|
Name |
Accession |
Description |
Interval |
E-value |
| PRK05096 |
PRK05096 |
guanosine 5'-monophosphate oxidoreductase; Provisional |
33-309 |
0e+00 |
|
guanosine 5'-monophosphate oxidoreductase; Provisional
Pssm-ID: 235343 [Multi-domain] Cd Length: 346 Bit Score: 552.63 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189131341 33 KFSLFTAVHKHYSLVQWQEF-AGQNPDCLEHLAASSGTGSSDFEQLEQILEAIPQVKYICLDVANGYSEHFVEFVKDVRK 111
Cdd:PRK05096 68 SFDILTAVHKHYSVEEWAAFvNNSSADVLKHVMVSTGTSDADFEKTKQILALSPALNFICIDVANGYSEHFVQFVAKARE 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189131341 112 RFPQHTIMAGNVVTGEMVEELILSGADIIKVGIGPGSVCTTRKKTGVGYPQLSAVMECADAAHGLKGHIISDGGCSCPGD 191
Cdd:PRK05096 148 AWPDKTICAGNVVTGEMVEELILSGADIVKVGIGPGSVCTTRVKTGVGYPQLSAVIECADAAHGLGGQIVSDGGCTVPGD 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189131341 192 VAKAFGAGADFVMLGGMLAGHSESGGELIERDGKKYKLFYGMSSEMAMKKYAGGVAEYRASEGKTVEVPFKGDVEHTIRD 271
Cdd:PRK05096 228 VAKAFGGGADFVMLGGMLAGHEESGGEIVEENGEKFMLFYGMSSESAMKRHVGGVAEYRAAEGKTVKLPLRGPVENTARD 307
|
250 260 270
....*....|....*....|....*....|....*...
gi 1189131341 272 ILGGIRSTCTYVGAAKLKELSRRTTFIRVTQQVNPIFS 309
Cdd:PRK05096 308 ILGGLRSACTYVGASRLKELTKRTTFIRVQEQENRVFN 345
|
|
| GMP_reduct_1 |
TIGR01305 |
guanosine monophosphate reductase, eukaryotic; A deep split separates two families of GMP ... |
33-308 |
0e+00 |
|
guanosine monophosphate reductase, eukaryotic; A deep split separates two families of GMP reductase. This family includes both eukaryotic and some proteobacterial sequences, while the other family contains other bacterial sequences. [Purines, pyrimidines, nucleosides, and nucleotides, Nucleotide and nucleoside interconversions]
Pssm-ID: 130372 Cd Length: 343 Bit Score: 517.17 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189131341 33 KFSLFTAVHKHYSLVQWQEFA-GQNPDCLEHLAASSGTGSSDFEQLEQILEAIPQVKYICLDVANGYSEHFVEFVKDVRK 111
Cdd:TIGR01305 67 QHSIFTAIHKHYSVDEWKAFAtNSSPDCLQNVAVSSGSSDNDLEKMTSILEAVPQLKFICLDVANGYSEHFVEFVKLVRE 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189131341 112 RFPQHTIMAGNVVTGEMVEELILSGADIIKVGIGPGSVCTTRKKTGVGYPQLSAVMECADAAHGLKGHIISDGGCSCPGD 191
Cdd:TIGR01305 147 AFPEHTIMAGNVVTGEMVEELILSGADIVKVGIGPGSVCTTRTKTGVGYPQLSAVIECADAAHGLKGHIISDGGCTCPGD 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189131341 192 VAKAFGAGADFVMLGGMLAGHSESGGELIERDGKKYKLFYGMSSEMAMKKYAGGVAEYRASEGKTVEVPFKGDVEHTIRD 271
Cdd:TIGR01305 227 VAKAFGAGADFVMLGGMFAGHTESGGEVIERNGRKFKLFYGMSSDTAMKKHAGGVAEYRASEGKTVEVPYRGDVENTILD 306
|
250 260 270
....*....|....*....|....*....|....*..
gi 1189131341 272 ILGGIRSTCTYVGAAKLKELSRRTTFIRVTQQVNPIF 308
Cdd:TIGR01305 307 ILGGLRSACTYVGAAKLKELSKRATFIRVTQQHNTVF 343
|
|
| IMPDH |
cd00381 |
IMPDH: The catalytic domain of the inosine monophosphate dehydrogenase. IMPDH catalyzes the ... |
64-300 |
7.05e-116 |
|
IMPDH: The catalytic domain of the inosine monophosphate dehydrogenase. IMPDH catalyzes the NAD-dependent oxidation of inosine 5'-monophosphate (IMP) to xanthosine 5' monophosphate (XMP). It is a rate-limiting step in the de novo synthesis of the guanine nucleotides. There is often a CBS domain inserted in the middle of this domain, which is proposed to play a regulatory role. IMPDH is a key enzyme in the regulation of cell proliferation and differentiation. It has been identified as an attractive target for developing chemotherapeutic agents.
Pssm-ID: 238223 [Multi-domain] Cd Length: 325 Bit Score: 337.18 E-value: 7.05e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189131341 64 AASSGTGSSDFEQLEQILEAIpqVKYICLDVANGYSEHFVEFVKDVRKRFPQHTIMAGNVVTGEMVEELILSGADIIKVG 143
Cdd:cd00381 86 GAAVGTREDDKERAEALVEAG--VDVIVIDSAHGHSVYVIEMIKFIKKKYPNVDVIAGNVVTAEAARDLIDAGADGVKVG 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189131341 144 IGPGSVCTTRKKTGVGYPQLSAVMECADAAHGLKGHIISDGGCSCPGDVAKAFGAGADFVMLGGMLAGHSESGGELIERD 223
Cdd:cd00381 164 IGPGSICTTRIVTGVGVPQATAVADVAAAARDYGVPVIADGGIRTSGDIVKALAAGADAVMLGSLLAGTDESPGEYIEIN 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189131341 224 GKKYKLFYGMSSEMAMKK-----YAGGVAEYRASEGKTVEVPFKGDVEHTIRDILGGIRSTCTYVGAAKLKELSRRTTFI 298
Cdd:cd00381 244 GKRYKEYRGMGSLGAMKKgggdrYFGEEAKKLVPEGVEGIVPYKGSVKDVLPQLVGGLRSSMGYCGAKSLKELQEKARFV 323
|
..
gi 1189131341 299 RV 300
Cdd:cd00381 324 RI 325
|
|
| GuaB |
COG0516 |
IMP dehydrogenase/GMP reductase [Nucleotide transport and metabolism]; IMP dehydrogenase/GMP ... |
58-301 |
1.08e-89 |
|
IMP dehydrogenase/GMP reductase [Nucleotide transport and metabolism]; IMP dehydrogenase/GMP reductase is part of the Pathway/BioSystem: Purine biosynthesis
Pssm-ID: 440282 [Multi-domain] Cd Length: 326 Bit Score: 270.54 E-value: 1.08e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189131341 58 DCLEHLAASSGTGSSDFEQLEQILEAIPQVKYICLDVANGYSEHfvEFVKDVRKRFPQHTIMAGNVVTGEMVEELILSGA 137
Cdd:COG0516 81 DDGLLLLVLVGVKDDDKEKARALAAADAGVDVLVIDAAHGHSGG--DAMKKIKLTFDDVLLIPGNSATVEPARALVDAGA 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189131341 138 DIIKVGIGPGSVCTTRKKTGVGYPQLSAVMECADAAHGLKgHIISDGGCSCPGDVAKAFGAGADFVMLGGMLAGHSESGG 217
Cdd:COG0516 159 DLTKVGIGPGSICTTRVVIGLGIPQLSAAMDTVTEARMAI-AIAADGGIGYIHDNAKALAAGADAVMLGSLFAGTEEQPG 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189131341 218 ELIERDGKKYKLFYGMSSEmamkkyaggvAEYRASEGKTVEVPFKGDVEHTIRDILGGIRSTCTYVGAAKLKELSRRTTF 297
Cdd:COG0516 238 EVILYQGRSVKRYRGMGSD----------AKKLVPEGIEGRVPYKGPLEDTLHQLLGGLRSGMGYCGARTIEELREKARF 307
|
....
gi 1189131341 298 IRVT 301
Cdd:COG0516 308 VRIT 311
|
|
| IMPDH |
pfam00478 |
IMP dehydrogenase / GMP reductase domain; This family is involved in biosynthesis of guanosine ... |
64-302 |
4.35e-83 |
|
IMP dehydrogenase / GMP reductase domain; This family is involved in biosynthesis of guanosine nucleotide. Members of this family contain a TIM barrel structure. In the inosine monophosphate dehydrogenases 2 CBS domains pfam00571 are inserted in the TIM barrel. This family is a member of the common phosphate binding site TIM barrel family.
Pssm-ID: 459826 [Multi-domain] Cd Length: 463 Bit Score: 258.09 E-value: 4.35e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189131341 64 AASSGTGSSDFEQLEQILEAipQVKYICLDVANGYSEHFVEFVKDVRKRFPQHTIMAGNVVTGEMVEELILSGADIIKVG 143
Cdd:pfam00478 212 GAAVGVGDDTLERAEALVEA--GVDVLVVDTAHGHSKGVIDTVKWIKKKYPDVQVIAGNVATAEGAKALIEAGADAVKVG 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189131341 144 IGPGSVCTTRKKTGVGYPQLSAVMECADAAHGLKGHIISDGGCSCPGDVAKAFGAGADFVMLGGMLAGHSESGGELIERD 223
Cdd:pfam00478 290 IGPGSICTTRVVAGVGVPQLTAIYDVAEAAKKYGVPVIADGGIKYSGDIVKALAAGADAVMLGSLLAGTDESPGEVILYQ 369
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189131341 224 GKKYKLFYGMSSEMAMKK------YAGGVAEYRASEGktVE--VPFKGDVEHTIRDILGGIRSTCTYVGAAKLKELSRRT 295
Cdd:pfam00478 370 GRRYKSYRGMGSLGAMKKgskdryFQEDDDKKLVPEG--VEgrVPYKGPLSDVVYQLVGGLRSGMGYCGAKTIEELREKA 447
|
....*..
gi 1189131341 296 TFIRVTQ 302
Cdd:pfam00478 448 RFVRITA 454
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK05096 |
PRK05096 |
guanosine 5'-monophosphate oxidoreductase; Provisional |
33-309 |
0e+00 |
|
guanosine 5'-monophosphate oxidoreductase; Provisional
Pssm-ID: 235343 [Multi-domain] Cd Length: 346 Bit Score: 552.63 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189131341 33 KFSLFTAVHKHYSLVQWQEF-AGQNPDCLEHLAASSGTGSSDFEQLEQILEAIPQVKYICLDVANGYSEHFVEFVKDVRK 111
Cdd:PRK05096 68 SFDILTAVHKHYSVEEWAAFvNNSSADVLKHVMVSTGTSDADFEKTKQILALSPALNFICIDVANGYSEHFVQFVAKARE 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189131341 112 RFPQHTIMAGNVVTGEMVEELILSGADIIKVGIGPGSVCTTRKKTGVGYPQLSAVMECADAAHGLKGHIISDGGCSCPGD 191
Cdd:PRK05096 148 AWPDKTICAGNVVTGEMVEELILSGADIVKVGIGPGSVCTTRVKTGVGYPQLSAVIECADAAHGLGGQIVSDGGCTVPGD 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189131341 192 VAKAFGAGADFVMLGGMLAGHSESGGELIERDGKKYKLFYGMSSEMAMKKYAGGVAEYRASEGKTVEVPFKGDVEHTIRD 271
Cdd:PRK05096 228 VAKAFGGGADFVMLGGMLAGHEESGGEIVEENGEKFMLFYGMSSESAMKRHVGGVAEYRAAEGKTVKLPLRGPVENTARD 307
|
250 260 270
....*....|....*....|....*....|....*...
gi 1189131341 272 ILGGIRSTCTYVGAAKLKELSRRTTFIRVTQQVNPIFS 309
Cdd:PRK05096 308 ILGGLRSACTYVGASRLKELTKRTTFIRVQEQENRVFN 345
|
|
| GMP_reduct_1 |
TIGR01305 |
guanosine monophosphate reductase, eukaryotic; A deep split separates two families of GMP ... |
33-308 |
0e+00 |
|
guanosine monophosphate reductase, eukaryotic; A deep split separates two families of GMP reductase. This family includes both eukaryotic and some proteobacterial sequences, while the other family contains other bacterial sequences. [Purines, pyrimidines, nucleosides, and nucleotides, Nucleotide and nucleoside interconversions]
Pssm-ID: 130372 Cd Length: 343 Bit Score: 517.17 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189131341 33 KFSLFTAVHKHYSLVQWQEFA-GQNPDCLEHLAASSGTGSSDFEQLEQILEAIPQVKYICLDVANGYSEHFVEFVKDVRK 111
Cdd:TIGR01305 67 QHSIFTAIHKHYSVDEWKAFAtNSSPDCLQNVAVSSGSSDNDLEKMTSILEAVPQLKFICLDVANGYSEHFVEFVKLVRE 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189131341 112 RFPQHTIMAGNVVTGEMVEELILSGADIIKVGIGPGSVCTTRKKTGVGYPQLSAVMECADAAHGLKGHIISDGGCSCPGD 191
Cdd:TIGR01305 147 AFPEHTIMAGNVVTGEMVEELILSGADIVKVGIGPGSVCTTRTKTGVGYPQLSAVIECADAAHGLKGHIISDGGCTCPGD 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189131341 192 VAKAFGAGADFVMLGGMLAGHSESGGELIERDGKKYKLFYGMSSEMAMKKYAGGVAEYRASEGKTVEVPFKGDVEHTIRD 271
Cdd:TIGR01305 227 VAKAFGAGADFVMLGGMFAGHTESGGEVIERNGRKFKLFYGMSSDTAMKKHAGGVAEYRASEGKTVEVPYRGDVENTILD 306
|
250 260 270
....*....|....*....|....*....|....*..
gi 1189131341 272 ILGGIRSTCTYVGAAKLKELSRRTTFIRVTQQVNPIF 308
Cdd:TIGR01305 307 ILGGLRSACTYVGAAKLKELSKRATFIRVTQQHNTVF 343
|
|
| IMPDH |
cd00381 |
IMPDH: The catalytic domain of the inosine monophosphate dehydrogenase. IMPDH catalyzes the ... |
64-300 |
7.05e-116 |
|
IMPDH: The catalytic domain of the inosine monophosphate dehydrogenase. IMPDH catalyzes the NAD-dependent oxidation of inosine 5'-monophosphate (IMP) to xanthosine 5' monophosphate (XMP). It is a rate-limiting step in the de novo synthesis of the guanine nucleotides. There is often a CBS domain inserted in the middle of this domain, which is proposed to play a regulatory role. IMPDH is a key enzyme in the regulation of cell proliferation and differentiation. It has been identified as an attractive target for developing chemotherapeutic agents.
Pssm-ID: 238223 [Multi-domain] Cd Length: 325 Bit Score: 337.18 E-value: 7.05e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189131341 64 AASSGTGSSDFEQLEQILEAIpqVKYICLDVANGYSEHFVEFVKDVRKRFPQHTIMAGNVVTGEMVEELILSGADIIKVG 143
Cdd:cd00381 86 GAAVGTREDDKERAEALVEAG--VDVIVIDSAHGHSVYVIEMIKFIKKKYPNVDVIAGNVVTAEAARDLIDAGADGVKVG 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189131341 144 IGPGSVCTTRKKTGVGYPQLSAVMECADAAHGLKGHIISDGGCSCPGDVAKAFGAGADFVMLGGMLAGHSESGGELIERD 223
Cdd:cd00381 164 IGPGSICTTRIVTGVGVPQATAVADVAAAARDYGVPVIADGGIRTSGDIVKALAAGADAVMLGSLLAGTDESPGEYIEIN 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189131341 224 GKKYKLFYGMSSEMAMKK-----YAGGVAEYRASEGKTVEVPFKGDVEHTIRDILGGIRSTCTYVGAAKLKELSRRTTFI 298
Cdd:cd00381 244 GKRYKEYRGMGSLGAMKKgggdrYFGEEAKKLVPEGVEGIVPYKGSVKDVLPQLVGGLRSSMGYCGAKSLKELQEKARFV 323
|
..
gi 1189131341 299 RV 300
Cdd:cd00381 324 RI 325
|
|
| GuaB |
COG0516 |
IMP dehydrogenase/GMP reductase [Nucleotide transport and metabolism]; IMP dehydrogenase/GMP ... |
58-301 |
1.08e-89 |
|
IMP dehydrogenase/GMP reductase [Nucleotide transport and metabolism]; IMP dehydrogenase/GMP reductase is part of the Pathway/BioSystem: Purine biosynthesis
Pssm-ID: 440282 [Multi-domain] Cd Length: 326 Bit Score: 270.54 E-value: 1.08e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189131341 58 DCLEHLAASSGTGSSDFEQLEQILEAIPQVKYICLDVANGYSEHfvEFVKDVRKRFPQHTIMAGNVVTGEMVEELILSGA 137
Cdd:COG0516 81 DDGLLLLVLVGVKDDDKEKARALAAADAGVDVLVIDAAHGHSGG--DAMKKIKLTFDDVLLIPGNSATVEPARALVDAGA 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189131341 138 DIIKVGIGPGSVCTTRKKTGVGYPQLSAVMECADAAHGLKgHIISDGGCSCPGDVAKAFGAGADFVMLGGMLAGHSESGG 217
Cdd:COG0516 159 DLTKVGIGPGSICTTRVVIGLGIPQLSAAMDTVTEARMAI-AIAADGGIGYIHDNAKALAAGADAVMLGSLFAGTEEQPG 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189131341 218 ELIERDGKKYKLFYGMSSEmamkkyaggvAEYRASEGKTVEVPFKGDVEHTIRDILGGIRSTCTYVGAAKLKELSRRTTF 297
Cdd:COG0516 238 EVILYQGRSVKRYRGMGSD----------AKKLVPEGIEGRVPYKGPLEDTLHQLLGGLRSGMGYCGARTIEELREKARF 307
|
....
gi 1189131341 298 IRVT 301
Cdd:COG0516 308 VRIT 311
|
|
| IMPDH |
pfam00478 |
IMP dehydrogenase / GMP reductase domain; This family is involved in biosynthesis of guanosine ... |
64-302 |
4.35e-83 |
|
IMP dehydrogenase / GMP reductase domain; This family is involved in biosynthesis of guanosine nucleotide. Members of this family contain a TIM barrel structure. In the inosine monophosphate dehydrogenases 2 CBS domains pfam00571 are inserted in the TIM barrel. This family is a member of the common phosphate binding site TIM barrel family.
Pssm-ID: 459826 [Multi-domain] Cd Length: 463 Bit Score: 258.09 E-value: 4.35e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189131341 64 AASSGTGSSDFEQLEQILEAipQVKYICLDVANGYSEHFVEFVKDVRKRFPQHTIMAGNVVTGEMVEELILSGADIIKVG 143
Cdd:pfam00478 212 GAAVGVGDDTLERAEALVEA--GVDVLVVDTAHGHSKGVIDTVKWIKKKYPDVQVIAGNVATAEGAKALIEAGADAVKVG 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189131341 144 IGPGSVCTTRKKTGVGYPQLSAVMECADAAHGLKGHIISDGGCSCPGDVAKAFGAGADFVMLGGMLAGHSESGGELIERD 223
Cdd:pfam00478 290 IGPGSICTTRVVAGVGVPQLTAIYDVAEAAKKYGVPVIADGGIKYSGDIVKALAAGADAVMLGSLLAGTDESPGEVILYQ 369
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189131341 224 GKKYKLFYGMSSEMAMKK------YAGGVAEYRASEGktVE--VPFKGDVEHTIRDILGGIRSTCTYVGAAKLKELSRRT 295
Cdd:pfam00478 370 GRRYKSYRGMGSLGAMKKgskdryFQEDDDKKLVPEG--VEgrVPYKGPLSDVVYQLVGGLRSGMGYCGAKTIEELREKA 447
|
....*..
gi 1189131341 296 TFIRVTQ 302
Cdd:pfam00478 448 RFVRITA 454
|
|
| IMP_dehydrog |
TIGR01302 |
inosine-5'-monophosphate dehydrogenase; This model describes IMP dehydrogenase, an enzyme of ... |
64-291 |
1.11e-65 |
|
inosine-5'-monophosphate dehydrogenase; This model describes IMP dehydrogenase, an enzyme of GMP biosynthesis. This form contains two CBS domains. This model describes a rather tightly conserved cluster of IMP dehydrogenase sequences, many of which are characterized. The model excludes two related families of proteins proposed also to be IMP dehydrogenases, but without characterized members. These are related families are the subject of separate models. [Purines, pyrimidines, nucleosides, and nucleotides, Purine ribonucleotide biosynthesis]
Pssm-ID: 273546 [Multi-domain] Cd Length: 450 Bit Score: 212.98 E-value: 1.11e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189131341 64 AASSGTGSSDFEQLEQILEAipQVKYICLDVANGYSEHFVEFVKDVRKRFPQHTIMAGNVVTGEMVEELILSGADIIKVG 143
Cdd:TIGR01302 216 GAAVGTREFDKERAEALVKA--GVDVIVIDSSHGHSIYVIDSIKEIKKTYPDLDIIAGNVATAEQAKALIDAGADGLRVG 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189131341 144 IGPGSVCTTRKKTGVGYPQLSAVMECADAAHGLKGHIISDGGCSCPGDVAKAFGAGADFVMLGGMLAGHSESGGELIERD 223
Cdd:TIGR01302 294 IGPGSICTTRIVAGVGVPQITAVYDVAEYAAQSGIPVIADGGIRYSGDIVKALAAGADAVMLGSLLAGTTESPGEYEIIN 373
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1189131341 224 GKKYKLFYGMSSEMAMKK-----Y--AGGVAEYRASEGKTVEVPFKGDVEHTIRDILGGIRSTCTYVGAAKLKEL 291
Cdd:TIGR01302 374 GRRYKQYRGMGSLGAMTKgssdrYlqDENKTKKFVPEGVEGAVPYKGSVLELLPQLVGGLKSGMGYVGARSIDEL 448
|
|
| PTZ00314 |
PTZ00314 |
inosine-5'-monophosphate dehydrogenase; Provisional |
64-303 |
1.66e-61 |
|
inosine-5'-monophosphate dehydrogenase; Provisional
Pssm-ID: 240355 [Multi-domain] Cd Length: 495 Bit Score: 203.28 E-value: 1.66e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189131341 64 AASSGTGSSDFEQLEQILEAipQVKYICLDVANGYSEHFVEFVKDVRKRFPQHTIMAGNVVTGEMVEELILSGADIIKVG 143
Cdd:PTZ00314 233 GAAISTRPEDIERAAALIEA--GVDVLVVDSSQGNSIYQIDMIKKLKSNYPHVDIIAGNVVTADQAKNLIDAGADGLRIG 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189131341 144 IGPGSVCTTRKKTGVGYPQLSAVMECADAAHGLKGHIISDGGCSCPGDVAKAFGAGADFVMLGGMLAGHSESGGELIERD 223
Cdd:PTZ00314 311 MGSGSICITQEVCAVGRPQASAVYHVARYARERGVPCIADGGIKNSGDICKALALGADCVMLGSLLAGTEEAPGEYFFKD 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189131341 224 GKKYKLFYGMSSEMAM------KKYAGGVAEYRASEGKTVEVPFKGDVEHTIRDILGGIRSTCTYVGAAKLKEL-----S 292
Cdd:PTZ00314 391 GVRLKVYRGMGSLEAMlskesgERYLDENETIKVAQGVSGSVVDKGSVAKLIPYLVKGVKHGMQYIGAHSIPELheklyS 470
|
250
....*....|.
gi 1189131341 293 RRTTFIRVTQQ 303
Cdd:PTZ00314 471 GQVRFERRSGS 481
|
|
| PRK07807 |
PRK07807 |
GuaB1 family IMP dehydrogenase-related protein; |
78-294 |
1.74e-59 |
|
GuaB1 family IMP dehydrogenase-related protein;
Pssm-ID: 181127 [Multi-domain] Cd Length: 479 Bit Score: 197.43 E-value: 1.74e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189131341 78 EQILEAipQVKYICLDVANGYSEHFVEFVKDVRKRFPQHTIMAGNVVTGEMVEELILSGADIIKVGIGPGSVCTTRKKTG 157
Cdd:PRK07807 233 RALLEA--GVDVLVVDTAHGHQEKMLEALRAVRALDPGVPIVAGNVVTAEGTRDLVEAGADIVKVGVGPGAMCTTRMMTG 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189131341 158 VGYPQLSAVMECADAAHGLKGHIISDGGCSCPGDVAKAFGAGADFVMLGGMLAGHSESGGEL-IERDGKKYKLFYGMSSE 236
Cdd:PRK07807 311 VGRPQFSAVLECAAAARELGAHVWADGGVRHPRDVALALAAGASNVMIGSWFAGTYESPGDLmRDRDGRPYKESFGMASA 390
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1189131341 237 MAMKKYAGGVAEY-RA---------SEGKTVEVPFKGDVEHTIRDILGGIRSTCTYVGAAKLKELSRR 294
Cdd:PRK07807 391 RAVAARTAGDSAFdRArkalfeegiSTSRMYLDPGRPGVEDLLDHITSGVRSSCTYAGARTLAEFHER 458
|
|
| IMP_DH_rel_1 |
TIGR01303 |
IMP dehydrogenase family protein; This model represents a family of proteins, often annotated ... |
78-296 |
3.20e-56 |
|
IMP dehydrogenase family protein; This model represents a family of proteins, often annotated as a putative IMP dehydrogenase, related to IMP dehydrogenase and GMP reductase and restricted to the high GC Gram-positive bacteria. All species in which a member is found so far (Corynebacterium glutamicum, Mycobacterium tuberculosis, Streptomyces coelicolor, etc.) also have IMP dehydrogenase as described by TIGRFAMs entry TIGR01302. [Unknown function, General]
Pssm-ID: 130370 [Multi-domain] Cd Length: 475 Bit Score: 188.96 E-value: 3.20e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189131341 78 EQILEAipQVKYICLDVANGYSEHFVEFVKDVRKRFPQHTIMAGNVVTGEMVEELILSGADIIKVGIGPGSVCTTRKKTG 157
Cdd:TIGR01303 231 KALLDA--GVDVLVIDTAHGHQVKMISAIKAVRALDLGVPIVAGNVVSAEGVRDLLEAGANIIKVGVGPGAMCTTRMMTG 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189131341 158 VGYPQLSAVMECADAAHGLKGHIISDGGCSCPGDVAKAFGAGADFVMLGGMLAGHSESGGELI-ERDGKKYKLFYGMSSE 236
Cdd:TIGR01303 309 VGRPQFSAVLECAAEARKLGGHVWADGGVRHPRDVALALAAGASNVMVGSWFAGTYESPGDLMrDRDGRPYKESFGMASK 388
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189131341 237 MAMKKYAGGVAEY-RA---------SEGKTVEVPFKGDVEHTIRDILGGIRSTCTYVGAAKLKELSRRTT 296
Cdd:TIGR01303 389 RAVVARTGADNAFdRArkalfeegiSTSRMGLDPDRGGVEDLIDHIISGVRSSCTYAGASSLEEFHERAV 458
|
|
| PRK05458 |
PRK05458 |
guanosine 5'-monophosphate oxidoreductase; Provisional |
66-310 |
4.98e-56 |
|
guanosine 5'-monophosphate oxidoreductase; Provisional
Pssm-ID: 235479 [Multi-domain] Cd Length: 326 Bit Score: 184.39 E-value: 4.98e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189131341 66 SSGTGSSDFEQLEQILEAIPQVKYICLDVANGYSEHFVEFVKDVRKRFPQHTIMAGNVVTGEMVEELILSGADIIKVGIG 145
Cdd:PRK05458 91 SVGVKDDEYDFVDQLAAEGLTPEYITIDIAHGHSDSVINMIQHIKKHLPETFVIAGNVGTPEAVRELENAGADATKVGIG 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189131341 146 PGSVCTTRKKTGVGYP--QLSAVMECADAAhglKGHIISDGGCSCPGDVAKAFGAGADFVMLGGMLAGHSESGGELIERD 223
Cdd:PRK05458 171 PGKVCITKIKTGFGTGgwQLAALRWCAKAA---RKPIIADGGIRTHGDIAKSIRFGATMVMIGSLFAGHEESPGKTVEID 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189131341 224 GKKYKLFYGMSSEmamkkYAGGvaEYRASEGKTVEVPFKGDVEHTIRDILGGIRSTCTYVGAAKLKELsRRTTFIRVTqq 303
Cdd:PRK05458 248 GKLYKEYFGSASE-----FQKG--EYKNVEGKKILVPHKGSLKDTLTEMEQDLQSSISYAGGRDLDAI-RKVDYVIVK-- 317
|
....*..
gi 1189131341 304 vNPIFSE 310
Cdd:PRK05458 318 -NSIFNG 323
|
|
| PRK06843 |
PRK06843 |
inosine 5-monophosphate dehydrogenase; Validated |
71-302 |
5.33e-52 |
|
inosine 5-monophosphate dehydrogenase; Validated
Pssm-ID: 180725 [Multi-domain] Cd Length: 404 Bit Score: 176.00 E-value: 5.33e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189131341 71 SSDFEQLEQILEAI-PQVKYICLDVANGYSEHFVEFVKDVRKRFPQHTIMAGNVVTGEMVEELILSGADIIKVGIGPGSV 149
Cdd:PRK06843 149 SIDIDTIERVEELVkAHVDILVIDSAHGHSTRIIELVKKIKTKYPNLDLIAGNIVTKEAALDLISVGADCLKVGIGPGSI 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189131341 150 CTTRKKTGVGYPQLSAVMECADAAHGLKGHIISDGGCSCPGDVAKAFGAGADFVMLGGMLAGHSESGGELIERDGKKYKL 229
Cdd:PRK06843 229 CTTRIVAGVGVPQITAICDVYEVCKNTNICIIADGGIRFSGDVVKAIAAGADSVMIGNLFAGTKESPSEEIIYNGKKFKS 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189131341 230 FYGMSSEMAMKKyaGGVAEY----------RASEGKTVEVPFKGDVEHTIRDILGGIRSTCTYVGAAKLKELSRRTTFIR 299
Cdd:PRK06843 309 YVGMGSISAMKR--GSKSRYfqlennepkkLVPEGIEGMVPYSGKLKDILTQLKGGLMSGMGYLGAATISDLKINSKFVK 386
|
...
gi 1189131341 300 VTQ 302
Cdd:PRK06843 387 ISH 389
|
|
| PLN02274 |
PLN02274 |
inosine-5'-monophosphate dehydrogenase |
64-290 |
6.21e-37 |
|
inosine-5'-monophosphate dehydrogenase
Pssm-ID: 215154 [Multi-domain] Cd Length: 505 Bit Score: 137.88 E-value: 6.21e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189131341 64 AASSGTGSSDFEQLEQILEAipQVKYICLDVANGYSEHFVEFVKDVRKRFPQHTIMAGNVVTGEMVEELILSGADIIKVG 143
Cdd:PLN02274 240 GAAIGTRESDKERLEHLVKA--GVDVVVLDSSQGDSIYQLEMIKYIKKTYPELDVIGGNVVTMYQAQNLIQAGVDGLRVG 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189131341 144 IGPGSVCTTRKKTGVGYPQLSAVMECADAAHGLKGHIISDGGCSCPGDVAKAFGAGADFVMLGGMLAGHSESGGELIERD 223
Cdd:PLN02274 318 MGSGSICTTQEVCAVGRGQATAVYKVASIAAQHGVPVIADGGISNSGHIVKALTLGASTVMMGSFLAGTTEAPGEYFYQD 397
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1189131341 224 GKKYKLFYGMSSEMAMKK-----YAGGVAEYRASEGKTVEVPFKGDVEHTIRDILGGIRSTCTYVGAAKLKE 290
Cdd:PLN02274 398 GVRVKKYRGMGSLEAMTKgsdqrYLGDTAKLKIAQGVSGAVADKGSVLKFVPYTMQAVKQGFQDLGASSLQS 469
|
|
| PRK07107 |
PRK07107 |
IMP dehydrogenase; |
55-301 |
2.15e-28 |
|
IMP dehydrogenase;
Pssm-ID: 180842 [Multi-domain] Cd Length: 502 Bit Score: 114.02 E-value: 2.15e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189131341 55 QNPDCL----EHLAASSGTGSSDF-EQLEQILEAipQVKYICLDVANGYSEHFVEFVKDVRKRFPQHT-IMAGNVVTGEM 128
Cdd:PRK07107 220 ENPLELldssKRYVVGAGINTRDYaERVPALVEA--GADVLCIDSSEGYSEWQKRTLDWIREKYGDSVkVGAGNVVDREG 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189131341 129 VEELILSGADIIKVGIGPGSVCTTRKKTGVGYPQLSAVMECADA------AHGLKGHIISDGGCSCPGDVAKAFGAGADF 202
Cdd:PRK07107 298 FRYLAEAGADFVKVGIGGGSICITREQKGIGRGQATALIEVAKArdeyfeETGVYIPICSDGGIVYDYHMTLALAMGADF 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189131341 203 VMLGGMLAGHSESGGELIERDGKKYKLFYGMSSEMAM--KKY-AGGVAEYRASEGKTVEVPFKGDVEHTIRDILGGIRST 279
Cdd:PRK07107 378 IMLGRYFARFDESPTNKVNINGNYMKEYWGEGSNRARnwQRYdLGGDKKLSFEEGVDSYVPYAGSLKDNVAITLSKVRST 457
|
250 260
....*....|....*....|..
gi 1189131341 280 CTYVGAAKLKELSRRTTFIRVT 301
Cdd:PRK07107 458 MCNCGALSIPELQQKAKITLVS 479
|
|
| TIM_phosphate_binding |
cd04722 |
TIM barrel proteins share a structurally conserved phosphate binding motif and in general ... |
86-207 |
6.74e-05 |
|
TIM barrel proteins share a structurally conserved phosphate binding motif and in general share an eight beta/alpha closed barrel structure. Specific for this family is the conserved phosphate binding site at the edges of strands 7 and 8. The phosphate comes either from the substrate, as in the case of inosine monophosphate dehydrogenase (IMPDH), or from ribulose-5-phosphate 3-epimerase (RPE) or from cofactors, like FMN.
Pssm-ID: 240073 [Multi-domain] Cd Length: 200 Bit Score: 42.96 E-value: 6.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189131341 86 QVKYICLDVANGYS-EHFVEFVKDVRKRFPQHTIMAGNVVTGEMVEE-LILSGADIIKVGIGPGsvcTTRKKTGVGYPQL 163
Cdd:cd04722 84 GADGVEIHGAVGYLaREDLELIRELREAVPDVKVVVKLSPTGELAAAaAEEAGVDEVGLGNGGG---GGGGRDAVPIADL 160
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1189131341 164 SAvmECADAAHGLKghIISDGGCSCPGDVAKAFGAGADFVMLGG 207
Cdd:cd04722 161 LL--ILAKRGSKVP--VIAGGGINDPEDAAEALALGADGVIVGS 200
|
|
| KDPG_aldolase |
cd00452 |
KDPG and KHG aldolase; KDPG and KHG aldolase. This family belongs to the class I adolases ... |
104-205 |
2.99e-04 |
|
KDPG and KHG aldolase; KDPG and KHG aldolase. This family belongs to the class I adolases whose reaction mechanism involves Schiff base formation between a substrate carbonyl and lysine residue in the active site. 2-keto-3-deoxy-6-phosphogluconate (KDPG) aldolase, is best known for its role in the Entner-Doudoroff pathway of bacteria, where it catalyzes the reversible cleavage of KDPG to pyruvate and glyceraldehyde-3-phosphate. 2-keto-4-hydroxyglutarate (KHG) aldolase, which has enzymatic specificity toward glyoxylate, forming KHG in the presence of pyruvate, and is capable of regulating glyoxylate levels in the glyoxylate bypass, an alternate pathway when bacteria are grown on acetate carbon sources.
Pssm-ID: 188632 Cd Length: 190 Bit Score: 40.96 E-value: 2.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189131341 104 EFVKDVRKRFPQHTIMAGNVVTGEMVEELILSGADIIkvgIGPGSVcttrkktgvgyPQLsavmecADAAHGLKGHIIsd 183
Cdd:cd00452 44 EAIRALRKEFPEALIGAGTVLTPEQADAAIAAGAQFI---VSPGLD-----------PEV------VKAANRAGIPLL-- 101
|
90 100
....*....|....*....|..
gi 1189131341 184 GGCSCPGDVAKAFGAGADFVML 205
Cdd:cd00452 102 PGVATPTEIMQALELGADIVKL 123
|
|
| Glu_synthase |
pfam01645 |
Conserved region in glutamate synthase; This family represents a region of the glutamate ... |
98-206 |
8.07e-03 |
|
Conserved region in glutamate synthase; This family represents a region of the glutamate synthase protein. This region is expressed as a separate subunit in the glutamate synthase alpha subunit from archaebacteria, or part of a large multidomain enzyme in other organizms. The aligned region of these proteins contains a putative FMN binding site and Fe-S cluster.
Pssm-ID: 396287 [Multi-domain] Cd Length: 367 Bit Score: 37.70 E-value: 8.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189131341 98 YS-EHFVEFVKDVRKRFPQHTIMAGnvVTGEMVEELILSG-----ADIIKV-GIGPG---SVCTTRKKTGVgyPQLSAVM 167
Cdd:pfam01645 184 YSiEDLAQLIYDLKEINPKAPISVK--LVSGHGVGTIAAGvakagADIILIdGYDGGtgaSPKTSIKHAGL--PWELALA 259
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1189131341 168 EcADAAHGLKGH-----IISDGGCSCPGDVAKAFGAGADFVMLG 206
Cdd:pfam01645 260 E-AHQTLKENGLrdrvsLIADGGLRTGADVAKAAALGADAVYIG 302
|
|
| |
