|
Name |
Accession |
Description |
Interval |
E-value |
| GMP_reduct_1 |
TIGR01305 |
guanosine monophosphate reductase, eukaryotic; A deep split separates two families of GMP ... |
1-290 |
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: 573.02 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039743937 1 MDTVGTFEMAVVMSQHAMFTAVHKHYSLDDWKCFA-ETHPECLQHVAVSSGSGQNDLERMSRILEAVPQVKFICLDVANG 79
Cdd:TIGR01305 53 MDTVGTFEMAAALSQHSIFTAIHKHYSVDEWKAFAtNSSPDCLQNVAVSSGSSDNDLEKMTSILEAVPQLKFICLDVANG 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039743937 80 YSEHFVEFVKLVRSKFPEHTIMAGNVVTGEMVEELILSGADIIKVGVGPGSVCTTRTKTGVGYPQLSAVIECADSAHGLK 159
Cdd:TIGR01305 133 YSEHFVEFVKLVREAFPEHTIMAGNVVTGEMVEELILSGADIVKVGIGPGSVCTTRTKTGVGYPQLSAVIECADAAHGLK 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039743937 160 GHIISDGGCTCPGDVAKAFGAGADFVMLGGMFSGHTECAGEVIERNGQKLKLFYGMSSDTAMKKHAGGVAEYRASEGKTV 239
Cdd:TIGR01305 213 GHIISDGGCTCPGDVAKAFGAGADFVMLGGMFAGHTESGGEVIERNGRKFKLFYGMSSDTAMKKHAGGVAEYRASEGKTV 292
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1039743937 240 EVPYKGDVENTILDILGGLRSTCTYVGAAKLKELSRRATFIRVTQQHNTVF 290
Cdd:TIGR01305 293 EVPYRGDVENTILDILGGLRSACTYVGAAKLKELSKRATFIRVTQQHNTVF 343
|
|
| PRK05096 |
PRK05096 |
guanosine 5'-monophosphate oxidoreductase; Provisional |
1-291 |
0e+00 |
|
guanosine 5'-monophosphate oxidoreductase; Provisional
Pssm-ID: 235343 [Multi-domain] Cd Length: 346 Bit Score: 569.19 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039743937 1 MDTVGTFEMAVVMSQHAMFTAVHKHYSLDDWKCFAETHP-ECLQHVAVSSGSGQNDLERMSRILEAVPQVKFICLDVANG 79
Cdd:PRK05096 54 MDTVGTFEMAKALASFDILTAVHKHYSVEEWAAFVNNSSaDVLKHVMVSTGTSDADFEKTKQILALSPALNFICIDVANG 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039743937 80 YSEHFVEFVKLVRSKFPEHTIMAGNVVTGEMVEELILSGADIIKVGVGPGSVCTTRTKTGVGYPQLSAVIECADSAHGLK 159
Cdd:PRK05096 134 YSEHFVQFVAKAREAWPDKTICAGNVVTGEMVEELILSGADIVKVGIGPGSVCTTRVKTGVGYPQLSAVIECADAAHGLG 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039743937 160 GHIISDGGCTCPGDVAKAFGAGADFVMLGGMFSGHTECAGEVIERNGQKLKLFYGMSSDTAMKKHAGGVAEYRASEGKTV 239
Cdd:PRK05096 214 GQIVSDGGCTVPGDVAKAFGGGADFVMLGGMLAGHEESGGEIVEENGEKFMLFYGMSSESAMKRHVGGVAEYRAAEGKTV 293
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1039743937 240 EVPYKGDVENTILDILGGLRSTCTYVGAAKLKELSRRATFIRVTQQHNTVFG 291
Cdd:PRK05096 294 KLPLRGPVENTARDILGGLRSACTYVGASRLKELTKRTTFIRVQEQENRVFN 345
|
|
| IMPDH |
cd00381 |
IMPDH: The catalytic domain of the inosine monophosphate dehydrogenase. IMPDH catalyzes the ... |
1-282 |
9.61e-113 |
|
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: 328.32 E-value: 9.61e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039743937 1 MDTVGTFEMAVVMSQHAMFTAVHKHYSLDDWKCFAETHPECLQhVAVSSGSGQNDLERMSRILEAVPQVkfICLDVANGY 80
Cdd:cd00381 42 MDTVTESEMAIAMARLGGIGVIHRNMSIEEQAEEVRKVKGRLL-VGAAVGTREDDKERAEALVEAGVDV--IVIDSAHGH 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039743937 81 SEHFVEFVKLVRSKFPEHTIMAGNVVTGEMVEELILSGADIIKVGVGPGSVCTTRTKTGVGYPQLSAVIECADSAHGLKG 160
Cdd:cd00381 119 SVYVIEMIKFIKKKYPNVDVIAGNVVTAEAARDLIDAGADGVKVGIGPGSICTTRIVTGVGVPQATAVADVAAAARDYGV 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039743937 161 HIISDGGCTCPGDVAKAFGAGADFVMLGGMFSGHTECAGEVIERNGQKLKLFYGMSSDTAMKKHAG-----GVAEYRASE 235
Cdd:cd00381 199 PVIADGGIRTSGDIVKALAAGADAVMLGSLLAGTDESPGEYIEINGKRYKEYRGMGSLGAMKKGGGdryfgEEAKKLVPE 278
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1039743937 236 GKTVEVPYKGDVENTILDILGGLRSTCTYVGAAKLKELSRRATFIRV 282
Cdd:cd00381 279 GVEGIVPYKGSVKDVLPQLVGGLRSSMGYCGAKSLKELQEKARFVRI 325
|
|
| GuaB |
COG0516 |
IMP dehydrogenase/GMP reductase [Nucleotide transport and metabolism]; IMP dehydrogenase/GMP ... |
1-283 |
7.73e-83 |
|
IMP dehydrogenase/GMP reductase [Nucleotide transport and metabolism]; IMP dehydrogenase/GMP reductase is part of the Pathway/BioSystem: Purine biosynthesis
Pssm-ID: 440282 [Multi-domain] Cd Length: 326 Bit Score: 252.44 E-value: 7.73e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039743937 1 MDTVGTFEMAVVMSQHAMFTAVHKHYSLDDW-KCFAETHPECLQHVAVSSGSGQNDLERMSRILEAVPQVKFICLDVANG 79
Cdd:COG0516 41 ALVVTTVIEKLLLVTVAGETALLALALLLLKkKKFLLLVDDDGLLLLVLVGVKDDDKEKARALAAADAGVDVLVIDAAHG 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039743937 80 YSEHfvEFVKLVRSKFPEHTIMAGNVVTGEMVEELILSGADIIKVGVGPGSVCTTRTKTGVGYPQLSAVIECADSAHGLK 159
Cdd:COG0516 121 HSGG--DAMKKIKLTFDDVLLIPGNSATVEPARALVDAGADLTKVGIGPGSICTTRVVIGLGIPQLSAAMDTVTEARMAI 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039743937 160 gHIISDGGCTCPGDVAKAFGAGADFVMLGGMFSGHTECAGEVIERNGQKLKLFYGMSSDtamkkhaggvAEYRASEGKTV 239
Cdd:COG0516 199 -AIAADGGIGYIHDNAKALAAGADAVMLGSLFAGTEEQPGEVILYQGRSVKRYRGMGSD----------AKKLVPEGIEG 267
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1039743937 240 EVPYKGDVENTILDILGGLRSTCTYVGAAKLKELSRRATFIRVT 283
Cdd:COG0516 268 RVPYKGPLEDTLHQLLGGLRSGMGYCGARTIEELREKARFVRIT 311
|
|
| IMPDH |
pfam00478 |
IMP dehydrogenase / GMP reductase domain; This family is involved in biosynthesis of guanosine ... |
45-284 |
2.97e-79 |
|
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: 2.97e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039743937 45 VAVSSGSGQNDLERMSRILEAvpQVKFICLDVANGYSEHFVEFVKLVRSKFPEHTIMAGNVVTGEMVEELILSGADIIKV 124
Cdd:pfam00478 211 VGAAVGVGDDTLERAEALVEA--GVDVLVVDTAHGHSKGVIDTVKWIKKKYPDVQVIAGNVATAEGAKALIEAGADAVKV 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039743937 125 GVGPGSVCTTRTKTGVGYPQLSAVIECADSAHGLKGHIISDGGCTCPGDVAKAFGAGADFVMLGGMFSGHTECAGEVIER 204
Cdd:pfam00478 289 GIGPGSICTTRVVAGVGVPQLTAIYDVAEAAKKYGVPVIADGGIKYSGDIVKALAAGADAVMLGSLLAGTDESPGEVILY 368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039743937 205 NGQKLKLFYGMSSDTAMKKHA------GGVAEYRASEGktVE--VPYKGDVENTILDILGGLRSTCTYVGAAKLKELSRR 276
Cdd:pfam00478 369 QGRRYKSYRGMGSLGAMKKGSkdryfqEDDDKKLVPEG--VEgrVPYKGPLSDVVYQLVGGLRSGMGYCGAKTIEELREK 446
|
....*...
gi 1039743937 277 ATFIRVTQ 284
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 ... |
1-290 |
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: 573.02 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039743937 1 MDTVGTFEMAVVMSQHAMFTAVHKHYSLDDWKCFA-ETHPECLQHVAVSSGSGQNDLERMSRILEAVPQVKFICLDVANG 79
Cdd:TIGR01305 53 MDTVGTFEMAAALSQHSIFTAIHKHYSVDEWKAFAtNSSPDCLQNVAVSSGSSDNDLEKMTSILEAVPQLKFICLDVANG 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039743937 80 YSEHFVEFVKLVRSKFPEHTIMAGNVVTGEMVEELILSGADIIKVGVGPGSVCTTRTKTGVGYPQLSAVIECADSAHGLK 159
Cdd:TIGR01305 133 YSEHFVEFVKLVREAFPEHTIMAGNVVTGEMVEELILSGADIVKVGIGPGSVCTTRTKTGVGYPQLSAVIECADAAHGLK 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039743937 160 GHIISDGGCTCPGDVAKAFGAGADFVMLGGMFSGHTECAGEVIERNGQKLKLFYGMSSDTAMKKHAGGVAEYRASEGKTV 239
Cdd:TIGR01305 213 GHIISDGGCTCPGDVAKAFGAGADFVMLGGMFAGHTESGGEVIERNGRKFKLFYGMSSDTAMKKHAGGVAEYRASEGKTV 292
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1039743937 240 EVPYKGDVENTILDILGGLRSTCTYVGAAKLKELSRRATFIRVTQQHNTVF 290
Cdd:TIGR01305 293 EVPYRGDVENTILDILGGLRSACTYVGAAKLKELSKRATFIRVTQQHNTVF 343
|
|
| PRK05096 |
PRK05096 |
guanosine 5'-monophosphate oxidoreductase; Provisional |
1-291 |
0e+00 |
|
guanosine 5'-monophosphate oxidoreductase; Provisional
Pssm-ID: 235343 [Multi-domain] Cd Length: 346 Bit Score: 569.19 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039743937 1 MDTVGTFEMAVVMSQHAMFTAVHKHYSLDDWKCFAETHP-ECLQHVAVSSGSGQNDLERMSRILEAVPQVKFICLDVANG 79
Cdd:PRK05096 54 MDTVGTFEMAKALASFDILTAVHKHYSVEEWAAFVNNSSaDVLKHVMVSTGTSDADFEKTKQILALSPALNFICIDVANG 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039743937 80 YSEHFVEFVKLVRSKFPEHTIMAGNVVTGEMVEELILSGADIIKVGVGPGSVCTTRTKTGVGYPQLSAVIECADSAHGLK 159
Cdd:PRK05096 134 YSEHFVQFVAKAREAWPDKTICAGNVVTGEMVEELILSGADIVKVGIGPGSVCTTRVKTGVGYPQLSAVIECADAAHGLG 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039743937 160 GHIISDGGCTCPGDVAKAFGAGADFVMLGGMFSGHTECAGEVIERNGQKLKLFYGMSSDTAMKKHAGGVAEYRASEGKTV 239
Cdd:PRK05096 214 GQIVSDGGCTVPGDVAKAFGGGADFVMLGGMLAGHEESGGEIVEENGEKFMLFYGMSSESAMKRHVGGVAEYRAAEGKTV 293
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1039743937 240 EVPYKGDVENTILDILGGLRSTCTYVGAAKLKELSRRATFIRVTQQHNTVFG 291
Cdd:PRK05096 294 KLPLRGPVENTARDILGGLRSACTYVGASRLKELTKRTTFIRVQEQENRVFN 345
|
|
| IMPDH |
cd00381 |
IMPDH: The catalytic domain of the inosine monophosphate dehydrogenase. IMPDH catalyzes the ... |
1-282 |
9.61e-113 |
|
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: 328.32 E-value: 9.61e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039743937 1 MDTVGTFEMAVVMSQHAMFTAVHKHYSLDDWKCFAETHPECLQhVAVSSGSGQNDLERMSRILEAVPQVkfICLDVANGY 80
Cdd:cd00381 42 MDTVTESEMAIAMARLGGIGVIHRNMSIEEQAEEVRKVKGRLL-VGAAVGTREDDKERAEALVEAGVDV--IVIDSAHGH 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039743937 81 SEHFVEFVKLVRSKFPEHTIMAGNVVTGEMVEELILSGADIIKVGVGPGSVCTTRTKTGVGYPQLSAVIECADSAHGLKG 160
Cdd:cd00381 119 SVYVIEMIKFIKKKYPNVDVIAGNVVTAEAARDLIDAGADGVKVGIGPGSICTTRIVTGVGVPQATAVADVAAAARDYGV 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039743937 161 HIISDGGCTCPGDVAKAFGAGADFVMLGGMFSGHTECAGEVIERNGQKLKLFYGMSSDTAMKKHAG-----GVAEYRASE 235
Cdd:cd00381 199 PVIADGGIRTSGDIVKALAAGADAVMLGSLLAGTDESPGEYIEINGKRYKEYRGMGSLGAMKKGGGdryfgEEAKKLVPE 278
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1039743937 236 GKTVEVPYKGDVENTILDILGGLRSTCTYVGAAKLKELSRRATFIRV 282
Cdd:cd00381 279 GVEGIVPYKGSVKDVLPQLVGGLRSSMGYCGAKSLKELQEKARFVRI 325
|
|
| GuaB |
COG0516 |
IMP dehydrogenase/GMP reductase [Nucleotide transport and metabolism]; IMP dehydrogenase/GMP ... |
1-283 |
7.73e-83 |
|
IMP dehydrogenase/GMP reductase [Nucleotide transport and metabolism]; IMP dehydrogenase/GMP reductase is part of the Pathway/BioSystem: Purine biosynthesis
Pssm-ID: 440282 [Multi-domain] Cd Length: 326 Bit Score: 252.44 E-value: 7.73e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039743937 1 MDTVGTFEMAVVMSQHAMFTAVHKHYSLDDW-KCFAETHPECLQHVAVSSGSGQNDLERMSRILEAVPQVKFICLDVANG 79
Cdd:COG0516 41 ALVVTTVIEKLLLVTVAGETALLALALLLLKkKKFLLLVDDDGLLLLVLVGVKDDDKEKARALAAADAGVDVLVIDAAHG 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039743937 80 YSEHfvEFVKLVRSKFPEHTIMAGNVVTGEMVEELILSGADIIKVGVGPGSVCTTRTKTGVGYPQLSAVIECADSAHGLK 159
Cdd:COG0516 121 HSGG--DAMKKIKLTFDDVLLIPGNSATVEPARALVDAGADLTKVGIGPGSICTTRVVIGLGIPQLSAAMDTVTEARMAI 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039743937 160 gHIISDGGCTCPGDVAKAFGAGADFVMLGGMFSGHTECAGEVIERNGQKLKLFYGMSSDtamkkhaggvAEYRASEGKTV 239
Cdd:COG0516 199 -AIAADGGIGYIHDNAKALAAGADAVMLGSLFAGTEEQPGEVILYQGRSVKRYRGMGSD----------AKKLVPEGIEG 267
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1039743937 240 EVPYKGDVENTILDILGGLRSTCTYVGAAKLKELSRRATFIRVT 283
Cdd:COG0516 268 RVPYKGPLEDTLHQLLGGLRSGMGYCGARTIEELREKARFVRIT 311
|
|
| IMPDH |
pfam00478 |
IMP dehydrogenase / GMP reductase domain; This family is involved in biosynthesis of guanosine ... |
45-284 |
2.97e-79 |
|
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: 2.97e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039743937 45 VAVSSGSGQNDLERMSRILEAvpQVKFICLDVANGYSEHFVEFVKLVRSKFPEHTIMAGNVVTGEMVEELILSGADIIKV 124
Cdd:pfam00478 211 VGAAVGVGDDTLERAEALVEA--GVDVLVVDTAHGHSKGVIDTVKWIKKKYPDVQVIAGNVATAEGAKALIEAGADAVKV 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039743937 125 GVGPGSVCTTRTKTGVGYPQLSAVIECADSAHGLKGHIISDGGCTCPGDVAKAFGAGADFVMLGGMFSGHTECAGEVIER 204
Cdd:pfam00478 289 GIGPGSICTTRVVAGVGVPQLTAIYDVAEAAKKYGVPVIADGGIKYSGDIVKALAAGADAVMLGSLLAGTDESPGEVILY 368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039743937 205 NGQKLKLFYGMSSDTAMKKHA------GGVAEYRASEGktVE--VPYKGDVENTILDILGGLRSTCTYVGAAKLKELSRR 276
Cdd:pfam00478 369 QGRRYKSYRGMGSLGAMKKGSkdryfqEDDDKKLVPEG--VEgrVPYKGPLSDVVYQLVGGLRSGMGYCGAKTIEELREK 446
|
....*...
gi 1039743937 277 ATFIRVTQ 284
Cdd:pfam00478 447 ARFVRITA 454
|
|
| IMP_dehydrog |
TIGR01302 |
inosine-5'-monophosphate dehydrogenase; This model describes IMP dehydrogenase, an enzyme of ... |
45-273 |
1.09e-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: 206.81 E-value: 1.09e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039743937 45 VAVSSGSGQNDLERMSRILEAvpQVKFICLDVANGYSEHFVEFVKLVRSKFPEHTIMAGNVVTGEMVEELILSGADIIKV 124
Cdd:TIGR01302 215 VGAAVGTREFDKERAEALVKA--GVDVIVIDSSHGHSIYVIDSIKEIKKTYPDLDIIAGNVATAEQAKALIDAGADGLRV 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039743937 125 GVGPGSVCTTRTKTGVGYPQLSAVIECADSAHGLKGHIISDGGCTCPGDVAKAFGAGADFVMLGGMFSGHTECAGEVIER 204
Cdd:TIGR01302 293 GIGPGSICTTRIVAGVGVPQITAVYDVAEYAAQSGIPVIADGGIRYSGDIVKALAAGADAVMLGSLLAGTTESPGEYEII 372
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1039743937 205 NGQKLKLFYGMSSDTAMKK-------HAGGVAEYRASEGKTVEVPYKGDVENTILDILGGLRSTCTYVGAAKLKEL 273
Cdd:TIGR01302 373 NGRRYKQYRGMGSLGAMTKgssdrylQDENKTKKFVPEGVEGAVPYKGSVLELLPQLVGGLKSGMGYVGARSIDEL 448
|
|
| PTZ00314 |
PTZ00314 |
inosine-5'-monophosphate dehydrogenase; Provisional |
45-285 |
6.28e-60 |
|
inosine-5'-monophosphate dehydrogenase; Provisional
Pssm-ID: 240355 [Multi-domain] Cd Length: 495 Bit Score: 198.27 E-value: 6.28e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039743937 45 VAVSSGSGQNDLERMSRILEAvpQVKFICLDVANGYSEHFVEFVKLVRSKFPEHTIMAGNVVTGEMVEELILSGADIIKV 124
Cdd:PTZ00314 232 VGAAISTRPEDIERAAALIEA--GVDVLVVDSSQGNSIYQIDMIKKLKSNYPHVDIIAGNVVTADQAKNLIDAGADGLRI 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039743937 125 GVGPGSVCTTRTKTGVGYPQLSAVIECADSAHGLKGHIISDGGCTCPGDVAKAFGAGADFVMLGGMFSGHTECAGEVIER 204
Cdd:PTZ00314 310 GMGSGSICITQEVCAVGRPQASAVYHVARYARERGVPCIADGGIKNSGDICKALALGADCVMLGSLLAGTEEAPGEYFFK 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039743937 205 NGQKLKLFYGMSSDTAMKKHAGG------VAEYRASEGKTVEVPYKGDVENTILDILGGLRSTCTYVGAAKLKEL----- 273
Cdd:PTZ00314 390 DGVRLKVYRGMGSLEAMLSKESGeryldeNETIKVAQGVSGSVVDKGSVAKLIPYLVKGVKHGMQYIGAHSIPELhekly 469
|
250
....*....|..
gi 1039743937 274 SRRATFIRVTQQ 285
Cdd:PTZ00314 470 SGQVRFERRSGS 481
|
|
| PRK07807 |
PRK07807 |
GuaB1 family IMP dehydrogenase-related protein; |
57-277 |
1.09e-55 |
|
GuaB1 family IMP dehydrogenase-related protein;
Pssm-ID: 181127 [Multi-domain] Cd Length: 479 Bit Score: 186.65 E-value: 1.09e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039743937 57 ERMSRILEAvpQVKFICLDVANGYSEHFVEFVKLVRSKFPEHTIMAGNVVTGEMVEELILSGADIIKVGVGPGSVCTTRT 136
Cdd:PRK07807 230 AKARALLEA--GVDVLVVDTAHGHQEKMLEALRAVRALDPGVPIVAGNVVTAEGTRDLVEAGADIVKVGVGPGAMCTTRM 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039743937 137 KTGVGYPQLSAVIECADSAHGLKGHIISDGGCTCPGDVAKAFGAGADFVMLGGMFSGHTECAGEV-IERNGQKLKLFYGM 215
Cdd:PRK07807 308 MTGVGRPQFSAVLECAAAARELGAHVWADGGVRHPRDVALALAAGASNVMIGSWFAGTYESPGDLmRDRDGRPYKESFGM 387
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039743937 216 SSDTAMKKHAGGVAEY-RA---------SEGKTVEVPYKGDVENTILDILGGLRSTCTYVGAAKLKELSRRA 277
Cdd:PRK07807 388 ASARAVAARTAGDSAFdRArkalfeegiSTSRMYLDPGRPGVEDLLDHITSGVRSSCTYAGARTLAEFHERA 459
|
|
| PRK06843 |
PRK06843 |
inosine 5-monophosphate dehydrogenase; Validated |
55-284 |
3.30e-54 |
|
inosine 5-monophosphate dehydrogenase; Validated
Pssm-ID: 180725 [Multi-domain] Cd Length: 404 Bit Score: 181.01 E-value: 3.30e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039743937 55 DLERMSRILEAV-PQVKFICLDVANGYSEHFVEFVKLVRSKFPEHTIMAGNVVTGEMVEELILSGADIIKVGVGPGSVCT 133
Cdd:PRK06843 151 DIDTIERVEELVkAHVDILVIDSAHGHSTRIIELVKKIKTKYPNLDLIAGNIVTKEAALDLISVGADCLKVGIGPGSICT 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039743937 134 TRTKTGVGYPQLSAVIECADSAHGLKGHIISDGGCTCPGDVAKAFGAGADFVMLGGMFSGHTECAGEVIERNGQKLKLFY 213
Cdd:PRK06843 231 TRIVAGVGVPQITAICDVYEVCKNTNICIIADGGIRFSGDVVKAIAAGADSVMIGNLFAGTKESPSEEIIYNGKKFKSYV 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039743937 214 GMSSDTAMKKhaGGVAEY----------RASEGKTVEVPYKGDVENTILDILGGLRSTCTYVGAAKLKELSRRATFIRVT 283
Cdd:PRK06843 311 GMGSISAMKR--GSKSRYfqlennepkkLVPEGIEGMVPYSGKLKDILTQLKGGLMSGMGYLGAATISDLKINSKFVKIS 388
|
.
gi 1039743937 284 Q 284
Cdd:PRK06843 389 H 389
|
|
| IMP_DH_rel_1 |
TIGR01303 |
IMP dehydrogenase family protein; This model represents a family of proteins, often annotated ... |
69-278 |
8.68e-54 |
|
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: 181.65 E-value: 8.68e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039743937 69 VKFICLDVANGYSEHFVEFVKLVRSKFPEHTIMAGNVVTGEMVEELILSGADIIKVGVGPGSVCTTRTKTGVGYPQLSAV 148
Cdd:TIGR01303 238 VDVLVIDTAHGHQVKMISAIKAVRALDLGVPIVAGNVVSAEGVRDLLEAGANIIKVGVGPGAMCTTRMMTGVGRPQFSAV 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039743937 149 IECADSAHGLKGHIISDGGCTCPGDVAKAFGAGADFVMLGGMFSGHTECAGEVI-ERNGQKLKLFYGMSSDTAMKKHAGG 227
Cdd:TIGR01303 318 LECAAEARKLGGHVWADGGVRHPRDVALALAAGASNVMVGSWFAGTYESPGDLMrDRDGRPYKESFGMASKRAVVARTGA 397
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1039743937 228 VAEY-RA---------SEGKTVEVPYKGDVENTILDILGGLRSTCTYVGAAKLKELSRRAT 278
Cdd:TIGR01303 398 DNAFdRArkalfeegiSTSRMGLDPDRGGVEDLIDHIISGVRSSCTYAGASSLEEFHERAV 458
|
|
| PRK05458 |
PRK05458 |
guanosine 5'-monophosphate oxidoreductase; Provisional |
1-275 |
3.17e-49 |
|
guanosine 5'-monophosphate oxidoreductase; Provisional
Pssm-ID: 235479 [Multi-domain] Cd Length: 326 Bit Score: 165.90 E-value: 3.17e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039743937 1 MDTVGTFEMAVVMSQHAMFTAVHKhYSLDDWKCFAETHPECLQHVAVSSGSGQNDLERMSRILEAVPQVKFICLDVANGY 80
Cdd:PRK05458 45 MQTIIDEKIAEWLAENGYFYIMHR-FDPEARIPFIKDMHEQGLIASISVGVKDDEYDFVDQLAAEGLTPEYITIDIAHGH 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039743937 81 SEHFVEFVKLVRSKFPEHTIMAGNVVTGEMVEELILSGADIIKVGVGPGSVCTTRTKTGVGYP--QLSAVIECADSAhgl 158
Cdd:PRK05458 124 SDSVINMIQHIKKHLPETFVIAGNVGTPEAVRELENAGADATKVGIGPGKVCITKIKTGFGTGgwQLAALRWCAKAA--- 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039743937 159 KGHIISDGGCTCPGDVAKAFGAGADFVMLGGMFSGHTECAGEVIERNGQKLKLFYGMSSDtaMKKhaggvAEYRASEGKT 238
Cdd:PRK05458 201 RKPIIADGGIRTHGDIAKSIRFGATMVMIGSLFAGHEESPGKTVEIDGKLYKEYFGSASE--FQK-----GEYKNVEGKK 273
|
250 260 270
....*....|....*....|....*....|....*..
gi 1039743937 239 VEVPYKGDVENTILDILGGLRSTCTYVGAAKLKELSR 275
Cdd:PRK05458 274 ILVPHKGSLKDTLTEMEQDLQSSISYAGGRDLDAIRK 310
|
|
| PLN02274 |
PLN02274 |
inosine-5'-monophosphate dehydrogenase |
45-223 |
9.26e-33 |
|
inosine-5'-monophosphate dehydrogenase
Pssm-ID: 215154 [Multi-domain] Cd Length: 505 Bit Score: 125.55 E-value: 9.26e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039743937 45 VAVSSGSGQNDLERMSRILEAvpQVKFICLDVANGYSEHFVEFVKLVRSKFPEHTIMAGNVVTGEMVEELILSGADIIKV 124
Cdd:PLN02274 239 VGAAIGTRESDKERLEHLVKA--GVDVVVLDSSQGDSIYQLEMIKYIKKTYPELDVIGGNVVTMYQAQNLIQAGVDGLRV 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039743937 125 GVGPGSVCTTRTKTGVGYPQLSAVIECADSAHGLKGHIISDGGCTCPGDVAKAFGAGADFVMLGGMFSGHTECAGEVIER 204
Cdd:PLN02274 317 GMGSGSICTTQEVCAVGRGQATAVYKVASIAAQHGVPVIADGGISNSGHIVKALTLGASTVMMGSFLAGTTEAPGEYFYQ 396
|
170
....*....|....*....
gi 1039743937 205 NGQKLKLFYGMSSDTAMKK 223
Cdd:PLN02274 397 DGVRVKKYRGMGSLEAMTK 415
|
|
| PRK07107 |
PRK07107 |
IMP dehydrogenase; |
50-283 |
2.87e-31 |
|
IMP dehydrogenase;
Pssm-ID: 180842 [Multi-domain] Cd Length: 502 Bit Score: 121.73 E-value: 2.87e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039743937 50 GSGQND---LERMSRILEAvpQVKFICLDVANGYSEHFVEFVKLVRSKFPEHT-IMAGNVVTGEMVEELILSGADIIKVG 125
Cdd:PRK07107 235 GAGINTrdyAERVPALVEA--GADVLCIDSSEGYSEWQKRTLDWIREKYGDSVkVGAGNVVDREGFRYLAEAGADFVKVG 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039743937 126 VGPGSVCTTRTKTGVGYPQLSAVIECADS------AHGLKGHIISDGGCTCPGDVAKAFGAGADFVMLGGMFSGHTECAG 199
Cdd:PRK07107 313 IGGGSICITREQKGIGRGQATALIEVAKArdeyfeETGVYIPICSDGGIVYDYHMTLALAMGADFIMLGRYFARFDESPT 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039743937 200 EVIERNGQKLKLFYGMSSDTA---MKKHAGGVAEYRASEGKTVEVPYKGDVENTILDILGGLRSTCTYVGAAKLKELSRR 276
Cdd:PRK07107 393 NKVNINGNYMKEYWGEGSNRArnwQRYDLGGDKKLSFEEGVDSYVPYAGSLKDNVAITLSKVRSTMCNCGALSIPELQQK 472
|
....*..
gi 1039743937 277 ATFIRVT 283
Cdd:PRK07107 473 AKITLVS 479
|
|
| KDPG_aldolase |
cd00452 |
KDPG and KHG aldolase; KDPG and KHG aldolase. This family belongs to the class I adolases ... |
86-187 |
7.74e-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: 42.51 E-value: 7.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039743937 86 EFVKLVRSKFPEHTIMAGNVVTGEMVEELILSGADIIkvgVGPGSvcttrtktgvgypqlsaVIECADSAHGLKGHIIsd 165
Cdd:cd00452 44 EAIRALRKEFPEALIGAGTVLTPEQADAAIAAGAQFI---VSPGL-----------------DPEVVKAANRAGIPLL-- 101
|
90 100
....*....|....*....|..
gi 1039743937 166 GGCTCPGDVAKAFGAGADFVML 187
Cdd:cd00452 102 PGVATPTEIMQALELGADIVKL 123
|
|
| DHOD_DHPD_FMN |
cd02810 |
Dihydroorotate dehydrogenase (DHOD) and Dihydropyrimidine dehydrogenase (DHPD) FMN-binding ... |
44-188 |
1.64e-04 |
|
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: 42.34 E-value: 1.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039743937 44 HVAVSSGSGQnDLERMSRILEAVPQVKFICLDVANGYSEHFVEFVKLVRSKfpEHTIMAGNVVTGEmveeliLSGADIIK 123
Cdd:cd02810 136 NVGGGRQLGQ-DPEAVANLLKAVKAAVDIPLLVKLSPYFDLEDIVELAKAA--ERAGADGLTAINT------ISGRVVDL 206
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1039743937 124 VGVGPGSVcttRTKTGV-GYPQLSAVIEC--ADSAHGLKG-HIISDGGCTCPGDVAKAFGAGADFVMLG 188
Cdd:cd02810 207 KTVGPGPK---RGTGGLsGAPIRPLALRWvaRLAARLQLDiPIIGVGGIDSGEDVLEMLMAGASAVQVA 272
|
|
| TIM_phosphate_binding |
cd04722 |
TIM barrel proteins share a structurally conserved phosphate binding motif and in general ... |
74-189 |
1.41e-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: 39.11 E-value: 1.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039743937 74 LDVANGYS-EHFVEFVKLVRSKFPEHTIMAGNVVTGEMVEE-LILSGADIIKVGvgpGSVCTTRTKTGVgyPQLSAVIEC 151
Cdd:cd04722 90 IHGAVGYLaREDLELIRELREAVPDVKVVVKLSPTGELAAAaAEEAGVDEVGLG---NGGGGGGGRDAV--PIADLLLIL 164
|
90 100 110
....*....|....*....|....*....|....*...
gi 1039743937 152 ADSAHGLKghIISDGGCTCPGDVAKAFGAGADFVMLGG 189
Cdd:cd04722 165 AKRGSKVP--VIAGGGINDPEDAAEALALGADGVIVGS 200
|
|
| Glu_synthase |
pfam01645 |
Conserved region in glutamate synthase; This family represents a region of the glutamate ... |
87-188 |
2.21e-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: 39.24 E-value: 2.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039743937 87 FVKLVrSKFPEHTIMAGnVVTGemveelilsGADIIKV---GVGPGSVCTTRTKTgVGYPQLSAVIEcADSAHGLKGH-- 161
Cdd:pfam01645 206 SVKLV-SGHGVGTIAAG-VAKA---------GADIILIdgyDGGTGASPKTSIKH-AGLPWELALAE-AHQTLKENGLrd 272
|
90 100 110
....*....|....*....|....*....|
gi 1039743937 162 ---IISDGGCTCPGDVAKAFGAGADFVMLG 188
Cdd:pfam01645 273 rvsLIADGGLRTGADVAKAAALGADAVYIG 302
|
|
| GltS_FMN |
cd02808 |
Glutamate synthase (GltS) FMN-binding domain. GltS is a complex iron-sulfur flavoprotein that ... |
156-191 |
8.49e-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: 37.52 E-value: 8.49e-03
10 20 30
....*....|....*....|....*....|....*...
gi 1039743937 156 HGLKGHI--ISDGGCTCPGDVAKAFGAGADFVMLGGMF 191
Cdd:cd02808 280 NGLRDRVslIASGGLRTGADVAKALALGADAVGIGTAA 317
|
|
| |
