|
Name |
Accession |
Description |
Interval |
E-value |
| purH |
TIGR00355 |
phosphoribosylaminoimidazolecarboxamide formyltransferase/IMP cyclohydrolase; PurH is ... |
5-355 |
6.68e-145 |
|
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: 419.62 E-value: 6.68e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26338005 5 QLALFSVSDKTGLVEFARSLASLGLSLVASGGTAKAIRDAGLAVRDVSELTGFPEMLGGRVKTLHPAVHAGILARNIPED 84
Cdd:TIGR00355 1 RRALLSVSDKTGIVEFAQGLVERGVELLSTGGTAKLLAEAGVPVTEVSDYTGFPEMMDGRVKTLHPKVHGGILARRGDDD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26338005 85 AADMARLDFNLVRVVVCNLYPFVKTVASPDVTVEAAVEQIDIGGVTLLRAAAKNHARVTVVCEPEDYAGVAAEMhgSDSK 164
Cdd:TIGR00355 81 DADLEEHGIEPIDLVVVNLYPFKETVAKPGVTLAEAVENIDIGGPTMLRAAAKNHADVTILVDPKDYSAILSEL--DEQG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26338005 165 DTSLETRRHLALKAFTHTAQYDEAISDYFRKQYSK---------GISQMPLRYGMNPHQTPAQLYTLKPKLPI----TVL 231
Cdd:TIGR00355 159 SISLALRFDLAIKAFEHTAAYDAAIANYFGKLVGEkeprqfnlnFTKKQTLRYGENPHQKAAFYVTQNVKEGSvataEQL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26338005 232 NG-APGFINLCDALNAWQLVTELrgavDIPAAASFKHVSPAGAAVGVPLSEdearvcmvydlyptltplavAYARARGAD 310
Cdd:TIGR00355 239 QGkELSYNNIADADAALEIVKEF----DEPAAVIVKHANPCGVALGKTILD--------------------AYDRAFGAD 294
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 26338005 311 RMSSFGDFVALSDICDVPTAKIISREVSDGIVAPGYEEEALKILS 355
Cdd:TIGR00355 295 PTSAFGGIIALNRELDVPTAKAIVRQFLEVIIAPGYSAEALEILA 339
|
|
| PurH |
COG0138 |
AICAR transformylase/IMP cyclohydrolase PurH [Nucleotide transport and metabolism]; AICAR ... |
3-355 |
4.27e-139 |
|
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: 404.79 E-value: 4.27e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26338005 3 PSQLALFSVSDKTGLVEFARSLASLGLSLVASGGTAKAIRDAGLAVRDVSELTGFPEMLGGRVKTLHPAVHAGILA-RNI 81
Cdd:COG0138 2 PIKRALISVSDKTGLVEFARALVELGVEIISTGGTAKALREAGIPVTEVSEVTGFPEILDGRVKTLHPKIHGGILArRDN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26338005 82 PEDAADMARLDFNLVRVVVCNLYPFVKTVASPDVTVEAAVEQIDIGGVTLLRAAAKNHARVTVVCEPEDYAGVAAEMhgS 161
Cdd:COG0138 82 PEHVAQLEEHGIEPIDLVVVNLYPFEETVAKPGATLEEAIENIDIGGPAMLRAAAKNHADVAVVVDPADYDAVLEEL--K 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26338005 162 DSKDTSLETRRHLALKAFTHTAQYDEAISDYFRKQYSK----------GISQMPLRYGMNPHQTpAQLYTLKPKLP---- 227
Cdd:COG0138 160 ANGGTSLETRRRLAAKAFAHTAAYDAAIANYLAEQLGEeefpetltlsFEKVQDLRYGENPHQK-AAFYRDPGAEGglat 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26338005 228 ITVLNGAP-GFINLCDALNAWQLVTELrgavDIPAAASFKHVSPAGAAVGVPLSEdearvcmvydlyptltplavAYARA 306
Cdd:COG0138 239 AEQLQGKElSYNNILDADAALELVKEF----DEPAVVIVKHANPCGVAVGDTLAE--------------------AYEKA 294
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 26338005 307 RGADRMSSFGDFVALSDICDVPTAKIISR---EVsdgIVAPGYEEEALKILS 355
Cdd:COG0138 295 YACDPVSAFGGIIAFNRPVDAATAEAIAKiflEV---IIAPDFSPEALEILA 343
|
|
| purH |
PRK00881 |
bifunctional phosphoribosylaminoimidazolecarboxamide formyltransferase/IMP cyclohydrolase; ... |
1-355 |
1.24e-137 |
|
bifunctional phosphoribosylaminoimidazolecarboxamide formyltransferase/IMP cyclohydrolase; Provisional
Pssm-ID: 234854 Cd Length: 513 Bit Score: 401.01 E-value: 1.24e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26338005 1 MAPSQLALFSVSDKTGLVEFARSLASLGLSLVASGGTAKAIRDAGLAVRDVSELTGFPEMLGGRVKTLHPAVHAGILA-R 79
Cdd:PRK00881 1 RRMIKRALISVSDKTGIVEFAKALVELGVEILSTGGTAKLLAEAGIPVTEVSDVTGFPEILDGRVKTLHPKIHGGILArR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26338005 80 NIPEDAADMARLDFNLVRVVVCNLYPFVKTVASPDVTVEAAVEQIDIGGVTLLRAAAKNHARVTVVCEPEDYAGVAAEMh 159
Cdd:PRK00881 81 DNPEHVAALEEHGIEPIDLVVVNLYPFEETVAKPGVTLEEAIENIDIGGPTMVRAAAKNHKDVAVVVDPADYDAVLEEL- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26338005 160 gSDSKDTSLETRRHLALKAFTHTAQYDEAISDYFRKQYSK---------GISQMPLRYGMNPHQTpAQLY-TLKPKLPI- 228
Cdd:PRK00881 160 -KANGSTTLETRFRLAAKAFAHTAAYDAAIANYLTEQVGEefpetlnlsFEKKQDLRYGENPHQK-AAFYrDPNAEGGVa 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26338005 229 --TVLNG-APGFINLCDALNAWQLVTELrgavDIPAAASFKHVSPAGAAVGVPLSEdearvcmvydlyptltplavAYAR 305
Cdd:PRK00881 238 taEQLQGkELSYNNIADADAALELVKEF----DEPACVIVKHANPCGVAVGDTILE--------------------AYDK 293
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 26338005 306 ARGADRMSSFGDFVALSDICDVPTAKIISR---EVsdgIVAPGYEEEALKILS 355
Cdd:PRK00881 294 AYACDPVSAFGGIIAFNREVDAETAEAIHKiflEV---IIAPSFSEEALEILA 343
|
|
| IMPCH |
cd01421 |
Inosine monophosphate cyclohydrolase domain. This is the N-terminal domain in the purine ... |
5-193 |
6.47e-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: 318.39 E-value: 6.47e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26338005 5 QLALFSVSDKTGLVEFARSLASLGLSLVASGGTAKAIRDAGLAVRDVSELTGFPEMLGGRVKTLHPAVHAGILARNIPED 84
Cdd:cd01421 1 KRALISVSDKTGLVEFAKELVELGVEILSTGGTAKFLKEAGIPVTDVSDITGFPEILGGRVKTLHPKIHGGILARRDNEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26338005 85 AADMARLDFNLVRVVVCNLYPFVKTVASPDVTVEAAVEQIDIGGVTLLRAAAKNHARVTVVCEPEDYAGVAAEMhgSDSK 164
Cdd:cd01421 81 HKDLEEHGIEPIDLVVVNLYPFEETVAKGNVTLEEAIENIDIGGPSLLRAAAKNYKDVTVLVDPADYQKVLEEL--KSNG 158
|
170 180
....*....|....*....|....*....
gi 26338005 165 DTSLETRRHLALKAFTHTAQYDEAISDYF 193
Cdd:cd01421 159 SISEETRRRLALKAFAHTAEYDAAISNYL 187
|
|
| AICARFT_IMPCHas |
smart00798 |
AICARFT/IMPCHase bienzyme; This is a family of bifunctional enzymes catalysing the last two ... |
135-355 |
9.31e-85 |
|
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: 258.96 E-value: 9.31e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26338005 135 AAKNHARVTVVCEPEDYAGVAAEMHGSDSkdTSLETRRHLALKAFTHTAQYDEAISDYFRKQYSK---------GISQMP 205
Cdd:smart00798 1 AAKNHKDVTVVVDPADYAEVLEELKANGG--LSLETRKRLAAKAFAHTAAYDAAISNYLAKQLASefpetltlsFEKKQD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26338005 206 LRYGMNPHQtPAQLYTLKPKL----PITVLNGAP-GFINLCDALNAWQLVTELrgavDIPAAASFKHVSPAGAAVGVPLS 280
Cdd:smart00798 79 LRYGENPHQ-KAAFYTDPDALggiaTAKQLQGKElSYNNILDADAALELVKEF----DEPACVIVKHANPCGVAVGDTLA 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 26338005 281 EdearvcmvydlyptltplavAYARARGADRMSSFGDFVALSDICDVPTAKIISREVSDGIVAPGYEEEALKILS 355
Cdd:smart00798 154 E--------------------AYRKAYAADPVSAFGGIIAFNRPVDEETAEAINKIFLEVIIAPDFDEEALEILS 208
|
|
| AICARFT_IMPCHas |
pfam01808 |
AICARFT/IMPCHase bienzyme; This is a family of bifunctional enzymes catalysing the last two ... |
135-355 |
7.31e-84 |
|
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: 256.56 E-value: 7.31e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26338005 135 AAKNHARVTVVCEPEDYAGVAAEMhgSDSKDTSLETRRHLALKAFTHTAQYDEAISDYFR-KQYSKGISQ-----MPLRY 208
Cdd:pfam01808 1 AAKNHKDVTVVVDPADYAEVLEEL--KANGGTSLETRRRLAAKAFAHTAAYDAAIANYLAgKEFPETLTLsfekvQDLRY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26338005 209 GMNPHQTpAQLYTLKPKLP----ITVLNG-APGFINLCDALNAWQLVTELrgavDIPAAASFKHVSPAGAAVGVPLSEde 283
Cdd:pfam01808 79 GENPHQK-AAFYRDPGPAGglatAEQLQGkELSYNNILDADAALELVKEF----DEPAAVIVKHANPCGVAVGDTLAE-- 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 26338005 284 arvcmvydlyptltplavAYARARGADRMSSFGDFVALSDICDVPTAKIISREVSDGIVAPGYEEEALKILS 355
Cdd:pfam01808 152 ------------------AYRRALAADPVSAFGGIIALNRPVDAATAEEISKIFLEVIIAPGFTPEALEILK 205
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| purH |
TIGR00355 |
phosphoribosylaminoimidazolecarboxamide formyltransferase/IMP cyclohydrolase; PurH is ... |
5-355 |
6.68e-145 |
|
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: 419.62 E-value: 6.68e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26338005 5 QLALFSVSDKTGLVEFARSLASLGLSLVASGGTAKAIRDAGLAVRDVSELTGFPEMLGGRVKTLHPAVHAGILARNIPED 84
Cdd:TIGR00355 1 RRALLSVSDKTGIVEFAQGLVERGVELLSTGGTAKLLAEAGVPVTEVSDYTGFPEMMDGRVKTLHPKVHGGILARRGDDD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26338005 85 AADMARLDFNLVRVVVCNLYPFVKTVASPDVTVEAAVEQIDIGGVTLLRAAAKNHARVTVVCEPEDYAGVAAEMhgSDSK 164
Cdd:TIGR00355 81 DADLEEHGIEPIDLVVVNLYPFKETVAKPGVTLAEAVENIDIGGPTMLRAAAKNHADVTILVDPKDYSAILSEL--DEQG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26338005 165 DTSLETRRHLALKAFTHTAQYDEAISDYFRKQYSK---------GISQMPLRYGMNPHQTPAQLYTLKPKLPI----TVL 231
Cdd:TIGR00355 159 SISLALRFDLAIKAFEHTAAYDAAIANYFGKLVGEkeprqfnlnFTKKQTLRYGENPHQKAAFYVTQNVKEGSvataEQL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26338005 232 NG-APGFINLCDALNAWQLVTELrgavDIPAAASFKHVSPAGAAVGVPLSEdearvcmvydlyptltplavAYARARGAD 310
Cdd:TIGR00355 239 QGkELSYNNIADADAALEIVKEF----DEPAAVIVKHANPCGVALGKTILD--------------------AYDRAFGAD 294
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 26338005 311 RMSSFGDFVALSDICDVPTAKIISREVSDGIVAPGYEEEALKILS 355
Cdd:TIGR00355 295 PTSAFGGIIALNRELDVPTAKAIVRQFLEVIIAPGYSAEALEILA 339
|
|
| PurH |
COG0138 |
AICAR transformylase/IMP cyclohydrolase PurH [Nucleotide transport and metabolism]; AICAR ... |
3-355 |
4.27e-139 |
|
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: 404.79 E-value: 4.27e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26338005 3 PSQLALFSVSDKTGLVEFARSLASLGLSLVASGGTAKAIRDAGLAVRDVSELTGFPEMLGGRVKTLHPAVHAGILA-RNI 81
Cdd:COG0138 2 PIKRALISVSDKTGLVEFARALVELGVEIISTGGTAKALREAGIPVTEVSEVTGFPEILDGRVKTLHPKIHGGILArRDN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26338005 82 PEDAADMARLDFNLVRVVVCNLYPFVKTVASPDVTVEAAVEQIDIGGVTLLRAAAKNHARVTVVCEPEDYAGVAAEMhgS 161
Cdd:COG0138 82 PEHVAQLEEHGIEPIDLVVVNLYPFEETVAKPGATLEEAIENIDIGGPAMLRAAAKNHADVAVVVDPADYDAVLEEL--K 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26338005 162 DSKDTSLETRRHLALKAFTHTAQYDEAISDYFRKQYSK----------GISQMPLRYGMNPHQTpAQLYTLKPKLP---- 227
Cdd:COG0138 160 ANGGTSLETRRRLAAKAFAHTAAYDAAIANYLAEQLGEeefpetltlsFEKVQDLRYGENPHQK-AAFYRDPGAEGglat 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26338005 228 ITVLNGAP-GFINLCDALNAWQLVTELrgavDIPAAASFKHVSPAGAAVGVPLSEdearvcmvydlyptltplavAYARA 306
Cdd:COG0138 239 AEQLQGKElSYNNILDADAALELVKEF----DEPAVVIVKHANPCGVAVGDTLAE--------------------AYEKA 294
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 26338005 307 RGADRMSSFGDFVALSDICDVPTAKIISR---EVsdgIVAPGYEEEALKILS 355
Cdd:COG0138 295 YACDPVSAFGGIIAFNRPVDAATAEAIAKiflEV---IIAPDFSPEALEILA 343
|
|
| purH |
PRK00881 |
bifunctional phosphoribosylaminoimidazolecarboxamide formyltransferase/IMP cyclohydrolase; ... |
1-355 |
1.24e-137 |
|
bifunctional phosphoribosylaminoimidazolecarboxamide formyltransferase/IMP cyclohydrolase; Provisional
Pssm-ID: 234854 Cd Length: 513 Bit Score: 401.01 E-value: 1.24e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26338005 1 MAPSQLALFSVSDKTGLVEFARSLASLGLSLVASGGTAKAIRDAGLAVRDVSELTGFPEMLGGRVKTLHPAVHAGILA-R 79
Cdd:PRK00881 1 RRMIKRALISVSDKTGIVEFAKALVELGVEILSTGGTAKLLAEAGIPVTEVSDVTGFPEILDGRVKTLHPKIHGGILArR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26338005 80 NIPEDAADMARLDFNLVRVVVCNLYPFVKTVASPDVTVEAAVEQIDIGGVTLLRAAAKNHARVTVVCEPEDYAGVAAEMh 159
Cdd:PRK00881 81 DNPEHVAALEEHGIEPIDLVVVNLYPFEETVAKPGVTLEEAIENIDIGGPTMVRAAAKNHKDVAVVVDPADYDAVLEEL- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26338005 160 gSDSKDTSLETRRHLALKAFTHTAQYDEAISDYFRKQYSK---------GISQMPLRYGMNPHQTpAQLY-TLKPKLPI- 228
Cdd:PRK00881 160 -KANGSTTLETRFRLAAKAFAHTAAYDAAIANYLTEQVGEefpetlnlsFEKKQDLRYGENPHQK-AAFYrDPNAEGGVa 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26338005 229 --TVLNG-APGFINLCDALNAWQLVTELrgavDIPAAASFKHVSPAGAAVGVPLSEdearvcmvydlyptltplavAYAR 305
Cdd:PRK00881 238 taEQLQGkELSYNNIADADAALELVKEF----DEPACVIVKHANPCGVAVGDTILE--------------------AYDK 293
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 26338005 306 ARGADRMSSFGDFVALSDICDVPTAKIISR---EVsdgIVAPGYEEEALKILS 355
Cdd:PRK00881 294 AYACDPVSAFGGIIAFNREVDAETAEAIHKiflEV---IIAPSFSEEALEILA 343
|
|
| IMPCH |
cd01421 |
Inosine monophosphate cyclohydrolase domain. This is the N-terminal domain in the purine ... |
5-193 |
6.47e-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: 318.39 E-value: 6.47e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26338005 5 QLALFSVSDKTGLVEFARSLASLGLSLVASGGTAKAIRDAGLAVRDVSELTGFPEMLGGRVKTLHPAVHAGILARNIPED 84
Cdd:cd01421 1 KRALISVSDKTGLVEFAKELVELGVEILSTGGTAKFLKEAGIPVTDVSDITGFPEILGGRVKTLHPKIHGGILARRDNEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26338005 85 AADMARLDFNLVRVVVCNLYPFVKTVASPDVTVEAAVEQIDIGGVTLLRAAAKNHARVTVVCEPEDYAGVAAEMhgSDSK 164
Cdd:cd01421 81 HKDLEEHGIEPIDLVVVNLYPFEETVAKGNVTLEEAIENIDIGGPSLLRAAAKNYKDVTVLVDPADYQKVLEEL--KSNG 158
|
170 180
....*....|....*....|....*....
gi 26338005 165 DTSLETRRHLALKAFTHTAQYDEAISDYF 193
Cdd:cd01421 159 SISEETRRRLALKAFAHTAEYDAAISNYL 187
|
|
| PRK07106 |
PRK07106 |
phosphoribosylaminoimidazolecarboxamide formyltransferase; |
203-355 |
4.15e-89 |
|
phosphoribosylaminoimidazolecarboxamide formyltransferase;
Pssm-ID: 180841 Cd Length: 390 Bit Score: 273.08 E-value: 4.15e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26338005 203 QMPLRYGMNPHQTPAQLYTLKPKLPITVLNGAPGFINLCDALNAWQLVTELRGAVDIPAAASFKHVSPAGAAVGVPLSED 282
Cdd:PRK07106 3 ELELKYGCNPNQKPARIFMKEGELPIEVLNGRPGYINFLDALNSWQLVKELKEATGLPAAASFKHVSPAGAAVGLPLSDT 82
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 26338005 283 EARVCMVYDLypTLTPLAVAYARARGADRMSSFGDFVALSDICDVPTAKIISREVSDGIVAPGYEEEALKILS 355
Cdd:PRK07106 83 LKKIYFVDDM--ELSPLACAYARARGADRMSSYGDFAALSDVCDVETAKLLKREVSDGIIAPGYTPEALEILK 153
|
|
| AICARFT_IMPCHas |
smart00798 |
AICARFT/IMPCHase bienzyme; This is a family of bifunctional enzymes catalysing the last two ... |
135-355 |
9.31e-85 |
|
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: 258.96 E-value: 9.31e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26338005 135 AAKNHARVTVVCEPEDYAGVAAEMHGSDSkdTSLETRRHLALKAFTHTAQYDEAISDYFRKQYSK---------GISQMP 205
Cdd:smart00798 1 AAKNHKDVTVVVDPADYAEVLEELKANGG--LSLETRKRLAAKAFAHTAAYDAAISNYLAKQLASefpetltlsFEKKQD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26338005 206 LRYGMNPHQtPAQLYTLKPKL----PITVLNGAP-GFINLCDALNAWQLVTELrgavDIPAAASFKHVSPAGAAVGVPLS 280
Cdd:smart00798 79 LRYGENPHQ-KAAFYTDPDALggiaTAKQLQGKElSYNNILDADAALELVKEF----DEPACVIVKHANPCGVAVGDTLA 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 26338005 281 EdearvcmvydlyptltplavAYARARGADRMSSFGDFVALSDICDVPTAKIISREVSDGIVAPGYEEEALKILS 355
Cdd:smart00798 154 E--------------------AYRKAYAADPVSAFGGIIAFNRPVDEETAEAINKIFLEVIIAPDFDEEALEILS 208
|
|
| AICARFT_IMPCHas |
pfam01808 |
AICARFT/IMPCHase bienzyme; This is a family of bifunctional enzymes catalysing the last two ... |
135-355 |
7.31e-84 |
|
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: 256.56 E-value: 7.31e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26338005 135 AAKNHARVTVVCEPEDYAGVAAEMhgSDSKDTSLETRRHLALKAFTHTAQYDEAISDYFR-KQYSKGISQ-----MPLRY 208
Cdd:pfam01808 1 AAKNHKDVTVVVDPADYAEVLEEL--KANGGTSLETRRRLAAKAFAHTAAYDAAIANYLAgKEFPETLTLsfekvQDLRY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26338005 209 GMNPHQTpAQLYTLKPKLP----ITVLNG-APGFINLCDALNAWQLVTELrgavDIPAAASFKHVSPAGAAVGVPLSEde 283
Cdd:pfam01808 79 GENPHQK-AAFYRDPGPAGglatAEQLQGkELSYNNILDADAALELVKEF----DEPAAVIVKHANPCGVAVGDTLAE-- 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 26338005 284 arvcmvydlyptltplavAYARARGADRMSSFGDFVALSDICDVPTAKIISREVSDGIVAPGYEEEALKILS 355
Cdd:pfam01808 152 ------------------AYRRALAADPVSAFGGIIALNRPVDAATAEEISKIFLEVIIAPGFTPEALEILK 205
|
|
| PLN02891 |
PLN02891 |
IMP cyclohydrolase |
7-354 |
4.60e-81 |
|
IMP cyclohydrolase
Pssm-ID: 178479 [Multi-domain] Cd Length: 547 Bit Score: 257.02 E-value: 4.60e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26338005 7 ALFSVSDKTGLVEFARSLASLGLSLVASGGTAKAIRDAGLAVRDVSELTGFPEMLGGRVKTLHPAVHAGILA-RNIPEDA 85
Cdd:PLN02891 25 ALISLSDKTDLALLANGLQELGYTIVSTGGTASALEAAGVSVTKVEELTNFPEMLDGRVKTLHPAVHGGILArRDQEHHM 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26338005 86 ADMARLDFNLVRVVVCNLYPFVKTVASPDVTVEAAVEQIDIGGVTLLRAAAKNHARVTVVCEPEDYAGVAAEMHGSDSKD 165
Cdd:PLN02891 105 EALNEHGIGTIDVVVVNLYPFYDTVTSGGISFEDGVENIDIGGPAMIRAAAKNHKDVLVVVDPADYPALLEYLKGKQDDQ 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26338005 166 TSLetRRHLALKAFTHTAQYDEAISDYFRKQYSKGISQMP-----------LRYGMNPHQtPAQLYTLKpklPITVLNGA 234
Cdd:PLN02891 185 QDF--RRKLAWKAFQHVASYDSAVSEWLWKQINGGGKFPPsltvpltlkssLRYGENPHQ-KAAFYVDK---SLSEVNAG 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26338005 235 P------------GFINLCDALNAWQLVTELRGavdiPAAASFKHVSPAGAAVGVPLSEdearvcmvydlyptltplavA 302
Cdd:PLN02891 259 GiataiqhhgkemSYNNYLDADAAWNCVSEFSN----PTCVVVKHTNPCGVASRGDILE--------------------A 314
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 26338005 303 YARARGADRMSSFGDFVALSDICDVPTAKIIS--REVSDG--------IVAPGYEEEALKIL 354
Cdd:PLN02891 315 YRLAVRADPVSAFGGIVAFNCEVDEDLAREIRefRSPTDGetrmfyeiVVAPKYTEKGLEVL 376
|
|
| MGS |
pfam02142 |
MGS-like domain; This domain composes the whole protein of methylglyoxal synthetase and the ... |
16-130 |
3.57e-23 |
|
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: 92.17 E-value: 3.57e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26338005 16 GLVEFARSLASLGLSLVASGGTAKAIRDAGLAVRDVSELTGFPeMLGGRVktlhpavhagilarnipEDAADMARLDFNL 95
Cdd:pfam02142 1 GLVELAKALVELGFELLATGGTAKFLREAGIPVTEVVEKTGEG-RPGGRV-----------------QIGDLIKNGEIDL 62
|
90 100 110
....*....|....*....|....*....|....*
gi 26338005 96 vrvVVCNLYPFVKTVAsPDVTVEAAVEQIDIGGVT 130
Cdd:pfam02142 63 ---VINTLYPFKATVH-DGYAIRRAAENIDIPGPT 93
|
|
| MGS |
smart00851 |
MGS-like domain; This domain composes the whole protein of methylglyoxal synthetase and the ... |
16-130 |
4.37e-23 |
|
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: 91.77 E-value: 4.37e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26338005 16 GLVEFARSLASLGLSLVASGGTAKAIRDAGLAVrdvseltgfpemlggrVKTLHPAVHAGILarnipedaADMARLDFNL 95
Cdd:smart00851 1 GLVEFAKRLAELGFELLATGGTAKFLREAGLPV----------------VKTLHPKVHGGIP--------QILDLIKNGE 56
|
90 100 110
....*....|....*....|....*....|....*
gi 26338005 96 VRVVVCNLYPFVKTVASPDVTVEAAVEQIDIGGVT 130
Cdd:smart00851 57 IDLVINTLYPFEAQAHEDGYSIRRAAENIDIPGPT 91
|
|
| MGS-like |
cd00532 |
MGS-like domain. This domain composes the whole protein of methylglyoxal synthetase, which ... |
6-151 |
3.51e-19 |
|
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: 81.79 E-value: 3.51e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26338005 6 LALFSVSD--KTGLVEFARSLASLGLSLVASGGTAKAIRDAGLAVRDVSELTGFpemlggrvktLHPAVHAGILARnipe 83
Cdd:cd00532 1 GVFLSVSDhvKAMLVDLAPKLSSDGFPLFATGGTSRVLADAGIPVRAVSKRHED----------GEPTVDAAIAEK---- 66
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 26338005 84 daadmarldfNLVRVVVCNLYPFVKtvaspdvtveaavEQIDIGGVTLLRAAAKNHarVTVVCEPEDY 151
Cdd:cd00532 67 ----------GKFDVVINLRDPRRD-------------RCTDEDGTALLRLARLYK--IPVTTPNATA 109
|
|
| MGS_CPS_II |
cd01424 |
Methylglyoxal synthase-like domain from type II glutamine-dependent carbamoyl phosphate ... |
7-51 |
6.96e-08 |
|
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: 50.17 E-value: 6.96e-08
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 26338005 7 ALFSV--SDKTGLVEFARSLASLGLSLVASGGTAKAIRDAGLAVRDV 51
Cdd:cd01424 3 VFISVadRDKPEAVEIAKRLAELGFKLVATEGTAKYLQEAGIPVEVV 49
|
|
| carB |
PRK05294 |
carbamoyl-phosphate synthase large subunit; |
7-51 |
4.01e-06 |
|
carbamoyl-phosphate synthase large subunit;
Pssm-ID: 235393 [Multi-domain] Cd Length: 1066 Bit Score: 48.55 E-value: 4.01e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 26338005 7 ALFSV--SDKTGLVEFARSLASLGLSLVASGGTAKAIRDAGLAVRDV 51
Cdd:PRK05294 940 VFLSVrdRDKEEVVELAKRLLELGFKILATSGTAKFLREAGIPVELV 986
|
|
| CPSaseII_lrg |
TIGR01369 |
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes ... |
12-119 |
4.63e-04 |
|
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: 42.29 E-value: 4.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26338005 12 SDKTGLVEFARSLASLGLSLVASGGTAKAIRDAG---LAVRDVSEltGFPEMLggrvktlhPAVHAG--ILARNIPEDAA 86
Cdd:TIGR01369 947 KDKEELLDLARKLAEKGYKLYATEGTAKFLGEAGikpELVLKVSE--GRPNIL--------DLIKNGeiELVINTTSKGA 1016
|
90 100 110
....*....|....*....|....*....|...
gi 26338005 87 DMARLDFNLVRVVVCNLYPFVKTVASPDVTVEA 119
Cdd:TIGR01369 1017 GTATDGYKIRREALDYGVPLITTLNTAEAFAEA 1049
|
|
| |
