|
Name |
Accession |
Description |
Interval |
E-value |
| PRK05500 |
PRK05500 |
bifunctional orotidine-5'-phosphate decarboxylase/orotate phosphoribosyltransferase; |
1-503 |
0e+00 |
|
bifunctional orotidine-5'-phosphate decarboxylase/orotate phosphoribosyltransferase;
Pssm-ID: 180119 [Multi-domain] Cd Length: 477 Bit Score: 708.76 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 427347770 1 MGFFVQLTDAIAARQSLLVTGLDPNPEMLQAwahrrGMGGRSFLSQARHWIKAVVEATADHVCAYKPSLGFYQALGPVGL 80
Cdd:PRK05500 1 MNFFDKLTQAIAQNQSLLVVGLDPNPEMMPG-----RYSSQSLIQQLWTWLKFIIEETADLVCAYKPTLGFYQALGSPGL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 427347770 81 ELLREVRELVPLDIPLIIDTKHGDLNSSSALAHYLFRELGADGVTLSPLAGQDIAAPFLLYPDKAVVITCHSSNAAARVL 160
Cdd:PRK05500 76 ELLLEVLAAIPPDIPIILDAKHGDLNTSTIFAKTIFEQWQVDAVTLSPYAGQDHVAPFLVYPDKGVFILCHTSNPGAIAL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 427347770 161 QHHPDESDPLYLRIVRECQLWATPDQLLLEVGTSDPAILARVRQEAPERFLILRSLWGEEDRLDALLEAGLSPAADGLLM 240
Cdd:PRK05500 156 QEYPTPENPFYLQVVKEAKTWGTPEQLGLEVGTTNPEVLAKIRQIAPERLILLRSIWAEKGNLNQILTAGLNSNGDGLLI 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 427347770 241 PLPQNLLVEDDIAVRAAALKQRISERRDRWLERRApdqgeACSLWLPER-RPEgsaeagagtdadgsGDPLASLIVDLFD 319
Cdd:PRK05500 236 PVPQDLLGAANLKEQVKSLREEINQIRQQIVQESS-----SCDLWTPDVcLLN--------------QHPHQDLILQLYD 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 427347770 320 IGCLLFGDYVQASGAVFNYYVDLRQIISDPNLFHRVLHAYAGQLGELVFDRIAGIPYGSLPTATGLSLQLHKPLLYPRKE 399
Cdd:PRK05500 297 IGCLLFGEYVQASGATFSYYIDLRKIISNPQLFHQVLSAYAEILKNLTFDRIAGIPYGSLPTATGLALHLHHPMIFPRKE 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 427347770 400 VKAHGARRLIEGDFEEGDRVVVVDDILITGTSVLEGIAKLESSGLEVEDVVVFIDHGGqadtSARQRLAKGGYRCHAVLD 479
Cdd:PRK05500 377 VKAHGTRRLIEGNFHPGETVVVVDDILITGKSVMEGAEKLKSAGLNVRDIVVFIDHEQ----GVKDKLQSHGYQAYSVLT 452
|
490 500
....*....|....*....|....
gi 427347770 480 IARITAVLHAAGRLSDDQAATLGH 503
Cdd:PRK05500 453 ISEITETLYQAGRINEEQYQALTE 476
|
|
| PyrE |
COG0461 |
Orotate phosphoribosyltransferase [Nucleotide transport and metabolism]; Orotate ... |
313-501 |
1.02e-56 |
|
Orotate phosphoribosyltransferase [Nucleotide transport and metabolism]; Orotate phosphoribosyltransferase is part of the Pathway/BioSystem: Pyrimidine biosynthesis
Pssm-ID: 440229 Cd Length: 201 Bit Score: 187.67 E-value: 1.02e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 427347770 313 LIVDLFDIGCLLFGDYVQASGAVFNYYVDLRQIISDPNLFHRVLHAYAGQLGELV--FDRIAGIPYGSLPTATGLSLQLH 390
Cdd:COG0461 7 LAELLLEIGALLFGHFTLSSGRHSPYYIDCRLVLSYPEALELLGEALAELIKELGpeFDAVAGPATGGIPLAAAVARALG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 427347770 391 KPLLYPRKEVKAHGARRLIEGDFEEGDRVVVVDDILITGTSVLEGIAKLESSGLEVEDVVVFIDHGGQadtsARQRLAKG 470
Cdd:COG0461 87 LPAIFVRKEAKDHGTGGQIEGGLLPGERVLVVEDVITTGGSVLEAVEALREAGAEVVGVAVIVDREEG----AAENLEEA 162
|
170 180 190
....*....|....*....|....*....|.
gi 427347770 471 GYRCHAVLDIARITAVLHAAGRLSDDQAATL 501
Cdd:COG0461 163 GVPLHSLLTLDDLLELLKEKGYIDPEELEAL 193
|
|
| pyrE |
TIGR00336 |
orotate phosphoribosyltransferase; Orotate phosphoribosyltransferase (OPRTase) is involved in ... |
317-469 |
1.75e-29 |
|
orotate phosphoribosyltransferase; Orotate phosphoribosyltransferase (OPRTase) is involved in the biosynthesis of pyrimidine nucleotides. Alpha-D-ribosyldiphosphate 5-phosphate (PRPP) and orotate are utilized to form pyrophosphate and orotidine 5'-monophosphate (OMP) in the presence of divalent cations, preferably Mg2+. In a number of eukaryotes, this protein is fused to a domain that catalyses the reaction (EC 4.1.1.23). The combined activity of EC 2.4.2.10 and EC 4.1.1.23 is termed uridine 5'-monophosphate synthase. The conserved Lys (K) residue at position 101 of the seed alignment has been proposed as the active site for the enzyme. [Purines, pyrimidines, nucleosides, and nucleotides, Pyrimidine ribonucleotide biosynthesis]
Pssm-ID: 129436 [Multi-domain] Cd Length: 173 Bit Score: 114.06 E-value: 1.75e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 427347770 317 LFDIGCLLFGDYVQASGAVFNYYVDLRQIISDPNLFHRVLHAYAGQLGELV-FDRIAGIPYGSLPTATGLSLQLHKP--- 392
Cdd:TIGR00336 3 LLEVQALKFGEFTLSSGRKSPYYFNIKLFNTGPELANLIARYAAAIIKSHLeFDVIAGPALGGIPIATAVSVKLAKPggd 82
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 427347770 393 --LLYPRKEVKAHGARRLIEGDFEEGDRVVVVDDILITGTSVLEGIAKLESSGLEVEDVVVFIDHGgqaDTSARQRLAK 469
Cdd:TIGR00336 83 ipLCFNRKEAKDHGEGGNIEGELLEGDKVVVVEDVITTGTSILEAVEIIQAAGGQVAGVIIAVDRQ---ERSAGQEFEK 158
|
|
| OMP_decarboxylase_like |
cd04725 |
Orotidine 5'-phosphate decarboxylase (ODCase) is a dimeric enzyme that decarboxylates ... |
50-212 |
3.79e-25 |
|
Orotidine 5'-phosphate decarboxylase (ODCase) is a dimeric enzyme that decarboxylates orotidine 5'-monophosphate (OMP) to form uridine 5'-phosphate (UMP), an essential step in the pyrimidine biosynthetic pathway. In mammals, UMP synthase contains two domains: the orotate phosphoribosyltransferase (OPRTase) domain that catalyzes the transfer of phosphoribosyl 5'-pyrophosphate (PRPP) to orotate to form OMP, and the orotidine-5'-phosphate decarboxylase (ODCase) domain that decarboxylates OMP to form UMP.
Pssm-ID: 240076 Cd Length: 216 Bit Score: 103.02 E-value: 3.79e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 427347770 50 WIKAVVEATADHVCAYKPSLGFYQALGPvglellREVRELVPLDIPLIIDTKHGDLNSSSALAHYLFRELGADGVTLSPL 129
Cdd:cd04725 12 FALALIDALGPYVCAVKVGLELFEAAGP------EIVKELRELGFLVFLDLKLGDIPNTVAAAAEALLGLGADAVTVHPY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 427347770 130 AGQDIAAPFLLYP---DKAVVITCHSSNAAARVLQH-HPDESDPLYLRIVRECQLWatpDQLLLEVGTSDPAILarVRQE 205
Cdd:cd04725 86 GGSDMLKAALEAAeekGKGLFAVTVLSSPGALDLQEgIPGSLEDLVERLAKLAREA---GVDGVVCGATEPEAL--RRAL 160
|
....*..
gi 427347770 206 APERFLI 212
Cdd:cd04725 161 GPDFLIL 167
|
|
| OMPdecase |
smart00934 |
Orotidine 5'-phosphate decarboxylase / HUMPS family; Orotidine 5'-phosphate decarboxylase ... |
51-213 |
3.73e-10 |
|
Orotidine 5'-phosphate decarboxylase / HUMPS family; Orotidine 5'-phosphate decarboxylase (OMPdecase) catalyzes the last step in the de novo biosynthesis of pyrimidines, the decarboxylation of OMP into UMP. In higher eukaryotes OMPdecase is part, with orotate phosphoribosyltransferase, of a bifunctional enzyme, while the prokaryotic and fungal OMPdecases are monofunctional protein.
Pssm-ID: 214921 Cd Length: 212 Bit Score: 59.87 E-value: 3.73e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 427347770 51 IKAVVEATADHVCAYKPSLGFYQALGPVGLELLREVRelvplDIPLIIDTKHGDLNSSSALAHYLFRELGADGVTLSPLA 130
Cdd:smart00934 14 ALELADALGDSVDIIKVGTELFLAEGPEGVKELKELF-----GFPVFLDLKLHDIPNTVARAARAAAELGADAVTVHAYA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 427347770 131 GQDIAAPFLLYPDK------AVVITchsSNAAARVLQHHPDESdpLYLRIVRECQLWATPDQLLLEVGTSDPAILarvRQ 204
Cdd:smart00934 89 GSDMIEAALEAAKKygpgllAVTVL---TSPGAEDLQELGDES--LEEQVLRLAKLAKEAGLDGVVCSATEPELI---RR 160
|
....*....
gi 427347770 205 EAPERFLIL 213
Cdd:smart00934 161 ALGPDFLIL 169
|
|
| Pribosyltran |
pfam00156 |
Phosphoribosyl transferase domain; This family includes a range of diverse phosphoribosyl ... |
369-456 |
1.84e-06 |
|
Phosphoribosyl transferase domain; This family includes a range of diverse phosphoribosyl transferase enzymes. This family includes: Adenine phosphoribosyl-transferase EC:2.4.2.7. Hypoxanthine-guanine-xanthine phosphoribosyl-transferase. Hypoxanthine phosphoribosyl-transferase EC:2.4.2.8. Ribose-phosphate pyrophosphokinase i EC:2.7.6.1. Amidophosphoribosyltransferase EC:2.4.2.14. Orotate phosphoribosyl-transferase EC:2.4.2.10. Uracil phosphoribosyl-transferase EC:2.4.2.9. Xanthine-guanine phosphoribosyl-transferase EC:2.4.2.22. In Arabidopsis, At the very N-terminus of this domain is the P-Loop NTPase domain.
Pssm-ID: 425489 [Multi-domain] Cd Length: 150 Bit Score: 47.74 E-value: 1.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 427347770 369 DRIAGIPYGSLPTATGLSLQLHKPLLYPRKEVKAHG-----ARRLIEGDFEeGDRVVVVDDILITGTSVLEGIAKLESSG 443
Cdd:pfam00156 31 DVVVGILRGGLPFAGILARRLDVPLAFVRKVSYNPDtsevmKTSSALPDLK-GKTVLIVDDILDTGGTLLKVLELLKNVG 109
|
90
....*....|...
gi 427347770 444 LEVEDVVVFIDHG 456
Cdd:pfam00156 110 PKEVKIAVLIDKP 122
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK05500 |
PRK05500 |
bifunctional orotidine-5'-phosphate decarboxylase/orotate phosphoribosyltransferase; |
1-503 |
0e+00 |
|
bifunctional orotidine-5'-phosphate decarboxylase/orotate phosphoribosyltransferase;
Pssm-ID: 180119 [Multi-domain] Cd Length: 477 Bit Score: 708.76 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 427347770 1 MGFFVQLTDAIAARQSLLVTGLDPNPEMLQAwahrrGMGGRSFLSQARHWIKAVVEATADHVCAYKPSLGFYQALGPVGL 80
Cdd:PRK05500 1 MNFFDKLTQAIAQNQSLLVVGLDPNPEMMPG-----RYSSQSLIQQLWTWLKFIIEETADLVCAYKPTLGFYQALGSPGL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 427347770 81 ELLREVRELVPLDIPLIIDTKHGDLNSSSALAHYLFRELGADGVTLSPLAGQDIAAPFLLYPDKAVVITCHSSNAAARVL 160
Cdd:PRK05500 76 ELLLEVLAAIPPDIPIILDAKHGDLNTSTIFAKTIFEQWQVDAVTLSPYAGQDHVAPFLVYPDKGVFILCHTSNPGAIAL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 427347770 161 QHHPDESDPLYLRIVRECQLWATPDQLLLEVGTSDPAILARVRQEAPERFLILRSLWGEEDRLDALLEAGLSPAADGLLM 240
Cdd:PRK05500 156 QEYPTPENPFYLQVVKEAKTWGTPEQLGLEVGTTNPEVLAKIRQIAPERLILLRSIWAEKGNLNQILTAGLNSNGDGLLI 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 427347770 241 PLPQNLLVEDDIAVRAAALKQRISERRDRWLERRApdqgeACSLWLPER-RPEgsaeagagtdadgsGDPLASLIVDLFD 319
Cdd:PRK05500 236 PVPQDLLGAANLKEQVKSLREEINQIRQQIVQESS-----SCDLWTPDVcLLN--------------QHPHQDLILQLYD 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 427347770 320 IGCLLFGDYVQASGAVFNYYVDLRQIISDPNLFHRVLHAYAGQLGELVFDRIAGIPYGSLPTATGLSLQLHKPLLYPRKE 399
Cdd:PRK05500 297 IGCLLFGEYVQASGATFSYYIDLRKIISNPQLFHQVLSAYAEILKNLTFDRIAGIPYGSLPTATGLALHLHHPMIFPRKE 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 427347770 400 VKAHGARRLIEGDFEEGDRVVVVDDILITGTSVLEGIAKLESSGLEVEDVVVFIDHGGqadtSARQRLAKGGYRCHAVLD 479
Cdd:PRK05500 377 VKAHGTRRLIEGNFHPGETVVVVDDILITGKSVMEGAEKLKSAGLNVRDIVVFIDHEQ----GVKDKLQSHGYQAYSVLT 452
|
490 500
....*....|....*....|....
gi 427347770 480 IARITAVLHAAGRLSDDQAATLGH 503
Cdd:PRK05500 453 ISEITETLYQAGRINEEQYQALTE 476
|
|
| PyrE |
COG0461 |
Orotate phosphoribosyltransferase [Nucleotide transport and metabolism]; Orotate ... |
313-501 |
1.02e-56 |
|
Orotate phosphoribosyltransferase [Nucleotide transport and metabolism]; Orotate phosphoribosyltransferase is part of the Pathway/BioSystem: Pyrimidine biosynthesis
Pssm-ID: 440229 Cd Length: 201 Bit Score: 187.67 E-value: 1.02e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 427347770 313 LIVDLFDIGCLLFGDYVQASGAVFNYYVDLRQIISDPNLFHRVLHAYAGQLGELV--FDRIAGIPYGSLPTATGLSLQLH 390
Cdd:COG0461 7 LAELLLEIGALLFGHFTLSSGRHSPYYIDCRLVLSYPEALELLGEALAELIKELGpeFDAVAGPATGGIPLAAAVARALG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 427347770 391 KPLLYPRKEVKAHGARRLIEGDFEEGDRVVVVDDILITGTSVLEGIAKLESSGLEVEDVVVFIDHGGQadtsARQRLAKG 470
Cdd:COG0461 87 LPAIFVRKEAKDHGTGGQIEGGLLPGERVLVVEDVITTGGSVLEAVEALREAGAEVVGVAVIVDREEG----AAENLEEA 162
|
170 180 190
....*....|....*....|....*....|.
gi 427347770 471 GYRCHAVLDIARITAVLHAAGRLSDDQAATL 501
Cdd:COG0461 163 GVPLHSLLTLDDLLELLKEKGYIDPEELEAL 193
|
|
| pyrE |
PRK00455 |
orotate phosphoribosyltransferase; Validated |
313-487 |
1.50e-36 |
|
orotate phosphoribosyltransferase; Validated
Pssm-ID: 234771 Cd Length: 202 Bit Score: 134.13 E-value: 1.50e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 427347770 313 LIVDLFDIGCLLFGDYVQASGAVFNYYVDLRQIISDPNLFHRVLHAYAGQLGELV--FDRIAGIPYGSLPTATGLSLQLH 390
Cdd:PRK00455 8 FIEFLLEIGALLFGHFTLSSGRKSPYYFDCRKLLSYPEALALLGRFLAEAIKDSGieFDVVAGPATGGIPLAAAVARALD 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 427347770 391 KPLLYPRKEVKAHGARRLIEGDFEEGDRVVVVDDILITGTSVLEGIAKLESSGLEVEDVVVFIDHGgqadTSARQRLAKG 470
Cdd:PRK00455 88 LPAIFVRKEAKDHGEGGQIEGRRLFGKRVLVVEDVITTGGSVLEAVEAIRAAGAEVVGVAVIVDRQ----SAAQEVFADA 163
|
170
....*....|....*..
gi 427347770 471 GYRCHAVLDIARITAVL 487
Cdd:PRK00455 164 GVPLISLITLDDLLEYA 180
|
|
| PRK13809 |
PRK13809 |
orotate phosphoribosyltransferase; Provisional |
312-499 |
3.34e-30 |
|
orotate phosphoribosyltransferase; Provisional
Pssm-ID: 184340 Cd Length: 206 Bit Score: 116.86 E-value: 3.34e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 427347770 312 SLIVDLFDIGCLLFGDYVQASGAVFNYYVDLRQIISDPNLFHRVLHAYAGQLGELVFDRIAGIPYGSLPTATGLSLQLHK 391
Cdd:PRK13809 12 QAVAILYQIGAIKFGKFILASGEETPIYVDMRLVISSPEVLQTIATLIWRLRPSFNSSLLCGVPYTALTLATSISLKYNI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 427347770 392 PLLYPRKEVKAHGARRLI--EGDFEEGDRVVVVDDILITGTSVLEGIAKLESSGLEVEDVVVFIDHggqaDTSARQRLAK 469
Cdd:PRK13809 92 PMVLRRKELKNVDPSDAIkvEGLFTPGQTCLVINDMVSSGKSIIETAVALEEEGLVVREALVFLDR----QKGACQPLGP 167
|
170 180 190
....*....|....*....|....*....|
gi 427347770 470 GGYRCHAVLDIARITAVLHAAGRLSDDQAA 499
Cdd:PRK13809 168 QGIKLSSVFTVPDLIKSLISYGKLSSGDLT 197
|
|
| pyrE |
TIGR00336 |
orotate phosphoribosyltransferase; Orotate phosphoribosyltransferase (OPRTase) is involved in ... |
317-469 |
1.75e-29 |
|
orotate phosphoribosyltransferase; Orotate phosphoribosyltransferase (OPRTase) is involved in the biosynthesis of pyrimidine nucleotides. Alpha-D-ribosyldiphosphate 5-phosphate (PRPP) and orotate are utilized to form pyrophosphate and orotidine 5'-monophosphate (OMP) in the presence of divalent cations, preferably Mg2+. In a number of eukaryotes, this protein is fused to a domain that catalyses the reaction (EC 4.1.1.23). The combined activity of EC 2.4.2.10 and EC 4.1.1.23 is termed uridine 5'-monophosphate synthase. The conserved Lys (K) residue at position 101 of the seed alignment has been proposed as the active site for the enzyme. [Purines, pyrimidines, nucleosides, and nucleotides, Pyrimidine ribonucleotide biosynthesis]
Pssm-ID: 129436 [Multi-domain] Cd Length: 173 Bit Score: 114.06 E-value: 1.75e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 427347770 317 LFDIGCLLFGDYVQASGAVFNYYVDLRQIISDPNLFHRVLHAYAGQLGELV-FDRIAGIPYGSLPTATGLSLQLHKP--- 392
Cdd:TIGR00336 3 LLEVQALKFGEFTLSSGRKSPYYFNIKLFNTGPELANLIARYAAAIIKSHLeFDVIAGPALGGIPIATAVSVKLAKPggd 82
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 427347770 393 --LLYPRKEVKAHGARRLIEGDFEEGDRVVVVDDILITGTSVLEGIAKLESSGLEVEDVVVFIDHGgqaDTSARQRLAK 469
Cdd:TIGR00336 83 ipLCFNRKEAKDHGEGGNIEGELLEGDKVVVVEDVITTGTSILEAVEIIQAAGGQVAGVIIAVDRQ---ERSAGQEFEK 158
|
|
| pyrF |
PRK00125 |
orotidine 5'-phosphate decarboxylase; Reviewed |
2-211 |
3.87e-26 |
|
orotidine 5'-phosphate decarboxylase; Reviewed
Pssm-ID: 234651 Cd Length: 278 Bit Score: 107.64 E-value: 3.87e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 427347770 2 GFFVQLTDAIAARQSLLVtGLDPNPEMLQAWAHRRGMGG-RSFlsqarhwIKAVVEATADHVCAYKPSLGFYQALGPVGL 80
Cdd:PRK00125 1 TFIDRLREAVARRGSLCV-GLDPHPSLLPAWGLSGDADGlFEF-------CRIIVDATADLVAAFKPQIAYFEAHGAEGL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 427347770 81 ELLRE-VRELVPLDIPLIIDTKHGDLNSSS---ALAHYLFReLGADGVTLSPLAGQDIAAPFLLYP---DKAVVITCHSS 153
Cdd:PRK00125 73 AQLERtIAYLREAGVLVIADAKRGDIGSTAeayAKAAFESP-LEADAVTVSPYMGFDSLEPYLEYAeehGKGVFVLCRTS 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 427347770 154 NAAARVLQHHPDESD-PLYLRIVRE-CQLWA----TPDQLLLEVGTSDPAILARVRQEAPERFL 211
Cdd:PRK00125 152 NPGGSDLQFLRTADGrPLYQHVADLaAALNNlgncGYGSIGLVVGATFPPELAAVRKILGGMPL 215
|
|
| OMP_decarboxylase_like |
cd04725 |
Orotidine 5'-phosphate decarboxylase (ODCase) is a dimeric enzyme that decarboxylates ... |
50-212 |
3.79e-25 |
|
Orotidine 5'-phosphate decarboxylase (ODCase) is a dimeric enzyme that decarboxylates orotidine 5'-monophosphate (OMP) to form uridine 5'-phosphate (UMP), an essential step in the pyrimidine biosynthetic pathway. In mammals, UMP synthase contains two domains: the orotate phosphoribosyltransferase (OPRTase) domain that catalyzes the transfer of phosphoribosyl 5'-pyrophosphate (PRPP) to orotate to form OMP, and the orotidine-5'-phosphate decarboxylase (ODCase) domain that decarboxylates OMP to form UMP.
Pssm-ID: 240076 Cd Length: 216 Bit Score: 103.02 E-value: 3.79e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 427347770 50 WIKAVVEATADHVCAYKPSLGFYQALGPvglellREVRELVPLDIPLIIDTKHGDLNSSSALAHYLFRELGADGVTLSPL 129
Cdd:cd04725 12 FALALIDALGPYVCAVKVGLELFEAAGP------EIVKELRELGFLVFLDLKLGDIPNTVAAAAEALLGLGADAVTVHPY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 427347770 130 AGQDIAAPFLLYP---DKAVVITCHSSNAAARVLQH-HPDESDPLYLRIVRECQLWatpDQLLLEVGTSDPAILarVRQE 205
Cdd:cd04725 86 GGSDMLKAALEAAeekGKGLFAVTVLSSPGALDLQEgIPGSLEDLVERLAKLAREA---GVDGVVCGATEPEAL--RRAL 160
|
....*..
gi 427347770 206 APERFLI 212
Cdd:cd04725 161 GPDFLIL 167
|
|
| PyrF |
COG0284 |
Orotidine-5'-phosphate decarboxylase [Nucleotide transport and metabolism]; Orotidine-5 ... |
52-213 |
2.20e-21 |
|
Orotidine-5'-phosphate decarboxylase [Nucleotide transport and metabolism]; Orotidine-5'-phosphate decarboxylase is part of the Pathway/BioSystem: Pyrimidine biosynthesis
Pssm-ID: 440053 Cd Length: 228 Bit Score: 92.86 E-value: 2.20e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 427347770 52 KAVVEATADHVCAYKPSLGFYQALGPVGLELLREvrelvpLDIPLIIDTKHGDLNSSSALAHYLFRELGADGVTLSPLAG 131
Cdd:COG0284 18 LAIVDALADLVCAYKPGLALFEAYGPEGVEALKE------RGLPVFLDLKRHDIPNTVAAAARAAAELGVDAVTVHAYGG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 427347770 132 QDIAAPFLLYPD---KAVVITCHSSNAAARVLQHHPDEsDPLYlRIVRECQLWATPDQLL-LEVGtsdPAILARVRQEAP 207
Cdd:COG0284 92 RDMLEPALEAADesgKGVFAVTVLTSPGAADLQELGIE-GPLY-EVVLRLAKLAKEAGLDgVVCS---ATEAAALRAALG 166
|
....*.
gi 427347770 208 ERFLIL 213
Cdd:COG0284 167 PDFLLL 172
|
|
| PRTases_typeI |
cd06223 |
Phosphoribosyl transferase (PRT)-type I domain; Phosphoribosyl transferase (PRT) domain. The ... |
366-454 |
7.17e-15 |
|
Phosphoribosyl transferase (PRT)-type I domain; Phosphoribosyl transferase (PRT) domain. The type I PRTases are identified by a conserved PRPP binding motif which features two adjacent acidic residues surrounded by one or more hydrophobic residue. PRTases catalyze the displacement of the alpha-1'-pyrophosphate of 5-phosphoribosyl-alpha1-pyrophosphate (PRPP) by a nitrogen-containing nucleophile. The reaction products are an alpha-1 substituted ribose-5'-phosphate and a free pyrophosphate (PP). PRPP, an activated form of ribose-5-phosphate, is a key metabolite connecting nucleotide synthesis and salvage pathways. The type I PRTase family includes a range of diverse phosphoribosyl transferase enzymes and regulatory proteins of the nucleotide synthesis and salvage pathways, including adenine phosphoribosyltransferase EC:2.4.2.7., hypoxanthine-guanine-xanthine phosphoribosyltransferase, hypoxanthine phosphoribosyltransferase EC:2.4.2.8., ribose-phosphate pyrophosphokinase EC:2.7.6.1., amidophosphoribosyltransferase EC:2.4.2.14., orotate phosphoribosyltransferase EC:2.4.2.10., uracil phosphoribosyltransferase EC:2.4.2.9., and xanthine-guanine phosphoribosyltransferase EC:2.4.2.22.
Pssm-ID: 206754 [Multi-domain] Cd Length: 130 Bit Score: 71.27 E-value: 7.17e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 427347770 366 LVFDRIAGIPYGSLPTATGLSLQLHKPLLYPRKEVKAHGARRLIEGDFE-------EGDRVVVVDDILITGTSVLEGIAK 438
Cdd:cd06223 14 LEPDVVVGILRGGLPLAAALARALGLPLAFIRKERKGPGRTPSEPYGLElplggdvKGKRVLLVDDVIATGGTLLAAIEL 93
|
90
....*....|....*.
gi 427347770 439 LESSGLEVEDVVVFID 454
Cdd:cd06223 94 LKEAGAKVVGVAVLLD 109
|
|
| Apt |
COG0503 |
Adenine/guanine phosphoribosyltransferase or related PRPP-binding protein [Nucleotide ... |
345-480 |
1.38e-11 |
|
Adenine/guanine phosphoribosyltransferase or related PRPP-binding protein [Nucleotide transport and metabolism]; Adenine/guanine phosphoribosyltransferase or related PRPP-binding protein is part of the Pathway/BioSystem: Purine salvage
Pssm-ID: 440269 Cd Length: 171 Bit Score: 62.79 E-value: 1.38e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 427347770 345 IISDPNLFHRVLHAYAGQLGELVFDRIAGIPYGSLPTATGLSLQLHKPLLYPRKEVKA------------HGARRLIE-- 410
Cdd:COG0503 26 LLGDPELFRAAGDELAERFADKGIDKVVGIEARGFILAAALAYALGVPFVPARKPGKLpgetvseeydleYGTGDTLElh 105
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 427347770 411 -GDFEEGDRVVVVDDILITGTSvLEGIAKL-ESSGLEVEDVVVFIDhggQADTSARQRLAkgGYRCHAVLDI 480
Cdd:COG0503 106 kDALKPGDRVLIVDDLLATGGT-AKAAIKLvEEAGAEVVGIAFLIE---LGFLGGREKLR--DYPVESLLTL 171
|
|
| OMPdecase |
smart00934 |
Orotidine 5'-phosphate decarboxylase / HUMPS family; Orotidine 5'-phosphate decarboxylase ... |
51-213 |
3.73e-10 |
|
Orotidine 5'-phosphate decarboxylase / HUMPS family; Orotidine 5'-phosphate decarboxylase (OMPdecase) catalyzes the last step in the de novo biosynthesis of pyrimidines, the decarboxylation of OMP into UMP. In higher eukaryotes OMPdecase is part, with orotate phosphoribosyltransferase, of a bifunctional enzyme, while the prokaryotic and fungal OMPdecases are monofunctional protein.
Pssm-ID: 214921 Cd Length: 212 Bit Score: 59.87 E-value: 3.73e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 427347770 51 IKAVVEATADHVCAYKPSLGFYQALGPVGLELLREVRelvplDIPLIIDTKHGDLNSSSALAHYLFRELGADGVTLSPLA 130
Cdd:smart00934 14 ALELADALGDSVDIIKVGTELFLAEGPEGVKELKELF-----GFPVFLDLKLHDIPNTVARAARAAAELGADAVTVHAYA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 427347770 131 GQDIAAPFLLYPDK------AVVITchsSNAAARVLQHHPDESdpLYLRIVRECQLWATPDQLLLEVGTSDPAILarvRQ 204
Cdd:smart00934 89 GSDMIEAALEAAKKygpgllAVTVL---TSPGAEDLQELGDES--LEEQVLRLAKLAKEAGLDGVVCSATEPELI---RR 160
|
....*....
gi 427347770 205 EAPERFLIL 213
Cdd:smart00934 161 ALGPDFLIL 169
|
|
| PRK02304 |
PRK02304 |
adenine phosphoribosyltransferase; Provisional |
345-480 |
6.12e-09 |
|
adenine phosphoribosyltransferase; Provisional
Pssm-ID: 235028 Cd Length: 175 Bit Score: 55.47 E-value: 6.12e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 427347770 345 IISDPNLFHRVLHAYAGQLGELVFDRIAGIPYGSLPTATGLSLQLHKPLL-------YPRKEVKAH-----GARRL-I-E 410
Cdd:PRK02304 29 LLADPEAFREVIDALVERYKDADIDKIVGIEARGFIFGAALAYKLGIGFVpvrkpgkLPRETISESyeleyGTDTLeIhK 108
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 427347770 411 GDFEEGDRVVVVDDILIT-GTsvLEGIAKL-ESSGLEVEDVVVFIDHGGQadtSARQRLakGGYRCHAVLDI 480
Cdd:PRK02304 109 DAIKPGDRVLIVDDLLATgGT--LEAAIKLlERLGAEVVGAAFVIELPDL---GGREKL--EGYPVKSLVKF 173
|
|
| PRK02277 |
PRK02277 |
orotate phosphoribosyltransferase-like protein; Provisional |
339-454 |
1.55e-06 |
|
orotate phosphoribosyltransferase-like protein; Provisional
Pssm-ID: 235023 [Multi-domain] Cd Length: 200 Bit Score: 48.71 E-value: 1.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 427347770 339 YVDLRQIISDPNLFHRVLHAYA--GQLGELVFDRIAGIPYGSLPTATGLSLQLHKPL--LYPRKEVKAHGARrlIEGDFE 414
Cdd:PRK02277 55 HIDWSSIGSSSSRLRYIASAMAdmLEKEDEEVDVVVGIAKSGVPLATLVADELGKDLaiYHPKKWDHGEGEK--KTGSFS 132
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 427347770 415 ------EGDRVVVVDDILITGTSVLEGIAKLESSGLEVEDVVVFID 454
Cdd:PRK02277 133 rnfasvEGKRCVIVDDVITSGTTMKETIEYLKEHGGKPVAVVVLID 178
|
|
| Pribosyltran |
pfam00156 |
Phosphoribosyl transferase domain; This family includes a range of diverse phosphoribosyl ... |
369-456 |
1.84e-06 |
|
Phosphoribosyl transferase domain; This family includes a range of diverse phosphoribosyl transferase enzymes. This family includes: Adenine phosphoribosyl-transferase EC:2.4.2.7. Hypoxanthine-guanine-xanthine phosphoribosyl-transferase. Hypoxanthine phosphoribosyl-transferase EC:2.4.2.8. Ribose-phosphate pyrophosphokinase i EC:2.7.6.1. Amidophosphoribosyltransferase EC:2.4.2.14. Orotate phosphoribosyl-transferase EC:2.4.2.10. Uracil phosphoribosyl-transferase EC:2.4.2.9. Xanthine-guanine phosphoribosyl-transferase EC:2.4.2.22. In Arabidopsis, At the very N-terminus of this domain is the P-Loop NTPase domain.
Pssm-ID: 425489 [Multi-domain] Cd Length: 150 Bit Score: 47.74 E-value: 1.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 427347770 369 DRIAGIPYGSLPTATGLSLQLHKPLLYPRKEVKAHG-----ARRLIEGDFEeGDRVVVVDDILITGTSVLEGIAKLESSG 443
Cdd:pfam00156 31 DVVVGILRGGLPFAGILARRLDVPLAFVRKVSYNPDtsevmKTSSALPDLK-GKTVLIVDDILDTGGTLLKVLELLKNVG 109
|
90
....*....|...
gi 427347770 444 LEVEDVVVFIDHG 456
Cdd:pfam00156 110 PKEVKIAVLIDKP 122
|
|
| PRK12560 |
PRK12560 |
adenine phosphoribosyltransferase; Provisional |
368-454 |
6.05e-05 |
|
adenine phosphoribosyltransferase; Provisional
Pssm-ID: 183595 Cd Length: 187 Bit Score: 44.00 E-value: 6.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 427347770 368 FDRIAGIPYGSLPTATGLSLQLHKPLLYPRK----------EVKAHGARRLiEGDF-----EEGDRVVVVDDILITGTSV 432
Cdd:PRK12560 52 IDKIVTEEDKGAPLATPVSLLSGKPLAMARWypyslselnyNVVEIGSEYF-EGVVylngiEKGDRVAIIDDTLSTGGTV 130
|
90 100
....*....|....*....|..
gi 427347770 433 LEGIAKLESSGLEVEDVVVFID 454
Cdd:PRK12560 131 IALIKAIENSGGIVSDVICVIE 152
|
|
| OMPdecase |
pfam00215 |
Orotidine 5'-phosphate decarboxylase / HUMPS family; This family includes Orotidine 5 ... |
53-139 |
6.47e-04 |
|
Orotidine 5'-phosphate decarboxylase / HUMPS family; This family includes Orotidine 5'-phosphate decarboxylase enzymes EC:4.1.1.23 that are involved in the final step of pyrimidine biosynthesis. The family also includes enzymes such as hexulose-6-phosphate synthase. This family appears to be distantly related to pfam00834.
Pssm-ID: 395160 Cd Length: 215 Bit Score: 41.10 E-value: 6.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 427347770 53 AVVEATADHVCAYKPSLGFYQALGPvglELLREVRELvplDIPLIIDTKHGDLNSSSALAHYLFRELGADGVTLSPLAGQ 132
Cdd:pfam00215 17 ELADELGPYVDILKVGTPLFEAFGL---KLVAELRKH---GFLIFLDLKFADIGNTVAKQAKYKAKLGADIVTVHAYAGE 90
|
....*..
gi 427347770 133 DIAAPFL 139
Cdd:pfam00215 91 GTLKAAK 97
|
|
| TMP_TenI |
cd00564 |
Thiamine monophosphate synthase (TMP synthase)/TenI. TMP synthase catalyzes an important step ... |
81-165 |
2.37e-03 |
|
Thiamine monophosphate synthase (TMP synthase)/TenI. TMP synthase catalyzes an important step in the thiamine biosynthesis pathway, the substitution of the pyrophosphate of 2-methyl-4-amino-5- hydroxymethylpyrimidine pyrophosphate by 4-methyl-5- (beta-hydroxyethyl) thiazole phosphate to yield thiamine phosphate. TenI is a enzymatically inactive regulatory protein involved in the regulation of several extracellular enzymes. This superfamily also contains other enzymatically inactive proteins with unknown functions.
Pssm-ID: 238317 [Multi-domain] Cd Length: 196 Bit Score: 39.42 E-value: 2.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 427347770 81 ELLREVRELVPL----DIPLIIdtkhgdlNSSSALAhylfRELGADGVTLSPLAGQDIAAPFLLYPDKAVVITCHSSNAA 156
Cdd:cd00564 40 ELLELARALRELcrkyGVPLII-------NDRVDLA----LAVGADGVHLGQDDLPVAEARALLGPDLIIGVSTHSLEEA 108
|
....*....
gi 427347770 157 ARVLQHHPD 165
Cdd:cd00564 109 LRAEELGAD 117
|
|
| PRK09219 |
PRK09219 |
xanthine phosphoribosyltransferase; Validated |
409-483 |
8.42e-03 |
|
xanthine phosphoribosyltransferase; Validated
Pssm-ID: 181705 Cd Length: 189 Bit Score: 37.46 E-value: 8.42e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 427347770 409 IEGDF-EEGDRVVVVDDILITGTSVLeGIAKL-ESSGLEVEDVVVFIDHGGQadtSARQRLAKGGYRchaVLDIARI 483
Cdd:PRK09219 109 VSKKFlSEGDRVLIIDDFLANGQAAL-GLIDIiEQAGAKVAGIGIVIEKSFQ---DGRKLLEEKGYR---VESLARI 178
|
|
| |
