|
Name |
Accession |
Description |
Interval |
E-value |
| GMP_reduct_1 |
TIGR01305 |
guanosine monophosphate reductase, eukaryotic; A deep split separates two families of GMP ... |
3-344 |
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: 692.43 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156104880 3 RIDADLKLDFKDVLLRPKRSSLKSRAEVDLERTFTFRNSKQTYSGIPIIVANMDTVGTFEMAAVMSQHSMFTAIHKHYSL 82
Cdd:TIGR01305 1 RIEADLKLDFKDVLLRPKRSTLKSRADVELERTFTFRNSKQTYSGVPIIAANMDTVGTFEMAAALSQHSIFTAIHKHYSV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156104880 83 DDWKLFATN-HPECLQNVAVSSGSGQNDLEKMTSILEAVPQVKFICLDVANGYSEHFVEFVKLVRAKFPEHTIMAGNVVT 161
Cdd:TIGR01305 81 DEWKAFATNsSPDCLQNVAVSSGSSDNDLEKMTSILEAVPQLKFICLDVANGYSEHFVEFVKLVREAFPEHTIMAGNVVT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156104880 162 GEMVEELILSGADIIKVGVGPGSVCTTRTKTGVGYPQLSAVIECADSAHGLKGHIISDGGCTCPGDVAKAFGAGADFVML 241
Cdd:TIGR01305 161 GEMVEELILSGADIVKVGIGPGSVCTTRTKTGVGYPQLSAVIECADAAHGLKGHIISDGGCTCPGDVAKAFGAGADFVML 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156104880 242 GGMFSGHTECAGEVFERNGRKLKLFYGMSSDTAMNKHAGGVAEYRASEGKTVEVPYKGDVENTILDILGGLRSTCTYVGA 321
Cdd:TIGR01305 241 GGMFAGHTESGGEVIERNGRKFKLFYGMSSDTAMKKHAGGVAEYRASEGKTVEVPYRGDVENTILDILGGLRSACTYVGA 320
|
330 340
....*....|....*....|...
gi 156104880 322 AKLKELSRRATFIRVTQQHNTVF 344
Cdd:TIGR01305 321 AKLKELSKRATFIRVTQQHNTVF 343
|
|
| PRK05096 |
PRK05096 |
guanosine 5'-monophosphate oxidoreductase; Provisional |
3-345 |
0e+00 |
|
guanosine 5'-monophosphate oxidoreductase; Provisional
Pssm-ID: 235343 [Multi-domain] Cd Length: 346 Bit Score: 673.96 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156104880 3 RIDADLKLDFKDVLLRPKRSSLKSRAEVDLERTFTFRNSKQTYSGIPIIVANMDTVGTFEMAAVMSQHSMFTAIHKHYSL 82
Cdd:PRK05096 2 RIEEDLKLGFKDVLIRPKRSTLKSRSDVELERQFTFKHSGQSWSGVPIIAANMDTVGTFEMAKALASFDILTAVHKHYSV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156104880 83 DDWKLFATNHP-ECLQNVAVSSGSGQNDLEKMTSILEAVPQVKFICLDVANGYSEHFVEFVKLVRAKFPEHTIMAGNVVT 161
Cdd:PRK05096 82 EEWAAFVNNSSaDVLKHVMVSTGTSDADFEKTKQILALSPALNFICIDVANGYSEHFVQFVAKAREAWPDKTICAGNVVT 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156104880 162 GEMVEELILSGADIIKVGVGPGSVCTTRTKTGVGYPQLSAVIECADSAHGLKGHIISDGGCTCPGDVAKAFGAGADFVML 241
Cdd:PRK05096 162 GEMVEELILSGADIVKVGIGPGSVCTTRVKTGVGYPQLSAVIECADAAHGLGGQIVSDGGCTVPGDVAKAFGGGADFVML 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156104880 242 GGMFSGHTECAGEVFERNGRKLKLFYGMSSDTAMNKHAGGVAEYRASEGKTVEVPYKGDVENTILDILGGLRSTCTYVGA 321
Cdd:PRK05096 242 GGMLAGHEESGGEIVEENGEKFMLFYGMSSESAMKRHVGGVAEYRAAEGKTVKLPLRGPVENTARDILGGLRSACTYVGA 321
|
330 340
....*....|....*....|....
gi 156104880 322 AKLKELSRRATFIRVTQQHNTVFS 345
Cdd:PRK05096 322 SRLKELTKRTTFIRVQEQENRVFN 345
|
|
| IMPDH |
cd00381 |
IMPDH: The catalytic domain of the inosine monophosphate dehydrogenase. IMPDH catalyzes the ... |
10-336 |
2.80e-127 |
|
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: 367.23 E-value: 2.80e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156104880 10 LDFKDVLLRPKRSSLkSRAEVDLERTFTfrnsKQTYSGIPIIVANMDTVGTFEMAAVMSQHSMFTAIHKHYSLDDWKLFA 89
Cdd:cd00381 2 LTFDDVLLVPGYSTV-LPSEVDLSTKLT----KNITLNIPLVSAPMDTVTESEMAIAMARLGGIGVIHRNMSIEEQAEEV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156104880 90 TNHPECLQnVAVSSGSGQNDLEKMTSILEAVPQVkfICLDVANGYSEHFVEFVKLVRAKFPEHTIMAGNVVTGEMVEELI 169
Cdd:cd00381 77 RKVKGRLL-VGAAVGTREDDKERAEALVEAGVDV--IVIDSAHGHSVYVIEMIKFIKKKYPNVDVIAGNVVTAEAARDLI 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156104880 170 LSGADIIKVGVGPGSVCTTRTKTGVGYPQLSAVIECADSAHGLKGHIISDGGCTCPGDVAKAFGAGADFVMLGGMFSGHT 249
Cdd:cd00381 154 DAGADGVKVGIGPGSICTTRIVTGVGVPQATAVADVAAAARDYGVPVIADGGIRTSGDIVKALAAGADAVMLGSLLAGTD 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156104880 250 ECAGEVFERNGRKLKLFYGMSSDTAMNKHAG-----GVAEYRASEGKTVEVPYKGDVENTILDILGGLRSTCTYVGAAKL 324
Cdd:cd00381 234 ESPGEYIEINGKRYKEYRGMGSLGAMKKGGGdryfgEEAKKLVPEGVEGIVPYKGSVKDVLPQLVGGLRSSMGYCGAKSL 313
|
330
....*....|..
gi 156104880 325 KELSRRATFIRV 336
Cdd:cd00381 314 KELQEKARFVRI 325
|
|
| GuaB |
COG0516 |
IMP dehydrogenase/GMP reductase [Nucleotide transport and metabolism]; IMP dehydrogenase/GMP ... |
15-337 |
9.43e-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: 264.38 E-value: 9.43e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156104880 15 VLLRPKRSSLKSRAEVDLERTFTFRNSKQTYSGIPIIVANMDTVGTFEMAAVMSQHSMFTAIHKHYSLDDWKL-FATNHP 93
Cdd:COG0516 1 LVLDALRRRLISRSGVVVVVVVGKLTIITTRRRRRDEAVKALVVTTVIEKLLLVTVAGETALLALALLLLKKKkFLLLVD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156104880 94 ECLQNVAVSSGSGQNDLEKMTSILEAVPQVKFICLDVANGYSEHfvEFVKLVRAKFPEHTIMAGNVVTGEMVEELILSGA 173
Cdd:COG0516 81 DDGLLLLVLVGVKDDDKEKARALAAADAGVDVLVIDAAHGHSGG--DAMKKIKLTFDDVLLIPGNSATVEPARALVDAGA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156104880 174 DIIKVGVGPGSVCTTRTKTGVGYPQLSAVIECADSAHGLKgHIISDGGCTCPGDVAKAFGAGADFVMLGGMFSGHTECAG 253
Cdd:COG0516 159 DLTKVGIGPGSICTTRVVIGLGIPQLSAAMDTVTEARMAI-AIAADGGIGYIHDNAKALAAGADAVMLGSLFAGTEEQPG 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156104880 254 EVFERNGRKLKLFYGMSSDtamnkhaggvAEYRASEGKTVEVPYKGDVENTILDILGGLRSTCTYVGAAKLKELSRRATF 333
Cdd:COG0516 238 EVILYQGRSVKRYRGMGSD----------AKKLVPEGIEGRVPYKGPLEDTLHQLLGGLRSGMGYCGARTIEELREKARF 307
|
....
gi 156104880 334 IRVT 337
Cdd:COG0516 308 VRIT 311
|
|
| IMPDH |
pfam00478 |
IMP dehydrogenase / GMP reductase domain; This family is involved in biosynthesis of guanosine ... |
99-338 |
1.83e-78 |
|
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: 247.30 E-value: 1.83e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156104880 99 VAVSSGSGQNDLEKMTSILEAvpQVKFICLDVANGYSEHFVEFVKLVRAKFPEHTIMAGNVVTGEMVEELILSGADIIKV 178
Cdd:pfam00478 211 VGAAVGVGDDTLERAEALVEA--GVDVLVVDTAHGHSKGVIDTVKWIKKKYPDVQVIAGNVATAEGAKALIEAGADAVKV 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156104880 179 GVGPGSVCTTRTKTGVGYPQLSAVIECADSAHGLKGHIISDGGCTCPGDVAKAFGAGADFVMLGGMFSGHTECAGEVFER 258
Cdd:pfam00478 289 GIGPGSICTTRVVAGVGVPQLTAIYDVAEAAKKYGVPVIADGGIKYSGDIVKALAAGADAVMLGSLLAGTDESPGEVILY 368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156104880 259 NGRKLKLFYGMSSDTAMNKHA------GGVAEYRASEGktVE--VPYKGDVENTILDILGGLRSTCTYVGAAKLKELSRR 330
Cdd:pfam00478 369 QGRRYKSYRGMGSLGAMKKGSkdryfqEDDDKKLVPEG--VEgrVPYKGPLSDVVYQLVGGLRSGMGYCGAKTIEELREK 446
|
....*...
gi 156104880 331 ATFIRVTQ 338
Cdd:pfam00478 447 ARFVRITA 454
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| GMP_reduct_1 |
TIGR01305 |
guanosine monophosphate reductase, eukaryotic; A deep split separates two families of GMP ... |
3-344 |
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: 692.43 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156104880 3 RIDADLKLDFKDVLLRPKRSSLKSRAEVDLERTFTFRNSKQTYSGIPIIVANMDTVGTFEMAAVMSQHSMFTAIHKHYSL 82
Cdd:TIGR01305 1 RIEADLKLDFKDVLLRPKRSTLKSRADVELERTFTFRNSKQTYSGVPIIAANMDTVGTFEMAAALSQHSIFTAIHKHYSV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156104880 83 DDWKLFATN-HPECLQNVAVSSGSGQNDLEKMTSILEAVPQVKFICLDVANGYSEHFVEFVKLVRAKFPEHTIMAGNVVT 161
Cdd:TIGR01305 81 DEWKAFATNsSPDCLQNVAVSSGSSDNDLEKMTSILEAVPQLKFICLDVANGYSEHFVEFVKLVREAFPEHTIMAGNVVT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156104880 162 GEMVEELILSGADIIKVGVGPGSVCTTRTKTGVGYPQLSAVIECADSAHGLKGHIISDGGCTCPGDVAKAFGAGADFVML 241
Cdd:TIGR01305 161 GEMVEELILSGADIVKVGIGPGSVCTTRTKTGVGYPQLSAVIECADAAHGLKGHIISDGGCTCPGDVAKAFGAGADFVML 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156104880 242 GGMFSGHTECAGEVFERNGRKLKLFYGMSSDTAMNKHAGGVAEYRASEGKTVEVPYKGDVENTILDILGGLRSTCTYVGA 321
Cdd:TIGR01305 241 GGMFAGHTESGGEVIERNGRKFKLFYGMSSDTAMKKHAGGVAEYRASEGKTVEVPYRGDVENTILDILGGLRSACTYVGA 320
|
330 340
....*....|....*....|...
gi 156104880 322 AKLKELSRRATFIRVTQQHNTVF 344
Cdd:TIGR01305 321 AKLKELSKRATFIRVTQQHNTVF 343
|
|
| PRK05096 |
PRK05096 |
guanosine 5'-monophosphate oxidoreductase; Provisional |
3-345 |
0e+00 |
|
guanosine 5'-monophosphate oxidoreductase; Provisional
Pssm-ID: 235343 [Multi-domain] Cd Length: 346 Bit Score: 673.96 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156104880 3 RIDADLKLDFKDVLLRPKRSSLKSRAEVDLERTFTFRNSKQTYSGIPIIVANMDTVGTFEMAAVMSQHSMFTAIHKHYSL 82
Cdd:PRK05096 2 RIEEDLKLGFKDVLIRPKRSTLKSRSDVELERQFTFKHSGQSWSGVPIIAANMDTVGTFEMAKALASFDILTAVHKHYSV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156104880 83 DDWKLFATNHP-ECLQNVAVSSGSGQNDLEKMTSILEAVPQVKFICLDVANGYSEHFVEFVKLVRAKFPEHTIMAGNVVT 161
Cdd:PRK05096 82 EEWAAFVNNSSaDVLKHVMVSTGTSDADFEKTKQILALSPALNFICIDVANGYSEHFVQFVAKAREAWPDKTICAGNVVT 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156104880 162 GEMVEELILSGADIIKVGVGPGSVCTTRTKTGVGYPQLSAVIECADSAHGLKGHIISDGGCTCPGDVAKAFGAGADFVML 241
Cdd:PRK05096 162 GEMVEELILSGADIVKVGIGPGSVCTTRVKTGVGYPQLSAVIECADAAHGLGGQIVSDGGCTVPGDVAKAFGGGADFVML 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156104880 242 GGMFSGHTECAGEVFERNGRKLKLFYGMSSDTAMNKHAGGVAEYRASEGKTVEVPYKGDVENTILDILGGLRSTCTYVGA 321
Cdd:PRK05096 242 GGMLAGHEESGGEIVEENGEKFMLFYGMSSESAMKRHVGGVAEYRAAEGKTVKLPLRGPVENTARDILGGLRSACTYVGA 321
|
330 340
....*....|....*....|....
gi 156104880 322 AKLKELSRRATFIRVTQQHNTVFS 345
Cdd:PRK05096 322 SRLKELTKRTTFIRVQEQENRVFN 345
|
|
| IMPDH |
cd00381 |
IMPDH: The catalytic domain of the inosine monophosphate dehydrogenase. IMPDH catalyzes the ... |
10-336 |
2.80e-127 |
|
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: 367.23 E-value: 2.80e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156104880 10 LDFKDVLLRPKRSSLkSRAEVDLERTFTfrnsKQTYSGIPIIVANMDTVGTFEMAAVMSQHSMFTAIHKHYSLDDWKLFA 89
Cdd:cd00381 2 LTFDDVLLVPGYSTV-LPSEVDLSTKLT----KNITLNIPLVSAPMDTVTESEMAIAMARLGGIGVIHRNMSIEEQAEEV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156104880 90 TNHPECLQnVAVSSGSGQNDLEKMTSILEAVPQVkfICLDVANGYSEHFVEFVKLVRAKFPEHTIMAGNVVTGEMVEELI 169
Cdd:cd00381 77 RKVKGRLL-VGAAVGTREDDKERAEALVEAGVDV--IVIDSAHGHSVYVIEMIKFIKKKYPNVDVIAGNVVTAEAARDLI 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156104880 170 LSGADIIKVGVGPGSVCTTRTKTGVGYPQLSAVIECADSAHGLKGHIISDGGCTCPGDVAKAFGAGADFVMLGGMFSGHT 249
Cdd:cd00381 154 DAGADGVKVGIGPGSICTTRIVTGVGVPQATAVADVAAAARDYGVPVIADGGIRTSGDIVKALAAGADAVMLGSLLAGTD 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156104880 250 ECAGEVFERNGRKLKLFYGMSSDTAMNKHAG-----GVAEYRASEGKTVEVPYKGDVENTILDILGGLRSTCTYVGAAKL 324
Cdd:cd00381 234 ESPGEYIEINGKRYKEYRGMGSLGAMKKGGGdryfgEEAKKLVPEGVEGIVPYKGSVKDVLPQLVGGLRSSMGYCGAKSL 313
|
330
....*....|..
gi 156104880 325 KELSRRATFIRV 336
Cdd:cd00381 314 KELQEKARFVRI 325
|
|
| GuaB |
COG0516 |
IMP dehydrogenase/GMP reductase [Nucleotide transport and metabolism]; IMP dehydrogenase/GMP ... |
15-337 |
9.43e-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: 264.38 E-value: 9.43e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156104880 15 VLLRPKRSSLKSRAEVDLERTFTFRNSKQTYSGIPIIVANMDTVGTFEMAAVMSQHSMFTAIHKHYSLDDWKL-FATNHP 93
Cdd:COG0516 1 LVLDALRRRLISRSGVVVVVVVGKLTIITTRRRRRDEAVKALVVTTVIEKLLLVTVAGETALLALALLLLKKKkFLLLVD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156104880 94 ECLQNVAVSSGSGQNDLEKMTSILEAVPQVKFICLDVANGYSEHfvEFVKLVRAKFPEHTIMAGNVVTGEMVEELILSGA 173
Cdd:COG0516 81 DDGLLLLVLVGVKDDDKEKARALAAADAGVDVLVIDAAHGHSGG--DAMKKIKLTFDDVLLIPGNSATVEPARALVDAGA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156104880 174 DIIKVGVGPGSVCTTRTKTGVGYPQLSAVIECADSAHGLKgHIISDGGCTCPGDVAKAFGAGADFVMLGGMFSGHTECAG 253
Cdd:COG0516 159 DLTKVGIGPGSICTTRVVIGLGIPQLSAAMDTVTEARMAI-AIAADGGIGYIHDNAKALAAGADAVMLGSLFAGTEEQPG 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156104880 254 EVFERNGRKLKLFYGMSSDtamnkhaggvAEYRASEGKTVEVPYKGDVENTILDILGGLRSTCTYVGAAKLKELSRRATF 333
Cdd:COG0516 238 EVILYQGRSVKRYRGMGSD----------AKKLVPEGIEGRVPYKGPLEDTLHQLLGGLRSGMGYCGARTIEELREKARF 307
|
....
gi 156104880 334 IRVT 337
Cdd:COG0516 308 VRIT 311
|
|
| IMPDH |
pfam00478 |
IMP dehydrogenase / GMP reductase domain; This family is involved in biosynthesis of guanosine ... |
99-338 |
1.83e-78 |
|
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: 247.30 E-value: 1.83e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156104880 99 VAVSSGSGQNDLEKMTSILEAvpQVKFICLDVANGYSEHFVEFVKLVRAKFPEHTIMAGNVVTGEMVEELILSGADIIKV 178
Cdd:pfam00478 211 VGAAVGVGDDTLERAEALVEA--GVDVLVVDTAHGHSKGVIDTVKWIKKKYPDVQVIAGNVATAEGAKALIEAGADAVKV 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156104880 179 GVGPGSVCTTRTKTGVGYPQLSAVIECADSAHGLKGHIISDGGCTCPGDVAKAFGAGADFVMLGGMFSGHTECAGEVFER 258
Cdd:pfam00478 289 GIGPGSICTTRVVAGVGVPQLTAIYDVAEAAKKYGVPVIADGGIKYSGDIVKALAAGADAVMLGSLLAGTDESPGEVILY 368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156104880 259 NGRKLKLFYGMSSDTAMNKHA------GGVAEYRASEGktVE--VPYKGDVENTILDILGGLRSTCTYVGAAKLKELSRR 330
Cdd:pfam00478 369 QGRRYKSYRGMGSLGAMKKGSkdryfqEDDDKKLVPEG--VEgrVPYKGPLSDVVYQLVGGLRSGMGYCGAKTIEELREK 446
|
....*...
gi 156104880 331 ATFIRVTQ 338
Cdd:pfam00478 447 ARFVRITA 454
|
|
| IMP_dehydrog |
TIGR01302 |
inosine-5'-monophosphate dehydrogenase; This model describes IMP dehydrogenase, an enzyme of ... |
99-327 |
2.42e-63 |
|
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: 207.97 E-value: 2.42e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156104880 99 VAVSSGSGQNDLEKMTSILEAvpQVKFICLDVANGYSEHFVEFVKLVRAKFPEHTIMAGNVVTGEMVEELILSGADIIKV 178
Cdd:TIGR01302 215 VGAAVGTREFDKERAEALVKA--GVDVIVIDSSHGHSIYVIDSIKEIKKTYPDLDIIAGNVATAEQAKALIDAGADGLRV 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156104880 179 GVGPGSVCTTRTKTGVGYPQLSAVIECADSAHGLKGHIISDGGCTCPGDVAKAFGAGADFVMLGGMFSGHTECAGEVFER 258
Cdd:TIGR01302 293 GIGPGSICTTRIVAGVGVPQITAVYDVAEYAAQSGIPVIADGGIRYSGDIVKALAAGADAVMLGSLLAGTTESPGEYEII 372
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 156104880 259 NGRKLKLFYGMSSDTAMNK-------HAGGVAEYRASEGKTVEVPYKGDVENTILDILGGLRSTCTYVGAAKLKEL 327
Cdd:TIGR01302 373 NGRRYKQYRGMGSLGAMTKgssdrylQDENKTKKFVPEGVEGAVPYKGSVLELLPQLVGGLKSGMGYVGARSIDEL 448
|
|
| PRK05458 |
PRK05458 |
guanosine 5'-monophosphate oxidoreductase; Provisional |
10-329 |
5.51e-59 |
|
guanosine 5'-monophosphate oxidoreductase; Provisional
Pssm-ID: 235479 [Multi-domain] Cd Length: 326 Bit Score: 192.86 E-value: 5.51e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156104880 10 LDFKDVLLRPKRSSLKSRAEVDLERTF---TFRnskqtysgIPIIVANMDTVGTFEMAAVMSQHSMFTAIHKhYSLDDWK 86
Cdd:PRK05458 5 FDYEDIQLIPNKCIVNSRSECDTSVTLgprTFK--------LPVVPANMQTIIDEKIAEWLAENGYFYIMHR-FDPEARI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156104880 87 LFATNHPECLQNVAVSSGSGQNDLEKMTSILEAVPQVKFICLDVANGYSEHFVEFVKLVRAKFPEHTIMAGNVVTGEMVE 166
Cdd:PRK05458 76 PFIKDMHEQGLIASISVGVKDDEYDFVDQLAAEGLTPEYITIDIAHGHSDSVINMIQHIKKHLPETFVIAGNVGTPEAVR 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156104880 167 ELILSGADIIKVGVGPGSVCTTRTKTGVGYP--QLSAVIECADSAhglKGHIISDGGCTCPGDVAKAFGAGADFVMLGGM 244
Cdd:PRK05458 156 ELENAGADATKVGIGPGKVCITKIKTGFGTGgwQLAALRWCAKAA---RKPIIADGGIRTHGDIAKSIRFGATMVMIGSL 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156104880 245 FSGHTECAGEVFERNGRKLKLFYGMSSDtaMNKhaggvAEYRASEGKTVEVPYKGDVENTILDILGGLRSTCTYVGAAKL 324
Cdd:PRK05458 233 FAGHEESPGKTVEIDGKLYKEYFGSASE--FQK-----GEYKNVEGKKILVPHKGSLKDTLTEMEQDLQSSISYAGGRDL 305
|
....*
gi 156104880 325 KELSR 329
Cdd:PRK05458 306 DAIRK 310
|
|
| PTZ00314 |
PTZ00314 |
inosine-5'-monophosphate dehydrogenase; Provisional |
99-339 |
4.78e-58 |
|
inosine-5'-monophosphate dehydrogenase; Provisional
Pssm-ID: 240355 [Multi-domain] Cd Length: 495 Bit Score: 195.19 E-value: 4.78e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156104880 99 VAVSSGSGQNDLEKMTSILEAvpQVKFICLDVANGYSEHFVEFVKLVRAKFPEHTIMAGNVVTGEMVEELILSGADIIKV 178
Cdd:PTZ00314 232 VGAAISTRPEDIERAAALIEA--GVDVLVVDSSQGNSIYQIDMIKKLKSNYPHVDIIAGNVVTADQAKNLIDAGADGLRI 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156104880 179 GVGPGSVCTTRTKTGVGYPQLSAVIECADSAHGLKGHIISDGGCTCPGDVAKAFGAGADFVMLGGMFSGHTECAGEVFER 258
Cdd:PTZ00314 310 GMGSGSICITQEVCAVGRPQASAVYHVARYARERGVPCIADGGIKNSGDICKALALGADCVMLGSLLAGTEEAPGEYFFK 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156104880 259 NGRKLKLFYGMSSDTAMNKHAGG------VAEYRASEGKTVEVPYKGDVENTILDILGGLRSTCTYVGAAKLKEL----- 327
Cdd:PTZ00314 390 DGVRLKVYRGMGSLEAMLSKESGeryldeNETIKVAQGVSGSVVDKGSVAKLIPYLVKGVKHGMQYIGAHSIPELhekly 469
|
250
....*....|..
gi 156104880 328 SRRATFIRVTQQ 339
Cdd:PTZ00314 470 SGQVRFERRSGS 481
|
|
| PRK07807 |
PRK07807 |
GuaB1 family IMP dehydrogenase-related protein; |
111-331 |
8.50e-57 |
|
GuaB1 family IMP dehydrogenase-related protein;
Pssm-ID: 181127 [Multi-domain] Cd Length: 479 Bit Score: 191.66 E-value: 8.50e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156104880 111 EKMTSILEAvpQVKFICLDVANGYSEHFVEFVKLVRAKFPEHTIMAGNVVTGEMVEELILSGADIIKVGVGPGSVCTTRT 190
Cdd:PRK07807 230 AKARALLEA--GVDVLVVDTAHGHQEKMLEALRAVRALDPGVPIVAGNVVTAEGTRDLVEAGADIVKVGVGPGAMCTTRM 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156104880 191 KTGVGYPQLSAVIECADSAHGLKGHIISDGGCTCPGDVAKAFGAGADFVMLGGMFSGHTECAGEV-FERNGRKLKLFYGM 269
Cdd:PRK07807 308 MTGVGRPQFSAVLECAAAARELGAHVWADGGVRHPRDVALALAAGASNVMIGSWFAGTYESPGDLmRDRDGRPYKESFGM 387
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 156104880 270 SSDTAM-NKHAGGVAEYRA---------SEGKTVEVPYKGDVENTILDILGGLRSTCTYVGAAKLKELSRRA 331
Cdd:PRK07807 388 ASARAVaARTAGDSAFDRArkalfeegiSTSRMYLDPGRPGVEDLLDHITSGVRSSCTYAGARTLAEFHERA 459
|
|
| PRK06843 |
PRK06843 |
inosine 5-monophosphate dehydrogenase; Validated |
10-338 |
4.72e-56 |
|
inosine 5-monophosphate dehydrogenase; Validated
Pssm-ID: 180725 [Multi-domain] Cd Length: 404 Bit Score: 187.55 E-value: 4.72e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156104880 10 LDFKDVLLRPKRSSLKSrAEVDLERTFTfrnsKQTYSGIPIIVANMDTVGTFEMAAVMSQHSMFTAIHKHYSLDDWK--- 86
Cdd:PRK06843 10 LTFDDVSLIPRKSSVLP-SEVSLKTQLT----KNISLNIPFLSSAMDTVTESQMAIAIAKEGGIGIIHKNMSIEAQRkei 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156104880 87 -------------------------LFATNH---PECLQN-------------------VAVSSGSGQNDLEKMTSILEA 119
Cdd:PRK06843 85 ekvktykfqktintngdtneqkpeiFTAKQHlekSDAYKNaehkedfpnackdlnnklrVGAAVSIDIDTIERVEELVKA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156104880 120 vpQVKFICLDVANGYSEHFVEFVKLVRAKFPEHTIMAGNVVTGEMVEELILSGADIIKVGVGPGSVCTTRTKTGVGYPQL 199
Cdd:PRK06843 165 --HVDILVIDSAHGHSTRIIELVKKIKTKYPNLDLIAGNIVTKEAALDLISVGADCLKVGIGPGSICTTRIVAGVGVPQI 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156104880 200 SAVIECADSAHGLKGHIISDGGCTCPGDVAKAFGAGADFVMLGGMFSGHTECAGEVFERNGRKLKLFYGMSSDTAMNKha 279
Cdd:PRK06843 243 TAICDVYEVCKNTNICIIADGGIRFSGDVVKAIAAGADSVMIGNLFAGTKESPSEEIIYNGKKFKSYVGMGSISAMKR-- 320
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 156104880 280 GGVAEY----------RASEGKTVEVPYKGDVENTILDILGGLRSTCTYVGAAKLKELSRRATFIRVTQ 338
Cdd:PRK06843 321 GSKSRYfqlennepkkLVPEGIEGMVPYSGKLKDILTQLKGGLMSGMGYLGAATISDLKINSKFVKISH 389
|
|
| IMP_DH_rel_1 |
TIGR01303 |
IMP dehydrogenase family protein; This model represents a family of proteins, often annotated ... |
112-332 |
6.54e-55 |
|
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: 186.65 E-value: 6.54e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156104880 112 KMTSILEAvpQVKFICLDVANGYSEHFVEFVKLVRAKFPEHTIMAGNVVTGEMVEELILSGADIIKVGVGPGSVCTTRTK 191
Cdd:TIGR01303 229 KAKALLDA--GVDVLVIDTAHGHQVKMISAIKAVRALDLGVPIVAGNVVSAEGVRDLLEAGANIIKVGVGPGAMCTTRMM 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156104880 192 TGVGYPQLSAVIECADSAHGLKGHIISDGGCTCPGDVAKAFGAGADFVMLGGMFSGHTECAGEV-FERNGRKLKLFYGMS 270
Cdd:TIGR01303 307 TGVGRPQFSAVLECAAEARKLGGHVWADGGVRHPRDVALALAAGASNVMVGSWFAGTYESPGDLmRDRDGRPYKESFGMA 386
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 156104880 271 SDTAMNKHAGGVAEY-RA---------SEGKTVEVPYKGDVENTILDILGGLRSTCTYVGAAKLKELSRRAT 332
Cdd:TIGR01303 387 SKRAVVARTGADNAFdRArkalfeegiSTSRMGLDPDRGGVEDLIDHIISGVRSSCTYAGASSLEEFHERAV 458
|
|
| PLN02274 |
PLN02274 |
inosine-5'-monophosphate dehydrogenase |
99-277 |
3.19e-33 |
|
inosine-5'-monophosphate dehydrogenase
Pssm-ID: 215154 [Multi-domain] Cd Length: 505 Bit Score: 128.63 E-value: 3.19e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156104880 99 VAVSSGSGQNDLEKMTSILEAvpQVKFICLDVANGYSEHFVEFVKLVRAKFPEHTIMAGNVVTGEMVEELILSGADIIKV 178
Cdd:PLN02274 239 VGAAIGTRESDKERLEHLVKA--GVDVVVLDSSQGDSIYQLEMIKYIKKTYPELDVIGGNVVTMYQAQNLIQAGVDGLRV 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156104880 179 GVGPGSVCTTRTKTGVGYPQLSAVIECADSAHGLKGHIISDGGCTCPGDVAKAFGAGADFVMLGGMFSGHTECAGEVFER 258
Cdd:PLN02274 317 GMGSGSICTTQEVCAVGRGQATAVYKVASIAAQHGVPVIADGGISNSGHIVKALTLGASTVMMGSFLAGTTEAPGEYFYQ 396
|
170
....*....|....*....
gi 156104880 259 NGRKLKLFYGMSSDTAMNK 277
Cdd:PLN02274 397 DGVRVKKYRGMGSLEAMTK 415
|
|
| PRK07107 |
PRK07107 |
IMP dehydrogenase; |
104-337 |
2.35e-30 |
|
IMP dehydrogenase;
Pssm-ID: 180842 [Multi-domain] Cd Length: 502 Bit Score: 120.57 E-value: 2.35e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156104880 104 GSGQND---LEKMTSILEAvpQVKFICLDVANGYSEHFVEFVKLVRAKFPEHT-IMAGNVVTGEMVEELILSGADIIKVG 179
Cdd:PRK07107 235 GAGINTrdyAERVPALVEA--GADVLCIDSSEGYSEWQKRTLDWIREKYGDSVkVGAGNVVDREGFRYLAEAGADFVKVG 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156104880 180 VGPGSVCTTRTKTGVGYPQLSAVIECADS------AHGLKGHIISDGGCTCPGDVAKAFGAGADFVMLGGMFSGHTECAG 253
Cdd:PRK07107 313 IGGGSICITREQKGIGRGQATALIEVAKArdeyfeETGVYIPICSDGGIVYDYHMTLALAMGADFIMLGRYFARFDESPT 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156104880 254 EVFERNGRKLKLFYGMSSDTAMN---KHAGGVAEYRASEGKTVEVPYKGDVENTILDILGGLRSTCTYVGAAKLKELSRR 330
Cdd:PRK07107 393 NKVNINGNYMKEYWGEGSNRARNwqrYDLGGDKKLSFEEGVDSYVPYAGSLKDNVAITLSKVRSTMCNCGALSIPELQQK 472
|
....*..
gi 156104880 331 ATFIRVT 337
Cdd:PRK07107 473 AKITLVS 479
|
|
| KDPG_aldolase |
cd00452 |
KDPG and KHG aldolase; KDPG and KHG aldolase. This family belongs to the class I adolases ... |
140-241 |
2.89e-05 |
|
KDPG and KHG aldolase; KDPG and KHG aldolase. This family belongs to the class I adolases whose reaction mechanism involves Schiff base formation between a substrate carbonyl and lysine residue in the active site. 2-keto-3-deoxy-6-phosphogluconate (KDPG) aldolase, is best known for its role in the Entner-Doudoroff pathway of bacteria, where it catalyzes the reversible cleavage of KDPG to pyruvate and glyceraldehyde-3-phosphate. 2-keto-4-hydroxyglutarate (KHG) aldolase, which has enzymatic specificity toward glyoxylate, forming KHG in the presence of pyruvate, and is capable of regulating glyoxylate levels in the glyoxylate bypass, an alternate pathway when bacteria are grown on acetate carbon sources.
Pssm-ID: 188632 Cd Length: 190 Bit Score: 44.05 E-value: 2.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156104880 140 EFVKLVRAKFPEHTIMAGNVVTGEMVEELILSGADIIkvgVGPGSvcttrtktgvgypqlsaVIECADSAHGLKGHIIsd 219
Cdd:cd00452 44 EAIRALRKEFPEALIGAGTVLTPEQADAAIAAGAQFI---VSPGL-----------------DPEVVKAANRAGIPLL-- 101
|
90 100
....*....|....*....|..
gi 156104880 220 GGCTCPGDVAKAFGAGADFVML 241
Cdd:cd00452 102 PGVATPTEIMQALELGADIVKL 123
|
|
| TIM_phosphate_binding |
cd04722 |
TIM barrel proteins share a structurally conserved phosphate binding motif and in general ... |
128-243 |
4.25e-04 |
|
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: 41.03 E-value: 4.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156104880 128 LDVANGYS-EHFVEFVKLVRAKFPEHTIMAGNVVTGEMVEE-LILSGADIIKVGvgpGSVCTTRTKTGVgyPQLSAVIEC 205
Cdd:cd04722 90 IHGAVGYLaREDLELIRELREAVPDVKVVVKLSPTGELAAAaAEEAGVDEVGLG---NGGGGGGGRDAV--PIADLLLIL 164
|
90 100 110
....*....|....*....|....*....|....*...
gi 156104880 206 ADSAHGLKghIISDGGCTCPGDVAKAFGAGADFVMLGG 243
Cdd:cd04722 165 AKRGSKVP--VIAGGGINDPEDAAEALALGADGVIVGS 200
|
|
| DHOD_DHPD_FMN |
cd02810 |
Dihydroorotate dehydrogenase (DHOD) and Dihydropyrimidine dehydrogenase (DHPD) FMN-binding ... |
98-242 |
1.55e-03 |
|
Dihydroorotate dehydrogenase (DHOD) and Dihydropyrimidine dehydrogenase (DHPD) FMN-binding domain. DHOD catalyzes the oxidation of (S)-dihydroorotate to orotate. This is the fourth step and the only redox reaction in the de novo biosynthesis of UMP, the precursor of all pyrimidine nucleotides. DHOD requires FMN as co-factor. DHOD divides into class 1 and class 2 based on their amino acid sequences and cellular location. Members of class 1 are cytosolic enzymes and multimers while class 2 enzymes are membrane associated and monomeric. The class 1 enzymes can be further divided into subtypes 1A and 1B which are homodimers and heterotetrameric proteins, respectively. DHPD catalyzes the first step in pyrimidine degradation: the NADPH-dependent reduction of uracil and thymine to the corresponding 5,6-dihydropyrimidines. DHPD contains two FAD, two FMN and eight [4Fe-4S] clusters, arranged in two electron transfer chains that pass its homodimeric interface twice. Two of the Fe-S clusters show a hitherto unobserved coordination involving a glutamine residue.
Pssm-ID: 239204 [Multi-domain] Cd Length: 289 Bit Score: 39.64 E-value: 1.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156104880 98 NVAVSSGSGQnDLEKMTSILEAVPQVKFICLDVANGYSEHFVEFVKLVRAKfpEHTIMAGNVVTGEmveeliLSGADIIK 177
Cdd:cd02810 136 NVGGGRQLGQ-DPEAVANLLKAVKAAVDIPLLVKLSPYFDLEDIVELAKAA--ERAGADGLTAINT------ISGRVVDL 206
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 156104880 178 VGVGPGSVcttRTKTGV-GYPQLSAVIEC--ADSAHGLKG-HIISDGGCTCPGDVAKAFGAGADFVMLG 242
Cdd:cd02810 207 KTVGPGPK---RGTGGLsGAPIRPLALRWvaRLAARLQLDiPIIGVGGIDSGEDVLEMLMAGASAVQVA 272
|
|
| Glu_synthase |
pfam01645 |
Conserved region in glutamate synthase; This family represents a region of the glutamate ... |
141-242 |
1.57e-03 |
|
Conserved region in glutamate synthase; This family represents a region of the glutamate synthase protein. This region is expressed as a separate subunit in the glutamate synthase alpha subunit from archaebacteria, or part of a large multidomain enzyme in other organizms. The aligned region of these proteins contains a putative FMN binding site and Fe-S cluster.
Pssm-ID: 396287 [Multi-domain] Cd Length: 367 Bit Score: 40.01 E-value: 1.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156104880 141 FVKLVrAKFPEHTIMAGnVVTGemveelilsGADIIKV---GVGPGSVCTTRTKTgVGYPQLSAVIEcADSAHGLKGH-- 215
Cdd:pfam01645 206 SVKLV-SGHGVGTIAAG-VAKA---------GADIILIdgyDGGTGASPKTSIKH-AGLPWELALAE-AHQTLKENGLrd 272
|
90 100 110
....*....|....*....|....*....|
gi 156104880 216 ---IISDGGCTCPGDVAKAFGAGADFVMLG 242
Cdd:pfam01645 273 rvsLIADGGLRTGADVAKAAALGADAVYIG 302
|
|
| GltS_FMN |
cd02808 |
Glutamate synthase (GltS) FMN-binding domain. GltS is a complex iron-sulfur flavoprotein that ... |
141-245 |
7.67e-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: 37.91 E-value: 7.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156104880 141 FVKLVrAKFPEHTIMAGnVVTGemveelilsGADIIKVGVGPGSvcttrtkTG---------VGYPQLSAVIEcADSA-- 209
Cdd:cd02808 218 GVKLV-AGHGEGDIAAG-VAAA---------GADFITIDGAEGG-------TGaapltfidhVGLPTELGLAR-AHQAlv 278
|
90 100 110
....*....|....*....|....*....|....*....
gi 156104880 210 -HGLKGHI--ISDGGCTCPGDVAKAFGAGADFVMLGGMF 245
Cdd:cd02808 279 kNGLRDRVslIASGGLRTGADVAKALALGADAVGIGTAA 317
|
|
| |
