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Conserved domains on  [gi|507080584|ref|WP_016151338|]
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MULTISPECIES: dihydroorotase [Enterobacteriaceae]

Protein Classification

dihydroorotase( domain architecture ID 10785469)

dihydroorotase catalyzes the reversible interconversion of carbamoyl aspartate to dihydroorotate, a key reaction in pyrimidine biosynthesis

CATH:  3.20.20.140|2.30.40.10
EC:  3.5.2.3
Gene Ontology:  GO:0004151|GO:0008270|GO:0006221
PubMed:  11401542|9144792|12626710
SCOP:  4002199|4002171

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PyrC COG0418
Dihydroorotase [Nucleotide transport and metabolism]; Dihydroorotase is part of the Pathway ...
 14-355 0e+00

Dihydroorotase [Nucleotide transport and metabolism]; Dihydroorotase is part of the Pathway/BioSystem: Pyrimidine biosynthesis


:

Pssm-ID: 440187  Cd Length: 344  Bit Score: 597.46  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507080584  14 LTLRRPDDFHLHLRDGEILKAVLPFTTKQFARAVVMPNLNPPVTTVAAMEAYREIILAAVPQGHDFTPLMTLYLCDDTLP 93
Cdd:COG0418    5 LTIRRPDDWHLHLRDGAMLAAVVPDTARQFGRAIVMPNLVPPVTTVAQALAYRERILAALPAGSDFEPLMTLYLTDNTTP 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507080584  94 EVIRVGHQKGILTAVKWYPAGATTHAEYGVTSVSRIRGCLDILQALGIPLLIHGESTRPDVDIFDRERVFIeDTVME-LR 172
Cdd:COG0418   85 EEIARAKASGVVTAVKLYPAGATTNSDSGVTDIDKIYPVLEAMQEIGMPLLVHGEVTDPDIDIFDREAVFI-DRVLEpLR 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507080584 173 CNYPQLKIVLEHITTQDAVRYIQEQEDGLtAATITPQHLLFNRNVLFNGGIRPHYYCLPVLKREYHRQSLLKAATSGDRR 252
Cdd:COG0418  164 RRFPELKVVFEHITTKEAVDFVRAAGDNV-AATITPHHLLYNRNAMLVGGIRPHYYCLPILKRETHRQALRAAATSGNPK 242

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507080584 253 FFAGTDSAPHPRTAKLAACGCAGIFNAPSALECYATAFEAAGALPHLQAFVSEYGARFYGLPLNTGTVTLARQPLILPEP 332
Cdd:COG0418  243 FFLGTDSAPHARHAKESACGCAGCYTAPAALELYAEVFEEAGALDKLEAFASLNGPDFYGLPRNTGTITLVREPWTVPES 322

                        330       340
                 ....*....|....*....|....
gi 507080584 333 LVVTEHvQIDPF-PGEvSLNWRLV 355
Cdd:COG0418  323 IPFGDD-TLVPFrAGE-TLNWRVV 344
 
Name Accession Description Interval E-value
PyrC COG0418
Dihydroorotase [Nucleotide transport and metabolism]; Dihydroorotase is part of the Pathway ...
 14-355 0e+00

Dihydroorotase [Nucleotide transport and metabolism]; Dihydroorotase is part of the Pathway/BioSystem: Pyrimidine biosynthesis


Pssm-ID: 440187  Cd Length: 344  Bit Score: 597.46  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507080584  14 LTLRRPDDFHLHLRDGEILKAVLPFTTKQFARAVVMPNLNPPVTTVAAMEAYREIILAAVPQGHDFTPLMTLYLCDDTLP 93
Cdd:COG0418    5 LTIRRPDDWHLHLRDGAMLAAVVPDTARQFGRAIVMPNLVPPVTTVAQALAYRERILAALPAGSDFEPLMTLYLTDNTTP 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507080584  94 EVIRVGHQKGILTAVKWYPAGATTHAEYGVTSVSRIRGCLDILQALGIPLLIHGESTRPDVDIFDRERVFIeDTVME-LR 172
Cdd:COG0418   85 EEIARAKASGVVTAVKLYPAGATTNSDSGVTDIDKIYPVLEAMQEIGMPLLVHGEVTDPDIDIFDREAVFI-DRVLEpLR 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507080584 173 CNYPQLKIVLEHITTQDAVRYIQEQEDGLtAATITPQHLLFNRNVLFNGGIRPHYYCLPVLKREYHRQSLLKAATSGDRR 252
Cdd:COG0418  164 RRFPELKVVFEHITTKEAVDFVRAAGDNV-AATITPHHLLYNRNAMLVGGIRPHYYCLPILKRETHRQALRAAATSGNPK 242

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507080584 253 FFAGTDSAPHPRTAKLAACGCAGIFNAPSALECYATAFEAAGALPHLQAFVSEYGARFYGLPLNTGTVTLARQPLILPEP 332
Cdd:COG0418  243 FFLGTDSAPHARHAKESACGCAGCYTAPAALELYAEVFEEAGALDKLEAFASLNGPDFYGLPRNTGTITLVREPWTVPES 322

                        330       340
                 ....*....|....*....|....
gi 507080584 333 LVVTEHvQIDPF-PGEvSLNWRLV 355
Cdd:COG0418  323 IPFGDD-TLVPFrAGE-TLNWRVV 344
PLN02599 PLN02599
dihydroorotase
 14-331 1.57e-172

dihydroorotase


Pssm-ID: 178209 [Multi-domain]  Cd Length: 364  Bit Score: 484.26  E-value: 1.57e-172
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507080584  14 LTLRRPDDFHLHLRDGEILKAVLPFTTKQFARAVVMPNLNPPVTTVAAMEAYREIILAAVPQGHDFTPLMTLYLCDDTLP 93
Cdd:PLN02599  23 LTITRPDDWHLHLRDGAKLAAVVPHSARHFGRAIVMPNLKPPVTTTARALAYRERIMKALPPGSSFEPLMTLYLTDNTTP 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507080584  94 EVIRVGHQKGILTAVKWYPAGATTHAEYGVTSVSRirgCLDILQA---LGIPLLIHGESTRPDVDIFDRERVFIEDTVME 170
Cdd:PLN02599 103 EEIKAAKASGVVFAVKLYPAGATTNSQAGVTDLGK---CLPVLEEmaeQGMPLLVHGEVTDPSVDIFDREKVFIDTILAP 179

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507080584 171 LRCNYPQLKIVLEHITTQDAVRYIQEQEDGLTAATITPQHLLFNRNVLFNGGIRPHYYCLPVLKREYHRQSLLKAATSGD 250
Cdd:PLN02599 180 LVQKLPQLKIVMEHITTMDAVEFVESCGDGNVAATVTPQHLLLNRNALFQGGLQPHNYCLPVLKREIHREALVKAATSGS 259

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507080584 251 RRFFAGTDSAPHPRTAKLAACGCAGIFNAPSALECYATAFEAAGALPHLQAFVSEYGARFYGLPLNTGTVTLARQPLILP 330
Cdd:PLN02599 260 KKFFLGTDSAPHPKRAKEASCGCAGIYSAPVALSLYAKAFEEAGALDKLEAFTSFNGPDFYGLPRNTSTITLVKSAWKVP 339


                 .
gi 507080584 331 E 331
Cdd:PLN02599 340 E 340
DHOase cd01294
Dihydroorotase (DHOase) catalyzes the reversible interconversion of carbamoyl aspartate to ...
 14-352 1.39e-165

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: 465.60  E-value: 1.39e-165
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507080584  14 LTLRRPDDFHLHLRDGEILKAVLPFTTKQFARAVVMPNLNPPVTTVAAMEAYREIILAAVPqGHDFTPLMTLYLCDDTLP 93
Cdd:cd01294    1 LTIPRPDDMHLHLRDGAMLKLVLPYTARGFSRAIVMPNLKPPVTTTADALAYRERILAADP-GPNFTPLMTLYLTENTTP 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507080584  94 EVIRVGHQKGILTAVKWYPAGATTHAEYGVTSVSRIRGCLDILQALGIPLLIHGESTRPDVDIFDRERVFIedTVME-LR 172
Cdd:cd01294   80 EELREAKKKGGIRGVKLYPAGATTNSQGGVTDLEKIYPVLEAMQKLGMPLLVHGEVPDFKIDVLDREAKFI--PVLEpLA 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507080584 173 CNYPQLKIVLEHITTQDAVRYIqEQEDGLTAATITPQHLLFNRNVLFNGGIRPHYYCLPVLKREYHRQSLLKAATSGDRR 252
Cdd:cd01294  158 QRFPKLKIVLEHITTADAVEYV-KSCNENVAATITPHHLLLTRDDLLGGGLNPHLYCKPVAKRPEDREALRKAATSGHPK 236

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507080584 253 FFAGTDSAPHPRTAKLAACGCAGIFNAPSALECYATAFEAAGALPHLQAFVSEYGARFYGLPLNTGTVTLARQPLILPEp 332
Cdd:cd01294  237 FFLGSDSAPHPKSNKESSCGCAGIFSAPIALPYLAEVFEEHNALDKLEAFASDNGPNFYGLPPNKKTITLVKEPWKVPE- 315

                        330       340
                 ....*....|....*....|
gi 507080584 333 LVVTEHVQIDPFPGEVSLNW 352
Cdd:cd01294  316 KIPFGNNGVVPFRAGETLRW 335
pyrC_dimer TIGR00856
dihydroorotase, homodimeric type; This homodimeric form of dihydroorotase is less common in ...
 14-355 2.48e-147

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: 419.61  E-value: 2.48e-147
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507080584   14 LTLRRPDDFHLHLRDGEILKAVLPFTTKQFARAVVMPNLNPPVTTVAAMEAYREIILAAVPQGHDFTPLMTLYLCDDTLP 93
Cdd:TIGR00856   2 LTIRRPDDWHLHLRDGAMLKAVLPYTSEIFSRAIVMPNLAPPVTTVEAAVAYRERILDAVPAGHDFTPLMTLYLTDSLTP 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507080584   94 EVIRVGHQKGILTAVKWYPAGATTHAEYGVTSVSRIRGCLDILQALGIPLLIHGESTRPDVDIFDRERVFIEDTVMELRC 173
Cdd:TIGR00856  82 EELERAKNEGVVRAVKLYPAGATTNSSHGVTDIDAIMPVLEAMEKIGLPLLLHGEVTHGDIDIFDREARFIESVLEPLRQ 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507080584  174 NYPQLKIVLEHITTQDAVRYIQEQEDGLtAATITPQHLLFNRNVLFNGGIRPHYYCLPVLKREYHRQSLLKAATSGDRRF 253
Cdd:TIGR00856 162 RFPALKVVLEHITTKDAIDYVEDGNNRL-AATITPQHLMFTRNDLLGGGVNPHLYCLPILKRNIHQQALLELAASGFPKF 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507080584  254 FAGTDSAPHPRTAKLAACGCAGIFNAPSALECYATAFEAAGALPHLQAFVSEYGARFYGLPLNTGTVTLARQPLILPEPL 333
Cdd:TIGR00856 241 FLGTDSAPHARHRKESSCGCAGCFSAPTALPSYAEVFEEMNALENLEAFCSDNGPQFYGLPVNSTKIELVKKEQQIPESI 320

                         330       340
                  ....*....|....*....|..
gi 507080584  334 VVTEhVQIDPFPGEVSLNWRLV 355
Cdd:TIGR00856 321 ALTD-DTLVPFRAGETLSWSVK 341
Amidohydro_1 pfam01979
Amidohydrolase family; This family of enzymes are a a large metal dependent hydrolase ...
 21-321 4.05e-12

Amidohydrolase family; This family of enzymes are a a large metal dependent hydrolase superfamily. The family includes Adenine deaminase EC:3.5.4.2 that hydrolyses adenine to form hypoxanthine and ammonia. Adenine deaminases reaction is important for adenine utilization as a purine and also as a nitrogen source. This family also includes dihydroorotase and N-acetylglucosamine-6-phosphate deacetylases, EC:3.5.1.25 These enzymes catalyze the reaction N-acetyl-D-glucosamine 6-phosphate + H2O <=> D-glucosamine 6-phosphate + acetate. This family includes the catalytic domain of urease alpha subunit. Dihydroorotases (EC:3.5.2.3) are also included.


Pssm-ID: 460401 [Multi-domain]  Cd Length: 334  Bit Score: 66.37  E-value: 4.05e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507080584   21 DFHLHLRDGEILKAVLP-FTTKQFARAVVMPNLNPPVTTVAAM------------EAYREIIL------AAVPQGHDFT- 80
Cdd:pfam01979   8 DAHVHLEMGLLRGIPVPpEFAYEALRLGITTMLKSGTTTVLDMgattstgieallEAAEELPLglrflgPGCSLDTDGEl 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507080584   81 -PLMTLYLCDDTLPEVIRVGHQKGILTAVKWYPAGATTHAEygvtsvsrIRGCLDILQALGIPLLIHGESTrpDVDIFDR 159
Cdd:pfam01979  88 eGRKALREKLKAGAEFIKGMADGVVFVGLAPHGAPTFSDDE--------LKAALEEAKKYGLPVAIHALET--KGEVEDA 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507080584  160 ERVFIEDT-------VMELRCNYPQLKIVLEHITTQDAvryiqeqedglTAATITPQHLLFNRNVLfnggirphyYCLPV 232
Cdd:pfam01979 158 IAAFGGGIehgthleVAESGGLLDIIKLILAHGVHLSP-----------TEANLLAEHLKGAGVAH---------CPFSN 217

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507080584  233 LKREYHRQSLLKAATSGDRrFFAGTDSAPHPRTAKLAACGcagIFNAPsalecyaTAFEAAGALPHLQAF--VSEYGARF 310
Cdd:pfam01979 218 SKLRSGRIALRKALEDGVK-VGLGTDGAGSGNSLNMLEEL---RLALE-------LQFDPEGGLSPLEALrmATINPAKA 286

                         330
                  ....*....|.
gi 507080584  311 YGLPLNTGTVT 321
Cdd:pfam01979 287 LGLDDKVGSIE 297
 
Name Accession Description Interval E-value
PyrC COG0418
Dihydroorotase [Nucleotide transport and metabolism]; Dihydroorotase is part of the Pathway ...
 14-355 0e+00

Dihydroorotase [Nucleotide transport and metabolism]; Dihydroorotase is part of the Pathway/BioSystem: Pyrimidine biosynthesis


Pssm-ID: 440187  Cd Length: 344  Bit Score: 597.46  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507080584  14 LTLRRPDDFHLHLRDGEILKAVLPFTTKQFARAVVMPNLNPPVTTVAAMEAYREIILAAVPQGHDFTPLMTLYLCDDTLP 93
Cdd:COG0418    5 LTIRRPDDWHLHLRDGAMLAAVVPDTARQFGRAIVMPNLVPPVTTVAQALAYRERILAALPAGSDFEPLMTLYLTDNTTP 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507080584  94 EVIRVGHQKGILTAVKWYPAGATTHAEYGVTSVSRIRGCLDILQALGIPLLIHGESTRPDVDIFDRERVFIeDTVME-LR 172
Cdd:COG0418   85 EEIARAKASGVVTAVKLYPAGATTNSDSGVTDIDKIYPVLEAMQEIGMPLLVHGEVTDPDIDIFDREAVFI-DRVLEpLR 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507080584 173 CNYPQLKIVLEHITTQDAVRYIQEQEDGLtAATITPQHLLFNRNVLFNGGIRPHYYCLPVLKREYHRQSLLKAATSGDRR 252
Cdd:COG0418  164 RRFPELKVVFEHITTKEAVDFVRAAGDNV-AATITPHHLLYNRNAMLVGGIRPHYYCLPILKRETHRQALRAAATSGNPK 242

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507080584 253 FFAGTDSAPHPRTAKLAACGCAGIFNAPSALECYATAFEAAGALPHLQAFVSEYGARFYGLPLNTGTVTLARQPLILPEP 332
Cdd:COG0418  243 FFLGTDSAPHARHAKESACGCAGCYTAPAALELYAEVFEEAGALDKLEAFASLNGPDFYGLPRNTGTITLVREPWTVPES 322

                        330       340
                 ....*....|....*....|....
gi 507080584 333 LVVTEHvQIDPF-PGEvSLNWRLV 355
Cdd:COG0418  323 IPFGDD-TLVPFrAGE-TLNWRVV 344
PLN02599 PLN02599
dihydroorotase
 14-331 1.57e-172

dihydroorotase


Pssm-ID: 178209 [Multi-domain]  Cd Length: 364  Bit Score: 484.26  E-value: 1.57e-172
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507080584  14 LTLRRPDDFHLHLRDGEILKAVLPFTTKQFARAVVMPNLNPPVTTVAAMEAYREIILAAVPQGHDFTPLMTLYLCDDTLP 93
Cdd:PLN02599  23 LTITRPDDWHLHLRDGAKLAAVVPHSARHFGRAIVMPNLKPPVTTTARALAYRERIMKALPPGSSFEPLMTLYLTDNTTP 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507080584  94 EVIRVGHQKGILTAVKWYPAGATTHAEYGVTSVSRirgCLDILQA---LGIPLLIHGESTRPDVDIFDRERVFIEDTVME 170
Cdd:PLN02599 103 EEIKAAKASGVVFAVKLYPAGATTNSQAGVTDLGK---CLPVLEEmaeQGMPLLVHGEVTDPSVDIFDREKVFIDTILAP 179

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507080584 171 LRCNYPQLKIVLEHITTQDAVRYIQEQEDGLTAATITPQHLLFNRNVLFNGGIRPHYYCLPVLKREYHRQSLLKAATSGD 250
Cdd:PLN02599 180 LVQKLPQLKIVMEHITTMDAVEFVESCGDGNVAATVTPQHLLLNRNALFQGGLQPHNYCLPVLKREIHREALVKAATSGS 259

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507080584 251 RRFFAGTDSAPHPRTAKLAACGCAGIFNAPSALECYATAFEAAGALPHLQAFVSEYGARFYGLPLNTGTVTLARQPLILP 330
Cdd:PLN02599 260 KKFFLGTDSAPHPKRAKEASCGCAGIYSAPVALSLYAKAFEEAGALDKLEAFTSFNGPDFYGLPRNTSTITLVKSAWKVP 339


                 .
gi 507080584 331 E 331
Cdd:PLN02599 340 E 340
DHOase cd01294
Dihydroorotase (DHOase) catalyzes the reversible interconversion of carbamoyl aspartate to ...
 14-352 1.39e-165

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: 465.60  E-value: 1.39e-165
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507080584  14 LTLRRPDDFHLHLRDGEILKAVLPFTTKQFARAVVMPNLNPPVTTVAAMEAYREIILAAVPqGHDFTPLMTLYLCDDTLP 93
Cdd:cd01294    1 LTIPRPDDMHLHLRDGAMLKLVLPYTARGFSRAIVMPNLKPPVTTTADALAYRERILAADP-GPNFTPLMTLYLTENTTP 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507080584  94 EVIRVGHQKGILTAVKWYPAGATTHAEYGVTSVSRIRGCLDILQALGIPLLIHGESTRPDVDIFDRERVFIedTVME-LR 172
Cdd:cd01294   80 EELREAKKKGGIRGVKLYPAGATTNSQGGVTDLEKIYPVLEAMQKLGMPLLVHGEVPDFKIDVLDREAKFI--PVLEpLA 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507080584 173 CNYPQLKIVLEHITTQDAVRYIqEQEDGLTAATITPQHLLFNRNVLFNGGIRPHYYCLPVLKREYHRQSLLKAATSGDRR 252
Cdd:cd01294  158 QRFPKLKIVLEHITTADAVEYV-KSCNENVAATITPHHLLLTRDDLLGGGLNPHLYCKPVAKRPEDREALRKAATSGHPK 236

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507080584 253 FFAGTDSAPHPRTAKLAACGCAGIFNAPSALECYATAFEAAGALPHLQAFVSEYGARFYGLPLNTGTVTLARQPLILPEp 332
Cdd:cd01294  237 FFLGSDSAPHPKSNKESSCGCAGIFSAPIALPYLAEVFEEHNALDKLEAFASDNGPNFYGLPPNKKTITLVKEPWKVPE- 315

                        330       340
                 ....*....|....*....|
gi 507080584 333 LVVTEHVQIDPFPGEVSLNW 352
Cdd:cd01294  316 KIPFGNNGVVPFRAGETLRW 335
pyrC_dimer TIGR00856
dihydroorotase, homodimeric type; This homodimeric form of dihydroorotase is less common in ...
 14-355 2.48e-147

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: 419.61  E-value: 2.48e-147
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507080584   14 LTLRRPDDFHLHLRDGEILKAVLPFTTKQFARAVVMPNLNPPVTTVAAMEAYREIILAAVPQGHDFTPLMTLYLCDDTLP 93
Cdd:TIGR00856   2 LTIRRPDDWHLHLRDGAMLKAVLPYTSEIFSRAIVMPNLAPPVTTVEAAVAYRERILDAVPAGHDFTPLMTLYLTDSLTP 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507080584   94 EVIRVGHQKGILTAVKWYPAGATTHAEYGVTSVSRIRGCLDILQALGIPLLIHGESTRPDVDIFDRERVFIEDTVMELRC 173
Cdd:TIGR00856  82 EELERAKNEGVVRAVKLYPAGATTNSSHGVTDIDAIMPVLEAMEKIGLPLLLHGEVTHGDIDIFDREARFIESVLEPLRQ 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507080584  174 NYPQLKIVLEHITTQDAVRYIQEQEDGLtAATITPQHLLFNRNVLFNGGIRPHYYCLPVLKREYHRQSLLKAATSGDRRF 253
Cdd:TIGR00856 162 RFPALKVVLEHITTKDAIDYVEDGNNRL-AATITPQHLMFTRNDLLGGGVNPHLYCLPILKRNIHQQALLELAASGFPKF 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507080584  254 FAGTDSAPHPRTAKLAACGCAGIFNAPSALECYATAFEAAGALPHLQAFVSEYGARFYGLPLNTGTVTLARQPLILPEPL 333
Cdd:TIGR00856 241 FLGTDSAPHARHRKESSCGCAGCFSAPTALPSYAEVFEEMNALENLEAFCSDNGPQFYGLPVNSTKIELVKKEQQIPESI 320

                         330       340
                  ....*....|....*....|..
gi 507080584  334 VVTEhVQIDPFPGEVSLNWRLV 355
Cdd:TIGR00856 321 ALTD-DTLVPFRAGETLSWSVK 341
Amidohydro_1 pfam01979
Amidohydrolase family; This family of enzymes are a a large metal dependent hydrolase ...
 21-321 4.05e-12

Amidohydrolase family; This family of enzymes are a a large metal dependent hydrolase superfamily. The family includes Adenine deaminase EC:3.5.4.2 that hydrolyses adenine to form hypoxanthine and ammonia. Adenine deaminases reaction is important for adenine utilization as a purine and also as a nitrogen source. This family also includes dihydroorotase and N-acetylglucosamine-6-phosphate deacetylases, EC:3.5.1.25 These enzymes catalyze the reaction N-acetyl-D-glucosamine 6-phosphate + H2O <=> D-glucosamine 6-phosphate + acetate. This family includes the catalytic domain of urease alpha subunit. Dihydroorotases (EC:3.5.2.3) are also included.


Pssm-ID: 460401 [Multi-domain]  Cd Length: 334  Bit Score: 66.37  E-value: 4.05e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507080584   21 DFHLHLRDGEILKAVLP-FTTKQFARAVVMPNLNPPVTTVAAM------------EAYREIIL------AAVPQGHDFT- 80
Cdd:pfam01979   8 DAHVHLEMGLLRGIPVPpEFAYEALRLGITTMLKSGTTTVLDMgattstgieallEAAEELPLglrflgPGCSLDTDGEl 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507080584   81 -PLMTLYLCDDTLPEVIRVGHQKGILTAVKWYPAGATTHAEygvtsvsrIRGCLDILQALGIPLLIHGESTrpDVDIFDR 159
Cdd:pfam01979  88 eGRKALREKLKAGAEFIKGMADGVVFVGLAPHGAPTFSDDE--------LKAALEEAKKYGLPVAIHALET--KGEVEDA 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507080584  160 ERVFIEDT-------VMELRCNYPQLKIVLEHITTQDAvryiqeqedglTAATITPQHLLFNRNVLfnggirphyYCLPV 232
Cdd:pfam01979 158 IAAFGGGIehgthleVAESGGLLDIIKLILAHGVHLSP-----------TEANLLAEHLKGAGVAH---------CPFSN 217

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507080584  233 LKREYHRQSLLKAATSGDRrFFAGTDSAPHPRTAKLAACGcagIFNAPsalecyaTAFEAAGALPHLQAF--VSEYGARF 310
Cdd:pfam01979 218 SKLRSGRIALRKALEDGVK-VGLGTDGAGSGNSLNMLEEL---RLALE-------LQFDPEGGLSPLEALrmATINPAKA 286

                         330
                  ....*....|.
gi 507080584  311 YGLPLNTGTVT 321
Cdd:pfam01979 287 LGLDDKVGSIE 297
Cyclic_amidohydrolases cd01302
Cyclic amidohydrolases, including hydantoinase, dihydropyrimidinase, allantoinase, and ...
 21-332 5.52e-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: 50.85  E-value: 5.52e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507080584  21 DFHLHLRDGEILKAVLPFTTKQFARA-------VVMPNLNPPVTTVAAMEayrEIILAAVPQGH-DFTplMTLYLCD-DT 91
Cdd:cd01302    9 DIHVHLRDPGGTTYKEDFESGSRAAAaggvttvIDMPNTGPPPIDLPAIE---LKIKLAEESSYvDFS--FHAGIGPgDV 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507080584  92 LPEvIRVGHQKGIlTAVKWYpaGATTHAEYGVTSVSRIRGCLDILQALGIPLLIHGEstrpdvdifdRERVFIEDTvmel 171
Cdd:cd01302   84 TDE-LKKLFDAGI-NSLKVF--MNYYFGELFDVDDGTLMRTFLEIASRGGPVMVHAE----------RAAQLAEEA---- 145

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507080584 172 rcnypQLKIVLEHITTQDAVRYIQE-QEDGLTA-ATITPQHLLFNRNVLFNGG----IRPhyyclPVLKREyHRQSLLKA 245
Cdd:cd01302  146 -----GANVHIAHVSSGEALELIKFaKNKGVKVtCEVCPHHLFLDESMLRLNGawgkVNP-----PLRSKE-DREALWEG 214

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507080584 246 ATSGDRRFFAgTDSAPHPRTAKlaaCGCAGIFNAPSA---LECYA----TAFEAAG-ALPHLQAFVSEYGARFYGLPLNT 317
Cdd:cd01302  215 VKNGKIDTIA-SDHAPHSKEEK---ESGKDIWKAPPGfpgLETRLpillTEGVKRGlSLETLVEILSENPARIFGLYPKG 290

                        330
                 ....*....|....*
gi 507080584 318 GTVTLARQPLILPEP 332
Cdd:cd01302  291 TIAVGYDADLVIVDP 305
DHOase_IIa cd01317
Dihydroorotase (DHOase), subgroup IIa; DHOases catalyze the reversible interconversion of ...
 179-314 2.71e-06

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: 48.77  E-value: 2.71e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507080584 179 KIVLEHITTQDAVRYIQE-QEDGLTA-ATITPQHLLFNRNVLFNGgiRPHYYCLPVLKREYHRQSLLKAATSGDRRFFAg 256
Cdd:cd01317  187 RVHFQHLSTARSLELIRKaKAKGLPVtAEVTPHHLLLDDEALESY--DTNAKVNPPLRSEEDREALIEALKDGTIDAIA- 263

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 507080584 257 TDSAPHPRTAKLAACGCA--GIFNAPSALECYATAFEAAGALPHLQA--FVSEYGARFYGLP 314
Cdd:cd01317  264 SDHAPHTDEEKDLPFAEAppGIIGLETALPLLWTLLVKGGLLTLPDLirALSTNPAKILGLP 325
DHOase_IIb cd01318
Dihydroorotase (DHOase), subgroup IIb; DHOases catalyze the reversible interconversion of ...
 12-314 3.13e-06

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: 48.48  E-value: 3.13e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507080584  12 GLLTLRRPDDFHLHLRD-GEILKAVLPFTTKQFAR----AVV-MPNLNPPVTTvaaMEAYRE-------------IILAA 72
Cdd:cd01318    1 GLLILPGVIDIHVHFREpGLTYKEDFVSGSRAAAAggvtTVMdMPNTKPPTTT---AEALYEklrlaaaksvvdyGLYFG 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507080584  73 VPQGHDFTPLmtlylcdDTLPEVirvghqkgiltAVKWYPAGAT--THAEYGVTSvsrirgclDILQALGIPLLIHGES- 149
Cdd:cd01318   78 VTGSEDLEEL-------DKAPPA-----------GYKIFMGDSTgdLLDDEETLE--------RIFAEGSVLVTFHAEDe 131

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507080584 150 ------TRPDVDIFDRERVFIEDT-------VMELRCNYPQLKIVLeHITTQDAVRYIQEQEDGLTAaTITPQHLLFNR- 215
Cdd:cd01318  132 drlrenRKELKGESAHPRIRDAEAaavatarALKLARRHGARLHIC-HVSTPEELKLIKKAKPGVTV-EVTPHHLFLDVe 209

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507080584 216 NVLFNGGIrphYYCLPVLKREYHRQSLLKAATSGDRRFFAgTDSAPHPRTAKLaacgcAGIFNAPS---ALECYATAFEA 292
Cdd:cd01318  210 DYDRLGTL---GKVNPPLRSREDRKALLQALADGRIDVIA-SDHAPHTLEEKR-----KGYPAAPSgipGVETALPLMLT 280

                        330       340
                 ....*....|....*....|....*...
gi 507080584 293 A---GALPhLQAFV---SEYGARFYGLP 314
Cdd:cd01318  281 LvnkGILS-LSRVVrltSHNPARIFGIK 307
pyrC PRK09357
dihydroorotase; Validated
 184-314 5.41e-04

dihydroorotase; Validated


Pssm-ID: 236479 [Multi-domain]  Cd Length: 423  Bit Score: 41.72  E-value: 5.41e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507080584 184 HITTQDAVRYI-QEQEDGLTA-ATITPQHLLFNRNVLFNGGirPHYYCLPVLKREYHRQSLLKAATSGDRRFFAgTDSAP 261
Cdd:PRK09357 231 HVSTAGSVELIrWAKALGIKVtAEVTPHHLLLTDEDLLTYD--PNYKVNPPLRTEEDREALIEGLKDGTIDAIA-TDHAP 307

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 507080584 262 HPRTAKLAACGCA--GIFNAPSALECYATAFEAAGA--LPHLQAFVSEYGARFYGLP 314
Cdd:PRK09357 308 HAREEKECEFEAApfGITGLETALSLLYTTLVKTGLldLEQLLEKMTINPARILGLP 364
PRK04250 PRK04250
dihydroorotase; Provisional
 184-276 7.93e-04

dihydroorotase; Provisional


Pssm-ID: 235265 [Multi-domain]  Cd Length: 398  Bit Score: 40.91  E-value: 7.93e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507080584 184 HITTQDAVRYIQEQEDGLTAATITPQHLLFNR-----NVLFNggirphyyCLPVLKREYHRQSLLKAATSGDrrfFAGTD 258
Cdd:PRK04250 204 HISTKDGLKLILKSNLPWVSFEVTPHHLFLTRkdyerNPLLK--------VYPPLRSEEDRKALWENFSKIP---IIASD 272

                         90
                 ....*....|....*...
gi 507080584 259 SAPHPRTAKLAacGCAGI 276
Cdd:PRK04250 273 HAPHTLEDKEA--GAAGI 288
LigW COG2159
5-carboxyvanillate decarboxylase LigW (lignin degradation), amidohydro domain [Carbohydrate ...
 21-184 1.04e-03

5-carboxyvanillate decarboxylase LigW (lignin degradation), amidohydro domain [Carbohydrate transport and metabolism];


Pssm-ID: 441762 [Multi-domain]  Cd Length: 253  Bit Score: 40.35  E-value: 1.04e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507080584  21 DFHLHLRDGEILKAVLpfttKQF--ARAVVMPNLNPPVTTVAAMEAYREIILAAVPQGHD-FTPLMTLYLCD--DTLPEV 95
Cdd:COG2159    5 DVHTHLGTPEERLADM----DEAgiDKAVLSPTPLADPELAALARAANDWLAELVARYPDrFIGFATVDPQDpdAAVEEL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507080584  96 IRVGHQKGiLTAVKWYPAgatthaeYGVTSVS--RIRGCLDILQALGIPLLIHGESTRPDVDIFDRERV--FIEDTVMEl 171
Cdd:COG2159   81 ERAVEELG-FRGVKLHPA-------VGGFPLDdpRLDPLYEAAAELGLPVLVHPGTPPGPPPGLDLYYAapLILSGVAE- 151

                        170
                 ....*....|...
gi 507080584 172 rcNYPQLKIVLEH 184
Cdd:COG2159  152 --RFPDLKFILAH 162
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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