|
Name |
Accession |
Description |
Interval |
E-value |
| PyrC |
COG0418 |
Dihydroorotase [Nucleotide transport and metabolism]; Dihydroorotase is part of the Pathway ... |
4-347 |
0e+00 |
|
Dihydroorotase [Nucleotide transport and metabolism]; Dihydroorotase is part of the Pathway/BioSystem: Pyrimidine biosynthesis
Pssm-ID: 440187 Cd Length: 344 Bit Score: 712.64 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052592 4 QPQVLKIRRPDDWHIHLRDGDMLKTVVPYTSEIYGRAIVMPNLVPPVTTVDAAMAYRQRILDAVPAGHDFTPLMTCYLTD 83
Cdd:COG0418 1 MMQTLTIRRPDDWHLHLRDGAMLAAVVPDTARQFGRAIVMPNLVPPVTTVAQALAYRERILAALPAGSDFEPLMTLYLTD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052592 84 SLDPNEVERGFNEGVFTAAKLYPANATTNSSHGVTSIDAIMPVLERMQKLGMPLLVHGEVTHAEIDIFDREARFIETVME 163
Cdd:COG0418 81 NTTPEEIARAKASGVVTAVKLYPAGATTNSDSGVTDIDKIYPVLEAMQEIGMPLLVHGEVTDPDIDIFDREAVFIDRVLE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052592 164 PLRQRLPALKVVFEHITTKDAAEYVRDGNDLIAATITPQHLMFNRNHMLVGGVRPHLYCLPILKRNIHQQALRELVASGF 243
Cdd:COG0418 161 PLRRRFPELKVVFEHITTKEAVDFVRAAGDNVAATITPHHLLYNRNAMLVGGIRPHYYCLPILKRETHRQALRAAATSGN 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052592 244 SRAFLGTDSAPHARHRKEASCGCAGCFNAPTALASYATVFEEMNALEHFEAFCSLNGPRFYGLPVNDTFIELERKASHVE 323
Cdd:COG0418 241 PKFFLGTDSAPHARHAKESACGCAGCYTAPAALELYAEVFEEAGALDKLEAFASLNGPDFYGLPRNTGTITLVREPWTVP 320
|
330 340
....*....|....*....|....
gi 697052592 324 ESIALTDDTLIPFLAGETVNWTVK 347
Cdd:COG0418 321 ESIPFGDDTLVPFRAGETLNWRVV 344
|
|
| pyrC_dimer |
TIGR00856 |
dihydroorotase, homodimeric type; This homodimeric form of dihydroorotase is less common in ... |
7-347 |
0e+00 |
|
dihydroorotase, homodimeric type; This homodimeric form of dihydroorotase is less common in microbial genomes than a related dihydroorotase that appears in a complex with aspartyltranscarbamoylase or as a homologous domain in multifunctional proteins of pyrimidine biosynthesis in higher eukaryotes. [Purines, pyrimidines, nucleosides, and nucleotides, Pyrimidine ribonucleotide biosynthesis]
Pssm-ID: 129935 Cd Length: 341 Bit Score: 573.30 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052592 7 VLKIRRPDDWHIHLRDGDMLKTVVPYTSEIYGRAIVMPNLVPPVTTVDAAMAYRQRILDAVPAGHDFTPLMTCYLTDSLD 86
Cdd:TIGR00856 1 ELTIRRPDDWHLHLRDGAMLKAVLPYTSEIFSRAIVMPNLAPPVTTVEAAVAYRERILDAVPAGHDFTPLMTLYLTDSLT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052592 87 PNEVERGFNEGVFTAAKLYPANATTNSSHGVTSIDAIMPVLERMQKLGMPLLVHGEVTHAEIDIFDREARFIETVMEPLR 166
Cdd:TIGR00856 81 PEELERAKNEGVVRAVKLYPAGATTNSSHGVTDIDAIMPVLEAMEKIGLPLLLHGEVTHGDIDIFDREARFIESVLEPLR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052592 167 QRLPALKVVFEHITTKDAAEYVRDGNDLIAATITPQHLMFNRNHMLVGGVRPHLYCLPILKRNIHQQALRELVASGFSRA 246
Cdd:TIGR00856 161 QRFPALKVVLEHITTKDAIDYVEDGNNRLAATITPQHLMFTRNDLLGGGVNPHLYCLPILKRNIHQQALLELAASGFPKF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052592 247 FLGTDSAPHARHRKEASCGCAGCFNAPTALASYATVFEEMNALEHFEAFCSLNGPRFYGLPVNDTFIELERKASHVEESI 326
Cdd:TIGR00856 241 FLGTDSAPHARHRKESSCGCAGCFSAPTALPSYAEVFEEMNALENLEAFCSDNGPQFYGLPVNSTKIELVKKEQQIPESI 320
|
330 340
....*....|....*....|.
gi 697052592 327 ALTDDTLIPFLAGETVNWTVK 347
Cdd:TIGR00856 321 ALTDDTLVPFRAGETLSWSVK 341
|
|
| DHOase |
cd01294 |
Dihydroorotase (DHOase) catalyzes the reversible interconversion of carbamoyl aspartate to ... |
8-344 |
0e+00 |
|
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: 563.44 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052592 8 LKIRRPDDWHIHLRDGDMLKTVVPYTSEIYGRAIVMPNLVPPVTTVDAAMAYRQRILDAVPaGHDFTPLMTCYLTDSLDP 87
Cdd:cd01294 1 LTIPRPDDMHLHLRDGAMLKLVLPYTARGFSRAIVMPNLKPPVTTTADALAYRERILAADP-GPNFTPLMTLYLTENTTP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052592 88 NEVERGFNEGVFTAAKLYPANATTNSSHGVTSIDAIMPVLERMQKLGMPLLVHGEVTHAEIDIFDREARFIeTVMEPLRQ 167
Cdd:cd01294 80 EELREAKKKGGIRGVKLYPAGATTNSQGGVTDLEKIYPVLEAMQKLGMPLLVHGEVPDFKIDVLDREAKFI-PVLEPLAQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052592 168 RLPALKVVFEHITTKDAAEYVRDGNDLIAATITPQHLMFNRNHMLVGGVRPHLYCLPILKRNIHQQALRELVASGFSRAF 247
Cdd:cd01294 159 RFPKLKIVLEHITTADAVEYVKSCNENVAATITPHHLLLTRDDLLGGGLNPHLYCKPVAKRPEDREALRKAATSGHPKFF 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052592 248 LGTDSAPHARHRKEASCGCAGCFNAPTALASYATVFEEMNALEHFEAFCSLNGPRFYGLPVNDTFIELERKASHVEESIA 327
Cdd:cd01294 239 LGSDSAPHPKSNKESSCGCAGIFSAPIALPYLAEVFEEHNALDKLEAFASDNGPNFYGLPPNKKTITLVKEPWKVPEKIP 318
|
330
....*....|....*..
gi 697052592 328 LTDDTLIPFLAGETVNW 344
Cdd:cd01294 319 FGNNGVVPFRAGETLRW 335
|
|
| PLN02599 |
PLN02599 |
dihydroorotase |
8-346 |
0e+00 |
|
dihydroorotase
Pssm-ID: 178209 [Multi-domain] Cd Length: 364 Bit Score: 514.30 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052592 8 LKIRRPDDWHIHLRDGDMLKTVVPYTSEIYGRAIVMPNLVPPVTTVDAAMAYRQRILDAVPAGHDFTPLMTCYLTDSLDP 87
Cdd:PLN02599 23 LTITRPDDWHLHLRDGAKLAAVVPHSARHFGRAIVMPNLKPPVTTTARALAYRERIMKALPPGSSFEPLMTLYLTDNTTP 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052592 88 NEVERGFNEGVFTAAKLYPANATTNSSHGVTSIDAIMPVLERMQKLGMPLLVHGEVTHAEIDIFDREARFIETVMEPLRQ 167
Cdd:PLN02599 103 EEIKAAKASGVVFAVKLYPAGATTNSQAGVTDLGKCLPVLEEMAEQGMPLLVHGEVTDPSVDIFDREKVFIDTILAPLVQ 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052592 168 RLPALKVVFEHITTKDAAEYVR---DGNdlIAATITPQHLMFNRNHMLVGGVRPHLYCLPILKRNIHQQALRELVASGFS 244
Cdd:PLN02599 183 KLPQLKIVMEHITTMDAVEFVEscgDGN--VAATVTPQHLLLNRNALFQGGLQPHNYCLPVLKREIHREALVKAATSGSK 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052592 245 RAFLGTDSAPHARHRKEASCGCAGCFNAPTALASYATVFEEMNALEHFEAFCSLNGPRFYGLPVNDTFIELERKASHVEE 324
Cdd:PLN02599 261 KFFLGTDSAPHPKRAKEASCGCAGIYSAPVALSLYAKAFEEAGALDKLEAFTSFNGPDFYGLPRNTSTITLVKSAWKVPE 340
|
330 340
....*....|....*....|..
gi 697052592 325 SIALTDDTLIPFLAGETVNWTV 346
Cdd:PLN02599 341 AYSFGGGTVVPMFAGETIPWSV 362
|
|
| Amidohydro_1 |
pfam01979 |
Amidohydrolase family; This family of enzymes are a a large metal dependent hydrolase ... |
15-348 |
3.30e-13 |
|
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: 69.45 E-value: 3.30e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052592 15 DWHIHLRDGDML-KTVVPYTSEIYGRAIVMPNLVPPVTTVDA----AMAYRQRILDAV---PAGHDFT---PLMTCYLTD 83
Cdd:pfam01979 8 DAHVHLEMGLLRgIPVPPEFAYEALRLGITTMLKSGTTTVLDmgatTSTGIEALLEAAeelPLGLRFLgpgCSLDTDGEL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052592 84 SLDPNEVER---------GFNEGVFTAAkLYPANATTNSShgvtsiDAIMPVLERMQKLGMPLLVHgeVTHAEIDIFDRE 154
Cdd:pfam01979 88 EGRKALREKlkagaefikGMADGVVFVG-LAPHGAPTFSD------DELKAALEEAKKYGLPVAIH--ALETKGEVEDAI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052592 155 ARFIETVMEPLRQR-------LPALKVVFEHITTKDAAEyvrdgndliaATITPQHLmfnRNHMLVggvrphLYCLPILK 227
Cdd:pfam01979 159 AAFGGGIEHGTHLEvaesgglLDIIKLILAHGVHLSPTE----------ANLLAEHL---KGAGVA------HCPFSNSK 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052592 228 RNIHQQALRELVASGFsRAFLGTDSapharhrkeASCGCAGCFNAPTALAS-YATVFEEMNALEHFEAFCSLNGPRFYGL 306
Cdd:pfam01979 220 LRSGRIALRKALEDGV-KVGLGTDG---------AGSGNSLNMLEELRLALeLQFDPEGGLSPLEALRMATINPAKALGL 289
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 697052592 307 PVNDTFIELERKAshveeSIALTDDTLIPFLAGETVNWTVKR 348
Cdd:pfam01979 290 DDKVGSIEVGKDA-----DLVVVDLDPLAAFFGLKPDGNVKK 326
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PyrC |
COG0418 |
Dihydroorotase [Nucleotide transport and metabolism]; Dihydroorotase is part of the Pathway ... |
4-347 |
0e+00 |
|
Dihydroorotase [Nucleotide transport and metabolism]; Dihydroorotase is part of the Pathway/BioSystem: Pyrimidine biosynthesis
Pssm-ID: 440187 Cd Length: 344 Bit Score: 712.64 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052592 4 QPQVLKIRRPDDWHIHLRDGDMLKTVVPYTSEIYGRAIVMPNLVPPVTTVDAAMAYRQRILDAVPAGHDFTPLMTCYLTD 83
Cdd:COG0418 1 MMQTLTIRRPDDWHLHLRDGAMLAAVVPDTARQFGRAIVMPNLVPPVTTVAQALAYRERILAALPAGSDFEPLMTLYLTD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052592 84 SLDPNEVERGFNEGVFTAAKLYPANATTNSSHGVTSIDAIMPVLERMQKLGMPLLVHGEVTHAEIDIFDREARFIETVME 163
Cdd:COG0418 81 NTTPEEIARAKASGVVTAVKLYPAGATTNSDSGVTDIDKIYPVLEAMQEIGMPLLVHGEVTDPDIDIFDREAVFIDRVLE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052592 164 PLRQRLPALKVVFEHITTKDAAEYVRDGNDLIAATITPQHLMFNRNHMLVGGVRPHLYCLPILKRNIHQQALRELVASGF 243
Cdd:COG0418 161 PLRRRFPELKVVFEHITTKEAVDFVRAAGDNVAATITPHHLLYNRNAMLVGGIRPHYYCLPILKRETHRQALRAAATSGN 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052592 244 SRAFLGTDSAPHARHRKEASCGCAGCFNAPTALASYATVFEEMNALEHFEAFCSLNGPRFYGLPVNDTFIELERKASHVE 323
Cdd:COG0418 241 PKFFLGTDSAPHARHAKESACGCAGCYTAPAALELYAEVFEEAGALDKLEAFASLNGPDFYGLPRNTGTITLVREPWTVP 320
|
330 340
....*....|....*....|....
gi 697052592 324 ESIALTDDTLIPFLAGETVNWTVK 347
Cdd:COG0418 321 ESIPFGDDTLVPFRAGETLNWRVV 344
|
|
| pyrC_dimer |
TIGR00856 |
dihydroorotase, homodimeric type; This homodimeric form of dihydroorotase is less common in ... |
7-347 |
0e+00 |
|
dihydroorotase, homodimeric type; This homodimeric form of dihydroorotase is less common in microbial genomes than a related dihydroorotase that appears in a complex with aspartyltranscarbamoylase or as a homologous domain in multifunctional proteins of pyrimidine biosynthesis in higher eukaryotes. [Purines, pyrimidines, nucleosides, and nucleotides, Pyrimidine ribonucleotide biosynthesis]
Pssm-ID: 129935 Cd Length: 341 Bit Score: 573.30 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052592 7 VLKIRRPDDWHIHLRDGDMLKTVVPYTSEIYGRAIVMPNLVPPVTTVDAAMAYRQRILDAVPAGHDFTPLMTCYLTDSLD 86
Cdd:TIGR00856 1 ELTIRRPDDWHLHLRDGAMLKAVLPYTSEIFSRAIVMPNLAPPVTTVEAAVAYRERILDAVPAGHDFTPLMTLYLTDSLT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052592 87 PNEVERGFNEGVFTAAKLYPANATTNSSHGVTSIDAIMPVLERMQKLGMPLLVHGEVTHAEIDIFDREARFIETVMEPLR 166
Cdd:TIGR00856 81 PEELERAKNEGVVRAVKLYPAGATTNSSHGVTDIDAIMPVLEAMEKIGLPLLLHGEVTHGDIDIFDREARFIESVLEPLR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052592 167 QRLPALKVVFEHITTKDAAEYVRDGNDLIAATITPQHLMFNRNHMLVGGVRPHLYCLPILKRNIHQQALRELVASGFSRA 246
Cdd:TIGR00856 161 QRFPALKVVLEHITTKDAIDYVEDGNNRLAATITPQHLMFTRNDLLGGGVNPHLYCLPILKRNIHQQALLELAASGFPKF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052592 247 FLGTDSAPHARHRKEASCGCAGCFNAPTALASYATVFEEMNALEHFEAFCSLNGPRFYGLPVNDTFIELERKASHVEESI 326
Cdd:TIGR00856 241 FLGTDSAPHARHRKESSCGCAGCFSAPTALPSYAEVFEEMNALENLEAFCSDNGPQFYGLPVNSTKIELVKKEQQIPESI 320
|
330 340
....*....|....*....|.
gi 697052592 327 ALTDDTLIPFLAGETVNWTVK 347
Cdd:TIGR00856 321 ALTDDTLVPFRAGETLSWSVK 341
|
|
| DHOase |
cd01294 |
Dihydroorotase (DHOase) catalyzes the reversible interconversion of carbamoyl aspartate to ... |
8-344 |
0e+00 |
|
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: 563.44 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052592 8 LKIRRPDDWHIHLRDGDMLKTVVPYTSEIYGRAIVMPNLVPPVTTVDAAMAYRQRILDAVPaGHDFTPLMTCYLTDSLDP 87
Cdd:cd01294 1 LTIPRPDDMHLHLRDGAMLKLVLPYTARGFSRAIVMPNLKPPVTTTADALAYRERILAADP-GPNFTPLMTLYLTENTTP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052592 88 NEVERGFNEGVFTAAKLYPANATTNSSHGVTSIDAIMPVLERMQKLGMPLLVHGEVTHAEIDIFDREARFIeTVMEPLRQ 167
Cdd:cd01294 80 EELREAKKKGGIRGVKLYPAGATTNSQGGVTDLEKIYPVLEAMQKLGMPLLVHGEVPDFKIDVLDREAKFI-PVLEPLAQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052592 168 RLPALKVVFEHITTKDAAEYVRDGNDLIAATITPQHLMFNRNHMLVGGVRPHLYCLPILKRNIHQQALRELVASGFSRAF 247
Cdd:cd01294 159 RFPKLKIVLEHITTADAVEYVKSCNENVAATITPHHLLLTRDDLLGGGLNPHLYCKPVAKRPEDREALRKAATSGHPKFF 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052592 248 LGTDSAPHARHRKEASCGCAGCFNAPTALASYATVFEEMNALEHFEAFCSLNGPRFYGLPVNDTFIELERKASHVEESIA 327
Cdd:cd01294 239 LGSDSAPHPKSNKESSCGCAGIFSAPIALPYLAEVFEEHNALDKLEAFASDNGPNFYGLPPNKKTITLVKEPWKVPEKIP 318
|
330
....*....|....*..
gi 697052592 328 LTDDTLIPFLAGETVNW 344
Cdd:cd01294 319 FGNNGVVPFRAGETLRW 335
|
|
| PLN02599 |
PLN02599 |
dihydroorotase |
8-346 |
0e+00 |
|
dihydroorotase
Pssm-ID: 178209 [Multi-domain] Cd Length: 364 Bit Score: 514.30 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052592 8 LKIRRPDDWHIHLRDGDMLKTVVPYTSEIYGRAIVMPNLVPPVTTVDAAMAYRQRILDAVPAGHDFTPLMTCYLTDSLDP 87
Cdd:PLN02599 23 LTITRPDDWHLHLRDGAKLAAVVPHSARHFGRAIVMPNLKPPVTTTARALAYRERIMKALPPGSSFEPLMTLYLTDNTTP 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052592 88 NEVERGFNEGVFTAAKLYPANATTNSSHGVTSIDAIMPVLERMQKLGMPLLVHGEVTHAEIDIFDREARFIETVMEPLRQ 167
Cdd:PLN02599 103 EEIKAAKASGVVFAVKLYPAGATTNSQAGVTDLGKCLPVLEEMAEQGMPLLVHGEVTDPSVDIFDREKVFIDTILAPLVQ 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052592 168 RLPALKVVFEHITTKDAAEYVR---DGNdlIAATITPQHLMFNRNHMLVGGVRPHLYCLPILKRNIHQQALRELVASGFS 244
Cdd:PLN02599 183 KLPQLKIVMEHITTMDAVEFVEscgDGN--VAATVTPQHLLLNRNALFQGGLQPHNYCLPVLKREIHREALVKAATSGSK 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052592 245 RAFLGTDSAPHARHRKEASCGCAGCFNAPTALASYATVFEEMNALEHFEAFCSLNGPRFYGLPVNDTFIELERKASHVEE 324
Cdd:PLN02599 261 KFFLGTDSAPHPKRAKEASCGCAGIYSAPVALSLYAKAFEEAGALDKLEAFTSFNGPDFYGLPRNTSTITLVKSAWKVPE 340
|
330 340
....*....|....*....|..
gi 697052592 325 SIALTDDTLIPFLAGETVNWTV 346
Cdd:PLN02599 341 AYSFGGGTVVPMFAGETIPWSV 362
|
|
| Amidohydro_1 |
pfam01979 |
Amidohydrolase family; This family of enzymes are a a large metal dependent hydrolase ... |
15-348 |
3.30e-13 |
|
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: 69.45 E-value: 3.30e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052592 15 DWHIHLRDGDML-KTVVPYTSEIYGRAIVMPNLVPPVTTVDA----AMAYRQRILDAV---PAGHDFT---PLMTCYLTD 83
Cdd:pfam01979 8 DAHVHLEMGLLRgIPVPPEFAYEALRLGITTMLKSGTTTVLDmgatTSTGIEALLEAAeelPLGLRFLgpgCSLDTDGEL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052592 84 SLDPNEVER---------GFNEGVFTAAkLYPANATTNSShgvtsiDAIMPVLERMQKLGMPLLVHgeVTHAEIDIFDRE 154
Cdd:pfam01979 88 EGRKALREKlkagaefikGMADGVVFVG-LAPHGAPTFSD------DELKAALEEAKKYGLPVAIH--ALETKGEVEDAI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052592 155 ARFIETVMEPLRQR-------LPALKVVFEHITTKDAAEyvrdgndliaATITPQHLmfnRNHMLVggvrphLYCLPILK 227
Cdd:pfam01979 159 AAFGGGIEHGTHLEvaesgglLDIIKLILAHGVHLSPTE----------ANLLAEHL---KGAGVA------HCPFSNSK 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052592 228 RNIHQQALRELVASGFsRAFLGTDSapharhrkeASCGCAGCFNAPTALAS-YATVFEEMNALEHFEAFCSLNGPRFYGL 306
Cdd:pfam01979 220 LRSGRIALRKALEDGV-KVGLGTDG---------AGSGNSLNMLEELRLALeLQFDPEGGLSPLEALRMATINPAKALGL 289
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 697052592 307 PVNDTFIELERKAshveeSIALTDDTLIPFLAGETVNWTVKR 348
Cdd:pfam01979 290 DDKVGSIEVGKDA-----DLVVVDLDPLAAFFGLKPDGNVKK 326
|
|
| DHOase_IIb |
cd01318 |
Dihydroorotase (DHOase), subgroup IIb; DHOases catalyze the reversible interconversion of ... |
15-319 |
1.54e-11 |
|
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: 64.66 E-value: 1.54e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052592 15 DWHIHLRDGDMLK--TVVPYTSE-IYG---RAIVMPNLVPPVTTVDAamaYRQRILDAvpAGH---DFTplmtCY--LTD 83
Cdd:cd01318 10 DIHVHFREPGLTYkeDFVSGSRAaAAGgvtTVMDMPNTKPPTTTAEA---LYEKLRLA--AAKsvvDYG----LYfgVTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052592 84 SLDPNEVERGFNEGVftaaKLYPAnattnSSHGVTSIDaiMPVLERMQKLGMPLL-VHGEV-------------THAEID 149
Cdd:cd01318 81 SEDLEELDKAPPAGY----KIFMG-----DSTGDLLDD--EETLERIFAEGSVLVtFHAEDedrlrenrkelkgESAHPR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052592 150 IFDREA--RFIETVMEpLRQRLPAlKVVFEHITTKDAAEYVRDGNDLIAATITPQHLMFNRNHmlVGGVRPHLYCLPILK 227
Cdd:cd01318 150 IRDAEAaaVATARALK-LARRHGA-RLHICHVSTPEELKLIKKAKPGVTVEVTPHHLFLDVED--YDRLGTLGKVNPPLR 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052592 228 RNIHQQALRELVASGfSRAFLGTDSAPHARHRKEascgcAGCFNAP-------TALASYAT-VFEEMNALEHFEAFCSLN 299
Cdd:cd01318 226 SREDRKALLQALADG-RIDVIASDHAPHTLEEKR-----KGYPAAPsgipgveTALPLMLTlVNKGILSLSRVVRLTSHN 299
|
330 340
....*....|....*....|
gi 697052592 300 GPRFYGLPvNDTFIELERKA 319
Cdd:cd01318 300 PARIFGIK-NKGRIAEGYDA 318
|
|
| metallo-dependent_hydrolases |
cd01292 |
Superfamily of metallo-dependent hydrolases (also called amidohydrolase superfamily) is a ... |
15-303 |
2.28e-10 |
|
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: 60.42 E-value: 2.28e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052592 15 DWHIHLRDGDMLKTVVPYTSEIYGR------------------------AIVMPNLVPPVTTVDAAMAYRQRILDA---- 66
Cdd:cd01292 3 DTHVHLDGSALRGTRLNLELKEAEElspedlyedtlraleallaggvttVVDMGSTPPPTTTKAAIEAVAEAARASagir 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052592 67 --VPAGHDFTPLMTCYLTDSLDPNEVERGFNEGvFTAAKLYPANATTNsshgvTSIDAIMPVLERMQKLGMPLLVHGEVT 144
Cdd:cd01292 83 vvLGLGIPGVPAAVDEDAEALLLELLRRGLELG-AVGLKLAGPYTATG-----LSDESLRRVLEEARKLGLPVVIHAGEL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052592 145 HAEIdifdreaRFIETVMEPLRqrlPALKVVFEHIT--TKDAAEYVRDGNDLIaaTITPQHLMFNRNHMlvggvrphlyc 222
Cdd:cd01292 157 PDPT-------RALEDLVALLR---LGGRVVIGHVShlDPELLELLKEAGVSL--EVCPLSNYLLGRDG----------- 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052592 223 lpilkrnIHQQALRELVASGfSRAFLGTDSAPHarhrkeascgcAGCFNAPTALASYATVFEEMNALEHFEAFCSLNGPR 302
Cdd:cd01292 214 -------EGAEALRRLLELG-IRVTLGTDGPPH-----------PLGTDLLALLRLLLKVLRLGLSLEEALRLATINPAR 274
|
.
gi 697052592 303 F 303
Cdd:cd01292 275 A 275
|
|
| AllB |
COG0044 |
Dihydroorotase or related cyclic amidohydrolase [Nucleotide transport and metabolism]; ... |
41-307 |
6.22e-08 |
|
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: 53.94 E-value: 6.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052592 41 IVMPNLVPPVTTVDAAMAYRQRILDAVPAghDFTPLMTcyLTDSLDPN--EVERGFNEGVfTAAKLYpanATTNSSHGVT 118
Cdd:COG0044 86 VDMPNTNPVTDTPEALEFKLARAEEKALV--DVGPHGA--LTKGLGENlaELGALAEAGA-VAFKVF---MGSDDGNPVL 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052592 119 SIDAIMPVLERMQKLGMPLLVH--------------GEVT----------HAEIDIFDREARFIETVMEPLRqrlpalkV 174
Cdd:COG0044 158 DDGLLRRALEYAAEFGALVAVHaedpdlirggvmneGKTSprlglkgrpaEAEEEAVARDIALAEETGARLH-------I 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052592 175 VfeHITTKDAAEYVRDGNDL-IAATI--TPQHLMFNrnHMLVGGVRPHLYCLPILKRNIHQQALRELVASG-FSraFLGT 250
Cdd:COG0044 231 V--HVSTAEAVELIREAKARgLPVTAevCPHHLTLT--DEDLERYGTNFKVNPPLRTEEDREALWEGLADGtID--VIAT 304
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 697052592 251 DSAPHARHRKEAScgcagCFNAP-------TALASyatVFEEMNA-----LEHFEAFCSLNGPRFYGLP 307
Cdd:COG0044 305 DHAPHTLEEKELP-----FAEAPngipgleTALPL---LLTELVHkgrlsLERLVELLSTNPARIFGLP 365
|
|
| DHOase_IIa |
cd01317 |
Dihydroorotase (DHOase), subgroup IIa; DHOases catalyze the reversible interconversion of ... |
111-307 |
1.48e-07 |
|
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: 52.62 E-value: 1.48e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052592 111 TNSSHGVTSIDAIMPVLERMQKLGMPLLVH--------------GEVTH----------AEIDIFDREARfietvmepLR 166
Cdd:cd01317 110 SDDGKPIQDAELLRRALEYAAMLDLPIIVHpedpslagggvmneGKVASrlglpgippeAETIMVARDLE--------LA 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052592 167 QRLPAlKVVFEHITTKDAAEYVRDGNDL---IAATITPQHLMFNRNhmLVGGVRPHLYCLPILKRNIHQQALRELVASGF 243
Cdd:cd01317 182 EATGA-RVHFQHLSTARSLELIRKAKAKglpVTAEVTPHHLLLDDE--ALESYDTNAKVNPPLRSEEDREALIEALKDGT 258
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 697052592 244 SRAfLGTDSAPHARHRKEASCGCA--GCFNAPTALASYATVF--EEMNALEHFEAFCSLNGPRFYGLP 307
Cdd:cd01317 259 IDA-IASDHAPHTDEEKDLPFAEAppGIIGLETALPLLWTLLvkGGLLTLPDLIRALSTNPAKILGLP 325
|
|
| PRK02382 |
PRK02382 |
dihydroorotase; Provisional |
15-263 |
2.50e-07 |
|
dihydroorotase; Provisional
Pssm-ID: 179417 [Multi-domain] Cd Length: 443 Bit Score: 51.96 E-value: 2.50e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052592 15 DWHIHLRDGDMLKTVVPYT---SEIYG--RAIV-MPNLVPPVTTVD-----AAMAYRQRILD-AVPAGhdftplmtcyLT 82
Cdd:PRK02382 58 DVHVHFREPGYTHKETWYTgsrSAAAGgvTTVVdQPNTDPPTVDGEsfdekAELAARKSIVDfGINGG----------VT 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052592 83 DSLDPneVERGFNEGVFTAAKLYPANATtnsshGVTSIDA--IMPVLERMQKLGMPLLVHGEvthaEIDIFDREARFIET 160
Cdd:PRK02382 128 GNWDP--LESLWERGVFALGEIFMADST-----GGMGIDEelFEEALAEAARLGVLATVHAE----DEDLFDELAKLLKG 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052592 161 VMEP---LRQRLP---------ALKVV--------FEHITTKDAAEYVRDGNdlIAATITPQHLMFNRNHMlvGGVRPHL 220
Cdd:PRK02382 197 DADAdawSAYRPAaaeaaaverALEVAsetgarihIAHISTPEGVDAARREG--ITCEVTPHHLFLSRRDW--ERLGTFG 272
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 697052592 221 YCLPILKRNIHQQALRELVASGfSRAFLGTDSAPHARHRKEAS 263
Cdd:PRK02382 273 KMNPPLRSEKRREALWERLNDG-TIDVVASDHAPHTREEKDAD 314
|
|
| Cyclic_amidohydrolases |
cd01302 |
Cyclic amidohydrolases, including hydantoinase, dihydropyrimidinase, allantoinase, and ... |
15-311 |
9.11e-07 |
|
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: 50.08 E-value: 9.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052592 15 DWHIHLRDGDMlkTVVPYTSEIYGRA---------IVMPNLVPPVTTVDA-AMAYRQRILDAVPaghDFTplMTCYLTDS 84
Cdd:cd01302 9 DIHVHLRDPGG--TTYKEDFESGSRAaaaggvttvIDMPNTGPPPIDLPAiELKIKLAEESSYV---DFS--FHAGIGPG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052592 85 LDPNEVERGFNEGvFTAAKLYpanatTNSSHGVT---SIDAIMPVLERMQKLGMPLLVhgevtHAEIDIFdrearfietv 161
Cdd:cd01302 82 DVTDELKKLFDAG-INSLKVF-----MNYYFGELfdvDDGTLMRTFLEIASRGGPVMV-----HAERAAQ---------- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052592 162 meplRQRLPALKVVFEHITTKDAAEYVRDGNDL---IAATITPQHLMFNRNHMLVGG----VRPhlyclPILKRNiHQQA 234
Cdd:cd01302 141 ----LAEEAGANVHIAHVSSGEALELIKFAKNKgvkVTCEVCPHHLFLDESMLRLNGawgkVNP-----PLRSKE-DREA 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052592 235 LRELVASGfSRAFLGTDSAPH-ARHRKEASCGCAGCFNAP---TALASYATVFEEMN-ALEHFEAFCSLNGPRFYGLPVN 309
Cdd:cd01302 211 LWEGVKNG-KIDTIASDHAPHsKEEKESGKDIWKAPPGFPgleTRLPILLTEGVKRGlSLETLVEILSENPARIFGLYPK 289
|
..
gi 697052592 310 DT 311
Cdd:cd01302 290 GT 291
|
|
| LigW |
COG2159 |
5-carboxyvanillate decarboxylase LigW (lignin degradation), amidohydro domain [Carbohydrate ... |
15-178 |
2.34e-05 |
|
5-carboxyvanillate decarboxylase LigW (lignin degradation), amidohydro domain [Carbohydrate transport and metabolism];
Pssm-ID: 441762 [Multi-domain] Cd Length: 253 Bit Score: 45.36 E-value: 2.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052592 15 DWHIHLRDGDMLKTVVpytsEIYG--RAIVMPNLVPPVTTVDAAMAYRQRILDAVPAGHD-FTPLMTcyltdsLDPN--- 88
Cdd:COG2159 5 DVHTHLGTPEERLADM----DEAGidKAVLSPTPLADPELAALARAANDWLAELVARYPDrFIGFAT------VDPQdpd 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052592 89 ----EVERGFNEGVFTAAKLYPAnattnsSHGVtSID--AIMPVLERMQKLGMPLLVHGEVTHAEIDIFDREARFIETVM 162
Cdd:COG2159 75 aaveELERAVEELGFRGVKLHPA------VGGF-PLDdpRLDPLYEAAAELGLPVLVHPGTPPGPPPGLDLYYAAPLILS 147
|
170
....*....|....*.
gi 697052592 163 EPLRqRLPALKVVFEH 178
Cdd:COG2159 148 GVAE-RFPDLKFILAH 162
|
|
| PRK04250 |
PRK04250 |
dihydroorotase; Provisional |
15-268 |
2.35e-05 |
|
dihydroorotase; Provisional
Pssm-ID: 235265 [Multi-domain] Cd Length: 398 Bit Score: 45.91 E-value: 2.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052592 15 DWHIHLRDGDML--KTVVPYT-SEIYGRAIV---MPNLVPPVTTVDAaMAYRQRILDavpaGHDFTPLMTCYLTDS--LD 86
Cdd:PRK04250 51 DVHVHLRDFEESykETIESGTkAALHGGITLvfdMPNTKPPIMDEKT-YEKRMRIAE----KKSYADYALNFLIAGncEK 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052592 87 PNEVERGFNEGVFTAA--KLYPANATTN--SSHGVTSIDA-----IMPVLERMQKlgmpllvhgevthAEIDIFDREARF 157
Cdd:PRK04250 126 AEEIKADFYKIFMGAStgGIFSENFEVDyaCAPGIVSVHAedpelIREFPERPPE-------------AEVVAIERALEA 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052592 158 IETVMEPLRqrlpalkvvFEHITTKDAAEYVRDGN-DLIAATITPQHLMFNRNHMLVGgvrPHLYCLPILKRNIHQQALR 236
Cdd:PRK04250 193 GKKLKKPLH---------ICHISTKDGLKLILKSNlPWVSFEVTPHHLFLTRKDYERN---PLLKVYPPLRSEEDRKALW 260
|
250 260 270
....*....|....*....|....*....|...
gi 697052592 237 ElvasGFSRA-FLGTDSAPHARHRKEAscGCAG 268
Cdd:PRK04250 261 E----NFSKIpIIASDHAPHTLEDKEA--GAAG 287
|
|
| pyrC |
PRK09357 |
dihydroorotase; Validated |
178-283 |
6.48e-04 |
|
dihydroorotase; Validated
Pssm-ID: 236479 [Multi-domain] Cd Length: 423 Bit Score: 41.33 E-value: 6.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052592 178 HITTKDAAEYVRDGNDL---IAATITPQHLMFNRNHMLvgGVRPHLYCLPILKRNIHQQALRELVASGfSRAFLGTDSAP 254
Cdd:PRK09357 231 HVSTAGSVELIRWAKALgikVTAEVTPHHLLLTDEDLL--TYDPNYKVNPPLRTEEDREALIEGLKDG-TIDAIATDHAP 307
|
90 100 110
....*....|....*....|....*....|.
gi 697052592 255 HARHRKEASCGCA--GCFNAPTALASYATVF 283
Cdd:PRK09357 308 HAREEKECEFEAApfGITGLETALSLLYTTL 338
|
|
| D-HYD |
cd01314 |
D-hydantoinases (D-HYD) also called dihydropyrimidases (DHPase) and related proteins; DHPases ... |
115-254 |
1.47e-03 |
|
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: 40.28 E-value: 1.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052592 115 HGVTSI--------------DAIMPVLERMQKLGMPLLVHGE--------------------VTHA-------EIDIFDR 153
Cdd:cd01314 142 KGISSFkvfmaykgllmvddEELLDVLKRAKELGALVMVHAEngdviaelqkkllaqgktgpEYHAlsrppevEAEATAR 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697052592 154 EARFIETVMEPLRqrlpalkVVfeHITTKDAAEYVRD----GNDLIAATItPQHLMFNRNHMLVGGVRPHLY-CLPILKR 228
Cdd:cd01314 222 AIRLAELAGAPLY-------IV--HVSSKEAADEIARarkkGLPVYGETC-PQYLLLDDSDYWKDWFEGAKYvCSPPLRP 291
|
170 180
....*....|....*....|....*.
gi 697052592 229 NIHQQALRELVASGFSRAFlGTDSAP 254
Cdd:cd01314 292 KEDQEALWDGLSSGTLQTV-GSDHCP 316
|
|
| |
