|
Name |
Accession |
Description |
Interval |
E-value |
| PRK05096 |
PRK05096 |
guanosine 5'-monophosphate oxidoreductase; Provisional |
3-317 |
0e+00 |
|
guanosine 5'-monophosphate oxidoreductase; Provisional
Pssm-ID: 235343 [Multi-domain] Cd Length: 346 Bit Score: 632.36 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545688070 3 HIDNDVKLDFKDVLLRPKRSTLKSRSEVDLTRSFSFRNSKQTYSGVPIIAANMDTVGTFEMAKVLCK------------- 69
Cdd:PRK05096 2 RIEEDLKLGFKDVLIRPKRSTLKSRSDVELERQFTFKHSGQSWSGVPIIAANMDTVGTFEMAKALASfdiltavhkhysv 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545688070 70 ----------------HLAASSGTGSSDFEQLEQILEAIPQVKYICLDVANGYSEHFVEFVKDVRKRFPQHTIMAGNVVT 133
Cdd:PRK05096 82 eewaafvnnssadvlkHVMVSTGTSDADFEKTKQILALSPALNFICIDVANGYSEHFVQFVAKAREAWPDKTICAGNVVT 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545688070 134 GEMVEELILSGADIIKVGIGPGSVCTTRKKTGVGYPQLSAVMECADAAHGLKGHIISDGGCSCPGDVAKAFGAGADFVML 213
Cdd:PRK05096 162 GEMVEELILSGADIVKVGIGPGSVCTTRVKTGVGYPQLSAVIECADAAHGLGGQIVSDGGCTVPGDVAKAFGGGADFVML 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545688070 214 GGMLAGHSESGGELIERDGKKYKLFYGMSSEMAMKKYAGGVAEYRASEGKTVEVPFKGDVEHTIRDILGGIRSTCTYVGA 293
Cdd:PRK05096 242 GGMLAGHEESGGEIVEENGEKFMLFYGMSSESAMKRHVGGVAEYRAAEGKTVKLPLRGPVENTARDILGGLRSACTYVGA 321
|
330 340
....*....|....*....|....
gi 545688070 294 AKLKELSRRTTFIRVTQQVNPIFS 317
Cdd:PRK05096 322 SRLKELTKRTTFIRVQEQENRVFN 345
|
|
| GMP_reduct_1 |
TIGR01305 |
guanosine monophosphate reductase, eukaryotic; A deep split separates two families of GMP ... |
4-316 |
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: 579.57 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545688070 4 IDNDVKLDFKDVLLRPKRSTLKSRSEVDLTRSFSFRNSKQTYSGVPIIAANMDTVGTFEMAKVLC--------------- 68
Cdd:TIGR01305 2 IEADLKLDFKDVLLRPKRSTLKSRADVELERTFTFRNSKQTYSGVPIIAANMDTVGTFEMAAALSqhsiftaihkhysvd 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545688070 69 --------------KHLAASSGTGSSDFEQLEQILEAIPQVKYICLDVANGYSEHFVEFVKDVRKRFPQHTIMAGNVVTG 134
Cdd:TIGR01305 82 ewkafatnsspdclQNVAVSSGSSDNDLEKMTSILEAVPQLKFICLDVANGYSEHFVEFVKLVREAFPEHTIMAGNVVTG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545688070 135 EMVEELILSGADIIKVGIGPGSVCTTRKKTGVGYPQLSAVMECADAAHGLKGHIISDGGCSCPGDVAKAFGAGADFVMLG 214
Cdd:TIGR01305 162 EMVEELILSGADIVKVGIGPGSVCTTRTKTGVGYPQLSAVIECADAAHGLKGHIISDGGCTCPGDVAKAFGAGADFVMLG 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545688070 215 GMLAGHSESGGELIERDGKKYKLFYGMSSEMAMKKYAGGVAEYRASEGKTVEVPFKGDVEHTIRDILGGIRSTCTYVGAA 294
Cdd:TIGR01305 242 GMFAGHTESGGEVIERNGRKFKLFYGMSSDTAMKKHAGGVAEYRASEGKTVEVPYRGDVENTILDILGGLRSACTYVGAA 321
|
330 340
....*....|....*....|..
gi 545688070 295 KLKELSRRTTFIRVTQQVNPIF 316
Cdd:TIGR01305 322 KLKELSKRATFIRVTQQHNTVF 343
|
|
| IMPDH |
cd00381 |
IMPDH: The catalytic domain of the inosine monophosphate dehydrogenase. IMPDH catalyzes the ... |
10-308 |
3.04e-132 |
|
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: 379.17 E-value: 3.04e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545688070 10 LDFKDVLLRPKRSTLkSRSEVDLTRSFSfrnsKQTYSGVPIIAANMDTVGTFEMAKVLCKH------------------- 70
Cdd:cd00381 2 LTFDDVLLVPGYSTV-LPSEVDLSTKLT----KNITLNIPLVSAPMDTVTESEMAIAMARLggigvihrnmsieeqaeev 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545688070 71 --------LAASSGTGSSDFEQLEQILEAIpqVKYICLDVANGYSEHFVEFVKDVRKRFPQHTIMAGNVVTGEMVEELIL 142
Cdd:cd00381 77 rkvkgrllVGAAVGTREDDKERAEALVEAG--VDVIVIDSAHGHSVYVIEMIKFIKKKYPNVDVIAGNVVTAEAARDLID 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545688070 143 SGADIIKVGIGPGSVCTTRKKTGVGYPQLSAVMECADAAHGLKGHIISDGGCSCPGDVAKAFGAGADFVMLGGMLAGHSE 222
Cdd:cd00381 155 AGADGVKVGIGPGSICTTRIVTGVGVPQATAVADVAAAARDYGVPVIADGGIRTSGDIVKALAAGADAVMLGSLLAGTDE 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545688070 223 SGGELIERDGKKYKLFYGMSSEMAMKK-----YAGGVAEYRASEGKTVEVPFKGDVEHTIRDILGGIRSTCTYVGAAKLK 297
Cdd:cd00381 235 SPGEYIEINGKRYKEYRGMGSLGAMKKgggdrYFGEEAKKLVPEGVEGIVPYKGSVKDVLPQLVGGLRSSMGYCGAKSLK 314
|
330
....*....|.
gi 545688070 298 ELSRRTTFIRV 308
Cdd:cd00381 315 ELQEKARFVRI 325
|
|
| GuaB |
COG0516 |
IMP dehydrogenase/GMP reductase [Nucleotide transport and metabolism]; IMP dehydrogenase/GMP ... |
70-309 |
1.58e-86 |
|
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: 262.84 E-value: 1.58e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545688070 70 HLAASSGTGSSDFEQLEQILEAIPQVKYICLDVANGYSEHfvEFVKDVRKRFPQHTIMAGNVVTGEMVEELILSGADIIK 149
Cdd:COG0516 85 LLLVLVGVKDDDKEKARALAAADAGVDVLVIDAAHGHSGG--DAMKKIKLTFDDVLLIPGNSATVEPARALVDAGADLTK 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545688070 150 VGIGPGSVCTTRKKTGVGYPQLSAVMECADAAHGLKgHIISDGGCSCPGDVAKAFGAGADFVMLGGMLAGHSESGGELIE 229
Cdd:COG0516 163 VGIGPGSICTTRVVIGLGIPQLSAAMDTVTEARMAI-AIAADGGIGYIHDNAKALAAGADAVMLGSLFAGTEEQPGEVIL 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545688070 230 RDGKKYKLFYGMSSEmamkkyaggvAEYRASEGKTVEVPFKGDVEHTIRDILGGIRSTCTYVGAAKLKELSRRTTFIRVT 309
Cdd:COG0516 242 YQGRSVKRYRGMGSD----------AKKLVPEGIEGRVPYKGPLEDTLHQLLGGLRSGMGYCGARTIEELREKARFVRIT 311
|
|
| IMPDH |
pfam00478 |
IMP dehydrogenase / GMP reductase domain; This family is involved in biosynthesis of guanosine ... |
72-310 |
8.64e-82 |
|
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: 255.01 E-value: 8.64e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545688070 72 AASSGTGSSDFEQLEQILEAipQVKYICLDVANGYSEHFVEFVKDVRKRFPQHTIMAGNVVTGEMVEELILSGADIIKVG 151
Cdd:pfam00478 212 GAAVGVGDDTLERAEALVEA--GVDVLVVDTAHGHSKGVIDTVKWIKKKYPDVQVIAGNVATAEGAKALIEAGADAVKVG 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545688070 152 IGPGSVCTTRKKTGVGYPQLSAVMECADAAHGLKGHIISDGGCSCPGDVAKAFGAGADFVMLGGMLAGHSESGGELIERD 231
Cdd:pfam00478 290 IGPGSICTTRVVAGVGVPQLTAIYDVAEAAKKYGVPVIADGGIKYSGDIVKALAAGADAVMLGSLLAGTDESPGEVILYQ 369
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545688070 232 GKKYKLFYGMSSEMAMKK------YAGGVAEYRASEGktVE--VPFKGDVEHTIRDILGGIRSTCTYVGAAKLKELSRRT 303
Cdd:pfam00478 370 GRRYKSYRGMGSLGAMKKgskdryFQEDDDKKLVPEG--VEgrVPYKGPLSDVVYQLVGGLRSGMGYCGAKTIEELREKA 447
|
....*..
gi 545688070 304 TFIRVTQ 310
Cdd:pfam00478 448 RFVRITA 454
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK05096 |
PRK05096 |
guanosine 5'-monophosphate oxidoreductase; Provisional |
3-317 |
0e+00 |
|
guanosine 5'-monophosphate oxidoreductase; Provisional
Pssm-ID: 235343 [Multi-domain] Cd Length: 346 Bit Score: 632.36 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545688070 3 HIDNDVKLDFKDVLLRPKRSTLKSRSEVDLTRSFSFRNSKQTYSGVPIIAANMDTVGTFEMAKVLCK------------- 69
Cdd:PRK05096 2 RIEEDLKLGFKDVLIRPKRSTLKSRSDVELERQFTFKHSGQSWSGVPIIAANMDTVGTFEMAKALASfdiltavhkhysv 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545688070 70 ----------------HLAASSGTGSSDFEQLEQILEAIPQVKYICLDVANGYSEHFVEFVKDVRKRFPQHTIMAGNVVT 133
Cdd:PRK05096 82 eewaafvnnssadvlkHVMVSTGTSDADFEKTKQILALSPALNFICIDVANGYSEHFVQFVAKAREAWPDKTICAGNVVT 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545688070 134 GEMVEELILSGADIIKVGIGPGSVCTTRKKTGVGYPQLSAVMECADAAHGLKGHIISDGGCSCPGDVAKAFGAGADFVML 213
Cdd:PRK05096 162 GEMVEELILSGADIVKVGIGPGSVCTTRVKTGVGYPQLSAVIECADAAHGLGGQIVSDGGCTVPGDVAKAFGGGADFVML 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545688070 214 GGMLAGHSESGGELIERDGKKYKLFYGMSSEMAMKKYAGGVAEYRASEGKTVEVPFKGDVEHTIRDILGGIRSTCTYVGA 293
Cdd:PRK05096 242 GGMLAGHEESGGEIVEENGEKFMLFYGMSSESAMKRHVGGVAEYRAAEGKTVKLPLRGPVENTARDILGGLRSACTYVGA 321
|
330 340
....*....|....*....|....
gi 545688070 294 AKLKELSRRTTFIRVTQQVNPIFS 317
Cdd:PRK05096 322 SRLKELTKRTTFIRVQEQENRVFN 345
|
|
| GMP_reduct_1 |
TIGR01305 |
guanosine monophosphate reductase, eukaryotic; A deep split separates two families of GMP ... |
4-316 |
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: 579.57 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545688070 4 IDNDVKLDFKDVLLRPKRSTLKSRSEVDLTRSFSFRNSKQTYSGVPIIAANMDTVGTFEMAKVLC--------------- 68
Cdd:TIGR01305 2 IEADLKLDFKDVLLRPKRSTLKSRADVELERTFTFRNSKQTYSGVPIIAANMDTVGTFEMAAALSqhsiftaihkhysvd 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545688070 69 --------------KHLAASSGTGSSDFEQLEQILEAIPQVKYICLDVANGYSEHFVEFVKDVRKRFPQHTIMAGNVVTG 134
Cdd:TIGR01305 82 ewkafatnsspdclQNVAVSSGSSDNDLEKMTSILEAVPQLKFICLDVANGYSEHFVEFVKLVREAFPEHTIMAGNVVTG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545688070 135 EMVEELILSGADIIKVGIGPGSVCTTRKKTGVGYPQLSAVMECADAAHGLKGHIISDGGCSCPGDVAKAFGAGADFVMLG 214
Cdd:TIGR01305 162 EMVEELILSGADIVKVGIGPGSVCTTRTKTGVGYPQLSAVIECADAAHGLKGHIISDGGCTCPGDVAKAFGAGADFVMLG 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545688070 215 GMLAGHSESGGELIERDGKKYKLFYGMSSEMAMKKYAGGVAEYRASEGKTVEVPFKGDVEHTIRDILGGIRSTCTYVGAA 294
Cdd:TIGR01305 242 GMFAGHTESGGEVIERNGRKFKLFYGMSSDTAMKKHAGGVAEYRASEGKTVEVPYRGDVENTILDILGGLRSACTYVGAA 321
|
330 340
....*....|....*....|..
gi 545688070 295 KLKELSRRTTFIRVTQQVNPIF 316
Cdd:TIGR01305 322 KLKELSKRATFIRVTQQHNTVF 343
|
|
| IMPDH |
cd00381 |
IMPDH: The catalytic domain of the inosine monophosphate dehydrogenase. IMPDH catalyzes the ... |
10-308 |
3.04e-132 |
|
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: 379.17 E-value: 3.04e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545688070 10 LDFKDVLLRPKRSTLkSRSEVDLTRSFSfrnsKQTYSGVPIIAANMDTVGTFEMAKVLCKH------------------- 70
Cdd:cd00381 2 LTFDDVLLVPGYSTV-LPSEVDLSTKLT----KNITLNIPLVSAPMDTVTESEMAIAMARLggigvihrnmsieeqaeev 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545688070 71 --------LAASSGTGSSDFEQLEQILEAIpqVKYICLDVANGYSEHFVEFVKDVRKRFPQHTIMAGNVVTGEMVEELIL 142
Cdd:cd00381 77 rkvkgrllVGAAVGTREDDKERAEALVEAG--VDVIVIDSAHGHSVYVIEMIKFIKKKYPNVDVIAGNVVTAEAARDLID 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545688070 143 SGADIIKVGIGPGSVCTTRKKTGVGYPQLSAVMECADAAHGLKGHIISDGGCSCPGDVAKAFGAGADFVMLGGMLAGHSE 222
Cdd:cd00381 155 AGADGVKVGIGPGSICTTRIVTGVGVPQATAVADVAAAARDYGVPVIADGGIRTSGDIVKALAAGADAVMLGSLLAGTDE 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545688070 223 SGGELIERDGKKYKLFYGMSSEMAMKK-----YAGGVAEYRASEGKTVEVPFKGDVEHTIRDILGGIRSTCTYVGAAKLK 297
Cdd:cd00381 235 SPGEYIEINGKRYKEYRGMGSLGAMKKgggdrYFGEEAKKLVPEGVEGIVPYKGSVKDVLPQLVGGLRSSMGYCGAKSLK 314
|
330
....*....|.
gi 545688070 298 ELSRRTTFIRV 308
Cdd:cd00381 315 ELQEKARFVRI 325
|
|
| GuaB |
COG0516 |
IMP dehydrogenase/GMP reductase [Nucleotide transport and metabolism]; IMP dehydrogenase/GMP ... |
70-309 |
1.58e-86 |
|
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: 262.84 E-value: 1.58e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545688070 70 HLAASSGTGSSDFEQLEQILEAIPQVKYICLDVANGYSEHfvEFVKDVRKRFPQHTIMAGNVVTGEMVEELILSGADIIK 149
Cdd:COG0516 85 LLLVLVGVKDDDKEKARALAAADAGVDVLVIDAAHGHSGG--DAMKKIKLTFDDVLLIPGNSATVEPARALVDAGADLTK 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545688070 150 VGIGPGSVCTTRKKTGVGYPQLSAVMECADAAHGLKgHIISDGGCSCPGDVAKAFGAGADFVMLGGMLAGHSESGGELIE 229
Cdd:COG0516 163 VGIGPGSICTTRVVIGLGIPQLSAAMDTVTEARMAI-AIAADGGIGYIHDNAKALAAGADAVMLGSLFAGTEEQPGEVIL 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545688070 230 RDGKKYKLFYGMSSEmamkkyaggvAEYRASEGKTVEVPFKGDVEHTIRDILGGIRSTCTYVGAAKLKELSRRTTFIRVT 309
Cdd:COG0516 242 YQGRSVKRYRGMGSD----------AKKLVPEGIEGRVPYKGPLEDTLHQLLGGLRSGMGYCGARTIEELREKARFVRIT 311
|
|
| IMPDH |
pfam00478 |
IMP dehydrogenase / GMP reductase domain; This family is involved in biosynthesis of guanosine ... |
72-310 |
8.64e-82 |
|
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: 255.01 E-value: 8.64e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545688070 72 AASSGTGSSDFEQLEQILEAipQVKYICLDVANGYSEHFVEFVKDVRKRFPQHTIMAGNVVTGEMVEELILSGADIIKVG 151
Cdd:pfam00478 212 GAAVGVGDDTLERAEALVEA--GVDVLVVDTAHGHSKGVIDTVKWIKKKYPDVQVIAGNVATAEGAKALIEAGADAVKVG 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545688070 152 IGPGSVCTTRKKTGVGYPQLSAVMECADAAHGLKGHIISDGGCSCPGDVAKAFGAGADFVMLGGMLAGHSESGGELIERD 231
Cdd:pfam00478 290 IGPGSICTTRVVAGVGVPQLTAIYDVAEAAKKYGVPVIADGGIKYSGDIVKALAAGADAVMLGSLLAGTDESPGEVILYQ 369
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545688070 232 GKKYKLFYGMSSEMAMKK------YAGGVAEYRASEGktVE--VPFKGDVEHTIRDILGGIRSTCTYVGAAKLKELSRRT 303
Cdd:pfam00478 370 GRRYKSYRGMGSLGAMKKgskdryFQEDDDKKLVPEG--VEgrVPYKGPLSDVVYQLVGGLRSGMGYCGAKTIEELREKA 447
|
....*..
gi 545688070 304 TFIRVTQ 310
Cdd:pfam00478 448 RFVRITA 454
|
|
| IMP_dehydrog |
TIGR01302 |
inosine-5'-monophosphate dehydrogenase; This model describes IMP dehydrogenase, an enzyme of ... |
72-299 |
5.90e-64 |
|
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: 208.74 E-value: 5.90e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545688070 72 AASSGTGSSDFEQLEQILEAipQVKYICLDVANGYSEHFVEFVKDVRKRFPQHTIMAGNVVTGEMVEELILSGADIIKVG 151
Cdd:TIGR01302 216 GAAVGTREFDKERAEALVKA--GVDVIVIDSSHGHSIYVIDSIKEIKKTYPDLDIIAGNVATAEQAKALIDAGADGLRVG 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545688070 152 IGPGSVCTTRKKTGVGYPQLSAVMECADAAHGLKGHIISDGGCSCPGDVAKAFGAGADFVMLGGMLAGHSESGGELIERD 231
Cdd:TIGR01302 294 IGPGSICTTRIVAGVGVPQITAVYDVAEYAAQSGIPVIADGGIRYSGDIVKALAAGADAVMLGSLLAGTTESPGEYEIIN 373
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 545688070 232 GKKYKLFYGMSSEMAMKK-----Y--AGGVAEYRASEGKTVEVPFKGDVEHTIRDILGGIRSTCTYVGAAKLKEL 299
Cdd:TIGR01302 374 GRRYKQYRGMGSLGAMTKgssdrYlqDENKTKKFVPEGVEGAVPYKGSVLELLPQLVGGLKSGMGYVGARSIDEL 448
|
|
| PRK05458 |
PRK05458 |
guanosine 5'-monophosphate oxidoreductase; Provisional |
10-318 |
7.80e-63 |
|
guanosine 5'-monophosphate oxidoreductase; Provisional
Pssm-ID: 235479 [Multi-domain] Cd Length: 326 Bit Score: 202.11 E-value: 7.80e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545688070 10 LDFKDVLLRPKRSTLKSRSEVDLTRSFSFRNSKqtysgVPIIAANMDTVGTFEMAKVLCKH------------------- 70
Cdd:PRK05458 5 FDYEDIQLIPNKCIVNSRSECDTSVTLGPRTFK-----LPVVPANMQTIIDEKIAEWLAENgyfyimhrfdpearipfik 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545688070 71 ------LAAS--SGTGSSDFEQLEQILEAIPQVKYICLDVANGYSEHFVEFVKDVRKRFPQHTIMAGNVVTGEMVEELIL 142
Cdd:PRK05458 80 dmheqgLIASisVGVKDDEYDFVDQLAAEGLTPEYITIDIAHGHSDSVINMIQHIKKHLPETFVIAGNVGTPEAVRELEN 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545688070 143 SGADIIKVGIGPGSVCTTRKKTGVGYP--QLSAVMECADAAhglKGHIISDGGCSCPGDVAKAFGAGADFVMLGGMLAGH 220
Cdd:PRK05458 160 AGADATKVGIGPGKVCITKIKTGFGTGgwQLAALRWCAKAA---RKPIIADGGIRTHGDIAKSIRFGATMVMIGSLFAGH 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545688070 221 SESGGELIERDGKKYKLFYGMSSEmamkkYAGGvaEYRASEGKTVEVPFKGDVEHTIRDILGGIRSTCTYVGAAKLKELs 300
Cdd:PRK05458 237 EESPGKTVEIDGKLYKEYFGSASE-----FQKG--EYKNVEGKKILVPHKGSLKDTLTEMEQDLQSSISYAGGRDLDAI- 308
|
330
....*....|....*...
gi 545688070 301 RRTTFIRVTqqvNPIFSE 318
Cdd:PRK05458 309 RKVDYVIVK---NSIFNG 323
|
|
| PTZ00314 |
PTZ00314 |
inosine-5'-monophosphate dehydrogenase; Provisional |
69-311 |
2.72e-60 |
|
inosine-5'-monophosphate dehydrogenase; Provisional
Pssm-ID: 240355 [Multi-domain] Cd Length: 495 Bit Score: 200.20 E-value: 2.72e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545688070 69 KHL--AASSGTGSSDFEQLEQILEAipQVKYICLDVANGYSEHFVEFVKDVRKRFPQHTIMAGNVVTGEMVEELILSGAD 146
Cdd:PTZ00314 228 GQLlvGAAISTRPEDIERAAALIEA--GVDVLVVDSSQGNSIYQIDMIKKLKSNYPHVDIIAGNVVTADQAKNLIDAGAD 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545688070 147 IIKVGIGPGSVCTTRKKTGVGYPQLSAVMECADAAHGLKGHIISDGGCSCPGDVAKAFGAGADFVMLGGMLAGHSESGGE 226
Cdd:PTZ00314 306 GLRIGMGSGSICITQEVCAVGRPQASAVYHVARYARERGVPCIADGGIKNSGDICKALALGADCVMLGSLLAGTEEAPGE 385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545688070 227 LIERDGKKYKLFYGMSSEMAM------KKYAGGVAEYRASEGKTVEVPFKGDVEHTIRDILGGIRSTCTYVGAAKLKEL- 299
Cdd:PTZ00314 386 YFFKDGVRLKVYRGMGSLEAMlskesgERYLDENETIKVAQGVSGSVVDKGSVAKLIPYLVKGVKHGMQYIGAHSIPELh 465
|
250
....*....|....*.
gi 545688070 300 ----SRRTTFIRVTQQ 311
Cdd:PTZ00314 466 eklySGQVRFERRSGS 481
|
|
| PRK07807 |
PRK07807 |
GuaB1 family IMP dehydrogenase-related protein; |
86-302 |
3.82e-58 |
|
GuaB1 family IMP dehydrogenase-related protein;
Pssm-ID: 181127 [Multi-domain] Cd Length: 479 Bit Score: 194.35 E-value: 3.82e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545688070 86 EQILEAipQVKYICLDVANGYSEHFVEFVKDVRKRFPQHTIMAGNVVTGEMVEELILSGADIIKVGIGPGSVCTTRKKTG 165
Cdd:PRK07807 233 RALLEA--GVDVLVVDTAHGHQEKMLEALRAVRALDPGVPIVAGNVVTAEGTRDLVEAGADIVKVGVGPGAMCTTRMMTG 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545688070 166 VGYPQLSAVMECADAAHGLKGHIISDGGCSCPGDVAKAFGAGADFVMLGGMLAGHSESGGEL-IERDGKKYKLFYGMSSE 244
Cdd:PRK07807 311 VGRPQFSAVLECAAAARELGAHVWADGGVRHPRDVALALAAGASNVMIGSWFAGTYESPGDLmRDRDGRPYKESFGMASA 390
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 545688070 245 MAMKKYAGGVAEY-RA---------SEGKTVEVPFKGDVEHTIRDILGGIRSTCTYVGAAKLKELSRR 302
Cdd:PRK07807 391 RAVAARTAGDSAFdRArkalfeegiSTSRMYLDPGRPGVEDLLDHITSGVRSSCTYAGARTLAEFHER 458
|
|
| IMP_DH_rel_1 |
TIGR01303 |
IMP dehydrogenase family protein; This model represents a family of proteins, often annotated ... |
86-304 |
2.69e-54 |
|
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: 183.96 E-value: 2.69e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545688070 86 EQILEAipQVKYICLDVANGYSEHFVEFVKDVRKRFPQHTIMAGNVVTGEMVEELILSGADIIKVGIGPGSVCTTRKKTG 165
Cdd:TIGR01303 231 KALLDA--GVDVLVIDTAHGHQVKMISAIKAVRALDLGVPIVAGNVVSAEGVRDLLEAGANIIKVGVGPGAMCTTRMMTG 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545688070 166 VGYPQLSAVMECADAAHGLKGHIISDGGCSCPGDVAKAFGAGADFVMLGGMLAGHSESGGELI-ERDGKKYKLFYGMSSE 244
Cdd:TIGR01303 309 VGRPQFSAVLECAAEARKLGGHVWADGGVRHPRDVALALAAGASNVMVGSWFAGTYESPGDLMrDRDGRPYKESFGMASK 388
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545688070 245 MAMKKYAGGVAEY-RA---------SEGKTVEVPFKGDVEHTIRDILGGIRSTCTYVGAAKLKELSRRTT 304
Cdd:TIGR01303 389 RAVVARTGADNAFdRArkalfeegiSTSRMGLDPDRGGVEDLIDHIISGVRSSCTYAGASSLEEFHERAV 458
|
|
| PRK06843 |
PRK06843 |
inosine 5-monophosphate dehydrogenase; Validated |
68-310 |
2.09e-52 |
|
inosine 5-monophosphate dehydrogenase; Validated
Pssm-ID: 180725 [Multi-domain] Cd Length: 404 Bit Score: 177.54 E-value: 2.09e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545688070 68 CKHLAASSGTGSS---DFEQLEQILEAI-PQVKYICLDVANGYSEHFVEFVKDVRKRFPQHTIMAGNVVTGEMVEELILS 143
Cdd:PRK06843 135 CKDLNNKLRVGAAvsiDIDTIERVEELVkAHVDILVIDSAHGHSTRIIELVKKIKTKYPNLDLIAGNIVTKEAALDLISV 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545688070 144 GADIIKVGIGPGSVCTTRKKTGVGYPQLSAVMECADAAHGLKGHIISDGGCSCPGDVAKAFGAGADFVMLGGMLAGHSES 223
Cdd:PRK06843 215 GADCLKVGIGPGSICTTRIVAGVGVPQITAICDVYEVCKNTNICIIADGGIRFSGDVVKAIAAGADSVMIGNLFAGTKES 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545688070 224 GGELIERDGKKYKLFYGMSSEMAMKKyaGGVAEY----------RASEGKTVEVPFKGDVEHTIRDILGGIRSTCTYVGA 293
Cdd:PRK06843 295 PSEEIIYNGKKFKSYVGMGSISAMKR--GSKSRYfqlennepkkLVPEGIEGMVPYSGKLKDILTQLKGGLMSGMGYLGA 372
|
250
....*....|....*..
gi 545688070 294 AKLKELSRRTTFIRVTQ 310
Cdd:PRK06843 373 ATISDLKINSKFVKISH 389
|
|
| PLN02274 |
PLN02274 |
inosine-5'-monophosphate dehydrogenase |
14-298 |
1.04e-36 |
|
inosine-5'-monophosphate dehydrogenase
Pssm-ID: 215154 [Multi-domain] Cd Length: 505 Bit Score: 137.49 E-value: 1.04e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545688070 14 DVLLRPKRSTLKSRSEVDLTRSFSFRNSKQTYSGVPiiAANMDTVGtfEMAKVLCkhlAASSGTGSSDFEQLEQILEAip 93
Cdd:PLN02274 189 AVLKDSKKGKLPLVNEDGELVDLVTRTDVKRVKGYP--KLGKPSVG--KDGKLLV---GAAIGTRESDKERLEHLVKA-- 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545688070 94 QVKYICLDVANGYSEHFVEFVKDVRKRFPQHTIMAGNVVTGEMVEELILSGADIIKVGIGPGSVCTTRKKTGVGYPQLSA 173
Cdd:PLN02274 260 GVDVVVLDSSQGDSIYQLEMIKYIKKTYPELDVIGGNVVTMYQAQNLIQAGVDGLRVGMGSGSICTTQEVCAVGRGQATA 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545688070 174 VMECADAAHGLKGHIISDGGCSCPGDVAKAFGAGADFVMLGGMLAGHSESGGELIERDGKKYKLFYGMSSEMAMKK---- 249
Cdd:PLN02274 340 VYKVASIAAQHGVPVIADGGISNSGHIVKALTLGASTVMMGSFLAGTTEAPGEYFYQDGVRVKKYRGMGSLEAMTKgsdq 419
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 545688070 250 -YAGGVAEYRASEGKTVEVPFKGDVEHTIRDILGGIRSTCTYVGAAKLKE 298
Cdd:PLN02274 420 rYLGDTAKLKIAQGVSGAVADKGSVLKFVPYTMQAVKQGFQDLGASSLQS 469
|
|
| PRK07107 |
PRK07107 |
IMP dehydrogenase; |
69-309 |
7.41e-28 |
|
IMP dehydrogenase;
Pssm-ID: 180842 [Multi-domain] Cd Length: 502 Bit Score: 112.87 E-value: 7.41e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545688070 69 KHLAASSGTGSSDF-EQLEQILEAipQVKYICLDVANGYSEHFVEFVKDVRKRFPQHT-IMAGNVVTGEMVEELILSGAD 146
Cdd:PRK07107 230 KRYVVGAGINTRDYaERVPALVEA--GADVLCIDSSEGYSEWQKRTLDWIREKYGDSVkVGAGNVVDREGFRYLAEAGAD 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545688070 147 IIKVGIGPGSVCTTRKKTGVGYPQLSAVMECADA------AHGLKGHIISDGGCSCPGDVAKAFGAGADFVMLGGMLAGH 220
Cdd:PRK07107 308 FVKVGIGGGSICITREQKGIGRGQATALIEVAKArdeyfeETGVYIPICSDGGIVYDYHMTLALAMGADFIMLGRYFARF 387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545688070 221 SESGGELIERDGKKYKLFYGMSSEMAM--KKY-AGGVAEYRASEGKTVEVPFKGDVEHTIRDILGGIRSTCTYVGAAKLK 297
Cdd:PRK07107 388 DESPTNKVNINGNYMKEYWGEGSNRARnwQRYdLGGDKKLSFEEGVDSYVPYAGSLKDNVAITLSKVRSTMCNCGALSIP 467
|
250
....*....|..
gi 545688070 298 ELSRRTTFIRVT 309
Cdd:PRK07107 468 ELQQKAKITLVS 479
|
|
| TIM_phosphate_binding |
cd04722 |
TIM barrel proteins share a structurally conserved phosphate binding motif and in general ... |
94-215 |
7.48e-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: 7.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545688070 94 QVKYICLDVANGYS-EHFVEFVKDVRKRFPQHTIMAGNVVTGEMVEE-LILSGADIIKVGIGPGsvcTTRKKTGVGYPQL 171
Cdd:cd04722 84 GADGVEIHGAVGYLaREDLELIRELREAVPDVKVVVKLSPTGELAAAaAEEAGVDEVGLGNGGG---GGGGRDAVPIADL 160
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 545688070 172 SAvmECADAAHGLKghIISDGGCSCPGDVAKAFGAGADFVMLGG 215
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 ... |
112-213 |
1.76e-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: 41.73 E-value: 1.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545688070 112 EFVKDVRKRFPQHTIMAGNVVTGEMVEELILSGADIIkvgIGPGSVcttrkktgvgyPQLsavmecADAAHGLKGHIIsd 191
Cdd:cd00452 44 EAIRALRKEFPEALIGAGTVLTPEQADAAIAAGAQFI---VSPGLD-----------PEV------VKAANRAGIPLL-- 101
|
90 100
....*....|....*....|..
gi 545688070 192 GGCSCPGDVAKAFGAGADFVML 213
Cdd:cd00452 102 PGVATPTEIMQALELGADIVKL 123
|
|
| Glu_synthase |
pfam01645 |
Conserved region in glutamate synthase; This family represents a region of the glutamate ... |
106-214 |
9.97e-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: 37.31 E-value: 9.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545688070 106 YS-EHFVEFVKDVRKRFPQHTIMAGnvVTGEMVEELILSG-----ADIIKV-GIGPG---SVCTTRKKTGVgyPQLSAVM 175
Cdd:pfam01645 184 YSiEDLAQLIYDLKEINPKAPISVK--LVSGHGVGTIAAGvakagADIILIdGYDGGtgaSPKTSIKHAGL--PWELALA 259
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 545688070 176 EcADAAHGLKGH-----IISDGGCSCPGDVAKAFGAGADFVMLG 214
Cdd:pfam01645 260 E-AHQTLKENGLrdrvsLIADGGLRTGADVAKAAALGADAVYIG 302
|
|
| |
