPGIPPEAETIMVARDLELAEATGARVHFQHLSTARSLELIRKAKAKGLPVTAEVTPHHLLLDDEALESYDTNAKVN 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765312 293 PPLREQRDTEALRQALLDGTIDCVATDHAPHGSEDKCVEFENARPGMLGLESSLAVITKLFVETGLADWRFIARVMSERP 372
Cdd:cd01317 239 PPLRSEEDREALIEALKDGTIDAIASDHAPHTDEEKDLPFAEAPPGIIGLETALPLLWTLLVKGGLLTLPDLIRALSTNP 318
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 552765312 373 AEITRLPGhGRpLEVGEPANLTIVDPQHHWVSDSAQLASKSQNNPYAGEEFGARVTHT 430
Cdd:cd01317 319 AKILGLPP-GR-LEVGAPADLVLFDPDAEWIVDEETFRSKSKNTPFDGQKLKGRVLAT 374
|
|
| PRK09059 |
PRK09059 |
dihydroorotase; Validated |
16-440 |
9.21e-103 |
|
dihydroorotase; Validated
Pssm-ID: 181631 [Multi-domain] Cd Length: 429 Bit Score: 312.74 E-value: 9.21e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765312 16 NPLLIKNIRLY----GEGEPTNVLIRGGVIDSIGPEVQADGA---AETIDGGGNVLLPGLVDMHVHLREPGREDTETIES 88
Cdd:PRK09059 3 RPILLANARIIdpsrGLDEIGTVLIEDGVIVAAGKGAGNQGApegAEIVDCAGKAVAPGLVDARVFVGEPGAEHRETIAS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765312 89 GSKAAAKGGFTAVFTMANTTPVTDQPIIAESVWAKSQALGLCDVHPVGSITKGLEGKSLTEFGMMarSDAKVRMFSDDGK 168
Cdd:PRK09059 83 ASRAAAAGGVTSIIMMPDTDPVIDDVALVEFVKRTARDTAIVNIHPAAAITKGLAGEEMTEFGLL--RAAGAVAFTDGRR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765312 169 CVQNPQLMRRALEYAKGMDVLLAQHAEDDRMTGGSSAHEGENAARLGLRGWPRVAEESIVARDALLARDYGNRVHICHAS 248
Cdd:PRK09059 161 SVANTQVMRRALTYARDFDAVIVHETRDPDLGGNGVMNEGLFASWLGLSGIPREAEVIPLERDLRLAALTRGRYHAAQIS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765312 249 TQGTVELLQWAKEHDIPLTAEVTPHHLLMTDDKLRTYDGLFRVNPPLREQRDTEALRQALLDGTIDCVATDHAPHGSEDK 328
Cdd:PRK09059 241 CAESAEALRRAKDRGLKVTAGVSINHLSLNENDIGEYRTFFKLSPPLRTEDDRVAMVEAVASGTIDIIVSSHDPQDVDTK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765312 329 CVEFENARPGMLGLESSLAVITKLfVETGLADWRFIARVMSERPAEITRLPGHgrPLEVGEPANLTIVDPQHHWVSDSAQ 408
Cdd:PRK09059 321 RLPFSEAAAGAIGLETLLAAALRL-YHNGEVPLLRLIEALSTRPAEIFGLPAG--TLKPGAPADIIVIDLDEPWVVDPED 397
|
410 420 430
....*....|....*....|....*....|..
gi 552765312 409 LASKSQNNPYAGEEFGARVTHTILRGSVTFDL 440
Cdd:PRK09059 398 LKSRSKNTPFEEARFQGRVVRTIVAGKTVYEL 429
|
|
| PRK07369 |
PRK07369 |
dihydroorotase; Provisional |
19-430 |
1.06e-91 |
|
dihydroorotase; Provisional
Pssm-ID: 236002 [Multi-domain] Cd Length: 418 Bit Score: 283.80 E-value: 1.06e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765312 19 LIKNIRL----YGEGEPTNVLIRGGVIDSIGP---EVQADgaAETIDGGGNVLLPGLVDMHVHLREPGREDTETIESGSK 91
Cdd:PRK07369 5 LLQQVRVldpvSNTDRIADVLIEDGKIQAIEPhidPIPPD--TQIIDASGLILGPGLVDLYSHSGEPGFEERETLASLAA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765312 92 AAAKGGFTAVFTMANTTPVTDQPIIAESVWAKSQALGLCDVHPVGSITKGLEGKSLTEFGMMARsdAKVRMFSDdGKCVQ 171
Cdd:PRK07369 83 AAAAGGFTRVAILPDTFPPLDNPATLARLQQQAQQIPPVQLHFWGALTLGGQGKQLTELAELAA--AGVVGFTD-GQPLE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765312 172 NPQLMRRALEYAKGMDVLLAQHAEDDRMTGGSSAHEGENAARLGLRGWPRVAEESIVARDALLARDYGNRVHICHASTQG 251
Cdd:PRK07369 160 NLALLRRLLEYLKPLGKPVALWPCDRSLAGNGVMREGLLALRLGLPGDPASAETTALAALLELVAAIGTPVHLMRISTAR 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765312 252 TVELLQWAKEHDIPLTAEVTPHHLLMTDDKLRTYDGLFRVNPPLREQRDTEALRQALLDGTIDCVATDHAPHGSEDKCVE 331
Cdd:PRK07369 240 SVELIAQAKARGLPITASTTWMHLLLDTEALASYDPNLRLDPPLGNPSDRQALIEGVRTGVIDAIAIDHAPYTYEEKTVA 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765312 332 FENARPGMLGLESSLAVITKLFVETG----LADWrfiaRVMSERPAEITRLPghGRPLEVGEPANLTIVDPQHHWVSDSA 407
Cdd:PRK07369 320 FAEAPPGAIGLELALPLLWQNLVETGelsaLQLW----QALSTNPARCLGQE--PPSLAPGQPAELILFDPQKTWTVSAQ 393
|
410 420
....*....|....*....|...
gi 552765312 408 QLASKSQNNPYAGEEFGARVTHT 430
Cdd:PRK07369 394 TLHSLSRNTPWLGQTLKGRVLQT 416
|
|
| PRK07627 |
PRK07627 |
dihydroorotase; Provisional |
18-439 |
4.08e-91 |
|
dihydroorotase; Provisional
Pssm-ID: 181059 [Multi-domain] Cd Length: 425 Bit Score: 282.72 E-value: 4.08e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765312 18 LLIKNIRLY----GEGEPTNVLIRGGVIDSIGPEVQADGAAETIDGGGNVLLPGLVDMHVHLREPGREDTETIESGSKAA 93
Cdd:PRK07627 3 IHIKGGRLIdpaaGTDRQADLYVAAGKIAAIGQAPAGFNADKTIDASGLIVCPGLVDLSARLREPGYEYKATLESEMAAA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765312 94 AKGGFTAVFTMANTTPVTDQPIIAESVWAKSQALGLCDVHPVGSITKGLEGKSLTEfgMMARSDAKVRMFSDDGKCVQNP 173
Cdd:PRK07627 83 VAGGVTSLVCPPDTDPVLDEPGLVEMLKFRARNLNQAHVYPLGALTVGLKGEVLTE--MVELTEAGCVGFSQANVPVVDT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765312 174 QLMRRALEYAKGMDVLLAQHAEDDRMTGGSSAHEGENAARLGLRGWPrVAEESIVARDAL-LARDYGNRVHICHASTQGT 252
Cdd:PRK07627 161 QVLLRALQYASTFGFTVWLRPLDAFLGRGGVAASGAVASRLGLSGVP-VAAETIALHTIFeLMRVTGARVHLARLSSAAG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765312 253 VELLQWAKEHDIPLTAEVTPHHLLMTDDKLRTYDGLFRVNPPLREQRDTEALRQALLDGTIDCVATDHAPHGSEDKCVEF 332
Cdd:PRK07627 240 VALVRAAKAEGLPVTCDVGVNHVHLIDVDIGYFDSQFRLDPPLRSQRDREAIRAALADGTIDAICSDHTPVDDDEKLLPF 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765312 333 ENARPGMLGLESSLAVITKLFVETGLADWRFIARVMSErPAEITRLP-GHgrpLEVGEPANLTIVDPQHHWVSDSAQLAS 411
Cdd:PRK07627 320 AEATPGATGLELLLPLTLKWADEAKVPLARALARITSA-PARVLGLPaGR---LAEGAPADLCVFDPDAHWRVEPRALKS 395
|
410 420
....*....|....*....|....*...
gi 552765312 412 KSQNNPYAGEEFGARVTHTILRGSVTFD 439
Cdd:PRK07627 396 QGKNTPFLGYELPGRVRATLVAGQVAFE 423
|
|
| DHOase_IIb |
cd01318 |
Dihydroorotase (DHOase), subgroup IIb; DHOases catalyze the reversible interconversion of ... |
61-434 |
1.96e-82 |
|
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: 258.03 E-value: 1.96e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765312 61 GNVLLPGLVDMHVHLREPGREDTETIESGSKAAAKGGFTAVFTMANTTPvtdQPIIAESVWAKsqaLGLCDVHPVGSITK 140
Cdd:cd01318 1 GLLILPGVIDIHVHFREPGLTYKEDFVSGSRAAAAGGVTTVMDMPNTKP---PTTTAEALYEK---LRLAAAKSVVDYGL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765312 141 GLEGKSLTEFGMMARSDA---KVRMFSDDGKCVQNPQLMRRALEYAKgmdVLLAQHAEDDRMTggsSAHEGENAARLGLR 217
Cdd:cd01318 75 YFGVTGSEDLEELDKAPPagyKIFMGDSTGDLLDDEETLERIFAEGS---VLVTFHAEDEDRL---RENRKELKGESAHP 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765312 218 GWPRvAEESIVARDALL--ARDYGNRVHICHASTQGTVELlqwAKEHDIPLTAEVTPHHLLMTDDKLRTYDGLFRVNPPL 295
Cdd:cd01318 149 RIRD-AEAAAVATARALklARRHGARLHICHVSTPEELKL---IKKAKPGVTVEVTPHHLFLDVEDYDRLGTLGKVNPPL 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765312 296 REQRDTEALRQALLDGTIDCVATDHAPHGSEDKCVEFENARPGMLGLESSLAVITKLFVETGLADWRFIaRVMSERPAEI 375
Cdd:cd01318 225 RSREDRKALLQALADGRIDVIASDHAPHTLEEKRKGYPAAPSGIPGVETALPLMLTLVNKGILSLSRVV-RLTSHNPARI 303
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 552765312 376 TRLPGHGRpLEVGEPANLTIVDPQHHWVSDSAQLASKSQNNPYAGEEFGARVTHTILRG 434
Cdd:cd01318 304 FGIKNKGR-IAEGYDADLTVVDLKEERTIRAEEFHSKAGWTPFEGFEVTGFPVMTIVRG 361
|
|
| L-HYD_ALN |
cd01315 |
L-Hydantoinases (L-HYDs) and Allantoinase (ALN); L-Hydantoinases are a member of the ... |
18-441 |
1.57e-81 |
|
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: 258.37 E-value: 1.57e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765312 18 LLIKNIRLY-GEGE-PTNVLIRGGVIDSIGPEVQADGAAETIDGGGNVLLPGLVDMHVHLREPGREDTETIESGSKAAAK 95
Cdd:cd01315 2 LVIKNGRVVtPDGVrEADIAVKGGKIAAIGPDIANTEAEEVIDAGGLVVMPGLIDTHVHINEPGRTEWEGFETGTKAAAA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765312 96 GGFTAVFTManttPVTDQP--IIAESVWAKSQALG---LCDVHPVGSITKGL--EGKSLTEFGMMA----RSDAKVRMFS 164
Cdd:cd01315 82 GGITTIIDM----PLNSIPptTTVENLEAKLEAAQgklHVDVGFWGGLVPGNldQLRPLDEAGVVGfkcfLCPSGVDEFP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765312 165 DdgkcVQNPQLMRrALEYAKGMDVLLAQHAEDDRMTggssAHEGENAARLGLRGW-------PRVAEESIVARDALLARD 237
Cdd:cd01315 158 A----VDDEQLEE-AMKELAKTGSVLAVHAENPEIT----EALQEQAKAKGKRDYrdylasrPVFTEVEAIQRILLLAKE 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765312 238 YGNRVHICHASTQGTVELLQWAKEHDIPLTAEVTPHHLLMTDDKLRTYDGLFRVNPPLREQRDTEALRQALLDGTIDCVA 317
Cdd:cd01315 229 TGCRLHIVHLSSAEAVPLIREARAEGVDVTVETCPHYLTFTAEDVPDGGTEFKCAPPIRDAANQEQLWEALENGDIDMVV 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765312 318 TDHAPHGSEDKCVEFEN---ARPGMLGLESSLAVITKLFVETGLADWRFIARVMSERPAEITRLPGHGRPLEVGEPANLT 394
Cdd:cd01315 309 SDHSPCTPELKLLGKGDffkAWGGISGLQLGLPVMLTEAVNKRGLSLEDIARLMCENPAKLFGLSHQKGRIAVGYDADFV 388
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 552765312 395 IVDPQHHWVSDSAQLASKSQNNPYAGEEFGARVTHTILRGSVTFDLN 441
Cdd:cd01315 389 VWDPEEEFTVDAEDLYYKNKISPYVGRTLKGRVHATILRGTVVYQDG 435
|
|
| PRK02382 |
PRK02382 |
dihydroorotase; Provisional |
18-439 |
3.17e-75 |
|
dihydroorotase; Provisional
Pssm-ID: 179417 [Multi-domain] Cd Length: 443 Bit Score: 241.87 E-value: 3.17e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765312 18 LLIKNIRLY--GEGEPTNVLIRGGVIDSIGPEVQADGAAETIDGGGNVLLPGLVDMHVHLREPGREDTETIESGSKAAAK 95
Cdd:PRK02382 4 ALLKDGRVYynNSLQPRDVRIDGGKITAVGKDLDGSSSEEVIDARGMLLLPGGIDVHVHFREPGYTHKETWYTGSRSAAA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765312 96 GGFTAVFTMANTTPVTdqpIIAESVWAK---SQALGLCDVHPVGSITKGLE-GKSLTEFGMMARSDakVRMFSDDGKCVQ 171
Cdd:PRK02382 84 GGVTTVVDQPNTDPPT---VDGESFDEKaelAARKSIVDFGINGGVTGNWDpLESLWERGVFALGE--IFMADSTGGMGI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765312 172 NPQLMRRALEYAKGMDVLLAQHAED-DRMTGGSSAHEGENAARLGLRGWPRVAEESIVARDALLARDYGNRVHICHASTQ 250
Cdd:PRK02382 159 DEELFEEALAEAARLGVLATVHAEDeDLFDELAKLLKGDADADAWSAYRPAAAEAAAVERALEVASETGARIHIAHISTP 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765312 251 GTVELLQWAKehdipLTAEVTPHHLLMTD---DKLRTYDglfRVNPPLREQRDTEALRQALLDGTIDCVATDHAPHGSED 327
Cdd:PRK02382 239 EGVDAARREG-----ITCEVTPHHLFLSRrdwERLGTFG---KMNPPLRSEKRREALWERLNDGTIDVVASDHAPHTREE 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765312 328 KCVEFENARPGMLGLESSLAVITKLFVETGLADWRFIaRVMSERPAEITRLPGHGRpLEVGEPANLTIVDPQHHWVSDSA 407
Cdd:PRK02382 311 KDADIWDAPSGVPGVETMLPLLLAAVRKNRLPLERVR-DVTAANPARIFGLDGKGR-IAEGYDADLVLVDPDAAREIRGD 388
|
410 420 430
....*....|....*....|....*....|..
gi 552765312 408 QLASKSQNNPYAGEEfGARVTHTILRGSVTFD 439
Cdd:PRK02382 389 DLHSKAGWTPFEGME-GVFPELTMVRGTVVWD 419
|
|
| allantoinase |
TIGR03178 |
allantoinase; This enzyme carries out the first step in the degradation of allantoin, a ... |
18-439 |
6.58e-75 |
|
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: 241.13 E-value: 6.58e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765312 18 LLIKNIRLYGEG--EPTNVLIRGGVIDSIGPEVQADGAaETIDGGGNVLLPGLVDMHVHLREPGREDTETIESGSKAAAK 95
Cdd:TIGR03178 2 LIIRGGRVILPNgeREADVGVKGGKIAAIGPDILGPAA-KIIDAGGLVVFPGVVDTHVHINEPGRTEWEGFETGTRAAAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765312 96 GGFTAVFTMA-NTTPVTdqpIIAESVWAKSQALglcdvhpvgsitkglEGKSLTEFG------------MMARSDAKVRM 162
Cdd:TIGR03178 81 GGITTYIDMPlNSIPAT---TTRASLEAKFEAA---------------KGKLAVDVGfwgglvpynlddLRELDEAGVVG 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765312 163 F--------SDDGKCVQNPQLMRRALEYAKgMDVLLAQHAEDDRMT---GGSSAHEGENAARLGLRGWPRVAEESIVARD 231
Cdd:TIGR03178 143 FkaflspsgDDEFPHVDDWQLYKGMRELAR-LGQLLLVHAENPAITsalGEEAPPQGGVGADAYLASRPVFAEVEAIRRT 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765312 232 ALLARDYGNRVHICHASTQGTVELLQWAKEHDIPLTAEVTPHHLLMTDDKLRTYDGLFRVNPPLREQRDTEALRQALLDG 311
Cdd:TIGR03178 222 LALAKVTGCRVHVVHLSSAEAVELITEAKQEGLDVTVETCPHYLTLTAEEVPDGGTLAKCAPPIRDLANQEGLWEALLNG 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765312 312 TIDCVATDHAPHGSEDKCVE-FENARPGMLGLESSL-AVITKLFVETGLAdWRFIARVMSERPAEITRLPGHGRpLEVGE 389
Cdd:TIGR03178 302 LIDCVVSDHSPCTPDLKRAGdFFKAWGGIAGLQSTLdVMFDEAVQKRGLP-LEDIARLMATNPAKRFGLAQKGR-IAPGK 379
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 552765312 390 PANLTIVDPQHHWVSDSAQLASKSQNNPYAGEEFGARVTHTILRGSVTFD 439
Cdd:TIGR03178 380 DADFVFVDPDESYTLTPDDLYYRHKVSPYVGRTIGGRVRATYLRGQCIYD 429
|
|
| Cyclic_amidohydrolases |
cd01302 |
Cyclic amidohydrolases, including hydantoinase, dihydropyrimidinase, allantoinase, and ... |
63-430 |
4.17e-72 |
|
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: 230.74 E-value: 4.17e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765312 63 VLLPGLVDMHVHLREPGREDT-ETIESGSKAAAKGGFTAVFTMANT-TPVTDQPIIAESVWAKSQ--------ALGLCDV 132
Cdd:cd01302 2 LVLPGFIDIHVHLRDPGGTTYkEDFESGSRAAAAGGVTTVIDMPNTgPPPIDLPAIELKIKLAEEssyvdfsfHAGIGPG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765312 133 HPVGSITKGLEgKSLTEFG-MMARSDAKVRMFSDDgkcvqnpQLMRRALEYAKGMDVLLAqHAEddrmtggssahegena 211
Cdd:cd01302 82 DVTDELKKLFD-AGINSLKvFMNYYFGELFDVDDG-------TLMRTFLEIASRGGPVMV-HAE---------------- 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765312 212 arlglrgwprvaeesivaRDALLARDYGNRVHICHASTQGTVELLQWAKEHDIPLTAEVTPHHLLMTDDKLRTYDGLFRV 291
Cdd:cd01302 137 ------------------RAAQLAEEAGANVHIAHVSSGEALELIKFAKNKGVKVTCEVCPHHLFLDESMLRLNGAWGKV 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765312 292 NPPLREQRDTEALRQALLDGTIDCVATDHAPHGSEDKC--VEFENARPGMLGLESSLAVITKLFVETGLADWRFIaRVMS 369
Cdd:cd01302 199 NPPLRSKEDREALWEGVKNGKIDTIASDHAPHSKEEKEsgKDIWKAPPGFPGLETRLPILLTEGVKRGLSLETLV-EILS 277
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 552765312 370 ERPAEITRLPGHGRpLEVGEPANLTIVDPQHHWVSDSAQLASKSQNNPYAGEEFGARVTHT 430
Cdd:cd01302 278 ENPARIFGLYPKGT-IAVGYDADLVIVDPKKEWKVTAEEIESKADWTPFEGMEVTGKPVST 337
|
|
| PRK06189 |
PRK06189 |
allantoinase; Provisional |
18-434 |
5.28e-67 |
|
allantoinase; Provisional
Pssm-ID: 235732 [Multi-domain] Cd Length: 451 Bit Score: 220.73 E-value: 5.28e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765312 18 LLIKNIRLYGEG--EPTNVLIRGGVIDSIGPEVQADgAAETIDGGGNVLLPGLVDMHVHLREPGREDTETIESGSKAAAK 95
Cdd:PRK06189 5 LIIRGGKVVTPEgvYRADIGIKNGKIAEIAPEISSP-AREIIDADGLYVFPGMIDVHVHFNEPGRTHWEGFATGSAALAA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765312 96 GGFTAVFTMA-NTTPVTdqpIIAESVWAKSQALglcdvhpvgsitkglEGKSLTEFGM--------------MARSDA-- 158
Cdd:PRK06189 84 GGCTTYFDMPlNSIPPT---VTREALDAKAELA---------------RQKSAVDFALwgglvpgnlehlreLAEAGVig 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765312 159 -KVRM---------FSDDGKCVQNpqlMRRALEYAKgmdvLLAQHAEDDRMTGGSS---AHEGENAARLGLRGWPRVAEE 225
Cdd:PRK06189 146 fKAFMsnsgtdefrSSDDLTLYEG---MKEIAALGK----ILALHAESDALTRHLTtqaRQQGKTDVRDYLESRPVVAEL 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765312 226 SIVARDALLARDYGNRVHICHASTQGTVELLQWAKEHDIPLTAEVTPHHLLMTDDKLRTYDGLFRVNPPLREQRDTEALR 305
Cdd:PRK06189 219 EAVQRALLYAQETGCPLHFVHISSGKAVALIAEAKKRGVDVSVETCPHYLLFTEEDFERIGAVAKCAPPLRSRSQKEELW 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765312 306 QALLDGTIDCVATDHAPHGSEDKCVE-FENARPGMLGLESSLAV-ITKLFVETGLAdWRFIARVMSERPAEITRLPGHGR 383
Cdd:PRK06189 299 RGLLAGEIDMISSDHSPCPPELKEGDdFFLVWGGISGGQSTLLVmLTEGYIERGIP-LETIARLLATNPAKRFGLPQKGR 377
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 552765312 384 pLEVGEPANLTIVDPQHHWVSDSAQLASKSQNNPYAGEEFGARVTHTILRG 434
Cdd:PRK06189 378 -LEVGADADFVLVDLDETYTLTKEDLFYRHKQSPYEGRTFPGRVVATYLRG 427
|
|
| PRK07575 |
PRK07575 |
dihydroorotase; Provisional |
17-439 |
1.10e-65 |
|
dihydroorotase; Provisional
Pssm-ID: 236055 [Multi-domain] Cd Length: 438 Bit Score: 216.85 E-value: 1.10e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765312 17 PLLIKNIRLY---GEGEPTNVLIRGGVIDSIGPEVQADGAAETIDGGGNVLLPGLVDMHVHLREPGREDTETIESGSKAA 93
Cdd:PRK07575 4 SLLIRNARILlpsGELLLGDVLVEDGKIVAIAPEISATAVDTVIDAEGLTLLPGVIDPQVHFREPGLEHKEDLFTASRAC 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765312 94 AKGGFTAVFTMANTTPVT-DQPIIAESVWAKSQalglcdvhpvgsitkglegKSLTEFGMM--ARSD------------- 157
Cdd:PRK07575 84 AKGGVTSFLEMPNTKPLTtTQAALDDKLARAAE-------------------KCVVNYGFFigATPDnlpelltanptcg 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765312 158 AKVRMFSDDGKCVQNPQlmrRALE--YAKGmDVLLAQHAEDDrmtggssAHEGENAARLGLRGWPRV-----AEES--IV 228
Cdd:PRK07575 145 IKIFMGSSHGPLLVDEE---AALEriFAEG-TRLIAVHAEDQ-------ARIRARRAEFAGISDPADhsqiqDEEAalLA 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765312 229 ARDAL-LARDYGNRVHICHASTQGTVELLQWAKEhdIPLTAEVTPHHLLMTDDKLRTYDGLFRVNPPLREQRDTEALRQA 307
Cdd:PRK07575 214 TRLALkLSKKYQRRLHILHLSTAIEAELLRQDKP--SWVTAEVTPQHLLLNTDAYERIGTLAQMNPPLRSPEDNEALWQA 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765312 308 LLDGTIDCVATDHAPHGSEDKCVEFENARPGMLGLESSLAVITKLFVEtGLADWRFIARVMSERPAEITRLPGHGRpLEV 387
Cdd:PRK07575 292 LRDGVIDFIATDHAPHTLEEKAQPYPNSPSGMPGVETSLPLMLTAAMR-GKCTVAQVVRWMSTAVARAYGIPNKGR-IAP 369
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 552765312 388 GEPANLTIVDPQHHWVSDSAQLASKSQNNPYAGEEFGARVTHTILRGSVTFD 439
Cdd:PRK07575 370 GYDADLVLVDLNTYRPVRREELLTKCGWSPFEGWNLTGWPVTTIVGGQIVFD 421
|
|
| PRK09236 |
PRK09236 |
dihydroorotase; Reviewed |
16-439 |
3.06e-58 |
|
dihydroorotase; Reviewed
Pssm-ID: 181716 Cd Length: 444 Bit Score: 197.40 E-value: 3.06e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765312 16 NPLLIKNIRLYGEGE--PTNVLIRGGVIDSIGPEVQADGAAETIDGGGNVLLPGLVDMHVHLREPGREDTETIESGSKAA 93
Cdd:PRK09236 2 KRILIKNARIVNEGKifEGDVLIENGRIAKIASSISAKSADTVIDAAGRYLLPGMIDDQVHFREPGLTHKGDIASESRAA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765312 94 AKGGFTAVFTMANTTPVTdqpIIAESVWAKSQALglcdvhpvgsitkglEGKSLTEFGMM-----------ARSDA---- 158
Cdd:PRK09236 82 VAGGITSFMEMPNTNPPT---TTLEALEAKYQIA---------------AQRSLANYSFYfgatndnldeiKRLDPkrvc 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765312 159 --KVRMFSDDGK-CVQNPQLMRRALEYAkgmDVLLAQHAEDDRMTGGSSAH----EGENaarLGLRGWPRV-AEESIVAR 230
Cdd:PRK09236 144 gvKVFMGASTGNmLVDNPETLERIFRDA---PTLIATHCEDTPTIKANLAKykekYGDD---IPAEMHPLIrSAEACYKS 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765312 231 DAL---LARDYGNRVHICHASTQGTVELLQwakehDIPL-----TAEVTPHHLLMTDDKLRTYDGLFRVNPPLREQRDTE 302
Cdd:PRK09236 218 SSLavsLAKKHGTRLHVLHISTAKELSLFE-----NGPLaekriTAEVCVHHLWFDDSDYARLGNLIKCNPAIKTASDRE 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765312 303 ALRQALLDGTIDCVATDHAPHGSEDKCVEFENARPGMLGLESSLAVITKLFVEtGLADWRFIARVMSERPAEITRLPGHG 382
Cdd:PRK09236 293 ALRQALADDRIDVIATDHAPHTWEEKQGPYFQAPSGLPLVQHALPALLELVHE-GKLSLEKVVEKTSHAPAILFDIKERG 371
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 552765312 383 RpLEVGEPANLTIVDPQHHWVSDSAQLASKSQNNPYAGEEFGARVTHTILRGSVTFD 439
Cdd:PRK09236 372 F-IREGYWADLVLVDLNSPWTVTKENILYKCGWSPFEGRTFRSRVATTFVNGQLVYH 427
|
|
| PRK04250 |
PRK04250 |
dihydroorotase; Provisional |
33-436 |
8.88e-58 |
|
dihydroorotase; Provisional
Pssm-ID: 235265 [Multi-domain] Cd Length: 398 Bit Score: 194.99 E-value: 8.88e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765312 33 NVLIRGGVIDSIGP-EVQADgaaETIDGGGNVLLPGLVDMHVHLREPGREDTETIESGSKAAAKGGFTAVFTMANTTPvt 111
Cdd:PRK04250 16 GIGIENGRISKISLrDLKGK---EVIKVKGGIILPGLIDVHVHLRDFEESYKETIESGTKAALHGGITLVFDMPNTKP-- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765312 112 dqPIIAESVWAKSQALglcdvhpvgsitkgLEGKSLTEF--GMMARSDAKV--RMFSDDGKCVQNPQLMRRALE-----Y 182
Cdd:PRK04250 91 --PIMDEKTYEKRMRI--------------AEKKSYADYalNFLIAGNCEKaeEIKADFYKIFMGASTGGIFSEnfevdY 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765312 183 AKGMDVLlAQHAEDDRMTGgssahegENAARlglrgwPRVAEESIVARDALLARDYGNRVHICHASTQGTVELLqwaKEH 262
Cdd:PRK04250 155 ACAPGIV-SVHAEDPELIR-------EFPER------PPEAEVVAIERALEAGKKLKKPLHICHISTKDGLKLI---LKS 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765312 263 DIP-LTAEVTPHHLLMTDDKLRTyDGLFRVNPPLREQRDTEALRQALldGTIDCVATDHAPHGSEDKcvefENARPGMLG 341
Cdd:PRK04250 218 NLPwVSFEVTPHHLFLTRKDYER-NPLLKVYPPLRSEEDRKALWENF--SKIPIIASDHAPHTLEDK----EAGAAGIPG 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765312 342 LESSLAVITKLfVETGLADWRFIARVMSERPAEITRLPGHGrpLEVGEPANLTIVDPQHHWVSDSAQLASKSQNNPYAGE 421
Cdd:PRK04250 291 LETEVPLLLDA-ANKGMISLFDIVEKMHDNPARIFGIKNYG--IEEGNYANFAVFDMKKEWTIKAEELYTKAGWTPYEGF 367
|
410
....*....|....*
gi 552765312 422 EFGARVTHTILRGSV 436
Cdd:PRK04250 368 KLKGKVIMTILRGEV 382
|
|
| PRK09060 |
PRK09060 |
dihydroorotase; Validated |
18-436 |
1.24e-54 |
|
dihydroorotase; Validated
Pssm-ID: 181632 [Multi-domain] Cd Length: 444 Bit Score: 188.21 E-value: 1.24e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765312 18 LLIKNIRLY---GEGEpTNVLIRGGVIDSIGPEVQADgAAETIDGGGNVLLPGLVDMHVHLREPGREDTETIESGSKAAA 94
Cdd:PRK09060 7 LILKGGTVVnpdGEGR-ADIGIRDGRIAAIGDLSGAS-AGEVIDCRGLHVLPGVIDSQVHFREPGLEHKEDLETGSRAAV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765312 95 KGGFTAVFTMANTTPVTDQPIIAESVWAKSQALGLCDV-HPVGSITKGLEgksltEFGMMARSDA----KVRMFSDDGKC 169
Cdd:PRK09060 85 LGGVTAVFEMPNTNPLTTTAEALADKLARARHRMHCDFaFYVGGTRDNAD-----ELAELERLPGcagiKVFMGSSTGDL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765312 170 -VQNPQLMRRALeyaKGMDVLLAQHAEDD---------RMTGGSSAH---EGENAARLGLRgwprvaeeSIVArdalLAR 236
Cdd:PRK09060 160 lVEDDEGLRRIL---RNGRRRAAFHSEDEyrlrerkglRVEGDPSSHpvwRDEEAALLATR--------RLVR----LAR 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765312 237 DYGNRVHICHASTQGTVELLQWAKehDIpLTAEVTPHHL-LMTDDKLRTYDGLFRVNPPLREQRDTEALRQALLDGTIDC 315
Cdd:PRK09060 225 ETGRRIHVLHVSTAEEIDFLADHK--DV-ATVEVTPHHLtLAAPECYERLGTLAQMNPPIRDARHRDGLWRGVRQGVVDV 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765312 316 VATDHAPHGSEDKCVEFENARPGMLGLESSLAVITKLFVETGLADWRFIaRVMSERPAEITRLPGHGRpLEVGEPANLTI 395
Cdd:PRK09060 302 LGSDHAPHTLEEKAKPYPASPSGMTGVQTLVPIMLDHVNAGRLSLERFV-DLTSAGPARIFGIAGKGR-IAVGYDADFTI 379
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 552765312 396 VDPQHHWVSDSAQLASKSQNNPYAGEEFGARVTHTILRGSV 436
Cdd:PRK09060 380 VDLKRRETITNEWIASRCGWTPYDGKEVTGWPVGTIVRGQR 420
|
|
| PRK08044 |
PRK08044 |
allantoinase AllB; |
18-439 |
4.74e-51 |
|
allantoinase AllB;
Pssm-ID: 169193 [Multi-domain] Cd Length: 449 Bit Score: 178.90 E-value: 4.74e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765312 18 LLIKN--IRLYGEGEPTNVLIRGGVIDSIGPEVQAdgAAETIDGGGNVLLPGLVDMHVHLREPGREDTETIESGSKAAAK 95
Cdd:PRK08044 5 LIIKNgtVILENEARVVDIAVKGGKIAAIGQDLGD--AKEVMDASGLVVSPGMVDAHTHISEPGRSHWEGYETGTRAAAK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765312 96 GGFTAVFTMA-NTTPVT-DQPIIAESVWAKSQALGLCDVHPVGSITKGLEG-KSLTEFGMMAR----SDAKVRMFSDDGK 168
Cdd:PRK08044 83 GGITTMIEMPlNQLPATvDRASIELKFDAAKGKLTIDAAQLGGLVSYNLDRlHELDEVGVVGFkcfvATCGDRGIDNDFR 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765312 169 CVQNPQLMRRALEYAKgMDVLLAQHAEDDRMT---GGSSAHEGENAARLGLRGWPRVAEESIVARDALLARDYGNRVHIC 245
Cdd:PRK08044 163 DVNDWQFYKGAQKLGE-LGQPVLVHCENALICdelGEEAKREGRVTAHDYVASRPVFTEVEAIRRVLYLAKVAGCRLHVC 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765312 246 HASTQGTVELLQWAKEHDIPLTAEVTPHHLLMTDDKLRTYDGLFRVNPPLREQRDTEALRQALLDGTIDCVATDHAPHGS 325
Cdd:PRK08044 242 HISSPEGVEEVTRARQEGQDVTCESCPHYFVLDTDQFEEIGTLAKCSPPIRDLENQKGMWEKLFNGEIDCLVSDHSPCPP 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765312 326 EDKCVEFENARPGMLGLESSLAVITKLFVETGLADWRFIARVMSERPAEITRLPGHGRpLEVGEPANLTIVDPQHHWVSD 405
Cdd:PRK08044 322 EMKAGNIMEAWGGIAGLQNCMDVMFDEAVQKRGMSLPMFGKLMATNAADIFGLQQKGR-IAPGKDADFVFIQPNSSYVLK 400
|
410 420 430
....*....|....*....|....*....|....
gi 552765312 406 SAQLASKSQNNPYAGEEFGARVTHTILRGSVTFD 439
Cdd:PRK08044 401 NEDLEYRHKVSPYVGRTIGARITKTILRGDVIYD 434
|
|
| D-HYD |
cd01314 |
D-hydantoinases (D-HYD) also called dihydropyrimidases (DHPase) and related proteins; DHPases ... |
18-439 |
1.22e-49 |
|
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: 174.71 E-value: 1.22e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765312 18 LLIKN--IRLYGEGEPTNVLIRGGVIDSIGPEVQADGAAETIDGGGNVLLPGLVDMHVHLREP--GREDTETIESGSKAA 93
Cdd:cd01314 1 LIIKNgtIVTADGSFKADILIEDGKIVAIGPNLEAPGGVEVIDATGKYVLPGGIDPHTHLELPfmGTVTADDFESGTRAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765312 94 AKGGFTAVFTMANTTPVTDqpiIAESV-----WAKSQAlgLCD-------VHPVGSITKGLE---GKSLTEFGM-MARSD 157
Cdd:cd01314 81 AAGGTTTIIDFAIPNKGQS---LLEAVekwrgKADGKS--VIDygfhmiiTDWTDSVIEELPelvKKGISSFKVfMAYKG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765312 158 AkvRMFSDDgkcvqnpqLMRRALEYAKGMDVLLAQHAEDDRMTggssAHEGENAARLGLRGW-------PRVAEESIVAR 230
Cdd:cd01314 156 L--LMVDDE--------ELLDVLKRAKELGALVMVHAENGDVI----AELQKKLLAQGKTGPeyhalsrPPEVEAEATAR 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765312 231 DALLARDYGNRVHICHASTQGTVELLQWAKEHDIPLTAEVTPHHLLMTDDKLR--TYDG-LFRVNPPLREQRDTEALRQA 307
Cdd:cd01314 222 AIRLAELAGAPLYIVHVSSKEAADEIARARKKGLPVYGETCPQYLLLDDSDYWkdWFEGaKYVCSPPLRPKEDQEALWDG 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765312 308 LLDGTIDCVATDHAPHGSEDKCVEFENAR--P-GMLGLESSLAVITKLFVETGLADW-RFIArVMSERPAEITRL-PGHG 382
Cdd:cd01314 302 LSSGTLQTVGSDHCPFNFAQKARGKDDFTkiPnGVPGVETRMPLLWSEGVAKGRITLeKFVE-LTSTNPAKIFGLyPRKG 380
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 552765312 383 RpLEVGEPANLTIVDPQHHWVSDSAQLASKSQNNPYAGEEFGARVTHTILRGSVTFD 439
Cdd:cd01314 381 T-IAVGSDADLVIWDPNAEKTISADTHHHNVDYNIFEGMKVKGWPVVTISRGKVVVE 436
|
|
| PRK08417 |
PRK08417 |
metal-dependent hydrolase; |
34-435 |
3.79e-48 |
|
metal-dependent hydrolase;
Pssm-ID: 236262 [Multi-domain] Cd Length: 386 Bit Score: 169.50 E-value: 3.79e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765312 34 VLIRGGVIDSIGPEVQADgaaETIDGGGNVLLPGLVDMHVHLREpGREDTETIESGSKAAAKGGFTAVFTMANTTPVTDQ 113
Cdd:PRK08417 1 IRIKDGKITEIGSDLKGE---EILDAKGKTLLPALVDLNVSLKN-DSLSSKNLKSLENECLKGGVGSIVLYPDSTPAIDN 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765312 114 PIIAEsvWAKSQALGLcDVHPVGSITKGLEGKSLTEFGMMARSDAK-VRMFSDdgkcvQNPQLMRRALEYAKGMDVLLAQ 192
Cdd:PRK08417 77 EIALE--LINSAQREL-PMQIFPSIRALDEDGKLSNIATLLKKGAKaLELSSD-----LDANLLKVIAQYAKMLDVPIFC 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765312 193 HAEDDRMTGGSSAHEGENAARLGLRGWPRVAEESIVARDALLARDYGNRVHICHASTQGTVELLQWAKEHDIPLTAEVTP 272
Cdd:PRK08417 149 RCEDSSFDDSGVMNDGELSFELGLPGIPSIAETKEVAKMKELAKFYKNKVLFDTLALPRSLELLDKFKSEGEKLLKEVSI 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765312 273 HHLLMTDDKLRTYDGLFRVNPPLREQRDTEALRQALLDGTIDCVATDHAPHGSEDKCVEFENARPGMLGLESSLAVI-TK 351
Cdd:PRK08417 229 HHLILDDSACENFNTAAKLNPPLRSKEDRLALLEALKEGKIDFLTSLHSAKSNSKKDLAFDEAAFGIDSICEYFSLCyTY 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765312 352 LfVETGLADWRFIARVMSERPAEITRLPGhGRpLEVGEPANLTIVDPQHHWVSDsaqlaskSQNNPYAGEEFGARVTHTI 431
Cdd:PRK08417 309 L-VKEGIITWSELSRFTSYNPAQFLGLNS-GE-IEVGKEADLVLFDPNESTIID-------DNFSLYSGDELYGKIEAVI 378
|
....
gi 552765312 432 LRGS 435
Cdd:PRK08417 379 IKGK 382
|
|
| PLN02795 |
PLN02795 |
allantoinase |
31-438 |
2.47e-42 |
|
allantoinase
Pssm-ID: 178392 [Multi-domain] Cd Length: 505 Bit Score: 156.47 E-value: 2.47e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765312 31 PTNVLIRGGVIDSIGPEVQADGAA---ETIDGGGNVLLPGLVDMHVHLREPGREDTETIESGSKAAAKGGFTAVFTMA-N 106
Cdd:PLN02795 61 PGAVEVEGGRIVSVTKEEEAPKSQkkpHVLDYGNAVVMPGLIDVHVHLNEPGRTEWEGFPTGTKAAAAGGITTLVDMPlN 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765312 107 TTPVTDQPIIAESVWAKSQALGLCDVHPVGSITKGLEGKSLTEFGMMARSDAKVRMFS-----DDGKCVqNPQLMRRALE 181
Cdd:PLN02795 141 SFPSTTSVETLELKIEAAKGKLYVDVGFWGGLVPENAHNASVLEELLDAGALGLKSFMcpsgiNDFPMT-TATHIKAALP 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765312 182 YAKGMDVLLAQHAEddRMTGGSSAHEGENAARL---GLRGWPRVAEESIVARDALLARD-------YGNRVHICHAS-TQ 250
Cdd:PLN02795 220 VLAKYGRPLLVHAE--VVSPVESDSRLDADPRSystYLKSRPPSWEQEAIRQLLEVAKDtrpggvaEGAHVHIVHLSdAE 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765312 251 GTVELLQWAKEHDIPLTAEVTPHHLLMTDDKLRTYDGLFRVNPPLREQRDTEALRQALLDGTIDCVATDHAPHGSEDKCV 330
Cdd:PLN02795 298 SSLELIKEAKAKGDSVTVETCPHYLAFSAEEIPDGDTRYKCAPPIRDAANRELLWKALLDGDIDMLSSDHSPSPPDLKLL 377
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765312 331 E---FENARPGMLGLESSLAVITKLFVETG--LADwrfIARVMSERPAEITRLPGHGRpLEVGEPANLTIVDPQHHW-VS 404
Cdd:PLN02795 378 EegnFLRAWGGISSLQFVLPATWTAGRAYGltLEQ---LARWWSERPAKLAGLDSKGA-IAPGKDADIVVWDPEAEFvLD 453
|
410 420 430
....*....|....*....|....*....|....*
gi 552765312 405 DSAQLASKSQN-NPYAGEEFGARVTHTILRGSVTF 438
Cdd:PLN02795 454 ESYPIYHKHKSlSPYLGTKLSGKVIATFVRGNLVF 488
|
|
| pyrC |
PRK00369 |
dihydroorotase; Provisional |
18-439 |
1.44e-40 |
|
dihydroorotase; Provisional
Pssm-ID: 234738 [Multi-domain] Cd Length: 392 Bit Score: 149.14 E-value: 1.44e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765312 18 LLIKNiRLYGEGEPTNVLIRGGV-IDSIGPEVQADGAAETidggGNVLLPGLVDMHVHLREPGREDTETIESGSKAAAKG 96
Cdd:PRK00369 3 LWIKG-KAYLGKEIKEICINFDRrIKEIKSRCKPDLDLPQ----GTLILPGAIDLHVHLRGLKLSYKEDVASGTSEAAYG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765312 97 GFTAVFTMANTTPVTDQPiiaESVWAKSQAL---GLCDVHPVGSITKGLEGksLTEFGMmarsdAKVRMFSDDgkcVQNP 173
Cdd:PRK00369 78 GVTLVADMPNTIPPLNTP---EAITEKLAELeyySRVDYFVYSGVTKDPEK--VDKLPI-----AGYKIFPED---LERE 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765312 174 QLMRRALEYAKgMDVLLAQHAEDDRmtggssaheGENAARLGLrgWPRVAeesivardAL-LARDYGNrVHICHASTQGT 252
Cdd:PRK00369 145 ETFRVLLKSRK-LKILHPEVPLALK---------SNRKLRRNC--WYEIA--------ALyYVKDYQN-VHITHASNPRT 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765312 253 VELlqwAKEhdIPLTAEVTPHHLLMtddkLRTYDGLFRVNPPLREQRDTEALRQALLDgtIDCVATDHAPHGSEDKCVEF 332
Cdd:PRK00369 204 VRL---AKE--LGFTVDITPHHLLV----NGEKDCLTKVNPPIRDINERLWLLQALSE--VDAIASDHAPHSSFEKLQPY 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765312 333 ENARPGMLGLESSLAVITKLFVETGLADWRFiARVMSERPAEITRLPghGRPLEVGEPANLTIV--DPQHHwvsdsAQLA 410
Cdd:PRK00369 273 EVCPPGIAALSFTPPFIYTLVSKGILSIDRA-VELISTNPARILGIP--YGEIKEGYRANFTVIqfEDWRY-----STKY 344
|
410 420
....*....|....*....|....*....
gi 552765312 411 SKSQNNPYAGEEFGARVTHTILRGSVTFD 439
Cdd:PRK00369 345 SKVIETPLDGFELKASVYATIVQGKLAYL 373
|
|
| D-hydantoinase |
TIGR02033 |
D-hydantoinase; This model represents the D-hydantoinase (dihydropyrimidinase) which primarily ... |
33-438 |
5.22e-38 |
|
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: 143.68 E-value: 5.22e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765312 33 NVLIRGGVIDSIGPEVQADGAAETIDGGGNVLLPGLVDMHVHLREP--GREDTETIESGSKAAAKGGFTAVFTMANTTPV 110
Cdd:TIGR02033 18 DVLIEGGKIVAVGDNLIPPDAVEVIDATGKYVLPGGIDVHTHLEMPfgGTTTADDFFTGTKAAAAGGTTTIIDFVVPEKG 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765312 111 TDQPIIAESVWAKSQALGLCDVHPVGSITKGLEGKSLTEFGMMAR---SDAKVRMFSDDGKCVQNPQLMrRALEYAKGMD 187
Cdd:TIGR02033 98 SSLTEALETWHEKAEGKSVIDYGFHMDITHWNDSVLEEHIPEVKEegiNSFKVFMAYKNLLMVDDEELF-EILKRLKELG 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765312 188 VLLAQHAED----DRMTG-----GSSAHEGENAARlglrgwPRVAEESIVARDALLARDYGNRVHICHASTQGTVELLQW 258
Cdd:TIGR02033 177 ALLQVHAENgdiiAELQArmlaqGITGPEYHALSR------PPELEAEAVARAITLAALADAPLYVVHVSTKDAADEIAQ 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765312 259 AKEHDIPLTAEVTPHHLLMTDDKL--RTYDGL-FRVNPPLREQRDTEALRQALLDGTIDCVATDHAPHGSEDKCV----E 331
Cdd:TIGR02033 251 ARKKGQPVFGETCPQYLVLDDTHYdkPGFEGAkYVCSPPLREPEDQDALWSALSSGALQTVGSDHCTFNFAQKKAigkdD 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765312 332 FENARPGMLGLESSLAVITKLFVETGLADWRFIARVMSERPAEITRL-PGHGRpLEVGEPANLTIVDPQHHWVSDSAQLA 410
Cdd:TIGR02033 331 FTKIPNGGPGVEERMSLLFDEGVAKGRITLEKFVEVTSTNPAKIFNLyPRKGT-IAVGSDADIVIWDPNRTTVISAETHH 409
|
410 420
....*....|....*....|....*...
gi 552765312 411 SKSQNNPYAGEEFGARVTHTILRGSVTF 438
Cdd:TIGR02033 410 SNADYNPFEGFKVRGAPVSVLSRGRVVV 437
|
|
| CAD_DHOase |
cd01316 |
The eukaryotic CAD protein is a trifunctional enzyme of carbamoylphosphate ... |
63-438 |
5.12e-34 |
|
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: 130.26 E-value: 5.12e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765312 63 VLLPGLVDMHVHLREPGREDTETIESGSKAAAKGGFTAVFTMANTTPVTDQPIIAESVWAKSQALGLCDVhpvgSITKGL 142
Cdd:cd01316 3 IRLPGLIDVHVHLREPGATHKEDFASGTKAALAGGFTMVRAMPNTNPSIVDVASLKLVQSLAQAKARCDY----AFSIGA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765312 143 EGKSLTEFGMMARSDAKVRMFSDDgkcvqnpqlmrraleyakgmdvllaqhaeddrmTGGSSAHEGENAARLGLRGWPRV 222
Cdd:cd01316 79 TSTNAATVGELASEAVGLKFYLNE---------------------------------TFSTLILDKITAWASHFNAWPST 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765312 223 ------AEESIVARDALLARDYGNRVHICHASTQGTVELLQWAKEHDIPLTAEVTPHHLLMTDDKLRtyDGLFRVNPPLR 296
Cdd:cd01316 126 kpivthAKSQTLAAVLLLASLHNRSIHICHVSSKEEINLIRLAKARGLKVTCEVSPHHLFLSQDDLP--RGQYEVRPFLP 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765312 297 EQRDTEALRQALldGTIDCVATDHAPHGSEDKCVefENARPGMLGLESSLAVITKLfVETGLADWRFIARVMSERPAEIT 376
Cdd:cd01316 204 TREDQEALWENL--DYIDCFATDHAPHTLAEKTG--NKPPPGFPGVETSLPLLLTA-VHEGRLTIEDIVDRLHTNPKRIF 278
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 552765312 377 RLPghgrplevGEPANLTIVDPQHHWVSDSAQLASKSQNNPYAGEEFGARVTHTILRGSVTF 438
Cdd:cd01316 279 NLP--------PQSDTYVEVDLDEEWTIPKNPLQSKKGWTPFEGKKVKGKVQRVVLRGETAF 332
|
|
| PRK01211 |
PRK01211 |
dihydroorotase; Provisional |
34-439 |
4.28e-33 |
|
dihydroorotase; Provisional
Pssm-ID: 179247 [Multi-domain] Cd Length: 409 Bit Score: 129.21 E-value: 4.28e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765312 34 VLIRGGVIDSIGPEVQADGAAEtIDGggnVLLPGLVDMHVHLREPGREDTETIESGSKAAAKGGFTAVFTMANTT-PVTD 112
Cdd:PRK01211 18 IEVEDGKIKSIKKDAGNIGKKE-LKG---AILPAATDIHVHFRTPGETEKEDFSTGTLSAIFGGTTFIMDMPNNNiPIKD 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765312 113 qpiiaesVWAKSQALGLCDvhpvgsitkgleGKSLTEFGMMA------------RSDA-KVRM---FSDDGKCVQNPQLm 176
Cdd:PRK01211 94 -------YNAFSDKLGRVA------------PKAYVDFSLYSmetgnnalildeRSIGlKVYMggtTNTNGTDIEGGEI- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765312 177 rralEYAKGMDVLLAQHAEDDRMTggsSAHEGEnAARLGLRGWPRVAEESIVARDALLARDYGNRvHICHASTQGTVEll 256
Cdd:PRK01211 154 ----KKINEANIPVFFHAELSECL---RKHQFE-SKNLRDHDLARPIECEIKAVKYVKNLDLKTK-IIAHVSSIDVIG-- 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765312 257 qwakehdiPLTAEVTPHHLLMTDD-KLRTYDglfRVNPPLREQRDTEALRQALLDGTIDCVATDHAPHGSEDKcVEFENA 335
Cdd:PRK01211 223 --------RFLREVTPHHLLLNDDmPLGSYG---KVNPPLRDRWTQERLLEEYISGRFDILSSDHAPHTEEDK-QEFEYA 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765312 336 RPGMLGLESSLAVITKLfVETGLADWRFIARVMSERPAEITRLPgHGRpLEVGEPANLTIVDPQHHWVSDSAQLASKSQN 415
Cdd:PRK01211 291 KSGIIGVETRVPLFLAL-VKKKILPLDVLYKTAIERPASLFGIK-KGK-IEEGYDADFMAFDFTNIKKINDKRLHSKCPV 367
|
410 420
....*....|....*....|....*
gi 552765312 416 NPYAGeeFGARVTHT-ILRGSVTFD 439
Cdd:PRK01211 368 SPFNG--FDAIFPSHvIMRGEVVID 390
|
|
| PRK08323 |
PRK08323 |
phenylhydantoinase; Validated |
34-439 |
1.22e-30 |
|
phenylhydantoinase; Validated
Pssm-ID: 236240 [Multi-domain] Cd Length: 459 Bit Score: 122.97 E-value: 1.22e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765312 34 VLIRGGVIDSIGpevqADGAAETIDGGGNVLLPGLVDMHVHLREP--GREDTETIESGSKAAAKGGFTAVFTMAntTPVT 111
Cdd:PRK08323 21 VLIEDGKIAAIG----ANLGDEVIDATGKYVMPGGIDPHTHMEMPfgGTVSSDDFETGTRAAACGGTTTIIDFA--LQPK 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765312 112 DQPIIaESV-----WAKSQALglCDV--HpvGSITkGLEGKSLTEFGMMAR---SDAKVRM------FSDDGkcvqnpQL 175
Cdd:PRK08323 95 GQSLR-EALeawhgKAAGKAV--IDYgfH--MIIT-DWNEVVLDEMPELVEegiTSFKLFMaykgalMLDDD------EL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765312 176 MRrALEYAKGMDVLLAQHAED----DRMTGGSSAhEGENAARLGLRGWPRVAEESIVARDALLARDYGNRVHICHASTQG 251
Cdd:PRK08323 163 LR-ALQRAAELGALPMVHAENgdaiAYLQAKLLA-EGKTGPEYHALSRPPEVEGEATNRAIMLAELAGAPLYIVHVSCKE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765312 252 TVELLQWAKEHDIPLTAEVTPHHLLMTDDKLR---TYDGLFRV-NPPLREQRDTEALRQALLDGTIDCVATDHAPHGSED 327
Cdd:PRK08323 241 ALEAIRRARARGQRVFGETCPQYLLLDESEYDgpdWFEGAKYVmSPPLRDKEHQDALWRGLQDGDLQVVATDHCPFCFEQ 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765312 328 KCVE----FENARPGMLGLESSLAVITKLFVETG-LADWRFIArVMSERPAEITRL-PGHGrPLEVGEPANLTIVDPQHH 401
Cdd:PRK08323 321 KKQLgrgdFTKIPNGTPGVEDRMPLLFSEGVMTGrITLNRFVE-LTSTNPAKIFGLyPRKG-TIAVGADADIVIWDPNAT 398
|
410 420 430
....*....|....*....|....*....|....*...
gi 552765312 402 WVSDSAQLASKSQNNPYAGEEFGARVTHTILRGSVTFD 439
Cdd:PRK08323 399 KTISASTLHSNVDYNPYEGFEVTGWPVTTLSRGEVVVE 436
|
|
| PRK13404 |
PRK13404 |
dihydropyrimidinase; Provisional |
36-436 |
1.94e-25 |
|
dihydropyrimidinase; Provisional
Pssm-ID: 184033 [Multi-domain] Cd Length: 477 Bit Score: 108.25 E-value: 1.94e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765312 36 IRGGVIDSIGPevQADGAAETIDGGGNVLLPGLVDMHVHLREP---GREDTETIESGSKAAAKGGFTAVFTMANTTPVTD 112
Cdd:PRK13404 26 IRGGRIAALGE--GLGPGAREIDATGRLVLPGGVDSHCHIDQPsgdGIMMADDFYTGTVSAAFGGTTTVIPFAAQHRGQS 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765312 113 QPIIAESVWAKSQALGLCDV--H-PVGSITKGLEGKSLTEFGMMARSDAKVRMFSDDGKCVQNPQLmrRALEYAKGMDVL 189
Cdd:PRK13404 104 LREAVEDYHRRAAGKAVIDYafHlIVADPTEEVLTEELPALIAQGYTSFKVFMTYDDLKLDDRQIL--DVLAVARRHGAM 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765312 190 LAQHAEDDRMTG---GSSAHEGENAARLGLRGWPRVAEESIVARDALLARDYGNRVHICHASTQGTVELLQWAKEHDIPL 266
Cdd:PRK13404 182 VMVHAENHDMIAwltKRLLAAGLTAPKYHAISRPMLAEREATHRAIALAELVDVPILIVHVSGREAAEQIRRARGRGLKI 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765312 267 TAEVTPHHLLMTDDKLRTyDGL----FRVNPPLREQRDTEALRQALLDGTIDCVATDHAPHGSEDKC--------VEFEN 334
Cdd:PRK13404 262 FAETCPQYLFLTAEDLDR-PGMegakYICSPPPRDKANQEAIWNGLADGTFEVFSSDHAPFRFDDTDgklaaganPSFKA 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765312 335 ARPGMLGLESSLAVITKLFVETG-LADWRFIArVMSERPAEITRLPGHGRPLEVGEPANLTIVDPQHHWVSDSAQLASKS 413
Cdd:PRK13404 341 IANGIPGIETRLPLLFSEGVVKGrISLNRFVA-LTSTNPAKLYGLYPRKGAIAIGADADIAIWDPDREVTITNADLHHAA 419
|
410 420
....*....|....*....|...
gi 552765312 414 QNNPYAGEEFGARVTHTILRGSV 436
Cdd:PRK13404 420 DYTPYEGMRVTGWPVTVLSRGRV 442
|
|
| PLN02942 |
PLN02942 |
dihydropyrimidinase |
28-439 |
1.10e-24 |
|
dihydropyrimidinase
Pssm-ID: 178530 Cd Length: 486 Bit Score: 106.08 E-value: 1.10e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765312 28 EGEPTNVLIRGGVIDSIGPEVQADGAAETIDGGGNVLLPGLVDMHVHLREP--GREDTETIESGSKAAAKGGFTAVFTMA 105
Cdd:PLN02942 19 HQELADVYVEDGIIVAVAPNLKVPDDVRVIDATGKFVMPGGIDPHTHLAMPfmGTETIDDFFSGQAAALAGGTTMHIDFV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765312 106 ntTPVTDQPIIAESVWAKSQALGLCDVHPVGSITKGLEGKSlTEFGMMARSDA--KVRMF-SDDGKCVQNPQLMRRALEY 182
Cdd:PLN02942 99 --IPVNGNLLAGYEAYEKKAEKSCMDYGFHMAITKWDDTVS-RDMETLVKEKGinSFKFFmAYKGSLMVTDELLLEGFKR 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765312 183 AKGMDVLLAQHAEDdrmtgGSSAHEGENAA-RLGLRG-------WPRVAEESIVARDALLARDYGNRVHICHASTQGTVE 254
Cdd:PLN02942 176 CKSLGALAMVHAEN-----GDAVFEGQKRMiELGITGpeghalsRPPLLEGEATARAIRLAKFVNTPLYVVHVMSIDAME 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765312 255 LLQWAKEHDIPLTAEVTPHHLLMTDDKLRTYD----GLFRVNPPLREQRDTEALRQALLDGTIDCVATDHAPHGSEDKCV 330
Cdd:PLN02942 251 EIARARKSGQRVIGEPVVSGLVLDDSKLWDPDftiaSKYVMSPPIRPAGHGKALQAALSSGILQLVGTDHCPFNSTQKAF 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765312 331 ---EFENARPGMLGLESSLAVITKLFVETGLADWRFIARVMSERPAEITRL-PGHGRPLeVGEPANLTIVDPQHHWVSDS 406
Cdd:PLN02942 331 gkdDFRKIPNGVNGIEERMHLVWDTMVESGQISPTDYVRVTSTECAKIFNIyPRKGAIL-AGSDADIIILNPNSTFTISA 409
|
410 420 430
....*....|....*....|....*....|...
gi 552765312 407 AQLASKSQNNPYAGEEFGARVTHTILRGSVTFD 439
Cdd:PLN02942 410 KTHHSRIDTNVYEGRRGKGKVEVTISQGRVVWE 442
|
|
| HutI |
COG1228 |
Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport ... |
9-218 |
1.10e-17 |
|
Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440841 [Multi-domain] Cd Length: 386 Bit Score: 84.24 E-value: 1.10e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765312 9 RLSAPAENPLLIKNIRLY-GEG----EPTNVLIRGGVIDSIGP--EVQADGAAETIDGGGNVLLPGLVDMHVHLREPGRE 81
Cdd:COG1228 1 KKAPAQAGTLLITNATLVdGTGggviENGTVLVEDGKIAAVGPaaDLAVPAGAEVIDATGKTVLPGLIDAHTHLGLGGGR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765312 82 DTETIESGS---------------KAAAKGGFTAVFTM-ANTTPVTDQPIIAESVWAKSQALgLCDVHPVgSITKGLEGK 145
Cdd:COG1228 81 AVEFEAGGGitptvdlvnpadkrlRRALAAGVTTVRDLpGGPLGLRDAIIAGESKLLPGPRV-LAAGPAL-SLTGGAHAR 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 552765312 146 SLTEFGMMARSDAK-----VRMFSDDGKCVQNPQLMRRALEYAKGMDVLLAQHAEddrmtggsSAHEGENAARLGLRG 218
Cdd:COG1228 159 GPEEARAALRELLAegadyIKVFAEGGAPDFSLEELRAILEAAHALGLPVAAHAH--------QADDIRLAVEAGVDS 228
|
|
| Amidohydro_1 |
pfam01979 |
Amidohydrolase family; This family of enzymes are a a large metal dependent hydrolase ... |
63-436 |
3.75e-15 |
|
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: 76.39 E-value: 3.75e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765312 63 VLLPGLVDMHVHLR--------EPGREDTETIESGSKAAAKGGFTAVFTMANTTPVTDqPIIAESvwAKSQALGLCDVHP 134
Cdd:pfam01979 1 IVLPGLIDAHVHLEmgllrgipVPPEFAYEALRLGITTMLKSGTTTVLDMGATTSTGI-EALLEA--AEELPLGLRFLGP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765312 135 VGSITKGLEGKSLTEFGMMARSDAKVRMFSDDG---------KCVQNPQ-LMRRALEYAKGMDVLLAQHAeddrmtgGSS 204
Cdd:pfam01979 78 GCSLDTDGELEGRKALREKLKAGAEFIKGMADGvvfvglaphGAPTFSDdELKAALEEAKKYGLPVAIHA-------LET 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765312 205 AHEGENAARLGLRGWPR-----VAEESIVARDALLArdygnRVHICHASTQGTVELLQWAKEHDIPltaevtphHLLMTD 279
Cdd:pfam01979 151 KGEVEDAIAAFGGGIEHgthleVAESGGLLDIIKLI-----LAHGVHLSPTEANLLAEHLKGAGVA--------HCPFSN 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765312 280 DKLRTydglfrvnpplreqrDTEALRQALLDGTIDCVATDHAPHGSedkcvEFENARPGMLGLESSlavitklFVETGLA 359
Cdd:pfam01979 218 SKLRS---------------GRIALRKALEDGVKVGLGTDGAGSGN-----SLNMLEELRLALELQ-------FDPEGGL 270
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 552765312 360 DWRFIARVMSERPAEITRLPGHGRPLEVGEPANLTIVDPQhhwvsdsaqlasksQNNPYAGEEFGARVTHTILRGSV 436
Cdd:pfam01979 271 SPLEALRMATINPAKALGLDDKVGSIEVGKDADLVVVDLD--------------PLAAFFGLKPDGNVKKVIVKGKI 333
|
|
| PRK05985 |
PRK05985 |
cytosine deaminase; Provisional |
16-75 |
3.89e-13 |
|
cytosine deaminase; Provisional
Pssm-ID: 180337 [Multi-domain] Cd Length: 391 Bit Score: 70.73 E-value: 3.89e-13
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765312 16 NPLLIKNIRLYGeGEPTNVLIRGGVIDSIGPEVQADGAAETIDGGGNVLLPGLVDMHVHL 75
Cdd:PRK05985 2 TDLLFRNVRPAG-GAAVDILIRDGRIAAIGPALAAPPGAEVEDGGGALALPGLVDGHIHL 60
|
|
| DHOase |
pfam12890 |
Dihydro-orotase-like; This is a small family of dihydro-orotase-like proteins from various ... |
61-250 |
3.06e-12 |
|
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: 63.74 E-value: 3.06e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765312 61 GNVLLPGLVDMHVHLREPGREDTETIEsgskaaakggfTAVFTMANTTPVTDQPIIAEsvwaksqalglcdvhpvgsitK 140
Cdd:pfam12890 1 GRLIVPGLAFLHVHLTAPSGEAQELKE-----------TTWAAYGVTFKAPAGITVED---------------------D 48
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765312 141 GLEGksltefgmmarsdakvRMFSDDGKCVQNPQLMRRALEYAKgMDVLLAQHAEDDRMTGGSSAHEGENAARLG--LRG 218
Cdd:pfam12890 49 SEEG----------------FIFTNDTYYITIQLLEGEGMKKSE-LDQELKAIATDDEVTNQSAVQDFELPQFYGtqLKG 111
|
170 180 190
....*....|....*....|....*....|..
gi 552765312 219 wprVAEESIVARDALLARDYGNRVHICHASTQ 250
Cdd:pfam12890 112 ---NCETEHCVYSYLLAKAAGCGFYVSIIYTK 140
|
|
| Bact_CD |
cd01293 |
Bacterial cytosine deaminase and related metal-dependent hydrolases. Cytosine deaminases (CDs) ... |
19-407 |
5.62e-12 |
|
Bacterial cytosine deaminase and related metal-dependent hydrolases. Cytosine deaminases (CDs) catalyze the deamination of cytosine, producing uracil and ammonia. They play an important role in pyrimidine salvage. CDs are present in prokaryotes and fungi, but not mammalian cells. The bacterial enzymes, but not the fungal enzymes, are related to the adenosine deaminases (ADA). The bacterial enzymes are iron dependent and hexameric.
Pssm-ID: 238618 [Multi-domain] Cd Length: 398 Bit Score: 66.89 E-value: 5.62e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765312 19 LIKNIRLYGEGEPT-NVLIRGGVIDSIGPEVQADGAAETIDGGGNVLLPGLVDMHVHLrepgreDTETIESGSKAAAKG- 96
Cdd:cd01293 1 LLRNARLADGGTALvDIAIEDGRIAAIGPALAVPPDAEEVDAKGRLVLPAFVDPHIHL------DKTFTGGRWPNNSGGt 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765312 97 GFTAVFTMANTTPVTDQPII---AESVWAKSQALGL------CDVHPVGSiTKGLEGksltefGMMARSDAKVR------ 161
Cdd:cd01293 75 LLEAIIAWEERKLLLTAEDVkerAERALELAIAHGTtairthVDVDPAAG-LKALEA------LLELREEWADLidlqiv 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765312 162 ------MFSDDGkcvqNPQLMRRALeyAKGMDVL-LAQHAEDDRMTGGSSA-----------------HEgenAARLGLR 217
Cdd:cd01293 148 afpqhgLLSTPG----GEELMREAL--KMGADVVgGIPPAEIDEDGEESLDtlfelaqehgldidlhlDE---TDDPGSR 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765312 218 GWPRVAEESIvardallARDYGNRVHICHASTQGTV------ELLQWAKEHDIPLTAEVTP-HHLLMTDDKLRTYDGLfr 290
Cdd:cd01293 219 TLEELAEEAE-------RRGMQGRVTCSHATALGSLpeaevsRLADLLAEAGISVVSLPPInLYLQGREDTTPKRRGV-- 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765312 291 vnPPLREqrdteaLRQALLDGTI--DCVaTDH-APHGSEDkcvefenarpgMLGLESSLAVITKLFVETGLAD-WRFIar 366
Cdd:cd01293 290 --TPVKE------LRAAGVNVALgsDNV-RDPwYPFGSGD-----------MLEVANLAAHIAQLGTPEDLALaLDLI-- 347
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 552765312 367 vmSERPAEITRLPGHGrpLEVGEPANLTIVDPQH--HWVSDSA 407
Cdd:cd01293 348 --TGNAARALGLEDYG--IKVGCPADLVLLDAEDvaEAVARQP 386
|
|
| PRK09237 |
PRK09237 |
amidohydrolase/deacetylase family metallohydrolase; |
18-74 |
3.22e-10 |
|
amidohydrolase/deacetylase family metallohydrolase;
Pssm-ID: 236423 [Multi-domain] Cd Length: 380 Bit Score: 61.40 E-value: 3.22e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 552765312 18 LLIKNIRL----YGEGEPTNVLIRGGVIDSIGPEVQADGAAETIDGGGNVLLPGLVDMHVH 74
Cdd:PRK09237 1 LLLRGGRVidpaNGIDGVIDIAIEDGKIAAVAGDIDGSQAKKVIDLSGLYVSPGWIDLHVH 61
|
|
| COG3964 |
COG3964 |
Predicted amidohydrolase [General function prediction only]; |
17-74 |
5.94e-10 |
|
Predicted amidohydrolase [General function prediction only];
Pssm-ID: 443164 [Multi-domain] Cd Length: 376 Bit Score: 60.57 E-value: 5.94e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 552765312 17 PLLIKNIRL----YGEGEPTNVLIRGGVIDSIGPEVQADGAAETIDGGGNVLLPGLVDMHVH 74
Cdd:COG3964 1 DLLIKGGRVidpaNGIDGVMDIAIKDGKIAAVAKDIDAAEAKKVIDASGLYVTPGLIDLHTH 62
|
|
| NagA |
cd00854 |
N-acetylglucosamine-6-phosphate deacetylase, NagA, catalyzes the hydrolysis of the N-acetyl ... |
18-74 |
4.51e-09 |
|
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: 57.97 E-value: 4.51e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 552765312 18 LLIKNIRLYGEG--EPTNVLIRGGVIDSIGPEVQADGAAETIDGGGNVLLPGLVDMHVH 74
Cdd:cd00854 1 LIIKNARILTPGglEDGAVLVEDGKIVAIGPEDELEEADEIIDLKGQYLVPGFIDIHIH 59
|
|
| NagA |
COG1820 |
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism]; |
19-74 |
5.30e-09 |
|
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism];
Pssm-ID: 441425 [Multi-domain] Cd Length: 373 Bit Score: 57.80 E-value: 5.30e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 552765312 19 LIKNIRLY-GEGEPTN--VLIRGGVIDSIGPEVQADgaAETIDGGGNVLLPGLVDMHVH 74
Cdd:COG1820 1 AITNARIFtGDGVLEDgaLLIEDGRIAAIGPGAEPD--AEVIDLGGGYLAPGFIDLHVH 57
|
|
| metallo-dependent_hydrolases |
cd01292 |
Superfamily of metallo-dependent hydrolases (also called amidohydrolase superfamily) is a ... |
68-326 |
9.50e-09 |
|
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: 56.19 E-value: 9.50e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765312 68 LVDMHVHLREPG-----------------REDT-ETIESGSKAAAKGGFTAVFTMANTTPVTDQPIIAESVWAKSQAL-- 127
Cdd:cd01292 1 FIDTHVHLDGSAlrgtrlnlelkeaeelsPEDLyEDTLRALEALLAGGVTTVVDMGSTPPPTTTKAAIEAVAEAARASag 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765312 128 -------GLCDVHPVGSITKGLEGKSLTEFGMMARSDAkVRMFSDDGKCVQNPQLMRRALEYAKGMDVLLAQHAEDdrmt 200
Cdd:cd01292 81 irvvlglGIPGVPAAVDEDAEALLLELLRRGLELGAVG-LKLAGPYTATGLSDESLRRVLEEARKLGLPVVIHAGE---- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765312 201 GGSSAHEGENAARLGLRgwprvaeesivardallardyGNRVHICHASTqGTVELLQWAKEHDIPLtaEVTPHHLLMTDd 280
Cdd:cd01292 156 LPDPTRALEDLVALLRL---------------------GGRVVIGHVSH-LDPELLELLKEAGVSL--EVCPLSNYLLG- 210
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 552765312 281 klrtydglfrvnpplREQRDTEALRQALLDGTIDCVATDHAPHGSE 326
Cdd:cd01292 211 ---------------RDGEGAEALRRLLELGIRVTLGTDGPPHPLG 241
|
|
| AdeC |
COG1001 |
Adenine deaminase [Nucleotide transport and metabolism]; |
12-106 |
1.78e-08 |
|
Adenine deaminase [Nucleotide transport and metabolism];
Pssm-ID: 440625 [Multi-domain] Cd Length: 559 Bit Score: 56.65 E-value: 1.78e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765312 12 APAEnpLLIKNIRLY----GEGEPTNVLIRGGVIDSIGPEVQAdgAAETIDGGGNVLLPGLVDMHVHlrepgredtetIE 87
Cdd:COG1001 3 EPAD--LVIKNGRLVnvftGEILEGDIAIAGGRIAGVGDYIGE--ATEVIDAAGRYLVPGFIDGHVH-----------IE 67
|
90 100 110
....*....|....*....|....*....|
gi 552765312 88 SG-------SKAAAKGGFTAVFT----MAN 106
Cdd:COG1001 68 SSmvtpaefARAVLPHGTTTVIAdpheIAN 97
|
|
| Isoaspartyl-dipeptidase |
cd01308 |
Isoaspartyl dipeptidase hydrolyzes the beta-L-isoaspartyl linkages in dipeptides, as part of ... |
18-143 |
2.59e-08 |
|
Isoaspartyl dipeptidase hydrolyzes the beta-L-isoaspartyl linkages in dipeptides, as part of the degradative pathway to eliminate proteins with beta-L-isoaspartyl peptide bonds, bonds whereby the beta-group of an aspartate forms the peptide link with the amino group of the following amino acid. Formation of this bond is a spontaneous nonenzymatic reaction in nature and can profoundly effect the function of the protein. Isoaspartyl dipeptidase is an octameric enzyme that contains a binuclear zinc center in the active site of each subunit and shows a strong preference of hydrolyzing Asp-Leu dipeptides.
Pssm-ID: 238633 [Multi-domain] Cd Length: 387 Bit Score: 55.47 E-value: 2.59e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765312 18 LLIKNIRLYGegePT-----NVLIRGGVIDSIGPEVQADG--AAETIDGGGNVLLPGLVDMHVHLREPGRE---DTETIE 87
Cdd:cd01308 2 TLIKNAEVYA---PEylgkkDILIAGGKILAIEDQLNLPGyeNVTVVDLHGKILVPGFIDQHVHIIGGGGEggpSTRTPE 78
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 552765312 88 SGSKAAAKGGFTAVFTMANTTPVTDQPiiaESVWAKSQAL---GL-CDVH------PVGSITKGLE 143
Cdd:cd01308 79 VTLSDLTTAGVTTVVGCLGTDGISRSM---EDLLAKARALeeeGItCFVYtgsyevPTRTITGSIR 141
|
|
| COG3653 |
COG3653 |
N-acyl-D-aspartate/D-glutamate deacylase [Secondary metabolites biosynthesis, transport and ... |
18-74 |
1.10e-07 |
|
N-acyl-D-aspartate/D-glutamate deacylase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442870 [Multi-domain] Cd Length: 528 Bit Score: 54.02 E-value: 1.10e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 552765312 18 LLIKNIRLY-GEGEP---TNVLIRGGVIDSIGpEVQADGAAETIDGGGNVLLPGLVDMHVH 74
Cdd:COG3653 4 LLIRGGTVVdGTGAPpfrADVAIKGGRIVAVG-DLAAAEAARVIDATGLVVAPGFIDIHTH 63
|
|
| SsnA |
COG0402 |
Cytosine/adenosine deaminase or related metal-dependent hydrolase [Nucleotide transport and ... |
34-75 |
1.12e-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: 53.68 E-value: 1.12e-07
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 552765312 34 VLIRGGVIDSIGPEVQAD---GAAETIDGGGNVLLPGLVDMHVHL 75
Cdd:COG0402 24 VLVEDGRIAAVGPGAELParyPAAEVIDAGGKLVLPGLVNTHTHL 68
|
|
| D-aminoacylase |
cd01297 |
D-aminoacylases (N-acyl-D-Amino acid amidohydrolases) catalyze the hydrolysis of ... |
18-74 |
5.72e-07 |
|
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: 51.53 E-value: 5.72e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 552765312 18 LLIKNIRLY-GEGEP---TNVLIRGGVIDSIGPeVQADGAAETIDGGGNVLLPGLVDMHVH 74
Cdd:cd01297 2 LVIRNGTVVdGTGAPpftADVGIRDGRIAAIGP-ILSTSAREVIDAAGLVVAPGFIDVHTH 61
|
|
| YtcJ |
COG1574 |
Predicted amidohydrolase YtcJ [General function prediction only]; |
18-75 |
6.36e-07 |
|
Predicted amidohydrolase YtcJ [General function prediction only];
Pssm-ID: 441182 [Multi-domain] Cd Length: 535 Bit Score: 51.72 E-value: 6.36e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 552765312 18 LLIKNIRLY----GEGEPTNVLIRGGVIDSIGP--EVQA--DGAAETIDGGGNVLLPGLVDMHVHL 75
Cdd:COG1574 10 LLLTNGRIYtmdpAQPVAEAVAVRDGRIVAVGSdaEVRAlaGPATEVIDLGGKTVLPGFIDAHVHL 75
|
|
| ATZ_TRZ_like |
cd01298 |
TRZ/ATZ family contains enzymes from the atrazine degradation pathway and related hydrolases. ... |
18-75 |
6.56e-07 |
|
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: 51.43 E-value: 6.56e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 552765312 18 LLIKNIRLYGEGEPT-----NVLIRGGVIDSIGPEVQADG--AAETIDGGGNVLLPGLVDMHVHL 75
Cdd:cd01298 1 ILIRNGTIVTTDPRRvledgDVLVEDGRIVAVGPALPLPAypADEVIDAKGKVVMPGLVNTHTHL 65
|
|
| PRK10027 |
PRK10027 |
cryptic adenine deaminase; Provisional |
6-75 |
2.14e-06 |
|
cryptic adenine deaminase; Provisional
Pssm-ID: 182201 [Multi-domain] Cd Length: 588 Bit Score: 49.83 E-value: 2.14e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 552765312 6 ATGRLSAPAEnpLLIKNIRLY----GEGEPTNVLIRGGVIDSIGPEVQADGAAETIDGGGNVLLPGLVDMHVHL 75
Cdd:PRK10027 22 AVSRGDAVAD--YIIDNVSILdlinGGEISGPIVIKGRYIAGVGAEYADAPALQRIDARGATAVPGFIDAHLHI 93
|
|
| Met_dep_hydrolase_B |
cd01307 |
Metallo-dependent hydrolases, subgroup B is part of the superfamily of metallo-dependent ... |
33-74 |
4.97e-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: 48.48 E-value: 4.97e-06
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 552765312 33 NVLIRGGVIDSIGPEVQADGAAETIDGGGNVLLPGLVDMHVH 74
Cdd:cd01307 1 DVAIENGKIAAVGAALAAPAATQIVDAGGCYVSPGWIDLHVH 42
|
|
| YtcJ_like |
cd01300 |
YtcJ_like metal dependent amidohydrolases. YtcJ is a Bacillus subtilis ORF of unknown function. ... |
34-244 |
5.21e-06 |
|
YtcJ_like metal dependent amidohydrolases. YtcJ is a Bacillus subtilis ORF of unknown function. The Arabidopsis homolog LAF3 has been identified as a factor required for phytochrome A signalling.
Pssm-ID: 238625 [Multi-domain] Cd Length: 479 Bit Score: 48.46 E-value: 5.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765312 34 VLIRGGVIDSIGPEVQA----DGAAETIDGGGNVLLPGLVDMHVHLREPG--------------REDTETIESGSKAAAK 95
Cdd:cd01300 2 VAVRDGRIVAVGSDAEAkalkGPATEVIDLKGKTVLPGFIDSHSHLLLGGlsllwldlsgvtskEEALARIREDAAAAPP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765312 96 G------GFTAVFTMANTTP--------VTDQPIIAESV-----WAKSQALGLCDVH------PVGSITKGLEGKSLTEF 150
Cdd:cd01300 82 GewilgfGWDESLLGEGRYPtraeldavSPDRPVLLLRRdghsaWVNSAALRLAGITrdtpdpPGGEIVRDADGEPTGVL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765312 151 GMMARSDAKVRMFSDDGKcvQNPQLMRRALEYA--KG------MDVLLAQHAEDDRmtggssAHEGENAARLGLRGWPRV 222
Cdd:cd01300 162 VEAAAALVLEAVPPPTPE--ERRAALRAAARELasLGvttvhdAGGGAADDIEAYR------RLAAAGELTLRVRVALYV 233
|
250 260
....*....|....*....|....*
gi 552765312 223 ---AEESIVARDALLARDYGNRVHI 244
Cdd:cd01300 234 splAEDLLEELGARKNGAGDDRLRL 258
|
|
| PRK07572 |
PRK07572 |
cytosine deaminase; Validated |
18-75 |
6.26e-06 |
|
cytosine deaminase; Validated
Pssm-ID: 181039 Cd Length: 426 Bit Score: 48.09 E-value: 6.26e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 552765312 18 LLIKNIRLYGEGEPTNVLIRGGVIDSIGPEVQADgAAETIDGGGNVLLPGLVDMHVHL 75
Cdd:PRK07572 4 LIVRNANLPDGRTGIDIGIAGGRIAAVEPGLQAE-AAEEIDAAGRLVSPPFVDPHFHM 60
|
|
| PRK15446 |
PRK15446 |
phosphonate metabolism protein PhnM; Provisional |
16-72 |
2.42e-05 |
|
phosphonate metabolism protein PhnM; Provisional
Pssm-ID: 237967 [Multi-domain] Cd Length: 383 Bit Score: 46.33 E-value: 2.42e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 552765312 16 NPLLIKNIRLYGEGE--PTNVLIRGGVIDSIGPEvqADGAAETIDGGGNVLLPGLVDMH 72
Cdd:PRK15446 2 MEMILSNARLVLPDEvvDGSLLIEDGRIAAIDPG--ASALPGAIDAEGDYLLPGLVDLH 58
|
|
| DHOase |
cd01294 |
Dihydroorotase (DHOase) catalyzes the reversible interconversion of carbamoyl aspartate to ... |
246-323 |
2.42e-05 |
|
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: 46.12 E-value: 2.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765312 246 HASTQGTVELLqwaKEHDIPLTAEVTPHHLLMT-DD----KLRTYdgLFrVNPPLREQRDTEALRQALLDGtidC----V 316
Cdd:cd01294 169 HITTADAVEYV---KSCNENVAATITPHHLLLTrDDllggGLNPH--LY-CKPVAKRPEDREALRKAATSG---HpkffL 239
|
....*..
gi 552765312 317 ATDHAPH 323
Cdd:cd01294 240 GSDSAPH 246
|
|
| Imidazolone-5PH |
cd01296 |
Imidazolonepropionase/imidazolone-5-propionate hydrolase (Imidazolone-5PH) catalyzes the third ... |
34-75 |
2.59e-05 |
|
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: 46.10 E-value: 2.59e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 552765312 34 VLIRGGVIDSIGPE--VQADG--AAETIDGGGNVLLPGLVDMHVHL 75
Cdd:cd01296 1 IAIRDGRIAAVGPAasLPAPGpaAAEEIDAGGRAVTPGLVDCHTHL 46
|
|
| PRK08204 |
PRK08204 |
hypothetical protein; Provisional |
34-75 |
3.43e-05 |
|
hypothetical protein; Provisional
Pssm-ID: 181288 [Multi-domain] Cd Length: 449 Bit Score: 46.15 E-value: 3.43e-05
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 552765312 34 VLIRGGVIDSIGPEVQADGAaETIDGGGNVLLPGLVDMHVHL 75
Cdd:PRK08204 26 ILIEGDRIAAVAPSIEAPDA-EVVDARGMIVMPGLVDTHRHT 66
|
|
| PRK07228 |
PRK07228 |
5'-deoxyadenosine deaminase; |
33-75 |
4.11e-05 |
|
5'-deoxyadenosine deaminase;
Pssm-ID: 180895 [Multi-domain] Cd Length: 445 Bit Score: 45.76 E-value: 4.11e-05
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 552765312 33 NVLIRGGVIDSIGPEVQADGAAETIDGGGNVLLPGLVDMHVHL 75
Cdd:PRK07228 23 DVLIEDDRIAAVGDRLDLEDYDDHIDATGKVVIPGLIQGHIHL 65
|
|
| PRK09230 |
PRK09230 |
cytosine deaminase; Provisional |
18-75 |
6.37e-05 |
|
cytosine deaminase; Provisional
Pssm-ID: 181713 Cd Length: 426 Bit Score: 45.08 E-value: 6.37e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 552765312 18 LLIKNIRLYGEGEPTNVLIRGGVIDSIGP-EVQADGAAETIDGGGNVLLPGLVDMHVHL 75
Cdd:PRK09230 6 MTIKNARLPGKEGLWQITIEDGKISAIEPqSEASLEAGEVLDAEGGLAIPPFIEPHIHL 64
|
|
| Met_dep_hydrolase_A |
cd01299 |
Metallo-dependent hydrolases, subgroup A is part of the superfamily of metallo-dependent ... |
54-105 |
7.63e-05 |
|
Metallo-dependent hydrolases, subgroup A 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: 238624 [Multi-domain] Cd Length: 342 Bit Score: 44.59 E-value: 7.63e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 552765312 54 AETIDGGGNVLLPGLVDMHVHLR-EPGREDTETIESGSKAAAKG----------GFTAVFTMA 105
Cdd:cd01299 1 AQVIDLGGKTLMPGLIDAHTHLGsDPGDLPLDLALPVEYRTIRAtrqaraalraGFTTVRDAG 63
|
|
| Met_dep_hydrolase_C |
cd01309 |
Metallo-dependent hydrolases, subgroup C is part of the superfamily of metallo-dependent ... |
39-84 |
7.78e-05 |
|
Metallo-dependent hydrolases, subgroup C is part of the superfamily of metallo-dependent hydrolases, a large group of proteins that show conservation in their 3-dimensional fold (TIM barrel) and in details of their active site. The vast majority of the members have a conserved metal binding site, involving four histidines and one aspartic acid residue. In the common reaction mechanism, the metal ion (or ions) deprotonate a water molecule for a nucleophilic attack on the substrate. The function of this subgroup is unknown.
Pssm-ID: 238634 [Multi-domain] Cd Length: 359 Bit Score: 44.61 E-value: 7.78e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 552765312 39 GVIDSIGPEVQADGAAETIDGGGNVLLPGLVDMHVHL--REPGREDTE 84
Cdd:cd01309 2 GKIVAVGAEITTPADAEVIDAKGKHVTPGLIDAHSHLglDEEGGVRET 49
|
|
| PRK08203 |
PRK08203 |
hydroxydechloroatrazine ethylaminohydrolase; Reviewed |
34-75 |
1.27e-04 |
|
hydroxydechloroatrazine ethylaminohydrolase; Reviewed
Pssm-ID: 236184 [Multi-domain] Cd Length: 451 Bit Score: 44.07 E-value: 1.27e-04
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 552765312 34 VLIRGGVIDSIGP-EVQADGAAETIDGGGNVLLPGLVDMHVHL 75
Cdd:PRK08203 26 LVVEGGRIVEVGPgGALPQPADEVFDARGHVVTPGLVNTHHHF 68
|
|
| PRK06038 |
PRK06038 |
N-ethylammeline chlorohydrolase; Provisional |
18-75 |
4.14e-04 |
|
N-ethylammeline chlorohydrolase; Provisional
Pssm-ID: 180363 [Multi-domain] Cd Length: 430 Bit Score: 42.43 E-value: 4.14e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 552765312 18 LLIKN--IRLYGEGEPTN--VLIRGGVIDSIGPEVQADgAAETIDGGGNVLLPGLVDMHVHL 75
Cdd:PRK06038 4 IIIKNayVLTMDAGDLKKgsVVIEDGTITEVSESTPGD-ADTVIDAKGSVVMPGLVNTHTHA 64
|
|
| PRK09045 |
PRK09045 |
TRZ/ATZ family hydrolase; |
30-74 |
4.54e-04 |
|
TRZ/ATZ family hydrolase;
Pssm-ID: 236366 [Multi-domain] Cd Length: 443 Bit Score: 42.21 E-value: 4.54e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 552765312 30 EPTNVL-------IRGGVIDSIGPEVQAD---GAAETIDGGGNVLLPGLVDMHVH 74
Cdd:PRK09045 20 EPAGVVledhavaIRDGRIVAILPRAEARaryAAAETVELPDHVLIPGLINAHTH 74
|
|
| PRK09228 |
PRK09228 |
guanine deaminase; Provisional |
34-74 |
5.13e-04 |
|
guanine deaminase; Provisional
Pssm-ID: 236419 [Multi-domain] Cd Length: 433 Bit Score: 42.10 E-value: 5.13e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 552765312 34 VLIRGGVIDSIGP--EV--QADGAAETIDGGGNVLLPGLVDMHVH 74
Cdd:PRK09228 34 LLVEDGRIVAAGPyaELraQLPADAEVTDYRGKLILPGFIDTHIH 78
|
|
| PRK06846 |
PRK06846 |
putative deaminase; Validated |
14-75 |
5.23e-04 |
|
putative deaminase; Validated
Pssm-ID: 235873 [Multi-domain] Cd Length: 410 Bit Score: 42.31 E-value: 5.23e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 552765312 14 AENPLLIKNIRL-----YGEGEPT-------NVLIRGGVIDSIGPEVQ-ADGAAETIDGGGNVLLPGLVDMHVHL 75
Cdd:PRK06846 2 TDPHYWLTNVRLetgfdYENGVIVqtetalcTLEIQDGKIVAIRPNKQvPDATLPTYDANGLLMLPAFREMHIHL 76
|
|
| PRK09061 |
PRK09061 |
D-glutamate deacylase; Validated |
33-79 |
6.90e-04 |
|
D-glutamate deacylase; Validated
Pssm-ID: 236369 [Multi-domain] Cd Length: 509 Bit Score: 41.99 E-value: 6.90e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 552765312 33 NVLIRGGVIDSIGpeVQADGAAETIDGGGNVLLPGLVDMHVHLREPG 79
Cdd:PRK09061 40 DVGIKGGKIAAVG--TAAIEGDRTIDATGLVVAPGFIDLHAHGQSVA 84
|
|
| FMDH_A |
cd01304 |
Formylmethanofuran dehydrogenase (FMDH) subunit A; Methanogenic bacteria and archea derive ... |
20-74 |
3.67e-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: 39.70 E-value: 3.67e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765312 20 IKNIRLYG-----EGEPTNVLIRGGvidSIGPEVQADGAAETIDGGGNVLLPGLVDMHVH 74
Cdd:cd01304 1 IKNGTVYDplngiNGEKMDIFIRDG---KIVESSSGAKPAKVIDASGKVVMAGGVDMHSH 57
|
|
| ureC |
PRK13308 |
urease subunit alpha; Reviewed |
20-109 |
3.84e-03 |
|
urease subunit alpha; Reviewed
Pssm-ID: 183965 [Multi-domain] Cd Length: 569 Bit Score: 39.69 E-value: 3.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 552765312 20 IKNIRLYGEGEPTNVLIRGGVIDS--IGPevqadgAAETIDGGGNVLLPGLVDMHVHLREPGREDtETIESGSKAAAKGG 97
Cdd:PRK13308 91 IRDGRIVGIGKAGNPDIMDGVDPRlvVGP------GTDVRPAEGLIATPGAIDVHVHFDSAQLVD-HALASGITTMLGGG 163
|
90
....*....|..
gi 552765312 98 FTAVFTMANTTP 109
Cdd:PRK13308 164 LGPTVGIDSGGP 175
|
|
| PRK06380 |
PRK06380 |
metal-dependent hydrolase; Provisional |
18-75 |
6.03e-03 |
|
metal-dependent hydrolase; Provisional
Pssm-ID: 180548 [Multi-domain] Cd Length: 418 Bit Score: 38.71 E-value: 6.03e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 552765312 18 LLIKNIRLYGEGEP-----TNVLIRGGVIDSIGP-EVQADgaaETIDGGGNVLLPGLVDMHVHL 75
Cdd:PRK06380 3 ILIKNAWIVTQNEKreilqGNVYIEGNKIVYVGDvNEEAD---YIIDATGKVVMPGLINTHAHV 63
|
|
| PRK07203 |
PRK07203 |
putative aminohydrolase SsnA; |
18-75 |
6.11e-03 |
|
putative aminohydrolase SsnA;
Pssm-ID: 235963 [Multi-domain] Cd Length: 442 Bit Score: 38.76 E-value: 6.11e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 552765312 18 LLIKNIRLYgEGEPTN-------VLIRGGVIDSIGPEV---QADGAAETIDGGGNVLLPGLVDMHVHL 75
Cdd:PRK07203 2 LLIGNGTAI-TRDPAKpviedgaIAIEGNVIVEIGTTDelkAKYPDAEFIDAKGKLIMPGLINSHNHI 68
|
|
| PRK07583 |
PRK07583 |
cytosine deaminase; |
32-75 |
8.86e-03 |
|
cytosine deaminase;
Pssm-ID: 236062 Cd Length: 438 Bit Score: 38.43 E-value: 8.86e-03
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 552765312 32 TNVLIRGGVIDSIGPEVQADGAAETIDGGGNVLLPGLVDMHVHL 75
Cdd:PRK07583 41 VDIEIADGKIAAILPAGGAPDELPAVDLKGRMVWPCFVDMHTHL 84
|
|
| |
