|
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: 767.57 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769929891 1 MRIEQDLKLGFKDVLFRPKRSTLKSRSQVELTREFTFKHSGRQWSGVPIIAANMDSVGSFEMVKALSKHNVMTAVHKHYT 80
Cdd:PRK05096 1 MRIEEDLKLGFKDVLIRPKRSTLKSRSDVELERQFTFKHSGQSWSGVPIIAANMDTVGTFEMAKALASFDILTAVHKHYS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769929891 81 VEQWADFISQNDASVLKNAMVSTGTSDADFQKTKDIMALTDDLIFICIDIANGYSEHLVEYVEKVRAAFPDKVISAGNVV 160
Cdd:PRK05096 81 VEEWAAFVNNSSADVLKHVMVSTGTSDADFEKTKQILALSPALNFICIDVANGYSEHFVQFVAKAREAWPDKTICAGNVV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769929891 161 TGDMVEELILAGADIVKVGIGPGSVCTTRVKTGVGYPQLSAIIECADAAHGLGGRIIGDGGCSCAGDVSKAFGGGADFVM 240
Cdd:PRK05096 161 TGEMVEELILSGADIVKVGIGPGSVCTTRVKTGVGYPQLSAVIECADAAHGLGGQIVSDGGCTVPGDVAKAFGGGADFVM 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769929891 241 LGGMLAAHDESGGELIEQDGKTFMKFYGMSSQSAMDKHSGGVAKYRAAEGKTVLLPYRGPVENTIQDIMGGVRSTCTYVG 320
Cdd:PRK05096 241 LGGMLAGHEESGGEIVEENGEKFMLFYGMSSESAMKRHVGGVAEYRAAEGKTVKLPLRGPVENTARDILGGLRSACTYVG 320
|
330 340
....*....|....*....|....*.
gi 769929891 321 AAQLKELTKRTTFIRVQEQENNVFGK 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: 581.88 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769929891 2 RIEQDLKLGFKDVLFRPKRSTLKSRSQVELTREFTFKHSGRQWSGVPIIAANMDSVGSFEMVKALSKHNVMTAVHKHYTV 81
Cdd:TIGR01305 1 RIEADLKLDFKDVLLRPKRSTLKSRADVELERTFTFRNSKQTYSGVPIIAANMDTVGTFEMAAALSQHSIFTAIHKHYSV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769929891 82 EQWADFISQNDASVLKNAMVSTGTSDADFQKTKDIMALTDDLIFICIDIANGYSEHLVEYVEKVRAAFPDKVISAGNVVT 161
Cdd:TIGR01305 81 DEWKAFATNSSPDCLQNVAVSSGSSDNDLEKMTSILEAVPQLKFICLDVANGYSEHFVEFVKLVREAFPEHTIMAGNVVT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769929891 162 GDMVEELILAGADIVKVGIGPGSVCTTRVKTGVGYPQLSAIIECADAAHGLGGRIIGDGGCSCAGDVSKAFGGGADFVML 241
Cdd:TIGR01305 161 GEMVEELILSGADIVKVGIGPGSVCTTRTKTGVGYPQLSAVIECADAAHGLKGHIISDGGCTCPGDVAKAFGAGADFVML 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769929891 242 GGMLAAHDESGGELIEQDGKTFMKFYGMSSQSAMDKHSGGVAKYRAAEGKTVLLPYRGPVENTIQDIMGGVRSTCTYVGA 321
Cdd:TIGR01305 241 GGMFAGHTESGGEVIERNGRKFKLFYGMSSDTAMKKHAGGVAEYRASEGKTVEVPYRGDVENTILDILGGLRSACTYVGA 320
|
330 340
....*....|....*....|...
gi 769929891 322 AQLKELTKRTTFIRVQEQENNVF 344
Cdd:TIGR01305 321 AKLKELSKRATFIRVTQQHNTVF 343
|
|
| IMPDH |
cd00381 |
IMPDH: The catalytic domain of the inosine monophosphate dehydrogenase. IMPDH catalyzes the ... |
9-336 |
2.26e-112 |
|
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: 329.48 E-value: 2.26e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769929891 9 LGFKDVLFRPKRSTLkSRSQVELTREFTFKHSGrqwsGVPIIAANMDSVGSFEMVKALSKHNVMTAVHKHYTVEQWADFI 88
Cdd:cd00381 2 LTFDDVLLVPGYSTV-LPSEVDLSTKLTKNITL----NIPLVSAPMDTVTESEMAIAMARLGGIGVIHRNMSIEEQAEEV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769929891 89 SQndasVLKNAMV--STGTSDADFQKTKDIMALTDDLIfiCIDIANGYSEHLVEYVEKVRAAFPDKVISAGNVVTGDMVE 166
Cdd:cd00381 77 RK----VKGRLLVgaAVGTREDDKERAEALVEAGVDVI--VIDSAHGHSVYVIEMIKFIKKKYPNVDVIAGNVVTAEAAR 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769929891 167 ELILAGADIVKVGIGPGSVCTTRVKTGVGYPQLSAIIECADAAHGLGGRIIGDGGCSCAGDVSKAFGGGADFVMLGGMLA 246
Cdd:cd00381 151 DLIDAGADGVKVGIGPGSICTTRIVTGVGVPQATAVADVAAAARDYGVPVIADGGIRTSGDIVKALAAGADAVMLGSLLA 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769929891 247 AHDESGGELIEQDGKTFMKFYGMSSQSAMDKHSG-----GVAKYRAAEGKTVLLPYRGPVENTIQDIMGGVRSTCTYVGA 321
Cdd:cd00381 231 GTDESPGEYIEINGKRYKEYRGMGSLGAMKKGGGdryfgEEAKKLVPEGVEGIVPYKGSVKDVLPQLVGGLRSSMGYCGA 310
|
330
....*....|....*
gi 769929891 322 AQLKELTKRTTFIRV 336
Cdd:cd00381 311 KSLKELQEKARFVRI 325
|
|
| GuaB |
COG0516 |
IMP dehydrogenase/GMP reductase [Nucleotide transport and metabolism]; IMP dehydrogenase/GMP ... |
14-336 |
2.16e-87 |
|
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: 265.92 E-value: 2.16e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769929891 14 VLFRPKRSTLKSRSQVELTREFTFKHSGRQWSGVPIIAANMDSVGSFEMVKALSKHNVMTAVHKHYTVEQWADFISQNDA 93
Cdd:COG0516 1 LVLDALRRRLISRSGVVVVVVVGKLTIITTRRRRRDEAVKALVVTTVIEKLLLVTVAGETALLALALLLLKKKKFLLLVD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769929891 94 SVLKNAMVSTGTSDADFQKTKDIMALTDDLIFICIDIANGYSEHlvEYVEKVRAAFPDKVISAGNVVTGDMVEELILAGA 173
Cdd:COG0516 81 DDGLLLLVLVGVKDDDKEKARALAAADAGVDVLVIDAAHGHSGG--DAMKKIKLTFDDVLLIPGNSATVEPARALVDAGA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769929891 174 DIVKVGIGPGSVCTTRVKTGVGYPQLSAIIECADAAHGLgGRIIGDGGCSCAGDVSKAFGGGADFVMLGGMLAAHDESGG 253
Cdd:COG0516 159 DLTKVGIGPGSICTTRVVIGLGIPQLSAAMDTVTEARMA-IAIAADGGIGYIHDNAKALAAGADAVMLGSLFAGTEEQPG 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769929891 254 ELIEQDGKTFMKFYGMSSqsamdkhsggVAKYRAAEGKTVLLPYRGPVENTIQDIMGGVRSTCTYVGAAQLKELTKRTTF 333
Cdd:COG0516 238 EVILYQGRSVKRYRGMGS----------DAKKLVPEGIEGRVPYKGPLEDTLHQLLGGLRSGMGYCGARTIEELREKARF 307
|
...
gi 769929891 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 |
5.10e-77 |
|
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: 243.84 E-value: 5.10e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769929891 104 GTSDADFQKtkdIMALTD---DliFICIDIANGYSEHLVEYVEKVRAAFPDKVISAGNVVTGDMVEELILAGADIVKVGI 180
Cdd:pfam00478 216 GVGDDTLER---AEALVEagvD--VLVVDTAHGHSKGVIDTVKWIKKKYPDVQVIAGNVATAEGAKALIEAGADAVKVGI 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769929891 181 GPGSVCTTRVKTGVGYPQLSAIIECADAAHGLGGRIIGDGGCSCAGDVSKAFGGGADFVMLGGMLAAHDESGGELIEQDG 260
Cdd:pfam00478 291 GPGSICTTRVVAGVGVPQLTAIYDVAEAAKKYGVPVIADGGIKYSGDIVKALAAGADAVMLGSLLAGTDESPGEVILYQG 370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769929891 261 KTFMKFYGMSSQSAMDKHS------GGVAKYRAAEGKTVLLPYRGPVENTIQDIMGGVRSTCTYVGAAQLKELTKRTTFI 334
Cdd:pfam00478 371 RRYKSYRGMGSLGAMKKGSkdryfqEDDDKKLVPEGVEGRVPYKGPLSDVVYQLVGGLRSGMGYCGAKTIEELREKARFV 450
|
..
gi 769929891 335 RV 336
Cdd:pfam00478 451 RI 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: 767.57 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769929891 1 MRIEQDLKLGFKDVLFRPKRSTLKSRSQVELTREFTFKHSGRQWSGVPIIAANMDSVGSFEMVKALSKHNVMTAVHKHYT 80
Cdd:PRK05096 1 MRIEEDLKLGFKDVLIRPKRSTLKSRSDVELERQFTFKHSGQSWSGVPIIAANMDTVGTFEMAKALASFDILTAVHKHYS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769929891 81 VEQWADFISQNDASVLKNAMVSTGTSDADFQKTKDIMALTDDLIFICIDIANGYSEHLVEYVEKVRAAFPDKVISAGNVV 160
Cdd:PRK05096 81 VEEWAAFVNNSSADVLKHVMVSTGTSDADFEKTKQILALSPALNFICIDVANGYSEHFVQFVAKAREAWPDKTICAGNVV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769929891 161 TGDMVEELILAGADIVKVGIGPGSVCTTRVKTGVGYPQLSAIIECADAAHGLGGRIIGDGGCSCAGDVSKAFGGGADFVM 240
Cdd:PRK05096 161 TGEMVEELILSGADIVKVGIGPGSVCTTRVKTGVGYPQLSAVIECADAAHGLGGQIVSDGGCTVPGDVAKAFGGGADFVM 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769929891 241 LGGMLAAHDESGGELIEQDGKTFMKFYGMSSQSAMDKHSGGVAKYRAAEGKTVLLPYRGPVENTIQDIMGGVRSTCTYVG 320
Cdd:PRK05096 241 LGGMLAGHEESGGEIVEENGEKFMLFYGMSSESAMKRHVGGVAEYRAAEGKTVKLPLRGPVENTARDILGGLRSACTYVG 320
|
330 340
....*....|....*....|....*.
gi 769929891 321 AAQLKELTKRTTFIRVQEQENNVFGK 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: 581.88 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769929891 2 RIEQDLKLGFKDVLFRPKRSTLKSRSQVELTREFTFKHSGRQWSGVPIIAANMDSVGSFEMVKALSKHNVMTAVHKHYTV 81
Cdd:TIGR01305 1 RIEADLKLDFKDVLLRPKRSTLKSRADVELERTFTFRNSKQTYSGVPIIAANMDTVGTFEMAAALSQHSIFTAIHKHYSV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769929891 82 EQWADFISQNDASVLKNAMVSTGTSDADFQKTKDIMALTDDLIFICIDIANGYSEHLVEYVEKVRAAFPDKVISAGNVVT 161
Cdd:TIGR01305 81 DEWKAFATNSSPDCLQNVAVSSGSSDNDLEKMTSILEAVPQLKFICLDVANGYSEHFVEFVKLVREAFPEHTIMAGNVVT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769929891 162 GDMVEELILAGADIVKVGIGPGSVCTTRVKTGVGYPQLSAIIECADAAHGLGGRIIGDGGCSCAGDVSKAFGGGADFVML 241
Cdd:TIGR01305 161 GEMVEELILSGADIVKVGIGPGSVCTTRTKTGVGYPQLSAVIECADAAHGLKGHIISDGGCTCPGDVAKAFGAGADFVML 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769929891 242 GGMLAAHDESGGELIEQDGKTFMKFYGMSSQSAMDKHSGGVAKYRAAEGKTVLLPYRGPVENTIQDIMGGVRSTCTYVGA 321
Cdd:TIGR01305 241 GGMFAGHTESGGEVIERNGRKFKLFYGMSSDTAMKKHAGGVAEYRASEGKTVEVPYRGDVENTILDILGGLRSACTYVGA 320
|
330 340
....*....|....*....|...
gi 769929891 322 AQLKELTKRTTFIRVQEQENNVF 344
Cdd:TIGR01305 321 AKLKELSKRATFIRVTQQHNTVF 343
|
|
| IMPDH |
cd00381 |
IMPDH: The catalytic domain of the inosine monophosphate dehydrogenase. IMPDH catalyzes the ... |
9-336 |
2.26e-112 |
|
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: 329.48 E-value: 2.26e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769929891 9 LGFKDVLFRPKRSTLkSRSQVELTREFTFKHSGrqwsGVPIIAANMDSVGSFEMVKALSKHNVMTAVHKHYTVEQWADFI 88
Cdd:cd00381 2 LTFDDVLLVPGYSTV-LPSEVDLSTKLTKNITL----NIPLVSAPMDTVTESEMAIAMARLGGIGVIHRNMSIEEQAEEV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769929891 89 SQndasVLKNAMV--STGTSDADFQKTKDIMALTDDLIfiCIDIANGYSEHLVEYVEKVRAAFPDKVISAGNVVTGDMVE 166
Cdd:cd00381 77 RK----VKGRLLVgaAVGTREDDKERAEALVEAGVDVI--VIDSAHGHSVYVIEMIKFIKKKYPNVDVIAGNVVTAEAAR 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769929891 167 ELILAGADIVKVGIGPGSVCTTRVKTGVGYPQLSAIIECADAAHGLGGRIIGDGGCSCAGDVSKAFGGGADFVMLGGMLA 246
Cdd:cd00381 151 DLIDAGADGVKVGIGPGSICTTRIVTGVGVPQATAVADVAAAARDYGVPVIADGGIRTSGDIVKALAAGADAVMLGSLLA 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769929891 247 AHDESGGELIEQDGKTFMKFYGMSSQSAMDKHSG-----GVAKYRAAEGKTVLLPYRGPVENTIQDIMGGVRSTCTYVGA 321
Cdd:cd00381 231 GTDESPGEYIEINGKRYKEYRGMGSLGAMKKGGGdryfgEEAKKLVPEGVEGIVPYKGSVKDVLPQLVGGLRSSMGYCGA 310
|
330
....*....|....*
gi 769929891 322 AQLKELTKRTTFIRV 336
Cdd:cd00381 311 KSLKELQEKARFVRI 325
|
|
| GuaB |
COG0516 |
IMP dehydrogenase/GMP reductase [Nucleotide transport and metabolism]; IMP dehydrogenase/GMP ... |
14-336 |
2.16e-87 |
|
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: 265.92 E-value: 2.16e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769929891 14 VLFRPKRSTLKSRSQVELTREFTFKHSGRQWSGVPIIAANMDSVGSFEMVKALSKHNVMTAVHKHYTVEQWADFISQNDA 93
Cdd:COG0516 1 LVLDALRRRLISRSGVVVVVVVGKLTIITTRRRRRDEAVKALVVTTVIEKLLLVTVAGETALLALALLLLKKKKFLLLVD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769929891 94 SVLKNAMVSTGTSDADFQKTKDIMALTDDLIFICIDIANGYSEHlvEYVEKVRAAFPDKVISAGNVVTGDMVEELILAGA 173
Cdd:COG0516 81 DDGLLLLVLVGVKDDDKEKARALAAADAGVDVLVIDAAHGHSGG--DAMKKIKLTFDDVLLIPGNSATVEPARALVDAGA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769929891 174 DIVKVGIGPGSVCTTRVKTGVGYPQLSAIIECADAAHGLgGRIIGDGGCSCAGDVSKAFGGGADFVMLGGMLAAHDESGG 253
Cdd:COG0516 159 DLTKVGIGPGSICTTRVVIGLGIPQLSAAMDTVTEARMA-IAIAADGGIGYIHDNAKALAAGADAVMLGSLFAGTEEQPG 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769929891 254 ELIEQDGKTFMKFYGMSSqsamdkhsggVAKYRAAEGKTVLLPYRGPVENTIQDIMGGVRSTCTYVGAAQLKELTKRTTF 333
Cdd:COG0516 238 EVILYQGRSVKRYRGMGS----------DAKKLVPEGIEGRVPYKGPLEDTLHQLLGGLRSGMGYCGARTIEELREKARF 307
|
...
gi 769929891 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 |
5.10e-77 |
|
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: 243.84 E-value: 5.10e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769929891 104 GTSDADFQKtkdIMALTD---DliFICIDIANGYSEHLVEYVEKVRAAFPDKVISAGNVVTGDMVEELILAGADIVKVGI 180
Cdd:pfam00478 216 GVGDDTLER---AEALVEagvD--VLVVDTAHGHSKGVIDTVKWIKKKYPDVQVIAGNVATAEGAKALIEAGADAVKVGI 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769929891 181 GPGSVCTTRVKTGVGYPQLSAIIECADAAHGLGGRIIGDGGCSCAGDVSKAFGGGADFVMLGGMLAAHDESGGELIEQDG 260
Cdd:pfam00478 291 GPGSICTTRVVAGVGVPQLTAIYDVAEAAKKYGVPVIADGGIKYSGDIVKALAAGADAVMLGSLLAGTDESPGEVILYQG 370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769929891 261 KTFMKFYGMSSQSAMDKHS------GGVAKYRAAEGKTVLLPYRGPVENTIQDIMGGVRSTCTYVGAAQLKELTKRTTFI 334
Cdd:pfam00478 371 RRYKSYRGMGSLGAMKKGSkdryfqEDDDKKLVPEGVEGRVPYKGPLSDVVYQLVGGLRSGMGYCGAKTIEELREKARFV 450
|
..
gi 769929891 335 RV 336
Cdd:pfam00478 451 RI 452
|
|
| IMP_dehydrog |
TIGR01302 |
inosine-5'-monophosphate dehydrogenase; This model describes IMP dehydrogenase, an enzyme of ... |
101-327 |
1.60e-60 |
|
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: 200.65 E-value: 1.60e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769929891 101 VSTGTSDADFQKTKDIMALTDDliFICIDIANGYSEHLVEYVEKVRAAFPDKVISAGNVVTGDMVEELILAGADIVKVGI 180
Cdd:TIGR01302 217 AAVGTREFDKERAEALVKAGVD--VIVIDSSHGHSIYVIDSIKEIKKTYPDLDIIAGNVATAEQAKALIDAGADGLRVGI 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769929891 181 GPGSVCTTRVKTGVGYPQLSAIIECADAAHGLGGRIIGDGGCSCAGDVSKAFGGGADFVMLGGMLAAHDESGGELIEQDG 260
Cdd:TIGR01302 295 GPGSICTTRIVAGVGVPQITAVYDVAEYAAQSGIPVIADGGIRYSGDIVKALAAGADAVMLGSLLAGTTESPGEYEIING 374
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 769929891 261 KTFMKFYGMSSQSAMDKHSGG-------VAKYRAAEGKTVLLPYRGPVENTIQDIMGGVRSTCTYVGAAQLKEL 327
Cdd:TIGR01302 375 RRYKQYRGMGSLGAMTKGSSDrylqdenKTKKFVPEGVEGAVPYKGSVLELLPQLVGGLKSGMGYVGARSIDEL 448
|
|
| PRK05458 |
PRK05458 |
guanosine 5'-monophosphate oxidoreductase; Provisional |
11-329 |
1.39e-58 |
|
guanosine 5'-monophosphate oxidoreductase; Provisional
Pssm-ID: 235479 [Multi-domain] Cd Length: 326 Bit Score: 192.09 E-value: 1.39e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769929891 11 FKDVLFRPKRSTLKSRSQVELTREF---TFKhsgrqwsgVPIIAANMDSVGSFEMVKALSKHNVMTAVHKhYTVEQWADF 87
Cdd:PRK05458 7 YEDIQLIPNKCIVNSRSECDTSVTLgprTFK--------LPVVPANMQTIIDEKIAEWLAENGYFYIMHR-FDPEARIPF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769929891 88 ISQNDASVLKnAMVSTGTSDADFQKTKDIMAltDDLI--FICIDIANGYSEHLVEYVEKVRAAFPDKVISAGNVVTGDMV 165
Cdd:PRK05458 78 IKDMHEQGLI-ASISVGVKDDEYDFVDQLAA--EGLTpeYITIDIAHGHSDSVINMIQHIKKHLPETFVIAGNVGTPEAV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769929891 166 EELILAGADIVKVGIGPGSVCTTRVKTGVGYP--QLSAIIECADAAHglgGRIIGDGGCSCAGDVSKAFGGGADFVMLGG 243
Cdd:PRK05458 155 RELENAGADATKVGIGPGKVCITKIKTGFGTGgwQLAALRWCAKAAR---KPIIADGGIRTHGDIAKSIRFGATMVMIGS 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769929891 244 MLAAHDESGGELIEQDGKTFMKFYGmssqSAMDKHSGgvaKYRAAEGKTVLLPYRGPVENTIQDIMGGVRSTCTYVGAAQ 323
Cdd:PRK05458 232 LFAGHEESPGKTVEIDGKLYKEYFG----SASEFQKG---EYKNVEGKKILVPHKGSLKDTLTEMEQDLQSSISYAGGRD 304
|
....*.
gi 769929891 324 LKELTK 329
Cdd:PRK05458 305 LDAIRK 310
|
|
| PRK07807 |
PRK07807 |
GuaB1 family IMP dehydrogenase-related protein; |
126-330 |
2.19e-54 |
|
GuaB1 family IMP dehydrogenase-related protein;
Pssm-ID: 181127 [Multi-domain] Cd Length: 479 Bit Score: 185.11 E-value: 2.19e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769929891 126 ICIDIANGYSEHLVEYVEKVRAAFPDKVISAGNVVTGDMVEELILAGADIVKVGIGPGSVCTTRVKTGVGYPQLSAIIEC 205
Cdd:PRK07807 243 LVVDTAHGHQEKMLEALRAVRALDPGVPIVAGNVVTAEGTRDLVEAGADIVKVGVGPGAMCTTRMMTGVGRPQFSAVLEC 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769929891 206 ADAAHGLGGRIIGDGGCSCAGDVSKAFGGGADFVMLGGMLAAHDESGGEL-IEQDGKTFMKFYGMSSQSAMDKHSGGVAK 284
Cdd:PRK07807 323 AAAARELGAHVWADGGVRHPRDVALALAAGASNVMIGSWFAGTYESPGDLmRDRDGRPYKESFGMASARAVAARTAGDSA 402
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 769929891 285 Y-RA-----AEG----KTVLLPYRGPVENTIQDIMGGVRSTCTYVGAAQLKELTKR 330
Cdd:PRK07807 403 FdRArkalfEEGistsRMYLDPGRPGVEDLLDHITSGVRSSCTYAGARTLAEFHER 458
|
|
| PTZ00314 |
PTZ00314 |
inosine-5'-monophosphate dehydrogenase; Provisional |
102-337 |
2.96e-54 |
|
inosine-5'-monophosphate dehydrogenase; Provisional
Pssm-ID: 240355 [Multi-domain] Cd Length: 495 Bit Score: 185.17 E-value: 2.96e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769929891 102 STGTSDADFQKTKDIMALTDDLIfiCIDIANGYSEHLVEYVEKVRAAFPDKVISAGNVVTGDMVEELILAGADIVKVGIG 181
Cdd:PTZ00314 235 AISTRPEDIERAAALIEAGVDVL--VVDSSQGNSIYQIDMIKKLKSNYPHVDIIAGNVVTADQAKNLIDAGADGLRIGMG 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769929891 182 PGSVCTTRVKTGVGYPQLSAIIECADAAHGLGGRIIGDGGCSCAGDVSKAFGGGADFVMLGGMLAAHDESGGELIEQDGK 261
Cdd:PTZ00314 313 SGSICITQEVCAVGRPQASAVYHVARYARERGVPCIADGGIKNSGDICKALALGADCVMLGSLLAGTEEAPGEYFFKDGV 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769929891 262 TFMKFYGMSSQSAM-DKHSGG-----VAKYRAAEGKTVLLPYRGPVENTIQDIMGGVRSTCTYVGAAQLKELTKRTTFIR 335
Cdd:PTZ00314 393 RLKVYRGMGSLEAMlSKESGEryldeNETIKVAQGVSGSVVDKGSVAKLIPYLVKGVKHGMQYIGAHSIPELHEKLYSGQ 472
|
..
gi 769929891 336 VQ 337
Cdd:PTZ00314 473 VR 474
|
|
| IMP_DH_rel_1 |
TIGR01303 |
IMP dehydrogenase family protein; This model represents a family of proteins, often annotated ... |
128-346 |
2.93e-52 |
|
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: 179.72 E-value: 2.93e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769929891 128 IDIANGYSEHLVEYVEKVRAAFPDKVISAGNVVTGDMVEELILAGADIVKVGIGPGSVCTTRVKTGVGYPQLSAIIECAD 207
Cdd:TIGR01303 243 IDTAHGHQVKMISAIKAVRALDLGVPIVAGNVVSAEGVRDLLEAGANIIKVGVGPGAMCTTRMMTGVGRPQFSAVLECAA 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769929891 208 AAHGLGGRIIGDGGCSCAGDVSKAFGGGADFVMLGGMLAAHDESGGELI-EQDGKTFMKFYGMSSQSAMDKHSGGVAKYR 286
Cdd:TIGR01303 323 EARKLGGHVWADGGVRHPRDVALALAAGASNVMVGSWFAGTYESPGDLMrDRDGRPYKESFGMASKRAVVARTGADNAFD 402
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769929891 287 AA------EG----KTVLLPYRGPVENTIQDIMGGVRSTCTYVGAAQLKELTKRTTfIRVQEQENNVFGK 346
Cdd:TIGR01303 403 RArkalfeEGistsRMGLDPDRGGVEDLIDHIISGVRSSCTYAGASSLEEFHERAV-VGVQSGAGYAEGK 471
|
|
| PRK06843 |
PRK06843 |
inosine 5-monophosphate dehydrogenase; Validated |
9-336 |
1.08e-50 |
|
inosine 5-monophosphate dehydrogenase; Validated
Pssm-ID: 180725 [Multi-domain] Cd Length: 404 Bit Score: 173.69 E-value: 1.08e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769929891 9 LGFKDVLFRPKRSTLKSrSQVELTREFTFKHSgrqwSGVPIIAANMDSVGSFEMVKALSKHNVMTAVHKHYTVEQWADFI 88
Cdd:PRK06843 10 LTFDDVSLIPRKSSVLP-SEVSLKTQLTKNIS----LNIPFLSSAMDTVTESQMAIAIAKEGGIGIIHKNMSIEAQRKEI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769929891 89 SQ----------NDASVLKNAMVSTGTSDADFQKTK--------------------------------DIMALTDDLI-- 124
Cdd:PRK06843 85 EKvktykfqktiNTNGDTNEQKPEIFTAKQHLEKSDayknaehkedfpnackdlnnklrvgaavsidiDTIERVEELVka 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769929891 125 ---FICIDIANGYSEHLVEYVEKVRAAFPDKVISAGNVVTGDMVEELILAGADIVKVGIGPGSVCTTRVKTGVGYPQLSA 201
Cdd:PRK06843 165 hvdILVIDSAHGHSTRIIELVKKIKTKYPNLDLIAGNIVTKEAALDLISVGADCLKVGIGPGSICTTRIVAGVGVPQITA 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769929891 202 IIECADAAHGLGGRIIGDGGCSCAGDVSKAFGGGADFVMLGGMLAAHDESGGELIEQDGKTFMKFYGMSSQSAMDKHS-- 279
Cdd:PRK06843 245 ICDVYEVCKNTNICIIADGGIRFSGDVVKAIAAGADSVMIGNLFAGTKESPSEEIIYNGKKFKSYVGMGSISAMKRGSks 324
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 769929891 280 ------GGVAKYRAAEGKTVLLPYRGPVENTIQDIMGGVRSTCTYVGAAQLKELTKRTTFIRV 336
Cdd:PRK06843 325 ryfqleNNEPKKLVPEGIEGMVPYSGKLKDILTQLKGGLMSGMGYLGAATISDLKINSKFVKI 387
|
|
| PLN02274 |
PLN02274 |
inosine-5'-monophosphate dehydrogenase |
102-326 |
1.23e-31 |
|
inosine-5'-monophosphate dehydrogenase
Pssm-ID: 215154 [Multi-domain] Cd Length: 505 Bit Score: 124.40 E-value: 1.23e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769929891 102 STGTSDADFQKTKDIMALTDDLIFIciDIANGYSEHLVEYVEKVRAAFPDKVISAGNVVTGDMVEELILAGADIVKVGIG 181
Cdd:PLN02274 242 AIGTRESDKERLEHLVKAGVDVVVL--DSSQGDSIYQLEMIKYIKKTYPELDVIGGNVVTMYQAQNLIQAGVDGLRVGMG 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769929891 182 PGSVCTTRVKTGVGYPQLSAIIECADAAHGLGGRIIGDGGCSCAGDVSKAFGGGADFVMLGGMLAAHDESGGELIEQDGK 261
Cdd:PLN02274 320 SGSICTTQEVCAVGRGQATAVYKVASIAAQHGVPVIADGGISNSGHIVKALTLGASTVMMGSFLAGTTEAPGEYFYQDGV 399
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769929891 262 TFMKFYGMSSQSAMDKHS-----GGVAKYRAAEGKTVLLPYRGPVENTIQDIMGGVRSTCTYVGAAQLKE 326
Cdd:PLN02274 400 RVKKYRGMGSLEAMTKGSdqrylGDTAKLKIAQGVSGAVADKGSVLKFVPYTMQAVKQGFQDLGASSLQS 469
|
|
| PRK07107 |
PRK07107 |
IMP dehydrogenase; |
126-336 |
1.86e-31 |
|
IMP dehydrogenase;
Pssm-ID: 180842 [Multi-domain] Cd Length: 502 Bit Score: 123.65 E-value: 1.86e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769929891 126 ICIDIANGYSEHLVEYVEKVRAAFPDKV-ISAGNVVTGDMVEELILAGADIVKVGIGPGSVCTTRVKTGVGYPQLSAIIE 204
Cdd:PRK07107 258 LCIDSSEGYSEWQKRTLDWIREKYGDSVkVGAGNVVDREGFRYLAEAGADFVKVGIGGGSICITREQKGIGRGQATALIE 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769929891 205 CADA------AHGLGGRIIGDGGCSCAGDVSKAFGGGADFVMLGGMLAAHDESGGELIEQDGkTFMKFY-GMSSQSAMD- 276
Cdd:PRK07107 338 VAKArdeyfeETGVYIPICSDGGIVYDYHMTLALAMGADFIMLGRYFARFDESPTNKVNING-NYMKEYwGEGSNRARNw 416
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 769929891 277 --KHSGGVAKYRAAEGKTVLLPYRGPVENTIQDIMGGVRSTCTYVGAAQLKELTKRTTFIRV 336
Cdd:PRK07107 417 qrYDLGGDKKLSFEEGVDSYVPYAGSLKDNVAITLSKVRSTMCNCGALSIPELQQKAKITLV 478
|
|
| Glu_synthase |
pfam01645 |
Conserved region in glutamate synthase; This family represents a region of the glutamate ... |
134-247 |
4.45e-04 |
|
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: 41.55 E-value: 4.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769929891 134 YS-EHLVEYVEKVRAAFPDKVIS----AGNVVtGDMVEELILAGADIVKV---GIGPGSVCTTRVKTgVGYPQLSAIIEC 205
Cdd:pfam01645 184 YSiEDLAQLIYDLKEINPKAPISvklvSGHGV-GTIAAGVAKAGADIILIdgyDGGTGASPKTSIKH-AGLPWELALAEA 261
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 769929891 206 ADA--AHGLGGR--IIGDGGCSCAGDVSKAFGGGADFVMLG-GMLAA 247
Cdd:pfam01645 262 HQTlkENGLRDRvsLIADGGLRTGADVAKAAALGADAVYIGtAALIA 308
|
|
| KDPG_aldolase |
cd00452 |
KDPG and KHG aldolase; KDPG and KHG aldolase. This family belongs to the class I adolases ... |
140-241 |
1.24e-03 |
|
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: 39.42 E-value: 1.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 769929891 140 EYVEKVRAAFPDKVISAGNVVTGDMVEELILAGADIVkvgIGPGSVcttrvktgvgypqlsaiIECADAAHGLGGRIIgd 219
Cdd:cd00452 44 EAIRALRKEFPEALIGAGTVLTPEQADAAIAAGAQFI---VSPGLD-----------------PEVVKAANRAGIPLL-- 101
|
90 100
....*....|....*....|..
gi 769929891 220 GGCSCAGDVSKAFGGGADFVML 241
Cdd:cd00452 102 PGVATPTEIMQALELGADIVKL 123
|
|
| |
