|
Name |
Accession |
Description |
Interval |
E-value |
| PRK05096 |
PRK05096 |
guanosine 5'-monophosphate oxidoreductase; Provisional |
1-344 |
0e+00 |
|
guanosine 5'-monophosphate oxidoreductase; Provisional
Pssm-ID: 235343 [Multi-domain] Cd Length: 346 Bit Score: 715.57 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1030080485 1 MRIEYDIKLGFKDVMFRPKRSTLKSRSEVSLEREFTFKHTKKKWQGTPIIAANMDTVGTFEMAVELAKDKIITAIHKHYS 80
Cdd:PRK05096 1 MRIEEDLKLGFKDVLIRPKRSTLKSRSDVELERQFTFKHSGQSWSGVPIIAANMDTVGTFEMAKALASFDILTAVHKHYS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1030080485 81 VEEWSDFLNSQPESIHQYIALSTGTGKADEEKLQQILEKHPKIEFLCIDVANGYSEHFVGFVKKARANFPDKIIIAGNVV 160
Cdd:PRK05096 81 VEEWAAFVNNSSADVLKHVMVSTGTSDADFEKTKQILALSPALNFICIDVANGYSEHFVQFVAKAREAWPDKTICAGNVV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1030080485 161 TGEMVEELLLVGADIIKVGIGPGSVCTTRVKTGVGYPQLSAIIECSDAAHGLGGHIIADGGCKVPGDVAKAFGGGADFVM 240
Cdd:PRK05096 161 TGEMVEELILSGADIVKVGIGPGSVCTTRVKTGVGYPQLSAVIECADAAHGLGGQIVSDGGCTVPGDVAKAFGGGADFVM 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1030080485 241 LGGMFAGHDESGGEIIEENGKKYRTFYGMSSKTAMDKHSGGVAEYRASEGKTVKVAYKGPVSETVKDILGGVRSTCTYVG 320
Cdd:PRK05096 241 LGGMLAGHEESGGEIVEENGEKFMLFYGMSSESAMKRHVGGVAEYRAAEGKTVKLPLRGPVENTARDILGGLRSACTYVG 320
|
330 340
....*....|....*....|....
gi 1030080485 321 ASKLKELSKRTTFIRVQEQENQVF 344
Cdd:PRK05096 321 ASRLKELTKRTTFIRVQEQENRVF 344
|
|
| 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: 583.42 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1030080485 2 RIEYDIKLGFKDVMFRPKRSTLKSRSEVSLEREFTFKHTKKKWQGTPIIAANMDTVGTFEMAVELAKDKIITAIHKHYSV 81
Cdd:TIGR01305 1 RIEADLKLDFKDVLLRPKRSTLKSRADVELERTFTFRNSKQTYSGVPIIAANMDTVGTFEMAAALSQHSIFTAIHKHYSV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1030080485 82 EEWSDFLNSQPESIHQYIALSTGTGKADEEKLQQILEKHPKIEFLCIDVANGYSEHFVGFVKKARANFPDKIIIAGNVVT 161
Cdd:TIGR01305 81 DEWKAFATNSSPDCLQNVAVSSGSSDNDLEKMTSILEAVPQLKFICLDVANGYSEHFVEFVKLVREAFPEHTIMAGNVVT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1030080485 162 GEMVEELLLVGADIIKVGIGPGSVCTTRVKTGVGYPQLSAIIECSDAAHGLGGHIIADGGCKVPGDVAKAFGGGADFVML 241
Cdd:TIGR01305 161 GEMVEELILSGADIVKVGIGPGSVCTTRTKTGVGYPQLSAVIECADAAHGLKGHIISDGGCTCPGDVAKAFGAGADFVML 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1030080485 242 GGMFAGHDESGGEIIEENGKKYRTFYGMSSKTAMDKHSGGVAEYRASEGKTVKVAYKGPVSETVKDILGGVRSTCTYVGA 321
Cdd:TIGR01305 241 GGMFAGHTESGGEVIERNGRKFKLFYGMSSDTAMKKHAGGVAEYRASEGKTVEVPYRGDVENTILDILGGLRSACTYVGA 320
|
330 340
....*....|....*....|...
gi 1030080485 322 SKLKELSKRTTFIRVQEQENQVF 344
Cdd:TIGR01305 321 AKLKELSKRATFIRVTQQHNTVF 343
|
|
| IMPDH |
cd00381 |
IMPDH: The catalytic domain of the inosine monophosphate dehydrogenase. IMPDH catalyzes the ... |
9-336 |
2.47e-123 |
|
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: 357.60 E-value: 2.47e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1030080485 9 LGFKDVMFRPKRSTLkSRSEVSLEREFTFKHTKKkwqgTPIIAANMDTVGTFEMAVELAKDKIITAIHKHYSVEEwsdfl 88
Cdd:cd00381 2 LTFDDVLLVPGYSTV-LPSEVDLSTKLTKNITLN----IPLVSAPMDTVTESEMAIAMARLGGIGVIHRNMSIEE----- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1030080485 89 nsQPESIHQ-----YIALSTGTGKADEEKLQQILEKhpKIEFLCIDVANGYSEHFVGFVKKARANFPDKIIIAGNVVTGE 163
Cdd:cd00381 72 --QAEEVRKvkgrlLVGAAVGTREDDKERAEALVEA--GVDVIVIDSAHGHSVYVIEMIKFIKKKYPNVDVIAGNVVTAE 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1030080485 164 MVEELLLVGADIIKVGIGPGSVCTTRVKTGVGYPQLSAIIECSDAAHGLGGHIIADGGCKVPGDVAKAFGGGADFVMLGG 243
Cdd:cd00381 148 AARDLIDAGADGVKVGIGPGSICTTRIVTGVGVPQATAVADVAAAARDYGVPVIADGGIRTSGDIVKALAAGADAVMLGS 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1030080485 244 MFAGHDESGGEIIEENGKKYRTFYGMSSKTAMDKHSG-----GVAEYRASEGKTVKVAYKGPVSETVKDILGGVRSTCTY 318
Cdd:cd00381 228 LLAGTDESPGEYIEINGKRYKEYRGMGSLGAMKKGGGdryfgEEAKKLVPEGVEGIVPYKGSVKDVLPQLVGGLRSSMGY 307
|
330
....*....|....*...
gi 1030080485 319 VGASKLKELSKRTTFIRV 336
Cdd:cd00381 308 CGAKSLKELQEKARFVRI 325
|
|
| GuaB |
COG0516 |
IMP dehydrogenase/GMP reductase [Nucleotide transport and metabolism]; IMP dehydrogenase/GMP ... |
14-336 |
2.06e-91 |
|
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: 276.32 E-value: 2.06e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1030080485 14 VMFRPKRSTLKSRSEVSLEREFTFKHTKKKWQGTPIIAANMDTVGTFEMAVELAKDKIITAIHKHYSVEEWSDFLNSQPE 93
Cdd:COG0516 1 LVLDALRRRLISRSGVVVVVVVGKLTIITTRRRRRDEAVKALVVTTVIEKLLLVTVAGETALLALALLLLKKKKFLLLVD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1030080485 94 SIHQYIALSTGTGKADEEKLQQILEKHPKIEFLCIDVANGYSEHfvGFVKKARANFPDKIIIAGNVVTGEMVEELLLVGA 173
Cdd:COG0516 81 DDGLLLLVLVGVKDDDKEKARALAAADAGVDVLVIDAAHGHSGG--DAMKKIKLTFDDVLLIPGNSATVEPARALVDAGA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1030080485 174 DIIKVGIGPGSVCTTRVKTGVGYPQLSAIIECSDAAHGLgGHIIADGGCKVPGDVAKAFGGGADFVMLGGMFAGHDESGG 253
Cdd:COG0516 159 DLTKVGIGPGSICTTRVVIGLGIPQLSAAMDTVTEARMA-IAIAADGGIGYIHDNAKALAAGADAVMLGSLFAGTEEQPG 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1030080485 254 EIIEENGKKYRTFYGMSSKtamdkhsggvAEYRASEGKTVKVAYKGPVSETVKDILGGVRSTCTYVGASKLKELSKRTTF 333
Cdd:COG0516 238 EVILYQGRSVKRYRGMGSD----------AKKLVPEGIEGRVPYKGPLEDTLHQLLGGLRSGMGYCGARTIEELREKARF 307
|
...
gi 1030080485 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 |
6.58e-81 |
|
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: 253.85 E-value: 6.58e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1030080485 104 GTGKADEEKLQQILEKHpkIEFLCIDVANGYSEHFVGFVKKARANFPDKIIIAGNVVTGEMVEELLLVGADIIKVGIGPG 183
Cdd:pfam00478 216 GVGDDTLERAEALVEAG--VDVLVVDTAHGHSKGVIDTVKWIKKKYPDVQVIAGNVATAEGAKALIEAGADAVKVGIGPG 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1030080485 184 SVCTTRVKTGVGYPQLSAIIECSDAAHGLGGHIIADGGCKVPGDVAKAFGGGADFVMLGGMFAGHDESGGEIIEENGKKY 263
Cdd:pfam00478 294 SICTTRVVAGVGVPQLTAIYDVAEAAKKYGVPVIADGGIKYSGDIVKALAAGADAVMLGSLLAGTDESPGEVILYQGRRY 373
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1030080485 264 RTFYGMSSKTAMDKHS------GGVAEYRASEGKTVKVAYKGPVSETVKDILGGVRSTCTYVGASKLKELSKRTTFIRV 336
Cdd:pfam00478 374 KSYRGMGSLGAMKKGSkdryfqEDDDKKLVPEGVEGRVPYKGPLSDVVYQLVGGLRSGMGYCGAKTIEELREKARFVRI 452
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK05096 |
PRK05096 |
guanosine 5'-monophosphate oxidoreductase; Provisional |
1-344 |
0e+00 |
|
guanosine 5'-monophosphate oxidoreductase; Provisional
Pssm-ID: 235343 [Multi-domain] Cd Length: 346 Bit Score: 715.57 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1030080485 1 MRIEYDIKLGFKDVMFRPKRSTLKSRSEVSLEREFTFKHTKKKWQGTPIIAANMDTVGTFEMAVELAKDKIITAIHKHYS 80
Cdd:PRK05096 1 MRIEEDLKLGFKDVLIRPKRSTLKSRSDVELERQFTFKHSGQSWSGVPIIAANMDTVGTFEMAKALASFDILTAVHKHYS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1030080485 81 VEEWSDFLNSQPESIHQYIALSTGTGKADEEKLQQILEKHPKIEFLCIDVANGYSEHFVGFVKKARANFPDKIIIAGNVV 160
Cdd:PRK05096 81 VEEWAAFVNNSSADVLKHVMVSTGTSDADFEKTKQILALSPALNFICIDVANGYSEHFVQFVAKAREAWPDKTICAGNVV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1030080485 161 TGEMVEELLLVGADIIKVGIGPGSVCTTRVKTGVGYPQLSAIIECSDAAHGLGGHIIADGGCKVPGDVAKAFGGGADFVM 240
Cdd:PRK05096 161 TGEMVEELILSGADIVKVGIGPGSVCTTRVKTGVGYPQLSAVIECADAAHGLGGQIVSDGGCTVPGDVAKAFGGGADFVM 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1030080485 241 LGGMFAGHDESGGEIIEENGKKYRTFYGMSSKTAMDKHSGGVAEYRASEGKTVKVAYKGPVSETVKDILGGVRSTCTYVG 320
Cdd:PRK05096 241 LGGMLAGHEESGGEIVEENGEKFMLFYGMSSESAMKRHVGGVAEYRAAEGKTVKLPLRGPVENTARDILGGLRSACTYVG 320
|
330 340
....*....|....*....|....
gi 1030080485 321 ASKLKELSKRTTFIRVQEQENQVF 344
Cdd:PRK05096 321 ASRLKELTKRTTFIRVQEQENRVF 344
|
|
| 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: 583.42 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1030080485 2 RIEYDIKLGFKDVMFRPKRSTLKSRSEVSLEREFTFKHTKKKWQGTPIIAANMDTVGTFEMAVELAKDKIITAIHKHYSV 81
Cdd:TIGR01305 1 RIEADLKLDFKDVLLRPKRSTLKSRADVELERTFTFRNSKQTYSGVPIIAANMDTVGTFEMAAALSQHSIFTAIHKHYSV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1030080485 82 EEWSDFLNSQPESIHQYIALSTGTGKADEEKLQQILEKHPKIEFLCIDVANGYSEHFVGFVKKARANFPDKIIIAGNVVT 161
Cdd:TIGR01305 81 DEWKAFATNSSPDCLQNVAVSSGSSDNDLEKMTSILEAVPQLKFICLDVANGYSEHFVEFVKLVREAFPEHTIMAGNVVT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1030080485 162 GEMVEELLLVGADIIKVGIGPGSVCTTRVKTGVGYPQLSAIIECSDAAHGLGGHIIADGGCKVPGDVAKAFGGGADFVML 241
Cdd:TIGR01305 161 GEMVEELILSGADIVKVGIGPGSVCTTRTKTGVGYPQLSAVIECADAAHGLKGHIISDGGCTCPGDVAKAFGAGADFVML 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1030080485 242 GGMFAGHDESGGEIIEENGKKYRTFYGMSSKTAMDKHSGGVAEYRASEGKTVKVAYKGPVSETVKDILGGVRSTCTYVGA 321
Cdd:TIGR01305 241 GGMFAGHTESGGEVIERNGRKFKLFYGMSSDTAMKKHAGGVAEYRASEGKTVEVPYRGDVENTILDILGGLRSACTYVGA 320
|
330 340
....*....|....*....|...
gi 1030080485 322 SKLKELSKRTTFIRVQEQENQVF 344
Cdd:TIGR01305 321 AKLKELSKRATFIRVTQQHNTVF 343
|
|
| IMPDH |
cd00381 |
IMPDH: The catalytic domain of the inosine monophosphate dehydrogenase. IMPDH catalyzes the ... |
9-336 |
2.47e-123 |
|
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: 357.60 E-value: 2.47e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1030080485 9 LGFKDVMFRPKRSTLkSRSEVSLEREFTFKHTKKkwqgTPIIAANMDTVGTFEMAVELAKDKIITAIHKHYSVEEwsdfl 88
Cdd:cd00381 2 LTFDDVLLVPGYSTV-LPSEVDLSTKLTKNITLN----IPLVSAPMDTVTESEMAIAMARLGGIGVIHRNMSIEE----- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1030080485 89 nsQPESIHQ-----YIALSTGTGKADEEKLQQILEKhpKIEFLCIDVANGYSEHFVGFVKKARANFPDKIIIAGNVVTGE 163
Cdd:cd00381 72 --QAEEVRKvkgrlLVGAAVGTREDDKERAEALVEA--GVDVIVIDSAHGHSVYVIEMIKFIKKKYPNVDVIAGNVVTAE 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1030080485 164 MVEELLLVGADIIKVGIGPGSVCTTRVKTGVGYPQLSAIIECSDAAHGLGGHIIADGGCKVPGDVAKAFGGGADFVMLGG 243
Cdd:cd00381 148 AARDLIDAGADGVKVGIGPGSICTTRIVTGVGVPQATAVADVAAAARDYGVPVIADGGIRTSGDIVKALAAGADAVMLGS 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1030080485 244 MFAGHDESGGEIIEENGKKYRTFYGMSSKTAMDKHSG-----GVAEYRASEGKTVKVAYKGPVSETVKDILGGVRSTCTY 318
Cdd:cd00381 228 LLAGTDESPGEYIEINGKRYKEYRGMGSLGAMKKGGGdryfgEEAKKLVPEGVEGIVPYKGSVKDVLPQLVGGLRSSMGY 307
|
330
....*....|....*...
gi 1030080485 319 VGASKLKELSKRTTFIRV 336
Cdd:cd00381 308 CGAKSLKELQEKARFVRI 325
|
|
| GuaB |
COG0516 |
IMP dehydrogenase/GMP reductase [Nucleotide transport and metabolism]; IMP dehydrogenase/GMP ... |
14-336 |
2.06e-91 |
|
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: 276.32 E-value: 2.06e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1030080485 14 VMFRPKRSTLKSRSEVSLEREFTFKHTKKKWQGTPIIAANMDTVGTFEMAVELAKDKIITAIHKHYSVEEWSDFLNSQPE 93
Cdd:COG0516 1 LVLDALRRRLISRSGVVVVVVVGKLTIITTRRRRRDEAVKALVVTTVIEKLLLVTVAGETALLALALLLLKKKKFLLLVD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1030080485 94 SIHQYIALSTGTGKADEEKLQQILEKHPKIEFLCIDVANGYSEHfvGFVKKARANFPDKIIIAGNVVTGEMVEELLLVGA 173
Cdd:COG0516 81 DDGLLLLVLVGVKDDDKEKARALAAADAGVDVLVIDAAHGHSGG--DAMKKIKLTFDDVLLIPGNSATVEPARALVDAGA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1030080485 174 DIIKVGIGPGSVCTTRVKTGVGYPQLSAIIECSDAAHGLgGHIIADGGCKVPGDVAKAFGGGADFVMLGGMFAGHDESGG 253
Cdd:COG0516 159 DLTKVGIGPGSICTTRVVIGLGIPQLSAAMDTVTEARMA-IAIAADGGIGYIHDNAKALAAGADAVMLGSLFAGTEEQPG 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1030080485 254 EIIEENGKKYRTFYGMSSKtamdkhsggvAEYRASEGKTVKVAYKGPVSETVKDILGGVRSTCTYVGASKLKELSKRTTF 333
Cdd:COG0516 238 EVILYQGRSVKRYRGMGSD----------AKKLVPEGIEGRVPYKGPLEDTLHQLLGGLRSGMGYCGARTIEELREKARF 307
|
...
gi 1030080485 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 |
6.58e-81 |
|
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: 253.85 E-value: 6.58e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1030080485 104 GTGKADEEKLQQILEKHpkIEFLCIDVANGYSEHFVGFVKKARANFPDKIIIAGNVVTGEMVEELLLVGADIIKVGIGPG 183
Cdd:pfam00478 216 GVGDDTLERAEALVEAG--VDVLVVDTAHGHSKGVIDTVKWIKKKYPDVQVIAGNVATAEGAKALIEAGADAVKVGIGPG 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1030080485 184 SVCTTRVKTGVGYPQLSAIIECSDAAHGLGGHIIADGGCKVPGDVAKAFGGGADFVMLGGMFAGHDESGGEIIEENGKKY 263
Cdd:pfam00478 294 SICTTRVVAGVGVPQLTAIYDVAEAAKKYGVPVIADGGIKYSGDIVKALAAGADAVMLGSLLAGTDESPGEVILYQGRRY 373
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1030080485 264 RTFYGMSSKTAMDKHS------GGVAEYRASEGKTVKVAYKGPVSETVKDILGGVRSTCTYVGASKLKELSKRTTFIRV 336
Cdd:pfam00478 374 KSYRGMGSLGAMKKGSkdryfqEDDDKKLVPEGVEGRVPYKGPLSDVVYQLVGGLRSGMGYCGAKTIEELREKARFVRI 452
|
|
| IMP_dehydrog |
TIGR01302 |
inosine-5'-monophosphate dehydrogenase; This model describes IMP dehydrogenase, an enzyme of ... |
99-327 |
5.30e-66 |
|
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: 214.90 E-value: 5.30e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1030080485 99 IALSTGTGKADEEKLQQILEKhpKIEFLCIDVANGYSEHFVGFVKKARANFPDKIIIAGNVVTGEMVEELLLVGADIIKV 178
Cdd:TIGR01302 215 VGAAVGTREFDKERAEALVKA--GVDVIVIDSSHGHSIYVIDSIKEIKKTYPDLDIIAGNVATAEQAKALIDAGADGLRV 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1030080485 179 GIGPGSVCTTRVKTGVGYPQLSAIIECSDAAHGLGGHIIADGGCKVPGDVAKAFGGGADFVMLGGMFAGHDESGGEIIEE 258
Cdd:TIGR01302 293 GIGPGSICTTRIVAGVGVPQITAVYDVAEYAAQSGIPVIADGGIRYSGDIVKALAAGADAVMLGSLLAGTTESPGEYEII 372
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1030080485 259 NGKKYRTFYGMSSKTAMDKHSGG-------VAEYRASEGKTVKVAYKGPVSETVKDILGGVRSTCTYVGASKLKEL 327
Cdd:TIGR01302 373 NGRRYKQYRGMGSLGAMTKGSSDrylqdenKTKKFVPEGVEGAVPYKGSVLELLPQLVGGLKSGMGYVGARSIDEL 448
|
|
| PTZ00314 |
PTZ00314 |
inosine-5'-monophosphate dehydrogenase; Provisional |
98-337 |
9.31e-62 |
|
inosine-5'-monophosphate dehydrogenase; Provisional
Pssm-ID: 240355 [Multi-domain] Cd Length: 495 Bit Score: 204.82 E-value: 9.31e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1030080485 98 YIALSTGTGKADEEKLQQILEKhpKIEFLCIDVANGYSEHFVGFVKKARANFPDKIIIAGNVVTGEMVEELLLVGADIIK 177
Cdd:PTZ00314 231 LVGAAISTRPEDIERAAALIEA--GVDVLVVDSSQGNSIYQIDMIKKLKSNYPHVDIIAGNVVTADQAKNLIDAGADGLR 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1030080485 178 VGIGPGSVCTTRVKTGVGYPQLSAIIECSDAAHGLGGHIIADGGCKVPGDVAKAFGGGADFVMLGGMFAGHDESGGEIIE 257
Cdd:PTZ00314 309 IGMGSGSICITQEVCAVGRPQASAVYHVARYARERGVPCIADGGIKNSGDICKALALGADCVMLGSLLAGTEEAPGEYFF 388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1030080485 258 ENGKKYRTFYGMSSKTAM-DKHSGG-----VAEYRASEGKTVKVAYKGPVSETVKDILGGVRSTCTYVGASKLKELSKRT 331
Cdd:PTZ00314 389 KDGVRLKVYRGMGSLEAMlSKESGEryldeNETIKVAQGVSGSVVDKGSVAKLIPYLVKGVKHGMQYIGAHSIPELHEKL 468
|
....*.
gi 1030080485 332 TFIRVQ 337
Cdd:PTZ00314 469 YSGQVR 474
|
|
| PRK05458 |
PRK05458 |
guanosine 5'-monophosphate oxidoreductase; Provisional |
11-329 |
1.50e-60 |
|
guanosine 5'-monophosphate oxidoreductase; Provisional
Pssm-ID: 235479 [Multi-domain] Cd Length: 326 Bit Score: 197.10 E-value: 1.50e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1030080485 11 FKDVMFRPKRSTLKSRSEVSLEREF---TFKhtkkkwqgTPIIAANMDTVGTFEMAVELAKDKIITAIHKhYSVEEWSDF 87
Cdd:PRK05458 7 YEDIQLIPNKCIVNSRSECDTSVTLgprTFK--------LPVVPANMQTIIDEKIAEWLAENGYFYIMHR-FDPEARIPF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1030080485 88 LnsqpESIHQ---YIALSTGTGKADEEKLQQILEKHPKIEFLCIDVANGYSEHFVGFVKKARANFPDKIIIAGNVVTGEM 164
Cdd:PRK05458 78 I----KDMHEqglIASISVGVKDDEYDFVDQLAAEGLTPEYITIDIAHGHSDSVINMIQHIKKHLPETFVIAGNVGTPEA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1030080485 165 VEELLLVGADIIKVGIGPGSVCTTRVKTGVGYP--QLSAIIECSDAAHglgGHIIADGGCKVPGDVAKAFGGGADFVMLG 242
Cdd:PRK05458 154 VRELENAGADATKVGIGPGKVCITKIKTGFGTGgwQLAALRWCAKAAR---KPIIADGGIRTHGDIAKSIRFGATMVMIG 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1030080485 243 GMFAGHDESGGEIIEENGKKYRTFYGmsskTAMDKHSGgvaEYRASEGKTVKVAYKGPVSETVKDILGGVRSTCTYVGAS 322
Cdd:PRK05458 231 SLFAGHEESPGKTVEIDGKLYKEYFG----SASEFQKG---EYKNVEGKKILVPHKGSLKDTLTEMEQDLQSSISYAGGR 303
|
....*..
gi 1030080485 323 KLKELSK 329
Cdd:PRK05458 304 DLDAIRK 310
|
|
| PRK06843 |
PRK06843 |
inosine 5-monophosphate dehydrogenase; Validated |
9-336 |
7.06e-60 |
|
inosine 5-monophosphate dehydrogenase; Validated
Pssm-ID: 180725 [Multi-domain] Cd Length: 404 Bit Score: 197.57 E-value: 7.06e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1030080485 9 LGFKDVMFRPKRSTLKSrSEVSLEREFTfkhtKKKWQGTPIIAANMDTVGTFEMAVELAKDKIITAIHKHYSVE------ 82
Cdd:PRK06843 10 LTFDDVSLIPRKSSVLP-SEVSLKTQLT----KNISLNIPFLSSAMDTVTESQMAIAIAKEGGIGIIHKNMSIEaqrkei 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1030080485 83 ------EWSDFLNSQPESIHQYIALSTGTGKADE-------------------------------------EKLQQILEK 119
Cdd:PRK06843 85 ekvktyKFQKTINTNGDTNEQKPEIFTAKQHLEKsdayknaehkedfpnackdlnnklrvgaavsididtiERVEELVKA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1030080485 120 HpkIEFLCIDVANGYSEHFVGFVKKARANFPDKIIIAGNVVTGEMVEELLLVGADIIKVGIGPGSVCTTRVKTGVGYPQL 199
Cdd:PRK06843 165 H--VDILVIDSAHGHSTRIIELVKKIKTKYPNLDLIAGNIVTKEAALDLISVGADCLKVGIGPGSICTTRIVAGVGVPQI 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1030080485 200 SAIIECSDAAHGLGGHIIADGGCKVPGDVAKAFGGGADFVMLGGMFAGHDESGGEIIEENGKKYRTFYGMSSKTAMDKhs 279
Cdd:PRK06843 243 TAICDVYEVCKNTNICIIADGGIRFSGDVVKAIAAGADSVMIGNLFAGTKESPSEEIIYNGKKFKSYVGMGSISAMKR-- 320
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1030080485 280 GGVAEYRASEG----KTVKVAYKG--PVSETVKDIL----GGVRSTCTYVGASKLKELSKRTTFIRV 336
Cdd:PRK06843 321 GSKSRYFQLENnepkKLVPEGIEGmvPYSGKLKDILtqlkGGLMSGMGYLGAATISDLKINSKFVKI 387
|
|
| PRK07807 |
PRK07807 |
GuaB1 family IMP dehydrogenase-related protein; |
126-330 |
9.58e-59 |
|
GuaB1 family IMP dehydrogenase-related protein;
Pssm-ID: 181127 [Multi-domain] Cd Length: 479 Bit Score: 196.66 E-value: 9.58e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1030080485 126 LCIDVANGYSEHFVGFVKKARANFPDKIIIAGNVVTGEMVEELLLVGADIIKVGIGPGSVCTTRVKTGVGYPQLSAIIEC 205
Cdd:PRK07807 243 LVVDTAHGHQEKMLEALRAVRALDPGVPIVAGNVVTAEGTRDLVEAGADIVKVGVGPGAMCTTRMMTGVGRPQFSAVLEC 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1030080485 206 SDAAHGLGGHIIADGGCKVPGDVAKAFGGGADFVMLGGMFAGHDESGGEI-IEENGKKYRTFYGMSSKTAMDKHSGGVAE 284
Cdd:PRK07807 323 AAAARELGAHVWADGGVRHPRDVALALAAGASNVMIGSWFAGTYESPGDLmRDRDGRPYKESFGMASARAVAARTAGDSA 402
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1030080485 285 Y-RA-----SEGKTVKVAYKGPVSETVKDIL----GGVRSTCTYVGASKLKELSKR 330
Cdd:PRK07807 403 FdRArkalfEEGISTSRMYLDPGRPGVEDLLdhitSGVRSSCTYAGARTLAEFHER 458
|
|
| IMP_DH_rel_1 |
TIGR01303 |
IMP dehydrogenase family protein; This model represents a family of proteins, often annotated ... |
99-332 |
8.25e-57 |
|
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: 191.66 E-value: 8.25e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1030080485 99 IALSTGTGKADEEKLQQILEKhpKIEFLCIDVANGYSEHFVGFVKKARANFPDKIIIAGNVVTGEMVEELLLVGADIIKV 178
Cdd:TIGR01303 216 IGAAVGINGDVGGKAKALLDA--GVDVLVIDTAHGHQVKMISAIKAVRALDLGVPIVAGNVVSAEGVRDLLEAGANIIKV 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1030080485 179 GIGPGSVCTTRVKTGVGYPQLSAIIECSDAAHGLGGHIIADGGCKVPGDVAKAFGGGADFVMLGGMFAGHDESGGEII-E 257
Cdd:TIGR01303 294 GVGPGAMCTTRMMTGVGRPQFSAVLECAAEARKLGGHVWADGGVRHPRDVALALAAGASNVMVGSWFAGTYESPGDLMrD 373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1030080485 258 ENGKKYRTFYGMSSKTAMDKHSGGVAEY-RA-----SEGKTVKVAY----KGPVSETVKDILGGVRSTCTYVGASKLKEL 327
Cdd:TIGR01303 374 RDGRPYKESFGMASKRAVVARTGADNAFdRArkalfEEGISTSRMGldpdRGGVEDLIDHIISGVRSSCTYAGASSLEEF 453
|
....*
gi 1030080485 328 SKRTT 332
Cdd:TIGR01303 454 HERAV 458
|
|
| PLN02274 |
PLN02274 |
inosine-5'-monophosphate dehydrogenase |
102-326 |
2.27e-34 |
|
inosine-5'-monophosphate dehydrogenase
Pssm-ID: 215154 [Multi-domain] Cd Length: 505 Bit Score: 131.71 E-value: 2.27e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1030080485 102 STGTGKADEEKLQQILEKhpKIEFLCIDVANGYSEHFVGFVKKARANFPDKIIIAGNVVTGEMVEELLLVGADIIKVGIG 181
Cdd:PLN02274 242 AIGTRESDKERLEHLVKA--GVDVVVLDSSQGDSIYQLEMIKYIKKTYPELDVIGGNVVTMYQAQNLIQAGVDGLRVGMG 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1030080485 182 PGSVCTTRVKTGVGYPQLSAIIECSDAAHGLGGHIIADGGCKVPGDVAKAFGGGADFVMLGGMFAGHDESGGEIIEENG- 260
Cdd:PLN02274 320 SGSICTTQEVCAVGRGQATAVYKVASIAAQHGVPVIADGGISNSGHIVKALTLGASTVMMGSFLAGTTEAPGEYFYQDGv 399
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1030080485 261 --KKYRtfyGMSSKTAMDKHS-----GGVAEYRASEGKTVKVAYKGPVSETVKDILGGVRSTCTYVGASKLKE 326
Cdd:PLN02274 400 rvKKYR---GMGSLEAMTKGSdqrylGDTAKLKIAQGVSGAVADKGSVLKFVPYTMQAVKQGFQDLGASSLQS 469
|
|
| PRK07107 |
PRK07107 |
IMP dehydrogenase; |
126-336 |
4.22e-31 |
|
IMP dehydrogenase;
Pssm-ID: 180842 [Multi-domain] Cd Length: 502 Bit Score: 122.50 E-value: 4.22e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1030080485 126 LCIDVANGYSEHFVGFVKKARANFPDKIII-AGNVVTGEMVEELLLVGADIIKVGIGPGSVCTTRVKTGVGYPQLSAIIE 204
Cdd:PRK07107 258 LCIDSSEGYSEWQKRTLDWIREKYGDSVKVgAGNVVDREGFRYLAEAGADFVKVGIGGGSICITREQKGIGRGQATALIE 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1030080485 205 CSDA------AHGLGGHIIADGGCKVPGDVAKAFGGGADFVMLGGMFAGHDESGGEIIEENGKKYRTFYGMSSKTAMD-- 276
Cdd:PRK07107 338 VAKArdeyfeETGVYIPICSDGGIVYDYHMTLALAMGADFIMLGRYFARFDESPTNKVNINGNYMKEYWGEGSNRARNwq 417
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1030080485 277 -KHSGGVAEYRASEGKTVKVAYKGPVSETVKDILGGVRSTCTYVGASKLKELSKRTTFIRV 336
Cdd:PRK07107 418 rYDLGGDKKLSFEEGVDSYVPYAGSLKDNVAITLSKVRSTMCNCGALSIPELQQKAKITLV 478
|
|
| IMP_DH_rel_2 |
TIGR01304 |
IMP dehydrogenase family protein; This model represents a family of proteins, often annotated ... |
154-329 |
5.14e-15 |
|
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. Most species with a member of this family belong to the high GC Gram-positive bacteria, and these also have the IMP dehydrogenase described by TIGRFAMs equivalog model TIGR01302. [Unknown function, General]
Pssm-ID: 273547 [Multi-domain] Cd Length: 369 Bit Score: 75.26 E-value: 5.14e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1030080485 154 IIAGNVVTGEMVEELLLVGAdiIKVGIGPGSVCTTRVKTGVGYPQLSAIIECS----DAAHGLGG---HIIADGGCKVPG 226
Cdd:TIGR01304 191 VIAGGVNDYTTALHLMRTGA--AGVIVGPGGANTTRLVLGIEVPMATAIADVAaarrDYLDETGGryvHVIADGGIETSG 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1030080485 227 DVAKAFGGGADFVMLGGMFAGHDESGGEiieengkkyRTFYGMSSKTAMDKHSGGVAEYRASEGKTVKVAYKGPVSET-- 304
Cdd:TIGR01304 269 DLVKAIACGADAVVLGSPLARAAEAPGR---------GYFWPAAAAHPRLPRGVVTESGTVGEAPTLEEILHGPSTLPdg 339
|
170 180
....*....|....*....|....*
gi 1030080485 305 VKDILGGVRSTCTYVGASKLKELSK 329
Cdd:TIGR01304 340 VENFEGGLKRAMAKCGYTDLKEFQK 364
|
|
| LldD |
COG1304 |
FMN-dependent dehydrogenase, includes L-lactate dehydrogenase and type II isopentenyl ... |
142-242 |
4.22e-04 |
|
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: 41.66 E-value: 4.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1030080485 142 VKKARANFPDKIIIAGnVVTGEMVEELLLVGADIIKV----GigpgsvctTRVKTGVgyPQLSAIIECSDAAHGlGGHII 217
Cdd:COG1304 217 IAWLRERWPGPLIVKG-VLSPEDARRAVDAGVDGIDVsnhgG--------RQLDGGP--PTIDALPEIRAAVGG-RIPVI 284
|
90 100
....*....|....*....|....*
gi 1030080485 218 ADGGCKVPGDVAKAFGGGADFVMLG 242
Cdd:COG1304 285 ADGGIRRGLDVAKALALGADAVGLG 309
|
|
| TIM_phosphate_binding |
cd04722 |
TIM barrel proteins share a structurally conserved phosphate binding motif and in general ... |
128-243 |
2.36e-03 |
|
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: 38.72 E-value: 2.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1030080485 128 IDVANGYS-EHFVGFVKKARANFPDKIIIAGNVVTGEMVEELLLV-GADIIKVGIGPGsvcTTRVKTGVGYPQLSAIIec 205
Cdd:cd04722 90 IHGAVGYLaREDLELIRELREAVPDVKVVVKLSPTGELAAAAAEEaGVDEVGLGNGGG---GGGGRDAVPIADLLLIL-- 164
|
90 100 110
....*....|....*....|....*....|....*...
gi 1030080485 206 sdAAHGLGGHIIADGGCKVPGDVAKAFGGGADFVMLGG 243
Cdd:cd04722 165 --AKRGSKVPVIAGGGINDPEDAAEALALGADGVIVGS 200
|
|
| GltS_FMN |
cd02808 |
Glutamate synthase (GltS) FMN-binding domain. GltS is a complex iron-sulfur flavoprotein that ... |
216-245 |
3.51e-03 |
|
Glutamate synthase (GltS) FMN-binding domain. GltS is a complex iron-sulfur flavoprotein that catalyzes the reductive synthesis of L-glutamate from 2-oxoglutarate and L-glutamine via intramolecular channelling of ammonia, a reaction in the plant, yeast and bacterial pathway for ammonia assimilation. It is a multifunctional enzyme that functions through three distinct active centers, carrying out L-glutamine hydrolysis, conversion of 2-oxoglutarate into L-glutamate, and electron uptake from an electron donor.
Pssm-ID: 239202 [Multi-domain] Cd Length: 392 Bit Score: 39.06 E-value: 3.51e-03
10 20 30
....*....|....*....|....*....|
gi 1030080485 216 IIADGGCKVPGDVAKAFGGGADFVMLGGMF 245
Cdd:cd02808 288 LIASGGLRTGADVAKALALGADAVGIGTAA 317
|
|
| KDPG_aldolase |
cd00452 |
KDPG and KHG aldolase; KDPG and KHG aldolase. This family belongs to the class I adolases ... |
141-241 |
4.16e-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: 37.88 E-value: 4.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1030080485 141 FVKKARANFPDKIIIAGNVVTGEMVEELLLVGADIIkvgIGPGSVcttrvktgvgypqlsaiIECSDAAHGLGGHIIAdg 220
Cdd:cd00452 45 AIRALRKEFPEALIGAGTVLTPEQADAAIAAGAQFI---VSPGLD-----------------PEVVKAANRAGIPLLP-- 102
|
90 100
....*....|....*....|.
gi 1030080485 221 GCKVPGDVAKAFGGGADFVML 241
Cdd:cd00452 103 GVATPTEIMQALELGADIVKL 123
|
|
| KGPDC_HPS |
cd04726 |
3-Keto-L-gulonate 6-phosphate decarboxylase (KGPDC) and D-arabino-3-hexulose-6-phosphate ... |
142-302 |
9.22e-03 |
|
3-Keto-L-gulonate 6-phosphate decarboxylase (KGPDC) and D-arabino-3-hexulose-6-phosphate synthase (HPS). KGPDC catalyzes the formation of L-xylulose 5-phosphate and carbon dioxide from 3-keto-L-gulonate 6-phosphate as part of the anaerobic pathway for L-ascorbate utilization in some eubacteria. HPS catalyzes the formation of D-arabino-3-hexulose-6-phosphate from D-ribulose 5-phosphate and formaldehyde in microorganisms that can use formaldehyde as a carbon source. Both catalyze reactions that involve the Mg2+-assisted formation and stabilization of 1,2-enediolate reaction intermediates.
Pssm-ID: 240077 [Multi-domain] Cd Length: 202 Bit Score: 36.79 E-value: 9.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1030080485 142 VKKARANFPDKIIIA-------GNVVTgEMVEElllVGADIIKV-GIGPgsvcttrvktgvgypqLSAIIECSDAAHGLG 213
Cdd:cd04726 44 VRALREAFPDKIIVAdlktadaGALEA-EMAFK---AGADIVTVlGAAP----------------LSTIKKAVKAAKKYG 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1030080485 214 GHIIAD-GGCKVPGDVAKAFGGGADFVmlgGMFAGHDESGGEIIEENGKKYRTFYGMSSKTAMdkhSGGVAEyrasegKT 292
Cdd:cd04726 104 KEVQVDlIGVEDPEKRAKLLKLGVDIV---ILHRGIDAQAAGGWWPEDDLKKVKKLLGVKVAV---AGGITP------DT 171
|
170
....*....|
gi 1030080485 293 VKVAYKGPVS 302
Cdd:cd04726 172 LPEFKKAGAD 181
|
|
| |
