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Conserved domains on  [gi|22331787|ref|NP_680130|]
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uridine 5'-monophosphate synthase / UMP synthase (PYRE-F) (UMPS) [Arabidopsis thaliana]

Protein Classification

uridine 5'-monophosphate synthase( domain architecture ID 10898500)

uridine 5'-monophosphate synthase catalyzes the last two steps of the UMP biosynthesis, the addition of ribose-P to orotate by orotate phosphoribosyltransferase, to form orotidine-5'-monophosphate (OMP), and the decarboxylation of OMP by orotidine-5'-phosphate decarboxylase to form uridine monophosphate (UMP); in bacteria, these two domains/functions are located in separate proteins

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
OMPdecase pfam00215
Orotidine 5'-phosphate decarboxylase / HUMPS family; This family includes Orotidine 5 ...
243-462 1.27e-67

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: 215.59  E-value: 1.27e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331787   243 TNLCLAADVGTAAELLDIADKVGPEICLLKTHVDILPDFTPDFGSKLRaiadKHKFLIFEDRKFADIGNTVTMQYEggiF 322
Cdd:pfam00215   1 PNLCVALDVPTLEEALELADELGPYVDILKVGTPLFEAFGLKLVAELR----KHGFLIFLDLKFADIGNTVAKQAK---Y 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331787   323 KILEWADIINAHVISGPGIVDGLKLKGMPRGRGLLLLAEMSSAGNLATGD-----YTAAAVKIADAHSDFVMGFISvnPA 397
Cdd:pfam00215  74 KAKLGADIVTVHAYAGEGTLKAAKEAAEEYGRGLLLVAELSSKGSLDLQEegdlgYTQEIVHRAADLAAGVDGVVA--SA 151
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 22331787   398 SWKCGYVYPSMIHATPGVQMvKGGDALGQQYNTPHSVITERGSDIIIVGRGIIKAENPAETAHEY 462
Cdd:pfam00215 152 TEALREILPDFLILTPGIGL-QGGDAGGQQRVTTPAVAKEAGADIIIVGRGITGAGDPVAAARAI 215
PRTases_typeI super family cl00309
Phosphoribosyl transferase (PRT)-type I domain; Phosphoribosyl transferase (PRT) domain. The ...
7-199 3.99e-66

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.


The actual alignment was detected with superfamily member PRK13809:

Pssm-ID: 444823  Cd Length: 206  Bit Score: 211.62  E-value: 3.99e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331787    7 LILQLHEIGAVKFGNFKLKSGIFSPVYIDLRLIVSYPSLLTQISqTLISSLPPSATFDVVCGVPYTALPIATVVSVSNGI 86
Cdd:PRK13809  13 AVAILYQIGAIKFGKFILASGEETPIYVDMRLVISSPEVLQTIA-TLIWRLRPSFNSSLLCGVPYTALTLATSISLKYNI 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331787   87 PMLMRRKEIKDYGTSKAI--EGIFEKDQTCLIIEDLVTSGASVLETAAPLRAVGLKVSDAVVLIDRQQGGRENLAENGIK 164
Cdd:PRK13809  92 PMVLRRKELKNVDPSDAIkvEGLFTPGQTCLVINDMVSSGKSIIETAVALEEEGLVVREALVFLDRQKGACQPLGPQGIK 171
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 22331787  165 LHSMIMLTDMVRVLKEKGKIEVEVEVNLLKFLEEN 199
Cdd:PRK13809 172 LSSVFTVPDLIKSLISYGKLSSGDLTLANKIIKIL 206
 
Name Accession Description Interval E-value
OMPdecase pfam00215
Orotidine 5'-phosphate decarboxylase / HUMPS family; This family includes Orotidine 5 ...
243-462 1.27e-67

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: 215.59  E-value: 1.27e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331787   243 TNLCLAADVGTAAELLDIADKVGPEICLLKTHVDILPDFTPDFGSKLRaiadKHKFLIFEDRKFADIGNTVTMQYEggiF 322
Cdd:pfam00215   1 PNLCVALDVPTLEEALELADELGPYVDILKVGTPLFEAFGLKLVAELR----KHGFLIFLDLKFADIGNTVAKQAK---Y 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331787   323 KILEWADIINAHVISGPGIVDGLKLKGMPRGRGLLLLAEMSSAGNLATGD-----YTAAAVKIADAHSDFVMGFISvnPA 397
Cdd:pfam00215  74 KAKLGADIVTVHAYAGEGTLKAAKEAAEEYGRGLLLVAELSSKGSLDLQEegdlgYTQEIVHRAADLAAGVDGVVA--SA 151
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 22331787   398 SWKCGYVYPSMIHATPGVQMvKGGDALGQQYNTPHSVITERGSDIIIVGRGIIKAENPAETAHEY 462
Cdd:pfam00215 152 TEALREILPDFLILTPGIGL-QGGDAGGQQRVTTPAVAKEAGADIIIVGRGITGAGDPVAAARAI 215
PRK13809 PRK13809
orotate phosphoribosyltransferase; Provisional
7-199 3.99e-66

orotate phosphoribosyltransferase; Provisional


Pssm-ID: 184340  Cd Length: 206  Bit Score: 211.62  E-value: 3.99e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331787    7 LILQLHEIGAVKFGNFKLKSGIFSPVYIDLRLIVSYPSLLTQISqTLISSLPPSATFDVVCGVPYTALPIATVVSVSNGI 86
Cdd:PRK13809  13 AVAILYQIGAIKFGKFILASGEETPIYVDMRLVISSPEVLQTIA-TLIWRLRPSFNSSLLCGVPYTALTLATSISLKYNI 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331787   87 PMLMRRKEIKDYGTSKAI--EGIFEKDQTCLIIEDLVTSGASVLETAAPLRAVGLKVSDAVVLIDRQQGGRENLAENGIK 164
Cdd:PRK13809  92 PMVLRRKELKNVDPSDAIkvEGLFTPGQTCLVINDMVSSGKSIIETAVALEEEGLVVREALVFLDRQKGACQPLGPQGIK 171
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 22331787  165 LHSMIMLTDMVRVLKEKGKIEVEVEVNLLKFLEEN 199
Cdd:PRK13809 172 LSSVFTVPDLIKSLISYGKLSSGDLTLANKIIKIL 206
PyrE COG0461
Orotate phosphoribosyltransferase [Nucleotide transport and metabolism]; Orotate ...
1-198 3.67e-64

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


Pssm-ID: 440229  Cd Length: 201  Bit Score: 206.16  E-value: 3.67e-64
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331787   1 MSAMEALILQLHEIGAVKFGNFKLKSGIFSPVYIDLRLIVSYPSLLTQISQTLISSLPPSA-TFDVVCGVPYTALPIATV 79
Cdd:COG0461   1 MSYKEELAELLLEIGALLFGHFTLSSGRHSPYYIDCRLVLSYPEALELLGEALAELIKELGpEFDAVAGPATGGIPLAAA 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331787  80 VSVSNGIPMLMRRKEIKDYGTSKAIEGIFEKDQTCLIIEDLVTSGASVLETAAPLRAVGLKVSDAVVLIDRQQGGRENLA 159
Cdd:COG0461  81 VARALGLPAIFVRKEAKDHGTGGQIEGGLLPGERVLVVEDVITTGGSVLEAVEALREAGAEVVGVAVIVDREEGAAENLE 160
                       170       180       190
                ....*....|....*....|....*....|....*....
gi 22331787 160 ENGIKLHSMIMLTDMVRVLKEKGKIEVEVEVNLLKFLEE 198
Cdd:COG0461 161 EAGVPLHSLLTLDDLLELLKEKGYIDPEELEALEAYREK 199
pyrF TIGR01740
orotidine 5'-phosphate decarboxylase, subfamily 1; This model represents orotidine 5 ...
245-463 7.66e-57

orotidine 5'-phosphate decarboxylase, subfamily 1; This model represents orotidine 5'-monophosphate decarboxylase, the PyrF protein of pyrimidine nucleotide biosynthesis. In many eukaryotes, the region hit by this model is part of a multifunctional protein. [Purines, pyrimidines, nucleosides, and nucleotides, Pyrimidine ribonucleotide biosynthesis]


Pssm-ID: 273785  Cd Length: 214  Bit Score: 187.56  E-value: 7.66e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331787   245 LCLAADVGTAAELLDIADKVGPEICLLKTHVDILPDFTPDFGSKLRAIADKhkflIFEDRKFADIGNTVTMQYEGgifKI 324
Cdd:TIGR01740   1 LIVALDVTTKEEALDLADSLGEEICVIKVGYDLLLSGGEKIIDELAKLNKL----IFLDLKFADIPNTVKLQYES---KI 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331787   325 LEWADIINAHVISGPGIVDGLK--LKGMPRgRGLLLLAEMSSAGNLATGDYTA-AAVKIADAHSDF-VMGFISVNPASWK 400
Cdd:TIGR01740  74 KLGADMVNVHGFAGSESVEAAKeaASEFGR-RGLLAVTELTSMGSEEYGEDTMeKVVEYAKEAKEFgLIGPVCSAEEAKE 152
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 22331787   401 CGYVYPSMIHATPGVQMvKGGDALGQQYNTPHSVITERGSDIIIVGRGIIKAENPAETAHEYR 463
Cdd:TIGR01740 153 IRKATGDFLILTPGIRL-DSKDADDQKRVVTLEEAKEAGADVIIVGRGIYAAEDPVEAAKRIR 214
OMP_decarboxylase_like cd04725
Orotidine 5'-phosphate decarboxylase (ODCase) is a dimeric enzyme that decarboxylates ...
245-462 8.03e-57

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: 187.77  E-value: 8.03e-57
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331787 245 LCLAADVGTAAELLDIADKVGPEICLLKTHVDILPDFTPDFGSKLRAIAdkhkFLIFEDRKFADIGNTVTMQYEGGIFKi 324
Cdd:cd04725   1 LIVALDPPDEEFALALIDALGPYVCAVKVGLELFEAAGPEIVKELRELG----FLVFLDLKLGDIPNTVAAAAEALLGL- 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331787 325 leWADIINAHVISGPGIVDGLKLKGMPRGRGLLLLAEMSSAGNL--------ATGDYTAAAVKIADAHSdfVMGFI-SVN 395
Cdd:cd04725  76 --GADAVTVHPYGGSDMLKAALEAAEEKGKGLFAVTVLSSPGALdlqegipgSLEDLVERLAKLAREAG--VDGVVcGAT 151
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 22331787 396 PASWKCGYVYPSMIHATPGVQMvKGGDALGQQYNTPHSVItERGSDIIIVGRGIIKAENPAETAHEY 462
Cdd:cd04725 152 EPEALRRALGPDFLILTPGIGA-QGSGDDQKRGGTPEDAI-RAGADYIVVGRPITQAADPVAAAEAI 216
OMPdecase smart00934
Orotidine 5'-phosphate decarboxylase / HUMPS family; Orotidine 5'-phosphate decarboxylase ...
244-462 2.33e-41

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: 146.93  E-value: 2.33e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331787    244 NLCLAADVGTAAELLDIADKVGPEICLLKTHVDILPDFTPDFgskLRAIADKHKFLIFEDRKFADIGNTVtmqyEGGIFK 323
Cdd:smart00934   1 RLIVALDVPDLEEALELADALGDSVDIIKVGTELFLAEGPEG---VKELKELFGFPVFLDLKLHDIPNTV----ARAARA 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331787    324 ILE-WADIINAHVISGPGIVDGLKLKGMPRGRGLLLLAEMSSAGNLATGD----YTAAAVKI--ADAHSDFVMGFIS--- 393
Cdd:smart00934  74 AAElGADAVTVHAYAGSDMIEAALEAAKKYGPGLLAVTVLTSPGAEDLQElgdeSLEEQVLRlaKLAKEAGLDGVVCsat 153
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331787    394 -VNPASWKCGyvyPSMIHATPGVQmvkggdalGQQYNTPHSVITERGSDIIIVGRGIIKAENPAETAHEY 462
Cdd:smart00934 154 ePELIRRALG---PDFLILTPGIG--------DQGRVATPAVAIGAGADIIVVGRPITQAADPVEAAEAI 212
pyrE TIGR00336
orotate phosphoribosyltransferase; Orotate phosphoribosyltransferase (OPRTase) is involved in ...
11-174 5.99e-37

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: 133.71  E-value: 5.99e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331787    11 LHEIGAVKFGNFKLKSGIFSPVYIDLRLIVSYPSLLTQISQTLISSLPPSATFDVVCGVPYTALPIATVVSV-----SNG 85
Cdd:TIGR00336   3 LLEVQALKFGEFTLSSGRKSPYYFNIKLFNTGPELANLIARYAAAIIKSHLEFDVIAGPALGGIPIATAVSVklakpGGD 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331787    86 IPMLMRRKEIKDYGTSKAIEGIFEKDQTCLIIEDLVTSGASVLETAAPLRAVGLKVSDAVVLIDRQQ--GGRENLAENGI 163
Cdd:TIGR00336  83 IPLCFNRKEAKDHGEGGNIEGELLEGDKVVVVEDVITTGTSILEAVEIIQAAGGQVAGVIIAVDRQErsAGQEFEKEYGL 162
                         170
                  ....*....|.
gi 22331787   164 KLHSMIMLTDM 174
Cdd:TIGR00336 163 PVISLITLKDL 173
PRTases_typeI cd06223
Phosphoribosyl transferase (PRT)-type I domain; Phosphoribosyl transferase (PRT) domain. The ...
63-167 3.97e-17

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: 77.44  E-value: 3.97e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331787  63 FDVVCGVPYTALPIATVVSVSNGIPMLMRRKEIKDYGTSK-------AIEGIFEKDQTCLIIEDLVTSGASVLETAAPLR 135
Cdd:cd06223  16 PDVVVGILRGGLPLAAALARALGLPLAFIRKERKGPGRTPsepygleLPLGGDVKGKRVLLVDDVIATGGTLLAAIELLK 95
                        90       100       110
                ....*....|....*....|....*....|..
gi 22331787 136 AVGLKVSDAVVLIDRQQGGRENLAENGIKLHS 167
Cdd:cd06223  96 EAGAKVVGVAVLLDKPEGGARELASPGDPVYS 127
PyrF COG0284
Orotidine-5'-phosphate decarboxylase [Nucleotide transport and metabolism]; Orotidine-5 ...
245-463 6.07e-16

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: 76.68  E-value: 6.07e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331787 245 LCLAADVGTAAELLDIADKVGPEICLLKTHVDILPDFTPDFgskLRAIADKHkFLIFEDRKFADIGNTVTMQYEGgifkI 324
Cdd:COG0284   5 LIVALDLPDAAEALAIVDALADLVCAYKPGLALFEAYGPEG---VEALKERG-LPVFLDLKRHDIPNTVAAAARA----A 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331787 325 LEW-ADIINAHVISGPGIVDGLKLKGMPRGRGLLLLAEMSSagnlaTGDYTAAAVKIADAHSDFVMGFISVNPASWKCGY 403
Cdd:COG0284  77 AELgVDAVTVHAYGGRDMLEPALEAADESGKGVFAVTVLTS-----PGAADLQELGIEGPLYEVVLRLAKLAKEAGLDGV 151
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 22331787 404 V----YPSMIHA---------TPGVQMVkgGDALGQQ--YNTPHSVItERGSDIIIVGRGIIKAENPAETAHEYR 463
Cdd:COG0284 152 VcsatEAAALRAalgpdflllTPGIRPQ--GGDAGDQkrVGTPAEAI-AAGADYLVVGRPITYAGDPRAAAEAIR 223
PRK13813 PRK13813
orotidine 5'-phosphate decarboxylase; Provisional
240-459 4.16e-11

orotidine 5'-phosphate decarboxylase; Provisional


Pssm-ID: 237520  Cd Length: 215  Bit Score: 62.31  E-value: 4.16e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331787  240 KKETNLCLAADVGTAAELLDIADKVGPEICLLKTHvdiLPDFTPDFGSKLRAIADKHKflIFEDRKFADIGNTVTM---- 315
Cdd:PRK13813   1 EKDSRIILALDVTDRERALKIAEELDDYVDAIKVG---WPLVLASGLGIIEELKRYAP--VIADLKVADIPNTNRLicea 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331787  316 QYEGGifkilewADIINAHVISGPGIVDGLKLKGMPRGRGLLLLAEMSSAGnlATGDYTAAAVKIADAHSDF-VMGFISv 394
Cdd:PRK13813  76 VFEAG-------AWGIIVHGFTGRDSLKAVVEAAAESGGKVFVVVEMSHPG--ALEFIQPHADKLAKLAQEAgAFGVVA- 145
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 22331787  395 nPASwkcgyvYPSMIHA------------TPGV--QMVKGGDALgqqyntphsvitERGSDIIIVGRGIIKAENPAETA 459
Cdd:PRK13813 146 -PAT------RPERVRYirsrlgdelkiiSPGIgaQGGKAADAI------------KAGADYVIVGRSIYNAADPREAA 205
Pribosyltran pfam00156
Phosphoribosyl transferase domain; This family includes a range of diverse phosphoribosyl ...
62-156 4.23e-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: 46.59  E-value: 4.23e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331787    62 TFDVVCGVPYTALPIATVVSVSNGIPMLMRRKEIK---DYGTSKAIEGIFE-KDQTCLIIEDLVTSGASVLETAAPLRAV 137
Cdd:pfam00156  29 KPDVVVGILRGGLPFAGILARRLDVPLAFVRKVSYnpdTSEVMKTSSALPDlKGKTVLIVDDILDTGGTLLKVLELLKNV 108
                          90
                  ....*....|....*....
gi 22331787   138 GLKVSDAVVLIDRQQGGRE 156
Cdd:pfam00156 109 GPKEVKIAVLIDKPAGTEP 127
 
Name Accession Description Interval E-value
OMPdecase pfam00215
Orotidine 5'-phosphate decarboxylase / HUMPS family; This family includes Orotidine 5 ...
243-462 1.27e-67

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: 215.59  E-value: 1.27e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331787   243 TNLCLAADVGTAAELLDIADKVGPEICLLKTHVDILPDFTPDFGSKLRaiadKHKFLIFEDRKFADIGNTVTMQYEggiF 322
Cdd:pfam00215   1 PNLCVALDVPTLEEALELADELGPYVDILKVGTPLFEAFGLKLVAELR----KHGFLIFLDLKFADIGNTVAKQAK---Y 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331787   323 KILEWADIINAHVISGPGIVDGLKLKGMPRGRGLLLLAEMSSAGNLATGD-----YTAAAVKIADAHSDFVMGFISvnPA 397
Cdd:pfam00215  74 KAKLGADIVTVHAYAGEGTLKAAKEAAEEYGRGLLLVAELSSKGSLDLQEegdlgYTQEIVHRAADLAAGVDGVVA--SA 151
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 22331787   398 SWKCGYVYPSMIHATPGVQMvKGGDALGQQYNTPHSVITERGSDIIIVGRGIIKAENPAETAHEY 462
Cdd:pfam00215 152 TEALREILPDFLILTPGIGL-QGGDAGGQQRVTTPAVAKEAGADIIIVGRGITGAGDPVAAARAI 215
PRK13809 PRK13809
orotate phosphoribosyltransferase; Provisional
7-199 3.99e-66

orotate phosphoribosyltransferase; Provisional


Pssm-ID: 184340  Cd Length: 206  Bit Score: 211.62  E-value: 3.99e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331787    7 LILQLHEIGAVKFGNFKLKSGIFSPVYIDLRLIVSYPSLLTQISqTLISSLPPSATFDVVCGVPYTALPIATVVSVSNGI 86
Cdd:PRK13809  13 AVAILYQIGAIKFGKFILASGEETPIYVDMRLVISSPEVLQTIA-TLIWRLRPSFNSSLLCGVPYTALTLATSISLKYNI 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331787   87 PMLMRRKEIKDYGTSKAI--EGIFEKDQTCLIIEDLVTSGASVLETAAPLRAVGLKVSDAVVLIDRQQGGRENLAENGIK 164
Cdd:PRK13809  92 PMVLRRKELKNVDPSDAIkvEGLFTPGQTCLVINDMVSSGKSIIETAVALEEEGLVVREALVFLDRQKGACQPLGPQGIK 171
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 22331787  165 LHSMIMLTDMVRVLKEKGKIEVEVEVNLLKFLEEN 199
Cdd:PRK13809 172 LSSVFTVPDLIKSLISYGKLSSGDLTLANKIIKIL 206
PyrE COG0461
Orotate phosphoribosyltransferase [Nucleotide transport and metabolism]; Orotate ...
1-198 3.67e-64

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


Pssm-ID: 440229  Cd Length: 201  Bit Score: 206.16  E-value: 3.67e-64
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331787   1 MSAMEALILQLHEIGAVKFGNFKLKSGIFSPVYIDLRLIVSYPSLLTQISQTLISSLPPSA-TFDVVCGVPYTALPIATV 79
Cdd:COG0461   1 MSYKEELAELLLEIGALLFGHFTLSSGRHSPYYIDCRLVLSYPEALELLGEALAELIKELGpEFDAVAGPATGGIPLAAA 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331787  80 VSVSNGIPMLMRRKEIKDYGTSKAIEGIFEKDQTCLIIEDLVTSGASVLETAAPLRAVGLKVSDAVVLIDRQQGGRENLA 159
Cdd:COG0461  81 VARALGLPAIFVRKEAKDHGTGGQIEGGLLPGERVLVVEDVITTGGSVLEAVEALREAGAEVVGVAVIVDREEGAAENLE 160
                       170       180       190
                ....*....|....*....|....*....|....*....
gi 22331787 160 ENGIKLHSMIMLTDMVRVLKEKGKIEVEVEVNLLKFLEE 198
Cdd:COG0461 161 EAGVPLHSLLTLDDLLELLKEKGYIDPEELEALEAYREK 199
pyrF TIGR01740
orotidine 5'-phosphate decarboxylase, subfamily 1; This model represents orotidine 5 ...
245-463 7.66e-57

orotidine 5'-phosphate decarboxylase, subfamily 1; This model represents orotidine 5'-monophosphate decarboxylase, the PyrF protein of pyrimidine nucleotide biosynthesis. In many eukaryotes, the region hit by this model is part of a multifunctional protein. [Purines, pyrimidines, nucleosides, and nucleotides, Pyrimidine ribonucleotide biosynthesis]


Pssm-ID: 273785  Cd Length: 214  Bit Score: 187.56  E-value: 7.66e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331787   245 LCLAADVGTAAELLDIADKVGPEICLLKTHVDILPDFTPDFGSKLRAIADKhkflIFEDRKFADIGNTVTMQYEGgifKI 324
Cdd:TIGR01740   1 LIVALDVTTKEEALDLADSLGEEICVIKVGYDLLLSGGEKIIDELAKLNKL----IFLDLKFADIPNTVKLQYES---KI 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331787   325 LEWADIINAHVISGPGIVDGLK--LKGMPRgRGLLLLAEMSSAGNLATGDYTA-AAVKIADAHSDF-VMGFISVNPASWK 400
Cdd:TIGR01740  74 KLGADMVNVHGFAGSESVEAAKeaASEFGR-RGLLAVTELTSMGSEEYGEDTMeKVVEYAKEAKEFgLIGPVCSAEEAKE 152
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 22331787   401 CGYVYPSMIHATPGVQMvKGGDALGQQYNTPHSVITERGSDIIIVGRGIIKAENPAETAHEYR 463
Cdd:TIGR01740 153 IRKATGDFLILTPGIRL-DSKDADDQKRVVTLEEAKEAGADVIIVGRGIYAAEDPVEAAKRIR 214
OMP_decarboxylase_like cd04725
Orotidine 5'-phosphate decarboxylase (ODCase) is a dimeric enzyme that decarboxylates ...
245-462 8.03e-57

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: 187.77  E-value: 8.03e-57
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331787 245 LCLAADVGTAAELLDIADKVGPEICLLKTHVDILPDFTPDFGSKLRAIAdkhkFLIFEDRKFADIGNTVTMQYEGGIFKi 324
Cdd:cd04725   1 LIVALDPPDEEFALALIDALGPYVCAVKVGLELFEAAGPEIVKELRELG----FLVFLDLKLGDIPNTVAAAAEALLGL- 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331787 325 leWADIINAHVISGPGIVDGLKLKGMPRGRGLLLLAEMSSAGNL--------ATGDYTAAAVKIADAHSdfVMGFI-SVN 395
Cdd:cd04725  76 --GADAVTVHPYGGSDMLKAALEAAEEKGKGLFAVTVLSSPGALdlqegipgSLEDLVERLAKLAREAG--VDGVVcGAT 151
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 22331787 396 PASWKCGYVYPSMIHATPGVQMvKGGDALGQQYNTPHSVItERGSDIIIVGRGIIKAENPAETAHEY 462
Cdd:cd04725 152 EPEALRRALGPDFLILTPGIGA-QGSGDDQKRGGTPEDAI-RAGADYIVVGRPITQAADPVAAAEAI 216
pyrE PRK00455
orotate phosphoribosyltransferase; Validated
1-181 1.43e-46

orotate phosphoribosyltransferase; Validated


Pssm-ID: 234771  Cd Length: 202  Bit Score: 160.32  E-value: 1.43e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331787    1 MSAMEALILQLHEIGAVKFGNFKLKSGIFSPVYIDLRLIVSYPSLLTQISQTLISSLPPSAT-FDVVCGVPYTALPIATV 79
Cdd:PRK00455   2 KMYAREFIEFLLEIGALLFGHFTLSSGRKSPYYFDCRKLLSYPEALALLGRFLAEAIKDSGIeFDVVAGPATGGIPLAAA 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331787   80 VSVSNGIPMLMRRKEIKDYGTSKAIEGIFEKDQTCLIIEDLVTSGASVLETAAPLRAVGLKVSDAVVLIDRQQGGRENLA 159
Cdd:PRK00455  82 VARALDLPAIFVRKEAKDHGEGGQIEGRRLFGKRVLVVEDVITTGGSVLEAVEAIRAAGAEVVGVAVIVDRQSAAQEVFA 161
                        170       180
                 ....*....|....*....|..
gi 22331787  160 ENGIKLHSMIMLTDMVRVLKEK 181
Cdd:PRK00455 162 DAGVPLISLITLDDLLEYAEEG 183
PRK05500 PRK05500
bifunctional orotidine-5'-phosphate decarboxylase/orotate phosphoribosyltransferase;
7-184 1.71e-42

bifunctional orotidine-5'-phosphate decarboxylase/orotate phosphoribosyltransferase;


Pssm-ID: 180119 [Multi-domain]  Cd Length: 477  Bit Score: 156.77  E-value: 1.71e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331787    7 LILQLHEIGAVKFGNFKLKSGIFSPVYIDLRLIVSYPSLLTQISQT---LISSLppsaTFDVVCGVPYTALPIATVVSVS 83
Cdd:PRK05500 290 LILQLYDIGCLLFGEYVQASGATFSYYIDLRKIISNPQLFHQVLSAyaeILKNL----TFDRIAGIPYGSLPTATGLALH 365
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331787   84 NGIPMLMRRKEIKDYGTSKAIEGIFEKDQTCLIIEDLVTSGASVLETAAPLRAVGLKVSDAVVLIDRQQGGRENLAENGI 163
Cdd:PRK05500 366 LHHPMIFPRKEVKAHGTRRLIEGNFHPGETVVVVDDILITGKSVMEGAEKLKSAGLNVRDIVVFIDHEQGVKDKLQSHGY 445
                        170       180
                 ....*....|....*....|.
gi 22331787  164 KLHSMIMLTDMVRVLKEKGKI 184
Cdd:PRK05500 446 QAYSVLTISEITETLYQAGRI 466
OMPdecase smart00934
Orotidine 5'-phosphate decarboxylase / HUMPS family; Orotidine 5'-phosphate decarboxylase ...
244-462 2.33e-41

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: 146.93  E-value: 2.33e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331787    244 NLCLAADVGTAAELLDIADKVGPEICLLKTHVDILPDFTPDFgskLRAIADKHKFLIFEDRKFADIGNTVtmqyEGGIFK 323
Cdd:smart00934   1 RLIVALDVPDLEEALELADALGDSVDIIKVGTELFLAEGPEG---VKELKELFGFPVFLDLKLHDIPNTV----ARAARA 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331787    324 ILE-WADIINAHVISGPGIVDGLKLKGMPRGRGLLLLAEMSSAGNLATGD----YTAAAVKI--ADAHSDFVMGFIS--- 393
Cdd:smart00934  74 AAElGADAVTVHAYAGSDMIEAALEAAKKYGPGLLAVTVLTSPGAEDLQElgdeSLEEQVLRlaKLAKEAGLDGVVCsat 153
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331787    394 -VNPASWKCGyvyPSMIHATPGVQmvkggdalGQQYNTPHSVITERGSDIIIVGRGIIKAENPAETAHEY 462
Cdd:smart00934 154 ePELIRRALG---PDFLILTPGIG--------DQGRVATPAVAIGAGADIIVVGRPITQAADPVEAAEAI 212
pyrE TIGR00336
orotate phosphoribosyltransferase; Orotate phosphoribosyltransferase (OPRTase) is involved in ...
11-174 5.99e-37

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: 133.71  E-value: 5.99e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331787    11 LHEIGAVKFGNFKLKSGIFSPVYIDLRLIVSYPSLLTQISQTLISSLPPSATFDVVCGVPYTALPIATVVSV-----SNG 85
Cdd:TIGR00336   3 LLEVQALKFGEFTLSSGRKSPYYFNIKLFNTGPELANLIARYAAAIIKSHLEFDVIAGPALGGIPIATAVSVklakpGGD 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331787    86 IPMLMRRKEIKDYGTSKAIEGIFEKDQTCLIIEDLVTSGASVLETAAPLRAVGLKVSDAVVLIDRQQ--GGRENLAENGI 163
Cdd:TIGR00336  83 IPLCFNRKEAKDHGEGGNIEGELLEGDKVVVVEDVITTGTSILEAVEIIQAAGGQVAGVIIAVDRQErsAGQEFEKEYGL 162
                         170
                  ....*....|.
gi 22331787   164 KLHSMIMLTDM 174
Cdd:TIGR00336 163 PVISLITLKDL 173
PRTases_typeI cd06223
Phosphoribosyl transferase (PRT)-type I domain; Phosphoribosyl transferase (PRT) domain. The ...
63-167 3.97e-17

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: 77.44  E-value: 3.97e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331787  63 FDVVCGVPYTALPIATVVSVSNGIPMLMRRKEIKDYGTSK-------AIEGIFEKDQTCLIIEDLVTSGASVLETAAPLR 135
Cdd:cd06223  16 PDVVVGILRGGLPLAAALARALGLPLAFIRKERKGPGRTPsepygleLPLGGDVKGKRVLLVDDVIATGGTLLAAIELLK 95
                        90       100       110
                ....*....|....*....|....*....|..
gi 22331787 136 AVGLKVSDAVVLIDRQQGGRENLAENGIKLHS 167
Cdd:cd06223  96 EAGAKVVGVAVLLDKPEGGARELASPGDPVYS 127
PyrF COG0284
Orotidine-5'-phosphate decarboxylase [Nucleotide transport and metabolism]; Orotidine-5 ...
245-463 6.07e-16

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: 76.68  E-value: 6.07e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331787 245 LCLAADVGTAAELLDIADKVGPEICLLKTHVDILPDFTPDFgskLRAIADKHkFLIFEDRKFADIGNTVTMQYEGgifkI 324
Cdd:COG0284   5 LIVALDLPDAAEALAIVDALADLVCAYKPGLALFEAYGPEG---VEALKERG-LPVFLDLKRHDIPNTVAAAARA----A 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331787 325 LEW-ADIINAHVISGPGIVDGLKLKGMPRGRGLLLLAEMSSagnlaTGDYTAAAVKIADAHSDFVMGFISVNPASWKCGY 403
Cdd:COG0284  77 AELgVDAVTVHAYGGRDMLEPALEAADESGKGVFAVTVLTS-----PGAADLQELGIEGPLYEVVLRLAKLAKEAGLDGV 151
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 22331787 404 V----YPSMIHA---------TPGVQMVkgGDALGQQ--YNTPHSVItERGSDIIIVGRGIIKAENPAETAHEYR 463
Cdd:COG0284 152 VcsatEAAALRAalgpdflllTPGIRPQ--GGDAGDQkrVGTPAEAI-AAGADYLVVGRPITYAGDPRAAAEAIR 223
PRK13813 PRK13813
orotidine 5'-phosphate decarboxylase; Provisional
240-459 4.16e-11

orotidine 5'-phosphate decarboxylase; Provisional


Pssm-ID: 237520  Cd Length: 215  Bit Score: 62.31  E-value: 4.16e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331787  240 KKETNLCLAADVGTAAELLDIADKVGPEICLLKTHvdiLPDFTPDFGSKLRAIADKHKflIFEDRKFADIGNTVTM---- 315
Cdd:PRK13813   1 EKDSRIILALDVTDRERALKIAEELDDYVDAIKVG---WPLVLASGLGIIEELKRYAP--VIADLKVADIPNTNRLicea 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331787  316 QYEGGifkilewADIINAHVISGPGIVDGLKLKGMPRGRGLLLLAEMSSAGnlATGDYTAAAVKIADAHSDF-VMGFISv 394
Cdd:PRK13813  76 VFEAG-------AWGIIVHGFTGRDSLKAVVEAAAESGGKVFVVVEMSHPG--ALEFIQPHADKLAKLAQEAgAFGVVA- 145
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 22331787  395 nPASwkcgyvYPSMIHA------------TPGV--QMVKGGDALgqqyntphsvitERGSDIIIVGRGIIKAENPAETA 459
Cdd:PRK13813 146 -PAT------RPERVRYirsrlgdelkiiSPGIgaQGGKAADAI------------KAGADYVIVGRSIYNAADPREAA 205
PRK02277 PRK02277
orotate phosphoribosyltransferase-like protein; Provisional
32-169 2.05e-09

orotate phosphoribosyltransferase-like protein; Provisional


Pssm-ID: 235023 [Multi-domain]  Cd Length: 200  Bit Score: 57.19  E-value: 2.05e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331787   32 VYIDLRLIVSYPSLLTQISQTLISSLPP-SATFDVVCGVPYTALPIATVVSVSNGIPMLMRRKEIKDYGTSKAIEGIFE- 109
Cdd:PRK02277  54 IHIDWSSIGSSSSRLRYIASAMADMLEKeDEEVDVVVGIAKSGVPLATLVADELGKDLAIYHPKKWDHGEGEKKTGSFSr 133
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 22331787  110 -----KDQTCLIIEDLVTSGASVLETAAPLRAVGLKVSDAVVLIDRqQGGREnlaENGIKLHSMI 169
Cdd:PRK02277 134 nfasvEGKRCVIVDDVITSGTTMKETIEYLKEHGGKPVAVVVLIDK-SGIDE---IDGVPVYSLI 194
PRK00230 PRK00230
orotidine-5'-phosphate decarboxylase;
245-461 1.42e-08

orotidine-5'-phosphate decarboxylase;


Pssm-ID: 234695  Cd Length: 230  Bit Score: 55.14  E-value: 1.42e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331787  245 LCLAADVGTAAELLDIADKVGPEICLLKTHVDILPDFTPDFGSKLRAIadkhKFLIFEDRKFADIGNTVtmqyEGGIFKI 324
Cdd:PRK00230   5 LIVALDFPSKEEALAFLDQLDPAVLFVKVGMELFTAGGPQFVRELKQR----GFKVFLDLKLHDIPNTV----AKAVRAL 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331787  325 LEW-ADIINAHVISGPGIVDGLKlKGMPRGRGLLLLA--EMSSagnlaTGDYTAAAVKIADAHSDFVM------------ 389
Cdd:PRK00230  77 AKLgVDMVNVHASGGPRMMKAAR-EALEPKSRPLLIAvtVLTS-----MDEEDLAELGINLSLEEQVLrlaklaqeagld 150
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 22331787  390 GFI-SVNPASW---KCGyvyPSMIHATPGVQMVkgGDALGQQYN--TPHSVItERGSDIIIVGRGIIKAENPAETAHE 461
Cdd:PRK00230 151 GVVcSAQEAAAireATG---PDFLLVTPGIRPA--GSDAGDQKRvmTPAQAI-AAGSDYIVVGRPITQAADPAAAYEA 222
Pribosyltran pfam00156
Phosphoribosyl transferase domain; This family includes a range of diverse phosphoribosyl ...
62-156 4.23e-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: 46.59  E-value: 4.23e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331787    62 TFDVVCGVPYTALPIATVVSVSNGIPMLMRRKEIK---DYGTSKAIEGIFE-KDQTCLIIEDLVTSGASVLETAAPLRAV 137
Cdd:pfam00156  29 KPDVVVGILRGGLPFAGILARRLDVPLAFVRKVSYnpdTSEVMKTSSALPDlKGKTVLIVDDILDTGGTLLKVLELLKNV 108
                          90
                  ....*....|....*....
gi 22331787   138 GLKVSDAVVLIDRQQGGRE 156
Cdd:pfam00156 109 GPKEVKIAVLIDKPAGTEP 127
PRK12560 PRK12560
adenine phosphoribosyltransferase; Provisional
63-179 1.34e-05

adenine phosphoribosyltransferase; Provisional


Pssm-ID: 183595  Cd Length: 187  Bit Score: 45.93  E-value: 1.34e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331787   63 FDVVCGVPYTALPIATVVSVSNGIPMLMRRK----------EIKDYGTSKAIEGIF----EKDQTCLIIEDLVTSGASVL 128
Cdd:PRK12560  52 IDKIVTEEDKGAPLATPVSLLSGKPLAMARWypyslselnyNVVEIGSEYFEGVVYlngiEKGDRVAIIDDTLSTGGTVI 131
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 22331787  129 ETAAPLRAVGLKVSDAVVLIDRQQ-GGRENLAE----NGIKLHSMIMLTDMVRVLK 179
Cdd:PRK12560 132 ALIKAIENSGGIVSDVICVIEKTQnNGRKKLFTqtgiNVKSLVKIDVKPHGVDIIE 187
Apt COG0503
Adenine/guanine phosphoribosyltransferase or related PRPP-binding protein [Nucleotide ...
24-164 1.36e-05

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: 45.45  E-value: 1.36e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331787  24 LKSGIfspVYIDLRLIVSYPSLLTQISQTLISSLPPSAtFDVVCGVPYTALPIATVVSVSNGIPMLMRRKEIK------- 96
Cdd:COG0503  14 PKPGI---LFRDITPLLGDPELFRAAGDELAERFADKG-IDKVVGIEARGFILAAALAYALGVPFVPARKPGKlpgetvs 89
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 22331787  97 -----DYGTSKAIE---GIFEKDQTCLIIEDLVTSGASVLETAAPLRAVGLKVSDAVVLID-RQQGGRENLAENGIK 164
Cdd:COG0503  90 eeydlEYGTGDTLElhkDALKPGDRVLIVDDLLATGGTAKAAIKLVEEAGAEVVGIAFLIElGFLGGREKLRDYPVE 166
PRK02304 PRK02304
adenine phosphoribosyltransferase; Provisional
75-169 7.20e-04

adenine phosphoribosyltransferase; Provisional


Pssm-ID: 235028  Cd Length: 175  Bit Score: 40.44  E-value: 7.20e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331787   75 PIATVVSVSNGIPMLMRRKEIK------------DYGTSKaIE---GIFEKDQTCLIIEDLVTSGASVLETAAPLRAVGL 139
Cdd:PRK02304  64 IFGAALAYKLGIGFVPVRKPGKlpretisesyelEYGTDT-LEihkDAIKPGDRVLIVDDLLATGGTLEAAIKLLERLGA 142
                         90       100       110
                 ....*....|....*....|....*....|.
gi 22331787  140 KVSDAVVLIDRQ-QGGRENLAenGIKLHSMI 169
Cdd:PRK02304 143 EVVGAAFVIELPdLGGREKLE--GYPVKSLV 171
 
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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