|
Name |
Accession |
Description |
Interval |
E-value |
| PyrC |
COG0418 |
Dihydroorotase [Nucleotide transport and metabolism]; Dihydroorotase is part of the Pathway ... |
1-344 |
0e+00 |
|
Dihydroorotase [Nucleotide transport and metabolism]; Dihydroorotase is part of the Pathway/BioSystem: Pyrimidine biosynthesis
Pssm-ID: 440187 Cd Length: 344 Bit Score: 721.11 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183286109 1 MSDRLTLLRPDDWHIHLRDGAVLPHTVGDVARTFARAIIMPNLVPPVRNAAEAGAYRERILAARPAGSRFEPLMVLYLTD 80
Cdd:COG0418 1 MMQTLTIRRPDDWHLHLRDGAMLAAVVPDTARQFGRAIVMPNLVPPVTTVAQALAYRERILAALPAGSDFEPLMTLYLTD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183286109 81 RTSPEDVRAAKASGIVYAAKLYPAGATTNSDSGVTSIDNIFPAIEALAEVGMPLLVHGEVTRSEIDVFDREKRFIDEHMR 160
Cdd:COG0418 81 NTTPEEIARAKASGVVTAVKLYPAGATTNSDSGVTDIDKIYPVLEAMQEIGMPLLVHGEVTDPDIDIFDREAVFIDRVLE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183286109 161 RLVERFPALNVVFEHITTSDAAQFVTEAPANVGATITSQHLLYNRNHMLVGGIRPHFYCLPILKRNTHQVALLDAATSGN 240
Cdd:COG0418 161 PLRRRFPELKVVFEHITTKEAVDFVRAAGDNVAATITPHHLLYNRNAMLVGGIRPHYYCLPILKRETHRQALRAAATSGN 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183286109 241 PKFFLGTDSAPHARHAKEAACGCAGCYTAYAAIELYAEAFEQRNALDKLEGFASLHGPAFYGLPANTDTITLVREEWTAP 320
Cdd:COG0418 241 PKFFLGTDSAPHARHAKESACGCAGCYTAPAALELYAEVFEEAGALDKLEAFASLNGPDFYGLPRNTGTITLVREPWTVP 320
|
330 340
....*....|....*....|....
gi 2183286109 321 QSLPFGEQTVVPLRAGEKLRWRLL 344
Cdd:COG0418 321 ESIPFGDDTLVPFRAGETLNWRVV 344
|
|
| PLN02599 |
PLN02599 |
dihydroorotase |
4-345 |
0e+00 |
|
dihydroorotase
Pssm-ID: 178209 [Multi-domain] Cd Length: 364 Bit Score: 557.83 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183286109 4 RLTLLRPDDWHIHLRDGAVLPHTVGDVARTFARAIIMPNLVPPVRNAAEAGAYRERILAARPAGSRFEPLMVLYLTDRTS 83
Cdd:PLN02599 22 ELTITRPDDWHLHLRDGAKLAAVVPHSARHFGRAIVMPNLKPPVTTTARALAYRERIMKALPPGSSFEPLMTLYLTDNTT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183286109 84 PEDVRAAKASGIVYAAKLYPAGATTNSDSGVTSIDNIFPAIEALAEVGMPLLVHGEVTRSEIDVFDREKRFIDEHMRRLV 163
Cdd:PLN02599 102 PEEIKAAKASGVVFAVKLYPAGATTNSQAGVTDLGKCLPVLEEMAEQGMPLLVHGEVTDPSVDIFDREKVFIDTILAPLV 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183286109 164 ERFPALNVVFEHITTSDAAQFVTEAPA-NVGATITSQHLLYNRNHMLVGGIRPHFYCLPILKRNTHQVALLDAATSGNPK 242
Cdd:PLN02599 182 QKLPQLKIVMEHITTMDAVEFVESCGDgNVAATVTPQHLLLNRNALFQGGLQPHNYCLPVLKREIHREALVKAATSGSKK 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183286109 243 FFLGTDSAPHARHAKEAACGCAGCYTAYAAIELYAEAFEQRNALDKLEGFASLHGPAFYGLPANTDTITLVREEWTAPQS 322
Cdd:PLN02599 262 FFLGTDSAPHPKRAKEASCGCAGIYSAPVALSLYAKAFEEAGALDKLEAFTSFNGPDFYGLPRNTSTITLVKSAWKVPEA 341
|
330 340
....*....|....*....|...
gi 2183286109 323 LPFGEQTVVPLRAGEKLRWRLLE 345
Cdd:PLN02599 342 YSFGGGTVVPMFAGETIPWSVVS 364
|
|
| DHOase |
cd01294 |
Dihydroorotase (DHOase) catalyzes the reversible interconversion of carbamoyl aspartate to ... |
5-341 |
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: 527.62 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183286109 5 LTLLRPDDWHIHLRDGAVLPHTVGDVARTFARAIIMPNLVPPVRNAAEAGAYRERILAARPaGSRFEPLMVLYLTDRTSP 84
Cdd:cd01294 1 LTIPRPDDMHLHLRDGAMLKLVLPYTARGFSRAIVMPNLKPPVTTTADALAYRERILAADP-GPNFTPLMTLYLTENTTP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183286109 85 EDVRAAKASGIVYAAKLYPAGATTNSDSGVTSIDNIFPAIEALAEVGMPLLVHGEVTRSEIDVFDREKRFIdEHMRRLVE 164
Cdd:cd01294 80 EELREAKKKGGIRGVKLYPAGATTNSQGGVTDLEKIYPVLEAMQKLGMPLLVHGEVPDFKIDVLDREAKFI-PVLEPLAQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183286109 165 RFPALNVVFEHITTSDAAQFVTEAPANVGATITSQHLLYNRNHMLVGGIRPHFYCLPILKRNTHQVALLDAATSGNPKFF 244
Cdd:cd01294 159 RFPKLKIVLEHITTADAVEYVKSCNENVAATITPHHLLLTRDDLLGGGLNPHLYCKPVAKRPEDREALRKAATSGHPKFF 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183286109 245 LGTDSAPHARHAKEAACGCAGCYTAYAAIELYAEAFEQRNALDKLEGFASLHGPAFYGLPANTDTITLVREEWTAPQSLP 324
Cdd:cd01294 239 LGSDSAPHPKSNKESSCGCAGIFSAPIALPYLAEVFEEHNALDKLEAFASDNGPNFYGLPPNKKTITLVKEPWKVPEKIP 318
|
330
....*....|....*..
gi 2183286109 325 FGEQTVVPLRAGEKLRW 341
Cdd:cd01294 319 FGNNGVVPFRAGETLRW 335
|
|
| pyrC_dimer |
TIGR00856 |
dihydroorotase, homodimeric type; This homodimeric form of dihydroorotase is less common in ... |
5-343 |
9.25e-170 |
|
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: 475.84 E-value: 9.25e-170
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183286109 5 LTLLRPDDWHIHLRDGAVLPHTVGDVARTFARAIIMPNLVPPVRNAAEAGAYRERILAARPAGSRFEPLMVLYLTDRTSP 84
Cdd:TIGR00856 2 LTIRRPDDWHLHLRDGAMLKAVLPYTSEIFSRAIVMPNLAPPVTTVEAAVAYRERILDAVPAGHDFTPLMTLYLTDSLTP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183286109 85 EDVRAAKASGIVYAAKLYPAGATTNSDSGVTSIDNIFPAIEALAEVGMPLLVHGEVTRSEIDVFDREKRFIDEHMRRLVE 164
Cdd:TIGR00856 82 EELERAKNEGVVRAVKLYPAGATTNSSHGVTDIDAIMPVLEAMEKIGLPLLLHGEVTHGDIDIFDREARFIESVLEPLRQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183286109 165 RFPALNVVFEHITTSDAAQFVTEAPANVGATITSQHLLYNRNHMLVGGIRPHFYCLPILKRNTHQVALLDAATSGNPKFF 244
Cdd:TIGR00856 162 RFPALKVVLEHITTKDAIDYVEDGNNRLAATITPQHLMFTRNDLLGGGVNPHLYCLPILKRNIHQQALLELAASGFPKFF 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183286109 245 LGTDSAPHARHAKEAACGCAGCYTAYAAIELYAEAFEQRNALDKLEGFASLHGPAFYGLPANTDTITLVREEWTAPQSLP 324
Cdd:TIGR00856 242 LGTDSAPHARHRKESSCGCAGCFSAPTALPSYAEVFEEMNALENLEAFCSDNGPQFYGLPVNSTKIELVKKEQQIPESIA 321
|
330
....*....|....*....
gi 2183286109 325 FGEQTVVPLRAGEKLRWRL 343
Cdd:TIGR00856 322 LTDDTLVPFRAGETLSWSV 340
|
|
| Amidohydro_1 |
pfam01979 |
Amidohydrolase family; This family of enzymes are a a large metal dependent hydrolase ... |
12-311 |
7.58e-09 |
|
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: 56.36 E-value: 7.58e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183286109 12 DWHIHLRDGAVL-PHTVGDVARTFARAIIMPNLVPPVRNAAEAGA----YRERILAA---RPAGSRFEPLMVLYLTDRT- 82
Cdd:pfam01979 8 DAHVHLEMGLLRgIPVPPEFAYEALRLGITTMLKSGTTTVLDMGAttstGIEALLEAaeeLPLGLRFLGPGCSLDTDGEl 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183286109 83 -----------SPEDVRAAKASGIVYAAkLYPAGATTNSDsgvtsiDNIFPAIEALAEVGMPLLVHgeVTRSEIDVFDRE 151
Cdd:pfam01979 88 egrkalreklkAGAEFIKGMADGVVFVG-LAPHGAPTFSD------DELKAALEEAKKYGLPVAIH--ALETKGEVEDAI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183286109 152 KRFIDEHMRRLVERFPA-------LNVVFEHITTSDAAqfvteapanvGATITSQHLlynRNHMLVggirphFYCLPILK 224
Cdd:pfam01979 159 AAFGGGIEHGTHLEVAEsgglldiIKLILAHGVHLSPT----------EANLLAEHL---KGAGVA------HCPFSNSK 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183286109 225 RNTHQVALLDAATSGNpKFFLGTDSAPHARHAKEAACGcagcytayaaIELYAEAFEQRNALDKLEGF--ASLHGPAFYG 302
Cdd:pfam01979 220 LRSGRIALRKALEDGV-KVGLGTDGAGSGNSLNMLEEL----------RLALELQFDPEGGLSPLEALrmATINPAKALG 288
|
....*....
gi 2183286109 303 LPANTDTIT 311
Cdd:pfam01979 289 LDDKVGSIE 297
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PyrC |
COG0418 |
Dihydroorotase [Nucleotide transport and metabolism]; Dihydroorotase is part of the Pathway ... |
1-344 |
0e+00 |
|
Dihydroorotase [Nucleotide transport and metabolism]; Dihydroorotase is part of the Pathway/BioSystem: Pyrimidine biosynthesis
Pssm-ID: 440187 Cd Length: 344 Bit Score: 721.11 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183286109 1 MSDRLTLLRPDDWHIHLRDGAVLPHTVGDVARTFARAIIMPNLVPPVRNAAEAGAYRERILAARPAGSRFEPLMVLYLTD 80
Cdd:COG0418 1 MMQTLTIRRPDDWHLHLRDGAMLAAVVPDTARQFGRAIVMPNLVPPVTTVAQALAYRERILAALPAGSDFEPLMTLYLTD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183286109 81 RTSPEDVRAAKASGIVYAAKLYPAGATTNSDSGVTSIDNIFPAIEALAEVGMPLLVHGEVTRSEIDVFDREKRFIDEHMR 160
Cdd:COG0418 81 NTTPEEIARAKASGVVTAVKLYPAGATTNSDSGVTDIDKIYPVLEAMQEIGMPLLVHGEVTDPDIDIFDREAVFIDRVLE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183286109 161 RLVERFPALNVVFEHITTSDAAQFVTEAPANVGATITSQHLLYNRNHMLVGGIRPHFYCLPILKRNTHQVALLDAATSGN 240
Cdd:COG0418 161 PLRRRFPELKVVFEHITTKEAVDFVRAAGDNVAATITPHHLLYNRNAMLVGGIRPHYYCLPILKRETHRQALRAAATSGN 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183286109 241 PKFFLGTDSAPHARHAKEAACGCAGCYTAYAAIELYAEAFEQRNALDKLEGFASLHGPAFYGLPANTDTITLVREEWTAP 320
Cdd:COG0418 241 PKFFLGTDSAPHARHAKESACGCAGCYTAPAALELYAEVFEEAGALDKLEAFASLNGPDFYGLPRNTGTITLVREPWTVP 320
|
330 340
....*....|....*....|....
gi 2183286109 321 QSLPFGEQTVVPLRAGEKLRWRLL 344
Cdd:COG0418 321 ESIPFGDDTLVPFRAGETLNWRVV 344
|
|
| PLN02599 |
PLN02599 |
dihydroorotase |
4-345 |
0e+00 |
|
dihydroorotase
Pssm-ID: 178209 [Multi-domain] Cd Length: 364 Bit Score: 557.83 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183286109 4 RLTLLRPDDWHIHLRDGAVLPHTVGDVARTFARAIIMPNLVPPVRNAAEAGAYRERILAARPAGSRFEPLMVLYLTDRTS 83
Cdd:PLN02599 22 ELTITRPDDWHLHLRDGAKLAAVVPHSARHFGRAIVMPNLKPPVTTTARALAYRERIMKALPPGSSFEPLMTLYLTDNTT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183286109 84 PEDVRAAKASGIVYAAKLYPAGATTNSDSGVTSIDNIFPAIEALAEVGMPLLVHGEVTRSEIDVFDREKRFIDEHMRRLV 163
Cdd:PLN02599 102 PEEIKAAKASGVVFAVKLYPAGATTNSQAGVTDLGKCLPVLEEMAEQGMPLLVHGEVTDPSVDIFDREKVFIDTILAPLV 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183286109 164 ERFPALNVVFEHITTSDAAQFVTEAPA-NVGATITSQHLLYNRNHMLVGGIRPHFYCLPILKRNTHQVALLDAATSGNPK 242
Cdd:PLN02599 182 QKLPQLKIVMEHITTMDAVEFVESCGDgNVAATVTPQHLLLNRNALFQGGLQPHNYCLPVLKREIHREALVKAATSGSKK 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183286109 243 FFLGTDSAPHARHAKEAACGCAGCYTAYAAIELYAEAFEQRNALDKLEGFASLHGPAFYGLPANTDTITLVREEWTAPQS 322
Cdd:PLN02599 262 FFLGTDSAPHPKRAKEASCGCAGIYSAPVALSLYAKAFEEAGALDKLEAFTSFNGPDFYGLPRNTSTITLVKSAWKVPEA 341
|
330 340
....*....|....*....|...
gi 2183286109 323 LPFGEQTVVPLRAGEKLRWRLLE 345
Cdd:PLN02599 342 YSFGGGTVVPMFAGETIPWSVVS 364
|
|
| DHOase |
cd01294 |
Dihydroorotase (DHOase) catalyzes the reversible interconversion of carbamoyl aspartate to ... |
5-341 |
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: 527.62 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183286109 5 LTLLRPDDWHIHLRDGAVLPHTVGDVARTFARAIIMPNLVPPVRNAAEAGAYRERILAARPaGSRFEPLMVLYLTDRTSP 84
Cdd:cd01294 1 LTIPRPDDMHLHLRDGAMLKLVLPYTARGFSRAIVMPNLKPPVTTTADALAYRERILAADP-GPNFTPLMTLYLTENTTP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183286109 85 EDVRAAKASGIVYAAKLYPAGATTNSDSGVTSIDNIFPAIEALAEVGMPLLVHGEVTRSEIDVFDREKRFIdEHMRRLVE 164
Cdd:cd01294 80 EELREAKKKGGIRGVKLYPAGATTNSQGGVTDLEKIYPVLEAMQKLGMPLLVHGEVPDFKIDVLDREAKFI-PVLEPLAQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183286109 165 RFPALNVVFEHITTSDAAQFVTEAPANVGATITSQHLLYNRNHMLVGGIRPHFYCLPILKRNTHQVALLDAATSGNPKFF 244
Cdd:cd01294 159 RFPKLKIVLEHITTADAVEYVKSCNENVAATITPHHLLLTRDDLLGGGLNPHLYCKPVAKRPEDREALRKAATSGHPKFF 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183286109 245 LGTDSAPHARHAKEAACGCAGCYTAYAAIELYAEAFEQRNALDKLEGFASLHGPAFYGLPANTDTITLVREEWTAPQSLP 324
Cdd:cd01294 239 LGSDSAPHPKSNKESSCGCAGIFSAPIALPYLAEVFEEHNALDKLEAFASDNGPNFYGLPPNKKTITLVKEPWKVPEKIP 318
|
330
....*....|....*..
gi 2183286109 325 FGEQTVVPLRAGEKLRW 341
Cdd:cd01294 319 FGNNGVVPFRAGETLRW 335
|
|
| pyrC_dimer |
TIGR00856 |
dihydroorotase, homodimeric type; This homodimeric form of dihydroorotase is less common in ... |
5-343 |
9.25e-170 |
|
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: 475.84 E-value: 9.25e-170
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183286109 5 LTLLRPDDWHIHLRDGAVLPHTVGDVARTFARAIIMPNLVPPVRNAAEAGAYRERILAARPAGSRFEPLMVLYLTDRTSP 84
Cdd:TIGR00856 2 LTIRRPDDWHLHLRDGAMLKAVLPYTSEIFSRAIVMPNLAPPVTTVEAAVAYRERILDAVPAGHDFTPLMTLYLTDSLTP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183286109 85 EDVRAAKASGIVYAAKLYPAGATTNSDSGVTSIDNIFPAIEALAEVGMPLLVHGEVTRSEIDVFDREKRFIDEHMRRLVE 164
Cdd:TIGR00856 82 EELERAKNEGVVRAVKLYPAGATTNSSHGVTDIDAIMPVLEAMEKIGLPLLLHGEVTHGDIDIFDREARFIESVLEPLRQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183286109 165 RFPALNVVFEHITTSDAAQFVTEAPANVGATITSQHLLYNRNHMLVGGIRPHFYCLPILKRNTHQVALLDAATSGNPKFF 244
Cdd:TIGR00856 162 RFPALKVVLEHITTKDAIDYVEDGNNRLAATITPQHLMFTRNDLLGGGVNPHLYCLPILKRNIHQQALLELAASGFPKFF 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183286109 245 LGTDSAPHARHAKEAACGCAGCYTAYAAIELYAEAFEQRNALDKLEGFASLHGPAFYGLPANTDTITLVREEWTAPQSLP 324
Cdd:TIGR00856 242 LGTDSAPHARHRKESSCGCAGCFSAPTALPSYAEVFEEMNALENLEAFCSDNGPQFYGLPVNSTKIELVKKEQQIPESIA 321
|
330
....*....|....*....
gi 2183286109 325 FGEQTVVPLRAGEKLRWRL 343
Cdd:TIGR00856 322 LTDDTLVPFRAGETLSWSV 340
|
|
| Amidohydro_1 |
pfam01979 |
Amidohydrolase family; This family of enzymes are a a large metal dependent hydrolase ... |
12-311 |
7.58e-09 |
|
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: 56.36 E-value: 7.58e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183286109 12 DWHIHLRDGAVL-PHTVGDVARTFARAIIMPNLVPPVRNAAEAGA----YRERILAA---RPAGSRFEPLMVLYLTDRT- 82
Cdd:pfam01979 8 DAHVHLEMGLLRgIPVPPEFAYEALRLGITTMLKSGTTTVLDMGAttstGIEALLEAaeeLPLGLRFLGPGCSLDTDGEl 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183286109 83 -----------SPEDVRAAKASGIVYAAkLYPAGATTNSDsgvtsiDNIFPAIEALAEVGMPLLVHgeVTRSEIDVFDRE 151
Cdd:pfam01979 88 egrkalreklkAGAEFIKGMADGVVFVG-LAPHGAPTFSD------DELKAALEEAKKYGLPVAIH--ALETKGEVEDAI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183286109 152 KRFIDEHMRRLVERFPA-------LNVVFEHITTSDAAqfvteapanvGATITSQHLlynRNHMLVggirphFYCLPILK 224
Cdd:pfam01979 159 AAFGGGIEHGTHLEVAEsgglldiIKLILAHGVHLSPT----------EANLLAEHL---KGAGVA------HCPFSNSK 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183286109 225 RNTHQVALLDAATSGNpKFFLGTDSAPHARHAKEAACGcagcytayaaIELYAEAFEQRNALDKLEGF--ASLHGPAFYG 302
Cdd:pfam01979 220 LRSGRIALRKALEDGV-KVGLGTDGAGSGNSLNMLEEL----------RLALELQFDPEGGLSPLEALrmATINPAKALG 288
|
....*....
gi 2183286109 303 LPANTDTIT 311
Cdd:pfam01979 289 LDDKVGSIE 297
|
|
| DHOase_IIb |
cd01318 |
Dihydroorotase (DHOase), subgroup IIb; DHOases catalyze the reversible interconversion of ... |
12-259 |
3.47e-08 |
|
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: 54.65 E-value: 3.47e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183286109 12 DWHIHLRDGAvLPHTvGDVARTFARAII--------MPNLVPPVRNAAeagAYRERILAARpAGSRFEPLMVLYLTDRTS 83
Cdd:cd01318 10 DIHVHFREPG-LTYK-EDFVSGSRAAAAggvttvmdMPNTKPPTTTAE---ALYEKLRLAA-AKSVVDYGLYFGVTGSED 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183286109 84 PEDVRAAKASGIvyaaKLYPAGATtnsdsGVTSIDNifPAIE-ALAEVGMPLLVHGEVTrseiDVFD-REKRFIDEHMRR 161
Cdd:cd01318 84 LEELDKAPPAGY----KIFMGDST-----GDLLDDE--ETLErIFAEGSVLVTFHAEDE----DRLReNRKELKGESAHP 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183286109 162 lVERFPALNVV-----------------FEHITTSDAAQFVTEAPANVGATITSQHLLYNRNHmlVGGIRPHFYCLPILK 224
Cdd:cd01318 149 -RIRDAEAAAVataralklarrhgarlhICHVSTPEELKLIKKAKPGVTVEVTPHHLFLDVED--YDRLGTLGKVNPPLR 225
|
250 260 270
....*....|....*....|....*....|....*
gi 2183286109 225 RNTHQVALLDAATSGNPKfFLGTDSAPHARHAKEA 259
Cdd:cd01318 226 SREDRKALLQALADGRID-VIASDHAPHTLEEKRK 259
|
|
| LigW |
COG2159 |
5-carboxyvanillate decarboxylase LigW (lignin degradation), amidohydro domain [Carbohydrate ... |
35-175 |
6.30e-07 |
|
5-carboxyvanillate decarboxylase LigW (lignin degradation), amidohydro domain [Carbohydrate transport and metabolism];
Pssm-ID: 441762 [Multi-domain] Cd Length: 253 Bit Score: 49.98 E-value: 6.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183286109 35 ARAIIMPNLVPPVRNAAEAGAYRERILA-ARPAGSRFEPLMVLYLTDrtsPEDV-----RAAKASGIVyAAKLYPagatt 108
Cdd:COG2159 26 DKAVLSPTPLADPELAALARAANDWLAElVARYPDRFIGFATVDPQD---PDAAveeleRAVEELGFR-GVKLHP----- 96
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2183286109 109 nsDSGVTSIDN--IFPAIEALAEVGMPLLVHGEVTRSEIDVFDREkRFIDEHMRRLVERFPALNVVFEH 175
Cdd:COG2159 97 --AVGGFPLDDprLDPLYEAAAELGLPVLVHPGTPPGPPPGLDLY-YAAPLILSGVAERFPDLKFILAH 162
|
|
| AllB |
COG0044 |
Dihydroorotase or related cyclic amidohydrolase [Nucleotide transport and metabolism]; ... |
38-304 |
8.26e-07 |
|
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: 50.48 E-value: 8.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183286109 38 IIMPNLVPPVRNAAEAGAYRERilAARPAGSRFEPLMVLYLTDRTSPEDVRAAKASGIVyAAKLYpagATTNSDSGVTSI 117
Cdd:COG0044 86 VDMPNTNPVTDTPEALEFKLAR--AEEKALVDVGPHGALTKGLGENLAELGALAEAGAV-AFKVF---MGSDDGNPVLDD 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183286109 118 DNIFPAIEALAEVGMPLLVHGEvtrseiDVFDREKRFIDE-------HMR---------------RLVERFPA-LNVVfe 174
Cdd:COG0044 160 GLLRRALEYAAEFGALVAVHAE------DPDLIRGGVMNEgktsprlGLKgrpaeaeeeavardiALAEETGArLHIV-- 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183286109 175 HITTSDAAQFVTEAPA---NVGATITSQHLLYNrnHMLVGGIRPHFYCLPILKRNTHQVALLDAATSGNPKFfLGTDSAP 251
Cdd:COG0044 232 HVSTAEAVELIREAKArglPVTAEVCPHHLTLT--DEDLERYGTNFKVNPPLRTEEDREALWEGLADGTIDV-IATDHAP 308
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2183286109 252 HARHAK-----EAACGCAGCYTAYAAieLYAEAFEQRNaLDkLEGFASL--HGPA-FYGLP 304
Cdd:COG0044 309 HTLEEKelpfaEAPNGIPGLETALPL--LLTELVHKGR-LS-LERLVELlsTNPArIFGLP 365
|
|
| pyrC_multi |
TIGR00857 |
dihydroorotase, multifunctional complex type; In contrast to the homodimeric type of ... |
12-272 |
8.68e-06 |
|
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: 47.05 E-value: 8.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183286109 12 DWHIHLRDGA------VLPHTVGDVARTFARAIIMPNLVPPVRNAAEagaYRERILaarpagsRFEplmvlyltdRTSPE 85
Cdd:TIGR00857 43 DLHVHLRDPGeeykedIESGSKAAAHGGFTTVADMPNTKPPIDTPET---LEWKLQ-------RLK---------KVSLV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183286109 86 DV-------RAAKASGIVYAAKLYPAGAT----TNSDSGVTSIDNIFPAIEALAEVGMPLLVHGEvtrsEIDVFDREKRF 154
Cdd:TIGR00857 104 DVhlyggvtQGNQGKELTEAYELKEAGAVgrmfTDDGSEVQDILSMRRALEYAAIAGVPIALHAE----DPDLIYGGVMH 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183286109 155 IDEHMRRL-------------VERFPAL------NVVFEHITTSDAAQFVTEA---PANVGATITSQHLLYNRNHmlVGG 212
Cdd:TIGR00857 180 EGPSAAQLglparppeaeevaVARLLELakhagcPVHICHISTKESLELIVKAksqGIKITAEVTPHHLLLSEED--VAR 257
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2183286109 213 IRPHFYCLPILKRNTHQVALLDAATSGNPKFFlGTDSAPHARHAK-----EAACGCAGCYTAYAA 272
Cdd:TIGR00857 258 LDGNGKVNPPLREKEDRLALIEGLKDGIIDII-ATDHAPHTLEEKtkefaAAPPGIPGLETALPL 321
|
|
| metallo-dependent_hydrolases |
cd01292 |
Superfamily of metallo-dependent hydrolases (also called amidohydrolase superfamily) is a ... |
12-253 |
1.50e-05 |
|
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: 45.79 E-value: 1.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183286109 12 DWHIHLRDGAVLP------------HTVGDVARTFARAI------------IMPNLVPPVRNAAEAGAYRERILAARP-- 65
Cdd:cd01292 3 DTHVHLDGSALRGtrlnlelkeaeeLSPEDLYEDTLRALeallaggvttvvDMGSTPPPTTTKAAIEAVAEAARASAGir 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183286109 66 ----AGSRFEPLMVLYLTDRTSPEDVRAAKASGIVyAAKLYPAGATTNSDSgvtsiDNIFPAIEALAEVGMPLLVHGEVT 141
Cdd:cd01292 83 vvlgLGIPGVPAAVDEDAEALLLELLRRGLELGAV-GLKLAGPYTATGLSD-----ESLRRVLEEARKLGLPVVIHAGEL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183286109 142 RSEidvfdrekrfiDEHMRRLVER-FPALNVVFEHITTSDAAQFVTEAPANVGATITSQHLLYnrnhmlvggirphfycl 220
Cdd:cd01292 157 PDP-----------TRALEDLVALlRLGGRVVIGHVSHLDPELLELLKEAGVSLEVCPLSNYL----------------- 208
|
250 260 270
....*....|....*....|....*....|...
gi 2183286109 221 piLKRNTHQVALLDAATSGNPKFFLGTDSAPHA 253
Cdd:cd01292 209 --LGRDGEGAEALRRLLELGIRVTLGTDGPPHP 239
|
|
| DHOase_IIa |
cd01317 |
Dihydroorotase (DHOase), subgroup IIa; DHOases catalyze the reversible interconversion of ... |
99-273 |
2.60e-04 |
|
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: 42.61 E-value: 2.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183286109 99 AKLYPAGATTNSDSGVTSIDN--IFPAIEALAEVGMPLLVH--------------GEVTR----------SEIDVFDRek 152
Cdd:cd01317 99 GELLEAGAVGFSDDGKPIQDAelLRRALEYAAMLDLPIIVHpedpslagggvmneGKVASrlglpgippeAETIMVAR-- 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183286109 153 rfidehMRRLVERFPAlNVVFEHITTSDAAQFVTEAPA---NVGATITSQHLLYNRNhmLVGGIRPHFYCLPILKRNTHQ 229
Cdd:cd01317 177 ------DLELAEATGA-RVHFQHLSTARSLELIRKAKAkglPVTAEVTPHHLLLDDE--ALESYDTNAKVNPPLRSEEDR 247
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2183286109 230 VALLDAATSGnPKFFLGTDSAPHARHAK-----EAACGCAGCYTAYAAI 273
Cdd:cd01317 248 EALIEALKDG-TIDAIASDHAPHTDEEKdlpfaEAPPGIIGLETALPLL 295
|
|
| pyrC |
PRK09357 |
dihydroorotase; Validated |
175-318 |
2.73e-03 |
|
dihydroorotase; Validated
Pssm-ID: 236479 [Multi-domain] Cd Length: 423 Bit Score: 39.41 E-value: 2.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183286109 175 HITTSDAAQFVTEAPA---NVGATITSQHLLYNRNHMLvgGIRPHFYCLPILKRNTHQVALLDAATSGNPKFfLGTDSAP 251
Cdd:PRK09357 231 HVSTAGSVELIRWAKAlgiKVTAEVTPHHLLLTDEDLL--TYDPNYKVNPPLRTEEDREALIEGLKDGTIDA-IATDHAP 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183286109 252 HARHAKE-----AACGCAGCYTAYAaieLYAEAFEQRNALDkLEGFASL--HGPA-FYGLPANT------DTITLV--RE 315
Cdd:PRK09357 308 HAREEKEcefeaAPFGITGLETALS---LLYTTLVKTGLLD-LEQLLEKmtINPArILGLPAGPlaegepADLVIFdpEA 383
|
...
gi 2183286109 316 EWT 318
Cdd:PRK09357 384 EWT 386
|
|
| PRK04250 |
PRK04250 |
dihydroorotase; Provisional |
173-271 |
4.19e-03 |
|
dihydroorotase; Provisional
Pssm-ID: 235265 [Multi-domain] Cd Length: 398 Bit Score: 38.60 E-value: 4.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2183286109 173 FEHITTSDAAQFVTEA-PANVGATITSQHLLYNRNHMLVGgirPHFYCLPILKRNTHQVALLDAATSGNpkfFLGTDSAP 251
Cdd:PRK04250 202 ICHISTKDGLKLILKSnLPWVSFEVTPHHLFLTRKDYERN---PLLKVYPPLRSEEDRKALWENFSKIP---IIASDHAP 275
|
90 100
....*....|....*....|.
gi 2183286109 252 HARHAKEA-ACGCAGCYTAYA 271
Cdd:PRK04250 276 HTLEDKEAgAAGIPGLETEVP 296
|
|
| |
