|
Name |
Accession |
Description |
Interval |
E-value |
| PRK05096 |
PRK05096 |
guanosine 5'-monophosphate oxidoreductase; Provisional |
1-346 |
0e+00 |
|
guanosine 5'-monophosphate oxidoreductase; Provisional
Pssm-ID: 235343 [Multi-domain] Cd Length: 346 Bit Score: 778.74 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216606901 1 MRIEEDLKLGFKDVLIRPKRSTLKSRSDVELERQFTFKHSGQTWSGVPIIAANMDTVGTFEMATALAQFDVLTAVHKHYS 80
Cdd:PRK05096 1 MRIEEDLKLGFKDVLIRPKRSTLKSRSDVELERQFTFKHSGQSWSGVPIIAANMDTVGTFEMAKALASFDILTAVHKHYS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216606901 81 TEEWSAFVASASADVVKHVMVSTGTSDADFEKTKQILNANPALNFVCIDVANGYSEHFVQFVSKARDAWPTKTIIAGNVV 160
Cdd:PRK05096 81 VEEWAAFVNNSSADVLKHVMVSTGTSDADFEKTKQILALSPALNFICIDVANGYSEHFVQFVAKAREAWPDKTICAGNVV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216606901 161 TGEMCEELILSGADIVKVGIGPGSVCTTRVKTGVGYPQLSAVIECADAAHGLGGQIISDGGCTMPGDVAKAFGGGADFVM 240
Cdd:PRK05096 161 TGEMVEELILSGADIVKVGIGPGSVCTTRVKTGVGYPQLSAVIECADAAHGLGGQIVSDGGCTVPGDVAKAFGGGADFVM 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216606901 241 LGGMLAGHEESGGTVVEENGEKFMLFYGMSSESAMTRHVGGVAKYRAAEGKTVKLPLRGPVEITARDILGGLRSACTYVG 320
Cdd:PRK05096 241 LGGMLAGHEESGGEIVEENGEKFMLFYGMSSESAMKRHVGGVAEYRAAEGKTVKLPLRGPVENTARDILGGLRSACTYVG 320
|
330 340
....*....|....*....|....*.
gi 2216606901 321 ASRLKELTKRTTFIRVQEQENRVFNS 346
Cdd:PRK05096 321 ASRLKELTKRTTFIRVQEQENRVFNN 346
|
|
| GMP_reduct_1 |
TIGR01305 |
guanosine monophosphate reductase, eukaryotic; A deep split separates two families of GMP ... |
2-344 |
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: 655.84 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216606901 2 RIEEDLKLGFKDVLIRPKRSTLKSRSDVELERQFTFKHSGQTWSGVPIIAANMDTVGTFEMATALAQFDVLTAVHKHYST 81
Cdd:TIGR01305 1 RIEADLKLDFKDVLLRPKRSTLKSRADVELERTFTFRNSKQTYSGVPIIAANMDTVGTFEMAAALSQHSIFTAIHKHYSV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216606901 82 EEWSAFVASASADVVKHVMVSTGTSDADFEKTKQILNANPALNFVCIDVANGYSEHFVQFVSKARDAWPTKTIIAGNVVT 161
Cdd:TIGR01305 81 DEWKAFATNSSPDCLQNVAVSSGSSDNDLEKMTSILEAVPQLKFICLDVANGYSEHFVEFVKLVREAFPEHTIMAGNVVT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216606901 162 GEMCEELILSGADIVKVGIGPGSVCTTRVKTGVGYPQLSAVIECADAAHGLGGQIISDGGCTMPGDVAKAFGGGADFVML 241
Cdd:TIGR01305 161 GEMVEELILSGADIVKVGIGPGSVCTTRTKTGVGYPQLSAVIECADAAHGLKGHIISDGGCTCPGDVAKAFGAGADFVML 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216606901 242 GGMLAGHEESGGTVVEENGEKFMLFYGMSSESAMTRHVGGVAKYRAAEGKTVKLPLRGPVEITARDILGGLRSACTYVGA 321
Cdd:TIGR01305 241 GGMFAGHTESGGEVIERNGRKFKLFYGMSSDTAMKKHAGGVAEYRASEGKTVEVPYRGDVENTILDILGGLRSACTYVGA 320
|
330 340
....*....|....*....|...
gi 2216606901 322 SRLKELTKRTTFIRVQEQENRVF 344
Cdd:TIGR01305 321 AKLKELSKRATFIRVTQQHNTVF 343
|
|
| IMPDH |
cd00381 |
IMPDH: The catalytic domain of the inosine monophosphate dehydrogenase. IMPDH catalyzes the ... |
9-336 |
2.71e-115 |
|
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: 2.71e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216606901 9 LGFKDVLIRPKRSTLkSRSDVELERQFTFKHSGQTwsgvPIIAANMDTVGTFEMATALAQFDVLTAVHKHYSTEEWSAFV 88
Cdd:cd00381 2 LTFDDVLLVPGYSTV-LPSEVDLSTKLTKNITLNI----PLVSAPMDTVTESEMAIAMARLGGIGVIHRNMSIEEQAEEV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216606901 89 AsasaDVVKHVMV--STGTSDADFEKTKQILNANpaLNFVCIDVANGYSEHFVQFVSKARDAWPTKTIIAGNVVTGEMCE 166
Cdd:cd00381 77 R----KVKGRLLVgaAVGTREDDKERAEALVEAG--VDVIVIDSAHGHSVYVIEMIKFIKKKYPNVDVIAGNVVTAEAAR 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216606901 167 ELILSGADIVKVGIGPGSVCTTRVKTGVGYPQLSAVIECADAAHGLGGQIISDGGCTMPGDVAKAFGGGADFVMLGGMLA 246
Cdd:cd00381 151 DLIDAGADGVKVGIGPGSICTTRIVTGVGVPQATAVADVAAAARDYGVPVIADGGIRTSGDIVKALAAGADAVMLGSLLA 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216606901 247 GHEESGGTVVEENGEKFMLFYGMSSESAMT-----RHVGGVAKYRAAEGKTVKLPLRGPVEITARDILGGLRSACTYVGA 321
Cdd:cd00381 231 GTDESPGEYIEINGKRYKEYRGMGSLGAMKkgggdRYFGEEAKKLVPEGVEGIVPYKGSVKDVLPQLVGGLRSSMGYCGA 310
|
330
....*....|....*
gi 2216606901 322 SRLKELTKRTTFIRV 336
Cdd:cd00381 311 KSLKELQEKARFVRI 325
|
|
| GuaB |
COG0516 |
IMP dehydrogenase/GMP reductase [Nucleotide transport and metabolism]; IMP dehydrogenase/GMP ... |
14-336 |
6.63e-83 |
|
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: 254.75 E-value: 6.63e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216606901 14 VLIRPKRSTLKSRSDVELERQFTFKHSGQTWSGVPIIAANMDTVGTFEMATALAQFDVLTAVHKHYSTEEWSAFVASASA 93
Cdd:COG0516 1 LVLDALRRRLISRSGVVVVVVVGKLTIITTRRRRRDEAVKALVVTTVIEKLLLVTVAGETALLALALLLLKKKKFLLLVD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216606901 94 DVVKHVMVSTGTSDADFEKTKQILNANPALNFVCIDVANGYSEHfvQFVSKARDAWPTKTIIAGNVVTGEMCEELILSGA 173
Cdd:COG0516 81 DDGLLLLVLVGVKDDDKEKARALAAADAGVDVLVIDAAHGHSGG--DAMKKIKLTFDDVLLIPGNSATVEPARALVDAGA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216606901 174 DIVKVGIGPGSVCTTRVKTGVGYPQLSAVIECADAAHGLgGQIISDGGCTMPGDVAKAFGGGADFVMLGGMLAGHEESGG 253
Cdd:COG0516 159 DLTKVGIGPGSICTTRVVIGLGIPQLSAAMDTVTEARMA-IAIAADGGIGYIHDNAKALAAGADAVMLGSLFAGTEEQPG 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216606901 254 TVVEENGEKFMLFYGMSSEsamtrhvggvAKYRAAEGKTVKLPLRGPVEITARDILGGLRSACTYVGASRLKELTKRTTF 333
Cdd:COG0516 238 EVILYQGRSVKRYRGMGSD----------AKKLVPEGIEGRVPYKGPLEDTLHQLLGGLRSGMGYCGARTIEELREKARF 307
|
...
gi 2216606901 334 IRV 336
Cdd:COG0516 308 VRI 310
|
|
| IMPDH |
pfam00478 |
IMP dehydrogenase / GMP reductase domain; This family is involved in biosynthesis of guanosine ... |
104-336 |
5.03e-71 |
|
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: 228.04 E-value: 5.03e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216606901 104 GTSDADFEKTKQILNANpaLNFVCIDVANGYSEHFVQFVSKARDAWPTKTIIAGNVVTGEMCEELILSGADIVKVGIGPG 183
Cdd:pfam00478 216 GVGDDTLERAEALVEAG--VDVLVVDTAHGHSKGVIDTVKWIKKKYPDVQVIAGNVATAEGAKALIEAGADAVKVGIGPG 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216606901 184 SVCTTRVKTGVGYPQLSAVIECADAAHGLGGQIISDGGCTMPGDVAKAFGGGADFVMLGGMLAGHEESGGTVVEENGEKF 263
Cdd:pfam00478 294 SICTTRVVAGVGVPQLTAIYDVAEAAKKYGVPVIADGGIKYSGDIVKALAAGADAVMLGSLLAGTDESPGEVILYQGRRY 373
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2216606901 264 MLFYGMSSESAMTRHV------GGVAKYRAAEGKTVKLPLRGPVEITARDILGGLRSACTYVGASRLKELTKRTTFIRV 336
Cdd:pfam00478 374 KSYRGMGSLGAMKKGSkdryfqEDDDKKLVPEGVEGRVPYKGPLSDVVYQLVGGLRSGMGYCGAKTIEELREKARFVRI 452
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK05096 |
PRK05096 |
guanosine 5'-monophosphate oxidoreductase; Provisional |
1-346 |
0e+00 |
|
guanosine 5'-monophosphate oxidoreductase; Provisional
Pssm-ID: 235343 [Multi-domain] Cd Length: 346 Bit Score: 778.74 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216606901 1 MRIEEDLKLGFKDVLIRPKRSTLKSRSDVELERQFTFKHSGQTWSGVPIIAANMDTVGTFEMATALAQFDVLTAVHKHYS 80
Cdd:PRK05096 1 MRIEEDLKLGFKDVLIRPKRSTLKSRSDVELERQFTFKHSGQSWSGVPIIAANMDTVGTFEMAKALASFDILTAVHKHYS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216606901 81 TEEWSAFVASASADVVKHVMVSTGTSDADFEKTKQILNANPALNFVCIDVANGYSEHFVQFVSKARDAWPTKTIIAGNVV 160
Cdd:PRK05096 81 VEEWAAFVNNSSADVLKHVMVSTGTSDADFEKTKQILALSPALNFICIDVANGYSEHFVQFVAKAREAWPDKTICAGNVV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216606901 161 TGEMCEELILSGADIVKVGIGPGSVCTTRVKTGVGYPQLSAVIECADAAHGLGGQIISDGGCTMPGDVAKAFGGGADFVM 240
Cdd:PRK05096 161 TGEMVEELILSGADIVKVGIGPGSVCTTRVKTGVGYPQLSAVIECADAAHGLGGQIVSDGGCTVPGDVAKAFGGGADFVM 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216606901 241 LGGMLAGHEESGGTVVEENGEKFMLFYGMSSESAMTRHVGGVAKYRAAEGKTVKLPLRGPVEITARDILGGLRSACTYVG 320
Cdd:PRK05096 241 LGGMLAGHEESGGEIVEENGEKFMLFYGMSSESAMKRHVGGVAEYRAAEGKTVKLPLRGPVENTARDILGGLRSACTYVG 320
|
330 340
....*....|....*....|....*.
gi 2216606901 321 ASRLKELTKRTTFIRVQEQENRVFNS 346
Cdd:PRK05096 321 ASRLKELTKRTTFIRVQEQENRVFNN 346
|
|
| GMP_reduct_1 |
TIGR01305 |
guanosine monophosphate reductase, eukaryotic; A deep split separates two families of GMP ... |
2-344 |
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: 655.84 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216606901 2 RIEEDLKLGFKDVLIRPKRSTLKSRSDVELERQFTFKHSGQTWSGVPIIAANMDTVGTFEMATALAQFDVLTAVHKHYST 81
Cdd:TIGR01305 1 RIEADLKLDFKDVLLRPKRSTLKSRADVELERTFTFRNSKQTYSGVPIIAANMDTVGTFEMAAALSQHSIFTAIHKHYSV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216606901 82 EEWSAFVASASADVVKHVMVSTGTSDADFEKTKQILNANPALNFVCIDVANGYSEHFVQFVSKARDAWPTKTIIAGNVVT 161
Cdd:TIGR01305 81 DEWKAFATNSSPDCLQNVAVSSGSSDNDLEKMTSILEAVPQLKFICLDVANGYSEHFVEFVKLVREAFPEHTIMAGNVVT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216606901 162 GEMCEELILSGADIVKVGIGPGSVCTTRVKTGVGYPQLSAVIECADAAHGLGGQIISDGGCTMPGDVAKAFGGGADFVML 241
Cdd:TIGR01305 161 GEMVEELILSGADIVKVGIGPGSVCTTRTKTGVGYPQLSAVIECADAAHGLKGHIISDGGCTCPGDVAKAFGAGADFVML 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216606901 242 GGMLAGHEESGGTVVEENGEKFMLFYGMSSESAMTRHVGGVAKYRAAEGKTVKLPLRGPVEITARDILGGLRSACTYVGA 321
Cdd:TIGR01305 241 GGMFAGHTESGGEVIERNGRKFKLFYGMSSDTAMKKHAGGVAEYRASEGKTVEVPYRGDVENTILDILGGLRSACTYVGA 320
|
330 340
....*....|....*....|...
gi 2216606901 322 SRLKELTKRTTFIRVQEQENRVF 344
Cdd:TIGR01305 321 AKLKELSKRATFIRVTQQHNTVF 343
|
|
| IMPDH |
cd00381 |
IMPDH: The catalytic domain of the inosine monophosphate dehydrogenase. IMPDH catalyzes the ... |
9-336 |
2.71e-115 |
|
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: 2.71e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216606901 9 LGFKDVLIRPKRSTLkSRSDVELERQFTFKHSGQTwsgvPIIAANMDTVGTFEMATALAQFDVLTAVHKHYSTEEWSAFV 88
Cdd:cd00381 2 LTFDDVLLVPGYSTV-LPSEVDLSTKLTKNITLNI----PLVSAPMDTVTESEMAIAMARLGGIGVIHRNMSIEEQAEEV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216606901 89 AsasaDVVKHVMV--STGTSDADFEKTKQILNANpaLNFVCIDVANGYSEHFVQFVSKARDAWPTKTIIAGNVVTGEMCE 166
Cdd:cd00381 77 R----KVKGRLLVgaAVGTREDDKERAEALVEAG--VDVIVIDSAHGHSVYVIEMIKFIKKKYPNVDVIAGNVVTAEAAR 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216606901 167 ELILSGADIVKVGIGPGSVCTTRVKTGVGYPQLSAVIECADAAHGLGGQIISDGGCTMPGDVAKAFGGGADFVMLGGMLA 246
Cdd:cd00381 151 DLIDAGADGVKVGIGPGSICTTRIVTGVGVPQATAVADVAAAARDYGVPVIADGGIRTSGDIVKALAAGADAVMLGSLLA 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216606901 247 GHEESGGTVVEENGEKFMLFYGMSSESAMT-----RHVGGVAKYRAAEGKTVKLPLRGPVEITARDILGGLRSACTYVGA 321
Cdd:cd00381 231 GTDESPGEYIEINGKRYKEYRGMGSLGAMKkgggdRYFGEEAKKLVPEGVEGIVPYKGSVKDVLPQLVGGLRSSMGYCGA 310
|
330
....*....|....*
gi 2216606901 322 SRLKELTKRTTFIRV 336
Cdd:cd00381 311 KSLKELQEKARFVRI 325
|
|
| GuaB |
COG0516 |
IMP dehydrogenase/GMP reductase [Nucleotide transport and metabolism]; IMP dehydrogenase/GMP ... |
14-336 |
6.63e-83 |
|
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: 254.75 E-value: 6.63e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216606901 14 VLIRPKRSTLKSRSDVELERQFTFKHSGQTWSGVPIIAANMDTVGTFEMATALAQFDVLTAVHKHYSTEEWSAFVASASA 93
Cdd:COG0516 1 LVLDALRRRLISRSGVVVVVVVGKLTIITTRRRRRDEAVKALVVTTVIEKLLLVTVAGETALLALALLLLKKKKFLLLVD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216606901 94 DVVKHVMVSTGTSDADFEKTKQILNANPALNFVCIDVANGYSEHfvQFVSKARDAWPTKTIIAGNVVTGEMCEELILSGA 173
Cdd:COG0516 81 DDGLLLLVLVGVKDDDKEKARALAAADAGVDVLVIDAAHGHSGG--DAMKKIKLTFDDVLLIPGNSATVEPARALVDAGA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216606901 174 DIVKVGIGPGSVCTTRVKTGVGYPQLSAVIECADAAHGLgGQIISDGGCTMPGDVAKAFGGGADFVMLGGMLAGHEESGG 253
Cdd:COG0516 159 DLTKVGIGPGSICTTRVVIGLGIPQLSAAMDTVTEARMA-IAIAADGGIGYIHDNAKALAAGADAVMLGSLFAGTEEQPG 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216606901 254 TVVEENGEKFMLFYGMSSEsamtrhvggvAKYRAAEGKTVKLPLRGPVEITARDILGGLRSACTYVGASRLKELTKRTTF 333
Cdd:COG0516 238 EVILYQGRSVKRYRGMGSD----------AKKLVPEGIEGRVPYKGPLEDTLHQLLGGLRSGMGYCGARTIEELREKARF 307
|
...
gi 2216606901 334 IRV 336
Cdd:COG0516 308 VRI 310
|
|
| IMPDH |
pfam00478 |
IMP dehydrogenase / GMP reductase domain; This family is involved in biosynthesis of guanosine ... |
104-336 |
5.03e-71 |
|
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: 228.04 E-value: 5.03e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216606901 104 GTSDADFEKTKQILNANpaLNFVCIDVANGYSEHFVQFVSKARDAWPTKTIIAGNVVTGEMCEELILSGADIVKVGIGPG 183
Cdd:pfam00478 216 GVGDDTLERAEALVEAG--VDVLVVDTAHGHSKGVIDTVKWIKKKYPDVQVIAGNVATAEGAKALIEAGADAVKVGIGPG 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216606901 184 SVCTTRVKTGVGYPQLSAVIECADAAHGLGGQIISDGGCTMPGDVAKAFGGGADFVMLGGMLAGHEESGGTVVEENGEKF 263
Cdd:pfam00478 294 SICTTRVVAGVGVPQLTAIYDVAEAAKKYGVPVIADGGIKYSGDIVKALAAGADAVMLGSLLAGTDESPGEVILYQGRRY 373
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2216606901 264 MLFYGMSSESAMTRHV------GGVAKYRAAEGKTVKLPLRGPVEITARDILGGLRSACTYVGASRLKELTKRTTFIRV 336
Cdd:pfam00478 374 KSYRGMGSLGAMKKGSkdryfqEDDDKKLVPEGVEGRVPYKGPLSDVVYQLVGGLRSGMGYCGAKTIEELREKARFVRI 452
|
|
| IMP_dehydrog |
TIGR01302 |
inosine-5'-monophosphate dehydrogenase; This model describes IMP dehydrogenase, an enzyme of ... |
90-327 |
5.88e-61 |
|
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: 201.81 E-value: 5.88e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216606901 90 SASADVVKHVMV--STGTSDADFEKTKQILNANpaLNFVCIDVANGYSEHFVQFVSKARDAWPTKTIIAGNVVTGEMCEE 167
Cdd:TIGR01302 204 HASKDENGRLIVgaAVGTREFDKERAEALVKAG--VDVIVIDSSHGHSIYVIDSIKEIKKTYPDLDIIAGNVATAEQAKA 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216606901 168 LILSGADIVKVGIGPGSVCTTRVKTGVGYPQLSAVIECADAAHGLGGQIISDGGCTMPGDVAKAFGGGADFVMLGGMLAG 247
Cdd:TIGR01302 282 LIDAGADGLRVGIGPGSICTTRIVAGVGVPQITAVYDVAEYAAQSGIPVIADGGIRYSGDIVKALAAGADAVMLGSLLAG 361
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216606901 248 HEESGGTVVEENGEKFMLFYGMSSESAMTRhvGGVAKY---------RAAEGKTVKLPLRGPVEITARDILGGLRSACTY 318
Cdd:TIGR01302 362 TTESPGEYEIINGRRYKQYRGMGSLGAMTK--GSSDRYlqdenktkkFVPEGVEGAVPYKGSVLELLPQLVGGLKSGMGY 439
|
....*....
gi 2216606901 319 VGASRLKEL 327
Cdd:TIGR01302 440 VGARSIDEL 448
|
|
| PRK05458 |
PRK05458 |
guanosine 5'-monophosphate oxidoreductase; Provisional |
11-329 |
7.39e-55 |
|
guanosine 5'-monophosphate oxidoreductase; Provisional
Pssm-ID: 235479 [Multi-domain] Cd Length: 326 Bit Score: 182.46 E-value: 7.39e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216606901 11 FKDVLIRPKRSTLKSRSDVELERQF---TFKhsgqtwsgVPIIAANMDTVGTFEMATALAQFDVLTAVHKhYSTEEWSAF 87
Cdd:PRK05458 7 YEDIQLIPNKCIVNSRSECDTSVTLgprTFK--------LPVVPANMQTIIDEKIAEWLAENGYFYIMHR-FDPEARIPF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216606901 88 VAS-------ASadvvkhvmVSTGTSDADFEKTKQILNANPALNFVCIDVANGYSEHFVQFVSKARDAWPTKTIIAGNVV 160
Cdd:PRK05458 78 IKDmheqgliAS--------ISVGVKDDEYDFVDQLAAEGLTPEYITIDIAHGHSDSVINMIQHIKKHLPETFVIAGNVG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216606901 161 TGEMCEELILSGADIVKVGIGPGSVCTTRVKTGVGYP--QLSAVIECADAAHglgGQIISDGGCTMPGDVAKAFGGGADF 238
Cdd:PRK05458 150 TPEAVRELENAGADATKVGIGPGKVCITKIKTGFGTGgwQLAALRWCAKAAR---KPIIADGGIRTHGDIAKSIRFGATM 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216606901 239 VMLGGMLAGHEESGGTVVEENGEKFMLFYGMSSEsamtrhvggVAK--YRAAEGKTVKLPLRGPVEITARDILGGLRSAC 316
Cdd:PRK05458 227 VMIGSLFAGHEESPGKTVEIDGKLYKEYFGSASE---------FQKgeYKNVEGKKILVPHKGSLKDTLTEMEQDLQSSI 297
|
330
....*....|...
gi 2216606901 317 TYVGASRLKELTK 329
Cdd:PRK05458 298 SYAGGRDLDAIRK 310
|
|
| PTZ00314 |
PTZ00314 |
inosine-5'-monophosphate dehydrogenase; Provisional |
91-337 |
2.58e-54 |
|
inosine-5'-monophosphate dehydrogenase; Provisional
Pssm-ID: 240355 [Multi-domain] Cd Length: 495 Bit Score: 185.56 E-value: 2.58e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216606901 91 ASADVVKHVMV--STGTSDADFEKTKQILNAnpALNFVCIDVANGYSEHFVQFVSKARDAWPTKTIIAGNVVTGEMCEEL 168
Cdd:PTZ00314 222 ASLDSNGQLLVgaAISTRPEDIERAAALIEA--GVDVLVVDSSQGNSIYQIDMIKKLKSNYPHVDIIAGNVVTADQAKNL 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216606901 169 ILSGADIVKVGIGPGSVCTTRVKTGVGYPQLSAVIECADAAHGLGGQIISDGGCTMPGDVAKAFGGGADFVMLGGMLAGH 248
Cdd:PTZ00314 300 IDAGADGLRIGMGSGSICITQEVCAVGRPQASAVYHVARYARERGVPCIADGGIKNSGDICKALALGADCVMLGSLLAGT 379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216606901 249 EESGGTVVEENGEKFMLFYGMSSESAM------TRHVGGVAKYRAAEGKTVKLPLRGPVEITARDILGGLRSACTYVGAS 322
Cdd:PTZ00314 380 EEAPGEYFFKDGVRLKVYRGMGSLEAMlskesgERYLDENETIKVAQGVSGSVVDKGSVAKLIPYLVKGVKHGMQYIGAH 459
|
250
....*....|....*
gi 2216606901 323 RLKELTKRTTFIRVQ 337
Cdd:PTZ00314 460 SIPELHEKLYSGQVR 474
|
|
| PRK06843 |
PRK06843 |
inosine 5-monophosphate dehydrogenase; Validated |
9-336 |
6.66e-53 |
|
inosine 5-monophosphate dehydrogenase; Validated
Pssm-ID: 180725 [Multi-domain] Cd Length: 404 Bit Score: 179.46 E-value: 6.66e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216606901 9 LGFKDVLIRPKRSTLKSrSDVELERQFTFKHSgqtwSGVPIIAANMDTVGTFEMATALAQFDVLTAVHKHYSTE------ 82
Cdd:PRK06843 10 LTFDDVSLIPRKSSVLP-SEVSLKTQLTKNIS----LNIPFLSSAMDTVTESQMAIAIAKEGGIGIIHKNMSIEaqrkei 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216606901 83 -----------------------------------------EWSAFVASASADVVKHVMVSTGTS-DAD-FEKTKQILNA 119
Cdd:PRK06843 85 ekvktykfqktintngdtneqkpeiftakqhleksdayknaEHKEDFPNACKDLNNKLRVGAAVSiDIDtIERVEELVKA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216606901 120 NpaLNFVCIDVANGYSEHFVQFVSKARDAWPTKTIIAGNVVTGEMCEELILSGADIVKVGIGPGSVCTTRVKTGVGYPQL 199
Cdd:PRK06843 165 H--VDILVIDSAHGHSTRIIELVKKIKTKYPNLDLIAGNIVTKEAALDLISVGADCLKVGIGPGSICTTRIVAGVGVPQI 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216606901 200 SAVIECADAAHGLGGQIISDGGCTMPGDVAKAFGGGADFVMLGGMLAGHEESGGTVVEENGEKFMLFYGMSSESAMTRhv 279
Cdd:PRK06843 243 TAICDVYEVCKNTNICIIADGGIRFSGDVVKAIAAGADSVMIGNLFAGTKESPSEEIIYNGKKFKSYVGMGSISAMKR-- 320
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2216606901 280 GGVAKYRAAEG----KTVKLPLRGPVEITA--RDIL----GGLRSACTYVGASRLKELTKRTTFIRV 336
Cdd:PRK06843 321 GSKSRYFQLENnepkKLVPEGIEGMVPYSGklKDILtqlkGGLMSGMGYLGAATISDLKINSKFVKI 387
|
|
| PRK07807 |
PRK07807 |
GuaB1 family IMP dehydrogenase-related protein; |
128-330 |
2.51e-50 |
|
GuaB1 family IMP dehydrogenase-related protein;
Pssm-ID: 181127 [Multi-domain] Cd Length: 479 Bit Score: 174.32 E-value: 2.51e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216606901 128 IDVANGYSEHFVQFVSKARDAWPTKTIIAGNVVTGEMCEELILSGADIVKVGIGPGSVCTTRVKTGVGYPQLSAVIECAD 207
Cdd:PRK07807 245 VDTAHGHQEKMLEALRAVRALDPGVPIVAGNVVTAEGTRDLVEAGADIVKVGVGPGAMCTTRMMTGVGRPQFSAVLECAA 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216606901 208 AAHGLGGQIISDGGCTMPGDVAKAFGGGADFVMLGGMLAG-HEESGGTVVEENGEKFMLFYGMSSESAM---TRHVGGVA 283
Cdd:PRK07807 325 AARELGAHVWADGGVRHPRDVALALAAGASNVMIGSWFAGtYESPGDLMRDRDGRPYKESFGMASARAVaarTAGDSAFD 404
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2216606901 284 KYRAA---EG-KTVKL---PLRGPVEITARDILGGLRSACTYVGASRLKELTKR 330
Cdd:PRK07807 405 RARKAlfeEGiSTSRMyldPGRPGVEDLLDHITSGVRSSCTYAGARTLAEFHER 458
|
|
| IMP_DH_rel_1 |
TIGR01303 |
IMP dehydrogenase family protein; This model represents a family of proteins, often annotated ... |
112-332 |
4.71e-49 |
|
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: 171.24 E-value: 4.71e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216606901 112 KTKQILNAnpALNFVCIDVANGYSEHFVQFVSKARDAWPTKTIIAGNVVTGEMCEELILSGADIVKVGIGPGSVCTTRVK 191
Cdd:TIGR01303 229 KAKALLDA--GVDVLVIDTAHGHQVKMISAIKAVRALDLGVPIVAGNVVSAEGVRDLLEAGANIIKVGVGPGAMCTTRMM 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216606901 192 TGVGYPQLSAVIECADAAHGLGGQIISDGGCTMPGDVAKAFGGGADFVMLGGMLAGHEESGGTVV-EENGEKFMLFYGMS 270
Cdd:TIGR01303 307 TGVGRPQFSAVLECAAEARKLGGHVWADGGVRHPRDVALALAAGASNVMVGSWFAGTYESPGDLMrDRDGRPYKESFGMA 386
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2216606901 271 SESAMTRHVGGVAKYRAA------EG-KTVKL---PLRGPVEITARDILGGLRSACTYVGASRLKELTKRTT 332
Cdd:TIGR01303 387 SKRAVVARTGADNAFDRArkalfeEGiSTSRMgldPDRGGVEDLIDHIISGVRSSCTYAGASSLEEFHERAV 458
|
|
| PLN02274 |
PLN02274 |
inosine-5'-monophosphate dehydrogenase |
99-290 |
1.72e-31 |
|
inosine-5'-monophosphate dehydrogenase
Pssm-ID: 215154 [Multi-domain] Cd Length: 505 Bit Score: 123.62 E-value: 1.72e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216606901 99 VMVSTGTSDADFEKTKQILNAnpALNFVCIDVANGYSEHFVQFVSKARDAWPTKTIIAGNVVTGEMCEELILSGADIVKV 178
Cdd:PLN02274 239 VGAAIGTRESDKERLEHLVKA--GVDVVVLDSSQGDSIYQLEMIKYIKKTYPELDVIGGNVVTMYQAQNLIQAGVDGLRV 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216606901 179 GIGPGSVCTTRVKTGVGYPQLSAVIECADAAHGLGGQIISDGGCTMPGDVAKAFGGGADFVMLGGMLAGHEESGGTVVEE 258
Cdd:PLN02274 317 GMGSGSICTTQEVCAVGRGQATAVYKVASIAAQHGVPVIADGGISNSGHIVKALTLGASTVMMGSFLAGTTEAPGEYFYQ 396
|
170 180 190
....*....|....*....|....*....|....*..
gi 2216606901 259 NGEKFMLFYGMSSESAMT-----RHVGGVAKYRAAEG 290
Cdd:PLN02274 397 DGVRVKKYRGMGSLEAMTkgsdqRYLGDTAKLKIAQG 433
|
|
| PRK07107 |
PRK07107 |
IMP dehydrogenase; |
94-336 |
1.73e-24 |
|
IMP dehydrogenase;
Pssm-ID: 180842 [Multi-domain] Cd Length: 502 Bit Score: 104.01 E-value: 1.73e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216606901 94 DVVKHVMVSTGTSDADFEKTKqilnanPAL-----NFVCIDVANGYSEHFVQFVSKARDAWPTKTII-AGNVVTGEMCEE 167
Cdd:PRK07107 227 DSSKRYVVGAGINTRDYAERV------PALveagaDVLCIDSSEGYSEWQKRTLDWIREKYGDSVKVgAGNVVDREGFRY 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216606901 168 LILSGADIVKVGIGPGSVCTTRVKTGVGYPQLSAVIECADA------AHGLGGQIISDGGCTMPGDVAKAFGGGADFVML 241
Cdd:PRK07107 301 LAEAGADFVKVGIGGGSICITREQKGIGRGQATALIEVAKArdeyfeETGVYIPICSDGGIVYDYHMTLALAMGADFIML 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216606901 242 GGMLAGHEESGGTVVEENGEKFMLFYGMSSESAMT---RHVGGVAKYRAAEGKTVKLPLRGP----VEITardiLGGLRS 314
Cdd:PRK07107 381 GRYFARFDESPTNKVNINGNYMKEYWGEGSNRARNwqrYDLGGDKKLSFEEGVDSYVPYAGSlkdnVAIT----LSKVRS 456
|
250 260
....*....|....*....|..
gi 2216606901 315 ACTYVGASRLKELTKRTTFIRV 336
Cdd:PRK07107 457 TMCNCGALSIPELQQKAKITLV 478
|
|
| MDH_FMN |
cd04736 |
Mandelate dehydrogenase (MDH)-like FMN-binding domain. MDH is part of a widespread family of ... |
114-256 |
1.17e-03 |
|
Mandelate dehydrogenase (MDH)-like FMN-binding domain. MDH is part of a widespread family of homologous FMN-dependent a-hydroxy acid oxidizing enzymes that oxidizes (S)-mandelate to phenylglyoxalate. MDH is an enzyme in the mandelate pathway that occurs in several strains of Pseudomonas which converts (R)-mandelate to benzoate. This family occurs in both prokaryotes and eukaryotes. Members of this family include flavocytochrome b2 (FCB2), glycolate oxidase (GOX), lactate monooxygenase (LMO), mandelate dehydrogenase (MDH), and long chain hydroxyacid oxidase (LCHAO).
Pssm-ID: 240087 Cd Length: 361 Bit Score: 40.59 E-value: 1.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216606901 114 KQILNANPAL-NFVCIDVANGYSEHFV-----------QFVSKARDAWPTKTIIAGnVVTGEMCEELILSGADIVkvgig 181
Cdd:cd04736 188 RFLRNGMPQLaNFASDDAIDVEVQAALmsrqmdasfnwQDLRWLRDLWPHKLLVKG-IVTAEDAKRCIELGADGV----- 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216606901 182 pgsvcttrVKTGVGYPQLSAVIECADA----AHGLGGQIISDGGCTMPGDVAKAFGGGADFVMLG-----GMLAGHEESG 252
Cdd:cd04736 262 --------ILSNHGGRQLDDAIAPIEAlaeiVAATYKPVLIDSGIRRGSDIVKALALGANAVLLGratlyGLAARGEAGV 333
|
....
gi 2216606901 253 GTVV 256
Cdd:cd04736 334 SEVL 337
|
|
| LldD |
COG1304 |
FMN-dependent dehydrogenase, includes L-lactate dehydrogenase and type II isopentenyl ... |
146-242 |
6.74e-03 |
|
FMN-dependent dehydrogenase, includes L-lactate dehydrogenase and type II isopentenyl diphosphate isomerase [Energy production and conversion, Lipid transport and metabolism, General function prediction only]; FMN-dependent dehydrogenase, includes L-lactate dehydrogenase and type II isopentenyl diphosphate isomerase is part of the Pathway/BioSystem: Isoprenoid biosynthesis
Pssm-ID: 440915 [Multi-domain] Cd Length: 357 Bit Score: 37.80 E-value: 6.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2216606901 146 RDAWPTKTIIAGnVVTGEMCEELILSGADIVKV----GigpgsvctTRVKTGVgyPQLSAVIECADAAHGlGGQIISDGG 221
Cdd:COG1304 221 RERWPGPLIVKG-VLSPEDARRAVDAGVDGIDVsnhgG--------RQLDGGP--PTIDALPEIRAAVGG-RIPVIADGG 288
|
90 100
....*....|....*....|.
gi 2216606901 222 CTMPGDVAKAFGGGADFVMLG 242
Cdd:COG1304 289 IRRGLDVAKALALGADAVGLG 309
|
|
| |
