|
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: 682.80 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369767 3 RIDADLKLDFKDVLLRPKRSSLKSRSEVDLERTFTFRNSKQTYSGIPVIVANMDTVGTFEMAVVMSQHAMFTAIHKHYSL 82
Cdd:TIGR01305 1 RIEADLKLDFKDVLLRPKRSTLKSRADVELERTFTFRNSKQTYSGVPIIAANMDTVGTFEMAAALSQHSIFTAIHKHYSV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369767 83 DDWKHFAEN-HPECLQHVAVSSGSGQNDLEKMSLILEAVPQVKFICLDVANGYSEHFVEFVKLVRSKFPEHTIMAGNVVT 161
Cdd:TIGR01305 81 DEWKAFATNsSPDCLQNVAVSSGSSDNDLEKMTSILEAVPQLKFICLDVANGYSEHFVEFVKLVREAFPEHTIMAGNVVT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369767 162 GEMVEELILSGADIIKVGVGPGSVCTTRTKTGVGYPQLSAVIECADSAHGLKGHIISDGGCTCPGDVAKAFGAGADFVML 241
Cdd:TIGR01305 161 GEMVEELILSGADIVKVGIGPGSVCTTRTKTGVGYPQLSAVIECADAAHGLKGHIISDGGCTCPGDVAKAFGAGADFVML 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369767 242 GGMFSGHTECAGEVIERNGQKLKLFYGMSSDTAMKKHAGGVAEYRASEGKTVEVPYKGDVENTILDILGGLRSTCTYVGA 321
Cdd:TIGR01305 241 GGMFAGHTESGGEVIERNGRKFKLFYGMSSDTAMKKHAGGVAEYRASEGKTVEVPYRGDVENTILDILGGLRSACTYVGA 320
|
330 340
....*....|....*....|...
gi 1937369767 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: 677.05 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369767 3 RIDADLKLDFKDVLLRPKRSSLKSRSEVDLERTFTFRNSKQTYSGIPVIVANMDTVGTFEMAVVMSQHAMFTAIHKHYSL 82
Cdd:PRK05096 2 RIEEDLKLGFKDVLIRPKRSTLKSRSDVELERQFTFKHSGQSWSGVPIIAANMDTVGTFEMAKALASFDILTAVHKHYSV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369767 83 DDWKHFAENHP-ECLQHVAVSSGSGQNDLEKMSLILEAVPQVKFICLDVANGYSEHFVEFVKLVRSKFPEHTIMAGNVVT 161
Cdd:PRK05096 82 EEWAAFVNNSSaDVLKHVMVSTGTSDADFEKTKQILALSPALNFICIDVANGYSEHFVQFVAKAREAWPDKTICAGNVVT 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369767 162 GEMVEELILSGADIIKVGVGPGSVCTTRTKTGVGYPQLSAVIECADSAHGLKGHIISDGGCTCPGDVAKAFGAGADFVML 241
Cdd:PRK05096 162 GEMVEELILSGADIVKVGIGPGSVCTTRVKTGVGYPQLSAVIECADAAHGLGGQIVSDGGCTVPGDVAKAFGGGADFVML 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369767 242 GGMFSGHTECAGEVIERNGQKLKLFYGMSSDTAMKKHAGGVAEYRASEGKTVEVPYKGDVENTILDILGGLRSTCTYVGA 321
Cdd:PRK05096 242 GGMLAGHEESGGEIVEENGEKFMLFYGMSSESAMKRHVGGVAEYRAAEGKTVKLPLRGPVENTARDILGGLRSACTYVGA 321
|
330 340
....*....|....*....|....
gi 1937369767 322 AKLKELSRRATFIRVTQQHNTVFG 345
Cdd:PRK05096 322 SRLKELTKRTTFIRVQEQENRVFN 345
|
|
| IMPDH |
cd00381 |
IMPDH: The catalytic domain of the inosine monophosphate dehydrogenase. IMPDH catalyzes the ... |
10-336 |
6.06e-128 |
|
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: 369.15 E-value: 6.06e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369767 10 LDFKDVLLRPKRSSLkSRSEVDLERTFTfrnsKQTYSGIPVIVANMDTVGTFEMAVVMSQHAMFTAIHKHYSLDDWKHFA 89
Cdd:cd00381 2 LTFDDVLLVPGYSTV-LPSEVDLSTKLT----KNITLNIPLVSAPMDTVTESEMAIAMARLGGIGVIHRNMSIEEQAEEV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369767 90 ENHPECLQhVAVSSGSGQNDLEKMSLILEAVPQVkfICLDVANGYSEHFVEFVKLVRSKFPEHTIMAGNVVTGEMVEELI 169
Cdd:cd00381 77 RKVKGRLL-VGAAVGTREDDKERAEALVEAGVDV--IVIDSAHGHSVYVIEMIKFIKKKYPNVDVIAGNVVTAEAARDLI 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369767 170 LSGADIIKVGVGPGSVCTTRTKTGVGYPQLSAVIECADSAHGLKGHIISDGGCTCPGDVAKAFGAGADFVMLGGMFSGHT 249
Cdd:cd00381 154 DAGADGVKVGIGPGSICTTRIVTGVGVPQATAVADVAAAARDYGVPVIADGGIRTSGDIVKALAAGADAVMLGSLLAGTD 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369767 250 ECAGEVIERNGQKLKLFYGMSSDTAMKKHAG-----GVAEYRASEGKTVEVPYKGDVENTILDILGGLRSTCTYVGAAKL 324
Cdd:cd00381 234 ESPGEYIEINGKRYKEYRGMGSLGAMKKGGGdryfgEEAKKLVPEGVEGIVPYKGSVKDVLPQLVGGLRSSMGYCGAKSL 313
|
330
....*....|..
gi 1937369767 325 KELSRRATFIRV 336
Cdd:cd00381 314 KELQEKARFVRI 325
|
|
| GuaB |
COG0516 |
IMP dehydrogenase/GMP reductase [Nucleotide transport and metabolism]; IMP dehydrogenase/GMP ... |
15-339 |
2.04e-87 |
|
IMP dehydrogenase/GMP reductase [Nucleotide transport and metabolism]; IMP dehydrogenase/GMP reductase is part of the Pathway/BioSystem: Purine biosynthesis
Pssm-ID: 440282 [Multi-domain] Cd Length: 326 Bit Score: 265.92 E-value: 2.04e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369767 15 VLLRPKRSSLKSRSEVDLERTFTFRNSKQTYSGIPVIVANMDTVGTFEMAVVMSQHAMFTAIHKHYSLDDWKH-FAENHP 93
Cdd:COG0516 1 LVLDALRRRLISRSGVVVVVVVGKLTIITTRRRRRDEAVKALVVTTVIEKLLLVTVAGETALLALALLLLKKKkFLLLVD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369767 94 ECLQHVAVSSGSGQNDLEKMSLILEAVPQVKFICLDVANGYSEHfvEFVKLVRSKFPEHTIMAGNVVTGEMVEELILSGA 173
Cdd:COG0516 81 DDGLLLLVLVGVKDDDKEKARALAAADAGVDVLVIDAAHGHSGG--DAMKKIKLTFDDVLLIPGNSATVEPARALVDAGA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369767 174 DIIKVGVGPGSVCTTRTKTGVGYPQLSAVIECADSAHGLKgHIISDGGCTCPGDVAKAFGAGADFVMLGGMFSGHTECAG 253
Cdd:COG0516 159 DLTKVGIGPGSICTTRVVIGLGIPQLSAAMDTVTEARMAI-AIAADGGIGYIHDNAKALAAGADAVMLGSLFAGTEEQPG 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369767 254 EVIERNGQKLKLFYGMSSDtamkkhaggvAEYRASEGKTVEVPYKGDVENTILDILGGLRSTCTYVGAAKLKELSRRATF 333
Cdd:COG0516 238 EVILYQGRSVKRYRGMGSD----------AKKLVPEGIEGRVPYKGPLEDTLHQLLGGLRSGMGYCGARTIEELREKARF 307
|
....*.
gi 1937369767 334 IRVTQQ 339
Cdd:COG0516 308 VRITSA 313
|
|
| IMPDH |
pfam00478 |
IMP dehydrogenase / GMP reductase domain; This family is involved in biosynthesis of guanosine ... |
99-338 |
6.49e-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: 246.15 E-value: 6.49e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369767 99 VAVSSGSGQNDLEKMSLILEAvpQVKFICLDVANGYSEHFVEFVKLVRSKFPEHTIMAGNVVTGEMVEELILSGADIIKV 178
Cdd:pfam00478 211 VGAAVGVGDDTLERAEALVEA--GVDVLVVDTAHGHSKGVIDTVKWIKKKYPDVQVIAGNVATAEGAKALIEAGADAVKV 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369767 179 GVGPGSVCTTRTKTGVGYPQLSAVIECADSAHGLKGHIISDGGCTCPGDVAKAFGAGADFVMLGGMFSGHTECAGEVIER 258
Cdd:pfam00478 289 GIGPGSICTTRVVAGVGVPQLTAIYDVAEAAKKYGVPVIADGGIKYSGDIVKALAAGADAVMLGSLLAGTDESPGEVILY 368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369767 259 NGQKLKLFYGMSSDTAMKKHA------GGVAEYRASEGktVE--VPYKGDVENTILDILGGLRSTCTYVGAAKLKELSRR 330
Cdd:pfam00478 369 QGRRYKSYRGMGSLGAMKKGSkdryfqEDDDKKLVPEG--VEgrVPYKGPLSDVVYQLVGGLRSGMGYCGAKTIEELREK 446
|
....*...
gi 1937369767 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: 682.80 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369767 3 RIDADLKLDFKDVLLRPKRSSLKSRSEVDLERTFTFRNSKQTYSGIPVIVANMDTVGTFEMAVVMSQHAMFTAIHKHYSL 82
Cdd:TIGR01305 1 RIEADLKLDFKDVLLRPKRSTLKSRADVELERTFTFRNSKQTYSGVPIIAANMDTVGTFEMAAALSQHSIFTAIHKHYSV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369767 83 DDWKHFAEN-HPECLQHVAVSSGSGQNDLEKMSLILEAVPQVKFICLDVANGYSEHFVEFVKLVRSKFPEHTIMAGNVVT 161
Cdd:TIGR01305 81 DEWKAFATNsSPDCLQNVAVSSGSSDNDLEKMTSILEAVPQLKFICLDVANGYSEHFVEFVKLVREAFPEHTIMAGNVVT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369767 162 GEMVEELILSGADIIKVGVGPGSVCTTRTKTGVGYPQLSAVIECADSAHGLKGHIISDGGCTCPGDVAKAFGAGADFVML 241
Cdd:TIGR01305 161 GEMVEELILSGADIVKVGIGPGSVCTTRTKTGVGYPQLSAVIECADAAHGLKGHIISDGGCTCPGDVAKAFGAGADFVML 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369767 242 GGMFSGHTECAGEVIERNGQKLKLFYGMSSDTAMKKHAGGVAEYRASEGKTVEVPYKGDVENTILDILGGLRSTCTYVGA 321
Cdd:TIGR01305 241 GGMFAGHTESGGEVIERNGRKFKLFYGMSSDTAMKKHAGGVAEYRASEGKTVEVPYRGDVENTILDILGGLRSACTYVGA 320
|
330 340
....*....|....*....|...
gi 1937369767 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: 677.05 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369767 3 RIDADLKLDFKDVLLRPKRSSLKSRSEVDLERTFTFRNSKQTYSGIPVIVANMDTVGTFEMAVVMSQHAMFTAIHKHYSL 82
Cdd:PRK05096 2 RIEEDLKLGFKDVLIRPKRSTLKSRSDVELERQFTFKHSGQSWSGVPIIAANMDTVGTFEMAKALASFDILTAVHKHYSV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369767 83 DDWKHFAENHP-ECLQHVAVSSGSGQNDLEKMSLILEAVPQVKFICLDVANGYSEHFVEFVKLVRSKFPEHTIMAGNVVT 161
Cdd:PRK05096 82 EEWAAFVNNSSaDVLKHVMVSTGTSDADFEKTKQILALSPALNFICIDVANGYSEHFVQFVAKAREAWPDKTICAGNVVT 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369767 162 GEMVEELILSGADIIKVGVGPGSVCTTRTKTGVGYPQLSAVIECADSAHGLKGHIISDGGCTCPGDVAKAFGAGADFVML 241
Cdd:PRK05096 162 GEMVEELILSGADIVKVGIGPGSVCTTRVKTGVGYPQLSAVIECADAAHGLGGQIVSDGGCTVPGDVAKAFGGGADFVML 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369767 242 GGMFSGHTECAGEVIERNGQKLKLFYGMSSDTAMKKHAGGVAEYRASEGKTVEVPYKGDVENTILDILGGLRSTCTYVGA 321
Cdd:PRK05096 242 GGMLAGHEESGGEIVEENGEKFMLFYGMSSESAMKRHVGGVAEYRAAEGKTVKLPLRGPVENTARDILGGLRSACTYVGA 321
|
330 340
....*....|....*....|....
gi 1937369767 322 AKLKELSRRATFIRVTQQHNTVFG 345
Cdd:PRK05096 322 SRLKELTKRTTFIRVQEQENRVFN 345
|
|
| IMPDH |
cd00381 |
IMPDH: The catalytic domain of the inosine monophosphate dehydrogenase. IMPDH catalyzes the ... |
10-336 |
6.06e-128 |
|
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: 369.15 E-value: 6.06e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369767 10 LDFKDVLLRPKRSSLkSRSEVDLERTFTfrnsKQTYSGIPVIVANMDTVGTFEMAVVMSQHAMFTAIHKHYSLDDWKHFA 89
Cdd:cd00381 2 LTFDDVLLVPGYSTV-LPSEVDLSTKLT----KNITLNIPLVSAPMDTVTESEMAIAMARLGGIGVIHRNMSIEEQAEEV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369767 90 ENHPECLQhVAVSSGSGQNDLEKMSLILEAVPQVkfICLDVANGYSEHFVEFVKLVRSKFPEHTIMAGNVVTGEMVEELI 169
Cdd:cd00381 77 RKVKGRLL-VGAAVGTREDDKERAEALVEAGVDV--IVIDSAHGHSVYVIEMIKFIKKKYPNVDVIAGNVVTAEAARDLI 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369767 170 LSGADIIKVGVGPGSVCTTRTKTGVGYPQLSAVIECADSAHGLKGHIISDGGCTCPGDVAKAFGAGADFVMLGGMFSGHT 249
Cdd:cd00381 154 DAGADGVKVGIGPGSICTTRIVTGVGVPQATAVADVAAAARDYGVPVIADGGIRTSGDIVKALAAGADAVMLGSLLAGTD 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369767 250 ECAGEVIERNGQKLKLFYGMSSDTAMKKHAG-----GVAEYRASEGKTVEVPYKGDVENTILDILGGLRSTCTYVGAAKL 324
Cdd:cd00381 234 ESPGEYIEINGKRYKEYRGMGSLGAMKKGGGdryfgEEAKKLVPEGVEGIVPYKGSVKDVLPQLVGGLRSSMGYCGAKSL 313
|
330
....*....|..
gi 1937369767 325 KELSRRATFIRV 336
Cdd:cd00381 314 KELQEKARFVRI 325
|
|
| GuaB |
COG0516 |
IMP dehydrogenase/GMP reductase [Nucleotide transport and metabolism]; IMP dehydrogenase/GMP ... |
15-339 |
2.04e-87 |
|
IMP dehydrogenase/GMP reductase [Nucleotide transport and metabolism]; IMP dehydrogenase/GMP reductase is part of the Pathway/BioSystem: Purine biosynthesis
Pssm-ID: 440282 [Multi-domain] Cd Length: 326 Bit Score: 265.92 E-value: 2.04e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369767 15 VLLRPKRSSLKSRSEVDLERTFTFRNSKQTYSGIPVIVANMDTVGTFEMAVVMSQHAMFTAIHKHYSLDDWKH-FAENHP 93
Cdd:COG0516 1 LVLDALRRRLISRSGVVVVVVVGKLTIITTRRRRRDEAVKALVVTTVIEKLLLVTVAGETALLALALLLLKKKkFLLLVD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369767 94 ECLQHVAVSSGSGQNDLEKMSLILEAVPQVKFICLDVANGYSEHfvEFVKLVRSKFPEHTIMAGNVVTGEMVEELILSGA 173
Cdd:COG0516 81 DDGLLLLVLVGVKDDDKEKARALAAADAGVDVLVIDAAHGHSGG--DAMKKIKLTFDDVLLIPGNSATVEPARALVDAGA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369767 174 DIIKVGVGPGSVCTTRTKTGVGYPQLSAVIECADSAHGLKgHIISDGGCTCPGDVAKAFGAGADFVMLGGMFSGHTECAG 253
Cdd:COG0516 159 DLTKVGIGPGSICTTRVVIGLGIPQLSAAMDTVTEARMAI-AIAADGGIGYIHDNAKALAAGADAVMLGSLFAGTEEQPG 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369767 254 EVIERNGQKLKLFYGMSSDtamkkhaggvAEYRASEGKTVEVPYKGDVENTILDILGGLRSTCTYVGAAKLKELSRRATF 333
Cdd:COG0516 238 EVILYQGRSVKRYRGMGSD----------AKKLVPEGIEGRVPYKGPLEDTLHQLLGGLRSGMGYCGARTIEELREKARF 307
|
....*.
gi 1937369767 334 IRVTQQ 339
Cdd:COG0516 308 VRITSA 313
|
|
| IMPDH |
pfam00478 |
IMP dehydrogenase / GMP reductase domain; This family is involved in biosynthesis of guanosine ... |
99-338 |
6.49e-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: 246.15 E-value: 6.49e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369767 99 VAVSSGSGQNDLEKMSLILEAvpQVKFICLDVANGYSEHFVEFVKLVRSKFPEHTIMAGNVVTGEMVEELILSGADIIKV 178
Cdd:pfam00478 211 VGAAVGVGDDTLERAEALVEA--GVDVLVVDTAHGHSKGVIDTVKWIKKKYPDVQVIAGNVATAEGAKALIEAGADAVKV 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369767 179 GVGPGSVCTTRTKTGVGYPQLSAVIECADSAHGLKGHIISDGGCTCPGDVAKAFGAGADFVMLGGMFSGHTECAGEVIER 258
Cdd:pfam00478 289 GIGPGSICTTRVVAGVGVPQLTAIYDVAEAAKKYGVPVIADGGIKYSGDIVKALAAGADAVMLGSLLAGTDESPGEVILY 368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369767 259 NGQKLKLFYGMSSDTAMKKHA------GGVAEYRASEGktVE--VPYKGDVENTILDILGGLRSTCTYVGAAKLKELSRR 330
Cdd:pfam00478 369 QGRRYKSYRGMGSLGAMKKGSkdryfqEDDDKKLVPEG--VEgrVPYKGPLSDVVYQLVGGLRSGMGYCGAKTIEELREK 446
|
....*...
gi 1937369767 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 |
2.92e-62 |
|
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: 205.27 E-value: 2.92e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369767 99 VAVSSGSGQNDLEKMSLILEAvpQVKFICLDVANGYSEHFVEFVKLVRSKFPEHTIMAGNVVTGEMVEELILSGADIIKV 178
Cdd:TIGR01302 215 VGAAVGTREFDKERAEALVKA--GVDVIVIDSSHGHSIYVIDSIKEIKKTYPDLDIIAGNVATAEQAKALIDAGADGLRV 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369767 179 GVGPGSVCTTRTKTGVGYPQLSAVIECADSAHGLKGHIISDGGCTCPGDVAKAFGAGADFVMLGGMFSGHTECAGEVIER 258
Cdd:TIGR01302 293 GIGPGSICTTRIVAGVGVPQITAVYDVAEYAAQSGIPVIADGGIRYSGDIVKALAAGADAVMLGSLLAGTTESPGEYEII 372
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1937369767 259 NGQKLKLFYGMSSDTAMKK-------HAGGVAEYRASEGKTVEVPYKGDVENTILDILGGLRSTCTYVGAAKLKEL 327
Cdd:TIGR01302 373 NGRRYKQYRGMGSLGAMTKgssdrylQDENKTKKFVPEGVEGAVPYKGSVLELLPQLVGGLKSGMGYVGARSIDEL 448
|
|
| PRK05458 |
PRK05458 |
guanosine 5'-monophosphate oxidoreductase; Provisional |
10-345 |
2.77e-60 |
|
guanosine 5'-monophosphate oxidoreductase; Provisional
Pssm-ID: 235479 [Multi-domain] Cd Length: 326 Bit Score: 196.33 E-value: 2.77e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369767 10 LDFKDVLLRPKRSSLKSRSEVDLERTF---TFRnskqtysgIPVIVANMDTVGTFEMAVVMSQHAMFTAIHKhYSLDDWK 86
Cdd:PRK05458 5 FDYEDIQLIPNKCIVNSRSECDTSVTLgprTFK--------LPVVPANMQTIIDEKIAEWLAENGYFYIMHR-FDPEARI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369767 87 HFAENHPECLQHVAVSSGSGQNDLEKMSLILEAVPQVKFICLDVANGYSEHFVEFVKLVRSKFPEHTIMAGNVVTGEMVE 166
Cdd:PRK05458 76 PFIKDMHEQGLIASISVGVKDDEYDFVDQLAAEGLTPEYITIDIAHGHSDSVINMIQHIKKHLPETFVIAGNVGTPEAVR 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369767 167 ELILSGADIIKVGVGPGSVCTTRTKTGVGYP--QLSAVIECADSAhglKGHIISDGGCTCPGDVAKAFGAGADFVMLGGM 244
Cdd:PRK05458 156 ELENAGADATKVGIGPGKVCITKIKTGFGTGgwQLAALRWCAKAA---RKPIIADGGIRTHGDIAKSIRFGATMVMIGSL 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369767 245 FSGHTECAGEVIERNGQKLKLFYGMSSDtaMKKhaggvAEYRASEGKTVEVPYKGDVENTILDILGGLRSTCTYVGAAKL 324
Cdd:PRK05458 233 FAGHEESPGKTVEIDGKLYKEYFGSASE--FQK-----GEYKNVEGKKILVPHKGSLKDTLTEMEQDLQSSISYAGGRDL 305
|
330 340
....*....|....*....|.
gi 1937369767 325 KELsRRATFIRVtqqHNTVFG 345
Cdd:PRK05458 306 DAI-RKVDYVIV---KNSIFN 322
|
|
| PTZ00314 |
PTZ00314 |
inosine-5'-monophosphate dehydrogenase; Provisional |
76-339 |
5.99e-59 |
|
inosine-5'-monophosphate dehydrogenase; Provisional
Pssm-ID: 240355 [Multi-domain] Cd Length: 495 Bit Score: 197.50 E-value: 5.99e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369767 76 IHKHYSLDDWKHFAenhpeclqhVAVSSGSGQNDLEKMSLILEAvpQVKFICLDVANGYSEHFVEFVKLVRSKFPEHTIM 155
Cdd:PTZ00314 218 GYPNASLDSNGQLL---------VGAAISTRPEDIERAAALIEA--GVDVLVVDSSQGNSIYQIDMIKKLKSNYPHVDII 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369767 156 AGNVVTGEMVEELILSGADIIKVGVGPGSVCTTRTKTGVGYPQLSAVIECADSAHGLKGHIISDGGCTCPGDVAKAFGAG 235
Cdd:PTZ00314 287 AGNVVTADQAKNLIDAGADGLRIGMGSGSICITQEVCAVGRPQASAVYHVARYARERGVPCIADGGIKNSGDICKALALG 366
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369767 236 ADFVMLGGMFSGHTECAGEVIERNGQKLKLFYGMSSDTAMKKHAGG------VAEYRASEGKTVEVPYKGDVENTILDIL 309
Cdd:PTZ00314 367 ADCVMLGSLLAGTEEAPGEYFFKDGVRLKVYRGMGSLEAMLSKESGeryldeNETIKVAQGVSGSVVDKGSVAKLIPYLV 446
|
250 260 270
....*....|....*....|....*....|....*
gi 1937369767 310 GGLRSTCTYVGAAKLKEL-----SRRATFIRVTQQ 339
Cdd:PTZ00314 447 KGVKHGMQYIGAHSIPELheklySGQVRFERRSGS 481
|
|
| PRK06843 |
PRK06843 |
inosine 5-monophosphate dehydrogenase; Validated |
10-338 |
1.98e-58 |
|
inosine 5-monophosphate dehydrogenase; Validated
Pssm-ID: 180725 [Multi-domain] Cd Length: 404 Bit Score: 194.10 E-value: 1.98e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369767 10 LDFKDVLLRPKRSSLKSrSEVDLERTFTfrnsKQTYSGIPVIVANMDTVGTFEMAVVMSQHAMFTAIHKHYSLDDWKHFA 89
Cdd:PRK06843 10 LTFDDVSLIPRKSSVLP-SEVSLKTQLT----KNISLNIPFLSSAMDTVTESQMAIAIAKEGGIGIIHKNMSIEAQRKEI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369767 90 E-----------NHPECLQHVAVSSGSGQNDLEK-----------------------------MSLILEAVPQVK----- 124
Cdd:PRK06843 85 EkvktykfqktiNTNGDTNEQKPEIFTAKQHLEKsdayknaehkedfpnackdlnnklrvgaaVSIDIDTIERVEelvka 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369767 125 ---FICLDVANGYSEHFVEFVKLVRSKFPEHTIMAGNVVTGEMVEELILSGADIIKVGVGPGSVCTTRTKTGVGYPQLSA 201
Cdd:PRK06843 165 hvdILVIDSAHGHSTRIIELVKKIKTKYPNLDLIAGNIVTKEAALDLISVGADCLKVGIGPGSICTTRIVAGVGVPQITA 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369767 202 VIECADSAHGLKGHIISDGGCTCPGDVAKAFGAGADFVMLGGMFSGHTECAGEVIERNGQKLKLFYGMSSDTAMKKhaGG 281
Cdd:PRK06843 245 ICDVYEVCKNTNICIIADGGIRFSGDVVKAIAAGADSVMIGNLFAGTKESPSEEIIYNGKKFKSYVGMGSISAMKR--GS 322
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1937369767 282 VAEY----------RASEGKTVEVPYKGDVENTILDILGGLRSTCTYVGAAKLKELSRRATFIRVTQ 338
Cdd:PRK06843 323 KSRYfqlennepkkLVPEGIEGMVPYSGKLKDILTQLKGGLMSGMGYLGAATISDLKINSKFVKISH 389
|
|
| PRK07807 |
PRK07807 |
GuaB1 family IMP dehydrogenase-related protein; |
123-331 |
9.69e-56 |
|
GuaB1 family IMP dehydrogenase-related protein;
Pssm-ID: 181127 [Multi-domain] Cd Length: 479 Bit Score: 188.57 E-value: 9.69e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369767 123 VKFICLDVANGYSEHFVEFVKLVRSKFPEHTIMAGNVVTGEMVEELILSGADIIKVGVGPGSVCTTRTKTGVGYPQLSAV 202
Cdd:PRK07807 240 VDVLVVDTAHGHQEKMLEALRAVRALDPGVPIVAGNVVTAEGTRDLVEAGADIVKVGVGPGAMCTTRMMTGVGRPQFSAV 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369767 203 IECADSAHGLKGHIISDGGCTCPGDVAKAFGAGADFVMLGGMFSGHTECAGEV-IERNGQKLKLFYGMSSDTAMKKHAGG 281
Cdd:PRK07807 320 LECAAAARELGAHVWADGGVRHPRDVALALAAGASNVMIGSWFAGTYESPGDLmRDRDGRPYKESFGMASARAVAARTAG 399
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369767 282 VAEY-RA---------SEGKTVEVPYKGDVENTILDILGGLRSTCTYVGAAKLKELSRRA 331
Cdd:PRK07807 400 DSAFdRArkalfeegiSTSRMYLDPGRPGVEDLLDHITSGVRSSCTYAGARTLAEFHERA 459
|
|
| IMP_DH_rel_1 |
TIGR01303 |
IMP dehydrogenase family protein; This model represents a family of proteins, often annotated ... |
123-332 |
1.63e-53 |
|
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: 182.80 E-value: 1.63e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369767 123 VKFICLDVANGYSEHFVEFVKLVRSKFPEHTIMAGNVVTGEMVEELILSGADIIKVGVGPGSVCTTRTKTGVGYPQLSAV 202
Cdd:TIGR01303 238 VDVLVIDTAHGHQVKMISAIKAVRALDLGVPIVAGNVVSAEGVRDLLEAGANIIKVGVGPGAMCTTRMMTGVGRPQFSAV 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369767 203 IECADSAHGLKGHIISDGGCTCPGDVAKAFGAGADFVMLGGMFSGHTECAGEVI-ERNGQKLKLFYGMSSDTAMKKHAGG 281
Cdd:TIGR01303 318 LECAAEARKLGGHVWADGGVRHPRDVALALAAGASNVMVGSWFAGTYESPGDLMrDRDGRPYKESFGMASKRAVVARTGA 397
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1937369767 282 VAEY-RA---------SEGKTVEVPYKGDVENTILDILGGLRSTCTYVGAAKLKELSRRAT 332
Cdd:TIGR01303 398 DNAFdRArkalfeegiSTSRMGLDPDRGGVEDLIDHIISGVRSSCTYAGASSLEEFHERAV 458
|
|
| PLN02274 |
PLN02274 |
inosine-5'-monophosphate dehydrogenase |
99-277 |
2.93e-32 |
|
inosine-5'-monophosphate dehydrogenase
Pssm-ID: 215154 [Multi-domain] Cd Length: 505 Bit Score: 125.94 E-value: 2.93e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369767 99 VAVSSGSGQNDLEKMSLILEAvpQVKFICLDVANGYSEHFVEFVKLVRSKFPEHTIMAGNVVTGEMVEELILSGADIIKV 178
Cdd:PLN02274 239 VGAAIGTRESDKERLEHLVKA--GVDVVVLDSSQGDSIYQLEMIKYIKKTYPELDVIGGNVVTMYQAQNLIQAGVDGLRV 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369767 179 GVGPGSVCTTRTKTGVGYPQLSAVIECADSAHGLKGHIISDGGCTCPGDVAKAFGAGADFVMLGGMFSGHTECAGEVIER 258
Cdd:PLN02274 317 GMGSGSICTTQEVCAVGRGQATAVYKVASIAAQHGVPVIADGGISNSGHIVKALTLGASTVMMGSFLAGTTEAPGEYFYQ 396
|
170
....*....|....*....
gi 1937369767 259 NGQKLKLFYGMSSDTAMKK 277
Cdd:PLN02274 397 DGVRVKKYRGMGSLEAMTK 415
|
|
| PRK07107 |
PRK07107 |
IMP dehydrogenase; |
104-337 |
3.19e-30 |
|
IMP dehydrogenase;
Pssm-ID: 180842 [Multi-domain] Cd Length: 502 Bit Score: 120.19 E-value: 3.19e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369767 104 GSGQND---LEKMSLILEAvpQVKFICLDVANGYSEHFVEFVKLVRSKFPEHT-IMAGNVVTGEMVEELILSGADIIKVG 179
Cdd:PRK07107 235 GAGINTrdyAERVPALVEA--GADVLCIDSSEGYSEWQKRTLDWIREKYGDSVkVGAGNVVDREGFRYLAEAGADFVKVG 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369767 180 VGPGSVCTTRTKTGVGYPQLSAVIECADS------AHGLKGHIISDGGCTCPGDVAKAFGAGADFVMLGGMFSGHTECAG 253
Cdd:PRK07107 313 IGGGSICITREQKGIGRGQATALIEVAKArdeyfeETGVYIPICSDGGIVYDYHMTLALAMGADFIMLGRYFARFDESPT 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369767 254 EVIERNGQKLKLFYGMSSDTA---MKKHAGGVAEYRASEGKTVEVPYKGDVENTILDILGGLRSTCTYVGAAKLKELSRR 330
Cdd:PRK07107 393 NKVNINGNYMKEYWGEGSNRArnwQRYDLGGDKKLSFEEGVDSYVPYAGSLKDNVAITLSKVRSTMCNCGALSIPELQQK 472
|
....*..
gi 1937369767 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 |
5.20e-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: 43.28 E-value: 5.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369767 140 EFVKLVRSKFPEHTIMAGNVVTGEMVEELILSGADIIkvgVGPGSvcttrtktgvgypqlsaVIECADSAHGLKGHIIsd 219
Cdd:cd00452 44 EAIRALRKEFPEALIGAGTVLTPEQADAAIAAGAQFI---VSPGL-----------------DPEVVKAANRAGIPLL-- 101
|
90 100
....*....|....*....|..
gi 1937369767 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 |
7.20e-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: 40.26 E-value: 7.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369767 128 LDVANGYS-EHFVEFVKLVRSKFPEHTIMAGNVVTGEMVEE-LILSGADIIKVGvgpGSVCTTRTKTGVgyPQLSAVIEC 205
Cdd:cd04722 90 IHGAVGYLaREDLELIRELREAVPDVKVVVKLSPTGELAAAaAEEAGVDEVGLG---NGGGGGGGRDAV--PIADLLLIL 164
|
90 100 110
....*....|....*....|....*....|....*...
gi 1937369767 206 ADSAHGLKghIISDGGCTCPGDVAKAFGAGADFVMLGG 243
Cdd:cd04722 165 AKRGSKVP--VIAGGGINDPEDAAEALALGADGVIVGS 200
|
|
| Glu_synthase |
pfam01645 |
Conserved region in glutamate synthase; This family represents a region of the glutamate ... |
141-242 |
1.89e-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: 39.62 E-value: 1.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369767 141 FVKLVrSKFPEHTIMAGnVVTGemveelilsGADIIKV---GVGPGSVCTTRTKTgVGYPQLSAVIEcADSAHGLKGH-- 215
Cdd:pfam01645 206 SVKLV-SGHGVGTIAAG-VAKA---------GADIILIdgyDGGTGASPKTSIKH-AGLPWELALAE-AHQTLKENGLrd 272
|
90 100 110
....*....|....*....|....*....|
gi 1937369767 216 ---IISDGGCTCPGDVAKAFGAGADFVMLG 242
Cdd:pfam01645 273 rvsLIADGGLRTGADVAKAAALGADAVYIG 302
|
|
| DHOD_DHPD_FMN |
cd02810 |
Dihydroorotate dehydrogenase (DHOD) and Dihydropyrimidine dehydrogenase (DHPD) FMN-binding ... |
98-242 |
3.57e-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: 38.49 E-value: 3.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369767 98 HVAVSSGSGQnDLEKMSLILEAVPQVKFICLDVANGYSEHFVEFVKLVRSKfpEHTIMAGNVVTGEmveeliLSGADIIK 177
Cdd:cd02810 136 NVGGGRQLGQ-DPEAVANLLKAVKAAVDIPLLVKLSPYFDLEDIVELAKAA--ERAGADGLTAINT------ISGRVVDL 206
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1937369767 178 VGVGPGSVcttRTKTGV-GYPQLSAVIEC--ADSAHGLKG-HIISDGGCTCPGDVAKAFGAGADFVMLG 242
Cdd:cd02810 207 KTVGPGPK---RGTGGLsGAPIRPLALRWvaRLAARLQLDiPIIGVGGIDSGEDVLEMLMAGASAVQVA 272
|
|
| GltS_FMN |
cd02808 |
Glutamate synthase (GltS) FMN-binding domain. GltS is a complex iron-sulfur flavoprotein that ... |
210-245 |
8.76e-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: 8.76e-03
10 20 30
....*....|....*....|....*....|....*...
gi 1937369767 210 HGLKGHI--ISDGGCTCPGDVAKAFGAGADFVMLGGMF 245
Cdd:cd02808 280 NGLRDRVslIASGGLRTGADVAKALALGADAVGIGTAA 317
|
|
| |
