|
Name |
Accession |
Description |
Interval |
E-value |
| Adenylsucc_synt |
pfam00709 |
Adenylosuccinate synthetase; |
6-249 |
1.87e-158 |
|
Adenylosuccinate synthetase;
Pssm-ID: 459912 Cd Length: 417 Bit Score: 446.03 E-value: 1.87e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000814583 6 EIDIEGQLKRLKGFAERIRPMVRDGVYFMYEALHGPpKKILVEGANAALLDIDFGTYPFVTSSNCTVGGVCTGLGIPPQN 85
Cdd:pfam00709 175 PLDVEEELEELLEYAERLKPYVVDTSYFLNKALKEG-KKILFEGAQGTLLDIDHGTYPYVTSSNTTAGGACTGLGIGPTK 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000814583 86 IGDVYGVVKAYTTRVGIGAFPTEQINEIGGLLQTRGHEWGVTTGRKRRCGWLDLMILRYAHMVNGFTALALTKLDILDVL 165
Cdd:pfam00709 254 IDEVIGVVKAYTTRVGEGPFPTELFDETGEKLRERGHEFGATTGRPRRCGWLDLVALRYAVRINGVTGLALTKLDVLDGL 333
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000814583 166 GEVKVGVSYKLNGKRIPYFPANQEMLQKVEVEYETLPGWKADTTGARRWEDLPPQAQNYIRFVENHVGVAVKWVGVGKSR 245
Cdd:pfam00709 334 DEIKVCVAYELDGKRIDYFPADLEDLEKVEPVYETLPGWKEDISGVRSFEDLPENARKYVEFIEELLGVPIKIISVGPDR 413
|
....
gi 1000814583 246 ESMI 249
Cdd:pfam00709 414 EQTI 417
|
|
| Adenylsucc_synt |
smart00788 |
Adenylosuccinate synthetase; Adenylosuccinate synthetase plays an important role in purine ... |
1-249 |
8.04e-143 |
|
Adenylosuccinate synthetase; Adenylosuccinate synthetase plays an important role in purine biosynthesis, by catalyzing the GTP-dependent conversion of IMP and aspartic acid to AMP. Adenylosuccinate synthetase has been characterized from various sources ranging from Escherichia coli (gene purA) to vertebrate tissues. In vertebrates, two isozymes are present - one involved in purine biosynthesis and the other in the purine nucleotide cycle. The crystal structure of adenylosuccinate synthetase from E. coli reveals that the dominant structural element of each monomer of the homodimer is a central beta-sheet of 10 strands. The first nine strands of the sheet are mutually parallel with right-handed crossover connections between the strands. The 10th strand is antiparallel with respect to the first nine strands. In addition, the enzyme has two antiparallel beta-sheets, comprised of two strands and three strands each, 11 alpha-helices and two short 3/10-helices. Further, it has been suggested that the similarities in the GTP-binding domains of the synthetase and the p21ras protein are an example of convergent evolution of two distinct families of GTP-binding proteins. Structures of adenylosuccinate synthetase from Triticum aestivum and Arabidopsis thaliana when compared with the known structures from E. coli reveals that the overall fold is very similar to that of the E. coli protein.
Pssm-ID: 197875 Cd Length: 417 Bit Score: 406.48 E-value: 8.04e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000814583 1 MFPTLEIDIEGQLKRLKGFAERIRPMVRDGVYFMYEALHGPpKKILVEGANAALLDIDFGTYPFVTSSNCTVGGVCTGLG 80
Cdd:smart00788 169 LYGAEPVDVEEILEELLEYAERLRPYVTDVSELLNEALKAG-KKVLFEGAQGTLLDIDHGTYPYVTSSNTTAGGAATGAG 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000814583 81 IPPQNIGDVYGVVKAYTTRVGIGAFPTEQINEIGGLLQTRGHEWGVTTGRKRRCGWLDLMILRYAHMVNGFTALALTKLD 160
Cdd:smart00788 248 IGPTRIDRVIGVVKAYTTRVGEGPFPTELFDETGEKLRERGHEFGTTTGRPRRCGWFDAVLLRYAVRINGITGLALTKLD 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000814583 161 ILDVLGEVKVGVSYKLNGKRIPYFPANQEMLQKVEVEYETLPGWKADTTGARRWEDLPPQAQNYIRFVENHVGVAVKWVG 240
Cdd:smart00788 328 VLDGLDEIKVCVAYKLDGKIIDYFPADLEDLERCEPIYEELPGWKEDTTGVRSYEDLPENAKKYIERIEELVGVPVSIIS 407
|
....*....
gi 1000814583 241 VGKSRESMI 249
Cdd:smart00788 408 TGPDREQTI 416
|
|
| PurA |
COG0104 |
Adenylosuccinate synthase [Nucleotide transport and metabolism]; Adenylosuccinate synthase is ... |
6-251 |
5.67e-135 |
|
Adenylosuccinate synthase [Nucleotide transport and metabolism]; Adenylosuccinate synthase is part of the Pathway/BioSystem: Purine biosynthesis
Pssm-ID: 439874 Cd Length: 423 Bit Score: 386.68 E-value: 5.67e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000814583 6 EIDIEGQLKRLKGFAERIRPMVRDGVYFMYEALH-GppKKILVEGANAALLDIDFGTYPFVTSSNCTVGGVCTGLGIPPQ 84
Cdd:COG0104 178 PLDFEELLEEYLEYAERLKPYVADTSELLNEALKaG--KKVLFEGAQGTLLDIDHGTYPYVTSSNTTAGGACTGSGVGPT 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000814583 85 NIGDVYGVVKAYTTRVGIGAFPTEQINEIGGLLQTRGHEWGVTTGRKRRCGWLDLMILRYAHMVNGFTALALTKLDILDV 164
Cdd:COG0104 256 KIDRVIGVVKAYTTRVGEGPFPTELFDETGERLRERGHEFGTTTGRPRRCGWLDAVALRYAVRINGLTGLALTKLDVLDG 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000814583 165 LGEVKVGVSYKLNGKRIPYFPANQEMLQKVEVEYETLPGWKADTTGARRWEDLPPQAQNYIRFVENHVGVAVKWVGVGKS 244
Cdd:COG0104 336 LDEIKVCVAYELDGERIDEFPASLEDLARCEPVYEELPGWKEDISGIRSFEDLPENARAYVERIEELLGVPISIVSVGPD 415
|
....*..
gi 1000814583 245 RESMIQL 251
Cdd:COG0104 416 REQTIVR 422
|
|
| PRK01117 |
PRK01117 |
adenylosuccinate synthetase; Provisional |
1-251 |
6.99e-133 |
|
adenylosuccinate synthetase; Provisional
Pssm-ID: 234904 Cd Length: 430 Bit Score: 381.70 E-value: 6.99e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000814583 1 MFPTLEIDIEGQLKRLKGFAERIRPMVRDGVYFMYEALH-GppKKILVEGANAALLDIDFGTYPFVTSSNCTVGGVCTGL 79
Cdd:PRK01117 175 YYGAEAVDFEEILDEYLEYAERLKPYVTDTSLLLNDALKaG--KRVLFEGAQGTLLDIDHGTYPFVTSSNTTAGGAATGS 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000814583 80 GIPPQNIGDVYGVVKAYTTRVGIGAFPTEQINEIGGLLQTRGHEWGVTTGRKRRCGWLDLMILRYAHMVNGFTALALTKL 159
Cdd:PRK01117 253 GVGPTKIDYVLGIAKAYTTRVGSGPFPTELFDEVGEHLRERGHEFGTTTGRPRRCGWFDAVALRYAVRVNGLTGLALTKL 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000814583 160 DILDVLGEVKVGVSYKLNGKRIPYFPANQEMLQKVEVEYETLPGWKADTTGARRWEDLPPQAQNYIRFVENHVGVAVKWV 239
Cdd:PRK01117 333 DVLDGLEEIKICVAYELDGKRIDYFPASLEDLARCEPIYEELPGWSESTTGVRSFDDLPENARKYIKRIEELTGVPISII 412
|
250
....*....|..
gi 1000814583 240 GVGKSRESMIQL 251
Cdd:PRK01117 413 STGPDRDQTIIL 424
|
|
| purA |
TIGR00184 |
adenylosuccinate synthase; Alternate name IMP--aspartate ligase. [Purines, pyrimidines, ... |
1-251 |
6.18e-105 |
|
adenylosuccinate synthase; Alternate name IMP--aspartate ligase. [Purines, pyrimidines, nucleosides, and nucleotides, Purine ribonucleotide biosynthesis]
Pssm-ID: 272949 Cd Length: 425 Bit Score: 310.63 E-value: 6.18e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000814583 1 MFPTLEIDIEGQLKRLKGFAERIRPMVRDGVYFMYEALHGPpKKILVEGANAALLDIDFGTYPFVTSSNCTVGGVCTGLG 80
Cdd:TIGR00184 171 YYKDEGVDYEKKLDEYMKYAEELKPFVVDVSVELNEALDEG-EKVLFEGAQGTMLDIDYGTYPYVTSSNTTAGGVATGVG 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000814583 81 IPPQNIGDVYGVVKAYTTRVGIGAFPTEQINEIGGLLQTRGHEWGVTTGRKRRCGWLDLMILRYAHMVNGFTALALTKLD 160
Cdd:TIGR00184 250 IGPTKVDEVIGVFKAYTTRVGAGPFPTELSDEEGEKLGTKGAEFGTTTGRRRRCGWFDLVAARYACRLNGATQLALTKLD 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000814583 161 ILDVLGEVKVGVSYKLNGKRIPYFPANQEMLQKVEVEYETLPGWKADTTGARRWEDLPPQAQNYIRFVENHVGVAVKWVG 240
Cdd:TIGR00184 330 VLDGIDEIKVCVAYRMKGEILELFPLDLKDLKGVEPIYETLPGWDKECTGVTEYSDLPENAKKYIERIEELTGVPVTIIS 409
|
250
....*....|.
gi 1000814583 241 VGKSRESMIQL 251
Cdd:TIGR00184 410 TGPEREQTIDL 420
|
|
| AdSS |
cd03108 |
adenylosuccinate synthetase; Adenylosuccinate synthetase (AdSS) catalyzes the first step in ... |
25-249 |
6.10e-94 |
|
adenylosuccinate synthetase; Adenylosuccinate synthetase (AdSS) catalyzes the first step in the de novo biosynthesis of AMP. IMP and L-aspartate are conjugated in a two-step reaction accompanied by the hydrolysis of GTP to GDP in the presence of Mg2+. In the first step, the r-phosphate group of GTP is transferred to the 6-oxygen atom of IMP. An aspartate then displaces this 6-phosphate group to form the product adenylosuccinate. Because of its critical role in purine biosynthesis, AdSS is a target of antibiotics, herbicides and antitumor drugs.
Pssm-ID: 349762 Cd Length: 316 Bit Score: 278.61 E-value: 6.10e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000814583 25 PMVRDGVYFMYEALHgPPKKILVEGANAALLDIDFGTYPFVTSSNCTVGGVCTGLGIPPQNIGDVYGVVKAYTTRVGIGA 104
Cdd:cd03108 150 PYVVDTVELLNEALK-AGKKVLFEGAQGTLLDIDFGTYPYVTSSNTTAGGVCTGLGIPPRRVDRVIGVVKAYTTRVGSGP 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000814583 105 FPTEQINEIGGLLQTRGHEWGVTTGRKRRCGWLDLMILRYAHMVNGFTALALTKLDIldvlgevkvgvsyklngkripyf 184
Cdd:cd03108 229 FPTELFDEEGEKLRELGHEYGTTTGRPRRCGWLDLVALRYAVRINGLTELALTKLDV----------------------- 285
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1000814583 185 panqemlqkveveyetlpgwkadttgarrwedlppQAQNYIRFVENHVGVAVKWVGVGKSRESMI 249
Cdd:cd03108 286 -----------------------------------NAQKYIERIEELLGVPITYISVGPDREQTI 315
|
|
| amino_Aden_PurZ |
NF038379 |
succino-amino-deoxyadenylate synthase PurZ; |
3-150 |
1.94e-08 |
|
succino-amino-deoxyadenylate synthase PurZ;
Pssm-ID: 468496 Cd Length: 292 Bit Score: 53.91 E-value: 1.94e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000814583 3 PTLEIDIEGQLKRLKGFAERIRPMVRDGVYFMYEALHGPPKKILVEGANAALLDIDFGTYPFVTSSNCTVGGVCTGLGIP 82
Cdd:NF038379 142 PSTLGDAEGDFGEGAVRDQPWEIAERVVDNALYDFALQAAERIQIEGTQGYSLGLHAGFYPYCTSRDCTPADFLADAGIP 221
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1000814583 83 PQNI--GDVYGVVKAYTTRVGIGAFPT---------EQIneigGLLQtrghEWGVTTGRKRRCGWLDLMILRYAHMVNG 150
Cdd:NF038379 222 LPNVdaFKVVGTARTYPIRVAGWSGNSypdqgettwEEL----GLPE----ELTTVTKKVRRVGTFSAEQVREAVQANG 292
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| Adenylsucc_synt |
pfam00709 |
Adenylosuccinate synthetase; |
6-249 |
1.87e-158 |
|
Adenylosuccinate synthetase;
Pssm-ID: 459912 Cd Length: 417 Bit Score: 446.03 E-value: 1.87e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000814583 6 EIDIEGQLKRLKGFAERIRPMVRDGVYFMYEALHGPpKKILVEGANAALLDIDFGTYPFVTSSNCTVGGVCTGLGIPPQN 85
Cdd:pfam00709 175 PLDVEEELEELLEYAERLKPYVVDTSYFLNKALKEG-KKILFEGAQGTLLDIDHGTYPYVTSSNTTAGGACTGLGIGPTK 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000814583 86 IGDVYGVVKAYTTRVGIGAFPTEQINEIGGLLQTRGHEWGVTTGRKRRCGWLDLMILRYAHMVNGFTALALTKLDILDVL 165
Cdd:pfam00709 254 IDEVIGVVKAYTTRVGEGPFPTELFDETGEKLRERGHEFGATTGRPRRCGWLDLVALRYAVRINGVTGLALTKLDVLDGL 333
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000814583 166 GEVKVGVSYKLNGKRIPYFPANQEMLQKVEVEYETLPGWKADTTGARRWEDLPPQAQNYIRFVENHVGVAVKWVGVGKSR 245
Cdd:pfam00709 334 DEIKVCVAYELDGKRIDYFPADLEDLEKVEPVYETLPGWKEDISGVRSFEDLPENARKYVEFIEELLGVPIKIISVGPDR 413
|
....
gi 1000814583 246 ESMI 249
Cdd:pfam00709 414 EQTI 417
|
|
| Adenylsucc_synt |
smart00788 |
Adenylosuccinate synthetase; Adenylosuccinate synthetase plays an important role in purine ... |
1-249 |
8.04e-143 |
|
Adenylosuccinate synthetase; Adenylosuccinate synthetase plays an important role in purine biosynthesis, by catalyzing the GTP-dependent conversion of IMP and aspartic acid to AMP. Adenylosuccinate synthetase has been characterized from various sources ranging from Escherichia coli (gene purA) to vertebrate tissues. In vertebrates, two isozymes are present - one involved in purine biosynthesis and the other in the purine nucleotide cycle. The crystal structure of adenylosuccinate synthetase from E. coli reveals that the dominant structural element of each monomer of the homodimer is a central beta-sheet of 10 strands. The first nine strands of the sheet are mutually parallel with right-handed crossover connections between the strands. The 10th strand is antiparallel with respect to the first nine strands. In addition, the enzyme has two antiparallel beta-sheets, comprised of two strands and three strands each, 11 alpha-helices and two short 3/10-helices. Further, it has been suggested that the similarities in the GTP-binding domains of the synthetase and the p21ras protein are an example of convergent evolution of two distinct families of GTP-binding proteins. Structures of adenylosuccinate synthetase from Triticum aestivum and Arabidopsis thaliana when compared with the known structures from E. coli reveals that the overall fold is very similar to that of the E. coli protein.
Pssm-ID: 197875 Cd Length: 417 Bit Score: 406.48 E-value: 8.04e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000814583 1 MFPTLEIDIEGQLKRLKGFAERIRPMVRDGVYFMYEALHGPpKKILVEGANAALLDIDFGTYPFVTSSNCTVGGVCTGLG 80
Cdd:smart00788 169 LYGAEPVDVEEILEELLEYAERLRPYVTDVSELLNEALKAG-KKVLFEGAQGTLLDIDHGTYPYVTSSNTTAGGAATGAG 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000814583 81 IPPQNIGDVYGVVKAYTTRVGIGAFPTEQINEIGGLLQTRGHEWGVTTGRKRRCGWLDLMILRYAHMVNGFTALALTKLD 160
Cdd:smart00788 248 IGPTRIDRVIGVVKAYTTRVGEGPFPTELFDETGEKLRERGHEFGTTTGRPRRCGWFDAVLLRYAVRINGITGLALTKLD 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000814583 161 ILDVLGEVKVGVSYKLNGKRIPYFPANQEMLQKVEVEYETLPGWKADTTGARRWEDLPPQAQNYIRFVENHVGVAVKWVG 240
Cdd:smart00788 328 VLDGLDEIKVCVAYKLDGKIIDYFPADLEDLERCEPIYEELPGWKEDTTGVRSYEDLPENAKKYIERIEELVGVPVSIIS 407
|
....*....
gi 1000814583 241 VGKSRESMI 249
Cdd:smart00788 408 TGPDREQTI 416
|
|
| PurA |
COG0104 |
Adenylosuccinate synthase [Nucleotide transport and metabolism]; Adenylosuccinate synthase is ... |
6-251 |
5.67e-135 |
|
Adenylosuccinate synthase [Nucleotide transport and metabolism]; Adenylosuccinate synthase is part of the Pathway/BioSystem: Purine biosynthesis
Pssm-ID: 439874 Cd Length: 423 Bit Score: 386.68 E-value: 5.67e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000814583 6 EIDIEGQLKRLKGFAERIRPMVRDGVYFMYEALH-GppKKILVEGANAALLDIDFGTYPFVTSSNCTVGGVCTGLGIPPQ 84
Cdd:COG0104 178 PLDFEELLEEYLEYAERLKPYVADTSELLNEALKaG--KKVLFEGAQGTLLDIDHGTYPYVTSSNTTAGGACTGSGVGPT 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000814583 85 NIGDVYGVVKAYTTRVGIGAFPTEQINEIGGLLQTRGHEWGVTTGRKRRCGWLDLMILRYAHMVNGFTALALTKLDILDV 164
Cdd:COG0104 256 KIDRVIGVVKAYTTRVGEGPFPTELFDETGERLRERGHEFGTTTGRPRRCGWLDAVALRYAVRINGLTGLALTKLDVLDG 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000814583 165 LGEVKVGVSYKLNGKRIPYFPANQEMLQKVEVEYETLPGWKADTTGARRWEDLPPQAQNYIRFVENHVGVAVKWVGVGKS 244
Cdd:COG0104 336 LDEIKVCVAYELDGERIDEFPASLEDLARCEPVYEELPGWKEDISGIRSFEDLPENARAYVERIEELLGVPISIVSVGPD 415
|
....*..
gi 1000814583 245 RESMIQL 251
Cdd:COG0104 416 REQTIVR 422
|
|
| PRK01117 |
PRK01117 |
adenylosuccinate synthetase; Provisional |
1-251 |
6.99e-133 |
|
adenylosuccinate synthetase; Provisional
Pssm-ID: 234904 Cd Length: 430 Bit Score: 381.70 E-value: 6.99e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000814583 1 MFPTLEIDIEGQLKRLKGFAERIRPMVRDGVYFMYEALH-GppKKILVEGANAALLDIDFGTYPFVTSSNCTVGGVCTGL 79
Cdd:PRK01117 175 YYGAEAVDFEEILDEYLEYAERLKPYVTDTSLLLNDALKaG--KRVLFEGAQGTLLDIDHGTYPFVTSSNTTAGGAATGS 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000814583 80 GIPPQNIGDVYGVVKAYTTRVGIGAFPTEQINEIGGLLQTRGHEWGVTTGRKRRCGWLDLMILRYAHMVNGFTALALTKL 159
Cdd:PRK01117 253 GVGPTKIDYVLGIAKAYTTRVGSGPFPTELFDEVGEHLRERGHEFGTTTGRPRRCGWFDAVALRYAVRVNGLTGLALTKL 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000814583 160 DILDVLGEVKVGVSYKLNGKRIPYFPANQEMLQKVEVEYETLPGWKADTTGARRWEDLPPQAQNYIRFVENHVGVAVKWV 239
Cdd:PRK01117 333 DVLDGLEEIKICVAYELDGKRIDYFPASLEDLARCEPIYEELPGWSESTTGVRSFDDLPENARKYIKRIEELTGVPISII 412
|
250
....*....|..
gi 1000814583 240 GVGKSRESMIQL 251
Cdd:PRK01117 413 STGPDRDQTIIL 424
|
|
| PTZ00350 |
PTZ00350 |
adenylosuccinate synthetase; Provisional |
2-249 |
6.43e-130 |
|
adenylosuccinate synthetase; Provisional
Pssm-ID: 240376 Cd Length: 436 Bit Score: 374.36 E-value: 6.43e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000814583 2 FPTLEIDIEGQLKRLKGFAERIRPMVRDGVYFMYEALHgPPKKILVEGANAALLDIDFGTYPFVTSSNCTVGGVCTGLGI 81
Cdd:PTZ00350 185 YNIEEYDAEEELERYKGYAEKLKDMIVDTVYFMNKAIK-EGKRVLVEGANATMLDIDFGTYPYVTSSNTTVGGVCTGLGI 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000814583 82 PPQNIGDVYGVVKAYTTRVGIGAFPTEQINEIGGLLQTRGHEWGVTTGRKRRCGWLDLMILRYAHMVNGFTALALTKLDI 161
Cdd:PTZ00350 264 PPNAIILVIGVVKAYTTRVGEGPFPTELFDENGDYLRKKGHEYGTTTGRPRRCGWLDIPALRYVQMINGFDSINLTKLDV 343
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000814583 162 LDVLGEVKVGVSYKLNGK--RIPYFPANQEMLQKVEVEYETLPGWKADTTGARRWEDLPPQAQNYIRFVENHVGVAVKWV 239
Cdd:PTZ00350 344 LSGLKEIKICVNYKNKGTglEIGRYPSSIEELEEYEPVYETMPGWKTDISKCKTFEELPENAQKYVLFIEELLGVPIVWI 423
|
250
....*....|
gi 1000814583 240 GVGKSRESMI 249
Cdd:PTZ00350 424 GVGPNRENMI 433
|
|
| PLN02513 |
PLN02513 |
adenylosuccinate synthase |
2-249 |
1.76e-121 |
|
adenylosuccinate synthase
Pssm-ID: 178129 Cd Length: 427 Bit Score: 352.41 E-value: 1.76e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000814583 2 FPTLEID---IEGQLKRLKGFAERIRPMVRDGVYFMYEAlHGPPKKILVEGANAALLDIDFGTYPFVTSSNCTVGGVCTG 78
Cdd:PLN02513 174 FEGFEYDasmVEEEVEAYKKFAERLEPFITDTVHYLNEA-IQAGKKILVEGAQATMLDIDFGTYPFVTSSNPSAGGICTG 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000814583 79 LGIPPQNIGDVYGVVKAYTTRVGIGAFPTEQINEIGGLLQTRGHEWGVTTGRKRRCGWLDLMILRYAHMVNGFTALALTK 158
Cdd:PLN02513 253 LGIAPRKLGDIIGVVKAYTTRVGSGPFPTELFGELGDLLREAGQEFGTTTGRPRRCGWLDIVALKYSCQINGFTSLNLTK 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000814583 159 LDILDVLGEVKVGVSYKL-NGKRIPYFPANQEMLQKVEVEYETLPGWKADTTGARRWEDLPPQAQNYIRFVENHVGVAVK 237
Cdd:PLN02513 333 LDVLSGLPEIKIGVAYKTpDGKVVKSFPADLDTLEQVEVVYEVLPGWQEDISSVRNYDDLPAAAQAYVERIEELVGVPVH 412
|
250
....*....|..
gi 1000814583 238 WVGVGKSRESMI 249
Cdd:PLN02513 413 YIGVGPGRDALI 424
|
|
| purA |
TIGR00184 |
adenylosuccinate synthase; Alternate name IMP--aspartate ligase. [Purines, pyrimidines, ... |
1-251 |
6.18e-105 |
|
adenylosuccinate synthase; Alternate name IMP--aspartate ligase. [Purines, pyrimidines, nucleosides, and nucleotides, Purine ribonucleotide biosynthesis]
Pssm-ID: 272949 Cd Length: 425 Bit Score: 310.63 E-value: 6.18e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000814583 1 MFPTLEIDIEGQLKRLKGFAERIRPMVRDGVYFMYEALHGPpKKILVEGANAALLDIDFGTYPFVTSSNCTVGGVCTGLG 80
Cdd:TIGR00184 171 YYKDEGVDYEKKLDEYMKYAEELKPFVVDVSVELNEALDEG-EKVLFEGAQGTMLDIDYGTYPYVTSSNTTAGGVATGVG 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000814583 81 IPPQNIGDVYGVVKAYTTRVGIGAFPTEQINEIGGLLQTRGHEWGVTTGRKRRCGWLDLMILRYAHMVNGFTALALTKLD 160
Cdd:TIGR00184 250 IGPTKVDEVIGVFKAYTTRVGAGPFPTELSDEEGEKLGTKGAEFGTTTGRRRRCGWFDLVAARYACRLNGATQLALTKLD 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000814583 161 ILDVLGEVKVGVSYKLNGKRIPYFPANQEMLQKVEVEYETLPGWKADTTGARRWEDLPPQAQNYIRFVENHVGVAVKWVG 240
Cdd:TIGR00184 330 VLDGIDEIKVCVAYRMKGEILELFPLDLKDLKGVEPIYETLPGWDKECTGVTEYSDLPENAKKYIERIEELTGVPVTIIS 409
|
250
....*....|.
gi 1000814583 241 VGKSRESMIQL 251
Cdd:TIGR00184 410 TGPEREQTIDL 420
|
|
| AdSS |
cd03108 |
adenylosuccinate synthetase; Adenylosuccinate synthetase (AdSS) catalyzes the first step in ... |
25-249 |
6.10e-94 |
|
adenylosuccinate synthetase; Adenylosuccinate synthetase (AdSS) catalyzes the first step in the de novo biosynthesis of AMP. IMP and L-aspartate are conjugated in a two-step reaction accompanied by the hydrolysis of GTP to GDP in the presence of Mg2+. In the first step, the r-phosphate group of GTP is transferred to the 6-oxygen atom of IMP. An aspartate then displaces this 6-phosphate group to form the product adenylosuccinate. Because of its critical role in purine biosynthesis, AdSS is a target of antibiotics, herbicides and antitumor drugs.
Pssm-ID: 349762 Cd Length: 316 Bit Score: 278.61 E-value: 6.10e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000814583 25 PMVRDGVYFMYEALHgPPKKILVEGANAALLDIDFGTYPFVTSSNCTVGGVCTGLGIPPQNIGDVYGVVKAYTTRVGIGA 104
Cdd:cd03108 150 PYVVDTVELLNEALK-AGKKVLFEGAQGTLLDIDFGTYPYVTSSNTTAGGVCTGLGIPPRRVDRVIGVVKAYTTRVGSGP 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000814583 105 FPTEQINEIGGLLQTRGHEWGVTTGRKRRCGWLDLMILRYAHMVNGFTALALTKLDIldvlgevkvgvsyklngkripyf 184
Cdd:cd03108 229 FPTELFDEEGEKLRELGHEYGTTTGRPRRCGWLDLVALRYAVRINGLTELALTKLDV----------------------- 285
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1000814583 185 panqemlqkveveyetlpgwkadttgarrwedlppQAQNYIRFVENHVGVAVKWVGVGKSRESMI 249
Cdd:cd03108 286 -----------------------------------NAQKYIERIEELLGVPITYISVGPDREQTI 315
|
|
| PRK13787 |
PRK13787 |
adenylosuccinate synthetase; Provisional |
16-251 |
1.78e-72 |
|
adenylosuccinate synthetase; Provisional
Pssm-ID: 172324 Cd Length: 423 Bit Score: 227.53 E-value: 1.78e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000814583 16 LKGFAERIRPMVRDGVYFMYEALHgPPKKILVEGANAALLDIDFGTYPFVTSSNCTVGGVCTGLGIPPQNIGDVYGVVKA 95
Cdd:PRK13787 190 LKFFLSKVGKNIINTAYYLDTELK-KGKRVLLEGAQGTGLDVDFGTYPYVTSSNPTTGGALIGTGISFQHLKHVIGITKA 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000814583 96 YTTRVGIGAFPTEQINEIGGLLQTRGHEWGVTTGRKRRCGWLDLMILRYAHMVNGFTALALTKLDILDVLGEVKVGVSYK 175
Cdd:PRK13787 269 YTTRVGEGPFPTELLGEAGEVLRQKGGEFGATTGRPRRCGWFDVEMLKHSVRINGITSIALTKIDILSDYDTIPVAVGYK 348
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1000814583 176 LNGKRIPYFPAnqEMLQKVEVEYETLPGWKADTTGARRWEDLPPQAQNYIRFVENHVGVAVKWVGVGKSRESMIQL 251
Cdd:PRK13787 349 LNGKTLDCFPS--QGLEKVEPLYEEFPGWKDDISGINEFQKLPEKCKNYISALEKWIGVKINLVSTGPDRKDTIIG 422
|
|
| PRK13786 |
PRK13786 |
adenylosuccinate synthetase; Provisional |
10-250 |
2.36e-70 |
|
adenylosuccinate synthetase; Provisional
Pssm-ID: 184325 Cd Length: 424 Bit Score: 221.98 E-value: 2.36e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000814583 10 EGQLKRLKGFAERIRPMVRDGVYFMYEALHgPPKKILVEGANAALLDIDFGTYPFVTSSNCTVGGVCTGLGIPPQNIGDV 89
Cdd:PRK13786 183 EALIDKYLELGRQLAPYITDVSYEINKALD-EGKSVLAEGAQGTHLDVIHGTQKFVTSSSTIAGSACANLGVGPTRVDNV 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000814583 90 YGVVKAYTTRVGIGAFPTEQINEIGGLLQTRGHEWGVTTGRKRRCGWLDLMILRYAHMVNGFTALALTKLDILDVLGEVK 169
Cdd:PRK13786 262 LGIVKAYITRVGEGPLPTELKDEAGEHLQDVGGEFGTTTGRPRRCGWFDLPLLKKAIYLNGYTEIALTKLDVLTGLDPIK 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000814583 170 VGVSYKLNGKRIPYFPANQEMLQKVEVEYETLPGWKADTTGARRWEDLPPQAQNYIRFVENHVGVAVKWVGVGKSRESMI 249
Cdd:PRK13786 342 ICVGYELDGEILDYPPELTSDLARCVPVYEELEGWSTDLTEVKAYEDLPENARNYVERLEELMGVPIKYISVGPGREQTF 421
|
.
gi 1000814583 250 Q 250
Cdd:PRK13786 422 K 422
|
|
| PRK13783 |
PRK13783 |
adenylosuccinate synthetase; Provisional |
5-251 |
2.36e-64 |
|
adenylosuccinate synthetase; Provisional
Pssm-ID: 237505 Cd Length: 404 Bit Score: 205.72 E-value: 2.36e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000814583 5 LEIDIEGQLKRLKGFAERIRPMVRDGVYfMYEALHGppKKILVEGANAALLDIDFGTYPFVTSSNCTVGGVCTGLGIPPQ 84
Cdd:PRK13783 172 IEFDVEKMMEDLLTFYEKIKDLVVSPVE-IKRILEE--KSVLFEGTQGVLLDLDVGTYPYVTSSNCSTTGVSAGMGFPVK 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000814583 85 nIGDVYGVVKAYTTRVGIGAFPTEQINEIGGLLQTRGHEWGVTTGRKRRCGWLDLMILRYAHMVNGFTALALTKLDILDV 164
Cdd:PRK13783 249 -VDEVIGVFKAYTTRVGEGPFPTELFGEEGEKLRKAGHEYGATTGRPRRCGWLDLPLLRYAIEVSGVDSLVMTKADVLNG 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000814583 165 LGEVKVGVSYKLNGKRIPYfPANQEMLQKVEVEYETLPGWKadTTGARRWEDlppqaqnYIRFVENHVGVAVKWVGVGKS 244
Cdd:PRK13783 328 FEKIKVCVRYEIGGKEVRD-PSSLRDLEKAEPVYEEFDGWK--SLEDKNFLK-------FVDFIERETGRKIAYISTGPK 397
|
....*..
gi 1000814583 245 RESMIQL 251
Cdd:PRK13783 398 IEEIVEV 404
|
|
| PRK13788 |
PRK13788 |
adenylosuccinate synthetase; Provisional |
9-246 |
2.16e-63 |
|
adenylosuccinate synthetase; Provisional
Pssm-ID: 184326 [Multi-domain] Cd Length: 404 Bit Score: 203.50 E-value: 2.16e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000814583 9 IEGQLKRLKGFAERIRPMVRDGVYFMYEAL-HGppKKILVEGANAALLDIDFGTYPFVTSSNCTVGGVCTGLGIPPQNIG 87
Cdd:PRK13788 172 VEKALADLAPMREILLPFIADTGSLLREAIrEG--KRVLFEGAQATLLDLNYGTYPYVTSSHPTVGGILVGAGVNHKAIN 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000814583 88 DVYGVVKAYTTRVGIGAFPTEQINEIGGLLQTRG----HEWGVTTGRKRRCGWLDLMILRYAHMVNGFTALALTKLDILD 163
Cdd:PRK13788 250 KVYGVAKAFTTRVGHGPFPTEVFGEMAIRLRGKGgnpwDEFGTTTGRARRVGWLDLVLLKYACEVNGFDGLVLTKLDVLS 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000814583 164 VLGEVKVGVSYKLNGKripyfpanqemlqkveVEYETLPGWkADTTGARRWEDLPPQAQNYIRFVENHVGVAVKWVGVGK 243
Cdd:PRK13788 330 GLEKVKVCVEYDDDGQ----------------PVYKELPGW-GDLDGVKSREALPKEAQAYLELIEETTGVPVVMFSTSP 392
|
...
gi 1000814583 244 SRE 246
Cdd:PRK13788 393 RRE 395
|
|
| PRK13785 |
PRK13785 |
adenylosuccinate synthetase; Provisional |
6-251 |
1.53e-57 |
|
adenylosuccinate synthetase; Provisional
Pssm-ID: 237506 Cd Length: 454 Bit Score: 189.58 E-value: 1.53e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000814583 6 EIDIEGQLKRLKGFAERIRP--MVRDGVYFMYEALHGPpKKILVEGANAALLDIDFGTYPFVTSSNCTVGGVCTGLGIPP 83
Cdd:PRK13785 184 AFDVDALFEEYREYGERLAEedMTVNAGDFLAERIDDG-DNVMLEGAQGTSIDIDHGNYPYVTSSNPTAGGAATGTGLGP 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000814583 84 QNIGD--VYGVVKAYTTRVGIGAFPTE---------------QINEIGGLLQTRGHEWGVTTGRKRRCGWLDLMILRYAH 146
Cdd:PRK13785 263 TVVGQgeVVGIVKAYLSRVGSGPLPTElggvegdtpdeggrpDEEELATYIREEGGEYGTVTGRPRRVGWLDMPMLRHAA 342
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000814583 147 MVNGFTALALTKLDILDVLGEVKVGVSYKLNGKRIPYFPANQEMLQKVEVEYETLPGWKA---DTTGARRWEDLPPQAQN 223
Cdd:PRK13785 343 RASGFTGLAINHIDVLAGLDEVKVGHSYELDGEELLTMPATTERWARCEPNFRSFDGWPEvdwAAVAEEGYDALPENART 422
|
250 260
....*....|....*....|....*...
gi 1000814583 224 YIRFVENHVGVAVKWVGVGKSRESMIQL 251
Cdd:PRK13785 423 YLEYVSDELDTPIYAVGVGPGREETVVL 450
|
|
| PRK13784 |
PRK13784 |
adenylosuccinate synthetase; Provisional |
2-249 |
1.42e-51 |
|
adenylosuccinate synthetase; Provisional
Pssm-ID: 172322 Cd Length: 428 Bit Score: 173.28 E-value: 1.42e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000814583 2 FPTLEIDIEgqlkRLKGFAERIRPMVRDGVYFMYEALhGPPKKILVEGANAALLDIDFGTYPFVTSSNCTVGGVCTGLGI 81
Cdd:PRK13784 180 YPTLEQEFD----KLFALGQKLKQYAADTFSIIDQAI-AAGKNVVYEGAQGVLLDVDYGTYPFVTSSNTSVAGVYSGATT 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000814583 82 PPQNIGDVYGVVKAYTTRVGIGAFPTEQINEIGGLLQTRGHEWGVTTGRKRRCGWLDLMILRYAHMVNGFTALALTKLDI 161
Cdd:PRK13784 255 AGHGLDHVIGITKAYTTRVGEGPFPTELFDDVGKFIQHKGGEIGVTTGRIRRCGWLDLPLLKYSAKCSNLTSIALTKVDV 334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000814583 162 LDVLGEVKVGVSYKLNGKRIpYFPANQEMLQKVEVEYETLPGWKADTTGARrwEDLPPQAQNYIRFVENHVGVAVKWVGV 241
Cdd:PRK13784 335 LSDMDTLKVCIGYKYEGKEI-YCAYPGIDLYKVEPILVEMEPFSIDETVTK--DNMPAALKTYLKTIENHVGIPISSLAY 411
|
....*...
gi 1000814583 242 GKSRESMI 249
Cdd:PRK13784 412 GPSREQIL 419
|
|
| PRK04293 |
PRK04293 |
adenylosuccinate synthetase; Provisional |
13-251 |
6.88e-36 |
|
adenylosuccinate synthetase; Provisional
Pssm-ID: 179812 Cd Length: 333 Bit Score: 130.00 E-value: 6.88e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000814583 13 LKRLKGFAErIRPMVRDGVYFMYEALHGPpKKILVEGANAALLDIDFGTYPFVTSSNCTVGGVCTGLGIPPQNIGDVYGV 92
Cdd:PRK04293 140 LKLAKDVEE-LEKYLTDVPEEVNEALDRG-ENVLIEGTQGFGLSLYYGTYPYVTSKDTTASGIASDVGVGPTKVDEVIVV 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000814583 93 VKAYTTRVGIGAFPTEQINEIGgllQTRG-HEWGVTTGRKRRCGWLDLMILRYAHMVNGFTALALTKLDILDvlgevkvg 171
Cdd:PRK04293 218 FKSYPTRVGEGPFPTELSLEEA---EKLGlVEYGTVTGRRRRVGPFDFELARRAARINGATQIAITKLDKLD-------- 286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000814583 172 vsyklngkripyfpanqemlqkveveyetlpgwkADTTGARRWEDLPPQAQNYIRFVENHVGVAVKWVGVGKSRESMIQL 251
Cdd:PRK04293 287 ----------------------------------KEAYGVTEYDKLPPEAKKFIEEIEEELGVPVTLISTGPELEDTIDL 332
|
|
| amino_Aden_PurZ |
NF038379 |
succino-amino-deoxyadenylate synthase PurZ; |
3-150 |
1.94e-08 |
|
succino-amino-deoxyadenylate synthase PurZ;
Pssm-ID: 468496 Cd Length: 292 Bit Score: 53.91 E-value: 1.94e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000814583 3 PTLEIDIEGQLKRLKGFAERIRPMVRDGVYFMYEALHGPPKKILVEGANAALLDIDFGTYPFVTSSNCTVGGVCTGLGIP 82
Cdd:NF038379 142 PSTLGDAEGDFGEGAVRDQPWEIAERVVDNALYDFALQAAERIQIEGTQGYSLGLHAGFYPYCTSRDCTPADFLADAGIP 221
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1000814583 83 PQNI--GDVYGVVKAYTTRVGIGAFPT---------EQIneigGLLQtrghEWGVTTGRKRRCGWLDLMILRYAHMVNG 150
Cdd:NF038379 222 LPNVdaFKVVGTARTYPIRVAGWSGNSypdqgettwEEL----GLPE----ELTTVTKKVRRVGTFSAEQVREAVQANG 292
|
|
|