|
Name |
Accession |
Description |
Interval |
E-value |
| PRK05096 |
PRK05096 |
guanosine 5'-monophosphate oxidoreductase; Provisional |
3-286 |
0e+00 |
|
guanosine 5'-monophosphate oxidoreductase; Provisional
Pssm-ID: 235343 [Multi-domain] Cd Length: 346 Bit Score: 566.11 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556758 3 HIDNDVKLDFKDVLLRPKRSTLKSRSEVDLTRSFSFRNSKQMYSGIPIIAANMDTVGTFEMAKVLCKFSLFTAIHKHYSI 82
Cdd:PRK05096 2 RIEEDLKLGFKDVLIRPKRSTLKSRSDVELERQFTFKHSGQSWSGVPIIAANMDTVGTFEMAKALASFDILTAVHKHYSV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556758 83 HQWQEF-ANQNPDCLEYLAASSGTGSADFEQLEQILEAIPQVKYICLDVANGYSEHFVESVKDVRKRFPQHTIMAGNVVT 161
Cdd:PRK05096 82 EEWAAFvNNSSADVLKHVMVSTGTSDADFEKTKQILALSPALNFICIDVANGYSEHFVQFVAKAREAWPDKTICAGNVVT 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556758 162 GEMVEELILSGADIIKVGIGPGSVCTTRKKTGVGYPQLSAVMECADAAHGLKGHIISDGGCSCPGDVAKAFGAGADFVML 241
Cdd:PRK05096 162 GEMVEELILSGADIVKVGIGPGSVCTTRVKTGVGYPQLSAVIECADAAHGLGGQIVSDGGCTVPGDVAKAFGGGADFVML 241
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 61556758 242 GGMLAGHSESGGELIERNGKKYKLFYGMSSEMAMKKYSGGVAEYR 286
Cdd:PRK05096 242 GGMLAGHEESGGEIVEENGEKFMLFYGMSSESAMKRHVGGVAEYR 286
|
|
| GMP_reduct_1 |
TIGR01305 |
guanosine monophosphate reductase, eukaryotic; A deep split separates two families of GMP ... |
4-286 |
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: 527.18 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556758 4 IDNDVKLDFKDVLLRPKRSTLKSRSEVDLTRSFSFRNSKQMYSGIPIIAANMDTVGTFEMAKVLCKFSLFTAIHKHYSIH 83
Cdd:TIGR01305 2 IEADLKLDFKDVLLRPKRSTLKSRADVELERTFTFRNSKQTYSGVPIIAANMDTVGTFEMAAALSQHSIFTAIHKHYSVD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556758 84 QWQEFA-NQNPDCLEYLAASSGTGSADFEQLEQILEAIPQVKYICLDVANGYSEHFVESVKDVRKRFPQHTIMAGNVVTG 162
Cdd:TIGR01305 82 EWKAFAtNSSPDCLQNVAVSSGSSDNDLEKMTSILEAVPQLKFICLDVANGYSEHFVEFVKLVREAFPEHTIMAGNVVTG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556758 163 EMVEELILSGADIIKVGIGPGSVCTTRKKTGVGYPQLSAVMECADAAHGLKGHIISDGGCSCPGDVAKAFGAGADFVMLG 242
Cdd:TIGR01305 162 EMVEELILSGADIVKVGIGPGSVCTTRTKTGVGYPQLSAVIECADAAHGLKGHIISDGGCTCPGDVAKAFGAGADFVMLG 241
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 61556758 243 GMLAGHSESGGELIERNGKKYKLFYGMSSEMAMKKYSGGVAEYR 286
Cdd:TIGR01305 242 GMFAGHTESGGEVIERNGRKFKLFYGMSSDTAMKKHAGGVAEYR 285
|
|
| IMPDH |
cd00381 |
IMPDH: The catalytic domain of the inosine monophosphate dehydrogenase. IMPDH catalyzes the ... |
10-280 |
3.04e-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: 336.80 E-value: 3.04e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556758 10 LDFKDVLLRPKRSTLkSRSEVDLTRSFSfrnsKQMYSGIPIIAANMDTVGTFEMAKVLCKFSLFTAIHKHYSIHQWQEFA 89
Cdd:cd00381 2 LTFDDVLLVPGYSTV-LPSEVDLSTKLT----KNITLNIPLVSAPMDTVTESEMAIAMARLGGIGVIHRNMSIEEQAEEV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556758 90 NQNPDCLeYLAASSGTGSADFEQLEQILEAIpqVKYICLDVANGYSEHFVESVKDVRKRFPQHTIMAGNVVTGEMVEELI 169
Cdd:cd00381 77 RKVKGRL-LVGAAVGTREDDKERAEALVEAG--VDVIVIDSAHGHSVYVIEMIKFIKKKYPNVDVIAGNVVTAEAARDLI 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556758 170 LSGADIIKVGIGPGSVCTTRKKTGVGYPQLSAVMECADAAHGLKGHIISDGGCSCPGDVAKAFGAGADFVMLGGMLAGHS 249
Cdd:cd00381 154 DAGADGVKVGIGPGSICTTRIVTGVGVPQATAVADVAAAARDYGVPVIADGGIRTSGDIVKALAAGADAVMLGSLLAGTD 233
|
250 260 270
....*....|....*....|....*....|.
gi 61556758 250 ESGGELIERNGKKYKLFYGMSSEMAMKKYSG 280
Cdd:cd00381 234 ESPGEYIEINGKRYKEYRGMGSLGAMKKGGG 264
|
|
| GuaB |
COG0516 |
IMP dehydrogenase/GMP reductase [Nucleotide transport and metabolism]; IMP dehydrogenase/GMP ... |
15-286 |
3.41e-73 |
|
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: 227.40 E-value: 3.41e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556758 15 VLLRPKRSTLKSRSEVDLTRSFSFRNSKQMYSGIPIIAANMDTVGTFEMAKVLCKFSLFTAIHKHYSIHQWQ-EFANQNP 93
Cdd:COG0516 1 LVLDALRRRLISRSGVVVVVVVGKLTIITTRRRRRDEAVKALVVTTVIEKLLLVTVAGETALLALALLLLKKkKFLLLVD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556758 94 DCLEYLAASSGTGSADFEQLEQILEAIPQVKYICLDVANGYSEHfvESVKDVRKRFPQHTIMAGNVVTGEMVEELILSGA 173
Cdd:COG0516 81 DDGLLLLVLVGVKDDDKEKARALAAADAGVDVLVIDAAHGHSGG--DAMKKIKLTFDDVLLIPGNSATVEPARALVDAGA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556758 174 DIIKVGIGPGSVCTTRKKTGVGYPQLSAVMECADAAHGLKgHIISDGGCSCPGDVAKAFGAGADFVMLGGMLAGHSESGG 253
Cdd:COG0516 159 DLTKVGIGPGSICTTRVVIGLGIPQLSAAMDTVTEARMAI-AIAADGGIGYIHDNAKALAAGADAVMLGSLFAGTEEQPG 237
|
250 260 270
....*....|....*....|....*....|....*
gi 61556758 254 ELIERNGKKYKLFYGMSSEMAMKKYSG--GVAEYR 286
Cdd:COG0516 238 EVILYQGRSVKRYRGMGSDAKKLVPEGieGRVPYK 272
|
|
| IMPDH |
pfam00478 |
IMP dehydrogenase / GMP reductase domain; This family is involved in biosynthesis of guanosine ... |
100-279 |
3.69e-68 |
|
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: 218.41 E-value: 3.69e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556758 100 AASSGTGSADFEQLEQILEAipQVKYICLDVANGYSEHFVESVKDVRKRFPQHTIMAGNVVTGEMVEELILSGADIIKVG 179
Cdd:pfam00478 212 GAAVGVGDDTLERAEALVEA--GVDVLVVDTAHGHSKGVIDTVKWIKKKYPDVQVIAGNVATAEGAKALIEAGADAVKVG 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556758 180 IGPGSVCTTRKKTGVGYPQLSAVMECADAAHGLKGHIISDGGCSCPGDVAKAFGAGADFVMLGGMLAGHSESGGELIERN 259
Cdd:pfam00478 290 IGPGSICTTRVVAGVGVPQLTAIYDVAEAAKKYGVPVIADGGIKYSGDIVKALAAGADAVMLGSLLAGTDESPGEVILYQ 369
|
170 180
....*....|....*....|
gi 61556758 260 GKKYKLFYGMSSEMAMKKYS 279
Cdd:pfam00478 370 GRRYKSYRGMGSLGAMKKGS 389
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK05096 |
PRK05096 |
guanosine 5'-monophosphate oxidoreductase; Provisional |
3-286 |
0e+00 |
|
guanosine 5'-monophosphate oxidoreductase; Provisional
Pssm-ID: 235343 [Multi-domain] Cd Length: 346 Bit Score: 566.11 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556758 3 HIDNDVKLDFKDVLLRPKRSTLKSRSEVDLTRSFSFRNSKQMYSGIPIIAANMDTVGTFEMAKVLCKFSLFTAIHKHYSI 82
Cdd:PRK05096 2 RIEEDLKLGFKDVLIRPKRSTLKSRSDVELERQFTFKHSGQSWSGVPIIAANMDTVGTFEMAKALASFDILTAVHKHYSV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556758 83 HQWQEF-ANQNPDCLEYLAASSGTGSADFEQLEQILEAIPQVKYICLDVANGYSEHFVESVKDVRKRFPQHTIMAGNVVT 161
Cdd:PRK05096 82 EEWAAFvNNSSADVLKHVMVSTGTSDADFEKTKQILALSPALNFICIDVANGYSEHFVQFVAKAREAWPDKTICAGNVVT 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556758 162 GEMVEELILSGADIIKVGIGPGSVCTTRKKTGVGYPQLSAVMECADAAHGLKGHIISDGGCSCPGDVAKAFGAGADFVML 241
Cdd:PRK05096 162 GEMVEELILSGADIVKVGIGPGSVCTTRVKTGVGYPQLSAVIECADAAHGLGGQIVSDGGCTVPGDVAKAFGGGADFVML 241
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 61556758 242 GGMLAGHSESGGELIERNGKKYKLFYGMSSEMAMKKYSGGVAEYR 286
Cdd:PRK05096 242 GGMLAGHEESGGEIVEENGEKFMLFYGMSSESAMKRHVGGVAEYR 286
|
|
| GMP_reduct_1 |
TIGR01305 |
guanosine monophosphate reductase, eukaryotic; A deep split separates two families of GMP ... |
4-286 |
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: 527.18 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556758 4 IDNDVKLDFKDVLLRPKRSTLKSRSEVDLTRSFSFRNSKQMYSGIPIIAANMDTVGTFEMAKVLCKFSLFTAIHKHYSIH 83
Cdd:TIGR01305 2 IEADLKLDFKDVLLRPKRSTLKSRADVELERTFTFRNSKQTYSGVPIIAANMDTVGTFEMAAALSQHSIFTAIHKHYSVD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556758 84 QWQEFA-NQNPDCLEYLAASSGTGSADFEQLEQILEAIPQVKYICLDVANGYSEHFVESVKDVRKRFPQHTIMAGNVVTG 162
Cdd:TIGR01305 82 EWKAFAtNSSPDCLQNVAVSSGSSDNDLEKMTSILEAVPQLKFICLDVANGYSEHFVEFVKLVREAFPEHTIMAGNVVTG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556758 163 EMVEELILSGADIIKVGIGPGSVCTTRKKTGVGYPQLSAVMECADAAHGLKGHIISDGGCSCPGDVAKAFGAGADFVMLG 242
Cdd:TIGR01305 162 EMVEELILSGADIVKVGIGPGSVCTTRTKTGVGYPQLSAVIECADAAHGLKGHIISDGGCTCPGDVAKAFGAGADFVMLG 241
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 61556758 243 GMLAGHSESGGELIERNGKKYKLFYGMSSEMAMKKYSGGVAEYR 286
Cdd:TIGR01305 242 GMFAGHTESGGEVIERNGRKFKLFYGMSSDTAMKKHAGGVAEYR 285
|
|
| IMPDH |
cd00381 |
IMPDH: The catalytic domain of the inosine monophosphate dehydrogenase. IMPDH catalyzes the ... |
10-280 |
3.04e-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: 336.80 E-value: 3.04e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556758 10 LDFKDVLLRPKRSTLkSRSEVDLTRSFSfrnsKQMYSGIPIIAANMDTVGTFEMAKVLCKFSLFTAIHKHYSIHQWQEFA 89
Cdd:cd00381 2 LTFDDVLLVPGYSTV-LPSEVDLSTKLT----KNITLNIPLVSAPMDTVTESEMAIAMARLGGIGVIHRNMSIEEQAEEV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556758 90 NQNPDCLeYLAASSGTGSADFEQLEQILEAIpqVKYICLDVANGYSEHFVESVKDVRKRFPQHTIMAGNVVTGEMVEELI 169
Cdd:cd00381 77 RKVKGRL-LVGAAVGTREDDKERAEALVEAG--VDVIVIDSAHGHSVYVIEMIKFIKKKYPNVDVIAGNVVTAEAARDLI 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556758 170 LSGADIIKVGIGPGSVCTTRKKTGVGYPQLSAVMECADAAHGLKGHIISDGGCSCPGDVAKAFGAGADFVMLGGMLAGHS 249
Cdd:cd00381 154 DAGADGVKVGIGPGSICTTRIVTGVGVPQATAVADVAAAARDYGVPVIADGGIRTSGDIVKALAAGADAVMLGSLLAGTD 233
|
250 260 270
....*....|....*....|....*....|.
gi 61556758 250 ESGGELIERNGKKYKLFYGMSSEMAMKKYSG 280
Cdd:cd00381 234 ESPGEYIEINGKRYKEYRGMGSLGAMKKGGG 264
|
|
| GuaB |
COG0516 |
IMP dehydrogenase/GMP reductase [Nucleotide transport and metabolism]; IMP dehydrogenase/GMP ... |
15-286 |
3.41e-73 |
|
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: 227.40 E-value: 3.41e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556758 15 VLLRPKRSTLKSRSEVDLTRSFSFRNSKQMYSGIPIIAANMDTVGTFEMAKVLCKFSLFTAIHKHYSIHQWQ-EFANQNP 93
Cdd:COG0516 1 LVLDALRRRLISRSGVVVVVVVGKLTIITTRRRRRDEAVKALVVTTVIEKLLLVTVAGETALLALALLLLKKkKFLLLVD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556758 94 DCLEYLAASSGTGSADFEQLEQILEAIPQVKYICLDVANGYSEHfvESVKDVRKRFPQHTIMAGNVVTGEMVEELILSGA 173
Cdd:COG0516 81 DDGLLLLVLVGVKDDDKEKARALAAADAGVDVLVIDAAHGHSGG--DAMKKIKLTFDDVLLIPGNSATVEPARALVDAGA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556758 174 DIIKVGIGPGSVCTTRKKTGVGYPQLSAVMECADAAHGLKgHIISDGGCSCPGDVAKAFGAGADFVMLGGMLAGHSESGG 253
Cdd:COG0516 159 DLTKVGIGPGSICTTRVVIGLGIPQLSAAMDTVTEARMAI-AIAADGGIGYIHDNAKALAAGADAVMLGSLFAGTEEQPG 237
|
250 260 270
....*....|....*....|....*....|....*
gi 61556758 254 ELIERNGKKYKLFYGMSSEMAMKKYSG--GVAEYR 286
Cdd:COG0516 238 EVILYQGRSVKRYRGMGSDAKKLVPEGieGRVPYK 272
|
|
| IMPDH |
pfam00478 |
IMP dehydrogenase / GMP reductase domain; This family is involved in biosynthesis of guanosine ... |
100-279 |
3.69e-68 |
|
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: 218.41 E-value: 3.69e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556758 100 AASSGTGSADFEQLEQILEAipQVKYICLDVANGYSEHFVESVKDVRKRFPQHTIMAGNVVTGEMVEELILSGADIIKVG 179
Cdd:pfam00478 212 GAAVGVGDDTLERAEALVEA--GVDVLVVDTAHGHSKGVIDTVKWIKKKYPDVQVIAGNVATAEGAKALIEAGADAVKVG 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556758 180 IGPGSVCTTRKKTGVGYPQLSAVMECADAAHGLKGHIISDGGCSCPGDVAKAFGAGADFVMLGGMLAGHSESGGELIERN 259
Cdd:pfam00478 290 IGPGSICTTRVVAGVGVPQLTAIYDVAEAAKKYGVPVIADGGIKYSGDIVKALAAGADAVMLGSLLAGTDESPGEVILYQ 369
|
170 180
....*....|....*....|
gi 61556758 260 GKKYKLFYGMSSEMAMKKYS 279
Cdd:pfam00478 370 GRRYKSYRGMGSLGAMKKGS 389
|
|
| IMP_dehydrog |
TIGR01302 |
inosine-5'-monophosphate dehydrogenase; This model describes IMP dehydrogenase, an enzyme of ... |
82-281 |
3.21e-59 |
|
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: 194.87 E-value: 3.21e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556758 82 IHQWQEFANQNPDCLEYL--AASSGTGSADFEQLEQILEAipQVKYICLDVANGYSEHFVESVKDVRKRFPQHTIMAGNV 159
Cdd:TIGR01302 196 IVKRRKFPHASKDENGRLivGAAVGTREFDKERAEALVKA--GVDVIVIDSSHGHSIYVIDSIKEIKKTYPDLDIIAGNV 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556758 160 VTGEMVEELILSGADIIKVGIGPGSVCTTRKKTGVGYPQLSAVMECADAAHGLKGHIISDGGCSCPGDVAKAFGAGADFV 239
Cdd:TIGR01302 274 ATAEQAKALIDAGADGLRVGIGPGSICTTRIVAGVGVPQITAVYDVAEYAAQSGIPVIADGGIRYSGDIVKALAAGADAV 353
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 61556758 240 MLGGMLAGHSESGGELIERNGKKYKLFYGMSSEMAMKKYSGG 281
Cdd:TIGR01302 354 MLGSLLAGTTESPGEYEIINGRRYKQYRGMGSLGAMTKGSSD 395
|
|
| PRK05458 |
PRK05458 |
guanosine 5'-monophosphate oxidoreductase; Provisional |
10-272 |
4.74e-57 |
|
guanosine 5'-monophosphate oxidoreductase; Provisional
Pssm-ID: 235479 [Multi-domain] Cd Length: 326 Bit Score: 185.93 E-value: 4.74e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556758 10 LDFKDVLLRPKRSTLKSRSEVDLTRSFSFRNSKqmysgIPIIAANMDTVGTFEMAKVLCKFSLFtaihkhYSIHQWQE-- 87
Cdd:PRK05458 5 FDYEDIQLIPNKCIVNSRSECDTSVTLGPRTFK-----LPVVPANMQTIIDEKIAEWLAENGYF------YIMHRFDPea 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556758 88 ---FANQNPDCLEYLAASSGTGSADFEQLEQILEAIPQVKYICLDVANGYSEHFVESVKDVRKRFPQHTIMAGNVVTGEM 164
Cdd:PRK05458 74 ripFIKDMHEQGLIASISVGVKDDEYDFVDQLAAEGLTPEYITIDIAHGHSDSVINMIQHIKKHLPETFVIAGNVGTPEA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556758 165 VEELILSGADIIKVGIGPGSVCTTRKKTGVGYP--QLSAVMECADAAhglKGHIISDGGCSCPGDVAKAFGAGADFVMLG 242
Cdd:PRK05458 154 VRELENAGADATKVGIGPGKVCITKIKTGFGTGgwQLAALRWCAKAA---RKPIIADGGIRTHGDIAKSIRFGATMVMIG 230
|
250 260 270
....*....|....*....|....*....|
gi 61556758 243 GMLAGHSESGGELIERNGKKYKLFYGMSSE 272
Cdd:PRK05458 231 SLFAGHEESPGKTVEIDGKLYKEYFGSASE 260
|
|
| PRK06843 |
PRK06843 |
inosine 5-monophosphate dehydrogenase; Validated |
10-279 |
1.09e-51 |
|
inosine 5-monophosphate dehydrogenase; Validated
Pssm-ID: 180725 [Multi-domain] Cd Length: 404 Bit Score: 174.46 E-value: 1.09e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556758 10 LDFKDVLLRPKRSTLKSrSEVDLTRSFSfrnsKQMYSGIPIIAANMDTVGTFEMAKVLCKFSLFTAIHKHYSI------- 82
Cdd:PRK06843 10 LTFDDVSLIPRKSSVLP-SEVSLKTQLT----KNISLNIPFLSSAMDTVTESQMAIAIAKEGGIGIIHKNMSIeaqrkei 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556758 83 -----HQWQEFANQNPDCLE----------YLAASSGTGSA----DF------------------------EQLEQILEA 119
Cdd:PRK06843 85 ekvktYKFQKTINTNGDTNEqkpeiftakqHLEKSDAYKNAehkeDFpnackdlnnklrvgaavsididtiERVEELVKA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556758 120 ipQVKYICLDVANGYSEHFVESVKDVRKRFPQHTIMAGNVVTGEMVEELILSGADIIKVGIGPGSVCTTRKKTGVGYPQL 199
Cdd:PRK06843 165 --HVDILVIDSAHGHSTRIIELVKKIKTKYPNLDLIAGNIVTKEAALDLISVGADCLKVGIGPGSICTTRIVAGVGVPQI 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556758 200 SAVMECADAAHGLKGHIISDGGCSCPGDVAKAFGAGADFVMLGGMLAGHSESGGELIERNGKKYKLFYGMSSEMAMKKYS 279
Cdd:PRK06843 243 TAICDVYEVCKNTNICIIADGGIRFSGDVVKAIAAGADSVMIGNLFAGTKESPSEEIIYNGKKFKSYVGMGSISAMKRGS 322
|
|
| PTZ00314 |
PTZ00314 |
inosine-5'-monophosphate dehydrogenase; Provisional |
98-277 |
1.45e-50 |
|
inosine-5'-monophosphate dehydrogenase; Provisional
Pssm-ID: 240355 [Multi-domain] Cd Length: 495 Bit Score: 173.23 E-value: 1.45e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556758 98 YLAASSGTGSADFEQLEQILEAipQVKYICLDVANGYSEHFVESVKDVRKRFPQHTIMAGNVVTGEMVEELILSGADIIK 177
Cdd:PTZ00314 231 LVGAAISTRPEDIERAAALIEA--GVDVLVVDSSQGNSIYQIDMIKKLKSNYPHVDIIAGNVVTADQAKNLIDAGADGLR 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556758 178 VGIGPGSVCTTRKKTGVGYPQLSAVMECADAAHGLKGHIISDGGCSCPGDVAKAFGAGADFVMLGGMLAGHSESGGELIE 257
Cdd:PTZ00314 309 IGMGSGSICITQEVCAVGRPQASAVYHVARYARERGVPCIADGGIKNSGDICKALALGADCVMLGSLLAGTEEAPGEYFF 388
|
170 180
....*....|....*....|
gi 61556758 258 RNGKKYKLFYGMSSEMAMKK 277
Cdd:PTZ00314 389 KDGVRLKVYRGMGSLEAMLS 408
|
|
| PRK07807 |
PRK07807 |
GuaB1 family IMP dehydrogenase-related protein; |
114-276 |
6.65e-50 |
|
GuaB1 family IMP dehydrogenase-related protein;
Pssm-ID: 181127 [Multi-domain] Cd Length: 479 Bit Score: 171.24 E-value: 6.65e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556758 114 EQILEAipQVKYICLDVANGYSEHFVESVKDVRKRFPQHTIMAGNVVTGEMVEELILSGADIIKVGIGPGSVCTTRKKTG 193
Cdd:PRK07807 233 RALLEA--GVDVLVVDTAHGHQEKMLEALRAVRALDPGVPIVAGNVVTAEGTRDLVEAGADIVKVGVGPGAMCTTRMMTG 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556758 194 VGYPQLSAVMECADAAHGLKGHIISDGGCSCPGDVAKAFGAGADFVMLGGMLAGHSESGGEL-IERNGKKYKLFYGMSSE 272
Cdd:PRK07807 311 VGRPQFSAVLECAAAARELGAHVWADGGVRHPRDVALALAAGASNVMIGSWFAGTYESPGDLmRDRDGRPYKESFGMASA 390
|
....
gi 61556758 273 MAMK 276
Cdd:PRK07807 391 RAVA 394
|
|
| IMP_DH_rel_1 |
TIGR01303 |
IMP dehydrogenase family protein; This model represents a family of proteins, often annotated ... |
114-285 |
4.07e-46 |
|
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: 161.23 E-value: 4.07e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556758 114 EQILEAipQVKYICLDVANGYSEHFVESVKDVRKRFPQHTIMAGNVVTGEMVEELILSGADIIKVGIGPGSVCTTRKKTG 193
Cdd:TIGR01303 231 KALLDA--GVDVLVIDTAHGHQVKMISAIKAVRALDLGVPIVAGNVVSAEGVRDLLEAGANIIKVGVGPGAMCTTRMMTG 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556758 194 VGYPQLSAVMECADAAHGLKGHIISDGGCSCPGDVAKAFGAGADFVMLGGMLAGHSESGGELI-ERNGKKYKLFYGMSSE 272
Cdd:TIGR01303 309 VGRPQFSAVLECAAEARKLGGHVWADGGVRHPRDVALALAAGASNVMVGSWFAGTYESPGDLMrDRDGRPYKESFGMASK 388
|
170
....*....|...
gi 61556758 273 MAMKKYSGGVAEY 285
Cdd:TIGR01303 389 RAVVARTGADNAF 401
|
|
| PLN02274 |
PLN02274 |
inosine-5'-monophosphate dehydrogenase |
100-279 |
1.26e-35 |
|
inosine-5'-monophosphate dehydrogenase
Pssm-ID: 215154 [Multi-domain] Cd Length: 505 Bit Score: 133.64 E-value: 1.26e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556758 100 AASSGTGSADFEQLEQILEAipQVKYICLDVANGYSEHFVESVKDVRKRFPQHTIMAGNVVTGEMVEELILSGADIIKVG 179
Cdd:PLN02274 240 GAAIGTRESDKERLEHLVKA--GVDVVVLDSSQGDSIYQLEMIKYIKKTYPELDVIGGNVVTMYQAQNLIQAGVDGLRVG 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556758 180 IGPGSVCTTRKKTGVGYPQLSAVMECADAAHGLKGHIISDGGCSCPGDVAKAFGAGADFVMLGGMLAGHSESGGELIERN 259
Cdd:PLN02274 318 MGSGSICTTQEVCAVGRGQATAVYKVASIAAQHGVPVIADGGISNSGHIVKALTLGASTVMMGSFLAGTTEAPGEYFYQD 397
|
170 180
....*....|....*....|
gi 61556758 260 GKKYKLFYGMSSEMAMKKYS 279
Cdd:PLN02274 398 GVRVKKYRGMGSLEAMTKGS 417
|
|
| PRK07107 |
PRK07107 |
IMP dehydrogenase; |
78-281 |
1.04e-24 |
|
IMP dehydrogenase;
Pssm-ID: 180842 [Multi-domain] Cd Length: 502 Bit Score: 102.85 E-value: 1.04e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556758 78 KHYSIHQwqefanQNPDCL----EYLAASSGTGSADF-EQLEQILEAipQVKYICLDVANGYSEHFVESVKDVRKRFPQH 152
Cdd:PRK07107 213 KDYDSHK------ENPLELldssKRYVVGAGINTRDYaERVPALVEA--GADVLCIDSSEGYSEWQKRTLDWIREKYGDS 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556758 153 T-IMAGNVVTGEMVEELILSGADIIKVGIGPGSVCTTRKKTGVGYPQLSAVMECADA------AHGLKGHIISDGGCSCP 225
Cdd:PRK07107 285 VkVGAGNVVDREGFRYLAEAGADFVKVGIGGGSICITREQKGIGRGQATALIEVAKArdeyfeETGVYIPICSDGGIVYD 364
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 61556758 226 GDVAKAFGAGADFVMLGGMLAGHSESGGELIERNGKKYKLFYGMSSEMAM--KKYSGG 281
Cdd:PRK07107 365 YHMTLALAMGADFIMLGRYFARFDESPTNKVNINGNYMKEYWGEGSNRARnwQRYDLG 422
|
|
| KDPG_aldolase |
cd00452 |
KDPG and KHG aldolase; KDPG and KHG aldolase. This family belongs to the class I adolases ... |
140-241 |
4.29e-05 |
|
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: 43.28 E-value: 4.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556758 140 ESVKDVRKRFPQHTIMAGNVVTGEMVEELILSGADIIkvgIGPGSVcttrkktgvgyPQLsavmecADAAHGLKGHIIsd 219
Cdd:cd00452 44 EAIRALRKEFPEALIGAGTVLTPEQADAAIAAGAQFI---VSPGLD-----------PEV------VKAANRAGIPLL-- 101
|
90 100
....*....|....*....|..
gi 61556758 220 GGCSCPGDVAKAFGAGADFVML 241
Cdd:cd00452 102 PGVATPTEIMQALELGADIVKL 123
|
|
| TIM_phosphate_binding |
cd04722 |
TIM barrel proteins share a structurally conserved phosphate binding motif and in general ... |
122-243 |
9.98e-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: 42.57 E-value: 9.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556758 122 QVKYICLDVANGYS-EHFVESVKDVRKRFPQHTIMAGNVVTGEMVEE-LILSGADIIKVGIGPGsvcTTRKKTGVGYPQL 199
Cdd:cd04722 84 GADGVEIHGAVGYLaREDLELIRELREAVPDVKVVVKLSPTGELAAAaAEEAGVDEVGLGNGGG---GGGGRDAVPIADL 160
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 61556758 200 SAvmECADAAHGLKghIISDGGCSCPGDVAKAFGAGADFVMLGG 243
Cdd:cd04722 161 LL--ILAKRGSKVP--VIAGGGINDPEDAAEALALGADGVIVGS 200
|
|
| |
