|
Name |
Accession |
Description |
Interval |
E-value |
| PurH |
COG0138 |
AICAR transformylase/IMP cyclohydrolase PurH [Nucleotide transport and metabolism]; AICAR ... |
1-511 |
0e+00 |
|
AICAR transformylase/IMP cyclohydrolase PurH [Nucleotide transport and metabolism]; AICAR transformylase/IMP cyclohydrolase PurH is part of the Pathway/BioSystem: Purine biosynthesis
Pssm-ID: 439908 Cd Length: 512 Bit Score: 995.30 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121125129 1 MKKRALVSVSDKTGVVEFVKGLLEQGIEVISTGGTKKLLEENGLQVIGISEVTGFPEIMDGRVKTLHPNIHGGLLAVRDN 80
Cdd:COG0138 2 PIKRALISVSDKTGLVEFARALVELGVEIISTGGTAKALREAGIPVTEVSEVTGFPEILDGRVKTLHPKIHGGILARRDN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121125129 81 ETHIAQMNELGMEPIDYVVVNLYPFKETIAKPDVTFADAIENIDIGGPTMIRSAAKNHKFVSVIVDPVDYDVVLAELKEN 160
Cdd:COG0138 82 PEHVAQLEEHGIEPIDLVVVNLYPFEETVAKPGATLEEAIENIDIGGPAMLRAAAKNHADVAVVVDPADYDAVLEELKAN 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121125129 161 GEVKEETKRKLAAKVFRHTAAYDALISNYLTEQMGEES-PETLTVTFEKKQDLRYGENPHQKATFYKAPFAvTSSVAYAE 239
Cdd:COG0138 162 GGTSLETRRRLAAKAFAHTAAYDAAIANYLAEQLGEEEfPETLTLSFEKVQDLRYGENPHQKAAFYRDPGA-EGGLATAE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121125129 240 QLHGKELSYNNINDADAALSIVKEFTEPAVVAVKHMNPCGVGVGTDIHEAYTRAYEADPVSIFGGIIAANREIDKATAEK 319
Cdd:COG0138 241 QLQGKELSYNNILDADAALELVKEFDEPAVVIVKHANPCGVAVGDTLAEAYEKAYACDPVSAFGGIIAFNRPVDAATAEA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121125129 320 LHEVFLEIVIAPSFSQEALDVLQSKKNLRLLTVDIEKATSASKKLTSVQGGLLVQEEDTLSLDESTISIPTKREPSEQEW 399
Cdd:COG0138 321 IAKIFLEVIIAPDFSPEALEILAKKKNLRLLELGGLDPPAPGLDVKSVSGGLLVQDRDLGLIDPADLKVVTKRAPTEEEL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121125129 400 KDLKLAWKVVKHVKSNAIVLANDNMTVGVGAGQMNRVGSAKIAITQAGEKAQGSALASDAFFPMPDTVEEAAKAGITAII 479
Cdd:COG0138 401 ADLLFAWKVVKHVKSNAIVLAKDGATVGIGAGQMSRVDSARIALEKAGERAKGSVLASDAFFPFRDGVEAAAKAGITAII 480
|
490 500 510
....*....|....*....|....*....|..
gi 1121125129 480 QPGGSIRDEDSIKVADKYGIAMVFTGVRHFKH 511
Cdd:COG0138 481 QPGGSIRDEEVIAAADEHGIAMVFTGMRHFRH 512
|
|
| purH |
PRK00881 |
bifunctional phosphoribosylaminoimidazolecarboxamide formyltransferase/IMP cyclohydrolase; ... |
1-511 |
0e+00 |
|
bifunctional phosphoribosylaminoimidazolecarboxamide formyltransferase/IMP cyclohydrolase; Provisional
Pssm-ID: 234854 Cd Length: 513 Bit Score: 990.36 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121125129 1 MKKRALVSVSDKTGVVEFVKGLLEQGIEVISTGGTKKLLEENGLQVIGISEVTGFPEIMDGRVKTLHPNIHGGLLAVRDN 80
Cdd:PRK00881 3 MIKRALISVSDKTGIVEFAKALVELGVEILSTGGTAKLLAEAGIPVTEVSDVTGFPEILDGRVKTLHPKIHGGILARRDN 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121125129 81 ETHIAQMNELGMEPIDYVVVNLYPFKETIAKPDVTFADAIENIDIGGPTMIRSAAKNHKFVSVIVDPVDYDVVLAELKEN 160
Cdd:PRK00881 83 PEHVAALEEHGIEPIDLVVVNLYPFEETVAKPGVTLEEAIENIDIGGPTMVRAAAKNHKDVAVVVDPADYDAVLEELKAN 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121125129 161 GEVKEETKRKLAAKVFRHTAAYDALISNYLTEQMGEESPETLTVTFEKKQDLRYGENPHQKATFYKAPFAvTSSVAYAEQ 240
Cdd:PRK00881 163 GSTTLETRFRLAAKAFAHTAAYDAAIANYLTEQVGEEFPETLNLSFEKKQDLRYGENPHQKAAFYRDPNA-EGGVATAEQ 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121125129 241 LHGKELSYNNINDADAALSIVKEFTEPAVVAVKHMNPCGVGVGTDIHEAYTRAYEADPVSIFGGIIAANREIDKATAEKL 320
Cdd:PRK00881 242 LQGKELSYNNIADADAALELVKEFDEPACVIVKHANPCGVAVGDTILEAYDKAYACDPVSAFGGIIAFNREVDAETAEAI 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121125129 321 HEVFLEIVIAPSFSQEALDVLQSKKNLRLLTVDieKATSASKKLTSVQGGLLVQEEDTLSLDESTISIPTKREPSEQEWK 400
Cdd:PRK00881 322 HKIFLEVIIAPSFSEEALEILAKKKNLRLLECP--FPGGWEGDFKSVSGGLLVQDRDLGMVDPADLKVVTKRQPTEQELK 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121125129 401 DLKLAWKVVKHVKSNAIVLANDNMTVGVGAGQMNRVGSAKIAITQAGEKA---QGSALASDAFFPMPDTVEEAAKAGITA 477
Cdd:PRK00881 400 DLLFAWKVVKHVKSNAIVYAKDGQTVGIGAGQMSRVDSARIAIEKAGDAGldlKGAVLASDAFFPFRDGVEAAAKAGITA 479
|
490 500 510
....*....|....*....|....*....|....
gi 1121125129 478 IIQPGGSIRDEDSIKVADKYGIAMVFTGVRHFKH 511
Cdd:PRK00881 480 IIQPGGSIRDEEVIAAADEHGIAMVFTGVRHFRH 513
|
|
| purH |
TIGR00355 |
phosphoribosylaminoimidazolecarboxamide formyltransferase/IMP cyclohydrolase; PurH is ... |
3-511 |
0e+00 |
|
phosphoribosylaminoimidazolecarboxamide formyltransferase/IMP cyclohydrolase; PurH is bifunctional: IMP cyclohydrolase (EC 3.5.4.10); phosphoribosylaminoimidazolecarboxamide formyltransferase (EC 2.1.2.3) Involved in purine ribonucleotide biosynthesis. The IMP cyclohydrolase activity is in the N-terminal region. [Purines, pyrimidines, nucleosides, and nucleotides, Purine ribonucleotide biosynthesis]
Pssm-ID: 273032 Cd Length: 511 Bit Score: 796.73 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121125129 3 KRALVSVSDKTGVVEFVKGLLEQGIEVISTGGTKKLLEENGLQVIGISEVTGFPEIMDGRVKTLHPNIHGGLLAVRDNET 82
Cdd:TIGR00355 1 RRALLSVSDKTGIVEFAQGLVERGVELLSTGGTAKLLAEAGVPVTEVSDYTGFPEMMDGRVKTLHPKVHGGILARRGDDD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121125129 83 HiAQMNELGMEPIDYVVVNLYPFKETIAKPDVTFADAIENIDIGGPTMIRSAAKNHKFVSVIVDPVDYDVVLAELKENGE 162
Cdd:TIGR00355 81 D-ADLEEHGIEPIDLVVVNLYPFKETVAKPGVTLAEAVENIDIGGPTMLRAAAKNHADVTILVDPKDYSAILSELDEQGS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121125129 163 VKEETKRKLAAKVFRHTAAYDALISNYLTEQMGEESPETLTVTFEKKQDLRYGENPHQKATFYKAPFAVTSSVAYAEQLH 242
Cdd:TIGR00355 160 ISLALRFDLAIKAFEHTAAYDAAIANYFGKLVGEKEPRQFNLNFTKKQTLRYGENPHQKAAFYVTQNVKEGSVATAEQLQ 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121125129 243 GKELSYNNINDADAALSIVKEFTEPAVVAVKHMNPCGVGVGTDIHEAYTRAYEADPVSIFGGIIAANREIDKATAEKLHE 322
Cdd:TIGR00355 240 GKELSYNNIADADAALEIVKEFDEPAAVIVKHANPCGVALGKTILDAYDRAFGADPTSAFGGIIALNRELDVPTAKAIVR 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121125129 323 VFLEIVIAPSFSQEALDVLQSKKNLRLLTVDIEKATSASKKLTSVQGGLLVQEEDTLSLDESTISIPTKREPSEQEWKDL 402
Cdd:TIGR00355 320 QFLEVIIAPGYSAEALEILAKKKNLRVLILGIWANRVPELDFKRVNGGLLVQDRDDGMVDQSTLKVVTKRQPTEQELIDL 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121125129 403 KLAWKVVKHVKSNAIVLANDNMTVGVGAGQMNRVGSAKIAITQA---GEKAQGSALASDAFFPMPDTVEEAAKAGITAII 479
Cdd:TIGR00355 400 LFAWKVAKHVKSNAIVYAKNNMTVGVGAGQMSRVGSAKIAGIKAddeGLEAKGSSLASDAFFPFRDGVEEAAAAGITCII 479
|
490 500 510
....*....|....*....|....*....|..
gi 1121125129 480 QPGGSIRDEDSIKVADKYGIAMVFTGVRHFKH 511
Cdd:TIGR00355 480 QPGGSMRDEDSIWAADEHGIVMVFTGMRHFRH 511
|
|
| AICARFT_IMPCHas |
pfam01808 |
AICARFT/IMPCHase bienzyme; This is a family of bifunctional enzymes catalysing the last two ... |
134-445 |
0e+00 |
|
AICARFT/IMPCHase bienzyme; This is a family of bifunctional enzymes catalysing the last two steps in de novo purine biosynthesis. The bifunctional enzyme is found in both prokaryotes and eukaryotes. The second last step is catalyzed by 5-aminoimidazole-4-carboxamide ribonucleotide formyltransferase EC:2.1.2.3 (AICARFT), this enzyme catalyzes the formylation of AICAR with 10-formyl-tetrahydrofolate to yield FAICAR and tetrahydrofolate. This is catalyzed by a pair of C-terminal deaminase fold domains in the protein, where the active site is formed by the dimeric interface of two monomeric units. The last step is catalyzed by the N-terminal IMP (Inosine monophosphate) cyclohydrolase domain EC:3.5.4.10 (IMPCHase), cyclizing FAICAR (5-formylaminoimidazole-4-carboxamide ribonucleotide) to IMP.
Pssm-ID: 460341 Cd Length: 308 Bit Score: 546.23 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121125129 134 AAKNHKFVSVIVDPVDYDVVLAELKENGEVKEETKRKLAAKVFRHTAAYDALISNYLTeqmGEESPETLTVTFEKKQDLR 213
Cdd:pfam01808 1 AAKNHKDVTVVVDPADYAEVLEELKANGGTSLETRRRLAAKAFAHTAAYDAAIANYLA---GKEFPETLTLSFEKVQDLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121125129 214 YGENPHQKATFYKAPFAvTSSVAYAEQLHGKELSYNNINDADAALSIVKEFTEPAVVAVKHMNPCGVGVGTDIHEAYTRA 293
Cdd:pfam01808 78 YGENPHQKAAFYRDPGP-AGGLATAEQLQGKELSYNNILDADAALELVKEFDEPAAVIVKHANPCGVAVGDTLAEAYRRA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121125129 294 YEADPVSIFGGIIAANREIDKATAEKLHEVFLEIVIAPSFSQEALDVLQSKKNLRLLTVDIEKATSASKKLTSVQGGLLV 373
Cdd:pfam01808 157 LAADPVSAFGGIIALNRPVDAATAEEISKIFLEVIIAPGFTPEALEILKKKKNLRLLEIDPLYPPPPGLEFRSVSGGLLV 236
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1121125129 374 QEEDTLSLDESTISIPTKREPSEQEWKDLKLAWKVVKHVKSNAIVLANDNMTVGVGAGQMNRVGSAKIAITQ 445
Cdd:pfam01808 237 QDRDDALIDPDDLKVVTKRAPTEEELRDLLFAWKVVKHVKSNAIVYAKDGQTVGIGAGQMSRVDSARIAIEK 308
|
|
| AICARFT_IMPCHas |
smart00798 |
AICARFT/IMPCHase bienzyme; This is a family of bifunctional enzymes catalysing the last two ... |
134-446 |
0e+00 |
|
AICARFT/IMPCHase bienzyme; This is a family of bifunctional enzymes catalysing the last two steps in de novo purine biosynthesis. The bifunctional enzyme is found in both prokaryotes and eukaryotes. The second last step is catalysed by 5-aminoimidazole-4-carboxamide ribonucleotide formyltransferase (AICARFT), this enzyme catalyses the formylation of AICAR with 10-formyl-tetrahydrofolate to yield FAICAR and tetrahydrofolate. The last step is catalysed by IMP (Inosine monophosphate) cyclohydrolase (IMPCHase), cyclizing FAICAR (5-formylaminoimidazole-4-carboxamide ribonucleotide) to IMP.
Pssm-ID: 214822 Cd Length: 311 Bit Score: 531.30 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121125129 134 AAKNHKFVSVIVDPVDYDVVLAELKENGEVKEETKRKLAAKVFRHTAAYDALISNYLTEQMGEESPETLTVTFEKKQDLR 213
Cdd:smart00798 1 AAKNHKDVTVVVDPADYAEVLEELKANGGLSLETRKRLAAKAFAHTAAYDAAISNYLAKQLASEFPETLTLSFEKKQDLR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121125129 214 YGENPHQKATFYKAPFAVtSSVAYAEQLHGKELSYNNINDADAALSIVKEFTEPAVVAVKHMNPCGVGVGTDIHEAYTRA 293
Cdd:smart00798 81 YGENPHQKAAFYTDPDAL-GGIATAKQLQGKELSYNNILDADAALELVKEFDEPACVIVKHANPCGVAVGDTLAEAYRKA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121125129 294 YEADPVSIFGGIIAANREIDKATAEKLHEVFLEIVIAPSFSQEALDVLQSKKNLRLLTVDiEKATSASKKLTSVQGGLLV 373
Cdd:smart00798 160 YAADPVSAFGGIIAFNRPVDEETAEAINKIFLEVIIAPDFDEEALEILSKKKNLRLLECG-PLPDPDGLEFKSVSGGLLV 238
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1121125129 374 QEEDTLSLDESTISIPTKREPSEQEWKDLKLAWKVVKHVKSNAIVLANDNMTVGVGAGQMNRVGSAKIAITQA 446
Cdd:smart00798 239 QDRDNGGIDPEDLKVVTKRQPTEEELADLLFAWKVVKHVKSNAIVYAKDGQTVGIGAGQMSRVDSARIAAEKA 311
|
|
| IMPCH |
cd01421 |
Inosine monophosphate cyclohydrolase domain. This is the N-terminal domain in the purine ... |
3-190 |
9.05e-110 |
|
Inosine monophosphate cyclohydrolase domain. This is the N-terminal domain in the purine biosynthesis pathway protein ATIC (purH). The bifunctional ATIC protein contains a C-terminal ATIC formylase domain that formylates 5-aminoimidazole-4-carboxamide-ribonucleotide. The IMPCH domain then converts the formyl-5-aminoimidazole-4-carboxamide-ribonucleotide to inosine monophosphate. This is the final step in de novo purine production.
Pssm-ID: 238709 [Multi-domain] Cd Length: 187 Bit Score: 323.78 E-value: 9.05e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121125129 3 KRALVSVSDKTGVVEFVKGLLEQGIEVISTGGTKKLLEENGLQVIGISEVTGFPEIMDGRVKTLHPNIHGGLLAVRDNET 82
Cdd:cd01421 1 KRALISVSDKTGLVEFAKELVELGVEILSTGGTAKFLKEAGIPVTDVSDITGFPEILGGRVKTLHPKIHGGILARRDNEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121125129 83 HiAQMNELGMEPIDYVVVNLYPFKETIAKPDVTFADAIENIDIGGPTMIRSAAKNHKFVSVIVDPVDYDVVLAELKENGE 162
Cdd:cd01421 81 H-KDLEEHGIEPIDLVVVNLYPFEETVAKGNVTLEEAIENIDIGGPSLLRAAAKNYKDVTVLVDPADYQKVLEELKSNGS 159
|
170 180
....*....|....*....|....*...
gi 1121125129 163 VKEETKRKLAAKVFRHTAAYDALISNYL 190
Cdd:cd01421 160 ISEETRRRLALKAFAHTAEYDAAISNYL 187
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PurH |
COG0138 |
AICAR transformylase/IMP cyclohydrolase PurH [Nucleotide transport and metabolism]; AICAR ... |
1-511 |
0e+00 |
|
AICAR transformylase/IMP cyclohydrolase PurH [Nucleotide transport and metabolism]; AICAR transformylase/IMP cyclohydrolase PurH is part of the Pathway/BioSystem: Purine biosynthesis
Pssm-ID: 439908 Cd Length: 512 Bit Score: 995.30 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121125129 1 MKKRALVSVSDKTGVVEFVKGLLEQGIEVISTGGTKKLLEENGLQVIGISEVTGFPEIMDGRVKTLHPNIHGGLLAVRDN 80
Cdd:COG0138 2 PIKRALISVSDKTGLVEFARALVELGVEIISTGGTAKALREAGIPVTEVSEVTGFPEILDGRVKTLHPKIHGGILARRDN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121125129 81 ETHIAQMNELGMEPIDYVVVNLYPFKETIAKPDVTFADAIENIDIGGPTMIRSAAKNHKFVSVIVDPVDYDVVLAELKEN 160
Cdd:COG0138 82 PEHVAQLEEHGIEPIDLVVVNLYPFEETVAKPGATLEEAIENIDIGGPAMLRAAAKNHADVAVVVDPADYDAVLEELKAN 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121125129 161 GEVKEETKRKLAAKVFRHTAAYDALISNYLTEQMGEES-PETLTVTFEKKQDLRYGENPHQKATFYKAPFAvTSSVAYAE 239
Cdd:COG0138 162 GGTSLETRRRLAAKAFAHTAAYDAAIANYLAEQLGEEEfPETLTLSFEKVQDLRYGENPHQKAAFYRDPGA-EGGLATAE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121125129 240 QLHGKELSYNNINDADAALSIVKEFTEPAVVAVKHMNPCGVGVGTDIHEAYTRAYEADPVSIFGGIIAANREIDKATAEK 319
Cdd:COG0138 241 QLQGKELSYNNILDADAALELVKEFDEPAVVIVKHANPCGVAVGDTLAEAYEKAYACDPVSAFGGIIAFNRPVDAATAEA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121125129 320 LHEVFLEIVIAPSFSQEALDVLQSKKNLRLLTVDIEKATSASKKLTSVQGGLLVQEEDTLSLDESTISIPTKREPSEQEW 399
Cdd:COG0138 321 IAKIFLEVIIAPDFSPEALEILAKKKNLRLLELGGLDPPAPGLDVKSVSGGLLVQDRDLGLIDPADLKVVTKRAPTEEEL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121125129 400 KDLKLAWKVVKHVKSNAIVLANDNMTVGVGAGQMNRVGSAKIAITQAGEKAQGSALASDAFFPMPDTVEEAAKAGITAII 479
Cdd:COG0138 401 ADLLFAWKVVKHVKSNAIVLAKDGATVGIGAGQMSRVDSARIALEKAGERAKGSVLASDAFFPFRDGVEAAAKAGITAII 480
|
490 500 510
....*....|....*....|....*....|..
gi 1121125129 480 QPGGSIRDEDSIKVADKYGIAMVFTGVRHFKH 511
Cdd:COG0138 481 QPGGSIRDEEVIAAADEHGIAMVFTGMRHFRH 512
|
|
| purH |
PRK00881 |
bifunctional phosphoribosylaminoimidazolecarboxamide formyltransferase/IMP cyclohydrolase; ... |
1-511 |
0e+00 |
|
bifunctional phosphoribosylaminoimidazolecarboxamide formyltransferase/IMP cyclohydrolase; Provisional
Pssm-ID: 234854 Cd Length: 513 Bit Score: 990.36 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121125129 1 MKKRALVSVSDKTGVVEFVKGLLEQGIEVISTGGTKKLLEENGLQVIGISEVTGFPEIMDGRVKTLHPNIHGGLLAVRDN 80
Cdd:PRK00881 3 MIKRALISVSDKTGIVEFAKALVELGVEILSTGGTAKLLAEAGIPVTEVSDVTGFPEILDGRVKTLHPKIHGGILARRDN 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121125129 81 ETHIAQMNELGMEPIDYVVVNLYPFKETIAKPDVTFADAIENIDIGGPTMIRSAAKNHKFVSVIVDPVDYDVVLAELKEN 160
Cdd:PRK00881 83 PEHVAALEEHGIEPIDLVVVNLYPFEETVAKPGVTLEEAIENIDIGGPTMVRAAAKNHKDVAVVVDPADYDAVLEELKAN 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121125129 161 GEVKEETKRKLAAKVFRHTAAYDALISNYLTEQMGEESPETLTVTFEKKQDLRYGENPHQKATFYKAPFAvTSSVAYAEQ 240
Cdd:PRK00881 163 GSTTLETRFRLAAKAFAHTAAYDAAIANYLTEQVGEEFPETLNLSFEKKQDLRYGENPHQKAAFYRDPNA-EGGVATAEQ 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121125129 241 LHGKELSYNNINDADAALSIVKEFTEPAVVAVKHMNPCGVGVGTDIHEAYTRAYEADPVSIFGGIIAANREIDKATAEKL 320
Cdd:PRK00881 242 LQGKELSYNNIADADAALELVKEFDEPACVIVKHANPCGVAVGDTILEAYDKAYACDPVSAFGGIIAFNREVDAETAEAI 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121125129 321 HEVFLEIVIAPSFSQEALDVLQSKKNLRLLTVDieKATSASKKLTSVQGGLLVQEEDTLSLDESTISIPTKREPSEQEWK 400
Cdd:PRK00881 322 HKIFLEVIIAPSFSEEALEILAKKKNLRLLECP--FPGGWEGDFKSVSGGLLVQDRDLGMVDPADLKVVTKRQPTEQELK 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121125129 401 DLKLAWKVVKHVKSNAIVLANDNMTVGVGAGQMNRVGSAKIAITQAGEKA---QGSALASDAFFPMPDTVEEAAKAGITA 477
Cdd:PRK00881 400 DLLFAWKVVKHVKSNAIVYAKDGQTVGIGAGQMSRVDSARIAIEKAGDAGldlKGAVLASDAFFPFRDGVEAAAKAGITA 479
|
490 500 510
....*....|....*....|....*....|....
gi 1121125129 478 IIQPGGSIRDEDSIKVADKYGIAMVFTGVRHFKH 511
Cdd:PRK00881 480 IIQPGGSIRDEEVIAAADEHGIAMVFTGVRHFRH 513
|
|
| purH |
TIGR00355 |
phosphoribosylaminoimidazolecarboxamide formyltransferase/IMP cyclohydrolase; PurH is ... |
3-511 |
0e+00 |
|
phosphoribosylaminoimidazolecarboxamide formyltransferase/IMP cyclohydrolase; PurH is bifunctional: IMP cyclohydrolase (EC 3.5.4.10); phosphoribosylaminoimidazolecarboxamide formyltransferase (EC 2.1.2.3) Involved in purine ribonucleotide biosynthesis. The IMP cyclohydrolase activity is in the N-terminal region. [Purines, pyrimidines, nucleosides, and nucleotides, Purine ribonucleotide biosynthesis]
Pssm-ID: 273032 Cd Length: 511 Bit Score: 796.73 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121125129 3 KRALVSVSDKTGVVEFVKGLLEQGIEVISTGGTKKLLEENGLQVIGISEVTGFPEIMDGRVKTLHPNIHGGLLAVRDNET 82
Cdd:TIGR00355 1 RRALLSVSDKTGIVEFAQGLVERGVELLSTGGTAKLLAEAGVPVTEVSDYTGFPEMMDGRVKTLHPKVHGGILARRGDDD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121125129 83 HiAQMNELGMEPIDYVVVNLYPFKETIAKPDVTFADAIENIDIGGPTMIRSAAKNHKFVSVIVDPVDYDVVLAELKENGE 162
Cdd:TIGR00355 81 D-ADLEEHGIEPIDLVVVNLYPFKETVAKPGVTLAEAVENIDIGGPTMLRAAAKNHADVTILVDPKDYSAILSELDEQGS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121125129 163 VKEETKRKLAAKVFRHTAAYDALISNYLTEQMGEESPETLTVTFEKKQDLRYGENPHQKATFYKAPFAVTSSVAYAEQLH 242
Cdd:TIGR00355 160 ISLALRFDLAIKAFEHTAAYDAAIANYFGKLVGEKEPRQFNLNFTKKQTLRYGENPHQKAAFYVTQNVKEGSVATAEQLQ 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121125129 243 GKELSYNNINDADAALSIVKEFTEPAVVAVKHMNPCGVGVGTDIHEAYTRAYEADPVSIFGGIIAANREIDKATAEKLHE 322
Cdd:TIGR00355 240 GKELSYNNIADADAALEIVKEFDEPAAVIVKHANPCGVALGKTILDAYDRAFGADPTSAFGGIIALNRELDVPTAKAIVR 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121125129 323 VFLEIVIAPSFSQEALDVLQSKKNLRLLTVDIEKATSASKKLTSVQGGLLVQEEDTLSLDESTISIPTKREPSEQEWKDL 402
Cdd:TIGR00355 320 QFLEVIIAPGYSAEALEILAKKKNLRVLILGIWANRVPELDFKRVNGGLLVQDRDDGMVDQSTLKVVTKRQPTEQELIDL 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121125129 403 KLAWKVVKHVKSNAIVLANDNMTVGVGAGQMNRVGSAKIAITQA---GEKAQGSALASDAFFPMPDTVEEAAKAGITAII 479
Cdd:TIGR00355 400 LFAWKVAKHVKSNAIVYAKNNMTVGVGAGQMSRVGSAKIAGIKAddeGLEAKGSSLASDAFFPFRDGVEEAAAAGITCII 479
|
490 500 510
....*....|....*....|....*....|..
gi 1121125129 480 QPGGSIRDEDSIKVADKYGIAMVFTGVRHFKH 511
Cdd:TIGR00355 480 QPGGSMRDEDSIWAADEHGIVMVFTGMRHFRH 511
|
|
| PLN02891 |
PLN02891 |
IMP cyclohydrolase |
2-511 |
0e+00 |
|
IMP cyclohydrolase
Pssm-ID: 178479 [Multi-domain] Cd Length: 547 Bit Score: 618.34 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121125129 2 KKRALVSVSDKTGVVEFVKGLLEQGIEVISTGGTKKLLEENGLQVIGISEVTGFPEIMDGRVKTLHPNIHGGLLAVRDNE 81
Cdd:PLN02891 22 KKQALISLSDKTDLALLANGLQELGYTIVSTGGTASALEAAGVSVTKVEELTNFPEMLDGRVKTLHPAVHGGILARRDQE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121125129 82 THIAQMNELGMEPIDYVVVNLYPFKETIAKPDVTFADAIENIDIGGPTMIRSAAKNHKFVSVIVDPVDYDVVLAELKENG 161
Cdd:PLN02891 102 HHMEALNEHGIGTIDVVVVNLYPFYDTVTSGGISFEDGVENIDIGGPAMIRAAAKNHKDVLVVVDPADYPALLEYLKGKQ 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121125129 162 EVKEETKRKLAAKVFRHTAAYDALISNYLTEQMGEES--PETLTVTFEKKQDLRYGENPHQKATFY--KAPFAVTS-SVA 236
Cdd:PLN02891 182 DDQQDFRRKLAWKAFQHVASYDSAVSEWLWKQINGGGkfPPSLTVPLTLKSSLRYGENPHQKAAFYvdKSLSEVNAgGIA 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121125129 237 YAEQLHGKELSYNNINDADAALSIVKEFTEPAVVAVKHMNPCGVGVGTDIHEAYTRAYEADPVSIFGGIIAANREIDKAT 316
Cdd:PLN02891 262 TAIQHHGKEMSYNNYLDADAAWNCVSEFSNPTCVVVKHTNPCGVASRGDILEAYRLAVRADPVSAFGGIVAFNCEVDEDL 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121125129 317 AEKLHE----------VFLEIVIAPSFSQEALDVLQSK-KNLRLLtvDIEKATSASKKLTSVQGGLLVQEEDTLSLDEST 385
Cdd:PLN02891 342 AREIREfrsptdgetrMFYEIVVAPKYTEKGLEVLKGKsKTLRIL--EAKPRKKGRLSLRQVGGGWLAQDSDDLTPEDIT 419
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121125129 386 ISIPTKREPSEQEWKDLKLAWKVVKHVKSNAIVLANDNMTVGVGAGQMNRVGSAKIAITQAGEKAQGSALASDAFFPMP- 464
Cdd:PLN02891 420 FTVVSEKVPTESELEDAKFAWLCVKHVKSNAIVVAKNNRMLGMGSGQPNRVESLRIALEKAGEEAKGAALASDAFFPFAw 499
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 1121125129 465 -DTVEEAAKAGITAIIQPGGSIRDEDSIKVADKYGIAMVFTGVRHFKH 511
Cdd:PLN02891 500 nDAVEEACQAGVKVIAEPGGSMRDQDAIDCCNKYGVALLFTGVRHFRH 547
|
|
| AICARFT_IMPCHas |
pfam01808 |
AICARFT/IMPCHase bienzyme; This is a family of bifunctional enzymes catalysing the last two ... |
134-445 |
0e+00 |
|
AICARFT/IMPCHase bienzyme; This is a family of bifunctional enzymes catalysing the last two steps in de novo purine biosynthesis. The bifunctional enzyme is found in both prokaryotes and eukaryotes. The second last step is catalyzed by 5-aminoimidazole-4-carboxamide ribonucleotide formyltransferase EC:2.1.2.3 (AICARFT), this enzyme catalyzes the formylation of AICAR with 10-formyl-tetrahydrofolate to yield FAICAR and tetrahydrofolate. This is catalyzed by a pair of C-terminal deaminase fold domains in the protein, where the active site is formed by the dimeric interface of two monomeric units. The last step is catalyzed by the N-terminal IMP (Inosine monophosphate) cyclohydrolase domain EC:3.5.4.10 (IMPCHase), cyclizing FAICAR (5-formylaminoimidazole-4-carboxamide ribonucleotide) to IMP.
Pssm-ID: 460341 Cd Length: 308 Bit Score: 546.23 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121125129 134 AAKNHKFVSVIVDPVDYDVVLAELKENGEVKEETKRKLAAKVFRHTAAYDALISNYLTeqmGEESPETLTVTFEKKQDLR 213
Cdd:pfam01808 1 AAKNHKDVTVVVDPADYAEVLEELKANGGTSLETRRRLAAKAFAHTAAYDAAIANYLA---GKEFPETLTLSFEKVQDLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121125129 214 YGENPHQKATFYKAPFAvTSSVAYAEQLHGKELSYNNINDADAALSIVKEFTEPAVVAVKHMNPCGVGVGTDIHEAYTRA 293
Cdd:pfam01808 78 YGENPHQKAAFYRDPGP-AGGLATAEQLQGKELSYNNILDADAALELVKEFDEPAAVIVKHANPCGVAVGDTLAEAYRRA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121125129 294 YEADPVSIFGGIIAANREIDKATAEKLHEVFLEIVIAPSFSQEALDVLQSKKNLRLLTVDIEKATSASKKLTSVQGGLLV 373
Cdd:pfam01808 157 LAADPVSAFGGIIALNRPVDAATAEEISKIFLEVIIAPGFTPEALEILKKKKNLRLLEIDPLYPPPPGLEFRSVSGGLLV 236
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1121125129 374 QEEDTLSLDESTISIPTKREPSEQEWKDLKLAWKVVKHVKSNAIVLANDNMTVGVGAGQMNRVGSAKIAITQ 445
Cdd:pfam01808 237 QDRDDALIDPDDLKVVTKRAPTEEELRDLLFAWKVVKHVKSNAIVYAKDGQTVGIGAGQMSRVDSARIAIEK 308
|
|
| AICARFT_IMPCHas |
smart00798 |
AICARFT/IMPCHase bienzyme; This is a family of bifunctional enzymes catalysing the last two ... |
134-446 |
0e+00 |
|
AICARFT/IMPCHase bienzyme; This is a family of bifunctional enzymes catalysing the last two steps in de novo purine biosynthesis. The bifunctional enzyme is found in both prokaryotes and eukaryotes. The second last step is catalysed by 5-aminoimidazole-4-carboxamide ribonucleotide formyltransferase (AICARFT), this enzyme catalyses the formylation of AICAR with 10-formyl-tetrahydrofolate to yield FAICAR and tetrahydrofolate. The last step is catalysed by IMP (Inosine monophosphate) cyclohydrolase (IMPCHase), cyclizing FAICAR (5-formylaminoimidazole-4-carboxamide ribonucleotide) to IMP.
Pssm-ID: 214822 Cd Length: 311 Bit Score: 531.30 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121125129 134 AAKNHKFVSVIVDPVDYDVVLAELKENGEVKEETKRKLAAKVFRHTAAYDALISNYLTEQMGEESPETLTVTFEKKQDLR 213
Cdd:smart00798 1 AAKNHKDVTVVVDPADYAEVLEELKANGGLSLETRKRLAAKAFAHTAAYDAAISNYLAKQLASEFPETLTLSFEKKQDLR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121125129 214 YGENPHQKATFYKAPFAVtSSVAYAEQLHGKELSYNNINDADAALSIVKEFTEPAVVAVKHMNPCGVGVGTDIHEAYTRA 293
Cdd:smart00798 81 YGENPHQKAAFYTDPDAL-GGIATAKQLQGKELSYNNILDADAALELVKEFDEPACVIVKHANPCGVAVGDTLAEAYRKA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121125129 294 YEADPVSIFGGIIAANREIDKATAEKLHEVFLEIVIAPSFSQEALDVLQSKKNLRLLTVDiEKATSASKKLTSVQGGLLV 373
Cdd:smart00798 160 YAADPVSAFGGIIAFNRPVDEETAEAINKIFLEVIIAPDFDEEALEILSKKKNLRLLECG-PLPDPDGLEFKSVSGGLLV 238
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1121125129 374 QEEDTLSLDESTISIPTKREPSEQEWKDLKLAWKVVKHVKSNAIVLANDNMTVGVGAGQMNRVGSAKIAITQA 446
Cdd:smart00798 239 QDRDNGGIDPEDLKVVTKRQPTEEELADLLFAWKVVKHVKSNAIVYAKDGQTVGIGAGQMSRVDSARIAAEKA 311
|
|
| IMPCH |
cd01421 |
Inosine monophosphate cyclohydrolase domain. This is the N-terminal domain in the purine ... |
3-190 |
9.05e-110 |
|
Inosine monophosphate cyclohydrolase domain. This is the N-terminal domain in the purine biosynthesis pathway protein ATIC (purH). The bifunctional ATIC protein contains a C-terminal ATIC formylase domain that formylates 5-aminoimidazole-4-carboxamide-ribonucleotide. The IMPCH domain then converts the formyl-5-aminoimidazole-4-carboxamide-ribonucleotide to inosine monophosphate. This is the final step in de novo purine production.
Pssm-ID: 238709 [Multi-domain] Cd Length: 187 Bit Score: 323.78 E-value: 9.05e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121125129 3 KRALVSVSDKTGVVEFVKGLLEQGIEVISTGGTKKLLEENGLQVIGISEVTGFPEIMDGRVKTLHPNIHGGLLAVRDNET 82
Cdd:cd01421 1 KRALISVSDKTGLVEFAKELVELGVEILSTGGTAKFLKEAGIPVTDVSDITGFPEILGGRVKTLHPKIHGGILARRDNEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121125129 83 HiAQMNELGMEPIDYVVVNLYPFKETIAKPDVTFADAIENIDIGGPTMIRSAAKNHKFVSVIVDPVDYDVVLAELKENGE 162
Cdd:cd01421 81 H-KDLEEHGIEPIDLVVVNLYPFEETVAKGNVTLEEAIENIDIGGPSLLRAAAKNYKDVTVLVDPADYQKVLEELKSNGS 159
|
170 180
....*....|....*....|....*...
gi 1121125129 163 VKEETKRKLAAKVFRHTAAYDALISNYL 190
Cdd:cd01421 160 ISEETRRRLALKAFAHTAEYDAAISNYL 187
|
|
| PRK07106 |
PRK07106 |
phosphoribosylaminoimidazolecarboxamide formyltransferase; |
212-511 |
6.72e-55 |
|
phosphoribosylaminoimidazolecarboxamide formyltransferase;
Pssm-ID: 180841 Cd Length: 390 Bit Score: 189.10 E-value: 6.72e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121125129 212 LRYGENPHQK-ATFY----KAPFAVtssvayaeqLHGKElSYNNINDADAALSIVKEFTE----PAVVAVKHMNPCGVGV 282
Cdd:PRK07106 6 LKYGCNPNQKpARIFmkegELPIEV---------LNGRP-GYINFLDALNSWQLVKELKEatglPAAASFKHVSPAGAAV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121125129 283 G------------------TDIHEAYTRAYEADPVSIFGGIIAANREIDKATAEKL-HEVfLEIVIAPSFSQEALDVLQS 343
Cdd:PRK07106 76 GlplsdtlkkiyfvddmelSPLACAYARARGADRMSSYGDFAALSDVCDVETAKLLkREV-SDGIIAPGYTPEALEILKA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121125129 344 KKNLRLLTVDIEKA-TSASKKLTSVQGGLLVQEEDTLSLDESTIS-IPTK-REPSEQEWKDLKLAWKVVKHVKSNAIVLA 420
Cdd:PRK07106 155 KKKGNYNIIKIDPNyEPAPIETKDVFGITFEQGRNELKIDEDLLKnIVTEnKELPDEAKRDLIIALITLKYTQSNSVCYA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121125129 421 NDNMTVGVGAGQMNRVGSAKIA---------------------------------------------------------- 442
Cdd:PRK07106 235 KDGQAIGIGAGQQSRIHCTRLAgnkadiwylrqhpkvlnlpfkegirrpdrdnaidvylsddymdvladgvwqqfftekp 314
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1121125129 443 --ITQAGEKA-----QGSALASDAFFPMPDTVEEAAKAGITAIIQPGGSIRDEDSIKVADKYGIAMVFTGVRHFKH 511
Cdd:PRK07106 315 epLTREEKRAwlatlTGVALGSDAFFPFGDNIERAAKSGVKYIAQPGGSIRDDNVIETCNKYGMTMAFTGVRLFHH 390
|
|
| MGS |
pfam02142 |
MGS-like domain; This domain composes the whole protein of methylglyoxal synthetase and the ... |
14-129 |
6.02e-24 |
|
MGS-like domain; This domain composes the whole protein of methylglyoxal synthetase and the domain is also found in Carbamoyl phosphate synthetase (CPS) where it forms a regulatory domain that binds to the allosteric effector ornithine. This family also includes inosicase. The known structures in this family show a common phosphate binding site.
Pssm-ID: 460462 [Multi-domain] Cd Length: 93 Bit Score: 95.63 E-value: 6.02e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121125129 14 GVVEFVKGLLEQGIEVISTGGTKKLLEENGLQVIGISEVTGFPeIMDGRVKtlhpnihggllavrdnetHIAQMNELGme 93
Cdd:pfam02142 1 GLVELAKALVELGFELLATGGTAKFLREAGIPVTEVVEKTGEG-RPGGRVQ------------------IGDLIKNGE-- 59
|
90 100 110
....*....|....*....|....*....|....*.
gi 1121125129 94 pIDYVVVNLYPFKETIAkPDVTFADAIENIDIGGPT 129
Cdd:pfam02142 60 -IDLVINTLYPFKATVH-DGYAIRRAAENIDIPGPT 93
|
|
| MGS |
smart00851 |
MGS-like domain; This domain composes the whole protein of methylglyoxal synthetase and the ... |
14-129 |
8.97e-24 |
|
MGS-like domain; This domain composes the whole protein of methylglyoxal synthetase and the domain is also found in Carbamoyl phosphate synthetase (CPS) where it forms a regulatory domain that binds to the allosteric effector ornithine. This family also includes inosicase. The known structures in this family show a common phosphate binding site.
Pssm-ID: 214855 [Multi-domain] Cd Length: 91 Bit Score: 95.23 E-value: 8.97e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121125129 14 GVVEFVKGLLEQGIEVISTGGTKKLLEENGLQVigisevtgfpeimdgrVKTLHPNIHGGLLAVRDnethiaqmnELGME 93
Cdd:smart00851 1 GLVEFAKRLAELGFELLATGGTAKFLREAGLPV----------------VKTLHPKVHGGIPQILD---------LIKNG 55
|
90 100 110
....*....|....*....|....*....|....*.
gi 1121125129 94 PIDYVVVNLYPFKETIAKPDVTFADAIENIDIGGPT 129
Cdd:smart00851 56 EIDLVINTLYPFEAQAHEDGYSIRRAAENIDIPGPT 91
|
|
| MGS-like |
cd00532 |
MGS-like domain. This domain composes the whole protein of methylglyoxal synthetase, which ... |
4-153 |
2.27e-09 |
|
MGS-like domain. This domain composes the whole protein of methylglyoxal synthetase, which catalyzes the enolization of dihydroxyacetone phosphate (DHAP) to produce methylglyoxal. The family also includes the C-terminal domain in carbamoyl phosphate synthetase (CPS) where it catalyzes the last phosphorylation of a coaboxyphosphate intermediate to form the product carbamoyl phosphate and may also play a regulatory role. This family also includes inosine monophosphate cyclohydrolase. The known structures in this family show a common phosphate binding site.
Pssm-ID: 238297 [Multi-domain] Cd Length: 112 Bit Score: 55.21 E-value: 2.27e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1121125129 4 RALVSVSD--KTGVVEFVKGLLEQGIEVISTGGTKKLLEENGLQVIGISEVTGFpeimdgrvktLHPNIHGGLLAvrdne 81
Cdd:cd00532 1 GVFLSVSDhvKAMLVDLAPKLSSDGFPLFATGGTSRVLADAGIPVRAVSKRHED----------GEPTVDAAIAE----- 65
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1121125129 82 thiaqmnelgMEPIDYVVVNLYPFKEtiakpdvtfadaiENIDIGGPTMIRSAAKNHkfVSVIVDPVDYDVV 153
Cdd:cd00532 66 ----------KGKFDVVINLRDPRRD-------------RCTDEDGTALLRLARLYK--IPVTTPNATAMFV 112
|
|
| carB |
PRK05294 |
carbamoyl-phosphate synthase large subunit; |
2-60 |
1.91e-06 |
|
carbamoyl-phosphate synthase large subunit;
Pssm-ID: 235393 [Multi-domain] Cd Length: 1066 Bit Score: 50.87 E-value: 1.91e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1121125129 2 KKRALVSV--SDKTGVVEFVKGLLEQGIEVISTGGTKKLLEENGLQVIGISEVT-GFPEIMD 60
Cdd:PRK05294 937 SGTVFLSVrdRDKEEVVELAKRLLELGFKILATSGTAKFLREAGIPVELVNKVHeGRPHIVD 998
|
|
| MGS_CPS_II |
cd01424 |
Methylglyoxal synthase-like domain from type II glutamine-dependent carbamoyl phosphate ... |
4-61 |
5.64e-06 |
|
Methylglyoxal synthase-like domain from type II glutamine-dependent carbamoyl phosphate synthetase (CSP). CSP, a CarA and CarB heterodimer, catalyzes the production of carbamoyl phosphate which is subsequently employed in the metabolic pathways responsible for the synthesis of pyrimidine nucleotides or arginine. The MGS-like domain is the C-terminal domain of CarB and appears to play a regulatory role in CPS function by binding allosteric effector molecules, including UMP and ornithine.
Pssm-ID: 238712 [Multi-domain] Cd Length: 110 Bit Score: 45.16 E-value: 5.64e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1121125129 4 RALVSV--SDKTGVVEFVKGLLEQGIEVISTGGTKKLLEENGLQVIGISEVT-GFPEIMDG 61
Cdd:cd01424 2 TVFISVadRDKPEAVEIAKRLAELGFKLVATEGTAKYLQEAGIPVEVVNKVSeGRPNIVDL 62
|
|
| CPSaseII_lrg |
TIGR01369 |
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes ... |
2-60 |
6.96e-03 |
|
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes the first committed step in pyrimidine, arginine, and urea biosynthesis. In general, it is a glutamine-dependent enzyme, EC 6.3.5.5, termed CPSase II in eukaryotes. An exception is the mammalian mitochondrial urea-cycle form, CPSase I, in which the glutamine amidotransferase domain active site Cys on the small subunit has been lost, and the enzyme is ammonia-dependent. In both CPSase I and the closely related, glutamine-dependent CPSase III (allosterically activated by acetyl-glutamate) demonstrated in some other vertebrates, the small and large chain regions are fused in a single polypeptide chain. This model represents the large chain of glutamine-hydrolysing carbamoyl-phosphate synthases, or the corresponding regions of larger, multifunctional proteins, as found in all domains of life, and CPSase I forms are considered exceptions within the family. In several thermophilic species (Methanobacterium thermoautotrophicum, Methanococcus jannaschii, Aquifex aeolicus), the large subunit appears split, at different points, into two separate genes. [Purines, pyrimidines, nucleosides, and nucleotides, Pyrimidine ribonucleotide biosynthesis]
Pssm-ID: 273581 [Multi-domain] Cd Length: 1050 Bit Score: 39.21 E-value: 6.96e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1121125129 2 KKRALVSV--SDKTGVVEFVKGLLEQGIEVISTGGTKKLLEENGLQ---VIGISEvtGFPEIMD 60
Cdd:TIGR01369 937 KGSVLLSVrdKDKEELLDLARKLAEKGYKLYATEGTAKFLGEAGIKpelVLKVSE--GRPNILD 998
|
|
| |
